FN Clarivate Analytics Web of Science
VR 1.0
PT J
AU Leduc, V
   Théroux, L
   Dea, D
   Dufour, R
   Poirier, J
AF Leduc, Valerie
   Theroux, Louise
   Dea, Doris
   Dufour, Robert
   Poirier, Judes
TI Effects of rs3846662 Variants on HMGCR mRNA and Protein Levels and on
   Markers of Alzheimer's Disease Pathology
SO JOURNAL OF MOLECULAR NEUROSCIENCE
LA English
DT Article
DE Alzheimer's disease; HMGCR; rs3846662; Alternative splicing; Tau
   proteins; Beta-amyloid
ID DENSITY-LIPOPROTEIN-CHOLESTEROL; COENZYME-A REDUCTASE; APOLIPOPROTEIN-E;
   GENE-EXPRESSION; STATIN THERAPY; TYPE-4 ALLELE; HUMAN BRAIN; RISK;
   ONSET; DEMENTIA
AB 3-Hydroxy-3-methyglutaryl coenzyme A reductase (HMGCR) is a cholesterol-regulating gene with statin relevance. rs3846662 being involved in regulation of HMGCR alternative splicing, we explored its impact on HMGCR messenger RNA (mRNA) and protein levels in the brain and the associations between those levels and levels of Alzheimer's disease pathological markers. We used brain samples derived from a cohort of 33 non-demented controls and 90 Alzheimer's disease autopsied-confirmed cases. HMGCR mRNA levels were determined in the frontal cortex (n = 114) and cerebellum (n = 110) using Taqman-qPCR, and HMGCR protein levels were determined in the frontal cortex (n = 117) using a commercial enzyme immunoassay. While densities of neurofibrillary tangles and senile plaques were determined in the frontal cortex (n = 74), total tau, phosphorylated Tau, and beta-amyloid 1-42 levels were determined in the frontal cortex (n = 94) and cerebellum (n = 91) using commercial enzyme immunoassays. Despite an increase in full-length HMGCR mRNA ratio in the frontal cortex of women carrying the AA genotype, there were no associations between rs3846662 and HMGCR mRNA or protein levels. An increased Delta 13 HMGCR mRNA ratio was associated with increased levels of HMGCR proteins and neurofibrillary tangles in the frontal cortex but with reduced beta-amyloid 1-42 levels in the cerebellum, suggesting a brain cell type- or a disease progression-dependent association.
C1 [Leduc, Valerie; Theroux, Louise; Dea, Doris; Poirier, Judes] Douglas Mental Hlth Univ Inst, Ctr Studies Prevent Alzheimers Dis, StoP AD Ctr, 6875 Lasalle, Verdun, PQ H4H 1R3, Canada.
   [Poirier, Judes] McGill Univ, Ctr Studies Prevent Alzheimers Dis, Montreal, PQ, Canada.
   [Leduc, Valerie; Dufour, Robert] Univ Montreal, Dept Nutr, Inst Rech Clin Montreal, Montreal, PQ H3C 3J7, Canada.
C3 McGill University; Institut de Recherche Clinique de Montreal (IRCM);
   Universite de Montreal
RP Poirier, J (corresponding author), Douglas Mental Hlth Univ Inst, Ctr Studies Prevent Alzheimers Dis, StoP AD Ctr, 6875 Lasalle, Verdun, PQ H4H 1R3, Canada.; Poirier, J (corresponding author), McGill Univ, Ctr Studies Prevent Alzheimers Dis, Montreal, PQ, Canada.
EM judes.poirier@mcgill.ca
OI Leduc, Valerie/0000-0002-7512-8821
FU Canadian Institute of Health Research; Natural Sciences and Engineering
   Research Council of Canada; JL Levesque foundation; Canadian Stroke
   Network; Leducq Fondation
FX This study was supported by the Canadian Institute of Health Research
   (VL, JP), the Natural Sciences and Engineering Research Council of
   Canada (JP), the JL Levesque foundation (JP), the Canadian Stroke
   Network (VL), and the Leducq Fondation (RD).
CR Adlard PA, 2004, NEUROBIOL AGING, V25, P725, DOI 10.1016/j.neurobiolaging.2003.12.016
   Aulchenko YS, 2009, NAT GENET, V41, P47, DOI 10.1038/ng.269
   Azevedo FAC, 2009, J COMP NEUROL, V513, P532, DOI 10.1002/cne.21974
   BENJAMIN R, 1994, LANCET, V344, P473, DOI 10.1016/S0140-6736(94)91804-X
   Berson A, 2012, EMBO MOL MED, V4, P730, DOI 10.1002/emmm.201100995
   BIAMONTI G, 1993, J MOL BIOL, V230, P77, DOI 10.1006/jmbi.1993.1127
   Boukakis G, 2010, BMC CANCER, V10, DOI 10.1186/1471-2407-10-434
   Burkhardt R, 2008, ARTERIOSCL THROM VAS, V28, P2078, DOI 10.1161/ATVBAHA.108.172288
   Chasman DI, 2004, JAMA-J AM MED ASSOC, V291, P2821, DOI 10.1001/jama.291.23.2821
   Chung JY, 2012, J CLIN PHARMACOL, V52, P339, DOI 10.1177/0091270011398239
   CORDER EH, 1994, NAT GENET, V7, P180, DOI 10.1038/ng0694-180
   CORDER EH, 1993, SCIENCE, V261, P921, DOI 10.1126/science.8346443
   Delacourte A, 1999, NEUROLOGY, V52, P1158, DOI 10.1212/WNL.52.6.1158
   ETIENNE P, 1986, NEUROSCIENCE, V19, P1279, DOI 10.1016/0306-4522(86)90142-9
   Feldman HH, 2010, NEUROLOGY, V74, P956, DOI 10.1212/WNL.0b013e3181d6476a
   GOLDSTEIN JL, 1990, NATURE, V343, P425, DOI 10.1038/343425a0
   Hiura Y, 2010, CIRC J, V74, P518, DOI 10.1253/circj.CJ-09-0790
   Hofman A, 1997, LANCET, V349, P151, DOI 10.1016/S0140-6736(96)09328-2
   HUBBARD K, 1995, EXP CELL RES, V218, P241, DOI 10.1006/excr.1995.1152
   Istvan ES, 2000, EMBO J, V19, P819, DOI 10.1093/emboj/19.5.819
   Jean-Philippe J, 2013, INT J MOL SCI, V14, P18999, DOI 10.3390/ijms140918999
   Jick H, 2000, LANCET, V356, P1627, DOI 10.1016/S0140-6736(00)03155-X
   Johnson JM, 2003, SCIENCE, V302, P2141, DOI 10.1126/science.1090100
   Kalaria RN, 2008, LANCET NEUROL, V7, P812, DOI 10.1016/S1474-4422(08)70169-8
   KAMMA H, 1995, EXP CELL RES, V221, P187, DOI 10.1006/excr.1995.1366
   KHACHATURIAN ZS, 1985, ARCH NEUROL-CHICAGO, V42, P1097, DOI 10.1001/archneur.1985.04060100083029
   KHATOON S, 1992, J NEUROCHEM, V59, P750, DOI 10.1111/j.1471-4159.1992.tb09432.x
   Krauss RM, 2008, CIRCULATION, V117, P1537, DOI 10.1161/CIRCULATIONAHA.107.708388
   Leduc V, 2015, MOL PSYCHIATR, V20, P867, DOI 10.1038/mp.2014.81
   Leduc V, 2016, PHARMACOGENET GENOM, V26, P1, DOI 10.1097/FPC.0000000000000178
   Leduc Valerie, 2011, Int J Alzheimers Dis, V2011, P974361, DOI 10.4061/2011/974361
   Leduc V, 2011, J NEUROSCI METH, V200, P14, DOI 10.1016/j.jneumeth.2011.05.026
   Li G, 2007, NEUROLOGY, V69, P878, DOI 10.1212/01.wnl.0000277657.95487.1c
   Lu YC, 2010, ATHEROSCLEROSIS, V213, P200, DOI 10.1016/j.atherosclerosis.2010.08.053
   Marchant NL, 2013, JAMA NEUROL, V70, P488, DOI 10.1001/2013.jamaneurol.405
   Medina MW, 2008, CIRCULATION, V118, P355, DOI 10.1161/CIRCULATIONAHA.108.773267
   Medina MW, 2011, PLOS ONE, V6, DOI 10.1371/journal.pone.0019420
   Medina MW, 2009, TRENDS CARDIOVAS MED, V19, P173, DOI 10.1016/j.tcm.2009.10.003
   Patry C, 2003, CANCER RES, V63, P7679
   Pino I, 2003, LUNG CANCER-J IASLC, V41, P131, DOI 10.1016/S0169-5002(03)00193-4
   Poirier J, 2005, NEUROBIOL AGING, V26, P355, DOI 10.1016/j.neurobiolaging.2004.09.003
   POIRIER J, 1993, LANCET, V342, P697, DOI 10.1016/0140-6736(93)91705-Q
   Riekse RG, 2006, J ALZHEIMERS DIS, V10, P399
   Rockwood K, 2002, ARCH NEUROL-CHICAGO, V59, P223, DOI 10.1001/archneur.59.2.223
   SAUNDERS AM, 1993, NEUROLOGY, V43, P1467, DOI 10.1212/WNL.43.8.1467
   Shimada N, 2009, RNA BIOL, V6, P293, DOI 10.4161/rna.6.3.8497
   Simmons CR, 2011, MOL NEURODEGENER, V6, DOI 10.1186/1750-1326-6-62
   Spies PE, 2014, CURR ALZHEIMER RES, V11, P40, DOI 10.2174/1567205010666131120101352
   STRITTMATTER WJ, 1993, P NATL ACAD SCI USA, V90, P1977, DOI 10.1073/pnas.90.5.1977
   Thal DR, 2002, NEUROLOGY, V58, P1791, DOI 10.1212/WNL.58.12.1791
   Ushigome M, 2005, INT J ONCOL, V26, P635
   Verdile G, 2004, NEUROLOGY, V63, P1385
   Wolozin B, 2000, ARCH NEUROL-CHICAGO, V57, P1439, DOI 10.1001/archneur.57.10.1439
   Wolozin B, 2007, BMC MED, V5, DOI 10.1186/1741-7015-5-20
   Yu CY, 2014, HUM MOL GENET, V23, P319, DOI 10.1093/hmg/ddt422
   Yu CJ, 2010, BBA-MOL CELL BIOL L, V1801, P819, DOI 10.1016/j.bbalip.2010.05.001
NR 56
TC 9
Z9 9
U1 0
U2 11
PU HUMANA PRESS INC
PI TOTOWA
PA 999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USA
SN 0895-8696
EI 1559-1166
J9 J MOL NEUROSCI
JI J. Mol. Neurosci.
PD JAN
PY 2016
VL 58
IS 1
BP 109
EP 119
DI 10.1007/s12031-015-0666-7
PG 11
WC Biochemistry & Molecular Biology; Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Neurosciences & Neurology
GA DC5RF
UT WOS:000369277400013
PM 26541602
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Wang, W
   Huang, HX
   Hou, DY
   Liu, P
   Wei, H
   Fu, XS
   Niu, WZ
AF Wang, Wei
   Huang, Haixia
   Hou, Dongyan
   Liu, Ping
   Wei, Hua
   Fu, Xiaosuo
   Niu, Weizhen
TI Mechanosensitivity of STREX-lacking BKCa channels in the
   colonic smooth muscle of the mouse
SO AMERICAN JOURNAL OF PHYSIOLOGY-GASTROINTESTINAL AND LIVER PHYSIOLOGY
LA English
DT Article
DE calcium-activated large-conductance potassium channels; Slo I
   alternative splicing; stretch; colon; patch clamp
ID ACTIVATED POTASSIUM CHANNEL; CA2+-ACTIVATED K+ CHANNELS; RAT
   SKELETAL-MUSCLE; LARGE-CONDUCTANCE; MEMBRANE STRETCH; ION CHANNELS;
   NITRIC-OXIDE; MECHANOELECTRIC FEEDBACK; VENTRICULAR MYOCYTES; CALCIUM
AB Stretch sensitivity of Ca2+-activated large-conductance K+ channels (BKCa) has been observed in a variety of cell types and considered to be a potential mechanism in mechanoelectric transduction (MET). Mechanical stress is a major stimulator for the smooth muscle in the gastrointestinal (GI) tract. However, much about the role and mechanism of MET in GI smooth muscles remains unknown. The BKCa shows a functional diversity due to intensive Slo I alternative splicing and different alpha/beta-subunit assembly in various cells. The stress-regulated exon (STREX) insert is suggested to be an indispensable domain for the mechanosensitivity of BKCa. The purpose of this study was to determine whether the BKCa in colonic myocytes of the adult mouse is sensitive to mechanical stimulation and whether the STREX insert is a crucial segment for the BKCa mechanosensitivity. The alpha- and beta 1-subunit mRNAs and the alpha-subunit protein of the BKCa channels were detected in the colonic muscularis. We found that the BKCa STREX-lacking variant was abundantly expressed in the smooth muscle, whereas the STREX variant was not detectable. We demonstrated that the STREX-lacking BKCa channels were also sensitive to membrane stretch. We suggest that in addition to the STREX domain, there are other additional structures in the channel responsible for mechanically coupling with the cell membrane.
C1 [Wang, Wei; Huang, Haixia; Hou, Dongyan; Liu, Ping; Wei, Hua; Fu, Xiaosuo; Niu, Weizhen] Capital Med Univ, Dept Physiol, Beijing 100069, Peoples R China.
C3 Capital Medical University
RP Niu, WZ (corresponding author), Capital Med Univ, Dept Physiol, Beijing 100069, Peoples R China.
EM niuwz@126.com
RI Wang, Yahui/JCO-6233-2023
OI Wang, Wei/0000-0003-1537-8471
FU National Natural Science Foundation of China [30770790, 30800377];
   Beijing Education Committee Foundation [KM200810025016]
FX This work was supported by National Natural Science Foundation of China
   Grants 30770790 and 30800377 and Beijing Education Committee Foundation
   Grant KM200810025016.
CR Allard B, 2000, J BIOL CHEM, V275, P25556, DOI 10.1074/jbc.M002327200
   Brenner R, 2000, NATURE, V407, P870, DOI 10.1038/35038011
   Chanrachakul B, 2003, REPRODUCTION, V126, P43, DOI 10.1530/reprod/126.1.43
   Chatterjee O, 2009, J NEUROENDOCRINOL, V21, P167, DOI 10.1111/j.1365-2826.2009.01823.x
   Chemin J, 2007, PFLUG ARCH EUR J PHY, V455, P97, DOI 10.1007/s00424-007-0250-2
   Chen L, 2005, J BIOL CHEM, V280, P33599, DOI 10.1074/jbc.M505383200
   DAVIDSON RM, 1993, J MEMBRANE BIOL, V131, P81, DOI 10.1007/BF02258536
   DAVIDSON RM, 1990, PFLUG ARCH EUR J PHY, V416, P646, DOI 10.1007/BF00370609
   Dick GM, 1998, AM J PHYSIOL-CELL PH, V275, pC940, DOI 10.1152/ajpcell.1998.275.4.C940
   DOPICO AM, 1994, AM J HYPERTENS, V7, P82, DOI 10.1093/ajh/7.1.82
   Eghbali M, 2003, J BIOL CHEM, V278, P45311, DOI 10.1074/jbc.M306564200
   Farrugia G, 1999, GASTROENTEROLOGY, V117, P900, DOI 10.1016/S0016-5085(99)70349-5
   FERGUSON WB, 1991, J GEN PHYSIOL, V98, P163, DOI 10.1085/jgp.98.1.163
   Franz MR, 2003, PROG BIOPHYS MOL BIO, V82, P163, DOI 10.1016/S0079-6107(03)00013-0
   Gasull X, 2003, INVEST OPHTH VIS SCI, V44, P706, DOI 10.1167/iovs.02-0384
   Gribkoff VK, 2001, NEUROSCIENTIST, V7, P166, DOI 10.1177/107385840100700211
   Honore E, 2006, P NATL ACAD SCI USA, V103, P6859, DOI 10.1073/pnas.0600463103
   Iversen HH, 1997, BRIT J PHARMACOL, V120, P702, DOI 10.1038/sj.bjp.0700967
   KIRBER MT, 1992, FEBS LETT, V297, P24, DOI 10.1016/0014-5793(92)80319-C
   KIRBER MT, 1988, PFLUG ARCH EUR J PHY, V412, P339, DOI 10.1007/BF01907549
   Kiseleva I, 2000, CARDIOVASC RES, V45, P370, DOI 10.1016/S0008-6363(99)00361-2
   Koh SD, 2001, J PHYSIOL-LONDON, V533, P155, DOI 10.1111/j.1469-7793.2001.0155b.x
   Koh SD, 2001, J BIOL CHEM, V276, P44338, DOI 10.1074/jbc.M108125200
   Lab MJ, 1996, CARDIOVASC RES, V32, P1
   Lai GJ, 2006, ENDOCRINOLOGY, V147, P3961, DOI 10.1210/en.2005-1551
   MacDonald SHF, 2006, BMC DEV BIOL, V6, DOI 10.1186/1471-213X-6-37
   Mahmoud SF, 2004, J NEUROENDOCRINOL, V16, P237, DOI 10.1111/j.0953-8194.2004.01154.x
   Mallouk N, 2000, AM J PHYSIOL-CELL PH, V278, pC473, DOI 10.1152/ajpcell.2000.278.3.C473
   MCMANUS OB, 1991, J PHYSIOL-LONDON, V443, P739, DOI 10.1113/jphysiol.1991.sp018861
   Mienville JM, 1996, J MEMBRANE BIOL, V153, P211, DOI 10.1007/s002329900124
   Morton MJ, 2004, J AM SOC NEPHROL, V15, P2981, DOI 10.1097/01.ASN.0000145046.24268.0D
   Naruse K, 2009, BIOCHEM BIOPH RES CO, V385, P634, DOI 10.1016/j.bbrc.2009.05.105
   Nishimura S, 2008, PROG BIOPHYS MOL BIO, V97, P282, DOI 10.1016/j.pbiomolbio.2008.02.011
   PACHA J, 1991, AM J PHYSIOL, V261, pF696, DOI 10.1152/ajprenal.1991.261.4.F696
   Patton C, 2004, CELL CALCIUM, V35, P427, DOI 10.1016/j.ceca.2003.10.006
   Poulsen AN, 2009, BBA-BIOMEMBRANES, V1788, P380, DOI 10.1016/j.bbamem.2008.10.001
   Qi Z, 2005, MOL MEMBR BIOL, V22, P519, DOI 10.1080/09687860500370703
   ROBITAILLE R, 1992, J NEUROSCI, V12, P297
   Sachs F, 1998, REV PHYSIOL BIOCH P, V132, P1, DOI 10.1007/BFb0004985
   Saffitz JE, 2004, CIRC RES, V94, P585, DOI 10.1161/01.RES.0000121575.34653.50
   Sanders KM, 2006, J PHYSIOL-LONDON, V570, P37, DOI 10.1113/jphysiol.2005.098897
   Shuttleworth CWR, 1996, P SOC EXP BIOL MED, V211, P16, DOI 10.3181/00379727-211-43950C
   SINGER JJ, 1987, PFLUG ARCH EUR J PHY, V408, P98, DOI 10.1007/BF00581337
   Suchyna TM, 2007, J PHYSIOL-LONDON, V581, P369, DOI 10.1113/jphysiol.2006.125021
   Tang QY, 2003, J MEMBRANE BIOL, V196, P185, DOI 10.1007/s00232-003-0637-8
   Tian LJ, 2008, P NATL ACAD SCI USA, V105, P21006, DOI 10.1073/pnas.0806700106
   Tian LJ, 2001, J BIOL CHEM, V276, P7717, DOI 10.1074/jbc.C000741200
   Uebele VN, 2000, J BIOL CHEM, V275, P23211, DOI 10.1074/jbc.M910187199
   Vergara C, 1999, J GEN PHYSIOL, V114, P365, DOI 10.1085/jgp.114.3.365
   Wu SN, 2003, J CARDIOVASC ELECTR, V14, P44, DOI 10.1046/j.1540-8167.2003.02040.x
   Wulf H, 2009, J MOL HISTOL, V40, P87, DOI 10.1007/s10735-009-9216-3
   Xie JY, 1998, SCIENCE, V280, P443, DOI 10.1126/science.280.5362.443
   Zhang YX, 2006, J GEN PHYSIOL, V128, P185, DOI 10.1085/jgp.200609493
   Zhao HC, 2008, CELL RES, V18, P871, DOI 10.1038/cr.2008.88
NR 54
TC 32
Z9 35
U1 0
U2 14
PU AMER PHYSIOLOGICAL SOC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA
SN 0193-1857
J9 AM J PHYSIOL-GASTR L
JI Am. J. Physiol.-Gastroint. Liver Physiol.
PD DEC
PY 2010
VL 299
IS 6
BP G1231
EP G1240
DI 10.1152/ajpgi.00268.2010
PG 10
WC Gastroenterology & Hepatology; Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Gastroenterology & Hepatology; Physiology
GA 688QV
UT WOS:000284867600003
PM 20864656
DA 2025-04-10
ER

PT J
AU Hashimoto, K
   Ishida, E
   Miura, A
   Ozawa, A
   Shibusawa, N
   Satoh, T
   Okada, S
   Yamada, M
   Mori, M
AF Hashimoto, Koshi
   Ishida, Emi
   Miura, Atsuko
   Ozawa, Atsushi
   Shibusawa, Nobuyuki
   Satoh, Tetsurou
   Okada, Shuichi
   Yamada, Masanobu
   Mori, Masatomo
TI A liver X receptor (LXR)-β alternative splicing variant (LXRBSV) is
   preferentially expressed in the pituitary
SO BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
LA English
DT Article
DE LXR-beta; LXRBSV; Gene regulation; 5 '-RACE
ID THYROID-HORMONE; CHOLESTEROL HOMEOSTASIS; GENE-EXPRESSION;
   TRANSCRIPTION; PROMOTERS; PATHWAYS
AB We have recently reported that an alternative splicing variant of liver X receptor (LXR)-beta acts as an RNA co-activator, which is referred to as LXRBSV The in vivo role of LXRBSV is yet to be clarified The LXRBSV gene is expressed in various tissues including the liver and brain We evaluated the gene expression of LXRBSV in various regions of the brain using real-time quantitative PR assays in the current study and found that LXRBSV is abundantly expressed in the pituitary 5'-rapid amplification of cDNA ends (5'-RACE) revealed that the transcriptional start site (TSS) of LXRBSV is located 40 base pairs (bp) downstream of LXR-beta We prepared two promoter constructs -1598/+35 bp and -15981+75 bp in pGL4 for LXR-beta and LXRBSV, respectively The latter promoter construct demonstrated significantly higher activity than the former construct in GH3 cells derived from the rat pituitary On the contrary, the promoter activities of these two constructs were indistinguishable in Hepa 1-6 cells derived from mouse hepatocytes Furthermore, the promoter region specific for LXRBSV itself exerted promoter activity in GH3 cells but not in Hepa 1-6 cells Taken together, we have concluded that LXRBSV is preferentially transcribed and expressed in the pituitary, indicating that LXRBSV plays a role in regulating pituitary gene expression These data provide clues to elucidating the physiological relevance of LXRBSV (C) 2010 Elsevier Inc All rights reserved
C1 [Hashimoto, Koshi; Ishida, Emi; Miura, Atsuko; Ozawa, Atsushi; Shibusawa, Nobuyuki; Satoh, Tetsurou; Okada, Shuichi; Yamada, Masanobu; Mori, Masatomo] Gunma Univ, Grad Sch Med, Dept Med & Mol Sci, Gunma 3718511, Japan.
C3 Gunma University
RP Hashimoto, K (corresponding author), Gunma Univ, Grad Sch Med, Dept Med & Mol Sci, 3-39-15 Showa Machi Maebashi, Gunma 3718511, Japan.
RI Hashimoto, Koshi/AAL-7339-2020
FU Kowa Life Foundation
FX This work was supported by a grant from Kowa Life Foundation (to K H.).
CR Allemand E, 2008, CURR OPIN GENET DEV, V18, P145, DOI 10.1016/j.gde.2008.01.006
   APFEL R, 1994, MOL CELL BIOL, V14, P7025, DOI 10.1128/MCB.14.10.7025
   Blencowe BJ, 2006, CELL, V126, P37, DOI 10.1016/j.cell.2006.06.023
   Cramer P, 1999, MOL CELL, V4, P251, DOI 10.1016/S1097-2765(00)80372-X
   Cramer P, 1997, P NATL ACAD SCI USA, V94, P11456, DOI 10.1073/pnas.94.21.11456
   DAVIS CMW, 2008, BREAST CANCER RES, V10, P207
   Gabbi C, 2009, MOL ENDOCRINOL, V23, P129, DOI 10.1210/me.2008-0398
   Hashimoto K, 2006, J BIOL CHEM, V281, P295, DOI 10.1074/jbc.M507877200
   Hashimoto K, 2009, BIOCHEM BIOPH RES CO, V390, P1260, DOI 10.1016/j.bbrc.2009.10.132
   Hashimoto K, 2009, ENDOCRINOLOGY, V150, P3417, DOI 10.1210/en.2009-0059
   Horiguchi K, 2009, CLIN CANCER RES, V15, P2620, DOI 10.1158/1078-0432.CCR-08-2473
   Joseph SB, 2003, NAT MED, V9, P213, DOI 10.1038/nm820
   Kornblihtt AR, 2005, CURR OPIN CELL BIOL, V17, P262, DOI 10.1016/j.ceb.2005.04.014
   Neugebauer KM, 2002, J CELL SCI, V115, P3865, DOI 10.1242/jcs.00073
   Repa JJ, 2000, ANNU REV CELL DEV BI, V16, P459, DOI 10.1146/annurev.cellbio.16.1.459
   Satoh T, 2009, BIOCHEM BIOPH RES CO, V389, P673, DOI 10.1016/j.bbrc.2009.09.056
   SISODIA SS, 1987, MOL CELL BIOL, V7, P3602, DOI 10.1128/MCB.7.10.3602
   SMALE ST, 1985, MOL CELL BIOL, V5, P352, DOI 10.1128/MCB.5.2.352
   Stulnig TM, 2002, MOL PHARMACOL, V62, P1299, DOI 10.1124/mol.62.6.1299
   Tomaru T, 2006, ENDOCRINOLOGY, V147, P377, DOI 10.1210/en.2005-0450
   Whitney KD, 2002, MOL ENDOCRINOL, V16, P1378, DOI 10.1210/me.16.6.1378
   WILLY PJ, 1995, GENE DEV, V9, P1033, DOI 10.1101/gad.9.9.1033
   Zavolan M, 2003, GENOME RES, V13, P1290, DOI 10.1101/gr.1017303
   Zelcer N, 2006, J CLIN INVEST, V116, P607, DOI 10.1172/JCI27883
NR 24
TC 1
Z9 2
U1 0
U2 2
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0006-291X
J9 BIOCHEM BIOPH RES CO
JI Biochem. Biophys. Res. Commun.
PD APR 9
PY 2010
VL 394
IS 3
BP 548
EP 552
DI 10.1016/j.bbrc.2010.03.013
PG 5
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA 584WY
UT WOS:000276785900020
PM 20211147
DA 2025-04-10
ER

PT J
AU Hu, RG
   Brower, CS
   Wang, HQ
   Davydov, IV
   Sheng, J
   Zhou, JM
   Kwon, YT
   Varshavsky, A
AF Hu, Rong-Gui
   Brower, Christopher S.
   Wang, Haiqing
   Davydov, Ilia V.
   Sheng, Jun
   Zhou, Jianmin
   Kwon, Yong Tae
   Varshavsky, Alexander
TI Arginyltransferase, its specificity, putative substrates, bidirectional
   promoter, and splicing-derived isoforms
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID N-END RULE; RNA-PROTEIN TRANSFERASE; E3 UBIQUITIN LIGASES; MICE LACKING;
   SUBCELLULAR-LOCALIZATION; COHESIN SUBUNIT; PATHWAY; GENE; DEGRADATION;
   PROTEASOME
AB Substrates of the N-end rule pathway include proteins with destabilizing N-terminal residues. Three of them, Asp, Glu, and (oxidized) Cys, function through their conjugation to Arg, one of destabilizing N-terminal residues that are recognized directly by the pathway's ubiquitin ligases. The conjugation of Arg is mediated by arginyltransferase, encoded by ATE1. Through its regulated degradation of specific proteins, the arginylation branch of the N-end rule pathway mediates, in particular, the cardiovascular development, the fidelity of chromosome segregation, and the control of signaling by nitric oxide. We show that mouse ATE1 specifies at least six mRNA isoforms, which are produced through alternative splicing, encode enzymatically active arginyltransferases, and are expressed at varying levels in mouse tissues. We also show that the ATE1 promoter is bidirectional, mediating the expression of both ATE1 and an oppositely oriented, previously uncharacterized gene. In addition, we identified GRP78 (glucose-regulated protein 78) and protein-disulfide isomerase as putative physiological substrates of arginyltransferase. Purified isoforms of arginyltransferase that contain the alternative first exons differentially arginylate these proteins in extract from ATE1(-/-) embryos, suggesting that specific isoforms may have distinct functions. Although the N-end rule pathway is apparently confined to the cytosol and the nucleus, and although GRP78 and protein-disulfide isomerase are located largely in the endoplasmic reticulum, recent evidence suggests that these proteins are also present in the cytosol and other compartments in vivo, where they may become N-end rule substrates.
C1 CALTECH, Div Biol, Pasadena, CA 91125 USA.
   Meso Scale Discovery, Gaithersburg, MD 20877 USA.
   Univ Pittsburgh, Sch Pharm, Ctr Pharmacogenet, Pittsburgh, PA 15261 USA.
   Univ Pittsburgh, Sch Pharm, Dept Pharmaceut Sci, Pittsburgh, PA 15261 USA.
C3 California Institute of Technology; Pennsylvania Commonwealth System of
   Higher Education (PCSHE); University of Pittsburgh; Pennsylvania
   Commonwealth System of Higher Education (PCSHE); University of
   Pittsburgh
RP Varshavsky, A (corresponding author), CALTECH, Div Biol, Pasadena, CA 91125 USA.
EM avarsh@caltech.edu
RI Zhou, jinamin/HPH-4897-2023
FU NIDDK NIH HHS [DK 39520] Funding Source: Medline; NIGMS NIH HHS [GM
   31530, GM 074000, GM 069482] Funding Source: Medline
CR Adachi N, 2002, CELL, V109, P807, DOI 10.1016/S0092-8674(02)00758-4
   An JY, 2006, P NATL ACAD SCI USA, V103, P6212, DOI 10.1073/pnas.0601700103
   Ardley HC, 2005, ESSAYS BIOCHEM, V41, P15, DOI 10.1042/EB0410015
   Ausubel F.M., 2002, CURRENT PROTOCOLS MO
   BACHMAIR A, 1989, CELL, V56, P1019, DOI 10.1016/0092-8674(89)90635-1
   BACHMAIR A, 1986, SCIENCE, V234, P179, DOI 10.1126/science.3018930
   Baker R T., 1991, Proc. Natl. Acad. Sci. USA, V87, P2374
   BAKER RT, 1995, J BIOL CHEM, V270, P12065, DOI 10.1074/jbc.270.20.12065
   BALZI E, 1990, J BIOL CHEM, V265, P7464
   Baumeister W, 1998, CELL, V92, P367, DOI 10.1016/S0092-8674(00)80929-0
   Bradshaw RA, 1998, TRENDS BIOCHEM SCI, V23, P263, DOI 10.1016/S0968-0004(98)01227-4
   Cardozo T, 2004, NAT REV MOL CELL BIO, V5, P739, DOI 10.1038/nrm1471
   Collins GA, 2006, CURR OPIN GENET DEV, V16, P197, DOI 10.1016/j.gde.2006.02.009
   Davydov IV, 2000, J BIOL CHEM, V275, P22931, DOI 10.1074/jbc.M001605200
   Ditzel M, 2003, NAT CELL BIOL, V5, P467, DOI 10.1038/ncb984
   Du FY, 2002, P NATL ACAD SCI USA, V99, P14110, DOI 10.1073/pnas.172527399
   Elsasser S, 2005, NAT CELL BIOL, V7, P742, DOI 10.1038/ncb0805-742
   Emoto M, 2005, GENE, V357, P47, DOI 10.1016/j.gene.2005.05.009
   Erbse A, 2006, NATURE, V439, P753, DOI 10.1038/nature04412
   Fang S, 2004, CELL MOL LIFE SCI, V61, P1546, DOI 10.1007/s00018-004-4129-5
   FINLEY D, 1989, NATURE, V338, P394, DOI 10.1038/338394a0
   FIRE A, 2006, Q REV BIOPHYS, V6, P1
   Ghislain M, 1996, EMBO J, V15, P4884, DOI 10.1002/j.1460-2075.1996.tb00869.x
   GLOTZER M, 1991, NATURE, V349, P132, DOI 10.1038/349132a0
   GONDA DK, 1989, J BIOL CHEM, V264, P16700
   Graciet E, 2006, P NATL ACAD SCI USA, V103, P3078, DOI 10.1073/pnas.0511224103
   Grune T, 2002, ARCH BIOCHEM BIOPHYS, V397, P407, DOI 10.1006/abbi.2001.2719
   Hauf S, 2001, SCIENCE, V293, P1320, DOI 10.1126/science.1061376
   Hershko A, 2000, NAT MED, V6, P1073, DOI 10.1038/80384
   Hochstrasser M, 2006, CELL, V124, P27, DOI 10.1016/j.cell.2005.12.025
   Hu RG, 2005, NATURE, V437, P981, DOI 10.1038/nature04027
   JOHNSON ES, 1990, NATURE, V346, P287, DOI 10.1038/346287a0
   JOHNSON ES, 1992, EMBO J, V11, P497, DOI 10.1002/j.1460-2075.1992.tb05080.x
   Kwon YT, 2003, MOL CELL BIOL, V23, P8255, DOI 10.1128/MCB.23.22.8255-8271.2003
   Kwon YT, 2000, MOL CELL BIOL, V20, P4135, DOI 10.1128/MCB.20.11.4135-4148.2000
   Kwon YT, 1999, MOL CELL BIOL, V19, P182
   Kwon YT, 2002, SCIENCE, V297, P96, DOI 10.1126/science.1069531
   Kwon YT, 2001, MOL CELL BIOL, V21, P8007, DOI 10.1128/MCB.21.23.8007-8021.2001
   Lareau LF, 2004, CURR OPIN STRUC BIOL, V14, P273, DOI 10.1016/j.sbi.2004.05.002
   Lee MJ, 2005, P NATL ACAD SCI USA, V102, P15030, DOI 10.1073/pnas.0507533102
   Lev-Maor G, 2003, SCIENCE, V300, P1288, DOI 10.1126/science.1082588
   LI J, 1995, BIOCHEMISTRY-US, V34, P15829, DOI 10.1021/bi00048a028
   Lynch M, 2006, SCIENCE, V311, P1727, DOI 10.1126/science.1118884
   Maniatis T, 2002, NATURE, V418, P236, DOI 10.1038/418236a
   Meier-Noorden M, 2004, GENE, V338, P197, DOI 10.1016/j.gene.2004.05.006
   MUMBERG D, 1994, NUCLEIC ACIDS RES, V22, P5767, DOI 10.1093/nar/22.25.5767
   Patton J, 2006, GENE, V369, P35, DOI 10.1016/j.gene.2005.10.009
   Peters JM, 2002, MOL CELL, V9, P931, DOI 10.1016/S1097-2765(02)00540-3
   Petroski MD, 2005, NAT REV MOL CELL BIO, V6, P9, DOI 10.1038/nrm1547
   Pickart CM, 2004, CELL, V116, P181, DOI 10.1016/S0092-8674(03)01074-2
   Prakash S, 2004, NAT STRUCT MOL BIOL, V11, P830, DOI 10.1038/nsmb814
   Preger E, 2004, P NATL ACAD SCI USA, V101, P1229, DOI 10.1073/pnas.0307952100
   Rai R, 2005, P NATL ACAD SCI USA, V102, P10123, DOI 10.1073/pnas.0504500102
   Rao H, 2001, NATURE, V410, P955, DOI 10.1038/35073627
   Rape M, 2002, NAT CELL BIOL, V4, pE113, DOI 10.1038/ncb0502-e113
   Rechsteiner M, 2005, TRENDS CELL BIOL, V15, P27, DOI 10.1016/j.tcb.2004.11.003
   Saleh A, 2004, IMMUNITY, V21, P55, DOI 10.1016/j.immuni.2004.06.005
   Schnell JD, 2003, J BIOL CHEM, V278, P35857, DOI 10.1074/jbc.R300018200
   Schröder M, 2005, ANNU REV BIOCHEM, V74, P739, DOI 10.1146/annurev.biochem.73.011303.074134
   Sheng J, 2002, EMBO J, V21, P6061, DOI 10.1093/emboj/cdf626
   SHRADER TE, 1993, J BACTERIOL, V175, P4364, DOI 10.1128/JB.175.14.4364-4374.1993
   Siepmann TJ, 2003, J BIOL CHEM, V278, P9448, DOI 10.1074/jbc.M211240200
   Stetefeld J, 2005, TRENDS BIOCHEM SCI, V30, P515, DOI 10.1016/j.tibs.2005.07.001
   Stockton JD, 2003, BIOCHEMISTRY-US, V42, P12821, DOI 10.1021/bi035087q
   Sun FC, 2006, BIOCHEM J, V396, P31, DOI 10.1042/BJ20051916
   Suzuki T, 1999, EMBO J, V18, P6017, DOI 10.1093/emboj/18.21.6017
   Takai D, 2004, MOL BIOL EVOL, V21, P463, DOI 10.1093/molbev/msh040
   Tasaki T, 2005, MOL CELL BIOL, V25, P7120, DOI 10.1128/MCB.25.16.7120-7136.2005
   TOBIAS JW, 1991, SCIENCE, V254, P1374, DOI 10.1126/science.1962196
   Travers MT, 2005, GENOMICS, V85, P71, DOI 10.1016/j.ygeno.2004.10.001
   Trinklein ND, 2004, GENOME RES, V14, P62, DOI 10.1101/gr.1982804
   Trotter KW, 1999, J CELL BIOL, V147, P1481, DOI 10.1083/jcb.147.7.1481
   Turano C, 2002, J CELL PHYSIOL, V193, P154, DOI 10.1002/jcp.10172
   Turner GC, 2000, NATURE, V405, P579, DOI 10.1038/35014629
   Uhlmann F, 1999, NATURE, V400, P37, DOI 10.1038/21831
   Varshavsky A, 2003, NAT CELL BIOL, V5, P373, DOI 10.1038/ncb0503-373
   Varshavsky A, 1996, P NATL ACAD SCI USA, V93, P12142, DOI 10.1073/pnas.93.22.12142
   Varshavsky A, 2005, METHOD ENZYMOL, V399, P777, DOI 10.1016/S0076-6879(05)99051-4
   Varshavsky A, 2004, CURR BIOL, V14, pR181, DOI 10.1016/j.cub.2004.02.014
   Varshavsky AV, 2006, PROTEIN SCI, V15, P647, DOI 10.1110/ps.052012306
   Vendel AC, 2006, J NEUROSCI, V26, P2635, DOI 10.1523/JNEUROSCI.0067-06.2006
   Whitehouse C, 2004, GENE, V326, P87, DOI 10.1016/j.gene.2003.10.008
   Wilkinson B, 2004, BBA-PROTEINS PROTEOM, V1699, P35, DOI 10.1016/j.bbapap.2004.02.017
   Wolf DH, 2004, BBA-MOL CELL RES, V1695, P19, DOI 10.1016/j.bbamcr.2004.10.007
   Xie YM, 1999, EMBO J, V18, P6832, DOI 10.1093/emboj/18.23.6832
   Yoshida S, 2002, PLANT J, V32, P129, DOI 10.1046/j.1365-313X.2002.01407.x
   Zenker M, 2005, NAT GENET, V37, P1345, DOI 10.1038/ng1681
NR 87
TC 62
Z9 74
U1 0
U2 11
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI ROCKVILLE
PA 11200 ROCKVILLE PIKE, SUITE 302, ROCKVILLE, MD, UNITED STATES
SN 0021-9258
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD OCT 27
PY 2006
VL 281
IS 43
BP 32559
EP 32573
DI 10.1074/jbc.M604355200
PG 15
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 096ZB
UT WOS:000241414500054
PM 16943202
OA hybrid, Green Accepted
DA 2025-04-10
ER

PT J
AU Ogut, O
   Jin, JP
AF Ogut, O
   Jin, JP
TI Developmentally regulated, alternative RNA splicing-generated pectoral
   muscle-specific troponin T isoforms and role of the
   NH2-terminal hypervariable region in the tolerance to
   acidosis
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID COMPLETE NUCLEOTIDE-SEQUENCE; METAL-BINDING CLUSTER; HYPERTROPHIC
   CARDIOMYOPATHY; ALPHA-TROPOMYOSIN; ADULT ISOFORMS; F-ACTIN;
   NONPOLYMERIZABLE TROPOMYOSIN; CA2+ SENSITIVITY; DIABETIC RAT; GENE
AB The structure-function relationship of the alternative RNA splicing-generated NH2-terminal variable region of troponin T (TnT) is essential for understanding the physiological significance of developmental or muscle-specific TnT isoforms, Representing the hypervariable nature of the NH2-terminal region, a repeating transition metal-binding sequence (H(E/A)EAH)(4-7) (Tx) has been found in chicken fast skeletal muscle TnT, In the present study, the developmentally regulated pectoral muscle-specific expression of this novel TnT isoform has been characterized. It was found that the variable amino terminus determined the isoelectric points of the TnT isoforms expressed, and the adult muscle-specific inclusion of the Tx sequence resulted in pectoralis TnTs, which were significantly more acidic in their NH2-terminal segment versus gastrocnemius TnTs, Experiments testing the effect of pH on TnT interaction with troponin I and tropomyosin indicated that although the interaction of acidic TnT isoforms with troponin I was less sensitive to the decrease of pH than the basic TnTs, the binding affinity of acidic TnT isoforms with tropomyosin was minimally affected by the decreased pH in contrast to basic TnT isoforms, Given that the majority of adult skeletal muscles express basic fast TnT isoforms, the switching between acidic and basic TnT isoforms may play a role in the functional adaptation of muscle to acidosis.
C1 Case Western Reserve Univ, Sch Med, Dept Physiol & Biophys, Cleveland, OH 44106 USA.
C3 University System of Ohio; Case Western Reserve University
RP Case Western Reserve Univ, Sch Med, Dept Physiol & Biophys, 10900 Euclid Ave, Cleveland, OH 44106 USA.
EM jxj12@po.cwru.edu
RI Jin, Jian-Ping/AAD-1149-2020
OI Jin, JP/0000-0001-9932-1063
CR AKELLA AB, 1995, CIRC RES, V76, P600, DOI 10.1161/01.RES.76.4.600
   ANDERSON PAW, 1995, CIRC RES, V76, P681, DOI 10.1161/01.RES.76.4.681
   BREITBART RE, 1986, J MOL BIOL, V188, P313, DOI 10.1016/0022-2836(86)90157-9
   BRIGGS MM, 1993, DEV BIOL, V158, P503, DOI 10.1006/dbio.1993.1208
   COOPER TA, 1985, J BIOL CHEM, V260, P1140
   FABIATO A, 1978, J PHYSIOL-LONDON, V276, P233, DOI 10.1113/jphysiol.1978.sp012231
   GAHLMANN R, 1987, J BIOL CHEM, V262, P16122
   GODT RE, 1991, CAN J PHYSIOL PHARM, V69, P1692, DOI 10.1139/y91-251
   Hastings KEM, 1997, CELL STRUCT FUNCT, V22, P205, DOI 10.1247/csf.22.205
   HEELEY DH, 1987, J BIOL CHEM, V262, P9971
   Jha PK, 1996, BIOCHEMISTRY-US, V35, P16573, DOI 10.1021/bi9622433
   JIN J-P, 1991, Journal of Cell Biology, V115, p180A
   JIN JP, 1990, ANN NY ACAD SCI, V588, P393, DOI 10.1111/j.1749-6632.1990.tb13243.x
   JIN JP, 1994, FEBS LETT, V341, P135, DOI 10.1016/0014-5793(94)80256-4
   Jin JP, 1998, GENE, V214, P121, DOI 10.1016/S0378-1119(98)00214-5
   JIN JP, 1988, J BIOL CHEM, V263, P7309
   JIN JP, 1992, J MOL BIOL, V227, P1269, DOI 10.1016/0022-2836(92)90540-Z
   JIN JP, 1995, J BIOL CHEM, V270, P6908
   JIN JP, 1989, J BIOL CHEM, V264, P14471
   LAGADICGOSSMANN D, 1990, J PHYSIOL-LONDON, V422, P481, DOI 10.1113/jphysiol.1990.sp017996
   LEAVIS PC, 1984, CRC CR REV BIOCH MOL, V16, P235, DOI 10.3109/10409238409108717
   Lin D, 1996, J CLIN INVEST, V97, P2842, DOI 10.1172/JCI118740
   LIN JJC, 1985, HYBRIDOMA, V4, P223, DOI 10.1089/hyb.1985.4.223
   Luo Y, 1997, BIOCHEMISTRY-US, V36, P11027, DOI 10.1021/bi962461w
   MAK AS, 1983, J BIOL CHEM, V258, P4330
   Malnic B, 1998, J BIOL CHEM, V273, P10594, DOI 10.1074/jbc.273.17.10594
   METZGER JM, 1993, P NATL ACAD SCI USA, V90, P9036, DOI 10.1073/pnas.90.19.9036
   NAKANISHI T, 1985, PEDIATR RES, V19, P482, DOI 10.1203/00006450-198505000-00015
   Nickel R., 1977, ANATOMY DOMESTIC BIR
   OFARRELL PZ, 1977, CELL, V12, P1133, DOI 10.1016/0092-8674(77)90176-3
   Ogut O, 1996, BIOCHEMISTRY-US, V35, P16581, DOI 10.1021/bi961712y
   PAN BS, 1991, J BIOL CHEM, V266, P12432
   PEARLSTONE JR, 1977, J BIOL CHEM, V252, P971
   PEARLSTONE JR, 1982, J BIOL CHEM, V257, P587
   SCHACHAT F, 1995, DEV BIOL, V171, P233, DOI 10.1006/dbio.1995.1274
   Schaertl S, 1995, BIOCHEMISTRY-US, V34, P15890, DOI 10.1021/bi00049a003
   SHENG ZL, 1992, J BIOL CHEM, V267, P25407
   Smillie L.B., 1996, BIOCH SMOOTH MUSCLE, P63
   SMILLIE LB, 1988, J BIOL CHEM, V263, P18816
   SMILLIE LB, 1982, METHOD ENZYMOL, V85, P234
   SOLARO RJ, 1988, CIRC RES, V63, P779, DOI 10.1161/01.RES.63.4.779
   THIERFELDER L, 1994, CELL, V77, P701, DOI 10.1016/0092-8674(94)90054-X
   TOBACMAN LS, 1987, J BIOL CHEM, V262, P4059
   Tobacman LS, 1996, ANNU REV PHYSIOL, V58, P447, DOI 10.1146/annurev.ph.58.030196.002311
   Wang J, 1997, GENE, V193, P105, DOI 10.1016/S0378-1119(97)00100-5
   WANG J, 1998, IN PRESS BIOCHEMISTR, V38
   WATKINS H, 1995, NEW ENGL J MED, V332, P1058, DOI 10.1056/NEJM199504203321603
   WHITE SP, 1987, NATURE, V325, P826, DOI 10.1038/325826a0
   ZOT AS, 1987, ANNU REV BIOPHYS BIO, V16, P535
NR 49
TC 46
Z9 51
U1 0
U2 1
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
SN 0021-9258
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD OCT 23
PY 1998
VL 273
IS 43
BP 27858
EP 27866
DI 10.1074/jbc.273.43.27858
PG 9
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 130ZD
UT WOS:000076549800016
PM 9774396
OA hybrid
DA 2025-04-10
ER

PT J
AU Levine, SJ
AF Levine, Stewart J.
TI Molecular mechanisms of soluble cytokine receptor generation
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Review
ID ALPHA-CONVERTING-ENZYME; NECROSIS-FACTOR-ALPHA; MESSENGER-RNA;
   GROWTH-FACTOR; TRANSMEMBRANE CHEMOKINES; INTERLEUKIN-6 RECEPTOR;
   CELLULAR CHOLESTEROL; PROTEOLYTIC ACTIVITY; BINDING-PROTEIN; TNF
   RECEPTOR
AB Soluble cytokine receptors play key roles in regulating cytokine-mediated biological events by binding and modulating the activity of target ligands in either an antagonistic or agonistic fashion. This Minireview will provide an overview of the molecular mechanisms mediating the generation of soluble cytokine receptors, which include sheddase-mediated proteolytic cleavage of cell-surface receptors, generation of soluble receptors by alternative gene splicing, transcription and translation of cytokine-binding genes, and extracellular release of membrane-bound receptors within vesicles such as exosomes.
C1 NHLBI, NIH, Pulm & Vasc Med Branch, Bethesda, MD 20892 USA.
C3 National Institutes of Health (NIH) - USA; NIH National Heart Lung &
   Blood Institute (NHLBI)
RP Levine, SJ (corresponding author), NHLBI, NIH, Pulm & Vasc Med Branch, Bldg 10, Bethesda, MD 20892 USA.
EM levines@nhlbi.nih.gov
FU Intramural NIH HHS Funding Source: Medline
CR Alcami A, 2003, NAT REV IMMUNOL, V3, P36, DOI 10.1038/nri980
   Alejo A, 2006, P NATL ACAD SCI USA, V103, P5995, DOI 10.1073/pnas.0510462103
   Baj-Krzyworzeka M, 2006, CANCER IMMUNOL IMMUN, V55, P808, DOI 10.1007/s00262-005-0075-9
   BERGERS G, 1994, EMBO J, V13, P1176, DOI 10.1002/j.1460-2075.1994.tb06367.x
   Black RA, 1997, NATURE, V385, P729, DOI 10.1038/385729a0
   Black RA, 2004, NAT GENET, V36, P934, DOI 10.1038/ng0904-934
   Black RA, 2002, INT J BIOCHEM CELL B, V34, P1, DOI 10.1016/S1357-2725(01)00097-8
   Blobel CP, 2005, NAT REV MOL CELL BIO, V6, P32, DOI 10.1038/nrm1548
   Borroto A, 2003, J BIOL CHEM, V278, P25933, DOI 10.1074/jbc.M301673200
   Bucay N, 1998, GENE DEV, V12, P1260, DOI 10.1101/gad.12.9.1260
   Bufler P, 2004, BIOCHEM J, V381, P503, DOI 10.1042/BJ20040217
   Bulanova E, 2007, J BIOL CHEM, V282, P13167, DOI 10.1074/jbc.M610036200
   Canault M, 2006, J CELL PHYSIOL, V208, P363, DOI 10.1002/jcp.20671
   Cui XL, 2002, J CLIN INVEST, V110, P515, DOI 10.1172/JCI200213847
   Diveu C, 2006, J BIOL CHEM, V281, P36673, DOI 10.1074/jbc.M607005200
   Doedens JR, 2000, J BIOL CHEM, V275, P14598, DOI 10.1074/jbc.275.19.14598
   Doedens JR, 2003, BIOCHEM BIOPH RES CO, V308, P331, DOI 10.1016/S0006-291X(03)01381-0
   Eichenauer DA, 2007, CANCER RES, V67, P332, DOI 10.1158/0008-5472.CAN-06-2470
   Elson GCA, 1998, J IMMUNOL, V161, P1371
   Fantuzzi G, 2003, J LEUKOCYTE BIOL, V74, P889, DOI 10.1189/jlb.0503230
   Garton KJ, 2006, J LEUKOCYTE BIOL, V79, P1105, DOI 10.1189/jlb.0106038
   Gómez MI, 2007, EMBO J, V26, P701, DOI 10.1038/sj.emboj.7601554
   Gonzales PE, 2004, J BIOL CHEM, V279, P31638, DOI 10.1074/jbc.M401311200
   Hansen HP, 2004, FASEB J, V18, P893, DOI 10.1096/fj.03-0901fje
   Hawari FI, 2004, P NATL ACAD SCI USA, V101, P1297, DOI 10.1073/pnas.0307981100
   Hinkle CL, 2004, J BIOL CHEM, V279, P24179, DOI 10.1074/jbc.M312141200
   Ho CH, 2007, J VIROL, V81, P4837, DOI 10.1128/JVI.02448-06
   Hundhausen C, 2007, J IMMUNOL, V178, P8064, DOI 10.4049/jimmunol.178.12.8064
   Huovila APJ, 2005, TRENDS BIOCHEM SCI, V30, P413, DOI 10.1016/j.tibs.2005.05.006
   Islam A, 2006, J BIOL CHEM, V281, P6860, DOI 10.1074/jbc.M509397200
   Islam A, 2007, J BIOL CHEM, V282, P9591, DOI 10.1074/jbc.M607122200
   Jostock T, 2001, EUR J BIOCHEM, V268, P160, DOI 10.1046/j.1432-1327.2001.01867.x
   Kawaguchi N, 2007, J CELL SCI, V120, P943, DOI 10.1242/jcs.03403
   Kim SH, 2000, P NATL ACAD SCI USA, V97, P1190, DOI 10.1073/pnas.97.3.1190
   Kuhn PH, 2007, J BIOL CHEM, V282, P11982, DOI 10.1074/jbc.M700356200
   Lainez B, 2004, INT IMMUNOL, V16, P169, DOI 10.1093/intimm/dxh014
   Lambert MH, 2005, COMB CHEM HIGH T SCR, V8, P327, DOI 10.2174/1386207054020840
   Leonard JD, 2005, BIOCHEM J, V387, P797, DOI 10.1042/BJ20041727
   Levine SJ, 2004, J IMMUNOL, V173, P5343, DOI 10.4049/jimmunol.173.9.5343
   MacKenzie A, 2001, IMMUNITY, V15, P825, DOI 10.1016/S1074-7613(01)00229-1
   Matthews V, 2003, J BIOL CHEM, V278, P38829, DOI 10.1074/jbc.M210584200
   Milla ME, 2006, CELL BIOCHEM BIOPHYS, V44, P342, DOI 10.1385/CBB:44:3:342
   Mohammed FF, 2004, NAT GENET, V36, P969, DOI 10.1038/ng1413
   Mortier E, 2004, J IMMUNOL, V173, P1681, DOI 10.4049/jimmunol.173.3.1681
   Moss ML, 2007, J BIOL CHEM, V282, P35712, DOI 10.1074/jbc.M703231200
   Moss ML, 1997, NATURE, V385, P733, DOI 10.1038/385733a0
   Moss ML, 2004, BIOCHEMISTRY-US, V43, P7227, DOI 10.1021/bi049677f
   Nishi E, 2006, J BIOL CHEM, V281, P31164, DOI 10.1074/jbc.M601316200
   Novick D, 2006, P NATL ACAD SCI USA, V103, P3316, DOI 10.1073/pnas.0511206103
   Peschon JJ, 1998, SCIENCE, V282, P1281, DOI 10.1126/science.282.5392.1281
   Pisitkun T, 2004, P NATL ACAD SCI USA, V101, P13368, DOI 10.1073/pnas.0403453101
   PORTEU F, 1991, J BIOL CHEM, V266, P18846
   Rose-John S, 2004, IMMUNITY, V20, P2, DOI 10.1016/S1074-7613(04)00003-2
   Sanada S, 2007, J CLIN INVEST, V117, P1538, DOI 10.1172/JCI30634
   Sanderson MP, 2008, J CELL BIOCHEM, V103, P1783, DOI 10.1002/jcb.21569
   Schulte A, 2007, BIOCHEM BIOPH RES CO, V358, P233, DOI 10.1016/j.bbrc.2007.04.100
   Shao MXG, 2005, P NATL ACAD SCI USA, V102, P767, DOI 10.1073/pnas.0408932102
   Sheu BC, 2001, CANCER RES, V61, P237
   Söderberg A, 2007, FREE RADICAL BIO MED, V43, P90, DOI 10.1016/j.freeradbiomed.2007.03.026
   Soond SM, 2005, J CELL SCI, V118, P2371, DOI 10.1242/jcs.02357
   Stoeck A, 2006, BIOCHEM J, V393, P609, DOI 10.1042/BJ20051013
   Tanaka M, 2004, J BIOL CHEM, V279, P41950, DOI 10.1074/jbc.M400086200
   Tellier E, 2006, EXP CELL RES, V312, P3969, DOI 10.1016/j.yexcr.2006.08.027
   Théry C, 2002, NAT REV IMMUNOL, V2, P569, DOI 10.1038/nri855
   Trajkovic K, 2008, SCIENCE, V319, P1244, DOI 10.1126/science.1153124
   von Tresckow B, 2004, J IMMUNOL, V172, P4324, DOI 10.4049/jimmunol.172.7.4324
   Wang J, 2003, J BIOL CHEM, V278, P21751, DOI 10.1074/jbc.M212662200
   Weskamp G, 2006, NAT IMMUNOL, V7, P1293, DOI 10.1038/ni1399
   Zhang HG, 2006, J IMMUNOL, V176, P7385, DOI 10.4049/jimmunol.176.12.7385
   Zhang JG, 1998, J BIOL CHEM, V273, P10798, DOI 10.1074/jbc.273.17.10798
   Zhang Q, 2006, P NATL ACAD SCI USA, V103, P6901, DOI 10.1073/pnas.0509719103
NR 71
TC 124
Z9 138
U1 0
U2 15
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
SN 0021-9258
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD MAY 23
PY 2008
VL 283
IS 21
BP 14177
EP 14181
DI 10.1074/jbc.R700052200
PG 5
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 302BL
UT WOS:000255941400002
PM 18385130
OA Green Published
DA 2025-04-10
ER

PT J
AU Zhang, XY
   Bailey, SD
   Lupien, M
AF Zhang, Xiaoyang
   Bailey, Swneke D.
   Lupien, Mathieu
TI Laying a solid foundation for Manhattan - 'setting the functional basis
   for the post-GWAS era'
SO TRENDS IN GENETICS
LA English
DT Review
DE GWAS; genetic risk variant; causal variant; missing heritability;
   functional genomic; non-coding
ID TRANSCRIPTION FACTOR-BINDING; GENOME-WIDE ASSOCIATION; SINGLE-NUCLEOTIDE
   POLYMORPHISMS; EXONIC SPLICING ENHANCERS; CORONARY-ARTERY-DISEASE; TERT
   PROMOTER MUTATIONS; LONG-RANGE INTERACTION; GENETIC-VARIATION; CHROMATIN
   STATES; NONCODING RNA
AB Genome-wide association studies (GWAS) have identified more than 8900 genetic variants, mainly single-nucleotide polymorphisms (SNPs), associated with hundreds of human traits and diseases, which define risk-associated loci. Variants that map to coding regions can affect protein sequence, translation rate, and alternative splicing, all of which influence protein function. However, the vast majority of sequence variants map to noncoding intergenic and intronic regions, and it has been much more challenging to assess the functional nature of these variants. Recent work annotating the non-coding regions of the genome has contributed to post-GWAS studies by facilitating the identification of the functional targets of risk-associated loci. Many non-coding genetic variants within risk-associated loci alter gene expression by modulating the activity of cis-regulatory elements. We review here these recent findings, discuss their implication for the post-GWAS era, and relate their importance to the interpretation of disease-associated mutations identified through whole-genome sequencing.
C1 [Zhang, Xiaoyang] Dartmouth Med Sch, Norris Cotton Canc Ctr, Dept Genet, Lebanon, NH USA.
   [Bailey, Swneke D.; Lupien, Mathieu] Univ Hlth Network, Princess Margaret Canc Ctr, Toronto, ON M5G 1L7, Canada.
   [Bailey, Swneke D.; Lupien, Mathieu] Univ Toronto, Dept Med Biophys, Toronto, ON, Canada.
   [Lupien, Mathieu] Ontario Inst Canc Res, Toronto, ON, Canada.
C3 Norris Cotton Cancer Center; Dartmouth College; University of Toronto;
   University Health Network Toronto; Princess Margaret Cancer Centre;
   University of Toronto; Ontario Institute for Cancer Research; University
   of Toronto
RP Zhang, XY (corresponding author), Dana Farber Canc Inst, Boston, MA 02115 USA.
EM mlupien@uhnres.utoronto.ca
RI zhang, xiao yu/JMA-9767-2023; Lupien, Mathieu/KFB-6691-2024
OI Zhang, Xiaoyang/0000-0002-0031-0290; Lupien, Mathieu/0000-0003-0929-9478
FU National Cancer Institute (NCI) of the National Institutes of Health
   (NIH) [R01CA155004]; Princess Margaret Cancer Foundation; Ontario
   Institute for Cancer Research; Canadian Institute of Health Research
   (CIHR); Knudson postdoctoral fellowship from the Princess Margaret
   Cancer Centre
FX The National Cancer Institute (NCI) of the National Institutes of Health
   (NIH) under Award Number R01CA155004 (M.L.) and the Princess Margaret
   Cancer Foundation (M.L.) supported the research reported in this
   publication. The research content reported is the sole responsibility of
   the authors and does not necessarily represent the official views of the
   funding sources. M.L holds a young investigator award from the Ontario
   Institute for Cancer Research and a new investigator salary award from
   the Canadian Institute of Health Research (CIHR). S.D.B. is supported by
   a Knudson postdoctoral fellowship from the Princess Margaret Cancer
   Centre.
CR Adzhubei IA, 2010, NAT METHODS, V7, P248, DOI 10.1038/nmeth0410-248
   Akhtar-Zaidi B, 2012, SCIENCE, V336, P736, DOI 10.1126/science.1217277
   Altshuler DM, 2012, NATURE, V491, P56, DOI 10.1038/nature11632
   Altshuler DM, 2010, NATURE, V467, P52, DOI 10.1038/nature09298
   Andrejeva J, 2004, P NATL ACAD SCI USA, V101, P17264, DOI 10.1073/pnas.0407639101
   [Anonymous], EVOLUTION SINCE DARW
   [Anonymous], 2005, Lehninger's Principles of Biochemistry
   Baca SC, 2013, CELL, V153, P666, DOI 10.1016/j.cell.2013.03.021
   Bahcall OG, 2013, NAT GENET, V45, P343, DOI 10.1038/ng.2592
   Bartel DP, 2009, CELL, V136, P215, DOI 10.1016/j.cell.2009.01.002
   Bauer DE, 2013, SCIENCE, V342, P253, DOI 10.1126/science.1242088
   Bell D, 2011, NATURE, V474, P609, DOI 10.1038/nature10166
   Benko S, 2009, NAT GENET, V41, P359, DOI 10.1038/ng.329
   Bernstein BE, 2010, NAT BIOTECHNOL, V28, P1045, DOI 10.1038/nbt1010-1045
   Bickmore WA, 2013, ANNU REV GENOM HUM G, V14, P67, DOI 10.1146/annurev-genom-091212-153515
   Birney E, 2007, NATURE, V447, P799, DOI 10.1038/nature05874
   Blencowe BJ, 2000, TRENDS BIOCHEM SCI, V25, P106, DOI 10.1016/S0968-0004(00)01549-8
   Bojesen SE, 2013, NAT GENET, V45, P371, DOI 10.1038/ng.2566
   BOSMA PJ, 1995, NEW ENGL J MED, V333, P1171, DOI 10.1056/NEJM199511023331802
   Boyer LA, 2005, CELL, V122, P947, DOI 10.1016/j.cell.2005.08.020
   Boyle AP, 2012, GENOME RES, V22, P1790, DOI 10.1101/gr.137323.112
   Brest P, 2011, NAT GENET, V43, P242, DOI 10.1038/ng.762
   Broadbent HM, 2008, HUM MOL GENET, V17, P806, DOI 10.1093/hmg/ddm352
   Califano A, 2012, NAT GENET, V44, P841, DOI 10.1038/ng.2355
   Cartegni L, 2002, NAT REV GENET, V3, P285, DOI 10.1038/nrg775
   Cingolani P, 2012, FLY, V6, P80, DOI 10.4161/fly.19695
   Cong L, 2013, SCIENCE, V339, P819, DOI 10.1126/science.1231143
   Corradin O, 2014, GENOME RES, V24, P1, DOI 10.1101/gr.164079.113
   Cowper-Sal-lari R, 2012, NAT GENET, V44, P1191, DOI 10.1038/ng.2416
   De Gobbi M, 2006, SCIENCE, V312, P1215, DOI 10.1126/science.1126431
   Degner JF, 2012, NATURE, V482, P390, DOI 10.1038/nature10808
   Dellino GI, 2013, GENOME RES, V23, P1, DOI 10.1101/gr.142331.112
   Dickson SP, 2010, PLOS BIOL, V8, DOI 10.1371/journal.pbio.1000294
   Dimas AS, 2009, SCIENCE, V325, P1246, DOI 10.1126/science.1174148
   Djebali S, 2012, NATURE, V489, P101, DOI 10.1038/nature11233
   Dunham I, 2012, NATURE, V489, P57, DOI 10.1038/nature11247
   Eeles RA, 2013, NAT GENET, V45, P385, DOI 10.1038/ng.2560
   Ernst J, 2011, NATURE, V473, P43, DOI 10.1038/nature09906
   Ernst J, 2010, NAT BIOTECHNOL, V28, P817, DOI 10.1038/nbt.1662
   Fairbrother WG, 2002, SCIENCE, V297, P1007, DOI 10.1126/science.1073774
   Fraser P, 2007, NATURE, V447, P413, DOI 10.1038/nature05916
   Frazer KA, 2009, NAT REV GENET, V10, P241, DOI 10.1038/nrg2554
   Fullwood MJ, 2009, NATURE, V462, P58, DOI 10.1038/nature08497
   Fung KL, 2009, BBA-PROTEINS PROTEOM, V1794, P860, DOI 10.1016/j.bbapap.2009.02.014
   Garcia-Closas M, 2013, NAT GENET, V45, P392, DOI 10.1038/ng.2561
   Gerstein MB, 2012, NATURE, V489, P91, DOI 10.1038/nature11245
   Gibcus JH, 2013, MOL CELL, V49, P773, DOI 10.1016/j.molcel.2013.02.011
   Gilad Y, 2008, TRENDS GENET, V24, P408, DOI 10.1016/j.tig.2008.06.001
   Graf T, 2009, NATURE, V462, P587, DOI 10.1038/nature08533
   Grant SFA, 2008, CLIN CHEM, V54, P1116, DOI 10.1373/clinchem.2008.105395
   Gregory AP, 2012, NATURE, V488, P508, DOI 10.1038/nature11307
   Grisanzio C, 2012, P NATL ACAD SCI USA, V109, P11252, DOI 10.1073/pnas.1200853109
   Guttman M, 2009, NATURE, V458, P223, DOI 10.1038/nature07672
   Handoko L, 2011, NAT GENET, V43, P630, DOI 10.1038/ng.857
   Hansen RS, 2010, P NATL ACAD SCI USA, V107, P139, DOI 10.1073/pnas.0912402107
   Harismendy O, 2011, NATURE, V470, P264, DOI 10.1038/nature09753
   Heintzman ND, 2007, NAT GENET, V39, P311, DOI 10.1038/ng1966
   Heintzman ND, 2009, NATURE, V459, P108, DOI 10.1038/nature07829
   HIGGS DR, 1989, BLOOD, V73, P1081
   Hindorff L., 2012, CATALOG PUBLISHED GE
   Hindorff LA, 2009, P NATL ACAD SCI USA, V106, P9362, DOI 10.1073/pnas.0903103106
   Hnisz D, 2013, CELL, V155, P934, DOI 10.1016/j.cell.2013.09.053
   Hoffmeyer S, 2000, P NATL ACAD SCI USA, V97, P3473, DOI 10.1073/pnas.050585397
   Horn S, 2013, SCIENCE, V339, P959, DOI 10.1126/science.1230062
   Huang FW, 2013, SCIENCE, V339, P957, DOI 10.1126/science.1229259
   Huang HY, 2006, NUCLEIC ACIDS RES, V34, pW429, DOI 10.1093/nar/gkl333
   Huang Y, 2007, P NATL ACAD SCI USA, V104, P985, DOI 10.1073/pnas.0609954104
   Imielinski M, 2012, CELL, V150, P1107, DOI 10.1016/j.cell.2012.08.029
   Ishii N, 2006, J HUM GENET, V51, P1087, DOI 10.1007/s10038-006-0070-9
   Jing HI, 2008, MOL CELL, V29, P232, DOI 10.1016/j.molcel.2007.11.020
   Jones PA, 2007, CELL, V128, P683, DOI 10.1016/j.cell.2007.01.029
   Kasowski M, 2013, SCIENCE, V342, P750, DOI 10.1126/science.1242510
   Kasowski M, 2010, SCIENCE, V328, P232, DOI 10.1126/science.1183621
   Kato H, 2006, NATURE, V441, P101, DOI 10.1038/nature04734
   Khurana E, 2013, SCIENCE, V342, P84, DOI 10.1126/science.1235587
   Kilpinen H, 2013, SCIENCE, V342, P744, DOI 10.1126/science.1242463
   Kimchi-Sarfaty C, 2007, SCIENCE, V315, P525, DOI 10.1126/science.1135308
   Komar AA, 2007, SCIENCE, V315, P466, DOI 10.1126/science.1138239
   Kooner JS, 2008, NAT GENET, V40, P149, DOI 10.1038/ng.2007.61
   Kwan T, 2008, NAT GENET, V40, P225, DOI 10.1038/ng.2007.57
   Li GL, 2012, CELL, V148, P84, DOI 10.1016/j.cell.2011.12.014
   Li QY, 2013, CELL, V152, P633, DOI 10.1016/j.cell.2012.12.034
   Lieberman-Aiden E, 2009, SCIENCE, V326, P289, DOI 10.1126/science.1181369
   Lupien M, 2008, CELL, V132, P958, DOI 10.1016/j.cell.2008.01.018
   Matlin AJ, 2005, NAT REV MOL CELL BIO, V6, P386, DOI 10.1038/nrm1645
   Maurano MT, 2012, SCIENCE, V337, P1190, DOI 10.1126/science.1222794
   McClellan J, 2010, CELL, V141, P210, DOI 10.1016/j.cell.2010.03.032
   McVicker G, 2013, SCIENCE, V342, P747, DOI 10.1126/science.1242429
   Michaelson JJ, 2012, CELL, V151, P1431, DOI 10.1016/j.cell.2012.11.019
   Michailidou K, 2013, NAT GENET, V45, P353, DOI 10.1038/ng.2563
   Mishiro T, 2009, EMBO J, V28, P1234, DOI 10.1038/emboj.2009.81
   Misteli T, 2007, CELL, V128, P787, DOI 10.1016/j.cell.2007.01.028
   Montgomery SB, 2011, NAT REV GENET, V12, P277, DOI 10.1038/nrg2969
   Morris AP, 2012, NAT GENET, V44, P981, DOI 10.1038/ng.2383
   Musunuru K, 2010, NATURE, V466, P714, DOI 10.1038/nature09266
   Muzny DM, 2012, NATURE, V487, P330, DOI 10.1038/nature11252
   Nejentsev S, 2009, SCIENCE, V324, P387, DOI 10.1126/science.1167728
   Nicolae DL, 2010, PLOS GENET, V6, DOI 10.1371/journal.pgen.1000888
   Niknafs N, 2013, HUM GENET, V132, P1235, DOI 10.1007/s00439-013-1325-0
   Onder TT, 2012, CURR OPIN GENET DEV, V22, P500, DOI 10.1016/j.gde.2012.05.005
   Ong CT, 2011, NAT REV GENET, V12, P283, DOI 10.1038/nrg2957
   Parker SCJ, 2013, P NATL ACAD SCI USA, V110, P17921, DOI 10.1073/pnas.1317023110
   Pharoah PDP, 2013, NAT GENET, V45, P362, DOI 10.1038/ng.2564
   Plessy C, 2010, NAT METHODS, V7, P528, DOI [10.1038/NMETH.1470, 10.1038/nmeth.1470]
   Pomerantz MM, 2010, PLOS GENET, V6, DOI 10.1371/journal.pgen.1001204
   Pomerantz MM, 2009, NAT GENET, V41, P882, DOI 10.1038/ng.403
   Ravasi T, 2010, CELL, V140, P744, DOI 10.1016/j.cell.2010.01.044
   Raychaudhuri S, 2011, CELL, V147, P57, DOI 10.1016/j.cell.2011.09.011
   Raychaudhuri S, 2009, PLOS GENET, V5, DOI 10.1371/journal.pgen.1000534
   REIJNEN MJ, 1992, P NATL ACAD SCI USA, V89, P6300, DOI 10.1073/pnas.89.14.6300
   Rinn JL, 2007, CELL, V129, P1311, DOI 10.1016/j.cell.2007.05.022
   Roix JJ, 2003, NAT GENET, V34, P287, DOI 10.1038/ng1177
   Ross-Innes CS, 2012, NATURE, V481, P389, DOI 10.1038/nature10730
   Ryba T, 2011, NAT PROTOC, V6, P870, DOI 10.1038/nprot.2011.328
   Sakoda LC, 2013, NAT GENET, V45, P345, DOI 10.1038/ng.2587
   Sanjana NE, 2012, NAT PROTOC, V7, P171, DOI 10.1038/nprot.2011.431
   Sanyal A, 2012, NATURE, V489, P109, DOI 10.1038/nature11279
   Schaub MA, 2012, GENOME RES, V22, P1748, DOI 10.1101/gr.136127.111
   Schoenfelder S, 2010, NAT GENET, V42, P53, DOI 10.1038/ng.496
   Segrè AV, 2010, PLOS GENET, V6, DOI 10.1371/journal.pgen.1001058
   Seo J, 2012, NUCLEIC ACIDS RES, V40, P5965, DOI 10.1093/nar/gks287
   Sharma S, 2010, CARCINOGENESIS, V31, P27, DOI 10.1093/carcin/bgp220
   Shen H, 2013, NAT COMMUN, V4, DOI 10.1038/ncomms2629
   Shen LX, 1999, P NATL ACAD SCI USA, V96, P7871, DOI 10.1073/pnas.96.14.7871
   Siepel A, 2005, GENOME RES, V15, P1034, DOI 10.1101/gr.3715005
   Singh SB, 2006, SCIENCE, V313, P1438, DOI 10.1126/science.1129577
   Smyth DJ, 2006, NAT GENET, V38, P617, DOI 10.1038/ng1800
   Soldner F, 2012, SCIENCE, V338, P1155, DOI 10.1126/science.1227682
   Soldner F, 2011, CELL, V146, P318, DOI 10.1016/j.cell.2011.06.019
   Son CG, 2005, GENOME RES, V15, P443, DOI 10.1101/gr.3124505
   Splinter E, 2006, GENE DEV, V20, P2349, DOI 10.1101/gad.399506
   Stergachis AB, 2013, SCIENCE, V342, P1367, DOI 10.1126/science.1243490
   Tang QZ, 2011, CANCER RES, V71, P6940, DOI 10.1158/0008-5472.CAN-11-2091
   Torkamani A, 2008, GENOMICS, V92, P265, DOI 10.1016/j.ygeno.2008.07.011
   Tsai MC, 2010, SCIENCE, V329, P689, DOI 10.1126/science.1192002
   Tuupanen S, 2009, NAT GENET, V41, P885, DOI 10.1038/ng.406
   Uyeda K, 2006, CELL METAB, V4, P107, DOI 10.1016/j.cmet.2006.06.008
   Visser M, 2012, GENOME RES, V22, P446, DOI 10.1101/gr.128652.111
   Voight BF, 2012, PLOS GENET, V8, DOI 10.1371/journal.pgen.1002793
   Voineagu I, 2011, NATURE, V474, P380, DOI 10.1038/nature10110
   Wang K, 2007, AM J HUM GENET, V81, P1278, DOI 10.1086/522374
   Wang K, 2010, NAT REV GENET, V11, P843, DOI 10.1038/nrg2884
   Wang KC, 2011, NATURE, V472, P120, DOI 10.1038/nature09819
   Ward LD, 2012, NAT BIOTECHNOL, V30, P1095, DOI 10.1038/nbt.2422
   Ward LD, 2012, SCIENCE, V337, P1675, DOI 10.1126/science.1225057
   Ward LD, 2012, NUCLEIC ACIDS RES, V40, pD930, DOI 10.1093/nar/gkr917
   Weedon MN, 2014, NAT GENET, V46, P61, DOI 10.1038/ng.2826
   Wray NR, 2011, PLOS BIOL, V9, DOI 10.1371/journal.pbio.1000579
   Wright JB, 2010, MOL CELL BIOL, V30, P1411, DOI 10.1128/MCB.01384-09
   Yan J, 2013, CELL, V154, P801, DOI 10.1016/j.cell.2013.07.034
   Yang JA, 2010, NAT GENET, V42, P565, DOI 10.1038/ng.608
   Zhang XY, 2012, GENOME RES, V22, P1437, DOI 10.1101/gr.135665.111
   Zhao J, 2008, SCIENCE, V322, P750, DOI 10.1126/science.1163045
NR 153
TC 75
Z9 84
U1 2
U2 49
PU CELL PRESS
PI CAMBRIDGE
PA 50 HAMPSHIRE ST, FLOOR 5, CAMBRIDGE, MA 02139 USA
SN 0168-9525
EI 1362-4555
J9 TRENDS GENET
JI Trends Genet.
PD APR
PY 2014
VL 30
IS 4
BP 140
EP 149
DI 10.1016/j.tig.2014.02.006
PG 10
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA AG4YM
UT WOS:000335426300004
PM 24661571
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Valentin, F
   Tippins, JR
   Field, MC
AF Valentin, F
   Tippins, JR
   Field, MC
TI The role of alternative splicing and C-terminal amino acids in
   thromboxane receptor stabilization
SO BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
LA English
DT Article
DE thromboxane; ER-associated degradation; isoprostane; protein turnover;
   mutagenesis; oxidative stress
ID GROWTH-FACTOR RECEPTOR; PROSTANOID RECEPTORS; BETA-ISOFORMS;
   3-HYDROXY-3-METHYLGLUTARYL-COA REDUCTASE; A2 RECEPTOR; ALPHA; A(2);
   ACTIVATION; KINASE; INTERNALIZATION
AB The thromboxane receptor has two alternatively spliced isoforms, alpha and beta, which differ only in sequences within the cytoplasmic C-terminal domain. Oxidative stress induced by H2O2 in a COS-7 cell model results in stabilization of the thromboxane receptor P isoform by translocation from the endoplasmic reticulum to the Golgi complex, which in turn results in protection of the receptor from degradation. We now report that both the alpha and beta thromboxane receptor isoforms respond identically to oxidative stress. Further, mutagenesis studies indicate that replacing the normal C-terminus with a nonsense sequence also does not alter stabilization behaviour ruling out a role for the distinct C-termini in this process. Further mutagenesis implicates a cluster of arginine residues within the C-terminal domain as involved in oxidative stress-induced stabilization. These data identify a region of the thromboxane receptor that is responsible for responding to oxidative challenge and open the possibility of identification of the molecular machinery underpinning this response. (c) 2005 Elsevier Inc. All rights reserved.
C1 Univ London Imperial Coll Sci Technol & Med, Div Cell & Mol Biol, London SW7 2AZ, England.
   Univ Cambridge, Dept Pathol, Cambridge CB2 1QP, England.
C3 Imperial College London; University of Cambridge
RP Univ London Imperial Coll Sci Technol & Med, Div Cell & Mol Biol, Biochem Bldg, London SW7 2AZ, England.
EM j.tippins@imperial.ac.uk
RI Field, Mark/AAD-6455-2021
OI Field, Mark/0000-0002-4866-2885
CR Cheng HH, 1999, J BIOL CHEM, V274, P17171, DOI 10.1074/jbc.274.24.17171
   COLEMAN RA, 1994, PHARMACOL REV, V46, P205
   DORN GW, 1990, CIRCULATION, V81, P212, DOI 10.1161/01.CIR.81.1.212
   Gallet C, 2003, BIOCHEM J, V371, P733, DOI 10.1042/BJ20021030
   Gao YL, 2001, J PHARMACOL EXP THER, V296, P426
   Hampton RY, 2002, ANNU REV CELL DEV BI, V18, P345, DOI 10.1146/annurev.cellbio.18.032002.131219
   HIRATA M, 1991, NATURE, V349, P617, DOI 10.1038/349617a0
   Katugampola SD, 2002, CLIN SCI, V103, p171S, DOI 10.1042/CS103S171S
   Katugampola SD, 2001, BRIT J PHARMACOL, V134, P1385, DOI 10.1038/sj.bjp.0704416
   Kinsella BT, 2001, BIOCHEM SOC T, V29, P641, DOI 10.1042/BST0290641
   Kromer BM, 1996, BRIT J PHARMACOL, V119, P1276, DOI 10.1111/j.1476-5381.1996.tb16033.x
   LI Z, 2003, J BIOL CHEM
   Miggin SM, 1998, BBA-GEN SUBJECTS, V1425, P543, DOI 10.1016/S0304-4165(98)00109-3
   Miggin SM, 2002, MOL PHARMACOL, V61, P817, DOI 10.1124/mol.61.4.817
   Narumiya S, 1999, PHYSIOL REV, V79, P1193, DOI 10.1152/physrev.1999.79.4.1193
   NEGISHI M, 1993, PROG LIPID RES, V32, P417, DOI 10.1016/0163-7827(93)90017-Q
   Parent JL, 2001, J BIOL CHEM, V276, P7079, DOI 10.1074/jbc.M009375200
   Pratico D, 1997, J CLIN INVEST, V100, P2028, DOI 10.1172/JCI119735
   RAYCHOWDHURY MK, 1994, J BIOL CHEM, V269, P19256
   Reilly MP, 1998, CIRCULATION, V98, P2822, DOI 10.1161/01.CIR.98.25.2822
   Rochdi MD, 2003, J BIOL CHEM, V278, P17827, DOI 10.1074/jbc.M210319200
   Rochdi MD, 2002, J BIOL CHEM, V277, P40751, DOI 10.1074/jbc.M207910200
   Rodrigues S, 2001, FASEB J, V15, P1517, DOI 10.1096/fj.00-0802com
   Roger S, 2004, FEBS LETT, V556, P227, DOI 10.1016/S0014-5793(03)01430-3
   Song BL, 2004, J BIOL CHEM, V279, P28798, DOI 10.1074/jbc.M402442200
   Valentin FO, 2004, J BIOL CHEM, V279, P8316, DOI 10.1074/jbc.M306761200
   Vassalle C, 2003, CORONARY ARTERY DIS, V14, P213, DOI 10.1097/01.mca.0000063504.13456.c3
   Walsh MT, 2000, BBA-MOL CELL RES, V1496, P164, DOI 10.1016/S0167-4889(00)00031-8
NR 28
TC 3
Z9 5
U1 0
U2 0
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0006-291X
EI 1090-2104
J9 BIOCHEM BIOPH RES CO
JI Biochem. Biophys. Res. Commun.
PD APR 15
PY 2005
VL 329
IS 3
BP 898
EP 904
DI 10.1016/j.bbrc.2005.02.058
PG 7
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA 909UI
UT WOS:000227885800014
PM 15752740
DA 2025-04-10
ER

PT J
AU Perales, S
   Sigamani, V
   Rajasingh, S
   Gurusamy, N
   Bittel, D
   Czirok, A
   Radic, M
   Rajasingh, J
AF Perales, Selene
   Sigamani, Vinoth
   Rajasingh, Sheeja
   Gurusamy, Narasimman
   Bittel, Douglas
   Czirok, Andras
   Radic, Marko
   Rajasingh, Johnson
TI scaRNA20 promotes pseudouridylatory modification of small nuclear snRNA
   U12 and improves cardiomyogenesis
SO EXPERIMENTAL CELL RESEARCH
LA English
DT Article
DE Cardiomyocytes; Differentiation; Induced pluripotent stem cells;
   Pseudouridylation; Small Cajal-body associated RNA
ID SMALL NUCLEOLAR RNAS; NONCODING RNAS; HEART; H/ACA; CARDIOMYOCYTES;
   EXPRESSION; MATURATION; PROTEIN; DIFFERENTIATION; ASSOCIATION
AB Non-coding RNAs, particularly small Cajal-body associated RNAs (scaRNAs), play a significant role in spliceosomal RNA modifications. While their involvement in ischemic myocardium regeneration is known, their role in cardiac development is unexplored. We investigated scaRNA20's role in iPSC differentiation into cardiomyocytes (iCMCs) via overexpression and knockdown assays. We measured scaRNA20-OE-iCMCs and scaRNA20-KDiCMCs contractility using Particle Image Velocimetry (PIV), comparing them to control iCMCs. We explored scaRNA20's impact on alternative splicing via pseudouridylation (psi) of snRNA U12, analyzing its functional consequences in cardiac differentiation. scaRNA20-OE-iPSC differentiation increased beating colonies, upregulated cardiac-specific genes, activated TP53 and STAT3, and preserved contractility under hypoxia. Conversely, scaRNA20-KD-iCMCs exhibited poor differentiation and contractility. STAT3 inhibition in scaRNA20-OE-iPSCs hindered cardiac differentiation. RNA immunoprecipitation revealed increased psi at the 28th uridine of U12 RNA in scaRNA20-OE iCMCs. U12-KD iCMCs had reduced cardiac differentiation, which improved upon U12 RNA introduction. In summary, scaRNA20-OE in iPSCs enhances cardiomyogenesis, preserves iCMC function under hypoxia, and may have implications for ischemic myocardium regeneration.
C1 [Perales, Selene; Sigamani, Vinoth; Rajasingh, Sheeja; Gurusamy, Narasimman; Rajasingh, Johnson] Univ Tennessee, Hlth Sci Ctr, Dept Biosci Res, 847 Monroe Ave, Memphis, TN 38163 USA.
   [Bittel, Douglas] Kansas City Univ Med & Biosci, Dept Biosci, Kansas City, MO USA.
   [Czirok, Andras] Univ Kansas, Med Ctr, Dept Anat & Cell Biol, Kansas City, KS USA.
   [Rajasingh, Johnson] Univ Tennessee, Dept Med Cardiol, Hlth Sci Ctr, Memphis, TN USA.
   [Radic, Marko; Rajasingh, Johnson] Univ Tennessee, Hlth Sci Ctr, Dept Microbiol Immunol & Biochem, Memphis, TN USA.
C3 University of Tennessee System; University of Tennessee Health Science
   Center; Kansas City University; University of Kansas; University of
   Kansas Medical Center; University of Tennessee System; University of
   Tennessee Health Science Center; University of Tennessee System;
   University of Tennessee Health Science Center
RP Rajasingh, J (corresponding author), Univ Tennessee, Hlth Sci Ctr, Dept Biosci Res, 847 Monroe Ave, Memphis, TN 38163 USA.
EM rjohn186@uthsc.edu
RI ; Czirok, Andras/E-4253-2014; Gurusamy, Narasimman/ABU-6455-2022
OI Bittel, Douglas/0000-0002-1033-7139; Czirok, Andras/0000-0002-2694-5163;
   SIGAMANI, VINOTH/0000-0002-7545-3907; Gurusamy,
   Narasimman/0000-0001-5579-1354
CR Antonicka H, 2017, EMBO REP, V18, P28, DOI 10.15252/embr.201643391
   Armiñán A, 2009, STEM CELLS DEV, V18, P907, DOI 10.1089/scd.2008.0292
   Batalov I, 2015, BIOMARK INSIGHTS, V10, P71, DOI 10.4137/BMI.S20050
   Cao T, 2018, TRENDS CARDIOVAS MED, V28, P81, DOI 10.1016/j.tcm.2017.08.002
   Carlile TM, 2015, METHOD ENZYMOL, V560, P219, DOI 10.1016/bs.mie.2015.03.011
   Castle JC, 2008, NAT GENET, V40, P1416, DOI 10.1038/ng.264
   Czirok A, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-10094-7
   Dez C, 2001, NUCLEIC ACIDS RES, V29, P598, DOI 10.1093/nar/29.3.598
   Enwerem II, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0122348
   Enwerem II, 2014, BIOL OPEN, V3, P240, DOI 10.1242/bio.20147443
   Esteller M, 2011, NAT REV GENET, V12, P861, DOI 10.1038/nrg3074
   Falaleeva M, 2016, P NATL ACAD SCI USA, V113, pE1625, DOI 10.1073/pnas.1519292113
   Farina AR, 2020, J EXP CLIN CANC RES, V39, DOI 10.1186/s13046-020-01616-9
   Gurusamy N, 2021, EXP CELL RES, V400, DOI 10.1016/j.yexcr.2021.112508
   Hebert MD, 2010, ARCH BIOCHEM BIOPHYS, V496, P69, DOI 10.1016/j.abb.2010.02.012
   Hendrickson DG, 2009, PLOS BIOL, V7, DOI 10.1371/journal.pbio.1000238
   Hilfiker-Kleiner D, 2005, PHARMACOL THERAPEUT, V107, P131, DOI 10.1016/j.pharmthera.2005.02.003
   Hilfiker-Kleiner D, 2004, CIRC RES, V95, P187, DOI 10.1161/01.RES.0000134921.50377.61
   Jacoby JJ, 2003, P NATL ACAD SCI USA, V100, P12929, DOI 10.1073/pnas.2134694100
   Kalsotra A, 2010, GENE DEV, V24, P653, DOI 10.1101/gad.1894310
   Kalsotra A, 2008, P NATL ACAD SCI USA, V105, P20333, DOI 10.1073/pnas.0809045105
   Khalil AM, 2009, P NATL ACAD SCI USA, V106, P11667, DOI 10.1073/pnas.0904715106
   Khan MAB, 2020, CUREUS J MED SCIENCE, V12, DOI 10.7759/cureus.9349
   Kim C, 2010, STEM CELLS DEV, V19, P783, DOI 10.1089/scd.2009.0349
   King TH, 2003, MOL CELL, V11, P425, DOI 10.1016/S1097-2765(03)00040-6
   KISS T, 1995, GENE DEV, V9, P1411, DOI 10.1101/gad.9.11.1411
   Kiss T, 2010, MOL CELL, V37, P597, DOI 10.1016/j.molcel.2010.01.032
   Lara-Pezzi E, 2012, DIS MODEL MECH, V5, P434, DOI 10.1242/dmm.009787
   Lestrade L, 2006, NUCLEIC ACIDS RES, V34, pD158, DOI 10.1093/nar/gkj002
   Levy DE, 2002, J CLIN INVEST, V109, P1143, DOI 10.1172/JCI200215650
   Liu YS, 2021, INT J STEM CELLS, V14, P410, DOI 10.15283/ijsc21051
   Lundy SD, 2013, STEM CELLS DEV, V22, P1991, DOI 10.1089/scd.2012.0490
   Ma J, 2016, LEUKEMIA, V30, P594, DOI 10.1038/leu.2015.285
   Marnef A, 2014, NUCLEIC ACIDS RES, V42, P6616, DOI 10.1093/nar/gku287
   Moreau PR, 2018, FRONT CARDIOVASC MED, V5, DOI 10.3389/fcvm.2018.00159
   Nagasawa CK, 2020, PEDIATR CARDIOL, V41, P341, DOI 10.1007/s00246-019-02263-4
   Nallamshetty S, 2013, FREE RADICAL BIO MED, V64, P20, DOI 10.1016/j.freeradbiomed.2013.05.022
   Natua S, 2021, CELL MOL LIFE SCI, V78, P2729, DOI 10.1007/s00018-020-03727-0
   O'Brien JE, 2012, CIRC-CARDIOVASC GENE, V5, P279, DOI 10.1161/CIRCGENETICS.111.961474
   Patil P, 2015, BBA-MOL BASIS DIS, V1852, P1619, DOI 10.1016/j.bbadis.2015.04.016
   Rajasingh J, 2007, CIRC RES, V101, P910, DOI 10.1161/CIRCRESAHA.107.156786
   Rajasingh S., 2021, Methods in Molecular Biology, V2454, P197
   Rajasingh S, 2021, J CELL MOL MED, V25, P8904, DOI 10.1111/jcmm.16851
   Rajasingh S, 2018, ACTA PHARMACOL SIN, V39, P1590, DOI 10.1038/aps.2017.183
   Rajasingh S, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0134093
   Richard P, 2003, EMBO J, V22, P4283, DOI 10.1093/emboj/cdg394
   Samanta S, 2016, TRENDS CARDIOVAS MED, V26, P407, DOI 10.1016/j.tcm.2016.02.004
   Samarsky DA, 1998, EMBO J, V17, P3747, DOI 10.1093/emboj/17.13.3747
   Schattner P, 2006, RNA, V12, P15, DOI 10.1261/rna.2210406
   Shabbir A, 2010, AM J PHYSIOL-HEART C, V299, pH1428, DOI 10.1152/ajpheart.00488.2010
   Sigamani V, 2021, CURR GENOMICS, V22, P526, DOI 10.2174/1389202922666211130144221
   Sun X, 2023, FRONT CELL DEV BIOL, V11, DOI 10.3389/fcell.2023.1292925
   Sun YJ, 2019, BIOMED PHARMACOTHER, V118, DOI 10.1016/j.biopha.2019.109391
   Szklarczyk D, 2019, NUCLEIC ACIDS RES, V47, pD607, DOI [10.1093/nar/gky1131, 10.1093/nar/gkac1000]
   Terns MP, 2002, GENE EXPRESSION, V10, P17
   Turunen JJ, 2013, WIRES RNA, V4, P61, DOI 10.1002/wrna.1141
   Ubil E, 2014, NATURE, V514, P585, DOI 10.1038/nature13839
   van Ingen E., Mol Ther Nucleic Acids, V30, P2022
   Vulliamy T, 2008, P NATL ACAD SCI USA, V105, P8073, DOI 10.1073/pnas.0800042105
   Wang J., 2019, Advances in Biological Chemistry, V9, P54, DOI 10.4236/abc.2019.92005
   Yang KC, 2014, CIRCULATION, V129, P1009, DOI 10.1161/CIRCULATIONAHA.113.003863
   Zhao CM, 2006, J NEUROSCI, V26, P3, DOI 10.1523/JNEUROSCI.3648-05.2006
   Zhao XL, 2004, RNA, V10, P996, DOI 10.1261/rna.7110804
   Zhao Y, 2018, FRONT BIOENG BIOTECH, V6, DOI 10.3389/fbioe.2018.00008
   Zhu Y, 2023, PLOS ONE, V18, DOI 10.1371/journal.pone.0281132
NR 65
TC 0
Z9 0
U1 0
U2 3
PU ELSEVIER INC
PI SAN DIEGO
PA 525 B STREET, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0014-4827
EI 1090-2422
J9 EXP CELL RES
JI Exp. Cell Res.
PD MAR 1
PY 2024
VL 436
IS 1
AR 113961
DI 10.1016/j.yexcr.2024.113961
EA FEB 2024
PG 17
WC Oncology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Oncology; Cell Biology
GA LC6I7
UT WOS:001184615700001
PM 38341080
DA 2025-04-10
ER

PT J
AU Ochs, ME
   McWhirter, RM
   Unckless, RL
   Miller, DM
   Lundquist, EA
AF Ochs, Matthew E.
   McWhirter, Rebecca M.
   Unckless, Robert L.
   Miller, David M., III
   Lundquist, Erik A.
TI Caenorhabditis elegans ETR-1/CELF has broad effects on the muscle
   cell transcriptome, including genes that regulate translation and
   neuroblast migration
SO BMC GENOMICS
LA English
DT Article
ID RNA-BINDING PROTEINS; C. ELEGANS; FUNCTIONAL-ANALYSIS; EXPRESSION
   ANALYSIS; MYOTONIC-DYSTROPHY; UNC-52 GENE; CUGBP1; FAMILY; REPEAT; ACTS
AB Migration of neuroblasts and neurons from their birthplace is central to the formation of neural circuits and networks. ETR-1 is the Caenorhabditis elegans homolog of the CELF1 (CUGBP, ELAV-like family 1) RNA-processing factor involved in neuromuscular disorders. etr-1 regulates body wall muscle differentiation. Our previous work showed that etr-1 in muscle has a non-autonomous role in neuronal migration, suggesting that ETR-1 is involved in the production of a signal emanating from body wall muscle that controls neuroblast migration and that interacts with Wnt signaling. etr-1 is extensively alternatively-spliced, and we identified the viable etr-1(lq61) mutant, caused by a stop codon in alternatively-spliced exon 8 and only affecting etr-1 isoforms containing exon 8. We took advantage of viable etr-1(lq61) to identify potential RNA targets of ETR-1 in body wall muscle using a combination of fluorescence activated cell sorting (FACS) of body wall muscles from wild-type and etr-1(lq61) and subsequent RNA-seq. This analysis revealed genes whose splicing and transcript levels were controlled by ETR-1 exon 8 isoforms, and represented a broad spectrum of genes involved in muscle differentiation, myofilament lattice structure, and physiology. Genes with transcripts underrepresented in etr-1(lq61) included those involved in ribosome function and translation, similar to potential CELF1 targets identified in chick cardiomyocytes. This suggests that at least some targets of ETR-1 might be conserved in vertebrates, and that ETR-1 might generally stimulate translation in muscles. As proof-of-principle, a functional analysis of a subset of ETR-1 targets revealed genes involved in AQR and PQR neuronal migration. One such gene, lev-11/tropomyosin, requires ETR-1 for alternative splicing, and another, unc-52/perlecan, requires ETR-1 for the production of long isoforms containing 3' exons. In sum, these studies identified gene targets of ETR-1/CELF1 in muscles, which included genes involved in muscle development and physiology, and genes with novel roles in neuronal migration.
C1 [Ochs, Matthew E.; Unckless, Robert L.; Lundquist, Erik A.] Univ Kansas, Dept Mol Biosci, Program Mol Cellular & Dev Biol, Lawrence, KS 66045 USA.
   [McWhirter, Rebecca M.; Miller, David M., III] Vanderbilt Univ, Dept Cell & Dev Biol, Nashville, TN 37203 USA.
   [McWhirter, Rebecca M.; Miller, David M., III] Vanderbilt Univ, Dept Biol Sci, Nashville, TN 37203 USA.
C3 University of Kansas; Vanderbilt University; Vanderbilt University
RP Lundquist, EA (corresponding author), Univ Kansas, Dept Mol Biosci, Program Mol Cellular & Dev Biol, Lawrence, KS 66045 USA.
EM erikl@ku.edu
OI McWhirter, Rebecca/0000-0002-7787-2224
FU National Institute of Health [R21NS100483, R01NS106951, R01NS10054,
   R01AI139154]; National Institute of General Medical Sciences
   [P20GM103638] Funding Source: NIH RePORTER
FX This work was supported by National Institute of Health projects
   R21NS100483 to E.A.L. and D.M.M.; R01NS106951 and R01NS10054 to D.M.M.;
   and R01AI139154 to R.L..
CR Anders S, 2013, NAT PROTOC, V8, P1765, DOI 10.1038/nprot.2013.099
   Anyanful A, 2001, J MOL BIOL, V313, P525, DOI 10.1006/jmbi.2001.5052
   Bänziger C, 2006, CELL, V125, P509, DOI 10.1016/j.cell.2006.02.049
   Berger Dara S, 2012, PLoS Curr, V4, pRRN1305
   Blech-Hermoni Y, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0149061
   Boateng R, 2018, GENETICS, V208, P79, DOI 10.1534/genetics.117.300482
   Boateng R, 2017, DEV BIOL, V429, P306, DOI 10.1016/j.ydbio.2017.06.015
   Broitman-Maduro G, 2005, DEV CELL, V8, P427, DOI 10.1016/j.devcel.2005.01.014
   Ch'ng' Q, 2003, GENETICS, V164, P1355
   CHALFIE M, 1981, DEV BIOL, V82, P358, DOI 10.1016/0012-1606(81)90459-0
   Chapman JO, 2008, DEV BIOL, V324, P245, DOI 10.1016/j.ydbio.2008.09.014
   Chen L, 2016, ELIFE, P5
   Chen SF, 2018, BIOINFORMATICS, V34, P884, DOI 10.1093/bioinformatics/bty560
   Dasgupta T, 2012, WIRES RNA, V3, P104, DOI 10.1002/wrna.107
   Daughters RS, 2009, PLOS GENET, V5, DOI 10.1371/journal.pgen.1000600
   Ebbing A, 2019, DEVELOPMENT, V146, DOI 10.1242/dev.180059
   Fire A, 1998, NATURE, V391, P806, DOI 10.1038/35888
   Fox RM, 2007, GENOME BIOL, V8, DOI 10.1186/gb-2007-8-9-r188
   Fu R, 2018, J CELL SCI, V131, DOI 10.1242/jcs.214379
   Gomes JE, 2001, DEVELOPMENT, V128, P4301
   Good PJ, 2000, J BIOL CHEM, V275, P28583, DOI 10.1074/jbc.M003083200
   Harterink M, 2011, DEVELOPMENT, V138, P2915, DOI 10.1242/dev.064733
   Ho TH, 2005, HUM MOL GENET, V14, P1539, DOI 10.1093/hmg/ddi162
   Honigberg L, 2000, DEVELOPMENT, V127, P4655
   Huang DW, 2009, NAT PROTOC, V4, P44, DOI 10.1038/nprot.2008.211
   Huang DW, 2009, NUCLEIC ACIDS RES, V37, P1, DOI 10.1093/nar/gkn923
   Huang X, 2003, DEVELOPMENT, V130, P3147, DOI 10.1242/dev.00518
   Josephson MP, 2017, GENETICS, V205, P737, DOI 10.1534/genetics.116.191957
   Josephson MP, 2016, GENETICS, V203, P1747, DOI [10.1534/genetics.116.188367, 10.1534/genetics.116.1]
   Josephson MP, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0148658
   Kagawa H, 1997, CELL STRUCT FUNCT, V22, P213, DOI 10.1247/csf.22.213
   Kalsotra A, 2008, P NATL ACAD SCI USA, V105, P20333, DOI 10.1073/pnas.0809045105
   Kamath RS, 2003, NATURE, V421, P231, DOI 10.1038/nature01278
   Kamath RS, 2003, METHODS, V30, P313, DOI 10.1016/S1046-2023(03)00050-1
   Kim D, 2019, NAT BIOTECHNOL, V37, P907, DOI 10.1038/s41587-019-0201-4
   Kim G, 2015, PLOS GENET, V11, DOI 10.1371/journal.pgen.1004992
   Koorman T, 2016, NAT CELL BIOL, V18, P337, DOI 10.1038/ncb3300
   Kuroyanagi H, 2013, NUCLEIC ACIDS RES, V41, P4015, DOI 10.1093/nar/gkt097
   Kuroyanagi H, 2013, PLOS GENET, V9, DOI 10.1371/journal.pgen.1003337
   Kuyumcu-Martinez NM, 2007, MOL CELL, V28, P68, DOI 10.1016/j.molcel.2007.07.027
   Ladd AN, 2005, MOL CELL BIOL, V25, P6267, DOI 10.1128/MCB.25.14.6267-6278.2005
   Ladd AN, 2001, MOL CELL BIOL, V21, P1285, DOI 10.1128/MCB.21.4.1285-1296.2001
   Lang AE, 2021, J DEV BIOL, V9, DOI 10.3390/jdb9010007
   Li DX, 2001, GENOMICS, V74, P396, DOI 10.1006/geno.2001.6558
   Li H, 2009, BIOINFORMATICS, V25, P1754, DOI [10.1093/bioinformatics/btp698, 10.1093/bioinformatics/btp324, 10.1093/bioinformatics/btp352]
   Liao Y, 2014, BIOINFORMATICS, V30, P923, DOI 10.1093/bioinformatics/btt656
   Loria PM, 2003, CURR BIOL, V13, P1317, DOI 10.1016/S0960-9822(03)00532-3
   Love MI, 2014, GENOME BIOL, V15, DOI 10.1186/s13059-014-0550-8
   Lundquist EA, 1996, DEVELOPMENT, V122, P1601
   Maloof JN, 1999, DEVELOPMENT, V126, P37
   Masuda H, 2012, FEBS LETT, V586, P740, DOI 10.1016/j.febslet.2012.01.031
   Merz DC, 2003, DEV BIOL, V256, P173, DOI 10.1016/S0012-1606(03)00014-9
   Middelkoop Teije C, 2014, WormBook, P1, DOI 10.1895/wormbook.1.173.1
   Middelkoop TC, 2012, DEV BIOL, V361, P338, DOI 10.1016/j.ydbio.2011.10.029
   Milne CA, 1999, CURR BIOL, V9, P1243, DOI 10.1016/S0960-9822(99)80504-1
   Mullen GP, 1999, MOL BIOL CELL, V10, P3205, DOI 10.1091/mbc.10.10.3205
   Norris AD, 2014, MOL CELL, V54, P946, DOI 10.1016/j.molcel.2014.05.004
   Ochs ME, 2020, G3-GENES GENOM GENET, V10, P2365, DOI 10.1534/g3.120.401182
   Pan CL, 2008, DEV CELL, V14, P132, DOI 10.1016/j.devcel.2007.12.001
   Pertea M, 2016, NAT PROTOC, V11, P1650, DOI 10.1038/nprot.2016.095
   Pertea M, 2015, NAT BIOTECHNOL, V33, P290, DOI 10.1038/nbt.3122
   Robinson JT, 2011, NAT BIOTECHNOL, V29, P24, DOI 10.1038/nbt.1754
   ROGALSKI TM, 1995, GENETICS, V139, P159
   Rogalski TM, 2001, BIOCHEM SOC T, V29, P171, DOI 10.1042/BST0290171
   ROGALSKI TM, 1993, GENE DEV, V7, P1471, DOI 10.1101/gad.7.8.1471
   Santoro M, 2010, EXP MOL PATHOL, V89, P158, DOI 10.1016/j.yexmp.2010.05.007
   Savkur RS, 2001, NAT GENET, V29, P40, DOI 10.1038/ng704
   Sawa Hitoshi, 2013, WormBook, P1, DOI 10.1895/wormbook.1.7.2
   Schoser B, 2010, CURR GENOMICS, V11, P77, DOI 10.2174/138920210790886844
   Singh NN, 2011, MOL CELL BIOL, V31, P935, DOI 10.1128/MCB.00945-10
   Sofola OA, 2007, NEURON, V55, P565, DOI 10.1016/j.neuron.2007.07.021
   Spencer WC, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0112102
   Spike CA, 2002, DEVELOPMENT, V129, P4999
   SULSTON JE, 1977, DEV BIOL, V56, P110, DOI 10.1016/0012-1606(77)90158-0
   Sundararajan L, 2015, G3-GENES GENOM GENET, V5, P1567, DOI 10.1534/g3.115.018770
   Sundararajan L, 2014, DEV BIOL, V392, P141, DOI 10.1016/j.ydbio.2014.06.009
   Sundararajan L, 2012, GENETICS, V192, P1373, DOI 10.1534/genetics.112.145706
   Sureau A, 2011, EXP CELL RES, V317, P94, DOI 10.1016/j.yexcr.2010.09.010
   Suzuki H, 2002, GENES CELLS, V7, P133, DOI 10.1046/j.1356-9597.2001.00506.x
   Tamayo JV, 2013, BMC GENOMICS, V14, DOI 10.1186/1471-2164-14-304
   Taylor SR, 2020, MOL TOPOGRAPHY ENTIR
   Terenzi F, 2009, J MOL CELL CARDIOL, V46, P395, DOI 10.1016/j.yjmcc.2008.10.030
   Thorvaldsdóttir H, 2013, BRIEF BIOINFORM, V14, P178, DOI 10.1093/bib/bbs017
   Timchenko NA, 2004, J BIOL CHEM, V279, P13129, DOI 10.1074/jbc.M312923200
   Timchenko NA, 2001, J BIOL CHEM, V276, P7820, DOI 10.1074/jbc.M005960200
   Wang XM, 2015, DEV BIOL, V399, P306, DOI 10.1016/j.ydbio.2015.01.007
   Watabe E, 2018, CYTOSKELETON, V75, P427, DOI 10.1002/cm.21489
   Wickham H, 2009, USE R, P1, DOI 10.1007/978-0-387-98141-3_1
   Wijsman EM, 2011, PLOS GENET, V7, DOI 10.1371/journal.pgen.1001308
   WILLIAMS BD, 1994, J CELL BIOL, V124, P475, DOI 10.1083/jcb.124.4.475
   Zhang C, 2012, RNA BIOL, V9, P1045, DOI 10.4161/rna.21246
   Zinovyeva AY, 2008, GENETICS, V179, P1357, DOI 10.1534/genetics.108.090290
NR 92
TC 2
Z9 2
U1 0
U2 6
PU BMC
PI LONDON
PA CAMPUS, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
SN 1471-2164
J9 BMC GENOMICS
JI BMC Genomics
PD JAN 6
PY 2022
VL 23
IS 1
AR 13
DI 10.1186/s12864-021-08217-6
PG 20
WC Biotechnology & Applied Microbiology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biotechnology & Applied Microbiology; Genetics & Heredity
GA YC0QS
UT WOS:000739405400002
PM 34986795
OA gold, Green Published, Green Submitted
DA 2025-04-10
ER

PT J
AU Vesel, S
   Stopar-Obreza, M
   Trebusak-Podkrajsek, K
   Jazbec, J
   Podnar, T
   Battelino, T
AF Vesel, S
   Stopar-Obreza, M
   Trebusak-Podkrajsek, K
   Jazbec, J
   Podnar, T
   Battelino, T
TI A novel mutation in the G4.5 (TAZ) gene in a kindred with Barth syndrome
SO EUROPEAN JOURNAL OF HUMAN GENETICS
LA English
DT Article
DE dilated cardiomyopathy; Barth syndrome; G4.5 (TAZ) gene mutations;
   neutropenia; organic aciduria
ID X-LINKED GENE; CARDIOMYOPATHY; NONCOMPACTION; NEUTROPENIA
AB Barth syndrome is an X-linked recessive disorder characterised by dilated cardiomyopathy and a variable expression of skeletal myopathy, short statue and neutropenia. Molecular genetic analysis is currently the most reliable diagnostic method. A kindred with a novel 535delC mutation in the G4.5 (TAZ) gene responsible for Barth syndrome is presented. Beside the patient, the same mutation was detected in patient's mother and grandmother. In contrast to the so far reported patients with mutations in the same region of G4.5 (TAZ) gene, the patient described here has only a mild and transitory clinical presentation. This could be attributed to alternative splicing of G4.5 (TAZ) gene, since mRNA lacking exon 6 (with 535delC mutation) was detected. Genetic analysis of the G4.5 (TAZ) gene was helpful for establishing the precise diagnosis of Barth syndrome and for adequate genetic counselling. Predicting the phenotype on the basis of mutations is unreliable especially if mutations are localised in alternatively spliced exons of the G4.5 (TAZ) gene which may result in a milder clinical presentation than expected.
C1 Univ Childrens Hosp, Cardiol Unit, SI-1000 Ljubljana, Slovenia.
   Univ Childrens Hosp, Ctr Med Genet, SI-1000 Ljubljana, Slovenia.
   Univ Childrens Hosp, Hematol & Oncol Unit, SI-1000 Ljubljana, Slovenia.
   Univ Childrens Hosp, Dept Paediat Endocrinol Diabet & Metab, SI-1000 Ljubljana, Slovenia.
C3 University Medical Centre Ljubljana; University Medical Centre
   Ljubljana; University Medical Centre Ljubljana; University Medical
   Centre Ljubljana
RP Battelino, T (corresponding author), Univ Childrens Hosp, Cardiol Unit, Vrazov Trg 1, SI-1000 Ljubljana, Slovenia.
RI Trebusak Podkrajsek, Katarina/AAE-2910-2019; Battelino,
   Tadej/JMH-1811-2023
OI Trebusak Podkrajsek, Katarina/0000-0002-0154-3547; Battelino,
   Tadej/0000-0002-0273-4732
CR BARTH PG, 1983, J NEUROL SCI, V62, P327, DOI 10.1016/0022-510X(83)90209-5
   Barth PG, 1999, J PEDIATR-US, V135, P273, DOI 10.1016/S0022-3476(99)70118-6
   Bione S, 1996, NAT GENET, V12, P385, DOI 10.1038/ng0496-385
   Bissler JJ, 2002, LAB INVEST, V82, P335, DOI 10.1038/labinvest.3780427
   Bleyl SB, 1997, AM J HUM GENET, V61, P868, DOI 10.1086/514879
   Cantlay AM, 1999, J PEDIATR-US, V135, P311, DOI 10.1016/S0022-3476(99)70126-5
   CHRISTODOULOU J, 1994, AM J MED GENET, V50, P255, DOI 10.1002/ajmg.1320500309
   DAdamo P, 1997, AM J HUM GENET, V61, P862, DOI 10.1086/514886
   GEDEON AK, 1995, J MED GENET, V32, P383, DOI 10.1136/jmg.32.5.383
   Ichida F, 2001, CIRCULATION, V103, P1256
   Johnston J, 1997, AM J HUM GENET, V61, P1053, DOI 10.1086/301604
   KELLEY RI, 1991, J PEDIATR-US, V119, P738, DOI 10.1016/S0022-3476(05)80289-6
   MILLER SA, 1988, NUCLEIC ACIDS RES, V16, P1215, DOI 10.1093/nar/16.3.1215
   Sakamoto O, 2001, HUM GENET, V109, P559, DOI 10.1007/s00439-001-0612-3
   Vreken P, 2000, BIOCHEM BIOPH RES CO, V279, P378, DOI 10.1006/bbrc.2000.3952
NR 15
TC 4
Z9 4
U1 0
U2 1
PU NATURE PUBLISHING GROUP
PI LONDON
PA MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
SN 1018-4813
J9 EUR J HUM GENET
JI Eur. J. Hum. Genet.
PD JAN
PY 2003
VL 11
IS 1
BP 97
EP 101
DI 10.1038/sj.ejhg.5200926
PG 5
WC Biochemistry & Molecular Biology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Genetics & Heredity
GA 640LP
UT WOS:000180690600018
PM 12529714
OA Bronze
DA 2025-04-10
ER

PT J
AU Klenke, S
   Kussmann, M
   Siffert, W
AF Klenke, Stefanie
   Kussmann, Martin
   Siffert, Winfried
TI The GNB3 C825T polymorphism as a pharmacogenetic marker in the
   treatment of hypertension, obesity, and depression
SO PHARMACOGENETICS AND GENOMICS
LA English
DT Review
DE depression; G protein; GNB3; hypertension; obesity pharmacogenetics;
   polymorphism; sibutramine
ID PROTEIN BETA-3 SUBUNIT; GENE SPLICE VARIANT; BLOOD-PRESSURE; 825T
   ALLELE; ANTIDEPRESSANT RESPONSE; SIBUTRAMINE THERAPY;
   SIGNAL-TRANSDUCTION; ETHNIC DISTRIBUTION; ADRENERGIC SYSTEM;
   WEIGHT-REDUCTION
AB Heterotrimeric guanine-binding proteins (G proteins) transmit signals from the cell surface to intracellular signal cascades. The beta 3-subunit encoded by the gene GNB3 is widely expressed and, therefore, involved in various physiological and pathophysiological processes. A C825T polymorphism located in exon 10 of GNB3 was described in 1998 and the T allele was associated with alternative splicing and with increased signal transduction in human cells and tissues. In several disease-association studies, the 825T allele could be linked to hypertension, obesity, and depression. Meta-analysis available for hypertension and depression confirmed association with these phenotypes. On the basis of these findings, subsequent studies investigated whether the C825T polymorphism serves as a pharmacogenetic marker. Most pharmacogenetic investigations have focused on the treatment of hypertension, obesity, and depression. In this study, we will comprehensively describe and discuss these studies. Pharmacogenetics and Genomics 21:594-606 (C) 2011 Wolters Kluwer Health | Lippincott Williams & Wilkins.
C1 [Klenke, Stefanie; Siffert, Winfried] Univ Duisburg Essen, Inst Pharmakogenet, D-45122 Essen, Germany.
   [Kussmann, Martin] Nestle Inst Hlth Sci, Lausanne, Switzerland.
   [Kussmann, Martin] Aarhus Univ, Fac Sci, Aarhus, Denmark.
C3 University of Duisburg Essen; Nestle SA; Nestle Research Center; Aarhus
   University
RP Klenke, S (corresponding author), Univ Duisburg Essen, Inst Pharmakogenet, Hufelandstr 55, D-45122 Essen, Germany.
EM Stefanie.Klenke@uk-essen.de
RI Kussmann, Martin/AAB-7453-2022
OI Kussmann, Martin/0000-0002-0966-2313
CR Bagos PG, 2007, J HYPERTENS, V25, P487, DOI 10.1097/HJH.0b013e328011db24
   Benjafield AV, 2001, INT J OBESITY, V25, P777, DOI 10.1038/sj.ijo.0801617
   Brand E, 2003, J HYPERTENS, V21, P729, DOI 10.1097/00004872-200304000-00016
   Filigheddu F, 2004, PHARMACOGENOMICS J, V4, P154, DOI 10.1038/sj.tpj.6500247
   Filigheddu F, 2010, PHARMACOGENOMICS, V11, P319, DOI [10.2217/pgs.09.158, 10.2217/PGS.09.158]
   Frey UH, 2008, PHARMACOGENET GENOM, V18, P141, DOI 10.1097/FPC.0b013e3282f49964
   Grudell ABM, 2008, GASTROENTEROLOGY, V135, P1142, DOI 10.1053/j.gastro.2008.07.009
   Gutersohn A, 2000, LANCET, V355, P1240, DOI 10.1016/S0140-6736(00)02093-6
   Hauner H, 2004, EXP CLIN ENDOCR DIAB, V112, P201, DOI 10.1055/s-2004-817934
   Hauner H, 2003, PHARMACOGENETICS, V13, P453, DOI 10.1097/00008571-200308000-00003
   Hauner H, 2002, HORM METAB RES, V34, P475, DOI 10.1055/s-2002-34786
   Hegele RA, 1999, GENOME RES, V9, P972, DOI 10.1101/gr.9.10.972
   Hong CJ, 2006, PHARMACOGENOMICS J, V6, P27, DOI 10.1038/sj.tpj.6500340
   Hsiao DJ, 2009, PHARMACOGENET GENOM, V19, P730, DOI 10.1097/FPC.0b013e3283307cf1
   HUDSON CJ, 1993, SYNAPSE, V13, P278, DOI 10.1002/syn.890130311
   Joyce PR, 2003, INT J NEUROPSYCHOPH, V6, P339, DOI 10.1017/S1461145703003663
   Kang RH, 2007, NEUROPSYCHOBIOLOGY, V56, P1, DOI 10.1159/000109970
   Kato M, 2010, MOL PSYCHIATR, V15, P473, DOI 10.1038/mp.2008.116
   Kato M, 2008, PROG NEURO-PSYCHOPH, V32, P1041, DOI 10.1016/j.pnpbp.2008.01.019
   Keers R, 2011, J PSYCHOPHARMACOL, V25, P867, DOI 10.1177/0269881110376683
   Lee HJ, 2004, PHARMACOGENOMICS J, V4, P29, DOI 10.1038/sj.tpj.6500217
   Lin E, 2009, PROG NEURO-PSYCHOPH, V33, P1167, DOI 10.1016/j.pnpbp.2009.06.015
   López-León S, 2008, MOL PSYCHIATR, V13, P772, DOI 10.1038/sj.mp.4002088
   Michalsen A, 2006, AM HEART J, V151, P870, DOI 10.1016/j.ahj.2005.06.025
   Michalsen A, 2009, ANN NUTR METAB, V54, P184, DOI 10.1159/000217815
   Poch E, 2002, CLIN EXP HYPERTENS, V24, P345, DOI 10.1081/CEH-120004796
   Rankinen T, 2002, PHYSIOL GENOMICS, V8, P151, DOI 10.1152/physiolgenomics.00102.2001
   Rasenick MM, 1996, J CLIN PSYCHIAT, V57, P49
   Rosskopf D, 2002, PHARMACOGENETICS, V12, P209, DOI 10.1097/00008571-200204000-00005
   Rydén M, 2002, DIABETES, V51, P1601, DOI 10.2337/diabetes.51.5.1601
   Schelleman H, 2006, PHARMACOGENOMICS J, V6, P22, DOI 10.1038/sj.tpj.6500339
   Schunkert H, 1998, HYPERTENSION, V32, P510, DOI 10.1161/01.HYP.32.3.510
   Serretti A, 2003, EUR NEUROPSYCHOPHARM, V13, P117, DOI 10.1016/S0924-977X(02)00154-2
   Siffert W, 1999, J HYPERTENS, V17, P1095, DOI 10.1097/00004872-199917080-00008
   Siffert W, 1999, J AM SOC NEPHROL, V10, P1921
   Siffert W, 1998, NAT GENET, V18, P45, DOI 10.1038/ng0198-45
   Stefan N, 2004, OBES RES, V12, P679, DOI 10.1038/oby.2004.78
   Turner ST, 2001, HYPERTENSION, V37, P739, DOI 10.1161/01.HYP.37.2.739
   Wilkie MJV, 2007, PHARMACOGENET GENOM, V17, P207, DOI 10.1097/FPC.0b013e32801a3be6
   Zill P, 2000, NEUROREPORT, V11, P1893, DOI 10.1097/00001756-200006260-00018
NR 40
TC 49
Z9 55
U1 0
U2 9
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA 530 WALNUT ST, PHILADELPHIA, PA 19106-3621 USA
SN 1744-6872
J9 PHARMACOGENET GENOM
JI Pharmacogenet. Genomics
PD SEP
PY 2011
VL 21
IS 9
BP 594
EP 606
DI 10.1097/FPC.0b013e3283491153
PG 13
WC Biotechnology & Applied Microbiology; Genetics & Heredity; Pharmacology
   & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biotechnology & Applied Microbiology; Genetics & Heredity; Pharmacology
   & Pharmacy
GA 805MO
UT WOS:000293731200011
PM 21709600
DA 2025-04-10
ER

PT J
AU Segarra-Casas, A
   Domínguez-González, C
   Hernández-Laín, A
   Sanchez-Calvin, MT
   Camacho, A
   Rivas, E
   Campo-Barasoain, A
   Madruga, M
   Ortez, C
   Natera-de Benito, D
   Nascimento, A
   Codina, A
   Rodriguez, MJ
   Gallano, P
   Gonzalez-Quereda, L
AF Segarra-Casas, Alba
   Dominguez-Gonzalez, Cristina
   Hernandez-Lain, Aurelio
   Teresa Sanchez-Calvin, Maria
   Camacho, Ana
   Rivas, Eloy
   Campo-Barasoain, Andrea
   Madruga, Marcos
   Ortez, Carlos
   Natera-de Benito, Daniel
   Nascimento, Andres
   Codina, Anna
   Jose Rodriguez, Maria
   Gallano, Pia
   Gonzalez-Quereda, Lidia
TI Genetic diagnosis of Duchenne and Becker muscular dystrophy through mRNA
   analysis: new splicing events
SO JOURNAL OF MEDICAL GENETICS
LA English
DT Article
DE Diagnosis; Frameshift Mutation; Neuromuscular Diseases;
   Cardiomyopathies; Sequence Analysis; RNA
ID DMD; EXPLANATION; VARIANTS; DATABASE
AB BackgroundUp to 7% of patients with Duchenne muscular dystrophy (DMD) or Becker muscular dystrophy (BMD) remain genetically undiagnosed after routine genetic testing. These patients are thought to carry deep intronic variants, structural variants or splicing alterations not detected through multiplex ligation-dependent probe amplification or exome sequencing. MethodsRNA was extracted from seven muscle biopsy samples of patients with genetically undiagnosed DMD/BMD after routine genetic diagnosis. RT-PCR of the DMD gene was performed to detect the presence of alternative transcripts. Droplet digital PCR and whole-genome sequencing were also performed in some patients. ResultsWe identified an alteration in the mRNA level in all the patients. We detected three pseudoexons in DMD caused by deep intronic variants, two of them not previously reported. We also identified a chromosomal rearrangement between Xp21.2 and 8p22. Furthermore, we detected three exon skipping events with unclear pathogenicity. ConclusionThese findings indicate that mRNA analysis of the DMD gene is a valuable tool to reach a precise genetic diagnosis in patients with a clinical and anatomopathological suspicion of dystrophinopathy that remain genetically undiagnosed after routine genetic testing.
C1 [Segarra-Casas, Alba; Jose Rodriguez, Maria; Gallano, Pia; Gonzalez-Quereda, Lidia] Hosp Santa Creu & Sant Pau, Inst Invest Biomed St Pau IIB St PAU, Genet Dept, Barcelona, Spain.
   [Segarra-Casas, Alba] Univ Autonoma Barcelona, Genet & Microbiol Dept, Bellaterra, Spain.
   [Dominguez-Gonzalez, Cristina] Hosp Univ 12 Octubre, Imas12 Res Inst, Neurol Dept, Neuromuscular Unit, Madrid, Spain.
   [Dominguez-Gonzalez, Cristina; Nascimento, Andres; Gallano, Pia; Gonzalez-Quereda, Lidia] Inst Salud Carlos III, Ctr Biomed Network Res Rare Dis CIBERER, Madrid, Spain.
   [Hernandez-Lain, Aurelio] Hosp Univ 12 Octubre, Imas12 Res Inst, Neuropathol Unit, Madrid, Spain.
   [Teresa Sanchez-Calvin, Maria] Hosp Univ 12 Octubre, Genet Dept, Clin Genet Unit, Madrid, Spain.
   [Teresa Sanchez-Calvin, Maria] Hosp Univ 12 Octubre, UDISGEN Unidad Dismorfol & Genet, Madrid, Spain.
   [Camacho, Ana] Univ Complutense Madrid, Hosp Univ 12 Octubre, Paediat Neurol Unit, Madrid, Spain.
   [Rivas, Eloy] Univ Seville, Hosp Univ Virgen del Rocio, Inst Biomed Sevilla, Pathol Dept,CSIC, Seville, Spain.
   [Campo-Barasoain, Andrea] Hosp Univ Virgen Macarena, UGC Pediat Dept, Seville, Spain.
   [Madruga, Marcos] Neurolinkia, Neurol Dept, Seville, Spain.
   [Madruga, Marcos] Hosp Viamed Santa Angela Cruz, Seville, Spain.
   [Ortez, Carlos; Natera-de Benito, Daniel; Nascimento, Andres] Hosp St Joan Deu, Neuromuscular Unit, Dept Neurol, Barcelona, Spain.
   [Ortez, Carlos; Natera-de Benito, Daniel; Nascimento, Andres; Codina, Anna] Inst Recerca St Joan de Nu, Appl Res Neuromuscular Dis, Barcelona, Spain.
C3 Hospital of Santa Creu i Sant Pau; Autonomous University of Barcelona;
   Hospital Universitario 12 de Octubre; CIBER - Centro de Investigacion
   Biomedica en Red; CIBERER; Instituto de Salud Carlos III; Hospital
   Universitario 12 de Octubre; Hospital Universitario 12 de Octubre;
   Hospital Universitario 12 de Octubre; Hospital Universitario 12 de
   Octubre; Complutense University of Madrid; Virgen del Rocio University
   Hospital; Consejo Superior de Investigaciones Cientificas (CSIC);
   University of Sevilla; CSIC-JA-USE - Instituto de Biomedicina de Sevilla
   (IBIS); Hospital Universitario Virgen Macarena; University of Barcelona
RP Gallano, P (corresponding author), Hosp Santa Creu & Sant Pau, Inst Invest Biomed St Pau IIB St PAU, Genet Dept, Barcelona, Spain.
EM pgallano@santpau.cat
RI Lain, Aurelio/S-6172-2018; CALVIN, MARIA TERESA/AAB-6663-2019;
   Gonzalez-Quereda, Lidia/E-7669-2013; Natera-de Benito,
   Daniel/AAC-9892-2021; Domínguez-González, Cristina/MTC-0213-2025;
   Camacho, Ana/AAB-6491-2019
OI Ortez Gonzalez, Carlos Ignacio/0000-0001-8187-8103; Dominguez,
   Cristina/0000-0001-5151-988X; Natera-de Benito,
   Daniel/0000-0001-7764-2085; Segarra Casas, Alba/0000-0001-5185-5031;
   Rivas Infante, Eloy/0000-0001-6014-8048; SANCHEZ CALVIN, MARIA
   TERESA/0000-0003-4504-4907; Nascimento, Andres/0000-0003-4952-5732;
   Gonzalez, Lidia/0000-0003-0715-6414; Camacho, Ana/0000-0002-8724-8476
FU Instituto de Salud Carlos III; FEDER, 'Una manera de hacer Europa';
   Ministerio de Universidades [FIS PI18/01585];  [FPU20/06692]
FX This study was supported by Instituto de Salud Carlos III and FEDER,
   'Una manera de hacer Europa' (grant number FIS PI18/01585, LG-Q and PG)
   and the Ministerio de Universidades (grant number FPU20/06692, AS -C).
CR Aartsma-Rus A, 2006, MUSCLE NERVE, V34, P135, DOI 10.1002/mus.20586
   Bougé AL, 2017, SCI REP-UK, V7, DOI 10.1038/srep39094
   Chen XY, 2016, BIOINFORMATICS, V32, P1220, DOI 10.1093/bioinformatics/btv710
   Cummings BB, 2017, SCI TRANSL MED, V9, DOI 10.1126/scitranslmed.aal5209
   Dent KM, 2005, AM J MED GENET A, V134A, P295, DOI 10.1002/ajmg.a.30617
   Emery A E, 1991, Neuromuscul Disord, V1, P19, DOI 10.1016/0960-8966(91)90039-U
   Juan-Mateu J, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0135189
   Lim KH, 2011, P NATL ACAD SCI USA, V108, P11093, DOI 10.1073/pnas.1101135108
   Mercuri E, 2019, LANCET, V394, P2025, DOI 10.1016/S0140-6736(19)32910-1
   Miro J, 2020, INT J MOL SCI, V21, DOI 10.3390/ijms21207803
   Monaco AP, 1988, GENOMICS, V2, P90, DOI 10.1016/0888-7543(88)90113-9
   Okubo M, 2023, HUM GENET, V142, P59, DOI 10.1007/s00439-022-02485-2
   Okubo M, 2016, J HUM GENET, V61, P483, DOI 10.1038/jhg.2016.7
   REISS J, 1994, HUM MOL GENET, V3, P295, DOI 10.1093/hmg/3.2.295
   Richards S, 2015, GENET MED, V17, P405, DOI 10.1038/gim.2015.30
   Riepe TV, 2021, HUM MUTAT, V42, P799, DOI 10.1002/humu.24212
   Tuffery-Giraud S, 2003, HUM MUTAT, V21, P608, DOI 10.1002/humu.10214
   Tuffery-Giraud S, 2017, HUM GENET, V136, P1155, DOI 10.1007/s00439-017-1820-9
   Tuffery-Giraud S, 2009, HUM MUTAT, V30, P934, DOI 10.1002/humu.20976
   Xie ZY, 2020, ANN CLIN TRANSL NEUR, V7, P2041, DOI 10.1002/acn3.51201
NR 20
TC 12
Z9 12
U1 0
U2 1
PU BMJ PUBLISHING GROUP
PI LONDON
PA BRITISH MED ASSOC HOUSE, TAVISTOCK SQUARE, LONDON WC1H 9JR, ENGLAND
SN 0022-2593
EI 1468-6244
J9 J MED GENET
JI J. Med. Genet.
PD JUN
PY 2023
VL 60
IS 6
BP 615
EP 619
DI 10.1136/jmg-2022-108828
EA DEC 2022
PG 5
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA L0ZA8
UT WOS:000900487500001
PM 36535754
OA Green Published, hybrid
DA 2025-04-10
ER

PT J
AU Mirtschink, P
   Jang, C
   Arany, Z
   Krek, W
AF Mirtschink, Peter
   Jang, Cholsoon
   Arany, Zoltan
   Krek, Wilhelm
TI Fructose metabolism, cardiometabolic risk, and the epidemic of coronary
   artery disease
SO EUROPEAN HEART JOURNAL
LA English
DT Review
DE Fructose; Cardiometabolic syndrome; Cardiac hypertrophy;
   Atherosclerosis; Nonalcoholic fatty liver disease; Diabetes type 2;
   Fructolysis; Ketohexokinase; Hypertension; Alternative splicing; SF3B1;
   HIF; Hypoxia
ID FATTY LIVER-DISEASE; DE-NOVO LIPOGENESIS; SUGAR-SWEETENED BEVERAGES;
   HEALTHY-YOUNG MEN; CARDIOVASCULAR-DISEASE; CORN SYRUP; DIETARY FRUCTOSE;
   ESC GUIDELINES; POSTPRANDIAL TRIGLYCERIDES; INSULIN SENSITIVITY
AB Despite strong indications that increased consumption of added sugars correlates with greater risks of developing cardiometabolic syndrome (CMS) and cardiovascular disease (CVD), independent of the caloric intake, the worldwide sugar consumption remains high. In considering the negative health impact of overconsumption of dietary sugars, increased attention is recently being given to the role of the fructose component of high-sugar foods in driving CMS. The primary organs capable of metabolizing fructose include liver, small intestine, and kidneys. In these organs, fructose metabolism is initiated by ketohexokinase (KHK) isoform C of the central fructose-metabolizing enzyme KHK. Emerging data suggest that this tissue restriction of fructose metabolism can be rescinded in oxygen-deprived environments. In this review, we highlight recent progress in understanding how fructose metabolism contributes to the development of major systemic pathologies that cooperatively promote CMS and CVD, reference recent insights into microenvironmental control of fructose metabolism under stress conditions and discuss how this understanding is shaping preventive actions and therapeutic approaches.
C1 [Mirtschink, Peter; Krek, Wilhelm] Swiss Fed Inst Technol, Inst Mol Hlth Sci, Dept Biol, Otto Stern Weg 7, CH-8093 Zurich, Switzerland.
   [Mirtschink, Peter] Univ Hosp Dresden, Inst Clin Chem & Lab Med, Dept Clin Pathobiochem, Fetscherstr 74, D-01307 Dresden, Germany.
   [Jang, Cholsoon; Arany, Zoltan] Univ Penn, Perelman Sch Med, Cardiovasc Inst, Dept Med, 11th Floor,3400 Civ Blvd, Philadelphia, PA 19104 USA.
   [Jang, Cholsoon; Arany, Zoltan] Univ Penn, Perelman Sch Med, Inst Diabet Obes & Metab, 11th Floor,3400 Civ Blvd, Philadelphia, PA 19104 USA.
C3 Swiss Federal Institutes of Technology Domain; ETH Zurich; Technische
   Universitat Dresden; Carl Gustav Carus University Hospital; University
   of Pennsylvania; University of Pennsylvania
RP Mirtschink, P (corresponding author), Swiss Fed Inst Technol, Inst Mol Hlth Sci, Dept Biol, Otto Stern Weg 7, CH-8093 Zurich, Switzerland.; Mirtschink, P (corresponding author), Univ Hosp Dresden, Inst Clin Chem & Lab Med, Dept Clin Pathobiochem, Fetscherstr 74, D-01307 Dresden, Germany.
EM peter.mirtschink@uniklinikum-dresden.de
OI Jang, Cholsoon/0000-0001-6651-4213
FU Swiss Heart Foundation; SNF Sinergia; NIH [NIDDK DK107667]
FX Grants from the Swiss Heart Foundation and SNF Sinergia to W. K.; and
   the NIH (NIDDK DK107667) to Z. A.
CR Abdelmalek MF, 2010, HEPATOLOGY, V51, P1961, DOI 10.1002/hep.23535
   Aeberli I, 2013, DIABETES CARE, V36, P150, DOI 10.2337/dc12-0540
   Aeberli I, 2011, AM J CLIN NUTR, V94, P479, DOI 10.3945/ajcn.111.013540
   Afonso MS, 2016, J NUTR BIOCHEM, V32, P91, DOI 10.1016/j.jnutbio.2016.01.005
   Alvarez AM, 2011, INT J ANGIOL, V20, P135, DOI 10.1055/s-0031-1284434
   Anitschkow N., 1913, CENTRALBLATT ALLGEME, V24, P1
   [Anonymous], 1976, JAMA, V235, P825
   [Anonymous], 2015, Advisory Report to the Secretary of Health and Human Services and the Secretary of Agriculture
   Ashrafian H, 2003, TRENDS GENET, V19, P263, DOI 10.1016/S0168-9525(03)00081-7
   Assy N, 2008, CAN J GASTROENTEROL, V22, P811, DOI 10.1155/2008/810961
   Balcells E, 2011, PUBLIC HEALTH NUTR, V14, P778, DOI 10.1017/S1368980010002788
   Bantle JP, 2000, AM J CLIN NUTR, V72, P1128
   Bermudez OI, 2011, ANN NUTR METAB, V57, P211, DOI 10.1159/000321542
   BOHANNON NV, 1980, J AM DIET ASSOC, V76, P555
   Bonnal S, 2012, NAT REV DRUG DISCOV, V11, P847, DOI 10.1038/nrd3823
   Borén J, 2014, CLIN CHIM ACTA, V431, P131, DOI 10.1016/j.cca.2014.01.015
   Bravo S, 2013, APPL PHYSIOL NUTR ME, V38, P681, DOI 10.1139/apnm-2012-0322
   Bray GA, 2004, AM J CLIN NUTR, V79, P537
   Bremer AA, 2010, CLIN PEDIATR, V49, P1134, DOI 10.1177/0009922810379043
   Charrez B, 2015, HORM MOL BIOL CLIN I, V22, P79, DOI 10.1515/hmbci-2015-0009
   Chatrath H, 2012, SEMIN LIVER DIS, V32, P22, DOI 10.1055/s-0032-1306423
   Choi JM, 2013, P NATL ACAD SCI USA, V110, P10171, DOI 10.1073/pnas.1300457110
   Chung M, 2014, AM J CLIN NUTR, V100, P833, DOI 10.3945/ajcn.114.086314
   Cohen DE, 2013, SEMIN LIVER DIS, V33, P380, DOI 10.1055/s-0033-1358519
   Cohen JD, 2010, AM J CARDIOL, V106, P969, DOI 10.1016/j.amjcard.2010.05.030
   CRAPO PA, 1984, AM J CLIN NUTR, V39, P525, DOI 10.1093/ajcn/39.4.525
   de Koning L, 2012, CIRCULATION, V125, P1735, DOI 10.1161/CIRCULATIONAHA.111.067017
   de Lorgeril M, 1999, CIRCULATION, V99, P779, DOI 10.1161/01.CIR.99.6.779
   de Souza RJ, 2015, BMJ-BRIT MED J, V351, DOI 10.1136/bmj.h3978
   Després JP, 2008, ARTERIOSCL THROM VAS, V28, P1039, DOI 10.1161/ATVBAHA.107.159228
   Di Cesare M, 2016, LANCET, V387, P1377, DOI 10.1016/s0140-6736(16)30054-x
   Diggle CP, 2009, J HISTOCHEM CYTOCHEM, V57, P763, DOI 10.1369/jhc.2009.953190
   Donnelly KL, 2005, J CLIN INVEST, V115, P1343, DOI [10.1172/JCI200523621, 10.1172/JCI23621]
   Drozdowski LA, 2006, WORLD J GASTROENTERO, V12, P1657, DOI 10.3748/wjg.v12.i11.1657
   Du L, 2012, MOL ENDOCRINOL, V26, P1773, DOI 10.1210/me.2012-1122
   Ebbeling CB, 2012, NEW ENGL J MED, V367, P1407, DOI 10.1056/NEJMoa1203388
   EGGLESTON LV, 1970, FEBS LETT, V6, P43, DOI 10.1016/0014-5793(70)80038-2
   Eldor R, 2009, DIABETES CARE, V32, pS384, DOI 10.2337/dc09-S345
   Estruch R, 2018, NEW ENGL J MED, V378, DOI [10.1056/NEJMoa1800389, 10.1056/NEJMoa1200303, 10.1056/nejmoa1800389]
   Fisher FM, 2017, MOL METAB, V6, P14, DOI 10.1016/j.molmet.2016.11.008
   Ford ES, 2005, DIABETES CARE, V28, P1769, DOI 10.2337/diacare.28.7.1769
   FORSTER H, 1973, DEUT MED WOCHENSCHR, V98, P1156, DOI 10.1055/s-0028-1106986
   Gakidou E, 2010, LANCET, V376, P959, DOI 10.1016/S0140-6736(10)61257-3
   Gearhardt Ashley N, 2011, Curr Drug Abuse Rev, V4, P140
   Goessling W, 2008, GASTROENTEROLOGY, V135, P1935, DOI 10.1053/j.gastro.2008.09.018
   HILL R, 1954, J BIOL CHEM, V209, P705
   HOLMES R, 1989, GUT, V30, P1667, DOI 10.1136/gut.30.12.1667
   HUTTUNEN JK, 1976, ACTA ODONTOL SCAND, V34, P345, DOI 10.3109/00016357609004646
   Ishimoto T, 2012, P NATL ACAD SCI USA, V109, P4320, DOI 10.1073/pnas.1119908109
   Ishiyama J, 2010, ATHEROSCLEROSIS, V209, P118, DOI 10.1016/j.atherosclerosis.2009.09.004
   Jameel F, 2014, LIPIDS HEALTH DIS, V13, DOI 10.1186/1476-511X-13-195
   Jin R, 2014, NUTRIENTS, V6, P3187, DOI 10.3390/nu6083187
   Johnson RK, 2009, CIRCULATION, V120, P1011, DOI 10.1161/CIRCULATIONAHA.109.192627
   Johnson RJ, 2007, AM J CLIN NUTR, V86, P899
   Johnson RJ, 2010, J AM SOC NEPHROL, V21, P2036, DOI 10.1681/ASN.2010050506
   Jornayvaz FR, 2012, CELL METAB, V15, P574, DOI 10.1016/j.cmet.2012.03.005
   Kawasaki T, 2002, DIABETES CARE, V25, P353, DOI 10.2337/diacare.25.2.353
   KEYS A, 1953, AM J PUBLIC HEALTH, V43, P1399
   KEYS A, 1995, AM J CLIN NUTR, V61, p1321S, DOI 10.1093/ajcn/61.6.1321S
   KEYS A, 1986, AM J EPIDEMIOL, V124, P903, DOI 10.1093/oxfordjournals.aje.a114480
   Kunutsor SK, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0096068
   Lambert JE, 2014, GASTROENTEROLOGY, V146, P726, DOI 10.1053/j.gastro.2013.11.049
   Lanaspa MA, 2013, NAT COMMUN, V4, DOI 10.1038/ncomms3929
   Le MT, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0157458
   Li HT, 2010, J HEPATOL, V53, P934, DOI 10.1016/j.jhep.2010.05.018
   Lim JS, 2010, NAT REV GASTRO HEPAT, V7, P251, DOI 10.1038/nrgastro.2010.41
   Loomba R, 2013, NAT REV GASTRO HEPAT, V10, P686, DOI 10.1038/nrgastro.2013.171
   Lowette Katrien, 2015, Front Nutr, V2, P5, DOI 10.3389/fnut.2015.00005
   Ludwig DS, 2001, LANCET, V357, P505, DOI 10.1016/S0140-6736(00)04041-1
   Ma WJ, 2015, AM J CLIN NUTR, V101, P153, DOI 10.3945/ajcn.114.092601
   Madan SA, 2015, EUR J GASTROEN HEPAT, V27, P1237, DOI 10.1097/MEG.0000000000000429
   Madero M, 2011, METABOLISM, V60, P1551, DOI 10.1016/j.metabol.2011.04.001
   Maersk M, 2012, AM J CLIN NUTR, V95, P283, DOI 10.3945/ajcn.111.022533
   Mager DR, 2015, JPEN-PARENTER ENTER, V39, P73, DOI 10.1177/0148607113501201
   Mahmod M, 2014, J CARDIOVASC MAGN R, V16, DOI 10.1186/1532-429X-16-29
   Malik VS, 2010, CIRCULATION, V121, P1356, DOI 10.1161/CIRCULATIONAHA.109.876185
   Maryanoff BE, 2011, ACS MED CHEM LETT, V2, P538, DOI 10.1021/ml200070g
   Mirtschink P, 2016, BBA-MOL CELL RES, V1863, P1822, DOI 10.1016/j.bbamcr.2016.02.011
   Mirtschink P, 2015, NATURE, V522, P444, DOI 10.1038/nature14508
   Montalescot G, 2013, EUR HEART J, V34, P2949, DOI 10.1093/eurheartj/eht296
   O'Keefe JH, 2007, AM J CARDIOL, V100, P899, DOI 10.1016/j.amjcard.2007.03.107
   Ouyang X, 2008, J HEPATOL, V48, P993, DOI 10.1016/j.jhep.2008.02.011
   Owen JL, 2012, P NATL ACAD SCI USA, V109, P16184, DOI 10.1073/pnas.1213343109
   Page KA, 2013, JAMA-J AM MED ASSOC, V309, P63, DOI 10.1001/jama.2012.116975
   Papandreou D, 2012, APPETITE, V59, P939, DOI 10.1016/j.appet.2012.09.006
   Park TJ, 2017, SCIENCE, V356, P305, DOI 10.1126/science.aab3896
   Patel C, 2015, FASEB J, V29, P4046, DOI 10.1096/fj.15-272195
   Piepoli MF, 2016, EUR HEART J, V37, P2315, DOI 10.1093/eurheartj/ehw106
   Poirier P, 2006, CIRCULATION, V113, P898, DOI 10.1161/CIRCULATIONAHA.106.171016
   Ponikowski P, 2016, EUR HEART J, V37, P2129, DOI 10.1093/eurheartj/ehw128
   Popkin BM, 2012, NUTR REV, V70, P3, DOI 10.1111/j.1753-4887.2011.00456.x
   Praagman J, 2016, ARTERIOSCL THROM VAS, V36, P2011, DOI 10.1161/ATVBAHA.116.307578
   Quercioli A, 2011, EUR HEART J, V32, P1369, DOI 10.1093/eurheartj/ehr029
   Ramsden CE, 2016, BMJ-BRIT MED J, V353, DOI 10.1136/bmj.i1246
   Rhee JJ, 2012, PUBLIC HEALTH NUTR, V15, P1347, DOI 10.1017/S1368980012001000
   RUMESSEN JJ, 1986, GUT, V27, P1161, DOI 10.1136/gut.27.10.1161
   Rydén L, 2013, EUR HEART J, V34, P3035, DOI 10.1093/eurheartj/eht108
   Saggerson D, 2008, ANNU REV NUTR, V28, P253, DOI 10.1146/annurev.nutr.28.061807.155434
   Sattar N, 2016, LANCET DIABETES ENDO, V4, P403, DOI 10.1016/S2213-8587(16)00003-6
   Scheidt-Nave C, 2013, BUNDESGESUNDHEITSBLA, V56, P661, DOI 10.1007/s00103-013-1670-0
   Schindhelm RK, 2007, ATHEROSCLEROSIS, V191, P391, DOI 10.1016/j.atherosclerosis.2006.04.006
   Schwarz JM, 2015, J CLIN ENDOCR METAB, V100, P2434, DOI 10.1210/jc.2014-3678
   Siegel KR, 2012, DIABETES RES CLIN PR, V96, P76, DOI 10.1016/j.diabres.2011.11.014
   Skoog SM, 2004, AM J GASTROENTEROL, V99, P2046, DOI 10.1111/j.1572-0241.2004.40266.x
   Softic S, 2016, DIGEST DIS SCI, V61, P1282, DOI 10.1007/s10620-016-4054-0
   Sokka T, 2008, CLIN EXP RHEUMATOL, V26, pS35, DOI 10.1161/CIRCULATIONAHA.109.192644
   Solga S, 2004, DIGEST DIS SCI, V49, P1578, DOI 10.1023/B:DDAS.0000043367.69470.b7
   Soltani Z, 2013, CURR HYPERTENS REP, V15, P175, DOI 10.1007/s11906-013-0344-5
   Stanhope KL, 2016, CRIT REV CL LAB SCI, V53, P52, DOI 10.3109/10408363.2015.1084990
   Stanhope KL, 2015, AM J CLIN NUTR, V101, P1144, DOI 10.3945/ajcn.114.100461
   Stanhope KL, 2011, J CLIN ENDOCR METAB, V96, pE1596, DOI 10.1210/jc.2011-1251
   Stanhope KL, 2009, J CLIN INVEST, V119, P1322, DOI 10.1172/JCI37385
   Strable MS, 2010, CRIT REV BIOCHEM MOL, V45, P199, DOI 10.3109/10409231003667500
   Targher G, 2010, NEW ENGL J MED, V363, P1341, DOI 10.1056/NEJMra0912063
   Te Morenga LA, 2014, AM J CLIN NUTR, V100, P65, DOI 10.3945/ajcn.113.081521
   Teff KL, 2004, J CLIN ENDOCR METAB, V89, P2963, DOI 10.1210/jc.2003-031855
   van Buul VJ, 2014, NUTR RES REV, V27, P119, DOI 10.1017/S0954422414000067
   Volynets V, 2013, EUR J NUTR, V52, P527, DOI 10.1007/s00394-012-0355-z
   Vos MB, 2009, ARCH PEDIAT ADOL MED, V163, P674, DOI 10.1001/archpediatrics.2009.93
   Wang DD, 2014, ATHEROSCLEROSIS, V232, P125, DOI 10.1016/j.atherosclerosis.2013.10.019
   Welsh JA, 2011, CIRCULATION, V123, P249, DOI 10.1161/CIRCULATIONAHA.110.972166
   Welsh JA, 2010, JAMA-J AM MED ASSOC, V303, P1490, DOI 10.1001/jama.2010.449
   Wood IS, 2007, BIOCHEM BIOPH RES CO, V361, P468, DOI 10.1016/j.bbrc.2007.07.032
   World Health Organization, 2015, Guideline: Sugars intake for adults and children
   Yamaoka K, 2012, BMC MED, V10, DOI 10.1186/1741-7015-10-138
   Yang QH, 2014, JAMA INTERN MED, V174, P516, DOI 10.1001/jamainternmed.2013.13563
   Yu ZP, 2013, NUTR RES, V33, P1043, DOI 10.1016/j.nutres.2013.07.020
   YUDKIN J, 1959, LANCET, V2, P1135
   YUDKIN J, 1964, P NUTR SOC, V23, P149, DOI 10.1079/PNS19640028
   Zelber-Sagil S, 2007, J HEPATOL, V47, P711, DOI 10.1016/j.jhep.2007.06.020
   Zhang XP, 2017, PLOS ONE, V12, DOI 10.1371/journal.pone.0176436
   Zhou B, 2016, LANCET, V387, P1513, DOI 10.1016/S0140-6736(16)00618-8
   Zubiría MG, 2013, FEBS J, V280, P5864, DOI 10.1111/febs.12511
   ,, 1961, Journal of the American Medical Association, V175, P389
NR 134
TC 68
Z9 75
U1 4
U2 45
PU OXFORD UNIV PRESS
PI OXFORD
PA GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND
SN 0195-668X
EI 1522-9645
J9 EUR HEART J
JI Eur. Heart J.
PD JUL 7
PY 2018
VL 39
IS 26
BP 2497
EP +
DI 10.1093/eurheartj/ehx518
PG 12
WC Cardiac & Cardiovascular Systems
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology
GA GM9GI
UT WOS:000438554000012
PM 29020416
OA Green Published, Bronze
DA 2025-04-10
ER

PT J
AU Mancuso, N
   Gayther, S
   Gusev, A
   Zheng, W
   Penney, KL
   Kote-Jarai, Z
   Eeles, R
   Freedman, M
   Haiman, C
   Pasaniuc, B
AF Mancuso, Nicholas
   Gayther, Simon
   Gusev, Alexander
   Zheng, Wei
   Penney, Kathryn L.
   Kote-Jarai, Zsofia
   Eeles, Rosalind
   Freedman, Matthew
   Haiman, Christopher
   Pasaniuc, Bogdan
CA PRACTICAL Consortium
TI Large-scale transcriptome-wide association study identifies new prostate
   cancer risk regions
SO NATURE COMMUNICATIONS
LA English
DT Article
ID GENE-EXPRESSION; SUSCEPTIBILITY LOCI; CARDIOVASCULAR RISK; CAUSAL GENES;
   HERITABILITY; MULTIPLE; VARIANTS; COMMON; GWAS
AB Although genome-wide association studies (GWAS) for prostate cancer (PrCa) have identified more than 100 risk regions, most of the risk genes at these regions remain largely unknown. Here we integrate the largest PrCa GWAS (N = 142,392) with gene expression measured in 45 tissues (N = 4458), including normal and tumor prostate, to perform a multi-tissue transcriptome-wide association study (TWAS) for PrCa. We identify 217 genes at 84 independent 1 Mb regions associated with PrCa risk, 9 of which are regions with no genome-wide significant SNP within 2 Mb. 23 genes are significant in TWAS only for alternative splicing models in prostate tumor thus supporting the hypothesis of splicing driving risk for continued oncogenesis. Finally, we use a Bayesian probabilistic approach to estimate credible sets of genes containing the causal gene at a pre-defined level; this reduced the list of 217 associations to 109 genes in the 90% credible set. Overall, our findings highlight the power of integrating expression with PrCa GWAS to identify novel risk loci and prioritize putative causal genes at known risk loci.
C1 [Mancuso, Nicholas; Pasaniuc, Bogdan] Univ Calif Los Angeles, David Geffen Sch Med, Dept Pathol & Lab Med, Los Angeles, CA 90095 USA.
   [Gayther, Simon] Cedars Sinai Med Ctr, Ctr Bioinformat & Funct Genom, Los Angeles, CA 90048 USA.
   [Gusev, Alexander] Dana Farber Canc Inst, Boston, MA 02215 USA.
   [Zheng, Wei] Vanderbilt Univ, Sch Med, Vanderbilt Ingram Canc Ctr, Vanderbilt Epidemiol Ctr,Dept Med,Div Epidemiol, Nashville, TN 37232 USA.
   [Penney, Kathryn L.] Harvard TH Chan Sch Publ Hlth, Dept Epidemiol, Boston, MA 02115 USA.
   [Penney, Kathryn L.] Harvard Med Sch, Brigham & Womens Hosp, Dept Med, Channing Div Network Med, Boston, MA 02115 USA.
   [Kote-Jarai, Zsofia; Eeles, Rosalind] Inst Canc Res, Div Genet & Epidemiol, London SW7 3RP, England.
   [Kote-Jarai, Zsofia; Eeles, Rosalind] Royal Marsden NHS Fdn Trust, London SW3 6JJ, England.
   [Freedman, Matthew] Dana Farber Canc Inst, Dept Med Oncol, Boston, MA 02215 USA.
   [Freedman, Matthew] Harvard Med Sch, Boston, MA 02215 USA.
   [Haiman, Christopher] Univ Southern Calif, Keck Sch Med, Norris Comprehens Canc Ctr, Dept Prevent Med, Los Angeles, CA 90015 USA.
   [Pasaniuc, Bogdan] Univ Calif Los Angeles, David Geffen Sch Med, Dept Human Genet, Los Angeles, CA 90095 USA.
   [Pasaniuc, Bogdan] Univ Calif Los Angeles, Bioinformat Interdept Program, Los Angeles, CA 90095 USA.
C3 University of California System; University of California Los Angeles;
   University of California Los Angeles Medical Center; David Geffen School
   of Medicine at UCLA; Cedars Sinai Medical Center; Harvard University;
   Harvard University Medical Affiliates; Dana-Farber Cancer Institute;
   Vanderbilt University; Harvard University; Harvard T.H. Chan School of
   Public Health; Harvard University; Harvard University Medical
   Affiliates; Brigham & Women's Hospital; Harvard Medical School;
   University of London; Institute of Cancer Research - UK; Royal Marsden
   NHS Foundation Trust; Royal Marsden NHS Foundation Trust; Harvard
   University; Harvard University Medical Affiliates; Dana-Farber Cancer
   Institute; Harvard University; Harvard Medical School; University of
   Southern California; University of California System; University of
   California Los Angeles; University of California Los Angeles Medical
   Center; David Geffen School of Medicine at UCLA; University of
   California System; University of California Los Angeles
RP Mancuso, N (corresponding author), Univ Calif Los Angeles, David Geffen Sch Med, Dept Pathol & Lab Med, Los Angeles, CA 90095 USA.
EM nmancuso@mednet.ucla.edu
RI Mancuso, Nicholas/GLQ-8627-2022; Haiman, Christopher/HGC-5586-2022;
   Pasaniuc, Bogdan/E-9310-2012; Zheng, Wei/O-3351-2013; Claessens,
   Frank/M-8565-2016; Menegaux, Florence/H-4261-2018; West, Catharine Mary
   Louise/J-4152-2012
OI Townsend, Paul A./0000-0001-8956-9508; Sorensen, Karina
   Dalsgaard/0000-0002-4902-5490; Lessel, Davor/0000-0003-4496-244X;
   Claessens, Frank/0000-0002-8676-7709; Vega, Ana/0000-0002-7416-5137;
   Menegaux, Florence/0000-0003-3363-6411; John,
   Esther/0000-0003-3259-8003; Hamdy, Freddie Charles/0000-0003-2627-2154;
   Gago, Manuela/0000-0001-6713-4351; Donovan, Jenny L/0000-0002-6488-5472;
   Nordestgaard, Borge/0000-0002-1954-7220; Koutros,
   Stella/0000-0001-5294-5485; Mancuso, Nicholas/0000-0002-9352-5927;
   batra, Jyotsna/0000-0003-4646-6247; Pashayan, Nora/0000-0003-0843-2468;
   Schleutker, Johanna/0000-0002-1863-0305; Eeles,
   Rosalind/0000-0002-3698-6241; West, Catharine Mary
   Louise/0000-0002-0839-3449; Schumacher, Fredrick/0000-0002-3073-7463;
   Kraft, Peter/0000-0002-4472-8103
FU NIH [R01-HG009120, R01-HG006399, U01-CA194393]; European Commission's
   Seventh Framework Programme [223175 (HEALTH-F2-2009-223175)]; Cancer
   Research UK [C5047/A7357, C1287/A16563, C5047/A3354, C5047/A10692,
   C16913/A6135, C1287/A10118, C1287/A 10710, C12292/A11174, C1281/A12014,
   C5047/A8384, C5047/A15007, C8197/A16565]; National Institute of Health
   (NIH) Cancer Post-Cancer GWAS initiative grant [1U19 CA 148537-01];
   Institute of Cancer Research and The Everyman Campaign; Prostate Cancer
   Research Foundation; Prostate Action; Orchid Cancer Appeal; National
   Cancer Research Network UK; National Cancer Research Institute (NCRI)
   UK; NIHR; National Health and Medical Research Council, Australia
   [126402, 209057, 251533, 396414, 450104, 504700, 504702, 504715, 623204,
   940394, 614296]; VicHealth; Cancer Council Victoria; Prostate Cancer
   Foundation of Australia; Whitten Foundation; Price Waterhouse Coopers;
   Tattersall's; US National Institutes of Health (NIH) [U19 CA 148537,
   X01HG007492, HHSN268201200008I]; NIH NCI [U01 CA188392]; European
   Community's Seventh Framework Programme [223175
   (HEALTH-F2-2009-223175)]; National Institutes of Health [CA128978];
   Post-Cancer GWAS initiative [1U19 CA148537, 1U19 CA148065, 1U19
   CA148112]; Department of Defence [W81XWH-10-1-0341]; Canadian Institutes
   of Health Research (CIHR); Komen Foundation for the Cure; Breast Cancer
   Research Foundation; Ovarian Cancer Research Fund; US National
   Institutes of Health, National Cancer Institute [U01-CA98233,
   U01-CA98710, U01-CA98216, U01-CA98758]; US National Institutes of
   Health, National Cancer Institute (Intramural Research Program of
   NIH/National Cancer Institute, Division of Cancer Epidemiology and
   Genetics); Swedish Cancer Foundation [09-0677, 11-484, 12-823]; Cancer
   Risk Prediction Center (CRisP); Linneus Centre [70867902]; Swedish
   Research Council; Swedish Research Council [K2010-70X-20430-04-3,
   2014-2269]; Intramural Research Program, Division of Cancer Epidemiology
   and Genetics, National Cancer Institute, National Institutes of Health;
   NIHR Biomedical Research Centre at the University of Cambridge; Canadian
   Institutes of Health Research; National Human Genome Research Institute
   [R01HG009120] Funding Source: NIH RePORTER; MRC [MR/N003284/1] Funding
   Source: UKRI
FX We wish to thank all GWAS study groups contributing to the meta-analysis
   dataset from which the transcriptome-wide association analyses were
   conducted: BPC3 (Breast and Prostate Cancer Cohort Consortium); CAPS
   (Cancer of the Prostate in Sweden); PEGASUS (Prostate Cancer Genome-wide
   Association Study of Uncommon Susceptibility Loci); APCB BioResource
   (Australian Prostate Cancer BioResource); and The PRACTICAL (Prostate
   Cancer Association Group to Investigate Cancer-Associated Alterations in
   the Genome) Consortium. This work was supported by NIH grants
   R01-HG009120, R01-HG006399, and U01-CA194393. This work was supported by
   the Canadian Institutes of Health Research, European Commission's
   Seventh Framework Programme grant agreement no 223175
   (HEALTH-F2-2009-223175), Cancer Research UK Grants C5047/A7357,
   C1287/A10118, C1287/A16563, C5047/A3354, C5047/A10692, C16913/A6135, and
   The National Institute of Health (NIH) Cancer Post-Cancer GWAS
   initiative grant: No. 1U19 CA 148537-01 (the GAME-ON initiative). We
   thank the following for funding support: The Institute of Cancer
   Research and The Everyman Campaign, The Prostate Cancer Research
   Foundation, Prostate Research Campaign UK (now Prostate Action), The
   Orchid Cancer Appeal, The National Cancer Research Network UK, The
   National Cancer Research Institute (NCRI) UK. We are grateful for
   support of NIHR funding to the NIHR Biomedical Research Centre at The
   Institute of Cancer Research and The Royal Marsden NHS Foundation Trust
   and the NIHR Biomedical Research Centre at the University of Cambridge.
   The Prostate Cancer Program of Cancer Council Victoria also acknowledge
   grant support from The National Health and Medical Research Council,
   Australia (126402, 209057, 251533, 396414, 450104, 504700, 504702,
   504715, 623204, 940394, and 614296), VicHealth, Cancer Council Victoria,
   The Prostate Cancer Foundation of Australia, The Whitten Foundation,
   Price Waterhouse Coopers, and Tattersall's. Genotyping of the OncoArray
   was funded by the US National Institutes of Health (NIH) [U19 CA 148537
   for ELucidating Loci Involved in Prostate cancer SuscEptibility
   (ELLIPSE) project and X01HG007492 to the Center for Inherited Disease
   Research (CIDR) under contract number HHSN268201200008I]. Additional
   analytic support was provided by NIH NCI U01 CA188392. Funding for the
   iCOGS infrastructure came from: the European Community's Seventh
   Framework Programme under grant agreement no 223175
   (HEALTH-F2-2009-223175) (COGS), Cancer Research UK (C1287/A10118,
   C1287/A 10710, C12292/A11174, C1281/A12014, C5047/A8384, C5047/A15007,
   C5047/A10692, and C8197/A16565), the National Institutes of Health
   (CA128978) and Post-Cancer GWAS initiative (1U19 CA148537, 1U19 CA148065
   and 1U19 CA148112-the GAME-ON initiative), the Department of Defence
   (W81XWH-10-1-0341), the Canadian Institutes of Health Research (CIHR)
   for the CIHR Team in Familial Risks of Breast Cancer, Komen Foundation
   for the Cure, the Breast Cancer Research Foundation, and the Ovarian
   Cancer Research Fund. The BPC3 was supported by the US National
   Institutes of Health, National Cancer Institute (cooperative agreements
   U01-CA98233 to D.J.H., U01-CA98710 to S.M.G., U01-CA98216 to E.R., and
   U01-CA98758 to B.E.H., and Intramural Research Program of NIH/National
   Cancer Institute, Division of Cancer Epidemiology and Genetics). CAPS
   GWAS study was supported by the Swedish Cancer Foundation (grant no
   09-0677, 11-484, 12-823), the Cancer Risk Prediction Center (CRisP;
   www.crispcenter. org), a Linneus Centre (Contract ID 70867902) financed
   by the Swedish Research Council, Swedish Research Council (grant no
   K2010-70X-20430-04-3, 2014-2269). PEGASUS was supported by the
   Intramural Research Program, Division of Cancer Epidemiology and
   Genetics, National Cancer Institute, National Institutes of Health.
CR Abeshouse A, 2015, CELL, V163, P1011, DOI 10.1016/j.cell.2015.10.025
   Al Olama AA, 2015, HUM MOL GENET, V24, P5589, DOI 10.1093/hmg/ddv203
   Al Olama AA, 2014, NAT GENET, V46, P1103, DOI 10.1038/ng.3094
   Al Olama AA, 2009, NAT GENET, V41, P1058, DOI 10.1038/ng.452
   Altshuler DM, 2010, NATURE, V467, P52, DOI 10.1038/nature09298
   Bu HJ, 2016, HUM MUTAT, V37, P52, DOI 10.1002/humu.22909
   Chen W, 2015, GENETICS, V200, P719, DOI 10.1534/genetics.115.176107
   Chun S, 2017, NAT GENET, V49, P600, DOI 10.1038/ng.3795
   Darido C, 2011, CANCER CELL, V20, P635, DOI 10.1016/j.ccr.2011.10.014
   de los Campos G, 2013, PLOS GENET, V9, DOI 10.1371/journal.pgen.1003608
   Eeles RA, 2008, NAT GENET, V40, P316, DOI 10.1038/ng.90
   Eeles RA, 2013, NAT GENET, V45, P385, DOI 10.1038/ng.2560
   Fromer M, 2016, NAT NEUROSCI, V19, P1442, DOI 10.1038/nn.4399
   Gamazon ER, 2015, NAT GENET, V47, P1091, DOI 10.1038/ng.3367
   Grisanzio C, 2012, P NATL ACAD SCI USA, V109, P11252, DOI 10.1073/pnas.1200853109
   Gusev A, 2018, NAT GENET, V50, P538, DOI 10.1038/s41588-018-0092-1
   Gusev A, 2016, NAT COMMUN, V7, DOI 10.1038/ncomms10979
   Gusev A, 2016, NAT GENET, V48, P245, DOI 10.1038/ng.3506
   Gutierrez-Arcelus M, 2015, PLOS GENET, V11, DOI 10.1371/journal.pgen.1004958
   Hazelett DJ, 2014, PLOS GENET, V10, DOI 10.1371/journal.pgen.1004102
   Hjelmborg JB, 2014, CANCER EPIDEM BIOMAR, V23, P2303, DOI 10.1158/1055-9965.EPI-13-0568
   Hormozdiari F, 2015, BIOINFORMATICS, V31, P206, DOI 10.1093/bioinformatics/btv240
   Huang QL, 2014, NAT GENET, V46, P126, DOI 10.1038/ng.2862
   Kundaje A, 2015, NATURE, V518, P317, DOI 10.1038/nature14248
   Li QY, 2014, HUM MOL GENET, V23, P5294, DOI 10.1093/hmg/ddu228
   Li YI, 2016, SCIENCE, V352, P600, DOI 10.1126/science.aad9417
   Lonsdale J, 2013, NAT GENET, V45, P580, DOI 10.1038/ng.2653
   Maller JB, 2012, NAT GENET, V44, P1294, DOI 10.1038/ng.2435
   Mancuso N, 2017, AM J HUM GENET, V100, P473, DOI 10.1016/j.ajhg.2017.01.031
   Matesic LE, 2001, P NATL ACAD SCI USA, V98, P10238, DOI 10.1073/pnas.181336698
   Maurano MT, 2012, SCIENCE, V337, P1190, DOI 10.1126/science.1222794
   McCarthy S, 2016, NAT GENET, V48, P1279, DOI 10.1038/ng.3643
   Mucci LA, 2016, JAMA-J AM MED ASSOC, V315, P68, DOI 10.1001/jama.2015.17703
   Nicolae DL, 2010, PLOS GENET, V6, DOI 10.1371/journal.pgen.1000888
   Nuotio J, 2014, SCAND J PUBLIC HEALT, V42, P563, DOI 10.1177/1403494814541597
   Pavlides JMW, 2016, GENOME MED, V8, DOI 10.1186/s13073-016-0338-4
   Penney KL, 2015, CANCER EPIDEM BIOMAR, V24, P255, DOI 10.1158/1055-9965.EPI-14-0694-T
   Pomerantz MM, 2010, PLOS GENET, V6, DOI 10.1371/journal.pgen.1001204
   Raitakari OT, 2008, INT J EPIDEMIOL, V37, P1220, DOI 10.1093/ije/dym225
   Schumacher FR, 2018, NAT GENET, V50, P928, DOI 10.1038/s41588-018-0142-8
   Siegel RL, 2016, CA-CANCER J CLIN, V66, P7, DOI 10.3322/caac.21332
   Spisák S, 2015, NAT MED, V21, P1357, DOI 10.1038/nm.3975
   Stancáková A, 2012, DIABETES, V61, P1895, DOI 10.2337/db11-1378
   Stancáková A, 2009, DIABETES, V58, P1212, DOI 10.2337/db08-1607
   Sutcliffe S, 2014, PROSTATE, V74, P569, DOI 10.1002/pros.22778
   The 1000 Genomes Project Consortium, 2015, NATURE, V526, P68
   Thibodeau SN, 2015, NAT COMMUN, V6, DOI 10.1038/ncomms9653
   Verhaagh S, 1999, GENOMICS, V55, P209, DOI 10.1006/geno.1998.5639
   Weinstein JN, 2013, NAT GENET, V45, P1113, DOI 10.1038/ng.2764
   Whitington T, 2016, NAT GENET, V48, P387, DOI 10.1038/ng.3523
   Wright FA, 2014, NAT GENET, V46, P430, DOI 10.1038/ng.2951
   Xu X, 2014, EUR J HUM GENET, V22, P558, DOI 10.1038/ejhg.2013.195
   Yang J, 2004, CANCER RES, V64, P5597, DOI 10.1158/0008-5472.CAN-04-0603
   Young MD, 2010, GENOME BIOL, V11, DOI 10.1186/gb-2010-11-2-r14
   Yuan F, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0069317
   Zhou X, 2013, PLOS GENET, V9, DOI 10.1371/journal.pgen.1003264
   Zhu ZH, 2016, NAT GENET, V48, P481, DOI 10.1038/ng.3538
NR 57
TC 105
Z9 113
U1 0
U2 12
PU NATURE PORTFOLIO
PI BERLIN
PA HEIDELBERGER PLATZ 3, BERLIN, 14197, GERMANY
EI 2041-1723
J9 NAT COMMUN
JI Nat. Commun.
PD OCT 4
PY 2018
VL 9
AR 4079
DI 10.1038/s41467-018-06302-1
PG 11
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA GV7NN
UT WOS:000446314600002
PM 30287866
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Biadun, M
   Karelus, R
   Krowarsch, D
   Opalinski, L
   Zakrzewska, M
AF Biadun, Martyna
   Karelus, Radoslaw
   Krowarsch, Daniel
   Opalinski, Lukasz
   Zakrzewska, Malgorzata
TI FGF12: biology and function
SO DIFFERENTIATION
LA English
DT Article
DE FGF; Fibroblast growth factor; FGF12; FHF1
ID FACTOR HOMOLOGOUS FACTORS; GROWTH-FACTOR 12; NERVOUS-SYSTEM; FIBROBLAST;
   MODULATION; EXPRESSION; GENE; MUTATIONS
AB Fibroblast growth factor 12 (FGF12) belongs to the fibroblast growth factor homologous factors (FHF) subfamily, which is also known as the FGF11 subfamily. The human FGF12 gene is located on chromosome 3 and consists of four introns and five coding exons. Their alternative splicing results in two FGF12 isoforms - the shorter 'b' isoform and the longer 'a' isoform. Structurally, the core domain of FGF12, is highly homologous to that of the other FGF proteins, providing the classical tertiary structure of beta-trefoil. FGF12 is expressed in various tissues, most abundantly in excitable cells such as neurons and cardiomyocytes. For many years, FGF12 was thought to be exclusively an intracellular protein, but recent studies have shown that it can be secreted despite the absence of a canonical signal for secretion. The best-studied function of FGF12 relates to its interaction with sodium channels. In addition, FGF12 forms complexes with signaling proteins, regulates the cytoskeletal system, binds to the FGF receptors activating signaling cascades to prevent apoptosis and interacts with the ribosome biogenesis complex. Importantly, FGF12 has been linked to nervous system disorders, cancers and cardiac diseases such as epileptic encephalopathy, pulmonary hypertension and cardiac arrhythmias, making it a potential target for gene therapy as well as a therapeutic agent.
C1 [Biadun, Martyna; Karelus, Radoslaw; Opalinski, Lukasz; Zakrzewska, Malgorzata] Univ Wroclaw, Fac Biotechnol, Dept Prot Engn, Joliot Curie 14a, PL-50383 Wroclaw, Poland.
   [Biadun, Martyna; Krowarsch, Daniel] Univ Wroclaw, Fac Biotechnol, Dept Prot Biotechnol, Joliot Curie 14a, PL-50383 Wroclaw, Poland.
C3 University of Wroclaw; University of Wroclaw
RP Zakrzewska, M (corresponding author), Univ Wroclaw, Fac Biotechnol, Dept Prot Engn, Joliot Curie 14a, PL-50383 Wroclaw, Poland.
EM malgorzata.zakrzewska@uwr.edu.pl
RI Biadun, Martyna/LDG-2310-2024
OI Karelus, Radoslaw/0000-0002-2316-9867; Opalinski,
   Lukasz/0000-0001-9656-8714; Biadun, Martyna/0000-0002-2648-6593;
   Zakrzewska, Malgorzata/0000-0001-8214-1533; Krowarsch,
   Daniel/0000-0003-2856-218X
FU National Science Centre in Poland [2018/31/B/NZ3/01656]
FX This work was funded by National Science Centre in Poland, OPUS grant
   2018/31/B/NZ3/01656.
CR Al-Mehmadi S, 2016, NEUROL-GENET, V2, DOI 10.1212/NXG.0000000000000115
   Amin AS, 2010, PFLUG ARCH EUR J PHY, V460, P223, DOI 10.1007/s00424-009-0761-0
   Antzelevitch C, 2007, CIRCULATION, V115, P442, DOI 10.1161/CIRCULATIONAHA.106.668392
   Bhushan A, 2017, OMICS, V21, P616, DOI 10.1089/omi.2017.0116
   Biadun M, 2023, FASEB J, V37, DOI 10.1096/fj.202300324R
   Cao GM, 2022, CELL COMMUN SIGNAL, V20, DOI 10.1186/s12964-022-00993-2
   Chen Y, 2021, J CLIN LAB ANAL, V35, DOI 10.1002/jcla.24018
   Dover K, 2010, J PHYSIOL-LONDON, V588, P3695, DOI 10.1113/jphysiol.2010.192559
   Duan C, 2010, ARTHRITIS RHEUM-US, V62, P771, DOI 10.1002/art.27282
   Feng PC, 2021, FRONT GENET, V12, DOI 10.3389/fgene.2021.625414
   Gao XY, 2022, BIOMED RES INT, V2022, DOI 10.1155/2022/9948461
   Goetz R, 2009, J BIOL CHEM, V284, P17883, DOI 10.1074/jbc.M109.001842
   Goldfarb M, 2005, CYTOKINE GROWTH F R, V16, P215, DOI 10.1016/j.cytogfr.2005.02.002
   Goldfarb M, 2007, NEURON, V55, P449, DOI 10.1016/j.neuron.2007.07.006
   Guella I, 2016, NEUROL-GENET, V2, DOI 10.1212/NXG.0000000000000120
   Hanada Y, 2018, SCI REP-UK, V8, DOI 10.1038/s41598-018-28618-0
   Hartung H, 1997, MECH DEVELOP, V64, P31, DOI 10.1016/S0925-4773(97)00042-7
   Hennessey JA, 2013, HEART RHYTHM, V10, P1886, DOI 10.1016/j.hrthm.2013.09.064
   König HG, 2012, J CELL SCI, V125, P6058, DOI 10.1242/jcs.111880
   Koffler T, 2015, OTOLARYNG CLIN N AM, V48, P1041, DOI 10.1016/j.otc.2015.07.007
   Liu CJ, 2003, J BIOL CHEM, V278, P1029, DOI 10.1074/jbc.M207074200
   Liu CJ, 2001, J BIOL CHEM, V276, P18925, DOI 10.1074/jbc.M101606200
   Liu Y, 1997, CYTOGENET CELL GENET, V78, P48, DOI 10.1159/000134625
   MARAZITA ML, 1993, AM J MED GENET, V46, P486, DOI 10.1002/ajmg.1320460504
   Mertins P, 2016, NATURE, V534, P55, DOI 10.1038/nature18003
   Mohammadi M, 2005, CYTOKINE GROWTH F R, V16, P107, DOI 10.1016/j.cytogfr.2005.01.008
   Munoz-Sanjuan I, 1999, DEVELOPMENT, V126, P409
   Munoz-Sanjuan I, 2000, J BIOL CHEM, V275, P2589, DOI 10.1074/jbc.275.4.2589
   Nakayama F, 2014, INT J RADIAT ONCOL, V88, P377, DOI 10.1016/j.ijrobp.2013.10.035
   Nakayama F, 2011, J BIOL CHEM, V286, P25823, DOI 10.1074/jbc.M110.198267
   Olsen SK, 2003, J BIOL CHEM, V278, P34226, DOI 10.1074/jbc.M303183200
   Ornitz DM, 2022, WIRES MECH DIS, V14, DOI 10.1002/wsbm.1549
   Pablo JL, 2016, NEUROSCIENTIST, V22, P19, DOI 10.1177/1073858414562217
   Rejali L, 2023, ENVIRON RES, V239, DOI 10.1016/j.envres.2023.117117
   Santucci J III, 2022, CIRC-ARRHYTHMIA ELEC, V15, DOI 10.1161/CIRCEP.122.011296
   Schoorlemmer J, 2002, J BIOL CHEM, V277, P49111, DOI 10.1074/jbc.M205520200
   Schoorlemmer J, 2001, CURR BIOL, V11, P793, DOI 10.1016/S0960-9822(01)00232-9
   Seiffert S, 2022, EBIOMEDICINE, V83, DOI 10.1016/j.ebiom.2022.104234
   Siekierska A, 2016, NEUROLOGY, V86, P2162, DOI 10.1212/WNL.0000000000002752
   Smallwood PM, 1996, P NATL ACAD SCI USA, V93, P9850, DOI 10.1073/pnas.93.18.9850
   Sochacka M, 2022, CELL COMMUN SIGNAL, V20, DOI 10.1186/s12964-022-01000-4
   Sochacka M, 2020, CELL COMMUN SIGNAL, V18, DOI 10.1186/s12964-020-00573-2
   Song SH, 2016, ARTERIOSCL THROM VAS, V36, P1928, DOI 10.1161/ATVBAHA.116.308017
   Steinlein OK, 2014, PROG BRAIN RES, V213, P97, DOI [10.1016/B978-0-444-63326-2.000053, 10.1016/B978-0-444-63326-2.00005-3]
   Stone R., 2009, Science, V324, DOI [10.1126/science.3241378, DOI 10.1126/SCIENCE.3241378]
   Takeguchi R, 2018, BRAIN DEV-JPN, V40, P728, DOI 10.1016/j.braindev.2018.04.002
   Velísková J, 2021, EPILEPSIA, V62, P1546, DOI 10.1111/epi.16916
   Wang CJ, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms5896
   Wildburger NC, 2015, MOL CELL PROTEOMICS, V14, P1288, DOI 10.1074/mcp.M114.040055
   Wu D, 2019, CANCER MED-US, V8, P1576, DOI 10.1002/cam4.2055
   Xiao YC, 2022, ELIFE, V11, DOI 10.7554/eLife.77558
   Xu S, 2020, CANCER MED-US, V9, P7686, DOI 10.1002/cam4.3403
   Yeo Y, 2020, HYPERTENSION, V76, P1778, DOI 10.1161/HYPERTENSIONAHA.120.15068
   Yue F, 2014, NATURE, V515, P355, DOI 10.1038/nature13992
   Zhang F, 2016, FUNCT INTEGR GENOMIC, V16, P13, DOI 10.1007/s10142-015-0462-z
NR 55
TC 2
Z9 2
U1 1
U2 4
PU ELSEVIER SCI LTD
PI London
PA 125 London Wall, London, ENGLAND
SN 0301-4681
EI 1432-0436
J9 DIFFERENTIATION
JI Differentiation
PD SEP-OCT
PY 2024
VL 139
AR 100740
DI 10.1016/j.diff.2023.100740
EA SEP 2024
PG 7
WC Cell Biology; Developmental Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Developmental Biology
GA G0P2X
UT WOS:001313733900001
PM 38042708
DA 2025-04-10
ER

PT J
AU Jain, A
   Wordinger, RJ
   Yorio, T
   Clark, AF
AF Jain, Ankur
   Wordinger, Robert J.
   Yorio, Thomas
   Clark, Abbot F.
TI Role of the Alternatively Spliced Glucocorticoid Receptor Isoform GRβ in
   Steroid Responsiveness and Glaucoma
SO JOURNAL OF OCULAR PHARMACOLOGY AND THERAPEUTICS
LA English
DT Review
ID TRABECULAR MESHWORK CELLS; INDUCED OCULAR HYPERTENSION; OPEN-ANGLE
   GLAUCOMA; INTRAOCULAR-PRESSURE RESPONSE; AQUEOUS-HUMOR OUTFLOW;
   NITRIC-OXIDE SYNTHASE; PROTEIN-KINASE-C; MESSENGER-RNA; TRANSCRIPTIONAL
   ACTIVATION; IMMUNOPHILIN FKBP51
AB Glucocorticoid (GC)-induced ocular hypertension (OHT) is a serious side effect of GC therapy in susceptible individuals. This OHT is due to increased aqueous humor (AH) outflow resistance in the trabecular meshwork (TM) caused by GC-mediated changes in TM structure and function. GCs may also play a role in the development of primary open-angle glaucoma (POAG). Elevated cortisol levels in the AH or enhanced GC sensitivity may be one of the reasons for elevated intraocular pressure in POAG patients. The GC OHT responder population is at greater risk of developing POAG compared with non-responders. We recently have gained insight into the molecular mechanisms responsible for this differential GC responsiveness, which is attributed to differences in GC receptor isoform expression in the TM. This article summarizes current knowledge on alternative GC receptor splicing to generate GC receptor alpha (GR alpha) and GR beta and their roles in the regulation of GC responsiveness in normal and glaucoma TM.
C1 [Jain, Ankur; Wordinger, Robert J.; Clark, Abbot F.] Univ N Texas, Hlth Sci Ctr, Dept Cell Biol & Immunol, Ft Worth, TX 76107 USA.
   [Jain, Ankur; Wordinger, Robert J.; Yorio, Thomas; Clark, Abbot F.] Univ N Texas, Hlth Sci Ctr, North Texas Eye Res Inst, Ft Worth, TX 76107 USA.
   [Yorio, Thomas] Univ N Texas, Hlth Sci Ctr, Dept Pharmacol & Neurosci, Ft Worth, TX 76107 USA.
C3 University of North Texas System; University of North Texas Health
   Science Center; University of North Texas System; University of North
   Texas Health Science Center; University of North Texas System;
   University of North Texas Health Science Center
RP Clark, AF (corresponding author), Univ N Texas, Hlth Sci Ctr, North Texas Eye Res Inst, CBH 441,3500 Camp Bowie Blvd, Ft Worth, TX 76107 USA.
EM abe.clark@unthsc.edu
RI Wordinger, Robert/A-6811-2009
OI Wordinger, Robert/0000-0002-2861-8967
FU NEI/NIH [R01 EY016242]
FX This work was supported by NEI/NIH grant R01 EY016242.
CR ARMALY MF, 1965, FED PROC, V24, P1274
   Ayroldi E, 2012, FASEB J, V26, P4805, DOI 10.1096/fj.12-216382
   Bell LM, 2000, J BIOL CHEM, V275, P25262, DOI 10.1074/jbc.M002076200
   Black DL, 2003, ANNU REV BIOCHEM, V72, P291, DOI 10.1146/annurev.biochem.72.121801.161720
   Blencowe BJ, 2000, TRENDS BIOCHEM SCI, V25, P106, DOI 10.1016/S0968-0004(00)01549-8
   Borrás T, 1999, GENE THER, V6, P515, DOI 10.1038/sj.gt.3300860
   Borras T, 1998, INVEST OPHTH VIS SCI, V39, P1503
   Bouazza B, 2014, AM J RESP CELL MOL, V50, P301, DOI 10.1165/rcmb.2012-0522OC
   Cáceres JF, 1998, GENE DEV, V12, P55, DOI 10.1101/gad.12.1.55
   Chen SY, 1997, J BIOL CHEM, V272, P14087, DOI 10.1074/jbc.272.22.14087
   Clark AF, 2009, EXP EYE RES, V88, P752, DOI 10.1016/j.exer.2008.10.004
   Clark AF, 2005, CELL MOTIL CYTOSKEL, V60, P83, DOI 10.1002/cm.20049
   CLARK AF, 1994, INVEST OPHTH VIS SCI, V35, P281
   Clark AF, 2001, INVEST OPHTH VIS SCI, V42, P1769
   CLARK AF, 1995, INVEST OPHTH VIS SCI, V36, P478
   Croxtall JD, 2000, BRIT J PHARMACOL, V130, P289, DOI 10.1038/sj.bjp.0703272
   Derijk RH, 2001, J RHEUMATOL, V28, P2383
   Dickerson JE, 1998, EXP EYE RES, V66, P731, DOI 10.1006/exer.1997.0470
   DuBois DC, 2013, STEROIDS, V78, P312, DOI 10.1016/j.steroids.2012.11.014
   Fingert JH, 2001, INVEST OPHTH VIS SCI, V42, P145
   Fingert JH, 2010, MOL VIS, V16, P596
   GADSON P, 1990, J CELL BIOCHEM, V43, P185, DOI 10.1002/jcb.240430209
   Gerometta R, 2004, ARCH OPHTHALMOL-CHIC, V122, P1492, DOI 10.1001/archopht.122.10.1492
   Gerometta R, 2009, INVEST OPHTH VIS SCI, V50, P669, DOI 10.1167/iovs.08-2410
   Hafezi-Moghadam A, 2002, NAT MED, V8, P473, DOI 10.1038/nm0502-473
   Hägg PM, 2010, BRIT J DERMATOL, V162, P318, DOI 10.1111/j.1365-2133.2009.09518.x
   Hamid QA, 1999, AM J RESP CRIT CARE, V159, P1600, DOI 10.1164/ajrccm.159.5.9804131
   Hamilos DL, 2001, J ALLERGY CLIN IMMUN, V108, P59
   Hinds TD, 2010, MOL ENDOCRINOL, V24, P1715, DOI 10.1210/me.2009-0411
   Honda M, 2000, GASTROENTEROLOGY, V118, P859, DOI 10.1016/S0016-5085(00)70172-7
   Huang YQ, 2003, MOL CELL, V11, P837, DOI 10.1016/S1097-2765(03)00089-3
   Huang YQ, 2001, MOL CELL, V7, P899, DOI 10.1016/S1097-2765(01)00233-7
   Hulley PA, 1998, ENDOCRINOLOGY, V139, P2423, DOI 10.1210/en.139.5.2423
   Jain A, 2013, INVEST OPHTH VIS SCI, V54, P3137, DOI 10.1167/iovs.12-11480
   Jain A, 2012, INVEST OPHTH VIS SCI, V53, P857, DOI 10.1167/iovs.11-8497
   Karmakar S, 2013, J BIOL CHEM, V288, P24020, DOI 10.1074/jbc.M113.473819
   Kino T, 2003, J STEROID BIOCHEM, V85, P457, DOI 10.1016/S0960-0760(03)00218-8
   Kino T, 2009, BIOCHEM BIOPH RES CO, V381, P671, DOI 10.1016/j.bbrc.2009.02.110
   KITAZAWA Y, 1981, ARCH OPHTHALMOL-CHIC, V99, P813
   Ko MK, 2013, MOL VIS, V19, P2561
   KOHTZ JD, 1994, NATURE, V368, P119, DOI 10.1038/368119a0
   Krstic MD, 1997, MOL CELL BIOL, V17, P3947, DOI 10.1128/MCB.17.7.3947
   LEWIS JM, 1988, AM J OPHTHALMOL, V106, P607, DOI 10.1016/0002-9394(88)90595-8
   Li Wen, 2012, Zhonghua Yi Xue Za Zhi, V92, P2570
   Limbourg FP, 2002, J CLIN INVEST, V110, P1729, DOI 10.1172/JCI200215481
   Liu XY, 2013, J NAT PROD, V76, P685, DOI 10.1021/np300913h
   Loewen N, 2004, INVEST OPHTH VIS SCI, V45, P3091, DOI 10.1167/iovs.04-0366
   Loewen N, 2002, INVEST OPHTH VIS SCI, V43, P3686
   Longui CA, 2000, HORM METAB RES, V32, P401, DOI 10.1055/s-2007-978661
   LORENZETTI OJ, 1970, J PHARMACOL EXP THER, V175, P763
   Lu NZ, 2005, MOL CELL, V18, P331, DOI 10.1016/j.molcel.2005.03.025
   Lucki A., 2013, J NEURAL TRANSM
   Mao WM, 2011, INVEST OPHTH VIS SCI, V52, P8068, DOI 10.1167/iovs.11-8133
   Martinez-Contreras R, 2007, ADV EXP MED BIOL, V623, P123, DOI 10.1007/978-0-387-77374-2_8
   Matsumoto Y, 1997, INVEST OPHTH VIS SCI, V38, P1902
   MCCONKEY DJ, 1989, J BIOL CHEM, V264, P13399
   McKay LI, 1998, MOL ENDOCRINOL, V12, P45, DOI 10.1210/mend.12.1.0044
   Michlewski G, 2008, MOL CELL, V30, P179, DOI 10.1016/j.molcel.2008.03.013
   MIGLIORATI G, 1992, Pharmacological Research, V26, P5
   Mitchell RA, 1999, J BIOL CHEM, V274, P18100, DOI 10.1074/jbc.274.25.18100
   Nguyen TD, 1998, J BIOL CHEM, V273, P6341, DOI 10.1074/jbc.273.11.6341
   Oakley RH, 1996, J BIOL CHEM, V271, P9550, DOI 10.1074/jbc.271.16.9550
   Pan Q, 2008, NAT GENET, V40, P1413, DOI 10.1038/ng.259
   RAY S, 1977, ANN OPHTHALMOL, V9, P1151
   Reynolds PD, 1999, J CLIN ENDOCR METAB, V84, P663, DOI 10.1210/jc.84.2.663
   ROZSIVAL P, 1981, CURR EYE RES, V1, P391, DOI 10.3109/02713688109019976
   SAMPLES JR, 1993, INVEST OPHTH VIS SCI, V34, P3386
   Sanford JR, 2004, GENE DEV, V18, P755, DOI 10.1101/gad.286404
   Savory JGA, 2001, MOL CELL BIOL, V21, P781, DOI 10.1128/MCB.21.3.781-793.2001
   Sawaguchi K, 2005, OPHTHALMIC RES, V37, P235, DOI 10.1159/000086946
   Scammell JG, 2001, GEN COMP ENDOCR, V124, P152, DOI 10.1006/gcen.2001.7696
   Schaaf MJM, 2008, ENDOCRINOLOGY, V149, P1591, DOI 10.1210/en.2007-1364
   SCHULE R, 1990, CELL, V62, P1217, DOI 10.1016/0092-8674(90)90397-W
   SCHWARTZ B, 1987, ARCH OPHTHALMOL-CHIC, V105, P1060
   Seftor R E, 1994, J Glaucoma, V3, P323
   Smith R S, 2001, BMC Dev Biol, V1, P3, DOI 10.1186/1471-213X-1-3
   SNYDER RW, 1993, EXP EYE RES, V57, P461, DOI 10.1006/exer.1993.1148
   Song CZ, 1999, P NATL ACAD SCI USA, V96, P11776, DOI 10.1073/pnas.96.21.11776
   STEELY HT, 1992, INVEST OPHTH VIS SCI, V33, P2242
   Swantek JL, 1997, MOL CELL BIOL, V17, P6274, DOI 10.1128/MCB.17.11.6274
   Vandevyver S, 2013, ENDOCRINOLOGY, V154, P993, DOI 10.1210/en.2012-2045
   Walker BR, 1998, HYPERTENSION, V31, P891, DOI 10.1161/01.HYP.31.4.891
   Whitlock NA, 2010, INVEST OPHTH VIS SCI, V51, P6496, DOI 10.1167/iovs.10-5430
   Will CL, 2011, CSH PERSPECT BIOL, V3, DOI 10.1101/cshperspect.a003707
   Wordinger RJ, 1999, PROG RETIN EYE RES, V18, P629, DOI 10.1016/S1350-9462(98)00035-4
   WU JY, 1993, CELL, V75, P1061, DOI 10.1016/0092-8674(93)90316-I
   Yan XB, 2010, MOL BIOL REP, V37, P1427, DOI 10.1007/s11033-009-9529-z
   YUN AJ, 1989, INVEST OPHTH VIS SCI, V30, P2012
   ZHAN GL, 1992, EXP EYE RES, V54, P211, DOI 10.1016/S0014-4835(05)80210-6
   Zhang Hong, 2006, Zhonghua Yan Ke Za Zhi, V42, P431
   Zhang XY, 2008, INVEST OPHTH VIS SCI, V49, P1037, DOI 10.1167/iovs.07-1279
   Zhang XY, 2007, EXP EYE RES, V84, P275, DOI 10.1016/j.exer.2006.09.022
   Zhang XY, 2006, INVEST OPHTH VIS SCI, V47, P700, DOI 10.1167/iovs.05-0697
   Zhang XY, 2005, INVEST OPHTH VIS SCI, V46, P4607, DOI 10.1167/iovs.05-0571
   Zhou LL, 1998, INT J MOL MED, V1, P339
   Zhu J, 2007, BBA-MOL CELL RES, V1773, P1087, DOI 10.1016/j.bbamcr.2007.04.016
NR 96
TC 22
Z9 26
U1 0
U2 11
PU MARY ANN LIEBERT, INC
PI NEW ROCHELLE
PA 140 HUGUENOT STREET, 3RD FL, NEW ROCHELLE, NY 10801 USA
SN 1080-7683
EI 1557-7732
J9 J OCUL PHARMACOL TH
JI J. Ocular Pharmacol. Ther.
PD MAR 1
PY 2014
VL 30
IS 2-3
SI SI
BP 121
EP 127
DI 10.1089/jop.2013.0239
PG 7
WC Ophthalmology; Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Ophthalmology; Pharmacology & Pharmacy
GA AE1XA
UT WOS:000333765100009
PM 24506296
OA Green Published
DA 2025-04-10
ER

PT J
AU Keyfi, F
   Sankian, M
   Moghaddassian, M
   Rolfs, A
   Varasteh, AR
AF Keyfi, F.
   Sankian, M.
   Moghaddassian, M.
   Rolfs, A.
   Varasteh, A. R.
TI Molecular, biochemical, and structural analysis of a novel mutation in
   patients with methylmalonyl-CoA mutase deficiency
SO GENE
LA English
DT Article
DE Mutation analysis; MUT gene; Biochemical analysis; Structural analysis;
   Methylmalonic aciduria
ID SWISS-MODEL; COMPLEMENTATION GROUP; IDENTIFICATION; ACIDEMIA; ACIDURIA;
   GENE; ENVIRONMENT; PROGRAM; MUT(0); LOCUS
AB Background: Methylmalonic aciduria (MMA) is an inborn error of metabolism resulting from genetic defects in methylmalonyl-CoA mutase (MCM). This enzyme is encoded by the MUT gene and is required for the degradation of odd-chain fatty adds, the amino adds valine, isoleucine, methionine, and threonine, and cholesterol.
   Method: Three unrelated affected patients with isolated MMA and their parents were studied. The MUT gene was analyzed by PCR and sequencing of its entire coding region and the highly conserved exon-intron splice junctions. The homology modeling of the novel mutation found in the MUT gene was performed using the online Swiss-Prot server for automated modeling and then analyzed with special bioinformatics software to better study the structural effects caused by the mutation.
   Result: We found one homozygous nucleotide change in intron 12 of the MUT gene (c.2125-3 C> G). The variant is located near the highly conserved acceptor splice site of intron 12. A region at the C-terminus of the protein from ASP709 to GLN748 has been deleted by the alteration of c.2125-3 C> Gin intron 12 of the MUTgene. Further studies of the novel mutation in the MUT gene by means of homology modeling revealed abnormalities in the protein's structure, which causes the protein to act malfunctioning and also the mRNA expression analysis of MUT gene confirmed these results.
   Conclusion: We report this novel mutation, including its clinical and biochemical features and genetic defects, in the MUTgene of three patients affected with isolated MMA. Structural analyses of the mutated protein identified changes in the energy and stereochemical features of the protein that unfortunately altered the protein's functionalities. Therefore, we demonstrate that a novel splice site mutation in intron 12 of the MUTgene is a potential highly pathogenic allele via inhibition of alternative splicing. (C) 2015 Elsevier B.V. All rights reserved.
C1 [Varasteh, A. R.] Mashhad Univ Med Sci, Sch Med, Allergy Res Ctr, Mashhad, Iran.
   [Keyfi, F.; Sankian, M.] Mashhad Univ Med Sci, Sch Med, Immunol Res Ctr, Mashhad, Iran.
   [Moghaddassian, M.] Mashhad Univ Med Sci, Avicenna Res Inst, Immunol Res Ctr, Div Human Genet, Mashhad, Iran.
   [Keyfi, F.; Moghaddassian, M.; Varasteh, A. R.] Pardis Clin & Genet Lab, Mashhad, Iran.
   [Rolfs, A.] Centogene AG, Rostock, Germany.
   [Rolfs, A.] Univ Rostock, Albrecht Kossel Inst Neuroregenerat, D-18055 Rostock, Germany.
C3 Mashhad University of Medical Sciences; Mashhad University of Medical
   Sciences; Mashhad University of Medical Sciences; CENTOGENE AG;
   University of Rostock
RP Varasteh, AR (corresponding author), Mashhad Univ Med Sci, Allergy Res Ctr, Mashhad, Iran.
EM varasteha@mums.ac.ir
RI Keyfi, Fatemeh/Y-2906-2019
FU Immunology Research Center, Medical School, Mashhad University of
   Medical Sciences, Mashhad, Iran [901001]
FX This research was supported and funded by Immunology Research Center,
   Medical School, Mashhad University of Medical Sciences (901001),
   Mashhad, Iran.
CR Arnold K, 2006, BIOINFORMATICS, V22, P195, DOI 10.1093/bioinformatics/bti770
   Chandler RJ, 2005, MOL GENET METAB, V86, P34, DOI 10.1016/j.ymgme.2005.07.020
   COULOMBE JT, 1981, PEDIATRICS, V67, P26
   Dobson CM, 2002, HUM MOL GENET, V11, P3361, DOI 10.1093/hmg/11.26.3361
   Dobson CM, 2002, P NATL ACAD SCI USA, V99, P15554, DOI 10.1073/pnas.242614799
   Dündar H, 2012, MOL GENET METAB, V106, P419, DOI 10.1016/j.ymgme.2012.05.014
   Fenton W.A., 2001, METABOLIC MOL BASES, P2165
   Fowler B, 2008, J INHERIT METAB DIS, V31, P350, DOI 10.1007/s10545-008-0839-4
   Guex N, 1997, ELECTROPHORESIS, V18, P2714, DOI 10.1002/elps.1150181505
   Karimzadeh P, 2013, IRAN J CHILD NEUROL, V7, P63
   LASKOWSKI RA, 1993, J APPL CRYSTALLOGR, V26, P283, DOI 10.1107/S0021889892009944
   LEDLEY FD, 1988, AM J HUM GENET, V42, P839
   Lempp TJ, 2007, MOL GENET METAB, V90, P284, DOI 10.1016/j.ymgme.2006.10.002
   LI ZQ, 1987, P NATL ACAD SCI USA, V84, P6611, DOI 10.1073/pnas.84.19.6611
   Martínez MA, 2005, MOL GENET METAB, V84, P317, DOI 10.1016/j.ymgme.2004.11.011
   MILLER SA, 1988, NUCLEIC ACIDS RES, V16, P1215, DOI 10.1093/nar/16.3.1215
   NHAM SU, 1990, GENOMICS, V8, P710, DOI 10.1016/0888-7543(90)90259-W
   OGASAWARA M, 1994, HUM MOL GENET, V3, P867, DOI 10.1093/hmg/3.6.867
   Peters Heidi L, 2002, Hum Mutat, V20, P406, DOI 10.1002/humu.9074
   Retey J., 1982, METHYLMALONYL COA MU, P357
   Rosenberg L.E., 1989, METABOLIC BASIS INHE, P822
   Rosenblatt DS., 2001, METABOLIC MOL BASES, P3897
   Schwede T, 2003, NUCLEIC ACIDS RES, V31, P3381, DOI 10.1093/nar/gkg520
   SHEVELL MI, 1993, AM J MED GENET, V45, P619, DOI 10.1002/ajmg.1320450521
   VRIEND G, 1990, J MOL GRAPHICS, V8, P52, DOI 10.1016/0263-7855(90)80070-V
   WEINER SJ, 1984, J AM CHEM SOC, V106, P765, DOI 10.1021/ja00315a051
   Zdobnov EM, 2001, BIOINFORMATICS, V17, P847, DOI 10.1093/bioinformatics/17.9.847
NR 27
TC 7
Z9 7
U1 0
U2 13
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 0378-1119
EI 1879-0038
J9 GENE
JI Gene
PD JAN 15
PY 2016
VL 576
IS 1
BP 208
EP 213
DI 10.1016/j.gene.2015.10.002
PN 2
PG 6
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA DE2NM
UT WOS:000370464000003
PM 26449400
DA 2025-04-10
ER

PT J
AU Jia, YT
   Mao, CF
   Ma, ZH
   Huang, JQ
   Li, WQ
   Ma, XL
   Zhang, ST
   Li, MH
   Yu, F
   Sun, YY
   Chen, JZ
   Feng, J
   Zhou, Y
   Xu, QB
   Zhao, L
   Fu, Y
   Kong, W
AF Jia, Yiting
   Mao, Chenfeng
   Ma, Zihan
   Huang, Jiaqi
   Li, Wenqiang
   Ma, Xiaolong
   Zhang, Siting
   Li, Meihong
   Yu, Fang
   Sun, Yingying
   Chen, Jingzhou
   Feng, Juan
   Zhou, Yuan
   Xu, Qingbo
   Zhao, Ling
   Fu, Yi
   Kong, Wei
TI PHB2 Maintains the Contractile Phenotype of VSMCs by Counteracting PKM2
   Splicing
SO CIRCULATION RESEARCH
LA English
DT Article
DE glycolysis; hnRNPA1; neointima; PKM; prohibitin 2; restenosis; vascular
   smooth muscle cell
ID SMOOTH-MUSCLE-CELL; RNA-BINDING PROTEIN; PROHIBITIN 2; AEROBIC
   GLYCOLYSIS; HNRNP A1; RECEPTOR; PROLIFERATION; MITOCHONDRIA;
   HYPERTENSION; METABOLISM
AB Background: Phenotypic transition of vascular smooth muscle cells (VSMCs) accounts for the pathogenesis of a variety of vascular diseases during the early stage. Recent studies indicate the metabolic reprogramming may be involved in VSMC phenotypic transition. However, the definite molecules that link energy metabolism to distinct VSMC phenotype remain elusive. Methods: A carotid artery injury model was used to study postinjury neointima formation as well as VSMC phenotypic transition in vivo. RNA-seq analysis, cell migration assay, collagen gel contraction assay, wire myography assay, immunoblotting, protein interactome analysis, co-immunoprecipitation, and mammalian 2-hybrid assay were performed to clarify the phenotype and elucidate the molecular mechanisms. Results: We collected cell energy-regulating genes by using Gene Ontology annotation and applied RNA-Seq analysis of transforming growth factor-beta or platelet-derived growth factor BB stimulated VSMCs. Six candidate genes were overlapped from energy metabolism-related genes and genes reciprocally upregulated by transforming growth factor-beta and downregulated by platelet-derived growth factor BB. Among them, prohibitin 2 has been reported to regulate mitochondrial oxidative phosphorylation. Indeed, prohibitin 2-deficient VSMCs lost the contractile phenotype as evidenced by reduced contractile proteins. Consistently, Phb2(SMCKO) mice were more susceptible to postinjury VSMC proliferation and neointima formation compared with Phb2(flox/flox) mice. Further protein interactome analysis, co-immunoprecipitation, and mammalian 2-hybrid assay revealed that prohibitin 2, through its C-terminus, directly interacts with hnRNPA1, a key modulator of pyruvate kinase M1/2 (PKM) mRNA splicing that promotes PKM2 expression and glycolysis. Prohibitin 2 deficiency facilitated PKM1/2 mRNA splicing and reversion from PKM1 to PKM2, and enhanced glycolysis in VSMCs. Blocking prohibitin 2-hnRNPA1 interaction resulted in increased PKM2 expression, enhanced glycolysis, repressed contractile marker genes expression in VSMCs, as well as aggravated postinjury neointima formation in vivo. Conclusions: Prohibitin 2 maintains VSMC contractile phenotype by interacting with hnRNPA1 to counteract hnRNPA1-mediated PKM alternative splicing and glucose metabolic reprogramming.
C1 [Jia, Yiting; Mao, Chenfeng; Ma, Zihan; Huang, Jiaqi; Li, Wenqiang; Ma, Xiaolong; Zhang, Siting; Li, Meihong; Yu, Fang; Feng, Juan; Zhou, Yuan; Fu, Yi; Kong, Wei] Peking Univ, Sch Basic Med Sci, Dept Physiol & Pathophysiol, Beijing, Peoples R China.
   [Jia, Yiting; Mao, Chenfeng; Ma, Zihan; Huang, Jiaqi; Li, Wenqiang; Ma, Xiaolong; Zhang, Siting; Li, Meihong; Yu, Fang; Feng, Juan; Zhou, Yuan; Fu, Yi; Kong, Wei] Minist Educ, Key Lab Mol Cardiovasc Sci, Beijing, Peoples R China.
   [Xu, Qingbo] Kings Coll London, Cardiovasc Div, BHF Ctr, London SE5 9NU, England.
   [Xu, Qingbo] Zhejiang Univ, Affiliated Hosp 1, Dept Cardiol, Sch Med, Hangzhou, Peoples R China.
   [Zhao, Ling] Sun Yat Sen Univ, Zhongshan Ophthalm Ctr, State Key Lab Ophthalmol, Guangdong Prov Key Lab Oph Thalmol & Visual Sci, Guangzhou, Peoples R China.
   [Mao, Chenfeng] Beijing Inst Biotechnol, Beijing, Peoples R China.
   [Sun, Yingying; Chen, Jingzhou] Chinese Acad Med Sci & Peking Union Med Coll, State Key Lab Cardiovasc Dis, Natl Ctr Cardiovasc Dis, Fuwai Hosp, Beijing, Peoples R China.
C3 Peking University; University of London; King's College London; Zhejiang
   University; Sun Yat Sen University; Chinese Academy of Medical Sciences
   - Peking Union Medical College; Fu Wai Hospital - CAMS; Peking Union
   Medical College
RP Jia, YT; Kong, W (corresponding author), Peking Univ, Dept Physiol & Pathophysiol, Basic Med Coll, Beijing 100191, Peoples R China.
EM yitingjia@bjmu.edu.cn; kongw@bjmu.edu.cn
RI Feng, Juan/KEI-9730-2024; Mao, Chenfeng/GYU-9882-2022; Zhao,
   Ling/D-9005-2015; sun, yingying/KIC-6104-2024
OI Huang, Jiaqi/0000-0002-3778-2398; Jia, Yiting/0000-0002-7055-3685; Zhao,
   Ling/0000-0002-6644-2886
FU National Natural Science Foundation of P. R. China [81730010, 91539203,
   81921001, 91839302, 31930056, 81900261]
FX This work was supported by funding from the National Natural Science
   Foundation of P. R. China (NSFC, 81730010, 91539203, 81921001, 91839302,
   31930056, and 81900261).
CR Alam MA, 2016, JOVE-J VIS EXP, DOI 10.3791/53991
   Ali L, 2018, CURR OPIN LIPIDOL, V29, P475, DOI 10.1097/MOL.0000000000000550
   Alves JC, 2016, FRONT IMMUNOL, V7, DOI 10.3389/fimmu.2016.00145
   Artal-Sanz M, 2009, TRENDS ENDOCRIN MET, V20, P394, DOI 10.1016/j.tem.2009.04.004
   Badran A, 2020, INT J MOL SCI, V21, DOI 10.3390/ijms21228764
   Bavelloni A, 2015, IUBMB LIFE, V67, P239, DOI 10.1002/iub.1366
   Bennett MR, 2016, CIRC RES, V118, P692, DOI 10.1161/CIRCRESAHA.115.306361
   Buehler U, 2018, EMBO J, V37, DOI 10.15252/embj.201899429
   Calvier L, 2017, CELL METAB, V25, P1118, DOI 10.1016/j.cmet.2017.03.011
   CHAMLEYCAMPBELL J, 1979, PHYSIOL REV, V59, P1, DOI 10.1152/physrev.1979.59.1.1
   Chen M, 2010, CANCER RES, V70, P8977, DOI 10.1158/0008-5472.CAN-10-2513
   Chen SY, 2019, OPEN MED-WARSAW, V14, P663, DOI 10.1515/med-2019-0077
   Chiong M, 2013, VASA, V42, P8, DOI 10.1024/0301-1526/a000243
   Cho SG, 2019, J AM SOC NEPHROL, V30, P1174, DOI 10.1681/ASN.2018111117
   David CJ, 2010, NATURE, V463, P364, DOI 10.1038/nature08697
   Davis-Dusenbery BN, 2011, ARTERIOSCL THROM VAS, V31, P2370, DOI 10.1161/ATVBAHA.111.226670
   Dayton TL, 2016, EMBO REP, V17, P1721, DOI 10.15252/embr.201643300
   Durham AL, 2018, CARDIOVASC RES, V114, P590, DOI 10.1093/cvr/cvy010
   Grootaert MOJ, 2018, CARDIOVASC RES, V114, P622, DOI 10.1093/cvr/cvy007
   Heiss EH, 2016, VASC PHARMACOL, V83, P47, DOI 10.1016/j.vph.2016.05.002
   Hubert MO, 2021, BIO-PROTOCOL, V11, DOI 10.21769/BioProtoc.3907
   Jain M, 2021, ARTERIOSCL THROM VAS, V41, P1724, DOI 10.1161/ATVBAHA.121.316021
   Jia YT, 2018, CELL DEATH DIS, V9, DOI 10.1038/s41419-018-0703-x
   Kasashima K, 2006, J BIOL CHEM, V281, P36401, DOI 10.1074/jbc.M605260200
   Kim CS, 2007, J VIROL, V81, P3852, DOI 10.1128/JVI.01311-06
   Kim JH, 2017, BIOCHEM BIOPH RES CO, V492, P41, DOI 10.1016/j.bbrc.2017.08.041
   Kim JW, 2009, CANCER SCI, V100, P1468, DOI 10.1111/j.1349-7006.2009.01209.x
   Lambert CM, 2010, CARDIOVASC RES, V88, P196, DOI 10.1093/cvr/cvq152
   Lee SJ, 2015, SCI REP-UK, V5, DOI 10.1038/srep16577
   Liu FB, 2017, NAT CELL BIOL, V19, P1358, DOI 10.1038/ncb3630
   Liu LM, 2012, HYPERTENSION, V60, P833, DOI 10.1161/HYPERTENSIONAHA.112.195115
   Liu MJ, 2019, ARTERIOSCL THROM VAS, V39, P1715, DOI 10.1161/ATVBAHA.119.312131
   Lu SL, 2018, J MOL MED, V96, P585, DOI 10.1007/s00109-018-1645-6
   Macintyre AN, 2011, MOL CELL, V42, P713, DOI 10.1016/j.molcel.2011.06.003
   Mao CF, 2021, CIRCULATION, V144, P1244, DOI 10.1161/CIRCULATIONAHA.120.053361
   Montano MM, 1999, P NATL ACAD SCI USA, V96, P6947, DOI 10.1073/pnas.96.12.6947
   Morita M, 2018, CANCER CELL, V33, P355, DOI 10.1016/j.ccell.2018.02.004
   Oller J, 2021, CIRCULATION, V143, P2091, DOI 10.1161/CIRCULATIONAHA.120.051171
   Paronetto MP, 2007, J CELL BIOL, V176, P929, DOI 10.1083/jcb.200701005
   Peng YT, 2015, APOPTOSIS, V20, P1135, DOI 10.1007/s10495-015-1143-z
   Polier G, 2012, CHEM BIOL, V19, P1093, DOI 10.1016/j.chembiol.2012.07.012
   Rehman J, 2010, ADV EXP MED BIOL, V661, P171, DOI 10.1007/978-1-60761-500-2_11
   Ren XF, 2020, MOL CANCER, V19, DOI 10.1186/s12943-020-01153-1
   Rodríguez AI, 2015, ARTERIOSCL THROM VAS, V35, P430, DOI 10.1161/ATVBAHA.114.304936
   Rombouts KB, 2022, EUR J CLIN INVEST, V52, DOI 10.1111/eci.13697
   Rossi L, 2014, STEM CELL REV REP, V10, P871, DOI 10.1007/s12015-014-9540-1
   Salabei JK, 2013, REDOX BIOL, V1, P542, DOI 10.1016/j.redox.2013.10.011
   Sanz MA, 2003, J BIOL CHEM, V278, P32091, DOI 10.1074/jbc.M304877200
   Shi J, 2020, AM J PHYSIOL-HEART C, V319, pH613, DOI 10.1152/ajpheart.00220.2020
   SIOMI H, 1995, J CELL BIOL, V129, P551, DOI 10.1083/jcb.129.3.551
   Steglich G, 1999, MOL CELL BIOL, V19, P3435
   Strub GM, 2011, FASEB J, V25, P600, DOI 10.1096/fj.10-167502
   Su WT, 2020, VIRUSES-BASEL, V12, DOI 10.3390/v12040414
   Tatsuta T, 2017, CURR BIOL, V27, pR629, DOI 10.1016/j.cub.2017.04.030
   TERASHIMA M, 1994, EMBO J, V13, P3782, DOI 10.1002/j.1460-2075.1994.tb06689.x
   Treiber T, 2017, MOL CELL, V66, P270, DOI 10.1016/j.molcel.2017.03.014
   Wang D, 2020, CELL MOL LIFE SCI, V77, P3525, DOI 10.1007/s00018-020-03475-1
   Wang L, 2009, CIRC RES, V104, P688, DOI 10.1161/CIRCRESAHA.108.188425
   Wang PB, 2020, J TRANSL INTERN MED, V8, P80, DOI 10.2478/jtim-2020-0013
   Wei YJ, 2017, CELL, V168, P224, DOI 10.1016/j.cell.2016.11.042
   Werle M, 2005, J BIOMED SCI, V12, P827, DOI 10.1007/s11373-005-9010-5
   Wu DC, 2020, CELL DEATH DIS, V11, DOI 10.1038/s41419-020-2374-7
   Yan CJ, 2020, AUTOPHAGY, V16, P419, DOI 10.1080/15548627.2019.1628520
   Yang WW, 2012, CELL, V150, P685, DOI 10.1016/j.cell.2012.07.018
   Yao F, 2018, CIRCULATION, V138, P2274, DOI 10.1161/CIRCULATIONAHA.117.033114
   Yuan XL, 2018, CIRC RES, V123, P538, DOI 10.1161/CIRCRESAHA.118.313527
   Zhang L, 2017, ARTERIOSCL THROM VAS, V37, P2182, DOI 10.1161/ATVBAHA.117.310020
   Zhang XD, 2016, ELIFE, V5, DOI [10.7554/eLife.13374, 10.7754/eLife.13374]
   Zhao XZ, 2020, ACTA BIOCH BIOPH SIN, V52, P9, DOI 10.1093/abbs/gmz135
   Zhou QL, 2019, J CELL PHYSIOL, V234, P14413, DOI 10.1002/jcp.28218
   Zhu Y, 2021, AM J PHYSIOL-HEART C, V320, pH2222, DOI 10.1152/ajpheart.01009.2020
NR 71
TC 44
Z9 46
U1 7
U2 36
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA TWO COMMERCE SQ, 2001 MARKET ST, PHILADELPHIA, PA 19103 USA
SN 0009-7330
EI 1524-4571
J9 CIRC RES
JI Circ.Res.
PD OCT 28
PY 2022
VL 131
IS 10
BP 807
EP 824
DI 10.1161/CIRCRESAHA.122.321005
PG 18
WC Cardiac & Cardiovascular Systems; Hematology; Peripheral Vascular
   Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology; Hematology
GA 5T7QF
UT WOS:000876055300006
PM 36200440
OA Bronze
DA 2025-04-10
ER

PT J
AU Yasuhara, O
   Matsuo, A
   Bellier, JP
   Aimi, Y
AF Yasuhara, Osamu
   Matsuo, Akinori
   Bellier, Jean-Pierre
   Aimi, Yoshinari
TI Demonstration of choline acetyltransferase of a peripheral type in the
   rat heart
SO JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY
LA English
DT Article
DE acetylcholine; acetylcholinesterase; choline acetyltransferase; cardiac
   neurons; nitric oxide synthase; tyrosine hydroxylase; vesicular
   acetylcholine transporter
ID GUINEA-PIG HEART; VESICULAR ACETYLCHOLINE TRANSPORTER; ALTERNATIVE
   SPLICE VARIANT; INTRINSIC CARDIAC NEURONS; NITRIC-OXIDE SYNTHASE;
   DORSAL-ROOT GANGLION; VAGAL-STIMULATION; NERVOUS-SYSTEM; IMMUNOREACTIVE
   NERVES; CONDUCTION SYSTEM
AB Cholinergic innervation of the heart has been analyzed using cholinergic markers including acetylcholinesterase, choline acetyltransferase (ChAT), and vesicular acetylcholine transporter (VAChT). In the present study we demonstrate putative cholinergic nerves in the rat heart using an antibody to ChAT of a peripheral type (pChAT), which is the product of a splice variant of ChAT mRNA and preferentially localized to peripheral cholinergic nerves. Expression of mRNAs for pChAT and the conventional form of ChAT (cChAT) were verified in the rat atrium by RT-PCR. Localization of both protein products in the atrium was confirmed by Western blotting. Virtually all neurons and small intensely fluorescent cells in the intrinsic cardiac ganglia were stained immunohistochemically for pChAT. The density of pChAT-positive fibers was very high in the conducting system, high in both atria, the right atrium in particular, and low in the ventricular walls. pChAT and VAChT immunoreactivities were closely associated in some fibers and fiber bundles in the ventricular walls. These results indicate that intrinsic cardiac neurons homogeneously express both pChAT and cChAT. Furthermore, innervation of the ventricular walls by pChAT- and VAChT-positive fibers provides morphological evidence for a significant role of cholinergic mechanisms in ventricular functions.
C1 Shiga Univ Med Sci, Mol Neurosci Res Ctr, Otsu, Shiga 5202192, Japan.
C3 Shiga University of Medical Science
RP Yasuhara, O (corresponding author), Shiga Univ Med Sci, Mol Neurosci Res Ctr, Otsu, Shiga 5202192, Japan.
EM yasuhara@belle.shiga-med.ac.jp
RI Bellier, Jean-Pierre/M-4845-2019
OI Bellier, Jean-Pierre/0000-0002-8758-8075
CR Ando M, 2005, CIRCULATION, V112, P164, DOI 10.1161/CIRCULATIONAHA.104.525493
   Ardell J. L., 2001, HEART PHYSL PATHOPHY, P45
   Arvidsson U, 1997, J COMP NEUROL, V378, P454
   BALUK P, 1990, CELL TISSUE RES, V261, P275, DOI 10.1007/BF00318669
   BRICE A, 1989, J NEUROSCI RES, V23, P266, DOI 10.1002/jnr.490230304
   BRUCE G, 1985, J NEUROCHEM, V45, P611, DOI 10.1111/j.1471-4159.1985.tb04030.x
   Calupca MA, 2000, J COMP NEUROL, V423, P26
   Cheng ZX, 1999, J COMP NEUROL, V410, P320
   Chiocchetti R, 2003, CELL TISSUE RES, V311, P11, DOI 10.1007/s00441-002-0652-6
   CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
   COSTA M, 1992, INT CONGR SER, V1008, P115
   Crick SJ, 1996, J ANAT, V188, P403
   CRICK SJ, 1994, CIRCULATION, V89, P1697, DOI 10.1161/01.CIR.89.4.1697
   HAHN M, 1992, P NATL ACAD SCI USA, V89, P4387, DOI 10.1073/pnas.89.10.4387
   HASSALL CJS, 1992, NEUROSCI LETT, V143, P65, DOI 10.1016/0304-3940(92)90234-X
   Hoover DB, 2004, CARDIOVASC RES, V62, P112, DOI 10.1016/j.cardiores.2004.01.012
   Horackova M, 1999, CELL TISSUE RES, V297, P409, DOI 10.1007/s004410051368
   HORACKOVA M, 1995, CARDIOVASC RES, V30, P326, DOI 10.1016/0008-6363(95)00105-0
   Kanayama H, 2003, NEUROSCIENCE, V118, P243, DOI 10.1016/S0306-4522(02)00868-0
   Kawada T, 2006, LIFE SCI, V78, P882, DOI 10.1016/j.lfs.2005.05.087
   KLIMASCHEWSKI L, 1992, CIRC RES, V71, P1533, DOI 10.1161/01.RES.71.6.1533
   KOELLE GB, 1955, J PHARMACOL EXP THER, V114, P167
   Kummer W, 1998, NEUROREPORT, V9, P2209, DOI 10.1097/00001756-199807130-00011
   Leger J, 1999, J COMP NEUROL, V407, P303
   Loewi O, 1921, PFLUG ARCH GES PHYS, V189, P239, DOI 10.1007/BF01738910
   Mabe AM, 2006, CELL TISSUE RES, V326, P57, DOI 10.1007/s00441-006-0215-3
   Matsui JI, 2000, JARO-J ASSOC RES OTO, V1, P46, DOI 10.1007/s101620010005
   Mawe GM, 1996, CELL TISSUE RES, V285, P281, DOI 10.1007/s004410050645
   Nakajima K, 2000, J CHEM NEUROANAT, V18, P31, DOI 10.1016/S0891-0618(99)00058-7
   Nakanishi Y, 1999, J CHEM NEUROANAT, V17, P21, DOI 10.1016/S0891-0618(99)00020-4
   PAPKA RE, 1981, NEUROSCI LETT, V27, P47, DOI 10.1016/0304-3940(81)90204-4
   Petrecca K, 1998, J ANAT, V192, P517, DOI 10.1046/j.1469-7580.1998.19240517.x
   Richardson RJ, 2003, CELL TISSUE RES, V314, P337, DOI 10.1007/s00441-003-0805-2
   SANN H, 1995, NEUROSCI LETT, V198, P17, DOI 10.1016/0304-3940(95)11951-R
   Schäfer MKH, 1998, NEUROSCIENCE, V84, P361, DOI 10.1016/S0306-4522(97)80196-0
   Schwartz PJ., 2000, CARDIAC ELECTROPHYSI, V3rd 3, P300
   Sequeira IM, 2005, ANN ANAT, V187, P345, DOI 10.1016/j.aanat.2005.05.003
   Slavíková J, 2003, NEUROCHEM RES, V28, P593, DOI 10.1023/A:1022837810357
   STEELE PA, 1994, NEUROSCIENCE, V62, P241, DOI 10.1016/0306-4522(94)90327-1
   TAGO H, 1986, J HISTOCHEM CYTOCHEM, V34, P1431, DOI 10.1177/34.11.2430009
   Takahashi H, 2003, JPN HEART J, V44, P257, DOI 10.1536/jhj.44.257
   Tata AM, 2004, J NEUROSCI RES, V75, P194, DOI 10.1002/jnr.10855
   Tooyama I, 2000, J CHEM NEUROANAT, V17, P217, DOI 10.1016/S0891-0618(99)00043-5
   VANOLI E, 1991, CIRC RES, V68, P1471, DOI 10.1161/01.RES.68.5.1471
   WEIHE E, 1984, CELL TISSUE RES, V236, P527
   WHARTON J, 1981, NEUROSCIENCE, V6, P2193, DOI 10.1016/0306-4522(81)90007-5
   Yasuhara O, 2004, J COMP NEUROL, V472, P232, DOI 10.1002/cne.20077
   Yasuhara O, 2003, J NEUROSCI, V23, P2872
NR 48
TC 25
Z9 29
U1 0
U2 1
PU HISTOCHEMICAL SOC INC
PI SEATTLE
PA UNIV WASHINGTON, DEPT BIOSTRUCTURE, BOX 357420, SEATTLE, WA 98195 USA
SN 0022-1554
J9 J HISTOCHEM CYTOCHEM
JI J. Histochem. Cytochem.
PD MAR
PY 2007
VL 55
IS 3
BP 287
EP 299
DI 10.1369/jhc.6A7092.2006
PG 13
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA 138PW
UT WOS:000244375700009
PM 17142806
OA Bronze
DA 2025-04-10
ER

PT J
AU Folkersen, L
   Kyriakou, T
   Goel, A
   Peden, J
   Mälarstig, A
   Paulsson-Berne, G
   Hamsten, A
   Franco-Cereceda, A
   Gabrielsen, A
   Eriksson, P
   Watkins, H
AF Folkersen, Lasse
   Kyriakou, Theodosios
   Goel, Anuj
   Peden, John
   Malarstig, Anders
   Paulsson-Berne, Gabrielle
   Hamsten, Anders
   Franco-Cereceda, Anders
   Gabrielsen, Anders
   Eriksson, Per
   Watkins, Hugh
CA Hugh Watkins PROCARDIS Consortia
TI Relationship between CAD Risk Genotype in the Chromosome 9p21 Locus and
   Gene Expression. Identification of Eight New ANRIL Splice
   Variants
SO PLOS ONE
LA English
DT Article
ID CORONARY-ARTERY-DISEASE; ASSOCIATION
AB Background: Several genome-wide association studies have recently linked a group of single nucleotide polymorphisms in the 9p21 region with cardiovascular disease. The molecular mechanisms of this link are not fully understood. We investigated five different expression microarray datasets in order to determine if the genotype had effect on expression of any gene transcript in aorta, mammary artery, carotid plaque and lymphoblastoid cells.
   Methodology/Principal Findings: After multiple testing correction, no genes were found to have relation to the rs2891168 risk genotype, either on a genome-wide scale or on a regional (8 MB) scale. The neighbouring ANRIL gene was found to have eight novel transcript variants not previously known from literature and these varied by tissue type. We therefore performed a detailed probe-level analysis and found small stretches of significant relation to genotype but no consistent associations. In all investigated tissues we found an inverse correlation between ANRIL and the MTAP gene and a positive correlation between ANRIL and CDKN2A and CDKN2B.
   Conclusions/Significance: Investigation of relation of the risk genotype to gene expression is complicated by the transcript complexity of the locus. With our investigation of a range of relevant tissue we wish to underscore the need for careful attention to the complexity of the alternative splicing issues in the region and its implications to the design of future gene expression studies.
RP Folkersen, L (corresponding author), Karolinska Inst, Dept Med, Stockholm, Sweden.
EM lasse.folkersen@ki.se
OI Folkersen, Lasse/0000-0003-0708-9530; Watkins, Hugh/0000-0002-5287-9016;
   Goel, Anuj/0000-0003-2307-4021; Kyriakou,
   Theodosios/0000-0001-7794-8789; Eriksson, Per/0000-0002-5635-2692
CR Benovoy D, 2008, NUCLEIC ACIDS RES, V36, P4417, DOI 10.1093/nar/gkn409
   Bolstad BM, 2003, BIOINFORMATICS, V19, P185, DOI 10.1093/bioinformatics/19.2.185
   Broadbent HM, 2008, HUM MOL GENET, V17, P806, DOI 10.1093/hmg/ddm352
   Burton PR, 2007, NATURE, V447, P661, DOI 10.1038/nature05911
   DABNEY A, 2009, BIOCONDUCTOR
   Edgar R, 2002, NUCLEIC ACIDS RES, V30, P207, DOI 10.1093/nar/30.1.207
   FOLKERSEN L, 2009, BIOINFORMATICS
   Gentleman RC, 2004, GENOME BIOL, V5, DOI 10.1186/gb-2004-5-10-r80
   Gibbs RA, 2003, NATURE, V426, P789, DOI 10.1038/nature02168
   Helgadottir A, 2008, NAT GENET, V40, P217, DOI 10.1038/ng.72
   Helgadottir A, 2007, SCIENCE, V316, P1491, DOI 10.1126/science.1142842
   JARINOVA O, 2009, ARTERIOSCLER THROMB
   Kent WJ, 2002, GENOME RES, V12, P996, DOI 10.1101/gr.229102
   Kwan T, 2008, NAT GENET, V40, P225, DOI 10.1038/ng.2007.57
   Liu Y, 2009, PLOS ONE, V4, DOI 10.1371/journal.pone.0005027
   McPherson R, 2007, SCIENCE, V316, P1488, DOI 10.1126/science.1142447
   Pasmant E, 2007, CANCER RES, V67, P3963, DOI 10.1158/0008-5472.CAN-06-2004
   Samani NJ, 2007, NEW ENGL J MED, V357, P443, DOI 10.1056/NEJMoa072366
   Zhang W, 2008, AM J HUM GENET, V82, P631, DOI 10.1016/j.ajhg.2007.12.015
NR 19
TC 136
Z9 154
U1 0
U2 11
PU PUBLIC LIBRARY SCIENCE
PI SAN FRANCISCO
PA 1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA
SN 1932-6203
J9 PLOS ONE
JI PLoS One
PD NOV 2
PY 2009
VL 4
IS 11
AR e7677
DI 10.1371/journal.pone.0007677
PG 6
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA 514RX
UT WOS:000271414400005
PM 19888323
OA Green Submitted, Green Published, gold
DA 2025-04-10
ER

PT J
AU Hurtado, C
   Wigle, JT
   Dibrov, E
   Maddaford, TG
   Pierce, GN
AF Hurtado, Cecilia
   Wigle, Jeffrey T.
   Dibrov, Elena
   Maddaford, Thane G.
   Pierce, Grant N.
TI A comparison of adenovirally delivered molecular methods to inhibit
   Na<SUP>+</SUP>/Ca<SUP>2+</SUP> exchange
SO JOURNAL OF MOLECULAR AND CELLULAR CARDIOLOGY
LA English
DT Article
DE sodium-calcium exchanger; RNAi; siRNA; antisense; XIP; adenovirus;
   NCX1.1; NCX1.3
ID SPLICE VARIANTS; NA+-CA2+
AB The ability to use molecular biology tools to down-regulate Na+/Ca2+ exchanger (NCX) expression will allow us to better understand the 2+ regulation of Ca-i(2+) and contractility in heart. Three different techniques to deplete NCX expression were compared: short hairpin RNA (shRNA), antisense RNA and exchanger inhibitory peptide expression via adenoviral transfection. Our results demonstrate that the most efficient method to deplete NCX expression and activity from cardiomyocytes is shRNA. It is also possible to replace the endogenous NCX with alternative isoforms or mutant forms of the NCX. Adenovirally delivered shRNA is an efficient tool for the study of the NCX and could be adapted for many other cardiac proteins. (C) 2007 Elsevier Inc. All rights reserved.
C1 St Boniface Gen Hosp, Inst Cardiovasc Sci, Res Ctr, Winnipeg, MB R2H 2A6, Canada.
   Univ Manitoba, Dept Physiol, Fac Med, Winnipeg, MB R2H 2A6, Canada.
   Univ Manitoba, Fac Pharm, Winnipeg, MB R2H 2A6, Canada.
   Univ Manitoba, Dept Biochem & Med Genet, Fac Med, Winnipeg, MB R2H 2A6, Canada.
C3 University of Manitoba; Children's Hospital Research Institute of
   Manitoba; University of Manitoba; University of Manitoba; University of
   Manitoba
RP Pierce, GN (corresponding author), St Boniface Gen Hosp, Inst Cardiovasc Sci, Res Ctr, Winnipeg, MB R2H 2A6, Canada.
EM gpiercc@sbrc.ca
RI ; Wigle, Jeffrey/G-2005-2014
OI Pierce, Grant/0000-0001-7674-0142; Wigle, Jeffrey/0000-0002-4985-7684
CR BARRY WH, 1993, CIRCULATION, V87, P1806, DOI 10.1161/01.CIR.87.6.1806
   Dyck C, 1999, J GEN PHYSIOL, V114, P701, DOI 10.1085/jgp.114.5.701
   ENYEDI A, 1993, J BIOL CHEM, V268, P17120
   Hurtado C, 2006, AM J PHYSIOL-HEART C, V290, pH2155, DOI 10.1152/ajpheart.00958.2005
   Hurtado C, 2005, J MOL CELL CARDIOL, V38, P647, DOI 10.1016/j.yjmcc.2005.02.007
   LI ZP, 1991, J BIOL CHEM, V266, P1014
   LIPP P, 1995, FEBS LETT, V364, P198, DOI 10.1016/0014-5793(95)00391-L
   Maddaford TG, 1999, AM J PHYSIOL-HEART C, V277, pH788, DOI 10.1152/ajpheart.1999.277.2.H788
   MINKS MA, 1979, J BIOL CHEM, V254, P180
   Paddison PJ, 2003, CURR OPIN MOL THER, V5, P217
   Pan Y, 2000, AM J PHYSIOL-CELL PH, V279, pC393, DOI 10.1152/ajpcell.2000.279.2.C393
   SCHAGGER H, 1987, ANAL BIOCHEM, V166, P368, DOI 10.1016/0003-2697(87)90587-2
   Shuba YM, 1998, J BIOL CHEM, V273, P18819, DOI 10.1074/jbc.273.30.18819
   Tadros GM, 2002, AM J PHYSIOL-HEART C, V283, pH1616, DOI 10.1152/ajpheart.00186.2002
NR 14
TC 6
Z9 6
U1 0
U2 0
PU ELSEVIER SCI LTD
PI OXFORD
PA THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND
SN 0022-2828
EI 1095-8584
J9 J MOL CELL CARDIOL
JI J. Mol. Cell. Cardiol.
PD JUL
PY 2007
VL 43
IS 1
BP 49
EP 53
DI 10.1016/j.yjmcc.2007.04.011
PG 5
WC Cardiac & Cardiovascular Systems; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology; Cell Biology
GA 189PQ
UT WOS:000248001400007
PM 17540404
DA 2025-04-10
ER

PT J
AU Manetti, M
   Guiducci, S
   Romano, E
   Ceccarelli, C
   Bellando-Randone, S
   Conforti, ML
   Ibba-Manneschi, L
   Matucci-Cerinic, M
AF Manetti, Mirko
   Guiducci, Serena
   Romano, Eloisa
   Ceccarelli, Claudia
   Bellando-Randone, Silvia
   Conforti, Maria Letizia
   Ibba-Manneschi, Lidia
   Matucci-Cerinic, Marco
TI Overexpression of VEGF165b, an Inhibitory Splice Variant of
   Vascular Endothelial Growth Factor, Leads to Insufficient Angiogenesis
   in Patients With Systemic Sclerosis
SO CIRCULATION RESEARCH
LA English
DT Article
DE systemic sclerosis; scleroderma; peripheral vascular diseases;
   angiogenesis; antiangiogenic agents; vascular endothelial growth factor
   A
ID FACTOR VEGF; EXPRESSION; ISOFORMS; SCLERODERMA; RECEPTOR; DISEASE; SKIN;
   CLASSIFICATION; PATHOGENESIS; MECHANISMS
AB Rationale: Systemic sclerosis (SSc) is characterized by widespread microangiopathy, fibrosis, and autoimmunity. Despite the lack of angiogenesis, the expression of vascular endothelial growth factor A (VEGF) was shown to be upregulated in SSc skin and circulation; however, previous studies did not distinguish between proangiogenic VEGF(165) and antiangiogenic VEGF(165)b isoforms, which are generated by alternative splicing in the terminal exon of VEGF pre-RNA.
   Objective: We investigated whether VEGF isoform expression could be altered in skin and circulation of patients with SSc.
   Methods and Results: Here, we show that the endogenous antiangiogenic VEGF(165)b splice variant is selectively overexpressed at both the mRNA and protein levels in SSc skin. Elevated VEGF(165)b expression correlated with increased expression of profibrotic transforming growth factor-beta 1 and serine/arginine protein 55 splicing factor in keratinocytes, fibroblasts, endothelial cells, and perivascular inflammatory cells. Circulating levels of VEGF(165)b were significantly higher in patients with SSc than in control subjects. Microvascular endothelial cells (MVECs) isolated from SSc skin expressed and released higher levels of VEGF(165)b than healthy MVECs. Transforming growth factor-beta 1 upregulated the expression of VEGF(165)b and serine/arginine protein 55 in both SSc and healthy MVECs. In SSc MVECs, VEGF receptor-2 was overexpressed, but its phosphorylation was impaired. Recombinant VEGF(165)b and SSc-MVEC-conditioned medium inhibited VEGF(165)-mediated VEGF receptor-2 phosphorylation and capillary morphogenesis in healthy MVECs. The addition of anti-VEGF(165)b blocking antibodies abrogated the antiangiogenic effect of SSc-MVEC-conditioned medium. Capillary morphogenesis was severely impaired in SSc MVECs and could be ameliorated by treatment with recombinant VEGF(165) and anti-VEGF(165)b blocking antibodies.
   Conclusions: In SSc, a switch from proangiogenic to antiangiogenic VEGF isoforms may have a crucial role in the insufficient angiogenic response to chronic ischemia. (Circ Res. 2011; 109: e14-e26.)
C1 [Manetti, Mirko; Ibba-Manneschi, Lidia] Univ Florence, Dept Anat Histol & Forens Med, I-50134 Florence, Italy.
   [Manetti, Mirko; Guiducci, Serena; Romano, Eloisa; Ceccarelli, Claudia; Bellando-Randone, Silvia; Conforti, Maria Letizia; Matucci-Cerinic, Marco] Univ Florence, Dept Biomed, Div Rheumatol, AOUC, I-50134 Florence, Italy.
   [Manetti, Mirko; Guiducci, Serena; Romano, Eloisa; Ceccarelli, Claudia; Bellando-Randone, Silvia; Conforti, Maria Letizia; Matucci-Cerinic, Marco] Univ Florence, Excellence Ctr Res Transfer & High Educ DENOthe, I-50134 Florence, Italy.
C3 University of Florence; University of Florence; Azienda Ospedaliero
   Universitaria Careggi; University of Florence
RP Manetti, M (corresponding author), Univ Florence, Dept Anat Histol & Forens Med, Viale GB Morgagni 85, I-50134 Florence, Italy.
EM mirkomanetti@yahoo.it
RI Manetti, Mirko/AEH-9944-2022; MATUCCI CERINIC, MARCO/AAO-2769-2020;
   Romano, Eloisa/AEZ-7072-2022
OI Manetti, Mirko/0000-0003-3956-8480
FU Fondazione Cassa di Risparmio di Pistoia e Pescia; University of
   Florence (Progetti di Ricerca di Ateneo)
FX This work was in part supported by Fondazione Cassa di Risparmio di
   Pistoia e Pescia, and the University of Florence (Progetti di Ricerca di
   Ateneo to L. I-M. and M.M.-C.).
CR Bates DO, 2002, CANCER RES, V62, P4123
   Byrne AM, 2005, J CELL MOL MED, V9, P777, DOI 10.1111/j.1582-4934.2005.tb00379.x
   Carmeliet P, 2000, NAT MED, V6, P389, DOI 10.1038/74651
   Choi JJ, 2003, J RHEUMATOL, V30, P1529
   CLEMENTS P, 1995, J RHEUMATOL, V22, P1281
   Clements PJ, 2003, Systemic sclerosis
   D'Alessio S, 2004, ARTHRITIS RHEUM-US, V50, P3275, DOI 10.1002/art.20562
   Davies CA, 2006, HUM PATHOL, V37, P190, DOI 10.1016/j.humpath.2005.10.007
   Denton CP, 2001, CURR OPIN RHEUMATOL, V13, P505, DOI 10.1097/00002281-200111000-00010
   Díaz R, 2008, INT J CANCER, V123, P1060, DOI 10.1002/ijc.23619
   Distler O, 2004, CIRC RES, V95, P109, DOI 10.1161/01.RES.0000134644.89917.96
   Distler O, 2002, ARTHRITIS RES, V4, DOI 10.1186/ar596
   Ergorul C, 2008, MOL VIS, V14, P1517
   Ferrara N, 1997, ENDOCR REV, V18, P4, DOI 10.1210/er.18.1.4
   FOLKMAN J, 1995, NAT MED, V1, P27, DOI 10.1038/nm0195-27
   Guiducci S, 2007, AUTOIMMUN REV, V6, P520, DOI 10.1016/j.autrev.2006.12.006
   Hashimoto A, 2007, ARTHRITIS RHEUM, V56, P1094, DOI 10.1002/art.22450
   HOUCK KA, 1991, MOL ENDOCRINOL, V5, P1806, DOI 10.1210/mend-5-12-1806
   Hummers LK, 2009, J RHEUMATOL, V36, P576, DOI 10.3899/jrheum.080516
   Konopatskaya O, 2006, MOL VIS, V12, P626
   LeRoy EC, 2001, J RHEUMATOL, V28, P1573
   LeRoy EC, 1996, RHEUM DIS CLIN N AM, V22, P675, DOI 10.1016/S0889-857X(05)70295-7
   LEROY EC, 1988, J RHEUMATOL, V15, P202
   Mackiewicz Z, 2002, CLIN EXP RHEUMATOL, V20, P641
   Manconi Frank, 2000, Methods in Cell Science, V22, P89, DOI 10.1023/A:1009895723488
   Manetti M, 2010, J CELL MOL MED, V14, P1241, DOI 10.1111/j.1582-4934.2010.01027.x
   Manetti M, 2010, ANN RHEUM DIS, V69, P598, DOI 10.1136/ard.2009.119321
   Margheri F, 2006, ARTHRITIS RHEUM-US, V54, P3926, DOI 10.1002/art.22263
   Medsger T.A., 1996, Systemic Sclerosis, P51
   Neufeld G, 1999, FASEB J, V13, P9, DOI 10.1096/fasebj.13.1.9
   Neufeld G, 1996, CANCER METAST REV, V15, P153, DOI 10.1007/BF00437467
   Nowak DG, 2008, J CELL SCI, V121, P3487, DOI 10.1242/jcs.016410
   Olsson AK, 2006, NAT REV MOL CELL BIO, V7, P359, DOI 10.1038/nrm1911
   Peiris-Pagès M, 2010, J PATHOL, V222, P138, DOI 10.1002/path.2746
   Perrin RM, 2005, DIABETOLOGIA, V48, P2422, DOI 10.1007/s00125-005-1951-8
   Pritchard-Jones RO, 2007, BRIT J CANCER, V97, P223, DOI 10.1038/sj.bjc.6603839
   Qiu Y, 2009, BIOCHEM SOC T, V37, P1207, DOI 10.1042/BST0371207
   Rennel ES, 2008, BRIT J CANCER, V98, P1250, DOI 10.1038/sj.bjc.6604309
   Rennel ES, 2009, FUTURE ONCOL, V5, P703, DOI [10.2217/fon.09.33, 10.2217/FON.09.33]
   SCOTT PAE, 1993, J CELL SCI, V105, P269
   Varey AHR, 2008, BRIT J CANCER, V98, P1366, DOI 10.1038/sj.bjc.6604308
   Varga J, 2007, J CLIN INVEST, V117, P557, DOI 10.1172/JCI31139
   Woolard J, 2004, CANCER RES, V64, P7822, DOI 10.1158/0008-5472.CAN-04-0934
NR 43
TC 146
Z9 156
U1 0
U2 15
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA 530 WALNUT ST, PHILADELPHIA, PA 19106-3621 USA
SN 0009-7330
J9 CIRC RES
JI Circ.Res.
PD JUL 22
PY 2011
VL 109
IS 3
BP E14
EP U35
DI 10.1161/CIRCRESAHA.111.242057
PG 27
WC Cardiac & Cardiovascular Systems; Hematology; Peripheral Vascular
   Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology; Hematology
GA 795FG
UT WOS:000292958200001
PM 21636803
OA Bronze
DA 2025-04-10
ER

PT J
AU Patni, N
   Xing, C
   Agarwal, AK
   Garg, A
AF Patni, Nivedita
   Xing, Chao
   Agarwal, Anil K.
   Garg, Abhimanyu
TI Juvenile-onset generalized lipodystrophy due to a novel heterozygous
   missense LMNA mutation affecting lamin C
SO AMERICAN JOURNAL OF MEDICAL GENETICS PART A
LA English
DT Article
DE diabetes mellitus; generalized lipodystrophy; hepatic steatosis;
   hypertension; lamin C; LMNA
ID GENE
AB The LMNA gene contains 12 exons and encodes lamins A and C by alternative splicing within exon 10. While mutations in lamin A specific residues cause several diseases including lipodystrophy, progeria, muscular dystrophy, neuropathy, and cardiomyopathy, only three families with mutations in lamin C-specific residues are reported with cardiomyopathy, neuropathy, and muscular dystrophy so far. We now report two brothers with juvenile-onset generalized lipodystrophy due to a lamin C-specific mutation. The proband, a 23-year-old Caucasian male was reported to have generalized lipodystrophy at 3 weeks of age, developed diabetes, hypertriglyceridemia, hypertension and liver problems and died with complications of cirrhosis, and kidney failure. His younger brother, a 37-year-old Caucasian male developed generalized lipodystrophy around 2 years of age and was diagnosed with diabetes, hypertriglyceridemia, fatty liver, and hypertension at 36 years of age. Their father also died of end stage renal disease at age 52 years. Exome sequencing of the proband revealed an extremely rare missense heterozygous variant c.1711_1712CG>TC; p.(Arg571Ser) in LMNA which was confirmed by Sanger sequencing in both the patients. Interestingly, the mutation had no effect on mRNA splicing or relative expression of lamin A or C mRNA and protein in the lymphoblasts. Our observations suggest that mutant lamin C disrupts its interaction with other cellular proteins resulting in generalized lipodystrophy due to defective development and maintenance of adipose tissue.
C1 [Patni, Nivedita] UT Southwestern Med Ctr, Ctr Human Nutr, Dept Pediat, Div Pediat Endocrinol, Dallas, TX USA.
   [Xing, Chao] UT Southwestern Med Ctr, McDermott Ctr Human Growth & Dev, Dallas, TX USA.
   [Xing, Chao] UT Southwestern Med Ctr, Dept Bioinformat, Dallas, TX USA.
   [Xing, Chao] UT Southwestern Med Ctr, Dept Clin Sci, Dallas, TX USA.
   [Agarwal, Anil K.; Garg, Abhimanyu] UT Southwestern Med Ctr, Dept Internal Med, Div Nutr & Metab Dis, Dallas, TX USA.
   [Agarwal, Anil K.; Garg, Abhimanyu] UT Southwestern Med Ctr, Ctr Human Nutr, Dallas, TX USA.
C3 University of Texas System; University of Texas Southwestern Medical
   Center Dallas; University of Texas System; University of Texas
   Southwestern Medical Center Dallas; University of Texas System;
   University of Texas Southwestern Medical Center Dallas; University of
   Texas System; University of Texas Southwestern Medical Center Dallas;
   University of Texas System; University of Texas Southwestern Medical
   Center Dallas; University of Texas System; University of Texas
   Southwestern Medical Center Dallas
RP Garg, A (corresponding author), Dept Internal Med, Div Nutr & Metab Dis, 5323 Harry Hines Blvd, Dallas, TX 75390 USA.; Garg, A (corresponding author), Ctr Human Nutr, 5323 Harry Hines Blvd, Dallas, TX 75390 USA.
EM abhimanyu.garg@utsouthwestern.edu
OI Patni, Nivedita/0000-0002-5926-7784; Xing, Chao/0000-0002-1838-0502
FU National Institute of Diabetes and Digestive and Kidney Diseases
   [R01-DK105448]; National Center for Advancing Translational Sciences
   [UL1 TR001105]
FX National Institute of Diabetes and Digestive and Kidney Diseases, Grant
   number: R01-DK105448; National Center for Advancing Translational
   Sciences, Grant number: UL1 TR001105
CR Agarwal AK, 2003, J CLIN ENDOCR METAB, V88, P4840, DOI 10.1210/jc.2003-030855
   Benedetti S, 2005, J NEUROL NEUROSUR PS, V76, P1019, DOI 10.1136/jnnp.2004.046110
   Fatkin D, 1999, NEW ENGL J MED, V341, P1715, DOI 10.1056/NEJM199912023412302
   Gruenbaum Y, 2005, NAT REV MOL CELL BIO, V6, P21, DOI 10.1038/nrm1550
   Jackson AS, 2004, BRIT J NUTR, V91, P161
   Lelliott CJ, 2002, J CLIN ENDOCR METAB, V87, P728, DOI 10.1210/jc.87.2.728
   LIN F, 1993, J BIOL CHEM, V268, P16321
   Ng KK, 2013, AUSTRALAS MED J, V6, P75, DOI 10.4066/AMJ.2013.1546
   Peinado JR, 2010, PROTEOMICS, V10, P3356, DOI 10.1002/pmic.201000350
   Worman HJ, 2007, EXP CELL RES, V313, P2121, DOI 10.1016/j.yexcr.2007.03.028
NR 10
TC 13
Z9 14
U1 2
U2 11
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 1552-4825
EI 1552-4833
J9 AM J MED GENET A
JI Am. J. Med. Genet. A
PD SEP
PY 2017
VL 173
IS 9
BP 2517
EP 2521
DI 10.1002/ajmg.a.38341
PG 5
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA FD9JW
UT WOS:000407839600033
PM 28686329
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Labbé, P
   Faure, E
   Lecointe, S
   Le Scounarnec, S
   Kyndt, F
   Marrec, M
   Le Tourneau, T
   Offmann, B
   Duplaá, C
   Zaffran, S
   Schott, JJ
   Merot, J
AF Labbe, Pauline
   Faure, Emilie
   Lecointe, Simon
   Le Scounarnec, Solena
   Kyndt, Florence
   Marrec, Marie
   Le Tourneau, Thierry
   Offmann, Bernard
   Duplaa, Cecile
   Zaffran, Stephane
   Schott, Jean Jacques
   Merot, Jean
TI The alternatively spliced LRRFIP1 Isoform-1 is a key regulator of the
   Wnt/β-catenin transcription pathway
SO BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
LA English
DT Article
DE Wnt catenin transcription; Leucine rich repeat; Coiled coil domain;
   Muscle differentiation; LEF-TCF
ID LEUCINE-RICH REPEAT; ACID SENSOR LRRFIP1; FLIGHTLESS-I; EXPRESSION;
   BINDING; PROTEIN; INTERACTS; DOMAIN
AB The GC-rich Binding Factor 2/Leucine Rich Repeat in the Flightless 1 Interaction Protein 1 gene (GCF2/LRRFIP1) is predicted to be alternatively spliced in five different isoforms. Although important peptide sequence differences are expected to result from this alternative splicing, to date, only the gene transcription regulator properties of LRRFIP1-Iso5 were unveiled. Based on molecular, cellular and biochemical data, we show here that the five isoforms define two molecular entities with different expression profiles in human tissues, subcellular localizations, oligomerization properties and transcription enhancer properties of the canonical Wnt pathway. We demonstrated that LRRFIP1-Iso3, -4 and -5, which share over 80% sequence identity, are primarily located in the cell cytoplasm and form homo and hetero-multimers between each other. In contrast, LRRFIP1-Isol and -2 are primarily located in the cell nucleus in part thanks to their shared C-terminal domain. Furthermore, we showed that LRRFIP1-Isol is preferentially expressed in the myocardium and skeletal muscle. Using the in vitro Topflash reporter assay we revealed that among LRRFIP1 isoforms, LRRFIP1-Isol is the strongest enhancer of the beta-catenin Wnt canonical transcription pathway thanks to a specific N-terminal domain harboring two critical tryptophan residues (W76, 82). In addition, we showed that the Wnt enhancer properties of LRRFIP1-Isol depend on its homo-dimerisation which is governed by its specific coiled coil domain. Together our study identified LRRFIP1-Isol as a critical regulator of the Wnt canonical pathway with a potential role in myocyte differentiation and myogenesis.
C1 [Labbe, Pauline; Le Scounarnec, Solena; Schott, Jean Jacques; Merot, Jean] Univ Nantes, CNRS, INSERM, Inst Thorax, Nantes, France.
   [Faure, Emilie; Zaffran, Stephane] Aix Marseille Univ, INSERM, GMGF, Marseille, France.
   [Lecointe, Simon; Kyndt, Florence; Marrec, Marie; Le Tourneau, Thierry; Schott, Jean Jacques] CHU Nantes, Nantes, France.
   [Offmann, Bernard] Univ Nantes, UMR CNRS 6286, Nantes, France.
   [Duplaa, Cecile] INSERM, Biol Cardiovasc Dis, U1034, F-33600 Pessac, France.
C3 Centre National de la Recherche Scientifique (CNRS); Institut National
   de la Sante et de la Recherche Medicale (Inserm); Nantes Universite; CHU
   de Nantes; Aix-Marseille Universite; Institut National de la Sante et de
   la Recherche Medicale (Inserm); Nantes Universite; CHU de Nantes; Nantes
   Universite; Institut National de la Sante et de la Recherche Medicale
   (Inserm); Universite de Bordeaux
RP Merot, J (corresponding author), Univ Nantes, CNRS, INSERM, Inst Thorax, Nantes, France.; Merot, J (corresponding author), CNRS 6291, INSERM UMR1087, Inst Thorax, 8 Quai Moncousu, F-44007 Nantes, France.
EM jean.merot@univ-nantes.fr
RI Le Tourneau, Thierry/D-5428-2015; MEROT, Jean/D-5741-2015; OFFMANN,
   Bernard/B-5901-2011; Le Scouarnec, Solena/D-3547-2015; Duplàa,
   cecile/GLU-6264-2022; LECOINTE, Simon/D-3565-2015; Zaffran,
   Stephane/I-2955-2016; KYNDT, Florence/D-6370-2015; Schott,
   jean-Jacques/F-8842-2013
OI MEROT, Jean/0000-0003-1840-8728; Zaffran, Stephane/0000-0002-0811-418X;
   KYNDT, Florence/0000-0001-6651-1696; Schott,
   jean-Jacques/0000-0002-9578-9475; Duplaa, cecile/0000-0001-8003-3969;
   OFFMANN, Bernard/0000-0002-6845-5883
FU Federation Francaise de Cardiologie [R15107NN-RAK15146NNA]; Fondation
   Coeur et Recherche (FCR PVM-Fed, Paris, France); Inserm; AAP
   Interdisciplinaire STIC-Sante de l'Universite de Nantes; Association
   Francaise contre les Myopathies (AFMTelethon)
FX We thank Steven Nedellec and Philippe Hulin and the microscopic facility
   MicroPICell SFR Bonamy in Nantes for their technical expertise and
   assistance cell imaging experiments. This work was funded by the
   Federation Francaise de Cardiologie, Grant R15107NN-RAK15146NNA (TLT,
   JM) and the Fondation Coeur et Recherche (FCR PVM-Fed, Paris, France).
   TLT is supported by Inserm (Inserm Translational Research Program
   2012-2016), the AAP Interdisciplinaire STIC-Sante de l'Universite de
   Nantes "LIU" (BO, JM). E.F. received a postdoctoral fellowship by the
   Association Francaise contre les Myopathies (AFMTelethon). Work in S.Z
   lab is supported by the INSERM and the Association Francaise contre les
   Myopathies (AFM-Telethon; Projet strategique: TRIM-RD).
CR Ariake K, 2012, CANCER LETT, V325, P99, DOI 10.1016/j.canlet.2012.06.012
   Boudreault S, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0161914
   Dyson HJ, 2005, NAT REV MOL CELL BIO, V6, P197, DOI 10.1038/nrm1589
   Fong KSK, 1999, GENOMICS, V58, P146, DOI 10.1006/geno.1999.5817
   Goodall AH, 2010, BLOOD, V116, P4646, DOI 10.1182/blood-2010-04-280925
   Khachigian LM, 1999, CIRC RES, V84, P1258, DOI 10.1161/01.RES.84.11.1258
   Lee YH, 2006, NUCLEIC ACIDS RES, V34, P5052, DOI 10.1093/nar/gkl652
   Lepourcelet M, 2004, CANCER CELL, V5, P91, DOI 10.1016/S1535-6108(03)00334-9
   Liu J, 2005, P NATL ACAD SCI USA, V102, P1927, DOI 10.1073/pnas.0409472102
   Liu Y, 2015, HEPAT MON, V15, DOI 10.5812/hepatmon.15(5)2015.28473
   Nguyen JB, 2013, J STRUCT BIOL, V181, P82, DOI 10.1016/j.jsb.2012.10.006
   Ohtsuka H, 2011, INT J CANCER, V129, P1599, DOI 10.1002/ijc.25837
   Reed AL, 1998, J BIOL CHEM, V273, P21594, DOI 10.1074/jbc.273.34.21594
   Rikiyama T, 2003, BBA-GENE STRUCT EXPR, V1629, P15, DOI 10.1016/S0167-4781(03)00156-8
   Rudolf A, 2016, CELL REP, V15, P1277, DOI 10.1016/j.celrep.2016.04.022
   Ryckebüsch L, 2010, CIRC RES, V106, P686, DOI 10.1161/CIRCRESAHA.109.205732
   Santiveri CM, 2010, BIOPOLYMERS, V94, P779, DOI 10.1002/bip.21436
   Shi LH, 2014, J IMMUNOL, V192, P3057, DOI 10.4049/jimmunol.1302063
   Spitz F, 2012, NAT REV GENET, V13, P613, DOI 10.1038/nrg3207
   Suriano AR, 2005, MOL CELL BIOL, V25, P9073, DOI 10.1128/MCB.25.20.9073-9081.2005
   Wei N, 2015, CELL REP, V13, P1647, DOI 10.1016/j.celrep.2015.10.038
   Wilson SA, 1998, NUCLEIC ACIDS RES, V26, P3460, DOI 10.1093/nar/26.15.3460
   Yang PY, 2010, NAT IMMUNOL, V11, P487, DOI 10.1038/ni.1876
NR 23
TC 14
Z9 17
U1 0
U2 12
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 0167-4889
EI 0006-3002
J9 BBA-MOL CELL RES
JI Biochim. Biophys. Acta-Mol. Cell Res.
PD JUL
PY 2017
VL 1864
IS 7
BP 1142
EP 1152
DI 10.1016/j.bbamcr.2017.03.008
PG 11
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA EW4TW
UT WOS:000402494800002
PM 28322931
DA 2025-04-10
ER

PT J
AU Ramchandani, D
   Unruh, D
   Lewis, CS
   Bogdanov, VY
   Weber, GF
AF Ramchandani, Divya
   Unruh, Dusten
   Lewis, Clayton S.
   Bogdanov, Vladimir Y.
   Weber, Georg F.
TI Activation of carbonic anhydrase IX by alternatively spliced tissue
   factor under late-stage tumor conditions
SO LABORATORY INVESTIGATION
LA English
DT Article
ID HEMOSTATIC SYSTEM; CANCER GROWTH; HYPOXIA; ANGIOGENESIS; EXPRESSION;
   COAGULATION; METASTASIS; CELLS; OSTEOPONTIN; ACIDOSIS
AB Molecules of the coagulation pathway predispose patients to cancer-associated thrombosis and also trigger intracellular signaling pathways that promote cancer progression. The primary transcript of tissue factor, the main physiologic trigger of blood clotting, can undergo alternative splicing yielding a secreted variant, termed asTF (alternatively spliced tissue factor). asTF is not required for normal hemostasis, but its expression levels positively correlate with advanced tumor stages in several cancers, including pancreatic adenocarcinoma. The asTF-overexpressing pancreatic ductal adenocarcinoma cell line Pt45.P1/asTF+ and its parent cell line Pt45.P1 were tested for growth and mobility under normoxic conditions that model early-stage tumors, and in the hypoxic environment of late-stage cancers. asTF overexpression in Pt45.P1 cells conveys increased proliferative ability. According to cell cycle analysis, the major fraction of Pt45.P1/asTF+ cells reside in the dividing G(2)/M phase of the cell cycle, whereas the parental Pt45.P1 cells are mostly confined to the quiescent G(0)/G(1) phase. asTF overexpression is also associated with significantly higher mobility in cells plated under either normoxia or hypoxia. A hypoxic environment leads to upregulation of carbonic anhydrase IX (CAIX), which is more pronounced in Pt45.P1/asTF+ cells. Inhibition of CAIX by the compound U-104 significantly decreases cell growth and mobility of Pt45.P1/asTF+ cells in hypoxia, but not in normoxia. U-104 also reduces the growth of Pt45.P1/asTF + orthotopic tumors in nude mice. CAIX is a novel downstream mediator of asTF in pancreatic cancer, particularly under hypoxic conditions that model late-stage tumor microenvironment.
C1 [Ramchandani, Divya; Weber, Georg F.] Univ Cincinnati, James L Winkle Coll Pharm, 3225 Eden Ave, Cincinnati, OH 45267 USA.
   [Unruh, Dusten; Lewis, Clayton S.; Bogdanov, Vladimir Y.] Univ Cincinnati, Coll Med, Cincinnati, OH 45267 USA.
C3 University System of Ohio; University of Cincinnati; University System
   of Ohio; University of Cincinnati
RP Weber, GF (corresponding author), Univ Cincinnati, James L Winkle Coll Pharm, 3225 Eden Ave, Cincinnati, OH 45267 USA.; Bogdanov, VY (corresponding author), Univ Cincinnati, Coll Med, Cincinnati, OH 45267 USA.
EM vladimir.bogdanov@uc.edu; georg.weber@uc.edu
RI Ramchandani, Divya/ABF-9322-2020
OI Bogdanov, Vladimir/0000-0003-4968-1129; Lewis,
   Clayton/0000-0002-4694-9970; Unruh, Dusten/0000-0003-1027-1982
FU DOD [PR094070]; NIH/NCI [1R21CA16029301-A1, 1R01CA190717-A0]
FX This research was supported in part by DOD grant PR094070 to GFW and
   NIH/NCI grant 1R21CA16029301-A1 and 1R01CA190717-A0 to VYB. The cell
   line Pt45P1 was generously provided by Professor Holger Kalthoff, UKSH,
   Campus Kiel, Germany.
CR Adler B, 1998, EUR J IMMUNOL, V28, P3749, DOI 10.1002/(SICI)1521-4141(199811)28:11<3749::AID-IMMU3749>3.0.CO;2-I
   Bogdanov VY, 2003, NAT MED, V9, P458, DOI 10.1038/nm841
   Carmeliet P, 2000, NATURE, V407, P249, DOI 10.1038/35025220
   Falanga A, 2013, J THROMB HAEMOST, V11, P223, DOI 10.1111/jth.12075
   Falanga Anna, 2003, Clin Adv Hematol Oncol, V1, P673
   Gatenby RA, 2007, BRIT J CANCER, V97, P646, DOI 10.1038/sj.bjc.6603922
   GEY GO, 1952, CANCER RES, V12, P264
   Haas SL, 2006, WORLD J GASTROENTERO, V12, P4843
   Hobbs JE, 2007, THROMB RES, V120, pS13, DOI 10.1016/S0049-3848(07)70126-3
   Keely S, 2009, FASEB J, V23, P1338, DOI 10.1096/fj.08-125344
   Kocatürk B, 2013, P NATL ACAD SCI USA, V110, P11517, DOI 10.1073/pnas.1307100110
   Kuroda Y, 2013, NAT PROTOC, V8, P1391, DOI 10.1038/nprot.2013.076
   Lal I, 2013, BREAST CANCER RES, V15, DOI 10.1186/bcr3425
   Li YJ, 2016, PATHOL ONCOL RES, V22, P277, DOI 10.1007/s12253-015-9935-6
   Lock FE, 2013, ONCOGENE, V32, P5210, DOI 10.1038/onc.2012.550
   Lou YM, 2011, CANCER RES, V71, P3364, DOI 10.1158/0008-5472.CAN-10-4261
   Mayer A, 2013, ADV EXP MED BIOL, V789, P203, DOI 10.1007/978-1-4614-7411-1_28
   Osinsky S, 2009, Exp Oncol, V31, P80
   Palumbo JS, 2008, SEMIN THROMB HEMOST, V34, P154, DOI 10.1055/s-2008-1079255
   Palumbo JS, 2000, BLOOD, V96, P3302, DOI 10.1182/blood.V96.10.3302
   Ratcliffe PJ, 2007, J CLIN INVEST, V117, P862, DOI 10.1172/JCI31750
   Rickles FR, 2001, INT J HEMATOL, V73, P145, DOI 10.1007/BF02981930
   Rosner M, 2013, NAT PROTOC, V8, P602, DOI 10.1038/nprot.2013.011
   Shi ZQ, 2014, CANCER LETT, V344, P47, DOI 10.1016/j.canlet.2013.10.008
   Signaevsky M, 2008, SEMIN THROMB HEMOST, V34, P161, DOI 10.1055/s-2008-1079256
   Sipos B, 2003, VIRCHOWS ARCH, V442, P444, DOI 10.1007/s00428-003-0784-4
   Srinivasan R, 2011, J THROMB HAEMOST, V9, P2087, DOI 10.1111/j.1538-7836.2011.04454.x
   Syed M, 2008, CLIN EXP METASTAS, V25, P787, DOI 10.1007/s10585-008-9192-0
   Unruh D, 2016, ONCOTARGET, V7, P25264, DOI 10.18632/oncotarget.7955
   Unruh D, 2014, INT J CANCER, V134, P9, DOI 10.1002/ijc.28327
   van den Berg YW, 2009, P NATL ACAD SCI USA, V106, P19497, DOI 10.1073/pnas.0905325106
   van Kuijk SJA, 2016, FRONT ONCOL, V6, DOI 10.3389/fonc.2016.00069
   Vaupel P, 2007, CANCER METAST REV, V26, P225, DOI 10.1007/s10555-007-9055-1
   Weber GF, 2014, BIOMED RES INT, V2014, DOI 10.1155/2014/141396
   Wojtukiewicz MZ, 2007, SEMIN THROMB HEMOST, V33, P621, DOI 10.1055/s-2007-991530
   Wojtukiewicz MZ, 2001, NEOPLASIA, V3, P371, DOI 10.1038/sj.neo.7900184
   Wykoff CC, 2000, CANCER RES, V60, P7075
   Zhang GX, 2003, MOL CELL BIOL, V23, P6507, DOI 10.1128/MCB.23.18.6507-6519.2003
NR 38
TC 11
Z9 11
U1 0
U2 6
PU NATURE PUBLISHING GROUP
PI NEW YORK
PA 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA
SN 0023-6837
EI 1530-0307
J9 LAB INVEST
JI Lab. Invest.
PD DEC
PY 2016
VL 96
IS 12
BP 1234
EP 1245
DI 10.1038/labinvest.2016.103
PG 12
WC Medicine, Research & Experimental; Pathology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Research & Experimental Medicine; Pathology
GA EC8ZK
UT WOS:000388431400001
PM 27721473
OA Green Accepted, Bronze
DA 2025-04-10
ER

PT J
AU Soardi, FC
   Penachioni, JY
   Justo, GZ
   Bachega, TASS
   Inácio, M
   Mendonça, BB
   de Castro, M
   de Mello, MP
AF Soardi, Fernanda C.
   Penachioni, Junia Y.
   Justo, Giselle Z.
   Bachega, Tania A. S. S.
   Inacio, Marlene
   Mendonca, Berenice B.
   de Castro, Margaret
   de Mello, Maricilda P.
TI Novel Mutations in CYP11B1 Gene Leading to 11β-Hydroxylase
   Deficiency in Brazilian Patients
SO JOURNAL OF CLINICAL ENDOCRINOLOGY & METABOLISM
LA English
DT Article
ID CONGENITAL ADRENAL-HYPERPLASIA; 21-HYDROXYLASE DEFICIENCY; HYPERTENSION;
   PREDICT; SITES
AB Background: Deficiency of 11 beta-hydroxylase results in the impairment of the last step of cortisol synthesis. In females, the phenotype of this disorder includes different degrees of genital ambiguity and arterial hypertension. Mutations in the CYP11B1 gene are responsible for this disease.
   Objective: The objective of the study was to screen the CYP11B1 gene for mutations in two unrelated Brazilian females with congenital adrenal hyperplasia due to 11 beta-hydroxylase deficiency.
   Design: The coding and intron-exon junction regions of CYP11B1 were totally sequenced. A putative splice mutation was further investigated by minigene transcription.
   Results: We report two novel CYP11B1 mutations in these Brazilian patients. An Arabian Lebanese descendent female was found to be homozygous for a cytosine insertion at the beginning of exon 8, changing the 404 arginine to proline. It alters the open reading frame, creating a putative truncated protein at 421 residue, which eliminates the domain necessary for the association of heme prosthetic group. A severely virilized female was homozygous for the g. 2791G>A transition in the last position of exon 4. This nucleotide is also part of 5' intron 4 donor splice site consensus sequence. Minigene experiments demonstrated that g. 2791G>A activated an alternative splice site within exon 4, leading to a 45-bp deletion in the transcript. The putative translation of such modified mRNA indicates a truncated protein at residue 280.
   Conclusions: We describe two novel mutations, g. 4671_4672insC and g. 2791G>A, that drastically affects normal protein structure. These mutations abolish normal enzyme activity, leading to a severe phenotype of congenital adrenal hyperplasia due to 11 beta-hydroxylase deficiency. (J Clin Endocrinol Metab 94: 3481-3485, 2009)
C1 [Soardi, Fernanda C.; Penachioni, Junia Y.; de Mello, Maricilda P.] Univ Estadual Campinas, Ctr Biol Mol & Engn Genet, BR-13083875 Campinas, SP, Brazil.
   [Justo, Giselle Z.] Univ Fed Sao Paulo, Dept Bioquim, Disciplina Biol Mol, BR-04023900 Sao Paulo, Brazil.
   [Bachega, Tania A. S. S.; Inacio, Marlene; Mendonca, Berenice B.] Univ Sao Paulo, Unidade Endocrinol Desenvolvimento Disciplina End, Lab Invest Med 42, Lab Hormonios & Genet Mol,Hosp Clin,Fac Med, BR-05403900 Sao Paulo, Brazil.
   Univ Sao Paulo, Fac Med Ribeirao Preto, Dept Clin Med, BR-05508090 Ribeirao Preto, Brazil.
C3 Universidade Estadual de Campinas; Universidade Federal de Sao Paulo
   (UNIFESP); Universidade de Sao Paulo; Universidade de Sao Paulo
RP de Mello, MP (corresponding author), Univ Estadual Campinas, Ctr Biol Mol & Engn Genet, Caixa Postal 6010, BR-13083875 Campinas, SP, Brazil.
EM mmello@unicamp.br
RI Soardi, Fernanda/N-9115-2013; Justo, Giselle/E-9424-2012; Bilharinho
   Mendonca, Berenice/J-6917-2015; de Castro, Margaret/A-4918-2009; Palandi
   de Mello, Maricilda/F-3010-2012; Bachega, Tania/C-3361-2013
OI Bilharinho Mendonca, Berenice/0000-0003-1762-1084; de Castro,
   Margaret/0000-0003-4932-4623; Palandi de Mello,
   Maricilda/0000-0003-0521-9100; Bachega, Tania/0000-0002-5219-3153;
   Soardi, Fernanda C/0000-0001-7801-2974
FU Fundacao de Amparo a Pesquisa do Estado de Sao Paulo [97/14076-4,
   05/00981-5, 98/16309-9, 03/01785-0]; Coordenacao de Aperfeic, oamento de
   Pessoal de Nivel Superior and Conselho Nacional de Desenvolvimento
   Cientifico e Tecnologico (Brasil); Fundacao de Amparo a Pesquisa do
   Estado de Sao Paulo (FAPESP) [05/00981-5] Funding Source: FAPESP
FX This work was supported by Grants 97/14076-4 and 05/00981-5 and
   Scholarships 98/16309-9 (to J.Y.P.) and 03/01785-0 (to F. C. S.) from
   Fundacao de Amparo a Pesquisa do Estado de Sao Paulo and grants from
   Coordenacao de Aperfeic, oamento de Pessoal de Nivel Superior and
   Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (Brasil).
CR Buratti E, 2007, NUCLEIC ACIDS RES, V35, P4250, DOI 10.1093/nar/gkm402
   Chabre O, 2000, ENDOCR RES, V26, P797, DOI 10.3109/07435800009048602
   CURNOW KM, 1993, P NATL ACAD SCI USA, V90, P4552, DOI 10.1073/pnas.90.10.4552
   De Carvalho CE, 1999, J ENDOCR GENET, V1, P79
   deAraujo M, 1996, BRAZ J MED BIOL RES, V29, P1
   HAGUE WM, 1983, CLIN ENDOCRINOL, V18, P505, DOI 10.1111/j.1365-2265.1983.tb02880.x
   Krawczak M, 1997, TRENDS GENET, V13, P121, DOI 10.1016/S0168-9525(97)01068-8
   Mermejo LM, 2005, J CLIN ENDOCR METAB, V90, P1287, DOI 10.1210/jc.2004-1552
   MOREIRA AC, 1992, J CLIN ENDOCR METAB, V74, P198, DOI 10.1210/jc.74.1.198
   MORNET E, 1989, J BIOL CHEM, V264, P20961
   MOUNT SM, 1982, NUCLEIC ACIDS RES, V10, P459, DOI 10.1093/nar/10.2.459
   RAVICHANDRAN KG, 1993, SCIENCE, V261, P731, DOI 10.1126/science.8342039
   Roumen L, 2007, J COMPUT AID MOL DES, V21, P455, DOI 10.1007/s10822-007-9128-9
   Skinner CA, 1996, J CLIN ENDOCR METAB, V81, P2389, DOI 10.1210/jc.81.6.2389
   Soardi FC, 2008, ARQ BRAS ENDOCRINOL, V52, P1388, DOI 10.1590/S0004-27302008000800030
   SPOUDEAS HA, 1993, CLIN ENDOCRINOL, V39, P245, DOI 10.1111/j.1365-2265.1993.tb01782.x
   White PC, 2000, ENDOCR REV, V21, P245, DOI 10.1210/er.21.3.245
   WHITE PC, 1994, ENDOCR REV, V15, P421, DOI 10.1210/er.15.4.421
   WHITE PC, 1995, ENDOCR RES, V21, P437, DOI 10.3109/07435809509030459
NR 19
TC 21
Z9 23
U1 0
U2 4
PU ENDOCRINE SOC
PI WASHINGTON
PA 2055 L ST NW, SUITE 600, WASHINGTON, DC 20036 USA
SN 0021-972X
EI 1945-7197
J9 J CLIN ENDOCR METAB
JI J. Clin. Endocrinol. Metab.
PD SEP
PY 2009
VL 94
IS 9
BP 3481
EP 3485
DI 10.1210/jc.2008-2521
PG 5
WC Endocrinology & Metabolism
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism
GA 491NB
UT WOS:000269584600047
PM 19567537
OA Bronze
DA 2025-04-10
ER

PT J
AU Rydén, M
   Faulds, G
   Hoffstedt, J
   Wennlund, A
   Arner, P
AF Rydén, M
   Faulds, G
   Hoffstedt, J
   Wennlund, A
   Arner, P
TI Effect of the (C825T) Gβ3 polymorphism on
   adrenoceptor-mediated lipolysis in human fat cells
SO DIABETES
LA English
DT Article
ID SUBUNIT 825T ALLELE; SPLICE VARIANT; ADIPOSE-TISSUE; OBESITY;
   HYPERTENSION; ASSOCIATION; RESISTANCE
AB A common Gbeta(3) gene polymorphism (C825T) influences G protein receptor-mediated signal transduction. We Investigated whether this polymorphism influences lipolysis in isolated subcutaneous fat cells from 114 healthy obese subjects. The Gbeta(3) protein content was markedly decreased in adipocytes of TT carriers, but the alternatively spliced short form of Gbeta(3) previously shown in platelets of 825T carriers was not detected. Fat cells of TT carriers showed a significant 10-fold decrease in the half-maximum effective concentration of agonists selective for lipolytic beta(1)- and beta(2)-adrenoceptors as well as for the antilipolytic alpha(2)A-adrenoceptor. In TT carriers, maximum beta-adrenoceptor agonist-stimulated lipolysis was decreased, but the maximum antilipolytic effect of alpha(2)-adrenoceptors was less marked. Norepinephrine induced adipocyte lipolysis and circulating fasting levels of free fatty acids and glycerol were reduced by half in TT carriers. The polymorphism did not influence the adipocyte content Of alpha(2)A-adrenoceptors, beta(2)-adrenoceptors, Galpha(i), or Galpha(s). In conclusion, the C825T variant of Go, influences lipolysis. Adipocytes of TT carriers have a lower Gbeta(3) protein content and a decreased function of native G(s)- as well as G(i)-coupled adrenoceptors, which reduces the lipolytic effect of catecholamines. These data differ from those obtained in other cell systems that have shown increased expression of an alternative spliced Gbeta(3) variant and enhanced G protein signaling in 825T carriers, indicating that the polymorphism has cell type-specific effects that may be of importance for type 2 diabetes and other insulin-resistant conditions.
C1 Huddinge Hosp, Ctr Metab & Endocrinol, Clin Res Ctr, S-14186 Huddinge, Sweden.
   Huddinge Univ Hosp, Karolinska Inst, Dept Med, S-14186 Huddinge, Sweden.
C3 Karolinska Institutet
RP Huddinge Hosp, Ctr Metab & Endocrinol, Clin Res Ctr, M63, S-14186 Huddinge, Sweden.
EM peter.arner@medhs.ki.se
OI Arner, Peter/0000-0002-6208-6220
CR ANDERSSON K, 1993, INT J OBESITY, V17, P675
   ARNER P, 1988, EUR J PHARMACOL, V146, P45, DOI 10.1016/0014-2999(88)90485-2
   Baumgart D, 1999, CIRC RES, V85, P965, DOI 10.1161/01.RES.85.10.965
   Benjafield AV, 2001, INT J OBESITY, V25, P777, DOI 10.1038/sj.ijo.0801617
   Carel JC, 1999, J CLIN ENDOCR METAB, V84, P4127, DOI 10.1210/jc.84.11.4127
   Carpéné C, 1998, ANN NY ACAD SCI, V839, P186, DOI 10.1111/j.1749-6632.1998.tb10756.x
   Gautam N, 1998, CELL SIGNAL, V10, P447, DOI 10.1016/S0898-6568(98)00006-0
   Gutersohn A, 2000, LANCET, V355, P1240, DOI 10.1016/S0140-6736(00)02093-6
   HagstromToft E, 1997, DIABETOLOGIA, V40, P1070, DOI 10.1007/s001250050789
   Hegele RA, 1999, GENOME RES, V9, P972, DOI 10.1101/gr.9.10.972
   Hildebrandt JD, 1997, BIOCHEM PHARMACOL, V54, P325, DOI 10.1016/S0006-2952(97)00269-4
   KENAKIN T, 1990, DRUGS, V40, P666, DOI 10.2165/00003495-199040050-00003
   KOLACZYNSKI JW, 1994, INT J OBESITY, V18, P161
   Large V, 1998, DIABETES METAB, V24, P409
   LONNQVIST F, 1993, BRIT J PHARMACOL, V110, P929
   Mauriège P, 2000, J CLIN ENDOCR METAB, V85, P2446, DOI 10.1210/jc.85.7.2446
   Ostrom RS, 2000, J PHARMACOL EXP THER, V294, P407
   REYNISDOTTIR S, 1994, DIABETOLOGIA, V37, P428, DOI 10.1007/s001250050128
   Rosskopf D, 2000, Eur J Med Res, V5, P484
   Siffert W, 2000, NEPHROL DIAL TRANSPL, V15, P1298, DOI 10.1093/ndt/15.9.1298
   Siffert W, 1998, KIDNEY INT, V53, P1466, DOI 10.1046/j.1523-1755.1998.00934.x
   Siffert W, 1999, J AM SOC NEPHROL, V10, P1921
   Siffert W, 1998, NAT GENET, V18, P45, DOI 10.1038/ng0198-45
   Virchow S, 1999, N-S ARCH PHARMACOL, V360, P27, DOI 10.1007/s002109900040
NR 24
TC 58
Z9 63
U1 0
U2 2
PU AMER DIABETES ASSOC
PI ALEXANDRIA
PA 1701 N BEAUREGARD ST, ALEXANDRIA, VA 22311-1717 USA
SN 0012-1797
EI 1939-327X
J9 DIABETES
JI Diabetes
PD MAY
PY 2002
VL 51
IS 5
BP 1601
EP 1608
DI 10.2337/diabetes.51.5.1601
PG 8
WC Endocrinology & Metabolism
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism
GA 550FF
UT WOS:000175492400038
PM 11978662
OA Bronze
DA 2025-04-10
ER

PT J
AU Sobue, K
   Hayashi, K
   Nishida, W
AF Sobue, K
   Hayashi, K
   Nishida, W
TI Expressional regulation of smooth muscle cell-specific genes in
   association with phenotypic modulation
SO MOLECULAR AND CELLULAR BIOCHEMISTRY
LA English
DT Review
DE smooth muscle cell; smooth muscle cell-specific markers; phenotypic
   modulation; transcription; splicing
ID MYOSIN HEAVY-CHAIN; ALPHA-ACTIN GENE; CHICKEN-EMBRYO FIBROBLASTS;
   TISSUE-SPECIFIC EXPRESSION; EXCLUSIVE EXON SELECTION; DNA-BINDING
   PROTEINS; AMINO-ACID SEQUENCE; LIGHT CHAIN; INTEGRIN GENE; SINGLE GENE
AB Phenotypic modulation of smooth muscle cells (SMCs) plays an integral role in atherosclerosis, hypertension and leiomyogenic tumorigenicity. The morphological, functional, and biochemical characteristics of SMCs in different phenotypes such as differentiated and dedifferentiated states have been well studied. Recent researches have focused on the expressional regulation of SMC-specific marker genes in association with phenotypic modulation of SMCs. The SMC-specific marker gems are regulated at the levels of transcription and splicing. The caldesmon, smooth muscle myosin heavy chain, alpha-smooth muscle actin, calponin, SM22, alpha- and beta-tropomyosins, and alpha 1 integrin genes are transcriptionally regulated; transcription of these genes except for the alpha-smooth muscle actin gene is upregulated in differentiated SMCs, but is downregulated in dedifferentiated SMCs. The expression pattern of alpha-smooth muscle actin is opposite in vascular and visceral SMCs. In almost all promoter regions of these genes, the CArG box and serum response factor (SRF) are involved in as the positive cis-element and the trans-acting factor, respectively. Isoform changes of caldesmon, alpha-tropomyosin, vinculin/metavinculin, and smooth muscle myosin heavy chain are regulated by alternative splicing in a SMC phenotype-dependent manner. Among them, isoform interconversions of caldesmon and alpha-tropomyosin are completely coordinated with phenotype of SMCs. The purpose of this paper is to summarize current knowledge of the expressional regulation of SMC-specific marker genes in different phenotypes of SMCs. (Mol Cell Biochem 190: 105-118, 1999).
C1 Osaka Univ, Sch Med, Biomed Res Ctr, Dept Neurochem & Neuropharmacol, Suita, Osaka 565, Japan.
C3 The University of Osaka
RP Sobue, K (corresponding author), Osaka Univ, Sch Med, Biomed Res Ctr, Dept Neurochem & Neuropharmacol, 2-2 Yamadaoka, Suita, Osaka 565, Japan.
CR ALMENDRAL JM, 1988, MOL CELL BIOL, V8, P2140, DOI 10.1128/MCB.8.5.2140
   APPLEGATE D, 1994, J BIOL CHEM, V269, P10683
   AUDET JF, 1994, DNA CELL BIOL, V13, P1071, DOI 10.1089/dna.1994.13.1071
   AZPIAZU N, 1993, GENE DEV, V7, P1325, DOI 10.1101/gad.7.7b.1325
   BELKIN AM, 1988, J BIOL CHEM, V263, P6631
   BELKIN VM, 1990, J CELL BIOL, V111, P2159, DOI 10.1083/jcb.111.5.2159
   BLANK RS, 1992, J BIOL CHEM, V267, P984
   BODMER R, 1993, DEVELOPMENT, V118, P719
   BURRIDGE K, 1988, ANNU REV CELL BIOL, V4, P487, DOI 10.1146/annurev.cellbio.4.1.487
   BUSHEL P, 1995, ONCOGENE, V10, P1361
   CAMPBELL JH, 1989, ARTERIOSCLEROSIS, V9, P633, DOI 10.1161/01.ATV.9.5.633
   CAREY DJ, 1991, ANNU REV PHYSIOL, V53, P161, DOI 10.1146/annurev.ph.53.030191.001113
   CHAMLEYCAMPBELL J, 1979, PHYSIOL REV, V59, P1, DOI 10.1152/physrev.1979.59.1.1
   CHOU RGR, 1992, DEV BIOL, V149, P339, DOI 10.1016/0012-1606(92)90289-S
   COGAN JG, 1995, J BIOL CHEM, V270, P11310, DOI 10.1074/jbc.270.19.11310
   Croissant JD, 1996, DEV BIOL, V177, P250, DOI 10.1006/dbio.1996.0160
   DEMEIRSMAN C, 1994, DNA CELL BIOL, V13, P743, DOI 10.1089/dna.1994.13.743
   DRAEGER A, 1989, J CELL SCI, V94, P703
   DUBAND JL, 1992, DEVELOPMENT, V116, P585
   EBASHI S, 1980, PROC R SOC SER B-BIO, V207, P259, DOI 10.1098/rspb.1980.0024
   FATIGATI V, 1984, J BIOL CHEM, V259, P4383
   GALLAGHER PJ, 1991, J BIOL CHEM, V266, P23945
   GEIGER B, 1981, J CELL BIOL, V91, P614, DOI 10.1083/jcb.91.3.614
   GLUKHOVA M, 1993, DEV BIOL, V157, P437, DOI 10.1006/dbio.1993.1147
   GLUKHOVA MA, 1990, J BIOL CHEM, V265, P13042
   GLUKHOVA MA, 1988, P NATL ACAD SCI USA, V85, P9542, DOI 10.1073/pnas.85.24.9542
   GMENEBERG DA, 1992, SCIENCE, V257, P1089
   GOODING C, 1994, EMBO J, V13, P3861, DOI 10.1002/j.1460-2075.1994.tb06697.x
   HARUNA M, 1993, BIOCHEM BIOPH RES CO, V197, P145, DOI 10.1006/bbrc.1993.2453
   HASEGAWA Y, 1992, J BIOCHEM-TOKYO, V111, P804, DOI 10.1093/oxfordjournals.jbchem.a123840
   HATHAWAY DR, 1991, CIRCULATION, V83, P382, DOI 10.1161/01.CIR.83.2.382
   HAYASHI K, 1992, P NATL ACAD SCI USA, V89, P12122, DOI 10.1073/pnas.89.24.12122
   HAYASHI K, 1998, IN PRESS J BIOL CHEM
   HEDIN U, 1988, J CELL BIOL, V107, P307, DOI 10.1083/jcb.107.1.307
   HELFMAN DM, 1986, MOL CELL BIOL, V6, P3582, DOI 10.1128/MCB.6.11.3582
   HELPER DJ, 1988, J BIOL CHEM, V263, P15748
   HEMLER ME, 1990, ANNU REV IMMUNOL, V8, P365, DOI 10.1146/annurev.iy.08.040190.002053
   HENDRICKS M, 1984, MOL CELL BIOL, V4, P1823, DOI 10.1128/MCB.4.9.1823
   HILL CS, 1995, CELL, V81, P1159, DOI 10.1016/S0092-8674(05)80020-0
   HUBER PAJ, 1995, BIOCHEM J, V312, P617, DOI 10.1042/bj3120617
   HUMPHREY MB, 1995, MOL CELL BIOL, V15, P3979
   HYNES RO, 1992, CELL, V69, P11, DOI 10.1016/0092-8674(92)90115-S
   IGNATIUS MJ, 1988, NEURON, V1, P713, DOI 10.1016/0896-6273(88)90170-5
   IIVANAINEN A, 1995, MATRIX BIOL, V14, P489, DOI 10.1016/0945-053X(95)90006-3
   ISHIKAWA R, 1989, J BIOL CHEM, V264, P7490
   ITO M, 1989, J BIOL CHEM, V264, P13971
   JOHNSON RJ, 1991, J CLIN INVEST, V87, P847, DOI 10.1172/JCI115089
   Kallmeier RC, 1995, J BIOL CHEM, V270, P30949, DOI 10.1074/jbc.270.52.30949
   KASHIWADA K, 1997, J BIOL CHEM
   KAWAMOTO S, 1991, J CELL BIOL, V112, P915, DOI 10.1083/jcb.112.5.915
   KELLEY CA, 1990, J BIOL CHEM, V265, P17876
   KELLEY CA, 1993, J BIOL CHEM, V268, P12848
   Kelm RJ, 1996, J BIOL CHEM, V271, P24278, DOI 10.1074/jbc.271.39.24278
   KIEHART DP, 1990, CELL, V60, P347, DOI 10.1016/0092-8674(90)90583-Z
   Kimura K, 1998, NUCLEIC ACIDS RES, V26, P2420, DOI 10.1093/nar/26.10.2420
   KIRK TZ, 1995, J BIOL CHEM, V270, P3423, DOI 10.1074/jbc.270.7.3423
   KORHONEN M, 1990, J CELL BIOL, V111, P1245, DOI 10.1083/jcb.111.3.1245
   KRAMER RH, 1989, J BIOL CHEM, V264, P4684
   KUROO M, 1991, J BIOL CHEM, V266, P3768
   KUROO M, 1989, J BIOL CHEM, V264, P18272
   LAZARD D, 1993, P NATL ACAD SCI USA, V90, P999, DOI 10.1073/pnas.90.3.999
   LEESMILLER JP, 1987, J BIOL CHEM, V262, P2988
   LEESMILLER JP, 1987, BIOCHEM J, V244, P705, DOI 10.1042/bj2440705
   LEESMILLER JP, 1991, BIOESSAYS, V13, P429, DOI 10.1002/bies.950130902
   LEMONNIER M, 1991, GENE, V107, P229, DOI 10.1016/0378-1119(91)90323-4
   LENZ S, 1989, J BIOL CHEM, V264, P9009
   Li L, 1996, CIRC RES, V78, P188, DOI 10.1161/01.RES.78.2.188
   Li L, 1996, J CELL BIOL, V132, P849, DOI 10.1083/jcb.132.5.849
   LIBRI D, 1989, J BIOL CHEM, V264, P2935
   LILLY B, 1995, SCIENCE, V267, P688, DOI 10.1126/science.7839146
   LIN JJC, 1985, J CELL BIOL, V100, P692, DOI 10.1083/jcb.100.3.692
   LOPEZCABRERA M, 1993, J BIOL CHEM, V268, P1187
   Mabuchi K, 1996, J MUSCLE RES CELL M, V17, P243, DOI 10.1007/BF00124246
   MAGUCHI M, 1995, BIOCHEM BIOPH RES CO, V217, P238, DOI 10.1006/bbrc.1995.2769
   MALMQVIST U, 1991, PFLUG ARCH EUR J PHY, V418, P523, DOI 10.1007/BF00370566
   MANO JM, 1996, J BIOL CHEM, V271, P7095
   MECHTERSHEIMER G, 1994, AM J PATHOL, V144, P1172
   Moessler H, 1996, DEVELOPMENT, V122, P2415
   MOISEYEVA EP, 1993, J BIOL CHEM, V268, P4318
   Momiyama T, 1998, BIOCHEM BIOPH RES CO, V242, P429, DOI 10.1006/bbrc.1997.7959
   MULLEN MP, 1991, GENE DEV, V5, P642, DOI 10.1101/gad.5.4.642
   NABESHIMA Y, 1987, J BIOL CHEM, V262, P10608
   NAGAI R, 1989, J BIOL CHEM, V264, P9734
   NODEN DM, 1989, AM REV RESPIR DIS, V140, P1097, DOI 10.1164/ajrccm/140.4.1097
   NUEDA A, 1993, J BIOL CHEM, V268, P19305
   OBATA H, 1997, J BIOL CHEM, V272, P26648
   OLSON NJ, 1990, P NATL ACAD SCI USA, V87, P2284, DOI 10.1073/pnas.87.6.2284
   OWENS GK, 1986, J BIOL CHEM, V261, P3373
   PATEL CV, 1992, J BIOL CHEM, V267, P26085
   PEARLSTONE JR, 1987, J BIOL CHEM, V262, P5985
   POOLE TJ, 1989, J EXP ZOOL, V251, P224, DOI 10.1002/jez.1402510210
   RISAU W, 1988, DEV BIOL, V125, P441, DOI 10.1016/0012-1606(88)90225-4
   ROLLINS RJ, 1989, ADV CANCER RES, P611
   ROSEN GD, 1994, J BIOL CHEM, V269, P15652
   ROSEN GD, 1991, P NATL ACAD SCI USA, V88, P4094, DOI 10.1073/pnas.88.10.4094
   ROSS R, 1993, NATURE, V362, P801, DOI 10.1038/362801a0
   SAGA H, 1998, IN PRESS EXP CELL RE
   Samaha FF, 1996, J BIOL CHEM, V271, P395, DOI 10.1074/jbc.271.1.395
   SARTORE S, 1994, J VASC RES, V31, P61, DOI 10.1159/000159033
   SELLERS JR, 1985, CURR TOP CELL REGUL, V27, P51
   SHANAHAN CM, 1993, CIRC RES, V73, P193, DOI 10.1161/01.RES.73.1.193
   SHIMIZU RT, 1995, J BIOL CHEM, V270, P7631, DOI 10.1074/jbc.270.13.7631
   SIFICIANO JD, 1987, J CELL BIOL, V104, P473
   SIMONS M, 1991, CIRC RES, V69, P530, DOI 10.1161/01.RES.69.2.530
   SKALLI O, 1986, J CELL BIOL, V103, P2787, DOI 10.1083/jcb.103.6.2787
   SKINNER MP, 1994, AM J PATHOL, V145, P1070
   SOBUE K, 1991, J BIOL CHEM, V266, P12115
   SOBUE K, 1985, P NATL ACAD SCI USA, V82, P5025, DOI 10.1073/pnas.82.15.5025
   SOMLYO AP, 1993, J MUSCLE RES CELL M, V14, P557, DOI 10.1007/BF00141552
   STRASSER P, 1993, FEBS LETT, V330, P13, DOI 10.1016/0014-5793(93)80909-E
   SUN SQ, 1995, MOL CELL BIOL, V15, P2429
   SWYNGHEDAUW B, 1986, PHYSIOL REV, V66, P710, DOI 10.1152/physrev.1986.66.3.710
   TAKAHASHI K, 1991, J BIOL CHEM, V266, P13284
   TOUTANT M, 1994, NUCLEIC ACIDS RES, V22, P1838, DOI 10.1093/nar/22.10.1838
   TREISMAN R, 1985, CELL, V42, P889, DOI 10.1016/0092-8674(85)90285-5
   Treisman R, 1990, Semin Cancer Biol, V1, P47
   UEKI N, 1987, P NATL ACAD SCI USA, V84, P9049, DOI 10.1073/pnas.84.24.9049
   UMEMOTO S, 1990, J BIOL CHEM, V265, P14864
   VANDEKERCKHOVE J, 1978, J MOL BIOL, V126, P783, DOI 10.1016/0022-2836(78)90020-7
   Watanabe M, 1996, CIRC RES, V78, P978, DOI 10.1161/01.RES.78.6.978
   WHITE S, 1993, MNRAS, V261, P8, DOI [DOI 10.1093/MNRAS/261.1.L8, 10.1093/mnras/stx1882, DOI 10.1093/MNRAS/STY817]
   White SL, 1996, J BIOL CHEM, V271, P15008, DOI 10.1074/jbc.271.25.15008
   WIECZOREK DF, 1988, MOL CELL BIOL, V8, P679, DOI 10.1128/MCB.8.2.679
   Winder SJ, 1996, CURR TOP CELL REGUL, V34, P33, DOI 10.1016/S0070-2137(96)80002-1
   YAMASHIROMATSUMURA S, 1988, J CELL BIOL, V106, P1973, DOI 10.1083/jcb.106.6.1973
   YANO H, 1995, J BIOL CHEM, V270, P23661, DOI 10.1074/jbc.270.40.23661
   YANO H, 1994, BIOCHEM BIOPH RES CO, V201, P618, DOI 10.1006/bbrc.1994.1746
   YU YT, 1992, GENE DEV, V6, P1783, DOI 10.1101/gad.6.9.1783
   ZAMORE PD, 1992, NATURE, V355, P609, DOI 10.1038/355609a0
   ZUTTER MM, 1994, J BIOL CHEM, V269, P463
NR 130
TC 199
Z9 255
U1 1
U2 19
PU KLUWER ACADEMIC PUBL
PI DORDRECHT
PA SPUIBOULEVARD 50, PO BOX 17, 3300 AA DORDRECHT, NETHERLANDS
SN 0300-8177
J9 MOL CELL BIOCHEM
JI Mol. Cell. Biochem.
PD JAN
PY 1999
VL 190
IS 1-2
BP 105
EP 118
DI 10.1023/A:1006941621170
PG 14
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA 172TZ
UT WOS:000078942000015
PM 10098977
DA 2025-04-10
ER

PT J
AU Jebbink, J
   Keijser, R
   Veenboer, G
   van der Post, J
   Ris-Stalpers, C
   Afink, G
AF Jebbink, Jiska
   Keijser, Remco
   Veenboer, Geertruda
   van der Post, Joris
   Ris-Stalpers, Carrie
   Afink, Gijs
TI Expression of Placental FLT1 Transcript Variants Relates to Both
   Gestational Hypertensive Disease and Fetal Growth
SO HYPERTENSION
LA English
DT Article
DE endothelial growth factors; gene expression; human; preeclampsia;
   pregnancy
ID FACTOR RECEPTOR-1 CONCENTRATION; CIRCULATING ANGIOGENIC FACTORS;
   TYROSINE KINASE 1; NORMOTENSIVE PREGNANCIES; PREECLAMPSIA; RESTRICTION;
   HYPOXIA; PLASMA; TROPHOBLAST; DIAGNOSIS
AB The recent discovery of additional alternative spliced FLT1 transcripts encoding novel soluble (s)FLT1 protein isoforms complicates both the predictive value and functional implications of sFLT1 in preeclampsia. We investigated FLT1 expression levels and splicing patterns in placentas of normotensive and preeclamptic women, and established the tissue specificity of all FLT1 transcript variants. mRNA levels of sFLT1 splice variants were determined by real-time polymerase chain reaction in 21 normal human tissues and placental biopsies from 91 normotensive and 55 preeclamptic women. Cellular localization of placental FLT1 expression was established by RNA in situ hybridization. Of all tissues investigated, placenta has by far the highest FLT1 mRNA expression level, mainly localized in the syncytiotrophoblast layer. More than 80% of placental transcripts correspond to sFLT1_v2. Compared with normotensive placenta, preeclamptic placenta has approximate to 3-fold higher expression of all FLT1 transcript variants (P<0.001), with a slight shift in favor of sFLT1_v1. Although to a lesser degree, transcript levels are also increased in placenta from normotensive women that deliver a small for gestational age neonate. We conclude that sFLT isoform-specific assays could potentially improve the accuracy of current sFLT1 assays for the prediction of preeclampsia. However, placental FLT1 transcript levels are increased not only in preeclampsia but also in normotensive pregnancy with a small for gestational age fetus. This may indicate a common pathway involved in the development of both conditions but complicates the use of circulating sFLT1 protein levels for the prediction or diagnosis of preeclampsia alone. (Hypertension. 2011;58:70-76.) . Online Data Supplement
C1 [Jebbink, Jiska; Keijser, Remco; Veenboer, Geertruda; Ris-Stalpers, Carrie; Afink, Gijs] Univ Amsterdam, Acad Med Ctr, Reprod Biol Lab, NL-1100 DD Amsterdam, Netherlands.
   [Jebbink, Jiska; van der Post, Joris; Ris-Stalpers, Carrie] Univ Amsterdam, Acad Med Ctr, Dept Obstet & Gynecol, NL-1100 DD Amsterdam, Netherlands.
C3 University of Amsterdam; Academic Medical Center Amsterdam; University
   of Amsterdam; Academic Medical Center Amsterdam
RP Afink, G (corresponding author), Univ Amsterdam, Acad Med Ctr, Reprod Biol Lab, POB 22660, NL-1100 DD Amsterdam, Netherlands.
EM g.b.afink@amc.uva.nl
RI van der Post, Joris/A-8991-2008; Afink, Gijs/AAB-2832-2021; Afink,
   Gijs/A-2025-2009
OI van der Post, Joris/0000-0003-3311-2116; Afink, Gijs/0000-0002-2155-725X
FU Academic Medical Center
FX This work was supported by intramural research funding from the Academic
   Medical Center.
CR Afink GB, 2010, THYROID, V20, P811, DOI 10.1089/thy.2009.0366
   Buimer M, 2008, PLACENTA, V29, P444, DOI 10.1016/j.placenta.2008.02.007
   Carmeliet P, 2001, NAT MED, V7, P575, DOI 10.1038/87904
   Chaiworapongsa T, 2005, J MATERN-FETAL NEO M, V17, P3, DOI 10.1080/14767050400028816
   Chaiworapongsa T, 2008, J MATERN-FETAL NEO M, V21, P25, DOI 10.1080/14767050701832833
   Crispi F, 2006, AM J OBSTET GYNECOL, V195, P201, DOI 10.1016/j.ajog.2006.01.014
   Ferrara N, 2003, NAT MED, V9, P669, DOI 10.1038/nm0603-669
   Heydarian M, 2009, PLACENTA, V30, P250, DOI 10.1016/j.placenta.2008.12.010
   Hirashima M, 2003, P NATL ACAD SCI USA, V100, P15637, DOI 10.1073/pnas.2635424100
   Huppertz B, 2008, HYPERTENSION, V51, P970, DOI 10.1161/HYPERTENSIONAHA.107.107607
   KENDALL RL, 1993, P NATL ACAD SCI USA, V90, P10705, DOI 10.1073/pnas.90.22.10705
   Koga K, 2003, J CLIN ENDOCR METAB, V88, P2348, DOI 10.1210/jc.2002-021942
   Lapaire O, 2010, EUR J OBSTET GYN R B, V151, P122, DOI 10.1016/j.ejogrb.2010.04.009
   Levine RJ, 2004, NEW ENGL J MED, V350, P672, DOI 10.1056/NEJMoa031884
   Maynard SE, 2003, J CLIN INVEST, V111, P649, DOI 10.1172/JCI200317189
   Munaut C, 2008, HUM REPROD, V23, P1407, DOI 10.1093/humrep/den114
   Nevo O, 2008, J CLIN ENDOCR METAB, V93, P285, DOI 10.1210/jc.2007-1042
   Nevo O, 2006, AM J PHYSIOL-REG I, V291, pR1085, DOI 10.1152/ajpregu.00794.2005
   Rajakumar A, 2004, PLACENTA, V25, P763, DOI 10.1016/j.placenta.2004.02.011
   Rajakumar A, 2009, PLACENTA, V30, P25, DOI 10.1016/j.placenta.2008.10.006
   Rajakumar A, 2007, AM J PHYSIOL-REG I, V293, pR766, DOI 10.1152/ajpregu.00097.2007
   Roberts JM, 2009, PLACENTA, V30, pS32, DOI 10.1016/j.placenta.2008.11.009
   Roberts JM, 2003, HYPERTENSION, V41, P437, DOI 10.1161/01.HYP.0000054981.03589.E9
   Sela S, 2008, CIRC RES, V102, P1566, DOI 10.1161/CIRCRESAHA.108.171504
   Shibata E, 2005, J CLIN ENDOCR METAB, V90, P4895, DOI 10.1210/jc.2004-1955
   Sibai BM, 2004, OBSTET GYNECOL, V103, P981, DOI 10.1097/01.AOG.0000126245.35811.2a
   Smith GCS, 2007, OBSTET GYNECOL, V109, P1316, DOI 10.1097/01.AOG.0000265804.09161.0d
   Srinivas SK, 2010, J MATERN-FETAL NEO M, V23, P1294, DOI 10.3109/14767051003677988
   Tammela T, 2005, CARDIOVASC RES, V65, P550, DOI 10.1016/j.cardiores.2004.12.002
   Thomas CP, 2010, NUCLEIC ACIDS RES, V38, P5130, DOI 10.1093/nar/gkq198
   Thomas CP, 2009, J CLIN ENDOCR METAB, V94, P2524, DOI 10.1210/jc.2009-0017
   Tsatsaris V, 2003, J CLIN ENDOCR METAB, V88, P5555, DOI 10.1210/jc.2003-030528
   Wallner W, 2007, CLIN SCI, V112, P51, DOI 10.1042/CS20060161
NR 33
TC 68
Z9 78
U1 0
U2 10
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA 530 WALNUT ST, PHILADELPHIA, PA 19106-3621 USA
SN 0194-911X
J9 HYPERTENSION
JI Hypertension
PD JUL
PY 2011
VL 58
IS 1
BP 70
EP U129
DI 10.1161/HYPERTENSIONAHA.110.164079
PG 17
WC Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology
GA 777WE
UT WOS:000291655000013
PM 21518965
OA Bronze
DA 2025-04-10
ER

PT J
AU Feng, JN
   Yan, J
   Buzin, CH
   Towbin, JA
   Sommer, SS
AF Feng, JN
   Yan, J
   Buzin, CH
   Towbin, JA
   Sommer, SS
TI Mutations in the dystrophin gene are associated with sporadic dilated
   cardiomyopathy
SO MOLECULAR GENETICS AND METABOLISM
LA English
DT Article
DE dilated cardiomyopathy; dystrophin gene; mutation detection; DOVAM-S
ID DUCHENNE MUSCULAR-DYSTROPHY; CYSTIC-FIBROSIS GENE; ATM MUTATIONS;
   MISSENSE MUTATIONS; DOVAM-S; EXPRESSION; MOSAICISM; DISEASE; ELEMENT;
   FAMILY
AB Dilated cardiomyopathy (DCM) is the major indication for heart transplantation. Approximately 30% of all DCM is thought to be inherited, while 70% is sporadic. Mutations in the dystrophin gene have been associated with the uncommon X-linked form of DCM. We hypothesized that missense mutations and other less severe mutations of the dystrophin gene might predispose to the common form of sporadic DCM. To test this hypothesis, 22 kb of genomic dystrophin DNA was scanned with DOVAM-S in each of the 22 patients with sporadic DCM, including all 79 coding sequences and splice junctions, as well as six alternative exon I dystrophin isoforms (484 kb, total). Three putative new mutations (IVS5 + 1 G > T, K18N, and F3228L) and seven polymorphisms were identified. The splice site mutation IVS5 + I is predicted to cause skipping of exon 5, which is within a region containing an actin binding site. The missense mutations occur at amino acids that display substantial evolutionary conservation. Screening of 236 control individuals failed to identify these three mutations. The three patients with putative mutations had CK-MM (creatine kinase, skeletal muscle) levels greater than 250 units while the 14 patients without mutations for which CK-MM were available had values ranging from 20 to 200. The first comprehensive mutation scanning of the exons and splice junctions of the dystrophin gene in patients with sporadic DCM presents the evidence that point mutations are associated with sporadic DCM without clinical evidence of skeletal myopathy. It may be prudent to measure CK-MM in all patients with dilated cardiomyopathy to identify candidates at high risk for dystrophin mutations. (C) 2002 Elsevier Science (USA). All rights reserved.
C1 City Hope Natl Med Ctr, Beckman Res Inst, Dept Mol Genet, Duarte, CA 91010 USA.
   Baylor Coll Med, Dept Pediat Cardiol & Mol & Human Genet, Houston, TX 77030 USA.
C3 City of Hope; Beckman Research Institute of City of Hope; Baylor College
   of Medicine
RP City Hope Natl Med Ctr, Beckman Res Inst, Dept Mol Genet, Duarte, CA 91010 USA.
EM sommerlab@coh.org
RI Towbin, Jeffrey/J-5595-2019
FU NHLBI NIH HHS [R01HL62570] Funding Source: Medline
CR Arbustini E, 2000, J AM COLL CARDIOL, V35, P1760, DOI 10.1016/S0735-1097(00)00650-1
   Badorff C, 2000, J BIOL CHEM, V275, P11191, DOI 10.1074/jbc.275.15.11191
   BEGGS AH, 1991, AM J HUM GENET, V49, P54
   BOTTEMA CDK, 1991, AM J HUM GENET, V49, P820
   Bowles NE, 2000, HERZ, V25, P168, DOI 10.1007/s000590050003
   Bullrich F, 1999, CANCER RES, V59, P24
   Buzin CH, 2000, BIOTECHNIQUES, V28, P746, DOI 10.2144/00284rr04
   Claustres M, 2000, HUM MUTAT, V16, P143, DOI 10.1002/1098-1004(200008)16:2<143::AID-HUMU7>3.0.CO;2-J
   Cohn JA, 1998, NEW ENGL J MED, V339, P653, DOI 10.1056/NEJM199809033391002
   Ferlini A, 1998, AM J HUM GENET, V63, P436, DOI 10.1086/301952
   GOLD R, 1992, MUSCLE NERVE, V15, P214, DOI 10.1002/mus.880150214
   GREEN MHL, 1995, MUTAT RES-ENVIR MUTA, V334, P323, DOI 10.1016/0165-1161(95)90070-5
   HUNSAKER RH, 1982, AM J MED, V73, P235, DOI 10.1016/0002-9343(82)90184-X
   Ketterling RP, 1999, HUM GENET, V105, P629, DOI 10.1007/s004390051155
   Krawczak M, 1996, HUM MUTAT, V8, P23
   Liu Q, 1999, BIOTECHNIQUES, V26, P932, DOI 10.2144/99265rr03
   Mendell JR, 2001, NEUROLOGY, V57, P645, DOI 10.1212/WNL.57.4.645
   Milasin J, 1996, HUM MOL GENET, V5, P73, DOI 10.1093/hmg/5.1.73
   MUNTONI F, 1995, AM J HUM GENET, V56, P151
   MUNTONI F, 1995, J CLIN INVEST, V96, P693, DOI 10.1172/JCI118112
   Muntoni F, 1997, HEART, V78, P608, DOI 10.1136/hrt.78.6.608
   MUNTONI F, 1993, NEW ENGL J MED, V329, P921, DOI 10.1056/NEJM199309233291304
   OrtizLopez R, 1997, CIRCULATION, V95, P2434, DOI 10.1161/01.CIR.95.10.2434
   PERLOFF JK, 1966, CIRCULATION, V33, P625, DOI 10.1161/01.CIR.33.4.625
   Schaffner C, 1999, BLOOD, V94, P748, DOI 10.1182/blood.V94.2.748.414k02_748_753
   Sharer N, 1998, NEW ENGL J MED, V339, P645, DOI 10.1056/NEJM199809033391001
   SOUSSI T, 1990, ONCOGENE, V5, P945
   Stankovic T, 1998, AM J HUM GENET, V62, P334, DOI 10.1086/301706
   TAYLOR SAM, 1991, P NATL ACAD SCI USA, V88, P39, DOI 10.1073/pnas.88.1.39
   TOWBIN JA, 1993, CIRCULATION, V87, P1854, DOI 10.1161/01.CIR.87.6.1854
   Vorechovsky I, 1997, NAT GENET, V17, P96, DOI 10.1038/ng0997-96
   Weinshenker Brian G., 2001, Mutation Research, V458, P7, DOI 10.1016/S1383-5726(00)00008-X
   WINDER SJ, 1995, FEBS LETT, V369, P27, DOI 10.1016/0014-5793(95)00398-S
   Yoshida K, 1998, HUM MOL GENET, V7, P1129, DOI 10.1093/hmg/7.7.1129
NR 34
TC 57
Z9 67
U1 0
U2 6
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 1096-7192
EI 1096-7206
J9 MOL GENET METAB
JI Mol. Genet. Metab.
PD SEP-OCT
PY 2002
VL 77
IS 1-2
BP 119
EP 126
AR PII S1096-7192(02)00153-1
DI 10.1016/S1096-7192(02)00153-1
PG 8
WC Endocrinology & Metabolism; Genetics & Heredity; Medicine, Research &
   Experimental
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism; Genetics & Heredity; Research & Experimental
   Medicine
GA 612KQ
UT WOS:000179074500017
PM 12359139
DA 2025-04-10
ER

PT J
AU Hirose, Y
   Chiba, K
   Karasugi, T
   Nakajima, M
   Kawaguchi, Y
   Mikami, Y
   Furuichi, T
   Mio, F
   Miyake, A
   Miyamoto, T
   Ozaki, K
   Takahashi, A
   Mizuta, H
   Kubo, T
   Kimura, T
   Tanaka, T
   Toyama, Y
   Ikegawa, S
AF Hirose, Yuichiro
   Chiba, Kazuhiro
   Karasugi, Tatsuki
   Nakajima, Masahiro
   Kawaguchi, Yoshiharu
   Mikami, Yasuo
   Furuichi, Tatsuya
   Mio, Futoshi
   Miyake, Atsushi
   Miyamoto, Takeshi
   Ozaki, Kouichi
   Takahashi, Atsushi
   Mizuta, Hiroshi
   Kubo, Toshikazu
   Kimura, Tomoatsu
   Tanaka, Toshihiro
   Toyama, Yoshiaki
   Ikegawa, Shiro
TI A functional polymorphism in THBS2 that affects alternative splicing and
   MMP binding is associated with lumbar-disc herniation
SO AMERICAN JOURNAL OF HUMAN GENETICS
LA English
DT Article
ID MAXIMUM-LIKELIHOOD-ESTIMATION; CHONDROSARCOMA CELL-LINE; GENOME-WIDE
   ASSOCIATION; GROWTH-FACTOR-BETA; MATRIX METALLOPROTEINASE-2; POPULATION
   STRATIFICATION; MATRICELLULAR PROTEINS; INTERVERTEBRAL DISC; ADHESIVE
   DEFECT; IV COLLAGENASE
AB Lumbar-disc herniation (LDH), one of the most common musculoskeletal diseases, has strong genetic determinants. Recently, several genes that encode extracellular matrix (ECM) proteins in the intervertebral disc have been reported to associate with LDH. Thrombospondins (THBSs) I and 2 are good candidates for the LDH susceptibility gene: They are intervertebral disc ECM proteins that regulate the effective levels of matrix metalloproteinases (MMPs) 2 and 9, which are key effectors of ECM remodeling. Here, we report that THBS2 is associated with LDH in Japanese populations. An intronic SNP in THBS2 (IVS10-8C -> T; rs9406328) showed significant association (p = 0.0000028) with LDH in two independent Japanese populations. This SNP, located in a polypyrimidine tract upstream of the 3' splice site of intron 10, exerts allelic differences on exon 11 skipping rates in vivo, with the susceptibility allele showing increased skipping. Skipping of exon 11 results in decreased THBS2 interaction with MMP2 and MMP9. Further, a missense SNP in MMP9 (Q279R; rs17576) is also strongly associated with LDH in the Japanese population (p = 0.00049) and shows a combinatorial effect with THBS2 (odds ratio 3.03, 95% confidence interval 1.58-5.77). Thus, a splicing-affecting SNP in THBS2 and a missense SNP in MMP9 are associated with susceptibility to LDH. Our data indicate that regulation of intervertebral disc ECM metabolism by the THBS2-MMP system plays an essential role in the etiology and pathogenesis of LDH.
C1 [Hirose, Yuichiro; Karasugi, Tatsuki; Nakajima, Masahiro; Furuichi, Tatsuya; Mio, Futoshi; Miyake, Atsushi; Ikegawa, Shiro] RIKEN, SNP Res Ctr, Lab Bone & Joint Dis, Minato Ku, Tokyo 1088639, Japan.
   [Hirose, Yuichiro; Chiba, Kazuhiro; Mio, Futoshi; Miyake, Atsushi; Miyamoto, Takeshi; Toyama, Yoshiaki] Keio Univ, Sch Med, Dept Orthopaed Surg, Shinjuku Ku, Tokyo 1608582, Japan.
   [Karasugi, Tatsuki; Mizuta, Hiroshi] Kumamoto Univ, Fac Med & Pharmaceut Sci, Dept Orthopaed & Neuro Musculoskeletal Surg, Kumamoto 8608556, Japan.
   Toyama Univ, Fac Med, Dept Orthopaed Surg, Toyama 9300194, Japan.
   Kyoto Prefectural Univ Med, Grad Sch Med Sci, Dept Orthopaed, Kamigyo Ku, Kyoto 6028566, Japan.
   [Ozaki, Kouichi; Tanaka, Toshihiro] RIKEN, SNP Res Ctr, Lab Cardiovasc Dis, Minato Ku, Tokyo 1088639, Japan.
   [Takahashi, Atsushi] RIKEN, SNP Res Ctr, Stat Lab, Minato Ku, Tokyo 1088639, Japan.
C3 RIKEN; Keio University; Kumamoto University; University of Toyama; Kyoto
   Prefectural University of Medicine; RIKEN; RIKEN
RP Ikegawa, S (corresponding author), RIKEN, SNP Res Ctr, Lab Bone & Joint Dis, Minato Ku, 4-6-1 Shirokanedai, Tokyo 1088639, Japan.
EM sikegawa@ims.u-tokyo.ac.jp
RI Nakajima, Masahiro/J-3566-2019; Ikegawa, Shiro/N-6895-2015; Miyake,
   Atsushi/AAR-4912-2021; MIZUTA, HIROSHI/F-1611-2011; Toyama,
   Yoshiaki/K-5743-2013; Tanaka, Toshihiro/J-9310-2014
OI Tanaka, Toshihiro/0000-0001-6201-9784; Ozaki,
   Kouichi/0000-0003-0028-1570; Furuichi, Tatsuya/0000-0001-5656-1235
CR Adams JC, 2000, DEV DYNAM, V218, P280
   Agah A, 2005, AM J PATHOL, V167, P81, DOI 10.1016/S0002-9440(10)62955-0
   ALLAN JA, 1995, BIOCHEM J, V309, P299, DOI 10.1042/bj3090299
   Andersson GBJ, 1999, LANCET, V354, P581, DOI 10.1016/S0140-6736(99)01312-4
   Annunen S, 1999, SCIENCE, V285, P409, DOI 10.1126/science.285.5426.409
   BATTIE MC, 1995, J BONE JOINT SURG AM, V77A, P1662, DOI 10.2106/00004623-199511000-00004
   Bein K, 2000, J BIOL CHEM, V275, P32167, DOI 10.1074/jbc.M003834200
   BORNSTEIN P, 1995, J CELL BIOL, V130, P503, DOI 10.1083/jcb.130.3.503
   BORNSTEIN P, 1994, METHOD ENZYMOL, V245, P62
   BORNSTEIN P, 1992, FASEB J, V6, P3290, DOI 10.1096/fasebj.6.14.1426766
   Chano T, 1998, VIRCHOWS ARCH, V432, P529, DOI 10.1007/s004280050201
   Emonard H, 2004, J BIOL CHEM, V279, P54944, DOI 10.1074/jbc.M406792200
   EXCOFFIER L, 1995, MOL BIOL EVOL, V12, P921
   Freedman ML, 2004, NAT GENET, V36, P388, DOI 10.1038/ng1333
   GOLDBERG GI, 1989, P NATL ACAD SCI USA, V86, P8207, DOI 10.1073/pnas.86.21.8207
   Gruber HE, 2006, SPINE, V31, P2556, DOI 10.1097/01.brs.0000241117.31510.e3
   Hahn-Dantona E, 2001, J BIOL CHEM, V276, P15498, DOI 10.1074/jbc.M100121200
   Hu ZB, 2005, CLIN CANCER RES, V11, P5433, DOI 10.1158/1078-0432.CCR-05-0311
   Kunisada T, 1998, INT J CANCER, V77, P854, DOI 10.1002/(SICI)1097-0215(19980911)77:6<854::AID-IJC10>3.0.CO;2-1
   Kyriakides TR, 1998, J CELL BIOL, V140, P419, DOI 10.1083/jcb.140.2.419
   Lawler J, 1998, J CLIN INVEST, V101, P982, DOI 10.1172/JCI1684
   Matsui H, 1998, SPINE, V23, P1029, DOI 10.1097/00007632-199805010-00013
   Natividad A, 2006, BMC MED GENET, V7, DOI 10.1186/1471-2350-7-40
   O'Farrell TJ, 2000, J BIOL CHEM, V275, P27964
   Ohnishi Y, 2001, J HUM GENET, V46, P471, DOI 10.1007/s100380170047
   Pritchard JK, 1999, AM J HUM GENET, V65, P220, DOI 10.1086/302449
   Ribeiro SMF, 1999, J BIOL CHEM, V274, P13586, DOI 10.1074/jbc.274.19.13586
   SAAL JA, 1989, SPINE, V14, P431, DOI 10.1097/00007632-198904000-00018
   Sambrook PN, 1999, ARTHRITIS RHEUM-US, V42, P366, DOI 10.1002/1529-0131(199902)42:2<366::AID-ANR20>3.0.CO;2-6
   SCHULTZCHERRY S, 1995, J BIOL CHEM, V270, P7304, DOI 10.1074/jbc.270.13.7304
   Seki S, 2005, NAT GENET, V37, P607, DOI 10.1038/ng1557
   Sladek R, 2007, NATURE, V445, P881, DOI 10.1038/nature05616
   WILHELM SM, 1989, J BIOL CHEM, V264, P17213
   Yamada R, 2001, AM J HUM GENET, V68, P674, DOI 10.1086/318789
   Yang ZT, 2001, J BIOL CHEM, V276, P8403, DOI 10.1074/jbc.M008925200
   Yang ZT, 2000, MOL BIOL CELL, V11, P3353, DOI 10.1091/mbc.11.10.3353
NR 36
TC 95
Z9 121
U1 1
U2 7
PU CELL PRESS
PI CAMBRIDGE
PA 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA
SN 0002-9297
J9 AM J HUM GENET
JI Am. J. Hum. Genet.
PD MAY
PY 2008
VL 82
IS 5
BP 1122
EP 1129
DI 10.1016/j.ajhg.2008.03.013
PG 8
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA 301VJ
UT WOS:000255923600011
PM 18455130
OA Green Accepted, Bronze, Green Published
DA 2025-04-10
ER

PT J
AU Berger, UV
   DeSilva, TM
   Chen, WZ
   Rosenberg, PA
AF Berger, UV
   DeSilva, TM
   Chen, WZ
   Rosenberg, PA
TI Cellular and subcellular mRNA localization of glutamate transporter
   isoforms GLT1a and GLT1b in rat brain by in situ hybridization
SO JOURNAL OF COMPARATIVE NEUROLOGY
LA English
DT Article
DE uptake; presynaptic; alternative splicing; excitotoxicity; excitatory;
   synapse; retina; pineal
ID 2 SPLICE VARIANTS; DIFFERENTIAL DISTRIBUTION; PICK1 INTERACTS;
   CEREBRAL-CORTEX; BINDING-PROTEIN; EXPRESSION; GLT-1; HIPPOCAMPUS;
   SUBSTRATE; RELEASE
AB GLT1, the predominant glutamate transporter of the forebrain, exists in two splice variant isoforms, i.e., GLT1a and GLT1b. Although GLT1 was originally detected only in astrocytes, we have recently demonstrated that GLT1a protein is expressed by neurons in the hippocampus as well. In the present study, the mRNA distribution patterns for the two isoforms were examined throughout the rat brain by using nonisotopic in situ hybridization and variant-specific RNA probes. Both isoforms were expressed in neuronal subgroups outside the hippocampus, such as in the cerebral cortex layer VI, or the neurons in the olfactory tubercle. As was the case in the hippocampus, GLT1a was the predominant transcript in neurons in these regions as well. Both GLT1 isoforms were widely expressed in astrocytes throughout the brain. GLT1a mRNA expression in astrocytes showed noticeable variation in labeling intensity in subregions of the hippocampus and other areas, whereas GLT1b expression in astrocytes was relatively homogeneous. On the subcellular level, GLT1a mRNA was expressed primarily in astrocyte processes, whereas GLT1b mRNA was more restricted to the astrocyte cell body. The two isoforms showed similar distributions in the subfornical organ and in tanycytes of the third ventricle. However, GLT1 expression in the pineal gland and the retina was due primarily to GLT1b, whereas GLT1a was more strongly expressed in Bergman glia in the cerebellum. These findings suggest that the expression of the two GLT1 isoforms is regulated by different mechanisms. Moreover, the function of the two isoforms may be subject to different regulatory processes.
C1 Childrens Hosp, Dept Neurol, Boston, MA 02115 USA.
   Harvard Univ, Sch Med, Program Neurosci, Boston, MA 02115 USA.
   UB In Situ, Natick, MA 01760 USA.
C3 Harvard University; Harvard University Medical Affiliates; Boston
   Children's Hospital; Harvard University; Harvard Medical School
RP Childrens Hosp, Dept Neurol, 300 Longwood Ave,Enders 349, Boston, MA 02115 USA.
EM paul.rosenberg@tch.harvard.edu
RI Chen, Honglei/ABG-8632-2021
OI DeSilva, Tara/0000-0002-1212-5762; Chen, Weizhi/0000-0002-5099-2680;
   Rosenberg, Paul/0000-0002-5185-1118
FU NICHD NIH HHS [HD 18655, P30 HD018655] Funding Source: Medline; NINDS
   NIH HHS [R01 NS041883, R01 NS040753, NS 40753, NS 41883] Funding Source:
   Medline
CR BASSAN M, 2004, SOC NEUR ABSTR
   BASSAN M, 2003, SOC NEUR ABSTR, V29
   Berger UV, 2000, J COMP NEUROL, V421, P385, DOI 10.1002/(SICI)1096-9861(20000605)421:3<385::AID-CNE7>3.0.CO;2-S
   Berger UV, 2001, J COMP NEUROL, V433, P101, DOI 10.1002/cne.1128
   Berger UV, 1998, ANAT EMBRYOL, V198, P13, DOI 10.1007/s004290050161
   Boudin H, 2000, NEURON, V28, P485, DOI 10.1016/S0896-6273(00)00127-6
   CHEN W, 2001, SOC NEUR ABSTR
   Chen WZ, 2004, J NEUROSCI, V24, P1136, DOI 10.1523/JNEUROSCI.1586-03.2004
   Chen WZ, 2002, J NEUROSCI, V22, P2142, DOI 10.1523/JNEUROSCI.22-06-02142.2002
   Danbolt NC, 2001, PROG NEUROBIOL, V65, P1, DOI 10.1016/S0301-0082(00)00067-8
   Dev KK, 1999, NEUROPHARMACOLOGY, V38, P635, DOI 10.1016/S0028-3908(98)00230-5
   Dev KK, 2000, J NEUROSCI, V20, P7252
   El Far O, 2000, EUR J NEUROSCI, V12, P4215, DOI 10.1111/j.1460-9568.2000.01309.x
   KUGLER P, 2003, HISTOCHEM CELL BIOL
   Lehre KP, 1998, J NEUROSCI, V18, P8751, DOI 10.1523/jneurosci.18-21-08751.1998
   MADL JE, 1993, J NEUROSCI, V13, P4429
   MAHADOMRONGKUL V, 2002, SOC NEUR ABSTR, V28
   MANGANO RM, 1983, BRAIN RES BULL, V10, P47, DOI 10.1016/0361-9230(83)90073-4
   Maragakis NJ, 2004, ANN NEUROL, V55, P469, DOI 10.1002/ana.20003
   Reagan LP, 2004, P NATL ACAD SCI USA, V101, P2179, DOI 10.1073/pnas.0307294101
   Reye P, 2002, J COMP NEUROL, V445, P1, DOI 10.1002/cne.10095
   Reye P, 2002, J COMP NEUROL, V447, P323, DOI 10.1002/cne.10218
   ROSENBERG PA, 1992, J NEUROSCI, V12, P56
   Rossi DJ, 2000, NATURE, V403, P316, DOI 10.1038/35002090
   ROTHSTEIN JD, 1994, NEURON, V13, P713, DOI 10.1016/0896-6273(94)90038-8
   Rusakov DA, 1998, J NEUROSCI, V18, P3158
   Schmitt A, 1996, NEUROSCIENCE, V71, P989, DOI 10.1016/0306-4522(95)00477-7
   Schmitt A, 2002, NEUROSCIENCE, V109, P45, DOI 10.1016/S0306-4522(01)00451-1
   Sheng M, 2001, ANNU REV NEUROSCI, V24, P1, DOI 10.1146/annurev.neuro.24.1.1
   STAUDINGER J, 1995, J CELL BIOL, V128, P263, DOI 10.1083/jcb.128.3.263
   Staudinger J, 1997, J BIOL CHEM, V272, P32019, DOI 10.1074/jbc.272.51.32019
   STORMMATHISEN J, 1992, PROG BRAIN RES, V94, P225
   Sullivan R, 2004, GLIA, V45, P155, DOI 10.1002/glia.10317
   SZATKOWSKI M, 1990, NATURE, V348, P443, DOI 10.1038/348443a0
   Tanaka K, 1997, SCIENCE, V276, P1699, DOI 10.1126/science.276.5319.1699
   Torp R, 1997, ANAT EMBRYOL, V195, P317, DOI 10.1007/s004290050051
   TORP R, 1995, EXP BRAIN RES, V103, P51
   TORP R, 1994, EUR J NEUROSCI, V6, P936, DOI 10.1111/j.1460-9568.1994.tb00587.x
   UtsunomiyaTate N, 1997, FEBS LETT, V416, P312, DOI 10.1016/S0014-5793(97)01232-5
   Wilson JMB, 2003, NEUROMOL MED, V3, P105, DOI 10.1385/NMM:3:2:105
   Xia J, 1999, NEURON, V22, P179, DOI 10.1016/S0896-6273(00)80689-3
NR 41
TC 92
Z9 108
U1 0
U2 3
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0021-9967
EI 1096-9861
J9 J COMP NEUROL
JI J. Comp. Neurol.
PD NOV 7
PY 2005
VL 492
IS 1
BP 78
EP 89
DI 10.1002/cne.20737
PG 12
WC Neurosciences; Zoology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology; Zoology
GA 970DF
UT WOS:000232284700006
PM 16175560
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Gong, J
   Hou, Y
   Zha, XF
   Lu, C
   Zhu, Y
   Xia, QY
AF Gong, Jing
   Hou, Yong
   Zha, Xing-Fu
   Lu, Cheng
   Zhu, Yong
   Xia, Qing-You
TI Molecular cloning and characterization of Bombyx mori sterol
   carrier protein x/sterol carrier protein 2 (SCPx/SCP2) gene
SO DNA SEQUENCE
LA English
DT Article
DE Bombyx mori; cholesterol; SCPx/SCP2; alternative splicing; gene
   expression
ID STEROL CARRIER PROTEIN-2; YELLOW-FEVER MOSQUITO; HELIOTHIS-ZEA;
   AEDES-AEGYPTI; MANDUCA-SEXTA; X GENE; EXPRESSION; CHOLESTEROL; SEQUENCE;
   THIOLASE
AB Cholesterol transport is a very important process in insect. We have isolated the Bombyx mori sterol carrier protein x (BmSCPx) cDNA and sterol carrier protein 2 (BmSCP2) cDNA: a 1.7 kb clone encoding SCPx, a 3-ketoacyl CoA thiolase, and 0.6 kb clone presumably encoding SCP2, which is thought to be an intracellular lipid transfer protein. Interestingly, the identical gene SCPx/SCP2 encodes the two types of transcripts by alternative splicing mechanism in Bombyx mori. The SCPx mRNA spans two exons in genome, and conceptual translation of the SCPx cDNA encodes a protein of 536 amino acids, which contains a thiolase domain and a SCP2 domain. Whereas the SCP2 mRNA partly lakes the first exon, and the SCP2 is a 146 amino acids containing a SCP2 domain only. Both BmSCPx and BmSCP2 have a putative peroxisomal targeting signal in the C-terminal region. BmSCPx shares 94 and 72% similarity to Spodoptera littoralis SCPx and human SCPx, respectively. RTPCR analysis reveals that transcripts of BmSCP2 were detected in all tissues analyzed. BmSCPx transcription expressed only in midgut and malpighian tubules. However, the BmSCPx and BmSCP2 express strong in midgut during the last instar larvae. The tissue-specific expression pattern of BmSCPx and BmSCP2 is consistent with a role for these proteins in cholesterol metabolism. The results suggest that SCPx/SCP2 may play a key role in sterol absorption and intracellular carrier in silkworm.
C1 Southwest Univ, Key Sericultural Lab, Minist Agr, Chongqing 400715, Peoples R China.
C3 Ministry of Agriculture & Rural Affairs; Southwest University - China
RP Xia, QY (corresponding author), Southwest Univ, Key Sericultural Lab, Minist Agr, Chongqing 400715, Peoples R China.
EM xiaqy@swau.cq.cn
RI li, yue/IXD-9935-2023; Zhang, Xinhua/A-3225-2011
OI Zha, Xingfu/0000-0003-2085-5260
CR BEYDON P, 1987, ARCH INSECT BIOCHEM, V5, P139, DOI 10.1002/arch.940050208
   Blitzer EJ, 2005, INSECT MOL BIOL, V14, P301, DOI 10.1111/j.1365-2583.2005.00560.x
   BunYa M, 1997, EUR J BIOCHEM, V245, P252, DOI 10.1111/j.1432-1033.1997.t01-1-00252.x
   DEBIANCHI AG, 1991, ARCH INSECT BIOCHEM, V17, P15, DOI 10.1002/arch.940170104
   Florea L, 1998, GENOME RES, V8, P967, DOI 10.1101/gr.8.9.967
   Gallegos AM, 2001, PROG LIPID RES, V40, P498, DOI 10.1016/S0163-7827(01)00015-7
   Gilbert LI, 2002, ANNU REV ENTOMOL, V47, P883, DOI 10.1146/annurev.ento.47.091201.145302
   GRIENEISEN ML, 1994, INSECT BIOCHEM MOLEC, V24, P115, DOI 10.1016/0965-1748(94)90078-7
   Jouni ZE, 2002, ARCH INSECT BIOCHEM, V49, P167, DOI 10.1002/arch.10017
   Kitamura T, 1996, DEV GROWTH DIFFER, V38, P373, DOI 10.1046/j.1440-169X.1996.t01-3-00005.x
   Krebs KC, 2003, INSECT MOL BIOL, V12, P51, DOI 10.1046/j.1365-2583.2003.00386.x
   KUTHIALA A, 1988, ARCH INSECT BIOCHEM, V7, P225, DOI 10.1002/arch.940070402
   Lan Q, 2004, INSECT MOL BIOL, V13, P519, DOI 10.1111/j.0962-1075.2004.00510.x
   Nes WD, 1997, LIPIDS, V32, P1317, DOI 10.1007/s11745-006-0170-5
   OHBA T, 1995, BIOCHEMISTRY-US, V34, P10660, DOI 10.1021/bi00033a042
   OHBA T, 1994, GENOMICS, V24, P370, DOI 10.1006/geno.1994.1630
   PFEIFER SM, 1993, ARCH BIOCHEM BIOPHYS, V304, P287, DOI 10.1006/abbi.1993.1351
   RITTER KS, 1981, J INSECT PHYSIOL, V27, P175, DOI 10.1016/0022-1910(81)90125-6
   Schroeder F, 2001, EXP BIOL MED, V226, P873, DOI 10.1177/153537020122601002
   Seedorf U, 2000, BBA-MOL CELL BIOL L, V1486, P45, DOI 10.1016/S1388-1981(00)00047-0
   SEEDORF U, 1991, J BIOL CHEM, V266, P630
   Seedorf U, 1998, GENE DEV, V12, P1189, DOI 10.1101/gad.12.8.1189
   SOULAGES JL, 1991, J LIPID RES, V32, P407
   Stolowich NJ, 2002, CELL MOL LIFE SCI, V59, P193, DOI 10.1007/s00018-002-8416-8
   SVOBODA JA, 1995, LIPIDS, V30, P263, DOI 10.1007/BF02537831
   Takeuchi H, 2004, BIOCHEM J, V382, P93, DOI 10.1042/BJ20040717
   TAN H, 1990, EUR J BIOCHEM, V190, P107, DOI 10.1111/j.1432-1033.1990.tb15552.x
   Thompson JD, 1997, NUCLEIC ACIDS RES, V25, P4876, DOI 10.1093/nar/25.24.4876
   THOMPSON S, 1989, BIOCHEMISTRY-US, V28, P5735, DOI 10.1021/bi00440a006
   Xia QY, 2004, SCIENCE, V306, P1937, DOI 10.1126/science.1102210
   Yamaguchi N, 2001, LANCET ONCOL, V2, P88, DOI 10.1016/S1470-2045(00)00225-4
NR 31
TC 17
Z9 22
U1 4
U2 15
PU INFORMA HEALTHCARE
PI NEW YORK
PA 52 VANDERBILT AVE, NEW YORK, NY 10017 USA
SN 1042-5179
J9 DNA SEQUENCE
JI DNA Seq.
PD OCT
PY 2006
VL 17
IS 5
BP 326
EP 333
DI 10.1080/10425170600886706
PG 8
WC Biotechnology & Applied Microbiology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biotechnology & Applied Microbiology; Genetics & Heredity
GA 122WI
UT WOS:000243257700002
PM 17343205
DA 2025-04-10
ER

PT J
AU Rainis, L
   Bercovich, D
   Strehl, S
   Teigler-Schlegel, A
   Stark, B
   Trka, J
   Amariglio, N
   Biondi, A
   Muler, I
   Rechavi, G
   Kempski, H
   Haas, OA
   Izraeli, S
AF Rainis, L
   Bercovich, D
   Strehl, S
   Teigler-Schlegel, A
   Stark, B
   Trka, J
   Amariglio, N
   Biondi, A
   Muler, I
   Rechavi, G
   Kempski, H
   Haas, OA
   Izraeli, S
TI Mutations in exon 2 of GATA1 are early events in megakaryocytic
   malignancies associated with trisomy 21
SO BLOOD
LA English
DT Article
ID TRANSIENT MYELOPROLIFERATIVE DISORDER; ACUTE MEGAKARYOBLASTIC LEUKEMIA;
   ACUTE MYELOID-LEUKEMIA; ACUTE MYELOGENOUS LEUKEMIA; DOWN-SYNDROME;
   ABNORMAL MYELOPOIESIS; TRANSCRIPTION FACTOR; ACQUIRED TRISOMY-21;
   HEMATOPOIESIS; THROMBOCYTOPENIA
AB Patients with Down syndrome (DS) frequently develop 2 kinds of clonal megakaryocytosis: a common, congenital, spontaneously resolving, transient myeloproliferative disorder (TMD) and, less commonly, childhood acute megakaryoblastic leukemia (AMKL). Recently, acquired mutations in exon 2 of GATA1, an X-linked gene encoding a transcription factor that promotes megakaryocytic differentiation, were described in 6 DS patients with AMKL. The mutations prevent the synthesis of the full-length GATA1, but allow the synthesis of a shorter GATA1 protein (GATA1s) that lacks the transactivation domain. To test whether mutated GATA1 is involved in the initiation of clonal megakaryoblastic proliferation or in the progression to AMKL, we screened 35 DS patients with either AMKL or TMD and 7 non-DS children with AMKL for mutations in exon 2 of GATA1. Mutations were identified in 16 of 18 DS patients with AMKL, in 16 of 17 DS patients with TMD, and in 2 identical twins with AMKL and acquired trisomy 21. Analysis revealed various types of mutations in GATA1, including deletion/insertions, splice mutations, and nonsense and missense point mutations, all of which prevent the generation of full-length GATA1, but preserve the translation of GATA1s. We also show that the likely mechanism of generation of GATA1 isoforms is alternative splicing of exon 2 rather than, or in addition to, alternative translation initiation, as was proposed before. These findings suggest that acquired intrauterine inactivating mutations in GATA1 and generation of GATA1s cooperate frequently with trisomy 21 in initiating megakaryoblastic proliferation, but are insufficient for progression to AMKL.
C1 Chaim Sheba Med Ctr, Safra Childrens Hosp, Dept Pediat Hematooncol, Res Sect, IL-52621 Tel Hashomer, Israel.
   Tel Aviv Sourasky Med Ctr, Inst Genet, Tel Aviv, Israel.
   Tel Aviv Sourasky Med Ctr, Prenatal Diag Unit, Tel Aviv, Israel.
   Migal Galilee Technol Ctr, Dept Human Mol Genet, Kyriat Shemona, Israel.
   St Anna Childrens Hosp, Childrens Canc Res Inst, A-1090 Vienna, Austria.
   Childrens Univ Hosp, Dept Pediat Hematol & Oncol, Oncogenet Lab, Giessen, Germany.
   Schneider Childrens Hosp, Dept Pediat Hematooncol, Petah Tiqwa, Israel.
   Charles Univ, Med Sch 2, Dept Pediat 2, Genet Mol Lab, Prague, Czech Republic.
   Univ Milano Bicocca, Pediat Clin, Ctr M Tettamanti, Monza, Italy.
   Great Ormond St Hosp Sick Children, London, England.
   Inst Child Hlth, London, England.
C3 Chaim Sheba Medical Center; Tel Aviv University; Sackler Faculty of
   Medicine; Tel Aviv Sourasky Medical Center; Tel Aviv University; Sackler
   Faculty of Medicine; Tel Aviv Sourasky Medical Center; Saint Anna
   Children's Hospital; St. Anna Children's Cancer Research Institute
   (CCRI); Charles University Prague; University of Milano-Bicocca;
   University of London; University College London; Great Ormond Street
   Hospital for Children NHS Foundation Trust; University of London;
   University College London
RP Izraeli, S (corresponding author), Chaim Sheba Med Ctr, Safra Childrens Hosp, Dept Pediat Hematooncol, Res Sect, IL-52621 Tel Hashomer, Israel.
RI Trka, Jan/Y-4820-2019; Haas, Oskar/AAM-5794-2020; Biondi,
   Andrea/K-9997-2016
OI Biondi, Andrea/0000-0002-6757-6173; Strehl, Sabine/0000-0002-0179-0628
CR Al-Kasim F, 2002, J PEDIAT HEMATOL ONC, V24, P9, DOI 10.1097/00043426-200201000-00004
   Arceci RJ, 2002, J PEDIAT HEMATOL ONC, V24, P1, DOI 10.1097/00043426-200201000-00001
   Bodamer OA, 2002, CLIN CHEM, V48, P1913
   CALLIGARIS R, 1995, P NATL ACAD SCI USA, V92, P11598, DOI 10.1073/pnas.92.25.11598
   Cantor AB, 2002, ONCOGENE, V21, P3368, DOI 10.1038/sj.onc.1205326
   Cavani S, 1998, BRIT J HAEMATOL, V103, P213, DOI 10.1046/j.1365-2141.1998.00924.x
   Dastugue N, 2002, BLOOD, V100, P618, DOI 10.1182/blood-2001-12-0241
   Freson K, 2002, HUM MOL GENET, V11, P147, DOI 10.1093/hmg/11.2.147
   Gamis AS, 2002, J PEDIAT HEMATOL ONC, V24, P2, DOI 10.1097/00043426-200201000-00002
   Gavert Nancy, 2002, Hum Mutat, V19, P664, DOI 10.1002/humu.9037
   Gilliland DG, 2002, BLOOD, V100, P1532, DOI 10.1182/blood-2002-02-0492
   Hasle H, 2001, LANCET ONCOL, V2, P429, DOI 10.1016/S1470-2045(00)00435-6
   Holt SE, 2002, J PEDIAT HEMATOL ONC, V24, P14, DOI 10.1097/00043426-200201000-00005
   Karandikar NJ, 2001, AM J CLIN PATHOL, V116, P204
   Kelly LM, 2002, ANNU REV GENOM HUM G, V3, P179, DOI 10.1146/annurev.genom.3.032802.115046
   KURAHASHI H, 1992, LEUKEMIA LYMPHOMA, V8, P465, DOI 10.3109/10428199209051029
   KURAHASHI H, 1991, BLOOD, V77, P1161
   Lange B, 2000, BRIT J HAEMATOL, V110, P512, DOI 10.1046/j.1365-2141.2000.02027.x
   Legare RD, 1997, LEUKEMIA, V11, P2111, DOI 10.1038/sj.leu.2400852
   Look AT, 2002, NAT GENET, V32, P83, DOI 10.1038/ng960
   Ma SK, 1999, LEUKEMIA, V13, P491, DOI 10.1038/sj.leu.2401330
   Ma SK, 2001, BRIT J HAEMATOL, V112, P824, DOI 10.1046/j.1365-2141.2001.02616.x
   Malkin D, 2000, CANCER GENET CYTOGEN, V116, P1, DOI 10.1016/S0165-4608(99)00072-2
   Nichols KE, 2000, NAT GENET, V24, P266, DOI 10.1038/73480
   Orkin S H, 1998, Stem Cells, V16 Suppl 2, P79
   Pabst T, 2001, NAT GENET, V27, P263, DOI 10.1038/85820
   Preudhomme C, 2000, BLOOD, V96, P2862, DOI 10.1182/blood.V96.8.2862.h8002862_2862_2869
   Shivdasani RA, 1997, EMBO J, V16, P3965, DOI 10.1093/emboj/16.13.3965
   Shivdasani RA, 2001, STEM CELLS, V19, P397, DOI 10.1634/stemcells.19-5-397
   Song WJ, 1999, NAT GENET, V23, P166, DOI 10.1038/13793
   Speck NA, 2002, NAT REV CANCER, V2, P502, DOI 10.1038/nrc840
   Stark B, 2002, BRIT J HAEMATOL, V118, P1082, DOI 10.1046/j.1365-2141.2002.03756.x
   Taketani T, 2002, LEUKEMIA, V16, P1866, DOI 10.1038/sj.leu.2402612
   Wechsler J, 2002, NAT GENET, V32, P148, DOI 10.1038/ng955
   Yu CN, 2002, BLOOD, V100, P2040, DOI 10.1182/blood-2002-02-0387
   Zipursky A, 1997, SEMIN PERINATOL, V21, P97, DOI 10.1016/S0146-0005(97)80025-0
   Zipursky A, 1999, CLIN LAB MED, V19, P157
   ZIPURSKY A, 1987, PEDIATR HEMAT ONCOL, V4, P211, DOI 10.3109/08880018709141272
   ZIPURSKY A, 1992, PEDIATR HEMAT ONCOL, V9, P139, DOI 10.3109/08880019209018329
NR 39
TC 229
Z9 243
U1 0
U2 12
PU AMER SOC HEMATOLOGY
PI WASHINGTON
PA 1900 M STREET. NW SUITE 200, WASHINGTON, DC 20036 USA
SN 0006-4971
J9 BLOOD
JI Blood
PD AUG 1
PY 2003
VL 102
IS 3
BP 981
EP 986
DI 10.1182/blood-2002-11-3599
PG 6
WC Hematology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Hematology
GA 705LD
UT WOS:000184395800044
PM 12649131
OA Bronze
DA 2025-04-10
ER

PT J
AU Tanizawa, Y
   Matsubara, A
   Ueda, K
   Katagiri, H
   Kuwano, A
   Ferrer, J
   Permutt, MA
   Oka, Y
AF Tanizawa, Y
   Matsubara, A
   Ueda, K
   Katagiri, H
   Kuwano, A
   Ferrer, J
   Permutt, MA
   Oka, Y
TI A human pancreatic islet inwardly rectifying potassium channel: cDNA
   cloning, determination of the genomic structure and genetic variations
   in Japanese NIDDM patients
SO DIABETOLOGIA
LA English
DT Article
DE potassium channel; inward rectifier; noninsulin-dependent diabetes
   mellitus; genetics; single strand conformation polymorphism
ID GLUCOKINASE GENE; FUNCTIONAL EXPRESSION; BETA-CELL
AB Ligand gated potassium channels, such as the ATP-regulated potassium channel, play crucial roles in coupling of stimuli to insulin secretion in pancreatic beta cells. Mutations in the genes might lead to the insulin secretory defects observed in patients with non-insulin-dependent diabetes mellitus (NIDDM). We isolated a cDNA encoding a putative subunit of a ligand gated potassium channel from a human islet cDNA library. The channel, which we designated hiGIRK2, appeared to be an alternative spliced variant and a human homologue of recently reported mbGIRK2, K-ATP-2/BIR1. Transcripts were detected in human brain and pancreas, but not in other tissues including cardiac muscle, The sizes of transcripts in the pancreas differed from those in the brain, suggesting tissue-specific alternative splicing and possible isoforms. We then isolated human genomic clones, determined the complete genomic structure and localized the gene to chromosome 21 (21q22). The gene was comprised of four exons and the protein was encoded by three exons. The entire coding region of the hiGIRK2 gene was scanned by polymerase chain reaction-single strand conformation polymorphism analysis in 80 Japanese NIDDM patients. We found five nucleotide substitutions; three were silent mutations of the third base of codons, one in the first intron, 9 bases upstream of exon 2, and one in the 3'-untranslated region. We conclude that mutations in the gene encoding hiGIRK2, a (subunit of) ligand gated potassium channel, is not a major determinant of the susceptibility to NIDDM in Japanese.
C1 UNIV TOKYO,FAC MED,DEPT INTERNAL MED 3,TOKYO 113,JAPAN.
   EHIME UNIV,SCH MED,DEPT HYG,MATSUYAMA,EHIME,JAPAN.
   UNIV WASHINGTON,SCH MED,DIV METAB,ST LOUIS,MO.
C3 University of Tokyo; Ehime University; Washington University (WUSTL)
RP Tanizawa, Y (corresponding author), YAMAGUCHI UNIV,SCH MED,DEPT INTERNAL MED 3,1144 KOGUSHI,UBE,YAMAGUCHI 755,JAPAN.
RI Ferrer, Jorge/A-3176-2012
OI Ferrer, Jorge/0000-0002-5959-5729
FU NIDDK NIH HHS [DK16746] Funding Source: Medline
CR AGUILARBRYAN L, 1995, SCIENCE, V268, P423, DOI 10.1126/science.7716547
   ALAWQATI Q, 1995, SCIENCE, V269, P805, DOI 10.1126/science.7543697
   ASHCROFT FM, 1989, PROG BIOPHYS MOL BIO, V54, P87, DOI 10.1016/0079-6107(89)90013-8
   ASHFORD MLJ, 1994, NATURE, V370, P456, DOI 10.1038/370456a0
   FERRER J, 1995, J BIOL CHEM, V270, P26086, DOI 10.1074/jbc.270.44.26086
   HO K, 1993, NATURE, V362, P31, DOI 10.1038/362031a0
   INAGAKI N, 1995, J BIOL CHEM, V270, P5691, DOI 10.1074/jbc.270.11.5691
   KANAME T, 1993, CYTOGENET CELL GENET, V64, P195, DOI 10.1159/000133573
   KOSA, 1995, IL, V367, P61
   KOSAKA K, 1977, DIABETES, V26, P944, DOI 10.2337/diab.26.10.944
   KRAPIVINSKY G, 1995, NATURE, V374, P135, DOI 10.1038/374135a0
   KUBO Y, 1993, NATURE, V362, P127, DOI 10.1038/362127a0
   KUBO Y, 1993, NATURE, V364, P802, DOI 10.1038/364802a0
   KUWANO A, 1991, AM J HUM GENET, V49, P707
   LESAGE F, 1994, FEBS LETT, V353, P37, DOI 10.1016/0014-5793(94)01007-2
   MIYAZAKI JI, 1990, ENDOCRINOLOGY, V127, P126, DOI 10.1210/endo-127-1-126
   NODA K, 1993, DIABETES, V42, P1147, DOI 10.2337/diabetes.42.8.1147
   ORITA M, 1989, GENOMICS, V5, P874, DOI 10.1016/0888-7543(89)90129-8
   PONGS O, 1992, PHYSIOL REV, V72, pS69, DOI 10.1152/physrev.1992.72.suppl_4.S69
   RORSMAN P, 1991, NATURE, V349, P77, DOI 10.1038/349077a0
   SAKURA H, 1995, FEBS LETT, V367, P193, DOI 10.1016/0014-5793(95)00498-X
   SCHWIEBERT EM, 1995, CELL, V81, P1063, DOI 10.1016/S0092-8674(05)80011-X
   TANIZAWA Y, 1992, MOL ENDOCRINOL, V6, P1070, DOI 10.1210/me.6.7.1070
   TANIZAWA Y, 1991, P NATL ACAD SCI USA, V88, P7294, DOI 10.1073/pnas.88.16.7294
   TAYLOR SI, 1994, DIABETES, V43, P735, DOI 10.2337/diab.43.6.735
   THOMAS PM, 1995, SCIENCE, V268, P426, DOI 10.1126/science.7716548
   TSAUR ML, 1995, DIABETES, V44, P592, DOI 10.2337/diabetes.44.5.592
   YASUDA K, 1995, BIOCHEM BIOPH RES CO, V211, P1036, DOI 10.1006/bbrc.1995.1915
   YONEDA H, 1992, DIABETES CARE, V15, P1517, DOI 10.2337/diacare.15.11.1517
   ZHANG Y, 1995, DIABETES, V44, P597, DOI 10.2337/diabetes.44.5.597
NR 30
TC 12
Z9 15
U1 0
U2 0
PU SPRINGER VERLAG
PI NEW YORK
PA 175 FIFTH AVE, NEW YORK, NY 10010
SN 0012-186X
J9 DIABETOLOGIA
JI Diabetologia
PD APR
PY 1996
VL 39
IS 4
BP 447
EP 452
DI 10.1007/s001250050464
PG 6
WC Endocrinology & Metabolism
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism
GA UB882
UT WOS:A1996UB88200009
PM 8777994
DA 2025-04-10
ER

PT J
AU Rani, AQM
   Yamamoto, T
   Kawaguchi, T
   Maeta, K
   Awano, H
   Nishio, H
   Matsuo, M
AF Rani, Abdul Qawee Mahyoob
   Yamamoto, Tetsushi
   Kawaguchi, Tatsuya
   Maeta, Kazuhiro
   Awano, Hiroyuki
   Nishio, Hisahide
   Matsuo, Masafumi
TI Intronic Alternative Polyadenylation in the Middle of the DMD
   Gene Produces Half-Size N-Terminal Dystrophin with a Potential
   Implication of ECG Abnormalities of DMD Patients
SO INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
LA English
DT Article
DE DMD; intronic alternative polyadenylation; dystrophin; Dpm234; Duchenne
   muscular dystrophy; iPS-derived cardiomyocytes
ID DUCHENNE MUSCULAR-DYSTROPHY; DP71; EXPRESSION; SURVIVAL; CELLS;
   ELECTROCARDIOGRAM; PREDICTORS
AB The DMD gene is one of the largest human genes, being composed of 79 exons, and encodes dystrophin Dp427m which is deficient in Duchenne muscular dystrophy (DMD). In some DMD patient, however, small size dystrophin reacting with antibody to N-terminal but not to C-terminal has been identified. The mechanism to produce N-terminal small size dystrophin remains unknown. Intronic polyadenylation is a mechanism that produces a transcript with a new 3 ' terminal exon and a C-terminal truncated protein. In this study, intronic alternative polyadenylation was disclosed to occur in the middle of the DMD gene and produce the half-size N-terminal dystrophin Dp427m, Dpm234. The 3 ' -rapid amplification of cDNA ends revealed 421 bp sequence in the downstream of DMD exon 41 in U-251 glioblastoma cells. The cloned sequence composing of the 5 ' end sequence of intron 41 was decided as the terminal exon, since it encoded poly (A) signal followed by poly (A) stretch. Subsequently, a fragment from DMD exon M1 to intron 41 was obtained by PCR amplification. This product was named Dpm234 after its molecular weight. However, Dpm234 was not PCR amplified in human skeletal and cardiac muscles. Remarkably, Dpm234 was PCR amplified in iPS-derived cardiomyocytes. Accordingly, Western blotting of cardiomyocyte proteins showed a band of 234 kDa reacting with dystrophin antibody to N-terminal, but not C-terminal. Clinically, DMD patients with mutations in the Dpm234 coding region were found to have a significantly higher likelihood of two ECG abnormal findings. Intronic alternative splicing was first revealed in Dp427m to produce small size dystrophin.
C1 [Rani, Abdul Qawee Mahyoob; Maeta, Kazuhiro; Nishio, Hisahide; Matsuo, Masafumi] Kobe Gakuin Univ, Res Ctr Locomot Biol, Nishi Ku, Kobe, Hyogo 6512180, Japan.
   [Rani, Abdul Qawee Mahyoob; Maeta, Kazuhiro; Matsuo, Masafumi] Kobe Gakuin Univ, Fac Rehabil, KNC Dept Nucle Acid Drug Discovery, Nishi Ku, Kobe, Hyogo 6512180, Japan.
   [Yamamoto, Tetsushi] Kobe Univ Hosp, Dept Clin Lab, Chuo Ku, Kobe, Hyogo 6500017, Japan.
   [Kawaguchi, Tatsuya] Daiichi Sankyo RD Novare Co Ltd, Translat Res Dept, Edogawa Ku, Tokyo 1348630, Japan.
   [Awano, Hiroyuki] Kobe Univ, Grad Sch Med, Dept Pediat, Chuo Ku, Kobe, Hyogo 6500017, Japan.
   [Nishio, Hisahide] Kobe Gakuin Univ, Fac Rehabil, Dept Occupat Therapy, Nishi Ku, Kobe, Hyogo 6512180, Japan.
C3 Kobe Gakuin University; Kobe Gakuin University; Kobe University; Daiichi
   Sankyo Company Limited; Kobe University; Kobe Gakuin University
RP Matsuo, M (corresponding author), Kobe Gakuin Univ, Res Ctr Locomot Biol, Nishi Ku, Kobe, Hyogo 6512180, Japan.; Matsuo, M (corresponding author), Kobe Gakuin Univ, Fac Rehabil, KNC Dept Nucle Acid Drug Discovery, Nishi Ku, Kobe, Hyogo 6512180, Japan.
EM rani@reha.kobegakuin.ac.jp; tetsushi@med.kobe-u.ac.jp;
   kawaguchi.tatsuya.sg@rdn.daiichisankyo.co.jp;
   maeta@reha.kobegakuin.ac.jp; awahiro@med.kobe-u.ac.jp;
   nishio@reha.kobegakuin.ac.jp; matsuo@kobe-u.ac.jp
RI HIROYUKI, AWANO/HTT-0752-2023
OI Rani, Abdul Qawee/0000-0003-0809-303X
FU JSPS KAKEN-HI [19K20673, 18K07845, 18K07861]; Intramural Research Grants
   for Neurological and Psychiatric Disorders from the National Center of
   Neurology and Psychiatry (NCNP) [29-3, 28-6]; Grants-in-Aid for
   Scientific Research [19K20673, 18K07861, 18K07845] Funding Source: KAKEN
FX This work was supported in part by JSPS KAKEN-HI Grant Number 19K20673,
   18K07845 and 18K07861 to Yamamoto, Awano and Matsuo, respectively, and
   Intramural Research Grants for Neurological and Psychiatric Disorders
   from the National Center of Neurology and Psychiatry (NCNP) (29-3 and
   28-6 to Awano and Matsuo, respectively).
CR Ashwath ML, 2014, AM J CARDIOL, V114, P284, DOI 10.1016/j.amjcard.2014.04.038
   Ben-Ari M, 2014, HEART RHYTHM, V11, P1808, DOI 10.1016/j.hrthm.2014.05.037
   Birnkrant DJ, 2016, PEDIATR PULM, V51, P70, DOI 10.1002/ppul.23215
   BULMAN DE, 1991, AM J HUM GENET, V48, P295
   Bushby K, 2010, LANCET NEUROL, V9, P77, DOI 10.1016/S1474-4422(09)70271-6
   Claudepierre T, 2000, INVEST OPHTH VIS SCI, V41, P294
   Doorenweerd N, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-12981-5
   Eagle M, 2002, NEUROMUSCULAR DISORD, V12, P926, DOI 10.1016/S0960-8966(02)00140-2
   Eisen B, 2019, J CELL MOL MED, V23, P2125, DOI 10.1111/jcmm.14124
   Elkon R, 2013, NAT REV GENET, V14, P496, DOI 10.1038/nrg3482
   FEENER CA, 1989, NATURE, V338, P509, DOI 10.1038/338509a0
   FITCH CW, 1967, CIRCULATION, V35, P1124, DOI 10.1161/01.CIR.35.6.1124
   Gazzoli I, 2016, RNA BIOL, V13, P290, DOI 10.1080/15476286.2015.1125074
   HELLIWELL TR, 1992, AM J HUM GENET, V50, P508
   HEYMSFIELD SB, 1978, AM HEART J, V95, P283, DOI 10.1016/0002-8703(78)90358-7
   Hoekstra M, 2012, FRONT PHYSIOL, V3, DOI 10.3389/fphys.2012.00346
   Ishikawa Y, 2011, NEUROMUSCULAR DISORD, V21, P47, DOI 10.1016/j.nmd.2010.09.006
   James J, 2011, NEUROMUSCULAR DISORD, V21, P462, DOI 10.1016/j.nmd.2011.04.005
   Jefferies JL, 2005, CIRCULATION, V112, P2799, DOI 10.1161/CIRCULATIONAHA.104.528281
   Lang RM, 2015, EUR HEART J-CARD IMG, V16, P233, DOI 10.1093/ehjci/jev014
   Massouridès E, 2015, SKELET MUSCLE, V5, DOI 10.1186/s13395-015-0062-6
   Matsumoto M, 2017, NEUROMUSCULAR DISORD, V27, P1023, DOI 10.1016/j.nmd.2017.06.007
   MATSUO M, 1991, J CLIN INVEST, V87, P2127, DOI 10.1172/JCI115244
   Matsuo M, 2017, GENES-BASEL, V8, DOI 10.3390/genes8100251
   Mitra Mithun, 2015, Trends Cell Mol Biol, V10, P37
   Moizard MP, 2000, EUR J HUM GENET, V8, P552, DOI 10.1038/sj.ejhg.5200488
   Molina KM, 2013, CIRC-HEART FAIL, V6, P1214, DOI 10.1161/CIRCHEARTFAILURE.113.000125
   Monaco AP, 1988, GENOMICS, V2, P90, DOI 10.1016/0888-7543(88)90113-9
   Muntoni F, 2003, LANCET NEUROL, V2, P731, DOI 10.1016/S1474-4422(03)00585-4
   Nishida A, 2015, HUM GENET, V134, P993, DOI 10.1007/s00439-015-1581-2
   PILLERS DAM, 1993, NAT GENET, V4, P82, DOI 10.1038/ng0593-82
   Rani AQM, 2019, BIOCHEM BIOPHYS REP, V20, DOI 10.1016/j.bbrep.2019.100703
   Rani AQM, 2019, BIOCHEM BIOPH RES CO, V508, P640, DOI 10.1016/j.bbrc.2018.11.168
   Rau F, 2015, NAT COMMUN, V6, DOI 10.1038/ncomms8205
   Ricotti V, 2016, EUR J HUM GENET, V24, P562, DOI 10.1038/ejhg.2015.135
   SANYAL SK, 1982, CIRCULATION, V66, P853, DOI 10.1161/01.CIR.66.4.853
   Takami Y, 2008, PEDIATR NEUROL, V39, P399, DOI 10.1016/j.pediatrneurol.2008.08.006
   TINSLEY JM, 1993, HUM MOL GENET, V2, P521, DOI 10.1093/hmg/2.5.521
   Tran VK, 2005, J HUM GENET, V50, P425, DOI 10.1007/s10038-005-0272-6
   Wang RJ, 2019, CELL REP, V26, P2766, DOI 10.1016/j.celrep.2019.02.049
   WEISENFELD S, 1952, AM HEART J, V43, P170, DOI 10.1016/0002-8703(52)90209-3
   Yamamoto T, 2018, CIRC-GENOM PRECIS ME, V11, DOI 10.1161/CIRCGEN.117.001782
   Zhao JL, 2016, HUM MOL GENET, V25, P3647, DOI 10.1093/hmg/ddw210
NR 43
TC 4
Z9 4
U1 0
U2 2
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
SN 1661-6596
EI 1422-0067
J9 INT J MOL SCI
JI Int. J. Mol. Sci.
PD MAY
PY 2020
VL 21
IS 10
AR 3555
DI 10.3390/ijms21103555
PG 13
WC Biochemistry & Molecular Biology; Chemistry, Multidisciplinary
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Chemistry
GA LW7GO
UT WOS:000539312100151
PM 32443516
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Moïse, N
   Dingar, D
   Mamarbachi, AM
   Villeneuve, LR
   Farhat, N
   Gaestel, M
   Khairallah, M
   Allen, BG
AF Moise, Nadege
   Dingar, Dharmendra
   Mamarbachi, Aida M.
   Villeneuve, Louis R.
   Farhat, Nada
   Gaestel, Matthias
   Khairallah, Maya
   Allen, Bruce G.
TI Characterization of a novel MK3 splice variant from murine ventricular
   myocardium
SO CELLULAR SIGNALLING
LA English
DT Article
DE p38 MAPK; MK3; Post-transcriptional regulation; Alternative splicing
ID ACTIVATED PROTEIN-KINASE; P38 MAP KINASE; SUBSTRATE-SPECIFICITY;
   CELLULAR STRESSES; IN-VIVO; C-JUN; 3PK; IDENTIFICATION; TRANSCRIPTION;
   STIMULATION
AB p38 MAP kinase (MAPK) isoforms alpha, beta, and gamma, are expressed in the heart. p38 alpha appears pro-apoptotic whereas p38 beta is pro-hypertrophic. The mechanisms mediating these divergent effects are unknown; hence elucidating the downstream signaling of p38 should further our understanding. Downstream effectors include MAPK-activated protein kinase (MK)-3, which is expressed in many tissues including skeletal muscles and heart. We cloned full-length MK3 (MK3.1, 384 aa) and a novel splice variant (MK3.2, 266 aa) from murine heart. For MK3.2, skipping of exons 8 and 9 resulted in a frame-shift in translation of the first 85 base pairs of exon 10 followed by an in-frame stop codon. Of 3 putative phosphorylation sites for p38 MAPK, only Thr-203 remained functional in MK3.2. In addition, MK3.2 lacked nuclear localization and export signals. Quantitative real-time PCR confirmed the presence of these mRNA species in heart and skeletal muscle; however, the relative abundance of MK3.2 differed. Furthermore, whereas total MK3 mRNA was increased, the relative abundance of MK3.2 mRNA decreased in MK2(-/-) mice. lmmunoblotting revealed 2 bands of MK3 immunoreactivity in ventricular lysates. Ectopically expressed MK3.1 localized to the nucleus whereas MK3.2 was distributed throughout the cell; however, whereas MK3.1 translocated to the cytoplasm in response to osmotic stress, MK3.2 was degraded. The p38 alpha/beta inhibitor SB203580 prevented the degradation of MK3.2. Furthermore, replacing Thr-203 with alanine prevented the loss of MK3.2 following osmotic stress, as did pretreatment with the proteosome inhibitor MG132. In vitro, GST-MK3.1 was strongly phosphorylated by p38 alpha and p38 beta, but a poor substrate for p38 delta and p38 gamma. GST-MK3.2 was poorly phosphorylated by p38 alpha and p38 beta and not phosphorylated by p38 delta and p38 gamma. Hence, differential regulation of MKs may, in part, explain diverse downstream effects mediated by p38 signaling. (C) 2010 Elsevier Inc. All rights reserved.
C1 [Moise, Nadege; Dingar, Dharmendra; Mamarbachi, Aida M.; Villeneuve, Louis R.; Farhat, Nada; Khairallah, Maya; Allen, Bruce G.] Univ Montreal, Montreal Heart Inst, Montreal, PQ H3C 3J7, Canada.
   [Moise, Nadege; Dingar, Dharmendra; Khairallah, Maya; Allen, Bruce G.] Univ Montreal, Dept Biochem, Montreal, PQ H3C 3J7, Canada.
   [Allen, Bruce G.] Univ Montreal, Dept Med, Montreal, PQ H3C 3J7, Canada.
   [Gaestel, Matthias] Hannover Med Sch, Inst Biochem, D-30625 Hannover, Germany.
   [Allen, Bruce G.] McGill Univ, Dept Pharmacol & Therapeut, Montreal, PQ H3G 1Y6, Canada.
C3 Universite de Montreal; Universite de Montreal; Universite de Montreal;
   Hannover Medical School; McGill University
RP Allen, BG (corresponding author), Montreal Heart Inst, 5000 Belanger St, Montreal, PQ H1T 1C8, Canada.
EM bruce.g.allen@umontreal.ca
RI Gaestel, Matthias/A-6560-2013; Allen, Bruce/B-4693-2008
OI Gaestel, Matthias/0000-0002-4944-4652; Allen, Bruce/0000-0001-9000-9495
FU Canadian Institutes of Health Research [MOP-77791]; New Investigator of
   the Heart and Stroke Foundation of Canada; Fondation de la Recherche en
   Sante du Quebec (FRSQ)
FX Supported by grants from the Canadian Institutes of Health Research
   (MOP-77791). BGA was a New Investigator of the Heart and Stroke
   Foundation of Canada and a Senior Scholar of the Fondation de la
   Recherche en Sante du Quebec (FRSQ).
CR Angenstein F, 1998, P NATL ACAD SCI USA, V95, P15078, DOI 10.1073/pnas.95.25.15078
   Askari N, 2007, J BIOL CHEM, V282, P91, DOI 10.1074/jbc.M608012200
   Boivin B, 2003, J BIOL CHEM, V278, P29153, DOI 10.1074/jbc.M301738200
   Boivin B, 2006, CARDIOVASC RES, V71, P69, DOI 10.1016/j.cardiores.2006.03.015
   BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
   Chen Y, 2003, AM J PHYSIOL-HEART C, V285, pH2578, DOI 10.1152/ajpheart.00365.2003
   Chevalier D, 2000, PROTEIN EXPRES PURIF, V18, P229, DOI 10.1006/prep.1999.1183
   Clark JE, 2007, CARDIOVASC RES, V74, P466, DOI 10.1016/j.cardiores.2007.02.027
   Clerk A, 1998, J CELL BIOL, V142, P523, DOI 10.1083/jcb.142.2.523
   Clerk A, 1998, J BIOL CHEM, V273, P7228, DOI 10.1074/jbc.273.13.7228
   Clifton AD, 1996, FEBS LETT, V392, P209, DOI 10.1016/0014-5793(96)00816-2
   Court NW, 2002, J MOL CELL CARDIOL, V34, P413, DOI 10.1006/jmcc.2001.1523
   Cuenda A, 1997, EMBO J, V16, P295, DOI 10.1093/emboj/16.2.295
   Engel K, 1998, EMBO J, V17, P3363, DOI 10.1093/emboj/17.12.3363
   ENGEL K, 1993, FEBS LETT, V336, P143, DOI 10.1016/0014-5793(93)81628-D
   Fiedler B, 2006, J BIOL CHEM, V281, P32831, DOI 10.1074/jbc.M603416200
   Fischer TA, 2001, HYPERTENSION, V37, P1222, DOI 10.1161/01.HYP.37.5.1222
   Gaestel M, 2006, NAT REV MOL CELL BIO, V7, P120, DOI 10.1038/nrm1834
   Gang L, 2006, J BIOL CHEM, V281, P6087, DOI 10.1074/jbc.M507610200
   Goedert M, 1997, EMBO J, V16, P3563, DOI 10.1093/emboj/16.12.3563
   Gum RJ, 1999, BIOCHEM BIOPH RES CO, V266, P284, DOI 10.1006/bbrc.1999.1787
   Hawkins J, 2000, ARCH BIOCHEM BIOPHYS, V382, P310, DOI 10.1006/abbi.2000.2005
   Kotlyarov A, 1999, NAT CELL BIOL, V1, P94, DOI 10.1038/10061
   Kumar S, 1997, BIOCHEM BIOPH RES CO, V235, P533, DOI 10.1006/bbrc.1997.6849
   Kyriakis JM, 2001, PHYSIOL REV, V81, P807, DOI 10.1152/physrev.2001.81.2.807
   Landry J, 1995, BIOCHEM CELL BIOL, V73, P703, DOI 10.1139/o95-078
   LARSEN JK, 1995, GENE, V161, P305, DOI 10.1016/0378-1119(95)00290-M
   LEE JC, 1994, NATURE, V372, P739, DOI 10.1038/372739a0
   Li MX, 2005, CIRCULATION, V111, P2494, DOI 10.1161/01.CIR.0000165117.71483.0C
   Li ZJ, 1996, BIOCHEM BIOPH RES CO, V228, P334, DOI 10.1006/bbrc.1996.1662
   Liang FQ, 1999, J CLIN INVEST, V104, P1603, DOI 10.1172/JCI7362
   Liao P, 2002, CIRC RES, V90, P190, DOI 10.1161/hh0202.104220
   Liao P, 2001, P NATL ACAD SCI USA, V98, P12283, DOI 10.1073/pnas.211086598
   Ludwig S, 1996, MOL CELL BIOL, V16, P6687
   Lukas SM, 2004, BIOCHEMISTRY-US, V43, P9950, DOI 10.1021/bi049508v
   Maizels ET, 2001, MOL ENDOCRINOL, V15, P716, DOI 10.1210/me.15.5.716
   Mawji IA, 2004, J BIOL CHEM, V279, P8655, DOI 10.1074/jbc.M312190200
   McLaughlin MM, 1996, J BIOL CHEM, V271, P8488, DOI 10.1074/jbc.271.14.8488
   Neufeld B, 2000, J BIOL CHEM, V275, P20239, DOI 10.1074/jbc.C901040199
   Pramanik R, 2003, J BIOL CHEM, V278, P4831, DOI 10.1074/jbc.M207732200
   Ronkina N, 2007, MOL CELL BIOL, V27, P170, DOI 10.1128/MCB.01456-06
   Shi Y, 2003, MOL CELL BIOL, V23, P7732, DOI 10.1128/MCB.23.21.7732-7741.2003
   Sithanandam G, 1996, MOL CELL BIOL, V16, P868
   STOKOE D, 1993, BIOCHEM J, V296, P843, DOI 10.1042/bj2960843
   Tenhunen O, 2006, CIRC RES, V99, P485, DOI 10.1161/01.RES.0000238387.85144.92
   Tibbles LA, 1999, CELL MOL LIFE SCI, V55, P1230, DOI 10.1007/s000180050369
   Vahebi S, 2007, CIRC RES, V100, P408, DOI 10.1161/01.RES.0000258116.60404.ad
   Voncken JW, 2005, J BIOL CHEM, V280, P5178, DOI 10.1074/jbc.M407155200
   Wang YB, 1998, J BIOL CHEM, V273, P2161, DOI 10.1074/jbc.273.4.2161
   Welsh MJ, 1998, ANN NY ACAD SCI, V851, P28, DOI 10.1111/j.1749-6632.1998.tb08973.x
   Werz O, 2000, P NATL ACAD SCI USA, V97, P5261, DOI 10.1073/pnas.050588997
   Zakowski V, 2004, EXP CELL RES, V299, P101, DOI 10.1016/j.yexcr.2004.05.027
   Zhang JY, 2007, TRENDS PHARMACOL SCI, V28, P286, DOI 10.1016/j.tips.2007.04.008
   ZU YL, 1994, BIOCHEM BIOPH RES CO, V200, P1118, DOI 10.1006/bbrc.1994.1566
   ZU YL, 1995, J BIOL CHEM, V270, P202, DOI 10.1074/jbc.270.1.202
NR 55
TC 6
Z9 8
U1 0
U2 1
PU ELSEVIER SCIENCE INC
PI NEW YORK
PA STE 800, 230 PARK AVE, NEW YORK, NY 10169 USA
SN 0898-6568
EI 1873-3913
J9 CELL SIGNAL
JI Cell. Signal.
PD OCT
PY 2010
VL 22
IS 10
BP 1502
EP 1512
DI 10.1016/j.cellsig.2010.05.019
PG 11
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA 634ZK
UT WOS:000280625000013
PM 20570725
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Bader, HL
   Wang, LW
   Ho, JC
   Tran, T
   Holden, P
   Fitzgerald, J
   Atit, RP
   Reinhardt, DP
   Apte, SS
AF Bader, Hannah L.
   Wang, Lauren W.
   Ho, Jason C.
   Thu Tran
   Holden, Paul
   Fitzgerald, Jamie
   Atit, Radhika P.
   Reinhardt, Dieter P.
   Apte, Suneel S.
TI A disintegrin-like and metalloprotease domain containing thrombospondin
   type 1 motif-like 5 (ADAMTSL5) is a novel fibrillin-1-, fibrillin-2-,
   and heparin-binding member of the ADAMTS superfamily containing a
   netrin-like module
SO MATRIX BIOLOGY
LA English
DT Article
DE ADAMTS; ADAMTS-like; Netrin-like module; Fibrillin microfibril; Heparin;
   Alternative splicing
ID C-PROTEINASE ENHANCER-1; EXTRACELLULAR-MATRIX; CAENORHABDITIS-ELEGANS;
   SECRETED GLYCOPROTEIN; HOMOLOGY; MICROFIBRILS; EXPRESSION; DEPOSITION;
   MUTATIONS; PROMOTES
AB ADAMTS-like proteins are related to ADAMTS metalloproteases by their similarity to ADAMTS ancillary domains. Here, we have characterized ADAMTSL5, a novel member of the superfamily with a unique modular organization that includes a single C-terminal netrin-like (NTR) module. Alternative splicing of ADAMTSL5 at its 5' end generates two transcripts that encode different signal peptides, but the same mature protein. These transcripts differ in their translational efficiency. Recombinant ADAMTSL5 is a secreted, N-glycosylated 60 kDa glycoprotein located in the subcellular matrix, on the cell-surface, and in the medium of transfected cells. RT-PCR and western blot analysis of adult mouse tissues showed broad expression. Western blot analysis suggested proteolytic release of the NTR module in transfected cells as well as in some mouse tissues. Immunostaining during mouse organogenesis identified ADAMTSL5 in musculoskeletal tissues such as skeletal muscle, cartilage and bone, as well as in many epithelia. Affinity-chromatography demonstrated heparin-binding of ADAMTSL5 through its NTR-module. Recombinant ADAMTSL5 bound to both fibrillin-1 and fibrillin-2, and co-localized with fibrillin microfibrils in the extracellular matrix of cultured fibroblasts, but without discernible effect on microfibril assembly. ADAMTSL5 is the first family member shown to bind both fibrillin-1 and fibrillin-2. Like other ADAMTS proteins implicated in microfibril biology through identification of human and animal mutations, ADAMTSL5 could have a role in modulating microfibril functions. (c) 2012 Elsevier B.V. All rights reserved.
C1 [Bader, Hannah L.; Wang, Lauren W.; Ho, Jason C.; Apte, Suneel S.] Cleveland Clin, Lerner Res Inst, Dept Biomed Engn, Cleveland, OH 44195 USA.
   [Thu Tran; Atit, Radhika P.] Case Western Reserve Univ, Dept Biol, Cleveland, OH 44106 USA.
   [Holden, Paul; Fitzgerald, Jamie] Oregon Hlth & Sci Univ, Dept Mol & Med Genet, Portland, OR 97239 USA.
   [Fitzgerald, Jamie] Oregon Hlth & Sci Univ, Dept Orthopaed & Rehabil, Portland, OR 97239 USA.
   [Reinhardt, Dieter P.] McGill Univ, Dept Anat & Cell Biol, Montreal, PQ H3A 0C7, Canada.
   [Reinhardt, Dieter P.] McGill Univ, Fac Dent, Montreal, PQ H3A 0C7, Canada.
C3 Cleveland Clinic Foundation; University System of Ohio; Case Western
   Reserve University; Oregon Health & Science University; Oregon Health &
   Science University; McGill University; McGill University
RP Apte, SS (corresponding author), Cleveland Clin, Lerner Res Inst, Dept Biomed Engn ND20, 9500 Euclid Ave, Cleveland, OH 44195 USA.
EM aptes@ccf.org
RI ; Reinhardt, Dieter/A-3102-2008
OI Apte, Suneel/0000-0001-8441-1226; Reinhardt, Dieter/0000-0001-6535-9872;
   Ho, Jason/0000-0003-2096-2752
FU National Institutes of Health [AR53890, EY021151, R01AR055957,
   R01DE01870]; post-doctoral fellowship from the National Institutes of
   Health [T32HL007914-08]
FX This work was supported by the National Institutes of Health awards
   AR53890 and EY021151 (to S.S.A.), R01AR055957 (to J.F.) and R01DE01870
   (to R.A.). HB was supported by a post-doctoral fellowship from the
   National Institutes of Health T32HL007914-08 (Training Program in
   Vascular Biology and Pathology, Principal Investigator: Edward Plow).
CR Ahram D, 2009, AM J HUM GENET, V84, P274, DOI 10.1016/j.ajhg.2009.01.007
   [Anonymous], J BIOL CHEM
   Apte SS, 2009, J BIOL CHEM, V284, P31493, DOI 10.1074/jbc.R109.052340
   Bader HL, 2010, PLOS ONE, V5, DOI 10.1371/journal.pone.0012817
   Bányai L, 1999, PROTEIN SCI, V8, P1636, DOI 10.1110/ps.8.8.1636
   Bekhouche M, 2010, J BIOL CHEM, V285, P15950, DOI 10.1074/jbc.M109.086447
   Buchner DA, 2003, GENE, V307, P23, DOI 10.1016/S0378-1119(03)00423-2
   Chong JM, 2002, J BIOL CHEM, V277, P5134, DOI 10.1074/jbc.M108533200
   Gabriel LAR, 2012, INVEST OPHTH VIS SCI, V53, P461, DOI 10.1167/iovs.10-5955
   Geisbrecht BV, 2003, J BIOL CHEM, V278, P32561, DOI 10.1074/jbc.M302943200
   Hall NG, 2003, MATRIX BIOL, V22, P501, DOI 10.1016/S0945-053X(03)00075-1
   Holmes G, 2001, DEV DYNAM, V222, P301, DOI 10.1002/dvdy.1182
   Hubmacher D, 2011, CELL MOL LIFE SCI, V68, P3137, DOI 10.1007/s00018-011-0780-9
   Jensen SA, 2001, J BIOL CHEM, V276, P39661, DOI 10.1074/jbc.M104533200
   Kappler J, 2000, BIOCHEM BIOPH RES CO, V271, P287, DOI 10.1006/bbrc.2000.2583
   Kinsey R, 2008, J CELL SCI, V121, P2696, DOI 10.1242/jcs.029819
   Koch M, 2000, J CELL BIOL, V151, P221, DOI 10.1083/jcb.151.2.221
   Koo BH, 2007, MATRIX BIOL, V26, P431, DOI 10.1016/j.matbio.2007.03.003
   Kramerova IA, 2000, DEVELOPMENT, V127, P5475
   Kutz WE, 2011, J BIOL CHEM, V286, P17156, DOI 10.1074/jbc.M111.231571
   Larrieu-Lahargue F, 2010, BLOOD, V115, P5418, DOI 10.1182/blood-2009-11-252338
   Le Goff C, 2008, NAT GENET, V40, P1119, DOI 10.1038/ng.199
   Le Goff C, 2011, AM J HUM GENET, V89, P7, DOI 10.1016/j.ajhg.2011.05.012
   Lin GQ, 2002, J BIOL CHEM, V277, P50795, DOI 10.1074/jbc.M210611200
   Piha-Gossack A, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0033560
   Ramirez F, 2010, CELL TISSUE RES, V339, P71, DOI 10.1007/s00441-009-0822-x
   Ramirez F, 2009, CURR OPIN CELL BIOL, V21, P616, DOI 10.1016/j.ceb.2009.05.005
   ROITSCH T, 1989, EUR J BIOCHEM, V181, P525, DOI 10.1111/j.1432-1033.1989.tb14755.x
   Sabatier L, 2009, MOL BIOL CELL, V20, P846, DOI 10.1091/mbc.E08-08-0830
   Seetharaman A, 2011, DEV CELL, V21, P669, DOI 10.1016/j.devcel.2011.07.020
   Sengle G, 2012, PLOS GENET, V8, DOI 10.1371/journal.pgen.1002425
   Somerville RPT, 2003, J BIOL CHEM, V278, P9503, DOI 10.1074/jbc.M211009200
   Tsutsui K, 2010, J BIOL CHEM, V285, P4870, DOI 10.1074/jbc.M109.076919
   Wang LW, 2007, J BIOL CHEM, V282, P17024, DOI 10.1074/jbc.M701065200
   Wang LW, 2009, J BIOL CHEM, V284, P30004, DOI 10.1074/jbc.M109.038059
   Weiss T, 2010, J BIOL CHEM, V285, P33867, DOI 10.1074/jbc.M110.141366
   Zheng X, 2001, J BIOL CHEM, V13, P13
NR 37
TC 43
Z9 51
U1 0
U2 13
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 0945-053X
EI 1569-1802
J9 MATRIX BIOL
JI Matrix Biol.
PD SEP-OCT
PY 2012
VL 31
IS 7-8
BP 398
EP 411
DI 10.1016/j.matbio.2012.09.003
PG 14
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA 066MQ
UT WOS:000313225300005
PM 23010571
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Sorimachi, H
   Freiburg, A
   Kolmerer, B
   Ishiura, S
   Stier, G
   Gregorio, CC
   Labeit, D
   Linke, WA
   Suzuki, K
   Labeit, S
AF Sorimachi, H
   Freiburg, A
   Kolmerer, B
   Ishiura, S
   Stier, G
   Gregorio, CC
   Labeit, D
   Linke, WA
   Suzuki, K
   Labeit, S
TI Tissue-specific expression and alpha-actinin binding properties of the
   Z-disc titin: Implications for the nature of vertebrate Z-discs
SO JOURNAL OF MOLECULAR BIOLOGY
LA English
DT Article
DE titin (connectin); alpha-actinin; Z-discs; striated and smooth muscles;
   alternative splicing
ID SKELETAL-MUSCLE; Z-BAND; PROTEIN; LINE; MYOFIBRILS; CONNECTIN; SEQUENCE;
   NEBULIN; SYSTEM; DOMAIN
AB Titins are giant filamentous proteins which connect Z-discs and M-lines in the sarcomeres of vertebrate striated muscles. Comparison of the N-terminal region of titin (Z-disc region) from different skeletal and cardiac muscles reveals a 900-residue segment which is expressed in different length variants, dependent on tissue type. When searching for ligands of this differentially expressed domain by a yeast-two hybrid approach, we detected binding to alpha-actinin. The isolated alpha-actinin cDNAs were derived from the C-terminal region of the alpha-actinin isoform (alpha actinin-2) encoded by the ACTN2 gene. Therefore, the two antiparallel subunits of an alpha-actinin-2 homodimer will attach to actin at their respective C termini, whereas they will bind to the Z-disc titin at their N termini. This may thus explain how alpha-actinins can cross-link antiparallel titin and thin filaments from opposing sarcomeres. The alpha-actinin-2 binding site of the Z-disc titin is located within a sequence of 45-residue repeats, referred to as Z-repeat region. Both the N-terminal and C-terminal Z-repeats have alpha-actinin binding properties and are expressed in all striated muscles. By contrast, the more central Z-repeats are expressed in slow and fast skeletal muscles, as well as embryonic and adult cardiac muscles, in different copy numbers. Such alternative splicing of the Z-disc titin appears to be important for the tissue and fibre type diversity of the Z-disc lattice. (C) 1997 Academic Press Limited.
C1 EUROPEAN MOL BIOL LAB,D-69012 HEIDELBERG,GERMANY.
   UNIV TOKYO,INST MOL & CELLULAR BIOSCI,BUNKYO KU,TOKYO 113,JAPAN.
   UNIV ARIZONA,DEPT CELL BIOL & ANAT,TUCSON,AZ 85724.
   UNIV KLINIKUM MANNHEIM,DEPT GYNAECOL,D-68167 MANNHEIM,GERMANY.
   UNIV HEIDELBERG,D-69120 HEIDELBERG,GERMANY.
C3 European Molecular Biology Laboratory (EMBL); University of Tokyo;
   University of Arizona; Ruprecht Karls University Heidelberg; Ruprecht
   Karls University Heidelberg
RI Linke, Wolfgang/IXD-9988-2023; Sorimachi, Hiroyuki/C-6448-2009
OI Linke, Wolfgang/0000-0003-0801-3773; Sorimachi,
   Hiroyuki/0000-0001-9509-6727
CR BEGGS AH, 1992, J BIOL CHEM, V267, P9281
   BENNETT JP, 1984, BIOCHEMISTRY-US, V23, P5081, DOI 10.1021/bi00316a039
   CARPEN O, 1992, J CELL BIOL, V118, P1223, DOI 10.1083/jcb.118.5.1223
   CHURCH GM, 1984, P NATL ACAD SCI-BIOL, V81, P1991, DOI 10.1073/pnas.81.7.1991
   DEVEREUX J, 1984, NUCLEIC ACIDS RES, V12, P387, DOI 10.1093/nar/12.1Part1.387
   FEINBERG AP, 1983, ANAL BIOCHEM, V13, P6
   FIELDS S, 1989, NATURE, V340, P245, DOI 10.1038/340245a0
   FURST DO, 1988, J CELL BIOL, V106, P1563, DOI 10.1083/jcb.106.5.1563
   Gautel M, 1996, J CELL SCI, V109, P2747
   GOLDSTEIN MA, 1986, J MUSCLE RES CELL M, V7, P527, DOI 10.1007/BF01753569
   GOLDSTEIN MA, 1989, AM J PHYSIOL, V256, pH552, DOI 10.1152/ajpheart.1989.256.2.H552
   GOLL DE, 1991, J BIOL CHEM, V266, P8501
   HAMMONDS RG, 1987, CELL, V51, P1, DOI 10.1016/0092-8674(87)90002-X
   LABEIT S, 1992, EMBO J, V11, P1711, DOI 10.1002/j.1460-2075.1992.tb05222.x
   LABEIT S, 1995, SCIENCE, V270, P293, DOI 10.1126/science.270.5234.293
   Labeit S, 1997, CIRC RES, V80, P290, DOI 10.1161/01.RES.80.2.290
   LEVINE BA, 1990, FEBS LETT, V263, P159, DOI 10.1016/0014-5793(90)80728-2
   MACDONALD RJ, 1987, METHOD ENZYMOL, V152, P219
   MARUYAMA K, 1994, BIOPHYS CHEM, V50, P73, DOI 10.1016/0301-4622(94)85021-6
   NAVE R, 1990, FEBS LETT, V269, P163, DOI 10.1016/0014-5793(90)81144-D
   Ohtsuka H, 1997, FEBS LETT, V401, P65, DOI 10.1016/S0014-5793(96)01432-9
   OHTSUKA H, 1997, IN PRESS BIOCH BIOPH
   PARR T, 1992, EUR J BIOCHEM, V210, P801, DOI 10.1111/j.1432-1033.1992.tb17483.x
   SAIKI RK, 1985, SCIENCE, V230, P1350, DOI 10.1126/science.2999980
   Schroeter JP, 1996, J CELL BIOL, V133, P571, DOI 10.1083/jcb.133.3.571
   SCHULTHEISS T, 1992, P NATL ACAD SCI USA, V89, P9282, DOI 10.1073/pnas.89.19.9282
   SCHULTHEISS T, 1990, J CELL BIOL, V110, P1159, DOI 10.1083/jcb.110.4.1159
   Sorimachi H, 1995, J BIOL CHEM, V270, P31158, DOI 10.1074/jbc.270.52.31158
   SOTERIOU A, 1993, J CELL SCI, V104, P119
   Squire JM, 1997, CURR OPIN STRUC BIOL, V7, P247, DOI 10.1016/S0959-440X(97)80033-4
   Squire JM., 1981, STRUCTURAL BASIS MUS
   STROMER MH, 1972, J MOL BIOL, V67, P489, DOI 10.1016/0022-2836(72)90465-2
   SUZUKI J, 1994, J BIOCHEM-TOKYO, V116, P406, DOI 10.1093/oxfordjournals.jbchem.a124539
   TOKUYASU KT, 1987, J CELL BIOL, V105, P2795, DOI 10.1083/jcb.105.6.2795
   TRINICK J, 1994, TRENDS BIOCHEM SCI, V19, P405, DOI 10.1016/0968-0004(94)90088-4
   Turnacioglu KK, 1996, CELL MOTIL CYTOSKEL, V34, P108, DOI 10.1002/(SICI)1097-0169(1996)34:2<108::AID-CM3>3.3.CO;2-N
   VIGOREAUX JO, 1994, J MUSCLE RES CELL M, V15, P237
   Yajima H, 1996, BIOCHEM BIOPH RES CO, V223, P160, DOI 10.1006/bbrc.1996.0862
   YAMAGUCHI M, 1985, J MOL BIOL, V184, P621, DOI 10.1016/0022-2836(85)90308-0
NR 39
TC 170
Z9 189
U1 0
U2 12
PU ACADEMIC PRESS LTD
PI LONDON
PA 24-28 OVAL RD, LONDON, ENGLAND NW1 7DX
SN 0022-2836
J9 J MOL BIOL
JI J. Mol. Biol.
PD AUG 1
PY 1997
VL 270
IS 5
BP 688
EP 695
DI 10.1006/jmbi.1997.1145
PG 8
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA XN949
UT WOS:A1997XN94900006
PM 9245597
DA 2025-04-10
ER

PT J
AU Goodarzi, H
   Najafabadi, HS
   Oikonomou, P
   Greco, TM
   Fish, L
   Salavati, R
   Cristea, IM
   Tavazoie, S
AF Goodarzi, Hani
   Najafabadi, Hamed S.
   Oikonomou, Panos
   Greco, Todd M.
   Fish, Lisa
   Salavati, Reza
   Cristea, Ileana M.
   Tavazoie, Saeed
TI Systematic discovery of structural elements governing stability of
   mammalian messenger RNAs
SO NATURE
LA English
DT Article
ID GENE-EXPRESSION; SECONDARY STRUCTURE; PREDICTION; MOTIFS; CHIP
AB Decoding post-transcriptional regulatory programs in RNA is a critical step towards the larger goal of developing predictive dynamical models of cellular behaviour. Despite recent efforts(1-3), the vast landscape of RNA regulatory elements remains largely uncharacterized. A long-standing obstacle is the contribution of local RNA secondary structure to the definition of interaction partners in a variety of regulatory contexts, including-but not limited to-transcript stability(3), alternative splicing(4) and localization(3). There are many documented instances where the presence of a structural regulatory element dictates alternative splicing patterns (for example, human cardiac troponin T) or affects other aspects of RNA biology(5). Thus, a full characterization of post-transcriptional regulatory programs requires capturing information provided by both local secondary structures and the underlying sequence(3,6). Here we present a computational framework based on context-free grammars(3,7) and mutual information(2) that systematically explores the immense space of small structural elements and reveals motifs that are significantly informative of genome-wide measurements of RNA behaviour. By applying this framework to genome-wide human mRNA stability data, we reveal eight highly significant elements with substantial structural information, for the strongest of which we show a major role in global mRNA regulation. Through biochemistry, mass spectrometry and in vivo binding studies, we identified human HNRPA2B1 (heterogeneous nuclear ribonucleoprotein A2/B1, also known as HNRNPA2B1) as the key regulator that binds this element and stabilizes a large number of its target genes. We created a global post-transcriptional regulatory map based on the identity of the discovered linear and structural cis-regulatory elements, their regulatory interactions and their target pathways. This approach could also be used to reveal the structural elements that modulate other aspects of RNA behaviour.
C1 [Goodarzi, Hani; Oikonomou, Panos; Tavazoie, Saeed] Princeton Univ, Lewis Sigler Inst Integrat Genom, Princeton, NJ 08540 USA.
   [Goodarzi, Hani; Oikonomou, Panos; Greco, Todd M.; Cristea, Ileana M.; Tavazoie, Saeed] Princeton Univ, Dept Mol Biol, Princeton, NJ 08540 USA.
   [Najafabadi, Hamed S.; Salavati, Reza] McGill Univ, Inst Parasitol, Montreal, PQ H3G 1Y6, Canada.
   [Najafabadi, Hamed S.; Salavati, Reza] McGill Univ, McGill Ctr Bioinformat, Montreal, PQ H3G 1Y6, Canada.
   [Fish, Lisa] Rockefeller Univ, Lab Syst Canc Biol, New York, NY 10065 USA.
   [Salavati, Reza] McGill Univ, Dept Biochem, Montreal, PQ H3G 1Y6, Canada.
C3 Princeton University; Princeton University; McGill University; McGill
   University; Rockefeller University; McGill University
RP Tavazoie, S (corresponding author), Columbia Univ, Dept Biochem & Mol Biophys, 630 W 168th St, New York, NY 10032 USA.
EM st2744@columbia.edu
RI ; Greco, Todd/E-8279-2010; Oikonomou, Panos/J-5106-2014
OI Goodarzi, Hani/0000-0002-9648-8949; Najafabadi,
   Hamed/0000-0003-2735-4231; Greco, Todd/0000-0002-5845-713X; Oikonomou,
   Panos/0000-0001-7387-0312; Fish, Lisa/0000-0001-9184-0512
FU Ruth L. Kirschstein National Research Service Award [T32-GM066699];
   NHGRI [2R01HG003219]; NIH
FX We thank the members of the Tavazoie laboratory for comments on the
   project and manuscript. We are also grateful to N. Pencheva, B. Tsui, S.
   Tavazoie and L. Dolken for their intellectual and technical
   contributions. L.F. was supported by a Ruth L. Kirschstein National
   Research Service Award (T32-GM066699). S.T. was supported by grants from
   NHGRI (2R01HG003219) and the NIH Director's Pioneer Award.
CR Barash Y, 2010, NATURE, V465, P53, DOI 10.1038/nature09000
   Beer MA, 2004, CELL, V117, P185, DOI 10.1016/S0092-8674(04)00304-6
   BIAMONTI G, 1994, NUCLEIC ACIDS RES, V22, P1996, DOI 10.1093/nar/22.11.1996
   Chi SW, 2009, NATURE, V460, P479, DOI 10.1038/nature08170
   Cutroneo KR, 2006, CRIT REV EUKAR GENE, V16, P23
   Dölken L, 2008, RNA, V14, P1959, DOI 10.1261/rna.1136108
   Elemento O, 2007, MOL CELL, V28, P337, DOI 10.1016/j.molcel.2007.09.027
   Giannopoulou EG, 2011, BMC BIOINFORMATICS, V12, DOI 10.1186/1471-2105-12-277
   Goodarzi H, 2009, MOL CELL, V36, P900, DOI 10.1016/j.molcel.2009.11.016
   Greco TM, 2011, MOL CELL PROTEOMICS, V10, DOI 10.1074/mcp.M110.004317
   Hofacker IL, 2002, J MOL BIOL, V319, P1059, DOI 10.1016/S0022-2836(02)00308-X
   Jensen Kirk B., 2008, V488, P85, DOI 10.1007/978-1-60327-475-3_6
   Keene JD, 2006, NAT PROTOC, V1, P302, DOI 10.1038/nprot.2006.47
   Kertesz M, 2010, NATURE, V467, P103, DOI 10.1038/nature09322
   Licatalosi DD, 2008, NATURE, V456, P464, DOI 10.1038/nature07488
   Michlewski G, 2010, NAT STRUCT MOL BIOL, V17, P1011, DOI 10.1038/nsmb.1874
   Pavesi G, 2004, NUCLEIC ACIDS RES, V32, P3258, DOI 10.1093/nar/gkh650
   Rabani M, 2008, P NATL ACAD SCI USA, V105, P14885, DOI 10.1073/pnas.0803169105
   Ross DT, 2000, NAT GENET, V24, P227, DOI 10.1038/73432
   Schwanhäusser B, 2011, NATURE, V473, P337, DOI 10.1038/nature10098
   Searls DB, 2002, NATURE, V420, P211, DOI 10.1038/nature01255
   Wan Y, 2011, NAT REV GENET, V12, P641, DOI 10.1038/nrg3049
   Wilusz CJ, 2001, NAT REV MOL CELL BIO, V2, P237, DOI 10.1038/35067025
   Windbichler N, 2006, NAT PROTOC, V1, P638, DOI 10.1038/nprot.2006.95
   Wisniewski JR, 2009, NAT METHODS, V6, P359, DOI [10.1038/nmeth.1322, 10.1038/NMETH.1322]
   Yang Y, 2011, NAT STRUCT MOL BIOL, V18, P159, DOI 10.1038/nsmb.1959
NR 26
TC 127
Z9 166
U1 0
U2 41
PU NATURE PUBLISHING GROUP
PI LONDON
PA MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
SN 0028-0836
EI 1476-4687
J9 NATURE
JI Nature
PD MAY 10
PY 2012
VL 485
IS 7397
BP 264
EP U160
DI 10.1038/nature11013
PG 7
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA 939HJ
UT WOS:000303799800047
PM 22495308
OA Green Accepted, Green Submitted
DA 2025-04-10
ER

PT J
AU Huuskonen, J
   Abedin, M
   Vishnu, M
   Pullinger, CR
   Baranzini, SE
   Kane, JP
   Fielding, PE
   Fielding, CJ
AF Huuskonen, J
   Abedin, M
   Vishnu, M
   Pullinger, CR
   Baranzini, SE
   Kane, JP
   Fielding, PE
   Fielding, CJ
TI Dynamic regulation of alternative ATP-binding cassette transporter A1
   transcripts
SO BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
LA English
DT Article
DE ABC transporters; HDL; lipoprotein metabolism; cholesterol;
   transcription; alternative splicing
ID HIGH-DENSITY-LIPOPROTEIN; LIVER-X-RECEPTOR; HUMAN ABCA1 GENE;
   TANGIER-DISEASE; CHOLESTEROL; PROMOTER; APOLIPOPROTEIN; EFFLUX; MICE;
   EXPRESSION
AB The ATP-binding cassette transporter A1 (ABCA1) gene, a major regulator of high-density lipoprotein (HDL) metabolism, utilizes several transcriptional start sites. The pattern of transcripts among tissues and cells differed significantly. The longest (class 1) transcripts were abundant in adult brain and fetal tissues. Class 2 transcripts predominated in most other tissues. The shortest (class 3) transcripts were present mainly in adult liver and lung. To study the biochemical significance of changes in transcript distribution, two cell models were compared. In primary human fibroblasts, upregulation of mRNA levels by oxysterols and retinoic acid increased the relative proportion of class 2 transcript compared to class 1. Phorbol ester stimulated human macrophage-derived THP-1 cells increased the abundance of class I transcripts relative to class 2. In both cell lines class 3 transcript levels were minimal and unchanged. It is shown here for the first time that the regulation of ABCA1 mRNA levels exploits the use of alternative transcription start sites. (C) 2003 Elsevier Science (USA). All rights reserved.
C1 Univ Calif San Francisco, Cardiovasc Res Inst, San Francisco, CA 94143 USA.
   Univ Calif San Francisco, Dept Neurol, San Francisco, CA 94143 USA.
   Univ Calif San Francisco, Dept Med, San Francisco, CA 94143 USA.
   Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USA.
   Univ Calif San Francisco, Dept Physiol, San Francisco, CA 94143 USA.
C3 University of California System; University of California San Francisco;
   University of California System; University of California San Francisco;
   University of California System; University of California San Francisco;
   University of California System; University of California San Francisco;
   University of California System; University of California San Francisco
RP Univ Calif San Francisco, Cardiovasc Res Inst, San Francisco, CA 94143 USA.
EM jhuu6676@itsa.ucsf.edu
RI Baranzini, Sergio/A-9422-2013; Pearson, John/AAT-4211-2020
OI Baranzini, Sergio/0000-0003-0067-194X
FU NHLBI NIH HHS [HL31210, HL 67294, HL57976] Funding Source: Medline;
   NIGMS NIH HHS [GM61390] Funding Source: Medline
CR Arakawa R, 2000, J LIPID RES, V41, P1952
   Ayoubi TAY, 1996, FASEB J, V10, P453, DOI 10.1096/fasebj.10.4.8647344
   Baranzini SE, 2000, J IMMUNOL, V165, P6576, DOI 10.4049/jimmunol.165.11.6576
   Bellincampi L, 2001, BIOCHEM BIOPH RES CO, V283, P590, DOI 10.1006/bbrc.2001.4823
   Bodzioch M, 1999, NAT GENET, V22, P347, DOI 10.1038/11914
   Brooks-Wilson A, 1999, NAT GENET, V22, P336, DOI 10.1038/11905
   Burgess JW, 2002, J BIOL CHEM, V277, P31318, DOI 10.1074/jbc.M204200200
   Cavelier LB, 2001, J BIOL CHEM, V276, P18046, DOI 10.1074/jbc.M100565200
   CHIMINI G, 2003, ABC PROTEINS BACTERI, P479
   Christiansen-Weber TA, 2000, AM J PATHOL, V157, P1017, DOI 10.1016/S0002-9440(10)64614-7
   Costet P, 2000, J BIOL CHEM, V275, P28240
   Dean M, 2001, J LIPID RES, V42, P1007
   Fielding PE, 2000, BIOCHEMISTRY-US, V39, P14113, DOI 10.1021/bi0004192
   Fu X, 2001, J BIOL CHEM, V276, P38378, DOI 10.1074/jbc.M105805200
   Kielar D, 2001, CLIN CHEM, V47, P2089
   Langmann T, 1999, BIOCHEM BIOPH RES CO, V257, P29, DOI 10.1006/bbrc.1999.0406
   Lawn RM, 2001, ARTERIOSCL THROM VAS, V21, P378, DOI 10.1161/01.ATV.21.3.378
   Lawn RM, 1999, J CLIN INVEST, V104, pR25, DOI 10.1172/JCI8119
   LUCIANI MF, 1994, GENOMICS, V21, P150, DOI 10.1006/geno.1994.1237
   McNeish J, 2000, P NATL ACAD SCI USA, V97, P4245, DOI 10.1073/pnas.97.8.4245
   Orsó E, 2000, NAT GENET, V24, P192, DOI 10.1038/72869
   Pecci A, 2001, J BIOL CHEM, V276, P21062, DOI 10.1074/jbc.M008665200
   Pullinger CR, 2000, BIOCHEM BIOPH RES CO, V271, P451, DOI 10.1006/bbrc.2000.2652
   RAJAGOPALAN S, 1993, P NATL ACAD SCI USA, V90, P6179, DOI 10.1073/pnas.90.13.6179
   Rust S, 1999, NAT GENET, V22, P352, DOI 10.1038/11921
   Santamarina-Fojo S, 2000, P NATL ACAD SCI USA, V97, P7987, DOI 10.1073/pnas.97.14.7987
   Schwartz K, 2000, BIOCHEM BIOPH RES CO, V274, P794, DOI 10.1006/bbrc.2000.3243
   Schwende H, 1996, J LEUKOCYTE BIOL, V59, P555, DOI 10.1002/jlb.59.4.555
   Singaraja RR, 2001, J BIOL CHEM, V276, P33969, DOI 10.1074/jbc.M102503200
   Zhang JL, 1997, J MOL BIOL, V274, P338, DOI 10.1006/jmbi.1997.1392
NR 30
TC 12
Z9 12
U1 0
U2 1
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0006-291X
EI 1090-2104
J9 BIOCHEM BIOPH RES CO
JI Biochem. Biophys. Res. Commun.
PD JUN 27
PY 2003
VL 306
IS 2
BP 463
EP 468
DI 10.1016/S0006-291X(03)00992-6
PG 6
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA 693TQ
UT WOS:000183734800022
PM 12804586
DA 2025-04-10
ER

PT J
AU Ji, Y
   Moon, I
   Zlatkovic, J
   Salavaggione, OE
   Thomae, BA
   Eckloff, BW
   Wieben, ED
   Schaid, DJ
   Weinshilboum, RM
AF Ji, Yuan
   Moon, Irene
   Zlatkovic, Jelena
   Salavaggione, Oreste E.
   Thomae, Bianca A.
   Eckloff, Bruce W.
   Wieben, Eric D.
   Schaid, Daniel J.
   Weinshilboum, Richard M.
TI Human hydroxysteriod sulfotransferase SULT2B1 pharmacogenomics: Gene
   sequence variation and functional genomics
SO JOURNAL OF PHARMACOLOGY AND EXPERIMENTAL THERAPEUTICS
LA English
DT Article
ID S-METHYLTRANSFERASE PHARMACOGENETICS; HUMAN CYTOSOLIC SULFOTRANSFERASES;
   DEHYDROEPIANDROSTERONE SULFOTRANSFERASE; CHOLESTEROL SULFOTRANSFERASE;
   SUBCELLULAR-LOCALIZATION; MOLECULAR-CLONING; TISSUE EXPRESSION; DNA
   POLYMORPHISM; ASSOCIATION; IDENTIFICATION
AB The human hydroxysteroid sulfotransferase (SULT) 2B1 gene is a member of the cytosolic SULT gene superfamily. The two SULT2B1 isoforms, SULT2B1a and SULT2B1b, are encoded by a single gene as a result of alternative transcription initiation and alternative splicing. SULT2B1b catalyzes the sulfonation of 3 beta- hydroxysteroid hormones and cholesterol, whereas SULT2B1a preferentially catalyzes pregnenolone sulfonation. We used a genotype-to-phenotype approach to identify and characterize common sequence variation in SULT2B1. Specifically, we resequenced all exons, splice junctions, and similar to 2.5 kb of the 5'- flanking regions (FRs) for each isoform using 60 DNA samples each from African-American and Caucasian-American subjects. We observed 100 polymorphisms, including four nonsynonymous coding single nucleotide polymorphisms and one 6-base pair deletion-all within the "shared" region of the open reading frame. Functional genomic studies of the wild type (WT) and five variant allozymes for each isoform performed with a mammalian expression system showed that variant allozyme activities ranged from 64 to 88% of WT for SULT2B1a and from 76 to 98% for SULT2B1b. Relative levels of immunoreactive protein were similar to those for enzyme activity. Luciferase reporter gene constructs for 2.5kb of the SULT2B1b 5'-FR displayed a cell line-dependent pattern of variation in activity. Finally, deletion of the proline-rich SULT2B1 carboxyl terminus resulted in intracellular protein aggregate formation and accelerated degradation of the truncated protein. These studies resulted in the identification of common SULT2B1 gene sequence variation, as well as insight into the effects of that variation on the function of this important steroid-metabolizing enzyme.
C1 Mayo Clin & Mayo Fdn, Mayo Clin, Coll Med, Dept Mol Pharmacol & Expt,Div Clin Pharmacol, Rochester, MN 55905 USA.
   Mayo Clin & Mayo Fdn, Mayo Clin, Coll Med, Dept Biochem & Mol Biol,Div Clin Pharmacol, Rochester, MN 55905 USA.
   Mayo Clin & Mayo Fdn, Mayo Clin, Coll Med, Dept Hlth Sci Res,Div Clin Pharmacol, Rochester, MN USA.
C3 Mayo Clinic; Mayo Clinic; Mayo Clinic
RP Weinshilboum, RM (corresponding author), Mayo Clin & Mayo Fdn, Mayo Clin, Coll Med, Dept Mol Pharmacol & Expt,Div Clin Pharmacol, 200 1st St SW, Rochester, MN 55905 USA.
EM weinshilboum.richard@mayo.edu
FU NCHHSTP CDC HHS [PS205195] Funding Source: Medline; NIGMS NIH HHS [R01
   GM28157, U01 GM61388, R01 GM35720] Funding Source: Medline
CR Adjei AA, 2003, BRIT J PHARMACOL, V139, P1373, DOI 10.1038/sj.bjp.0705369
   Elias PM, 2004, J INVEST DERMATOL, V122, P314, DOI 10.1046/j.1523-1747.2003.22258.x
   Elias PM, 2002, EXP DERMATOL, V11, P248, DOI 10.1034/j.1600-0625.2001.110308.x
   EPSTEIN EH, 1984, J AM ACAD DERMATOL, V10, P866, DOI 10.1016/S0190-9622(84)80144-9
   EXCOFFIER L, 1995, MOL BIOL EVOL, V12, P921
   Falany CN, 2006, J STEROID BIOCHEM, V102, P214, DOI 10.1016/j.jsbmb.2006.09.011
   Falany CN, 1997, FASEB J, V11, P1
   Falany CN, 1997, FASEB J, V11, P206, DOI 10.1096/fasebj.11.4.9068609
   Freimuth RR, 2004, PHARMACOGENOMICS J, V4, P54, DOI 10.1038/sj.tpj.6500223
   Fuda H, 2002, J BIOL CHEM, V277, P36161, DOI 10.1074/jbc.M207165200
   Furihata S, 2006, GENETICS, V174, P1505, DOI 10.1534/genetics.105.054452
   Geese WJ, 2001, BIOCHEM BIOPH RES CO, V288, P280, DOI 10.1006/bbrc.2001.5746
   HARTL DL, 2000, ORG GENETIC VARIATIO
   Hazan Carole, 2005, Dermatol Online J, V11, P12
   He DN, 2005, BBA-GEN SUBJECTS, V1724, P119, DOI 10.1016/j.bbagen.2005.03.018
   He DN, 2004, BIOCHEM J, V379, P533, DOI 10.1042/BJ20031524
   He DN, 2006, DRUG METAB DISPOS, V34, P1749, DOI 10.1124/dmd.106.011114
   Hendrick P., 2000, Genetics of populations
   Her C, 1998, GENOMICS, V53, P284, DOI 10.1006/geno.1998.5518
   Higashi Y, 2004, J INVEST DERMATOL, V122, P1207, DOI 10.1111/j.0022-202X.2004.22416.x
   Hildebrandt HAT, 2004, BIOCHEM BIOPH RES CO, V321, P870, DOI 10.1016/j.bbrc.2004.07.038
   Hildebrandt MAT, 2007, PHARMACOGENOMICS J, V7, P133, DOI 10.1038/sj.tpj.6500404
   Javitt NB, 2001, ENDOCRINOLOGY, V142, P2978, DOI 10.1210/en.142.7.2978
   Ji Y, 2005, J NEUROCHEM, V95, P1766, DOI 10.1111/j.1471-4159.2005.03453.x
   Kohjitani A, 2006, GENE, V367, P66, DOI 10.1016/j.gene.2005.09.009
   Kroboth PD, 1999, J CLIN PHARMACOL, V39, P327, DOI 10.1177/00912709922007903
   Labrie F, 2003, ANN ENDOCRINOL-PARIS, V64, P95
   Lee HL, 2003, TAPPI J, V2, P3
   Lee YC, 2005, FEBS LETT, V579, P3639, DOI 10.1016/j.febslet.2005.05.041
   LONG JC, 1995, AM J HUM GENET, V56, P799
   Miller WL, 2002, MOL CELL ENDOCRINOL, V198, P7, DOI 10.1016/S0303-7207(02)00363-5
   Nimmagadda Deepthi, 2006, Indian Journal of Experimental Biology, V44, P171
   OTTERNESS DM, 1992, MOL PHARMACOL, V41, P865
   OTTERNESS DM, 1995, DNA CELL BIOL, V14, P331, DOI 10.1089/dna.1995.14.331
   Raftogianis RB, 1999, BIOCHEM PHARMACOL, V58, P605, DOI 10.1016/S0006-2952(99)00145-8
   Raftogianis RB, 1997, BIOCHEM BIOPH RES CO, V239, P298, DOI 10.1006/bbrc.1997.7466
   Schaid DJ, 2002, AM J HUM GENET, V70, P425, DOI 10.1086/338688
   TAJIMA F, 1989, GENETICS, V123, P229
   TAJIMA F, 1989, GENETICS, V123, P585
   Thomae BA, 2003, J NEUROCHEM, V87, P809, DOI 10.1046/j.1471-4159.2003.02027.x
   Thomas O., 1902, P ZOOL SOC LOND, V2, P2
   Wang LW, 2003, PHARMACOGENETICS, V13, P555, DOI 10.1097/00008571-200309000-00004
   Wang LW, 2005, P NATL ACAD SCI USA, V102, P9394, DOI 10.1073/pnas.0502352102
   Weinshilboum R, 2004, NAT REV DRUG DISCOV, V3, P739, DOI 10.1038/nrd1497
   Yanai H, 2004, CIRCULATION, V109, P92, DOI 10.1161/01.CIR.0000108925.95658.8D
NR 45
TC 29
Z9 40
U1 0
U2 3
PU AMER SOC PHARMACOLOGY EXPERIMENTAL THERAPEUTICS
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3995 USA
SN 0022-3565
J9 J PHARMACOL EXP THER
JI J. Pharmacol. Exp. Ther.
PD AUG
PY 2007
VL 322
IS 2
BP 529
EP 540
DI 10.1124/jpet.107.122895
PG 12
WC Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Pharmacology & Pharmacy
GA 192IM
UT WOS:000248194600013
PM 17496163
DA 2025-04-10
ER

PT J
AU Goodwin, LO
   Leeds, NB
   Guzowski, D
   Hurley, IR
   Pergolizzi, RG
   Benoff, S
AF Goodwin, LO
   Leeds, NB
   Guzowski, D
   Hurley, IR
   Pergolizzi, RG
   Benoff, S
TI Identification of structural elements of the testis-specific voltage
   dependent calcium channel that potentially regulate its biophysical
   properties
SO MOLECULAR HUMAN REPRODUCTION
LA English
DT Article
DE acrosome reaction; alternative splicing; alternative promoters; calcium
   channel; calcium currents
ID RNA-BINDING PROTEIN; SMOOTH-MUSCLE CELLS; FUNCTIONAL EXPRESSION; T-TYPE;
   ALPHA-1 SUBUNIT; CA2+ CHANNEL; RAT-BRAIN; ACROSOME REACTION;
   MESSENGER-RNA; ZONA-PELLUCIDA
AB Calcium influx through voltage-dependent calcium channels regulates the physiological acrosome reaction of mammalian spermatozoa. Expression of the mRNA for these voltage-dependent calcium channels and its co-ordinated translation is initiated early in rat mate germ line development and continues throughout spermatogenesis. Herein, we report the complete mRNA and deduced amino acid sequence of the alpha 1(C) pore-forming subunit of the rat testis-specific L-type calcium channel. This subunit is transcribed from the alpha 1(C) gene, which is also expressed in brain and cardiac muscle. The cardiac- and testis-specific isoforms of the ale subunit are produced by alternate splicing of the same primary transcript. The testis-specific isoform differs from that of cardiac tissue at its amino terminus and in transmembrane segments IS6, IIIS2 and IVS3, which are also dihydropyridine binding sites. In somatic tissues, segments S2 and S3 regulate channel activation while the amino terminus and segment IS6 contribute to channel inactivation kinetics. The amino terminus and IS6 segment of the testis-specific alpha 1(C) subunit are also expressed respectively, in the brain and in smooth muscle from lung where they alter the electrophysiological characteristics of the subunit to produce relatively slow inactivation kinetics. These findings provide a molecular explanation for the detection by others, by patch clamp analysis, of T-type calcium currents in immature spermatogenic cells and of atypical L-type calcium currents in mature spermatozoa.
C1 NYU, N Shore Univ Hosp, Sch Med, Dept Res, Manhasset, NY 11030 USA.
   NYU, N Shore Univ Hosp, Sch Med, Dept Obstet & Gynecol, Manhasset, NY 11030 USA.
   NYU, Sch Med, Dept Cell Biol, Manhasset, NY USA.
C3 Northwell Health; North Shore University Hospital; New York University;
   New York University; Northwell Health; North Shore University Hospital;
   New York University
RP NYU, N Shore Univ Hosp, Sch Med, Dept Res, Manhasset, NY 11030 USA.
FU NIEHS NIH HHS [ES 06100] Funding Source: Medline
CR AKAIKE N, 1989, J PHYSIOL-LONDON, V412, P181, DOI 10.1113/jphysiol.1989.sp017610
   Armstrong C, 1998, SCIENCE, V280, P56, DOI 10.1126/science.280.5360.56
   Arnoult C, 1996, P NATL ACAD SCI USA, V93, P13004, DOI 10.1073/pnas.93.23.13004
   Arnoult C, 1996, J CELL BIOL, V134, P637, DOI 10.1083/jcb.134.3.637
   Arnoult C, 1997, EMBO J, V16, P1593, DOI 10.1093/emboj/16.7.1593
   BENOFF S, 1998, FRONTIERS BIOSCIENCE, pD1220
   BEZPROZVANNY L, 1995, MOL PHARMACOL, V48, P540
   BIEL M, 1991, EUR J BIOCHEM, V200, P81, DOI 10.1111/j.1432-1033.1991.tb21051.x
   BIEL M, 1990, FEBS LETT, V269, P409, DOI 10.1016/0014-5793(90)81205-3
   BIRNBAUMER L, 1994, NEURON, V13, P505, DOI 10.1016/0896-6273(94)90021-3
   Bolger GB, 1996, J BIOL CHEM, V271, P1065, DOI 10.1074/jbc.271.2.1065
   Bourinet E, 1996, J NEUROSCI, V16, P4983
   Breitbart H, 1997, MOL HUM REPROD, V3, P195, DOI 10.1093/molehr/3.3.195
   Brereton HM, 1997, CELL CALCIUM, V22, P39, DOI 10.1016/S0143-4160(97)90088-9
   CATTERALL WA, 1988, SCIENCE, V242, P50, DOI 10.1126/science.2459775
   CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
   CHOU PY, 1979, BIOPHYS J, V26, P367, DOI 10.1016/S0006-3495(79)85259-5
   CLERMONT Y, 1957, AM J ANAT, V100, P241, DOI 10.1002/aja.1001000205
   DEMO SD, 1991, NEURON, V7, P743, DOI 10.1016/0896-6273(91)90277-7
   DIEBOLD RJ, 1992, P NATL ACAD SCI USA, V89, P1497, DOI 10.1073/pnas.89.4.1497
   Doring F, 1996, J BIOL CHEM, V271, P11745, DOI 10.1074/jbc.271.20.11745
   Doyle DA, 1998, SCIENCE, V280, P69, DOI 10.1126/science.280.5360.69
   Eddy EM, 1998, CURR TOP DEV BIOL, V37, P141
   ELLINOR PT, 1993, NATURE, V363, P455, DOI 10.1038/363455a0
   FLORMAN HM, 1994, DEV BIOL, V165, P152, DOI 10.1006/dbio.1994.1242
   FLORMAN HM, 1992, DEV BIOL, V152, P304, DOI 10.1016/0012-1606(92)90137-6
   Florman HM, 1998, BIOL REPROD, V59, P12, DOI 10.1095/biolreprod59.1.12
   FORESTA C, 1992, J BIOL CHEM, V267, P19443
   FORESTA C, 1993, BIOCHEM J, V294, P279, DOI 10.1042/bj2940279
   GARNIER J, 1978, J MOL BIOL, V120, P97, DOI 10.1016/0022-2836(78)90297-8
   Goodwin LO, 1998, MOL HUM REPROD, V4, P215, DOI 10.1093/molehr/4.3.215
   Goodwin LO, 1997, MOL HUM REPROD, V3, P255, DOI 10.1093/molehr/3.3.255
   GOODWIN LO, 1997, 53 ANN M AM SOC REPR, pS30
   GOODWIN LO, 1998, 54 ANN M, pS207
   GOODWIN LO, 1998, 23 ANN M AM SOC AN S, P26
   GOODWIN LO, 1997, 44 ANN M, pA238
   GU W, 1995, J BIOL CHEM, V270, P236, DOI 10.1074/jbc.270.1.236
   GUERRERO A, 1989, J BIOL CHEM, V264, P19593
   GUY HR, 1990, TRENDS NEUROSCI, V13, P201
   HAN JR, 1995, BIOL REPROD, V53, P707, DOI 10.1095/biolreprod53.3.707
   HAN JR, 1995, P NATL ACAD SCI USA, V92, P9550, DOI 10.1073/pnas.92.21.9550
   HARTMANN HA, 1991, SCIENCE, V251, P942, DOI 10.1126/science.2000495
   Hoog C, 1995, INT J DEV BIOL, V39, P719
   HOSEY MM, 1988, J MEMBRANE BIOL, V104, P81, DOI 10.1007/BF01870922
   HOSHI T, 1990, SCIENCE, V250, P533, DOI 10.1126/science.2122519
   HUI A, 1991, NEURON, V7, P35, DOI 10.1016/0896-6273(91)90072-8
   Janssen LJ, 1997, AM J PHYSIOL-CELL PH, V272, pC1757, DOI 10.1152/ajpcell.1997.272.6.C1757
   KADONAGA JT, 1986, TRENDS BIOCHEM SCI, V11, P20, DOI 10.1016/0968-0004(86)90226-4
   KILPATRICK DL, 1990, MOL CELL BIOL, V10, P3717, DOI 10.1128/MCB.10.7.3717
   KOCH WJ, 1990, J BIOL CHEM, V265, P17786
   KOCH WJ, 1989, FEBS LETT, V250, P386, DOI 10.1016/0014-5793(89)80761-6
   KOZAK M, 1991, J BIOL CHEM, V266, P19867
   LEONARD JP, 1987, J NEUROSCI, V7, P875
   LIEVANO A, 1994, AM J PHYSIOL, V267, pC411, DOI 10.1152/ajpcell.1994.267.2.C411
   LIN SC, 1991, J BIOL CHEM, V266, P23347
   MA WJ, 1992, J BIOL CHEM, V267, P22728
   MACKINNON R, 1990, SCIENCE, V250, P276, DOI 10.1126/science.2218530
   Maniatis T., 1987, MOL CLONING, V3nd
   MCCARREY JR, 1987, GENE, V61, P291, DOI 10.1016/0378-1119(87)90192-2
   Meir A, 1998, NEURON, V20, P341, DOI 10.1016/S0896-6273(00)80461-4
   MIKAMI A, 1989, NATURE, V340, P230, DOI 10.1038/340230a0
   MITCHELL PJ, 1989, SCIENCE, V245, P371, DOI 10.1126/science.2667136
   MLINAR B, 1994, MOL PHARMACOL, V46, P743
   MOUNT SM, 1982, NUCLEIC ACIDS RES, V10, P459, DOI 10.1093/nar/10.2.459
   Nakayama S, 1996, BRIT J PHARMACOL, V119, P716, DOI 10.1111/j.1476-5381.1996.tb15731.x
   Olcese R, 1997, J GEN PHYSIOL, V110, P579, DOI 10.1085/jgp.110.5.579
   Perez-Reyes E, 1998, NATURE, V391, P896, DOI 10.1038/36110
   PEREZREYES E, 1995, KIDNEY INT, V48, P1111, DOI 10.1038/ki.1995.395
   Piedras-Rentería ES, 1997, P NATL ACAD SCI USA, V94, P14936, DOI 10.1073/pnas.94.26.14936
   Randall AD, 1997, NEUROPHARMACOLOGY, V36, P879, DOI 10.1016/S0028-3908(97)00086-5
   RICH A, 1993, AM J PHYSIOL, V264, pC745, DOI 10.1152/ajpcell.1993.264.3.C745
   Santi CM, 1996, AM J PHYSIOL-CELL PH, V271, pC1583, DOI 10.1152/ajpcell.1996.271.5.C1583
   SATHER WA, 1993, NEURON, V11, P291, DOI 10.1016/0896-6273(93)90185-T
   SCHNEIDER T, 1994, RECEPTOR CHANNEL, V2, P255
   SCHULTZ D, 1993, P NATL ACAD SCI USA, V90, P6228, DOI 10.1073/pnas.90.13.6228
   SHARMA PM, 1992, CANCER RES, V52, P6407
   SNUTCH TP, 1990, P NATL ACAD SCI USA, V87, P3391, DOI 10.1073/pnas.87.9.3391
   SNUTCH TP, 1991, NEURON, V7, P45, DOI 10.1016/0896-6273(91)90073-9
   SOLDATOV NM, 1992, P NATL ACAD SCI USA, V89, P4628, DOI 10.1073/pnas.89.10.4628
   SOLDATOV NM, 1995, J BIOL CHEM, V270, P10540, DOI 10.1074/jbc.270.18.10540
   SOLDATOV NM, 1994, GENOMICS, V22, P77, DOI 10.1006/geno.1994.1347
   SOONG TW, 1993, SCIENCE, V260, P1133, DOI 10.1126/science.8388125
   Spungin B, 1996, J CELL SCI, V109, P1947
   TANABE T, 1987, NATURE, V328, P313, DOI 10.1038/328313a0
   TANABE T, 1991, NATURE, V352, P800, DOI 10.1038/352800a0
   TANABE T, 1988, NATURE, V336, P134, DOI 10.1038/336134a0
   TIWARIWOODRUFF SK, 1995, AM J PHYSIOL-CELL PH, V268, pC1284, DOI 10.1152/ajpcell.1995.268.5.C1284
   TSIEN RW, 1991, TRENDS PHARMACOL SCI, V12, P349, DOI 10.1016/0165-6147(91)90595-J
   VIRBASIUS JV, 1988, J BIOL CHEM, V263, P6791
   WAKAMORI M, 1994, RECEPTOR CHANNEL, V2, P303
   WATERS SH, 1985, MOL CELL BIOL, V5, P1649, DOI 10.1128/MCB.5.7.1649
   Wei X, 1996, RECEPTOR CHANNEL, V4, P205
   WELLING A, 1993, CIRC RES, V73, P974, DOI 10.1161/01.RES.73.5.974
   WIDLAK W, 1995, BBA-GENE STRUCT EXPR, V1264, P191, DOI 10.1016/0167-4781(95)00135-4
   YANAGIMACHI R, 1974, EXP CELL RES, V89, P161, DOI 10.1016/0014-4827(74)90199-2
   YIU GK, 1994, NUCLEIC ACIDS RES, V22, P4599, DOI 10.1093/nar/22.22.4599
   ZHANG JF, 1994, NATURE, V372, P97, DOI 10.1038/372097a0
   ZHANG JF, 1993, NEUROPHARMACOLOGY, V32, P1075, DOI 10.1016/0028-3908(93)90003-L
NR 98
TC 17
Z9 19
U1 0
U2 0
PU OXFORD UNIV PRESS
PI OXFORD
PA GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND
SN 1360-9947
EI 1460-2407
J9 MOL HUM REPROD
JI Mol. Hum. Reprod.
PD APR
PY 1999
VL 5
IS 4
BP 311
EP 322
DI 10.1093/molehr/5.4.311
PG 12
WC Developmental Biology; Obstetrics & Gynecology; Reproductive Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Developmental Biology; Obstetrics & Gynecology; Reproductive Biology
GA 183DU
UT WOS:000079539400004
PM 10321802
OA Bronze
DA 2025-04-10
ER

PT J
AU Liu, YC
   Ferguson, JF
   Xue, CY
   Silverman, IM
   Gregory, B
   Reilly, MP
   Li, MY
AF Liu, Yichuan
   Ferguson, Jane F.
   Xue, Chenyi
   Silverman, Ian M.
   Gregory, Brian
   Reilly, Muredach P.
   Li, Mingyao
TI Evaluating the Impact of Sequencing Depth on Transcriptome Profiling in
   Human Adipose
SO PLOS ONE
LA English
DT Article
ID RNA-SEQ; GENE-EXPRESSION; INFLAMMATION; ENDOTOXIN; DISEASE; BIOMARKERS
AB Recent advances in RNA sequencing (RNA-Seq) have enabled the discovery of novel transcriptomic variations that are not possible with traditional microarray-based methods. Tissue and cell specific transcriptome changes during pathophysiological stress in disease cases versus controls and in response to therapies are of particular interest to investigators studying cardiometabolic diseases. Thus, knowledge on the relationships between sequencing depth and detection of transcriptomic variation is needed for designing RNA-Seq experiments and for interpreting results of analyses. Using deeply sequenced Illumina HiSeq 2000 101 bp paired-end RNA-Seq data derived from adipose of a healthy individual before and after systemic administration of endotoxin (LPS), we investigated the sequencing depths needed for studies of gene expression and alternative splicing (AS). In order to detect expressed genes and AS events, we found that similar to 100 to 150 million (M) filtered reads were needed. However, the requirement on sequencing depth for the detection of LPS modulated differential expression (DE) and differential alternative splicing (DAS) was much higher. To detect 80% of events, similar to 300 M filtered reads were needed for DE analysis whereas at least 400 M filtered reads were necessary for detecting DAS. Although the majority of expressed genes and AS events can be detected with modest sequencing depths (similar to 100 M filtered reads), the estimated gene expression levels and exon/intron inclusion levels were less accurate. We report the first study that evaluates the relationship between RNA-Seq depth and the ability to detect DE and DAS in human adipose. Our results suggest that a much higher sequencing depth is needed to reliably identify DAS events than for DE genes.
C1 [Liu, Yichuan; Li, Mingyao] Univ Penn, Perelman Sch Med, Dept Biostat & Epidemiol, Philadelphia, PA 19104 USA.
   [Ferguson, Jane F.; Xue, Chenyi; Reilly, Muredach P.] Univ Penn, Perelman Sch Med, Cardiovasc Inst, Philadelphia, PA 19104 USA.
   [Silverman, Ian M.; Gregory, Brian] Univ Penn, Perelman Sch Med, Dept Biol, Philadelphia, PA 19104 USA.
   [Silverman, Ian M.; Gregory, Brian] Univ Penn, Sch Arts & Sci, Philadelphia, PA 19104 USA.
C3 University of Pennsylvania; University of Pennsylvania; University of
   Pennsylvania; University of Pennsylvania
RP Reilly, MP (corresponding author), Univ Penn, Perelman Sch Med, Cardiovasc Inst, Philadelphia, PA 19104 USA.
EM muredach@mail.med.upenn.edu; mingyao@mail.med.upenn.edu
RI Ferguson, Jane/C-7154-2011; Liu, Yichuan/AAF-3893-2021; Gregory,
   Brian/G-2890-2010
OI LIU, YICHUAN/0000-0003-2023-072X; Silverman, Ian/0000-0003-3819-6726;
   Reilly, Muredach/0000-0002-3035-9386; Ferguson, Jane/0000-0001-6896-1025
FU pilot grant from Penn Genomes Frontiers Institute [R01-HL-113147];
   National Center for Research Resources; National Center for Advancing
   Translational Sciences, National Institutes of Health [UL1TR000003];
   NIH-NHLBI SCCOR Project grant [P50-HL-083799];  [R01-HG-004517]; 
   [R01-HG-005854];  [R01-HL-111694];  [R01-DK-090505];  [U01-HL-108636]; 
   [K24-HL-107643]
FX This work was supported by a pilot grant from Penn Genomes Frontiers
   Institute and R01-HL-113147 (ML and MPR) as well as by the National
   Center for Research Resources and the National Center for Advancing
   Translational Sciences, National Institutes of Health, through Grant
   UL1TR000003 and a NIH-NHLBI SCCOR Project grant (P50-HL-083799) to MPR.
   ML is also supported by R01-HG-004517 and R01-HG-005854. MPR is also
   supported by R01-HL-111694, R01-DK-090505, U01-HL-108636, and
   K24-HL-107643. The funders had no role in study design, data collection
   and analysis, decision to publish, or preparation of the manuscript.
CR Agwunobi AO, 2000, J CLIN ENDOCR METAB, V85, P3770, DOI 10.1210/jc.85.10.3770
   Armah KA, 2012, CLIN INFECT DIS, V55, P126, DOI 10.1093/cid/cis406
   Cabili MN, 2011, GENE DEV, V25, P1915, DOI 10.1101/gad.17446611
   Chartoumpekis DV, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0034872
   Copeland S, 2005, CLIN DIAGN LAB IMMUN, V12, P60, DOI 10.1128/CDLI.12.1.60-67.2005
   Emilsson V, 2008, NATURE, V452, P423, DOI 10.1038/nature06758
   Ferguson JF, 2013, J TRANSL MED, V11, DOI 10.1186/1479-5876-11-63
   Hu Y, 2013, NUCLEIC ACIDS RES, V41, DOI 10.1093/nar/gks1026
   Hudgins LC, 2003, J LIPID RES, V44, P1489, DOI 10.1194/jlr.M200440-JLR200
   Katz Y, 2010, NAT METHODS, V7, P1009, DOI 10.1038/NMETH.1528
   Labaj PP, 2011, BIOINFORMATICS, V27, pI383, DOI 10.1093/bioinformatics/btr247
   Levanon EY, 2004, NAT BIOTECHNOL, V22, P1001, DOI 10.1038/nbt996
   Li MY, 2011, SCIENCE, V333, P53, DOI 10.1126/science.1207018
   Marioni JC, 2008, GENOME RES, V18, P1509, DOI 10.1101/gr.079558.108
   McGillicuddy FC, 2009, CIRCULATION, V119, P1135, DOI 10.1161/CIRCULATIONAHA.108.810721
   Mehta NN, 2010, DIABETES, V59, P172, DOI 10.2337/db09-0367
   Mitelman F, 2007, NAT REV CANCER, V7, P233, DOI 10.1038/nrc2091
   Mortazavi A, 2008, NAT METHODS, V5, P621, DOI 10.1038/nmeth.1226
   Nica AC, 2011, PLOS GENET, V7, DOI 10.1371/journal.pgen.1002003
   Pedrotty DM, 2012, PROG CARDIOVASC DIS, V55, P64, DOI 10.1016/j.pcad.2012.06.003
   SCHENA M, 1995, SCIENCE, V270, P467, DOI 10.1126/science.270.5235.467
   Shah R, 2009, DIABETES, V58, P2211, DOI 10.2337/db09-0256
   Shen SH, 2012, NUCLEIC ACIDS RES, V40, DOI 10.1093/nar/gkr1291
   SUFFREDINI AF, 1989, NEW ENGL J MED, V321, P280, DOI 10.1056/NEJM198908033210503
   Toung JM, 2011, GENOME RES, V21, P991, DOI 10.1101/gr.116335.110
   Trapnell C, 2010, NAT BIOTECHNOL, V28, P511, DOI 10.1038/nbt.1621
   Trapnell C, 2009, BIOINFORMATICS, V25, P1105, DOI 10.1093/bioinformatics/btp120
   Wang ET, 2008, NATURE, V456, P470, DOI 10.1038/nature07509
   Wang Y, 2011, BMC BIOINFORMATICS, V12, DOI 10.1186/1471-2105-12-S10-S5
   Wilhelm BT, 2009, METHODS, V48, P249, DOI 10.1016/j.ymeth.2009.03.016
NR 30
TC 45
Z9 59
U1 0
U2 8
PU PUBLIC LIBRARY SCIENCE
PI SAN FRANCISCO
PA 1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA
SN 1932-6203
J9 PLOS ONE
JI PLoS One
PD JUN 24
PY 2013
VL 8
IS 6
AR e66883
DI 10.1371/journal.pone.0066883
PG 10
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA 182JP
UT WOS:000321738400077
PM 23826166
OA Green Published, gold, Green Submitted
DA 2025-04-10
ER

PT J
AU Ogut, O
   Granzier, H
   Jin, JP
AF Ogut, O
   Granzier, H
   Jin, JP
TI Acidic and basic troponin T isoforms in mature fast-twitch skeletal
   muscle and effect on contractility
SO AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY
LA English
DT Article
DE alternative ribonucleic acid splicing; developmental regulation;
   calcium; activation of force and stiffness; tropomyosin
ID NH2-TERMINAL VARIABLE REGION; COMPLETE NUCLEOTIDE-SEQUENCE;
   METAL-BINDING CLUSTER; MOLECULAR-BASIS; CARDIAC-MUSCLE; ADULT ISOFORMS;
   TROPOMYOSIN; EXPRESSION; GENE; SENSITIVITY
AB Developmentally regulated alternative RNA splicing generates distinct classes of acidic and basic troponin T (TnT) isoforms. In fast-twitch skeletal muscles, an acidic-to-basic TnT isoform switch ensures basic isoform expression in the adult. As an exception, an acidic segment in the NH2-terminal variable region of adult chicken breast muscle TnT isoforms is responsible for the unique exclusive expression of acidic TnTs in this muscle (O. Ogut and J.-P. Jin. J. Biol. Chem. 273: 27858-27866, 1998). To understand the relationship between acidic vs. basic TnT isoform expression and muscle contraction, the contractile properties of fibers from adult chicken breast muscle were compared with those of the levator coccygeus muscle, which expresses solely basic TnT isoforms. With use of Triton X-100-skinned muscle fibers, the force and stiffness responses to Ca2+ were measured. Relative to the levator coccygeus muscle, the breast muscle fibers showed significantly increased sensitivity to Ca2+ of force and stiffness with a shift of similar to 0.15 in the pCa at which force or stiffness was 50% of maximal. The expression of tropomyosin, troponin I, and troponin C isoforms was also determined to delineate their contribution to thin-filament regulation. The data indicate that TnT isoforms differing in their NH2-terminal charge are able to alter the sensitivity of the myofibrillar contractile apparatus to Ca2+. These results provide evidence linking the regulated expression of distinct acidic and basic TnT isoform classes to the contractility of striated muscle.
C1 Case Western Reserve Univ, Dept Physiol & Biophys, Sch Med, Cleveland, OH 44106 USA.
   Washington State Univ, Dept Vet & Comparat Anat Pharmacol & Physiol, Pullman, WA 99164 USA.
C3 University System of Ohio; Case Western Reserve University; Washington
   State University
RP Case Western Reserve Univ, Dept Physiol & Biophys, Sch Med, 10900 Euclid Ave, Cleveland, OH 44106 USA.
EM jxj12@po.cwru.edu
RI Jin, Jian-Ping/AAD-1149-2020
OI Jin, JP/0000-0001-9932-1063
CR AKELLA AB, 1995, CIRC RES, V76, P600, DOI 10.1161/01.RES.76.4.600
   ANDERSON PAW, 1995, CIRC RES, V76, P681, DOI 10.1161/01.RES.76.4.681
   BREITBART RE, 1986, J MOL BIOL, V188, P313, DOI 10.1016/0022-2836(86)90157-9
   BRISSON JR, 1986, BIOCHEMISTRY-US, V25, P4548, DOI 10.1021/bi00364a014
   CHASE PB, 1988, BIOPHYS J, V53, P935, DOI 10.1016/S0006-3495(88)83174-6
   COLLINS JH, 1991, J MUSCLE RES CELL M, V12, P3, DOI 10.1007/BF01781170
   COOPER TA, 1985, J BIOL CHEM, V260, P1140
   FABIATO A, 1988, METHOD ENZYMOL, V157, P378
   FUJITA S, 1992, J BIOCHEM-TOKYO, V112, P306, DOI 10.1093/oxfordjournals.jbchem.a123896
   GODT RE, 1991, CAN J PHYSIOL PHARM, V69, P1692, DOI 10.1139/y91-251
   GRANZIER HL, 1995, BIOPHYS J, V68, P1027, DOI 10.1016/S0006-3495(95)80278-X
   GRANZIER HLM, 1987, J MUSCLE RES CELL M, V8, P242, DOI 10.1007/BF01574592
   HEELEY DH, 1987, J BIOL CHEM, V262, P9971
   JIN JP, 1990, ANN NY ACAD SCI, V588, P393, DOI 10.1111/j.1749-6632.1990.tb13243.x
   JIN JP, 1994, FEBS LETT, V341, P135, DOI 10.1016/0014-5793(94)80256-4
   Jin JP, 1998, GENE, V214, P121, DOI 10.1016/S0378-1119(98)00214-5
   JIN JP, 1988, J BIOL CHEM, V263, P7309
   JIN JP, 1992, J MOL BIOL, V227, P1269, DOI 10.1016/0022-2836(92)90540-Z
   Jin JP, 1996, GENE, V168, P217, DOI 10.1016/0378-1119(95)00803-9
   LEAVIS PC, 1984, CRC CR REV BIOCH MOL, V16, P235, DOI 10.3109/10409238409108717
   LEESMILLER JP, 1991, BIOESSAYS, V13, P429, DOI 10.1002/bies.950130902
   LIN JJC, 1985, HYBRIDOMA, V4, P223, DOI 10.1089/hyb.1985.4.223
   MARTYN DA, 1992, J GEN PHYSIOL, V99, P795, DOI 10.1085/jgp.99.5.795
   Nickel R., 1977, ANATOMY DOMESTIC BIR
   Ogut O, 1996, BIOCHEMISTRY-US, V35, P16581, DOI 10.1021/bi961712y
   Ogut O, 1998, J BIOL CHEM, V273, P27858, DOI 10.1074/jbc.273.43.27858
   Palmiter KA, 1996, J BIOL CHEM, V271, P11611, DOI 10.1074/jbc.271.20.11611
   PAN BS, 1991, J BIOL CHEM, V266, P12432
   PEARLSTONE JR, 1982, J BIOL CHEM, V257, P587
   PEARLSTONE JR, 1977, J BIOL CHEM, V252, P983
   Perry SV, 1998, J MUSCLE RES CELL M, V19, P575
   POTTER JD, 1982, METHOD ENZYMOL, V85, P241
   REISER PJ, 1992, J PHYSIOL-LONDON, V449, P573, DOI 10.1113/jphysiol.1992.sp019102
   SCHACHAT F, 1995, DEV BIOL, V171, P233, DOI 10.1006/dbio.1995.1274
   SCHACHAT FH, 1987, J MOL BIOL, V198, P551, DOI 10.1016/0022-2836(87)90300-7
   SMILLIE LB, 1988, J BIOL CHEM, V263, P18816
   SOLARO RJ, 1988, CIRC RES, V63, P779, DOI 10.1161/01.RES.63.4.779
   Squire JM, 1998, FASEB J, V12, P761, DOI 10.1096/fasebj.12.10.761
   TOBACMAN LS, 1988, J BIOL CHEM, V263, P2668
   Wang J, 1998, BIOCHEMISTRY-US, V37, P14519, DOI 10.1021/bi9812322
   Wang J, 1997, GENE, V193, P105, DOI 10.1016/S0378-1119(97)00100-5
   Westfall MV, 1997, P NATL ACAD SCI USA, V94, P5444, DOI 10.1073/pnas.94.10.5444
   WU QL, 1994, DNA CELL BIOL, V13, P217, DOI 10.1089/dna.1994.13.217
   Yonemura I, 1996, BIOCHEM BIOPH RES CO, V226, P200, DOI 10.1006/bbrc.1996.1333
NR 44
TC 69
Z9 73
U1 0
U2 2
PU AMER PHYSIOLOGICAL SOC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA
SN 0363-6143
EI 1522-1563
J9 AM J PHYSIOL-CELL PH
JI Am. J. Physiol.-Cell Physiol.
PD MAY
PY 1999
VL 276
IS 5
BP C1162
EP C1170
DI 10.1152/ajpcell.1999.276.5.C1162
PG 9
WC Cell Biology; Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Physiology
GA 195HR
UT WOS:000080245000021
DA 2025-04-10
ER

PT J
AU Dooley, CM
   James, J
   McGlade, CJ
   Ahmad, I
AF Dooley, CM
   James, J
   McGlade, CJ
   Ahmad, I
TI Involvement of Numb in vertebrate retinal development: Evidence for
   multiple roles of Numb in neural differentiation and maturation
SO JOURNAL OF NEUROBIOLOGY
LA English
DT Article
DE Numb; Notch; retina; asymmetric; progenitors; neurogenesis; development
ID SENSORY ORGAN LINEAGE; CELL FATES; ASYMMETRIC LOCALIZATION; CORTICAL
   NEUROGENESIS; GANGLION-CELLS; XENOPUS RETINA; CHICK RETINA; MOUSE NUMB;
   NOTCH; DIVISION
AB Cell fate specification is regulated in part by lateral inhibition mediated by Notch signaling. Notch signaling is negatively regulated by Numb, an intrinsic factor that regulates cellular competence. In this study we have examined the involvement of Numb in retinal development, which has been shown to be influenced by Notch signaling. In the developing retina, Numb is asymmetrically distributed towards the ventricular and vitreal poles of different cells. Asymmetric localization is evident not only in mitotic cells but in postmitotic ganglion cells as well, suggesting that the subcellular distribution of Numb may play a role after cells have exited the cell cycle. This is supported by the expression of Numb in terminally differentiated neurons in the adult retina. Although Numb is an intrinsic factor, it is observed that its subcellular distribution is influenced by epigenetic cues such that a higher proportion of cells cultured at high density express Numb asymmetrically. A correlation is observed between asymmetric localization and cellular competence; cells in which Numb is asymmetric differentiate more readily in culture than those that express Numb symmetrically. We have identified alternative splice variants in the developing and adult retina that correspond to isoforms that have been shown to regulate proliferation and differentiation. The dynamic temporal expression patterns of alternative splice variants and isoforms suggest that Numb may influence proliferation and differentiation of retinal progenitors during neurogenesis and maturation of postmitotic neurons. Together, these results demonstrate the complex role of the distribution of Numb within progenitors and postmitotic neurons. (C) 2002 Wiley Periodicals, Inc.
C1 Univ Nebraska, Med Ctr, Omaha, NE 68198 USA.
C3 University of Nebraska System; University of Nebraska Medical Center
RP Ahmad, I (corresponding author), Univ Nebraska, Med Ctr, 600 S 42nd St, Omaha, NE 68198 USA.
RI James/F-4346-2010
OI James, Jackson/0000-0002-7038-2687
CR AHMAD I, 1995, MECH DEVELOP, V53, P73, DOI 10.1016/0925-4773(95)00425-4
   Ahmad I, 1999, BRAIN RES, V831, P1, DOI 10.1016/S0006-8993(99)01376-1
   Ahmad I, 1997, DEV BIOL, V185, P92, DOI 10.1006/dbio.1997.8546
   Ahmad I, 1995, Brain Res Dev Brain Res, V90, P184
   Ahmad I, 1998, DEV BIOL, V194, P86, DOI 10.1006/dbio.1997.8809
   AHMAD I, 1994, NEURON, V12, P155, DOI 10.1016/0896-6273(94)90160-0
   AUSTIN CP, 1995, DEVELOPMENT, V121, P3637
   Bao ZZ, 1997, J NEUROSCI, V17, P1425
   Berezovska O, 1999, NEUROSCIENCE, V93, P433, DOI 10.1016/S0306-4522(99)00157-8
   Byrd JC, 1999, J BIOL CHEM, V274, P24408, DOI 10.1074/jbc.274.34.24408
   Cayouette M, 2001, J NEUROSCI, V21, P5643, DOI 10.1523/JNEUROSCI.21-15-05643.2001
   CHRISTIE GA, 1964, J MORPHOL, V114, P263, DOI 10.1002/jmor.1051140207
   Dho SE, 1999, J BIOL CHEM, V274, P33097, DOI 10.1074/jbc.274.46.33097
   Dorsky RI, 1997, NATURE, V385, P67, DOI 10.1038/385067a0
   DORSKY RI, 1995, NEURON, V14, P487, DOI 10.1016/0896-6273(95)90305-4
   Franklin JL, 1999, CURR BIOL, V9, P1448, DOI 10.1016/S0960-9822(00)80114-1
   Frise E, 1996, P NATL ACAD SCI USA, V93, P11925, DOI 10.1073/pnas.93.21.11925
   Guo M, 1996, NEURON, V17, P27, DOI 10.1016/S0896-6273(00)80278-0
   Henrique D, 1997, CURR BIOL, V7, P661, DOI 10.1016/S0960-9822(06)00293-4
   Imai T, 2001, MOL CELL BIOL, V21, P3888, DOI 10.1128/MCB.21.12.3888-3900.2001
   KNOBLICH JA, 1995, NATURE, V377, P624, DOI 10.1038/377624a0
   Lindsell CE, 1996, MOL CELL NEUROSCI, V8, P14, DOI 10.1006/mcne.1996.0040
   PRADA C, 1991, EUR J NEUROSCI, V3, P559, DOI 10.1111/j.1460-9568.1991.tb00843.x
   Redmond L, 2000, NAT NEUROSCI, V3, P30, DOI 10.1038/71104
   RHYU MS, 1994, CELL, V76, P477, DOI 10.1016/0092-8674(94)90112-0
   ROBINSON SR, 1991, NEUROANATOMY VISUAL, P69
   Sestan N, 1999, SCIENCE, V286, P741, DOI 10.1126/science.286.5440.741
   Spana EP, 1996, NEURON, V17, P21, DOI 10.1016/S0896-6273(00)80277-9
   SPANA EP, 1995, DEVELOPMENT, V121, P3489
   TURNER DL, 1990, NEURON, V4, P833, DOI 10.1016/0896-6273(90)90136-4
   TURNER DL, 1987, NATURE, V328, P131, DOI 10.1038/328131a0
   UEMURA T, 1989, CELL, V58, P349, DOI 10.1016/0092-8674(89)90849-0
   Verdi JM, 1999, P NATL ACAD SCI USA, V96, P10472, DOI 10.1073/pnas.96.18.10472
   VERDI JM, 1996, CURR BIOL, V6, P134
   Wakamatsu Y, 2000, DEVELOPMENT, V127, P2811
   Wakamatsu Y, 1999, NEURON, V23, P71, DOI 10.1016/S0896-6273(00)80754-0
   Wang SW, 1997, DEVELOPMENT, V124, P4435
   WETTS R, 1988, SCIENCE, V239, P1142, DOI 10.1126/science.2449732
   YOUNG RW, 1985, ANAT RECORD, V212, P199, DOI 10.1002/ar.1092120215
   Zhong WM, 1996, NEURON, V17, P43, DOI 10.1016/S0896-6273(00)80279-2
   Zhong WM, 2000, P NATL ACAD SCI USA, V97, P6844, DOI 10.1073/pnas.97.12.6844
   Zilian O, 2001, CURR BIOL, V11, P494, DOI 10.1016/S0960-9822(01)00149-X
NR 42
TC 36
Z9 47
U1 0
U2 1
PU JOHN WILEY & SONS INC
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN, NJ 07030 USA
SN 0022-3034
J9 J NEUROBIOL
JI J. Neurobiol.
PD FEB 5
PY 2003
VL 54
IS 2
BP 313
EP 325
DI 10.1002/neu.10176
PG 13
WC Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA 636ND
UT WOS:000180461500001
PM 12500307
DA 2025-04-10
ER

PT J
AU Norrbom, J
   Sällstedt, EK
   Fischer, H
   Sundberg, CJ
   Rundqvist, H
   Gustafsson, T
AF Norrbom, J.
   Sallstedt, E. K.
   Fischer, H.
   Sundberg, C. J.
   Rundqvist, H.
   Gustafsson, T.
TI Alternative splice variant PGC-1α-b is strongly induced by exercise in
   human skeletal muscle
SO AMERICAN JOURNAL OF PHYSIOLOGY-ENDOCRINOLOGY AND METABOLISM
LA English
DT Article
DE peroxisome proliferator-activated receptor-gamma coactivator-1 alpha-b
ID RECEPTOR-GAMMA COACTIVATOR-1-ALPHA; MESSENGER-RNA EXPRESSION; ACTIVATED
   PROTEIN-KINASE; MITOCHONDRIAL BIOGENESIS; TRANSCRIPTIONAL COACTIVATOR;
   CONTRACTILE ACTIVITY; GENE-EXPRESSION; DEFICIENT MICE; PGC-1; INCREASES
AB Norrbom J, Sallstedt EK, Fischer H, Sundberg CJ, Rundqvist H, Gustafsson T. Alternative splice variant PGC-1 alpha-b is strongly induced by exercise in human skeletal muscle. Am J Physiol Endocrinol Metab 301: E1092-E1098, 2011. First published August 23, 2011; doi: 10.1152/ajpendo.00119.2011.-The present study investigated whether exercise induces the expression of PGC-1 alpha splice variants in human skeletal muscle and the possible influence of metabolic perturbation on this response. The subjects exercised one leg for 45 min with restricted blood flow (R-leg), followed by 45 min of exercise using the other leg at the same absolute workload but with normal blood flow (NR-leg). This ischemic model (R-leg) has been shown previously to induce a greater metabolic perturbation and enhance the expression of PGC-1 alpha beyond that observed in the NR-leg. Cultured human myotubes were used to test suggested exercise-induced regulatory stimuli of PGC-1 alpha. We showed, for the first time, that transcripts from both the canonical promoter (PGC-1 alpha-a) and the proposed upstream-located promoter (PGC-1 alpha-b) are present in human skeletal muscle. Both transcripts were upregulated after exercise in the R-leg, but the fold change increase of PGC-1 alpha-b was much greater than that of PGC-1 alpha-a. No differences were observed between the two conditions regarding the marker for calcineurin activation, MCIP1, or p38 phosphorylation. AMPK phosphorylation increased to a greater extent in the R-leg, and AICAR stimulation of cultured human myotubes induced the expression of PGC-1 alpha-a and PGC-1 alpha-b. AICAR combined with norepinephrine yielded an additive effect on the PGC-1 alpha-b expression only. Our results indicate clearly that exercise can activate an upstream promoter in humans and support AMPK as a major regulator of transcripts from the canonical PGC-1 alpha promoter and the involvement of beta-adrenergic stimulation in combination with AMPK in the regulation of PGC-1 alpha-b.
C1 [Norrbom, J.; Sallstedt, E. K.; Sundberg, C. J.] Karolinska Inst, Dept Physiol & Pharmacol, S-17177 Stockholm, Sweden.
   [Fischer, H.; Gustafsson, T.] Karolinska Inst, Dept Lab Med, S-17177 Stockholm, Sweden.
   [Rundqvist, H.] Karolinska Inst, Dept Pathol & Oncol, S-17177 Stockholm, Sweden.
C3 Karolinska Institutet; Karolinska Institutet; Karolinska Institutet
RP Norrbom, J (corresponding author), Karolinska Inst, Dept Physiol & Pharmacol, S-17177 Stockholm, Sweden.
EM jessica.norrbom@ki.se
RI Sundberg, Carl/B-9356-2013; Rundqvist, Helene/AAE-7334-2020; Gustafsson,
   Thomas/AAH-1056-2019
OI Sundberg, Carl Johan/0000-0002-7000-466X; Gidlund,
   Eva-karin/0000-0003-2359-0739; Gustafsson, Thomas/0000-0002-1559-4206;
   Rundqvist, Helene/0000-0002-5617-9076
FU Swedish National Centre for Research in Sports; Swedish Medical
   Association; Karolinska Institutet Foundation; Wallenberg Foundation;
   Trygg-Hansa Foundation; Ake Wiberg Foundation; Magnus Bergvall
   Foundation; Swedish Medical Research Council
FX This study was supported by grants from the Swedish National Centre for
   Research in Sports, the Swedish Medical Association, the Karolinska
   Institutet Foundation, the Wallenberg Foundation, the Trygg-Hansa
   Foundation, the Ake Wiberg Foundation, the Magnus Bergvall Foundation,
   and the Swedish Medical Research Council.
CR Akimoto T, 2005, J BIOL CHEM, V280, P19587, DOI 10.1074/jbc.M408862200
   Akimoto T, 2004, AM J PHYSIOL-CELL PH, V287, pC1311, DOI 10.1152/ajpcell.00248.2004
   Arany Z, 2008, NATURE, V451, P1008, DOI 10.1038/nature06613
   Baar K, 2002, FASEB J, V16, P1879, DOI 10.1096/fj.02-0367com
   BLAU HM, 1981, P NATL ACAD SCI-BIOL, V78, P5623, DOI 10.1073/pnas.78.9.5623
   Chinsomboon J, 2009, P NATL ACAD SCI USA, V106, P21401, DOI 10.1073/pnas.0909131106
   CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
   Egan B, 2010, J PHYSIOL-LONDON, V588, P1779, DOI 10.1113/jphysiol.2010.188011
   EIKEN O, 1987, ACTA PHYSIOL SCAND, V131, P339, DOI 10.1111/j.1748-1716.1987.tb08248.x
   ESBJORNSSON M, 1993, ACTA PHYSIOL SCAND, V148, P233, DOI 10.1111/j.1748-1716.1993.tb09554.x
   Finck BN, 2006, J CLIN INVEST, V116, P615, DOI 10.1172/JCI27794
   Garcia-Roves PM, 2006, AM J PHYSIOL-ENDOC M, V290, pE1172, DOI 10.1152/ajpendo.00633.2005
   Garnier A, 2005, FASEB J, V19, P43, DOI 10.1096/fj.04-2173com
   Gustafsson T, 2005, J APPL PHYSIOL, V98, P2137, DOI 10.1152/japplphysiol.01402.2004
   Handschin C, 2003, P NATL ACAD SCI USA, V100, P7111, DOI 10.1073/pnas.1232352100
   Hood DA, 2006, J EXP BIOL, V209, P2265, DOI 10.1242/jeb.02182
   Irrcher I, 2003, AM J PHYSIOL-CELL PH, V284, pC1669, DOI 10.1152/ajpcell.00409.2002
   Kelly DP, 2004, GENE DEV, V18, P357, DOI 10.1101/gad.1177604
   Kusuhara K, 2007, BIOL CHEM, V388, P481, DOI 10.1515/BC.2007.052
   Lee WJ, 2006, BIOCHEM BIOPH RES CO, V340, P291, DOI 10.1016/j.bbrc.2005.12.011
   Lin JD, 2005, CELL METAB, V1, P361, DOI 10.1016/j.cmet.2005.05.004
   Miura S, 2008, ENDOCRINOLOGY, V149, P4527, DOI 10.1210/en.2008-0466
   Miura S, 2007, ENDOCRINOLOGY, V148, P3441, DOI 10.1210/en.2006-1646
   Norrbom J, 2004, J APPL PHYSIOL, V96, P189, DOI 10.1152/japplphysiol.00765.2003
   Ojuka EO, 2003, FASEB J, V17, P675, DOI 10.1096/fj.02-0951com
   Pilegaard H, 2003, J PHYSIOL-LONDON, V546, P851, DOI 10.1113/jphysiol.2002.034850
   Puigserver P, 2003, ENDOCR REV, V24, P78, DOI 10.1210/er.2002-0012
   Puigserver P, 2001, MOL CELL, V8, P971, DOI 10.1016/S1097-2765(01)00390-2
   SALTIN B, 1968, CIRCULATION, V38, P1104, DOI 10.1161/01.CIR.38.6.1104
   Sundberg C J, 1994, Acta Physiol Scand Suppl, V615, P1
   Tadaishi M, 2011, AM J PHYSIOL-ENDOC M, V300, pE341, DOI 10.1152/ajpendo.00400.2010
   Vaarmann A, 2008, BBA-BIOENERGETICS, V1777, P39, DOI 10.1016/j.bbabio.2007.11.003
   Williams R. S., 1996, HDB PHYSIOL 12, P1124
   Winder WW, 1996, AM J PHYSIOL-ENDOC M, V270, pE299, DOI 10.1152/ajpendo.1996.270.2.E299
   Winer J, 1999, ANAL BIOCHEM, V270, P41, DOI 10.1006/abio.1999.4085
   Wright DC, 2007, J BIOL CHEM, V282, P18793, DOI 10.1074/jbc.M611252200
   Wu H, 2002, SCIENCE, V296, P349, DOI 10.1126/science.1071163
   Yang J, 2000, CIRC RES, V87, pE61, DOI 10.1161/01.RES.87.12.e61
   Zong HH, 2002, P NATL ACAD SCI USA, V99, P15983, DOI 10.1073/pnas.252625599
NR 39
TC 56
Z9 67
U1 0
U2 8
PU AMER PHYSIOLOGICAL SOC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA
SN 0193-1849
EI 1522-1555
J9 AM J PHYSIOL-ENDOC M
JI Am. J. Physiol.-Endocrinol. Metab.
PD DEC
PY 2011
VL 301
IS 6
BP E1092
EP E1098
DI 10.1152/ajpendo.00119.2011
PG 7
WC Endocrinology & Metabolism; Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism; Physiology
GA 863CT
UT WOS:000298141100006
PM 21862727
DA 2025-04-10
ER

PT J
AU White, AL
   Bix, GJ
AF White, Amanda Louise
   Bix, Gregory Jaye
TI VEGFA Isoforms as Pro-Angiogenic Therapeutics for Cerebrovascular
   Diseases
SO BIOMOLECULES
LA English
DT Review
DE VEGFA; isoforms; cerebral vasculature; angiogenic therapy
ID ENDOTHELIAL GROWTH-FACTOR; CORONARY-ARTERY-DISEASE; FOCAL
   CEREBRAL-ISCHEMIA; GENE-THERAPY; FOLLOW-UP; INTRAMYOCARDIAL INJECTION;
   ENHANCES ANGIOGENESIS; MYOCARDIAL-PERFUSION; LESION MODEL; BRAIN-INJURY
AB Therapeutic angiogenesis has long been considered a viable treatment for vasculature disruptions, including cerebral vasculature diseases. One widely-discussed treatment method to increase angiogenesis is vascular endothelial growth factor (VEGF) A. In animal models, treatment with VEGFA proved beneficial, resulting in increased angiogenesis, increased neuronal density, and improved outcome. However, VEGFA administration in clinical trials has thus far failed to replicate the promising results seen in animal models. The lack of beneficial effects in humans and the difficulty in medicinal translation may be due in part to administration methods and VEGFA's ability to increase vascular permeability. One solution to mitigate the side effects of VEGFA may be found in the VEGFA isoforms. VEGFA is able to produce several different isoforms through alternative splicing. Each VEGFA isoform interacts differently with both the cellular components and the VEGF receptors. Because of the different biological effects elicited, VEGFA isoforms may hold promise as a tangible potential therapeutic for cerebrovascular diseases.
C1 [White, Amanda Louise; Bix, Gregory Jaye] Tulane Univ, Clin Neurosci Res Ctr, Dept Neurosurg, Sch Med, New Orleans, LA 70112 USA.
   [White, Amanda Louise; Bix, Gregory Jaye] Tulane Univ, Tulane Brain Inst, New Orleans, LA 70112 USA.
   [Bix, Gregory Jaye] Tulane Univ, Sch Med, New Orleans, LA 70112 USA.
   [Bix, Gregory Jaye] Tulane Univ, Dept Neurol, Sch Med, New Orleans, LA 70112 USA.
   [Bix, Gregory Jaye] Tulane Univ, Dept Microbiol & Immunol, Sch Med, New Orleans, LA 70112 USA.
   [Bix, Gregory Jaye] Tulane Univ, Sch Publ Hlth & Trop Med, New Orleans, LA 70122 USA.
C3 Tulane University; Tulane University; Tulane University; Tulane
   University; Tulane University; Tulane University
RP Bix, GJ (corresponding author), Tulane Univ, Clin Neurosci Res Ctr, Dept Neurosurg, Sch Med, New Orleans, LA 70112 USA.; Bix, GJ (corresponding author), Tulane Univ, Tulane Brain Inst, New Orleans, LA 70112 USA.; Bix, GJ (corresponding author), Tulane Univ, Sch Med, New Orleans, LA 70112 USA.; Bix, GJ (corresponding author), Tulane Univ, Dept Neurol, Sch Med, New Orleans, LA 70112 USA.; Bix, GJ (corresponding author), Tulane Univ, Dept Microbiol & Immunol, Sch Med, New Orleans, LA 70112 USA.; Bix, GJ (corresponding author), Tulane Univ, Sch Publ Hlth & Trop Med, New Orleans, LA 70122 USA.
EM gbix@tulane.edu
OI Bix, Gregory/0000-0002-8969-9553; White, Amanda/0000-0003-4858-0860
CR Alrafiah A, 2021, J INFLAMM RES, V14, P4893, DOI 10.2147/JIR.S331868
   Anttila V, 2023, MOL THER, V31, P866, DOI 10.1016/j.ymthe.2022.11.017
   Barc P, 2021, J CARDIOVASC TRANSL, V14, P409, DOI 10.1007/s12265-020-10066-9
   Barthels D, 2020, BBA-MOL BASIS DIS, V1866, DOI 10.1016/j.bbadis.2018.09.012
   Becker PM, 2005, CIRC RES, V96, P1257, DOI 10.1161/01.RES.0000171756.13554.49
   Castillo GM, 1998, DIABETES, V47, P612, DOI 10.2337/diabetes.47.4.612
   Clarke DN, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0045257
   Cudmore MJ, 2012, NAT COMMUN, V3, DOI 10.1038/ncomms1977
   Dallinga MG, 2021, CELLS-BASEL, V10, DOI 10.3390/cells10040926
   Deev RV, 2015, J CARDIOVASC PHARM T, V20, P473, DOI 10.1177/1074248415574336
   Delcombel R, 2013, ANGIOGENESIS, V16, P353, DOI 10.1007/s10456-012-9320-y
   Domingues A, 2021, BIOMOLECULES, V11, DOI 10.3390/biom11050666
   Dzietko M, 2013, TRANSL STROKE RES, V4, P189, DOI 10.1007/s12975-012-0221-6
   Eswarappa SM, 2014, CELL, V157, P1605, DOI 10.1016/j.cell.2014.04.033
   Favaloro L, 2013, CATHETER CARDIO INTE, V82, P899, DOI 10.1002/ccd.24555
   Favier B, 2006, BLOOD, V108, P1243, DOI 10.1182/blood-2005-11-4447
   Feigin VL, 2022, INT J STROKE, V17, P18, DOI 10.1177/17474930211065917
   Ferrara N, 1999, KIDNEY INT, V56, P794, DOI 10.1046/j.1523-1755.1999.00610.x
   Gan LS, 2004, ACTA OPHTHALMOL SCAN, V82, P557, DOI 10.1111/j.1600-0420.2004.00312.x
   Geiseler SJ, 2018, INT J MOL SCI, V19, DOI 10.3390/ijms19051362
   Ghori A, 2022, TRANSL STROKE RES, V13, P774, DOI 10.1007/s12975-022-00991-z
   Giacca M, 2012, GENE THER, V19, P622, DOI 10.1038/gt.2012.17
   Giusti II, 2013, HUM GENE THER METHOD, V24, P298, DOI 10.1089/hgtb.2012.221
   Goyal MS, 2018, J PEDIATR GASTR NUTR, V66, pS46, DOI 10.1097/MPG.0000000000001875
   Grammas Paula, 2011, Cleve Clin J Med, V78 Suppl 1, pS50, DOI 10.3949/ccjm.78.s1.09
   Guyot Melanie, 2015, Methods Mol Biol, V1332, P3, DOI 10.1007/978-1-4939-2917-7_1
   Gyöngyösi M, 2005, CIRCULATION, V112, pI157, DOI 10.1161/01.CIRCULATIONAHA.105.525782
   Hayashi T, 1998, J CEREBR BLOOD F MET, V18, P887, DOI 10.1097/00004647-199808000-00009
   Hayes AJ, 2022, FRONT CELL DEV BIOL, V10, DOI 10.3389/fcell.2022.856261
   Hedman M, 2009, GENE THER, V16, P629, DOI 10.1038/gt.2009.4
   Henry TD, 2003, CIRCULATION, V107, P1359, DOI 10.1161/01.CIR.0000061911.47710.8A
   Herrán E, 2014, INT J NANOMED, V9, P2677, DOI 10.2147/IJN.S61940
   Herrán E, 2013, EUR J PHARM BIOPHARM, V85, P1183, DOI 10.1016/j.ejpb.2013.03.034
   Kaji T, 2006, BBA-GEN SUBJECTS, V1760, P1465, DOI 10.1016/j.bbagen.2006.06.010
   Kastrup J, 2011, EUROINTERVENTION, V6, P813, DOI 10.4244/EIJV6I7A140
   Kaya D, 2005, J CEREBR BLOOD F MET, V25, P1111, DOI 10.1038/sj.jcbfm.9600109
   Kofler N, 2016, CURR OPIN HEMATOL, V23, P260, DOI 10.1097/MOH.0000000000000233
   Kühn C, 2019, FRONT PHYSIOL, V10, DOI 10.3389/fphys.2019.00288
   Kukula K, 2019, AM HEART J, V215, P78, DOI 10.1016/j.ahj.2019.06.009
   Lange C, 2016, NAT REV NEUROL, V12, P439, DOI 10.1038/nrneurol.2016.88
   Lee B, 2011, J CLIN INVEST, V121, P3005, DOI 10.1172/JCI46358
   Lee HJ, 2007, PLOS ONE, V2, DOI 10.1371/journal.pone.0000156
   Lei JX, 1998, BBA-GENE STRUCT EXPR, V1443, P400, DOI 10.1016/S0167-4781(98)00240-1
   Lennmyr F, 1998, J NEUROPATH EXP NEUR, V57, P874, DOI 10.1097/00005072-199809000-00009
   Li Z, 2008, NEUROL RES, V30, P868, DOI 10.1179/174313208X309720
   Liu SM, 2019, CNS NEUROSCI THER, V25, P375, DOI 10.1111/cns.13056
   Liu Y, 2021, J CONTROL RELEASE, V338, P610, DOI 10.1016/j.jconrel.2021.08.057
   Lord MS, 2017, J CONTROL RELEASE, V250, P48, DOI 10.1016/j.jconrel.2017.02.009
   Mamer SB, 2020, SCI REP-UK, V10, DOI 10.1038/s41598-020-71484-y
   Manoonkitiwongsa PS, 2006, VASC PHARMACOL, V44, P316, DOI 10.1016/j.vph.2006.01.008
   MARLER JR, 1995, NEW ENGL J MED, V333, P1581, DOI 10.1056/nejm199512143332401
   Melincovici CS, 2018, ROM J MORPHOL EMBRYO, V59, P455
   Mergenthaler P, 2013, TRENDS NEUROSCI, V36, P587, DOI 10.1016/j.tins.2013.07.001
   Mineur P, 2007, J CELL BIOL, V179, P1261, DOI 10.1083/jcb.200703052
   Neufeld G, 1996, CANCER METAST REV, V15, P153, DOI 10.1007/BF00437467
   Olmez I, 2012, NEUROCHEM INT, V60, P208, DOI 10.1016/j.neuint.2011.11.009
   Ourradi K, 2017, RESP RES, V18, DOI 10.1186/s12931-017-0602-1
   Peach CJ, 2018, INT J MOL SCI, V19, DOI 10.3390/ijms19041264
   Petrelis AM, 2022, AGING-US, V14, P2524, DOI 10.18632/aging.203984
   Pikula A, 2013, STROKE, V44, P2768, DOI 10.1161/STROKEAHA.113.001447
   Rhim T, 2013, PHARM RES-DORDR, V30, P2429, DOI 10.1007/s11095-012-0959-2
   Ripa RS, 2006, EUR HEART J, V27, P1785, DOI 10.1093/eurheartj/ehl117
   Rosengart TK, 2013, HUM GENE THER, V24, P203, DOI 10.1089/hum.2012.137
   Sarkar N, 2001, J INTERN MED, V250, P373, DOI 10.1046/j.1365-2796.2001.00905.x
   Shen FX, 2006, STROKE, V37, P2601, DOI 10.1161/01.STR.0000240407.14765.e8
   Shibuya M, 2013, J BIOCHEM, V153, P13, DOI 10.1093/jb/mvs136
   Shibuya M, 2009, FEBS J, V276, P4636, DOI 10.1111/j.1742-4658.2009.07175.x
   Slevin M, 2000, STROKE, V31, P1863, DOI 10.1161/01.STR.31.8.1863
   Stewart DJ, 2006, GENE THER, V13, P1503, DOI 10.1038/sj.gt.3302802
   Sun MJ, 2022, FRONT MOL NEUROSCI, V15, DOI 10.3389/fnmol.2022.937350
   Symes JF, 1999, ANN THORAC SURG, V68, P830, DOI 10.1016/S0003-4975(99)00807-3
   Thau-Zuchman O, 2010, J CEREBR BLOOD F MET, V30, P1008, DOI 10.1038/jcbfm.2009.271
   Tong X, 2019, PREV CHRONIC DIS, V16, DOI 10.5888/pcd16.180411
   Trout AL, 2021, TRANSL STROKE RES, V12, P72, DOI 10.1007/s12975-020-00800-5
   Woolard J, 2009, MICROCIRCULATION, V16, P572, DOI 10.1080/10739680902997333
   Xin H, 2016, CELL, V167, P275, DOI 10.1016/j.cell.2016.08.054
   Yang JP, 2009, NEUROSCI LETT, V461, P212, DOI 10.1016/j.neulet.2009.06.060
   Zhang ZG, 2000, J CLIN INVEST, V106, P829, DOI 10.1172/JCI9369
NR 78
TC 18
Z9 19
U1 2
U2 6
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
EI 2218-273X
J9 BIOMOLECULES
JI Biomolecules
PD APR
PY 2023
VL 13
IS 4
AR 702
DI 10.3390/biom13040702
PG 17
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA E8CX3
UT WOS:000977769200001
PM 37189449
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Matsuyama, M
   Chijiwa, T
   Inoue, Y
   Abe, Y
   Nishi, M
   Miyazaki, N
   Furukawa, D
   Mukai, M
   Suemizu, H
   Sekido, Y
   Ueyama, Y
   Nakamura, M
AF Matsuyama, Masahiro
   Chijiwa, Tsuyosht
   Inoue, Yoshimasa
   Abe, Yoshiyuki
   Nishi, Masatake
   Miyazaki, Noriyuki
   Furukawa, Datsuke
   Mukai, Masaya
   Suemizu, Hiroshi
   Sekido, Yasutomo
   Ueyama, Yoshito
   Nakamura, Masato
TI Alternative splicing variant of vascular endothelial growth factor-A is
   a critical prognostic factor in non-small cell lung cancer
SO ONCOLOGY REPORTS
LA English
DT Article
DE VEGF189; non-small cell lung cancer; prognosis; multivariate analysis
ID INCREASED S100A4 EXPRESSION; FACTOR VEGF; E-CADHERIN; PULMONARY
   ADENOCARCINOMA; EXTRACELLULAR-MATRIX; POOR-PROGNOSIS; MESSENGER-RNA;
   PANCREATIC-CANCER; CARCINOMA-CELLS; FACTOR ISOFORM
AB Lung cancer is one of the most common malignant diseases in the world, and its prognosis is generally poor. Cancer and metastasis involve numerous biological steps, including angiogenesis in both the primary and metastatic sites. Although various molecules that are involved in both tumor neovascularization (angiogenesis) and invasion have been identified, little is known about how these molecules interact in cancerous microenvironments. We previously reported that the gene expressions of some factors associated with vascularization correlated with the prognosis of non-small cell lung cancer (NSCLC). In this study, we performed multivariate analysis of the mRNA levels of 10 selected genes [VEGF-A, VEGF121, VEGF165, VEGF189, S100A4, E-cadherin, Thrombospondin (TSP)-1, TSP-2, matrix metalloproteinase (MMP)-2, and MMP-9] in 130 NSCLC specimens using the real-time quantitative reverse transcription-polymerase chain reaction. Spearman's rank correlation test was used to determine the co-expression patterns. The analysis demonstrated highly significant coexpressions (P<0.0001) among the VEGF isoforms (VEGF-A, VEGF121, VEGF165, and VEGF189). We also analyzed the correlations among the prognosis, gene expressions, clinical factors (age and gender), and pathological features (histological types, TNM status, stages, lymphatic involvement, and venous involvement) using the Cox proportional hazards model. Multivariate analyses showed that only VEGF189 expression was an independent prognostic indicator (P=0.0252). The alternative splicing variant VEGF189, the cell binding isoform, plays a leading role in the progression of NSCLC.
C1 [Chijiwa, Tsuyosht; Miyazaki, Noriyuki; Nakamura, Masato] Tokai Univ, Sch Med, Dept Pathol, Kanagawa 2591193, Japan.
   [Matsuyama, Masahiro; Furukawa, Datsuke] Tokai Univ, Sch Med, Dept Surg, Kanagawa 2591193, Japan.
   [Abe, Yoshiyuki] Tokorozawa PET Diagnost Imaging Clin, Tokorozawa, Saitama 3591124, Japan.
   [Inoue, Yoshimasa; Mukai, Masaya] Tokai Univ, Hachioji Hosp, Dept Surg, Tokyo 1920032, Japan.
   [Sekido, Yasutomo; Ueyama, Yoshito] Tokai Univ, Hachioji Hosp, Dept Pathol, Tokyo 1920032, Japan.
   [Suemizu, Hiroshi; Nakamura, Masato] Cent Inst Expt Anim, Kawasaki Ku, Kanagawa 2160003, Japan.
   [Nishi, Masatake] Undersea Med Ctr, Kanagawa 2390826, Japan.
   [Chijiwa, Tsuyosht] Natl Disaster Med Ctr, Tokyo 1900014, Japan.
C3 Tokai University; Tokai University; Tokai University; Tokai University
RP Nakamura, M (corresponding author), Tokai Univ, Sch Med, Dept Pathol, 143 Shimokasuya, Kanagawa 2591193, Japan.
EM mnakamur@is.icc.u-tokai.ac.jp
OI Inoue, Yoshimasa/0000-0003-0245-5570
FU Grants-in-Aid for Scientific Research [21240042] Funding Source: KAKEN
CR Abe Y, 1996, BRIT J CANCER, V74, P1929, DOI 10.1038/bjc.1996.655
   [Anonymous], 1982, Am J Clin Pathol, V77, P123
   Baillie R, 2001, J CLIN PATHOL, V54, P116, DOI 10.1136/jcp.54.2.116
   BEHRENS J, 1989, J CELL BIOL, V108, P2435, DOI 10.1083/jcb.108.6.2435
   Chijiwa Tsuyoshi, 2009, Int J Oncol, V34, P5
   Chijiwa T, 2009, ONCOL REP, V22, P279, DOI 10.3892/or_00000435
   Decaussin M, 1999, J PATHOL, V188, P369
   FERRARA N, 1991, J CELL BIOCHEM, V47, P211, DOI 10.1002/jcb.240470305
   Fontanini G, 1999, BRIT J CANCER, V79, P363, DOI 10.1038/sj.bjc.6690058
   FRIXEN UH, 1991, J CELL BIOL, V113, P173, DOI 10.1083/jcb.113.1.173
   GOOD DJ, 1990, P NATL ACAD SCI USA, V87, P6624, DOI 10.1073/pnas.87.17.6624
   Han H, 2001, ANN SURG ONCOL, V8, P72, DOI 10.1245/aso.2001.8.1.72
   HOUCK KA, 1991, MOL ENDOCRINOL, V5, P1806, DOI 10.1210/mend-5-12-1806
   Inoue K, 1997, CANCER, V79, P206, DOI 10.1002/(SICI)1097-0142(19970115)79:2<206::AID-CNCR2>3.0.CO;2-I
   Kamochi J, 2003, ONCOL REP, V10, P881
   Kazuno M, 1999, EUR J CANCER, V35, P502, DOI 10.1016/S0959-8049(98)00374-8
   Kim MS, 2006, BRIT J DERMATOL, V155, P1131, DOI 10.1111/j.1365-2133.2006.07510.x
   Kyriakides TR, 2001, AM J PATHOL, V159, P1255, DOI 10.1016/S0002-9440(10)62512-6
   Kyriakides TR, 1998, J HISTOCHEM CYTOCHEM, V46, P1007, DOI 10.1177/002215549804600904
   Lawler J, 2000, CURR OPIN CELL BIOL, V12, P634, DOI 10.1016/S0955-0674(00)00143-5
   Lee YH, 1999, EUR J CANCER, V35, P1089, DOI 10.1016/S0959-8049(99)00073-8
   Maelandsmo GM, 1996, CANCER RES, V56, P5490
   Miyazaki N, 2006, INT J ONCOL, V28, P1369
   Nakamura M, 2008, MOL MED REP, V1, P423
   Nishi M, 2005, INT J ONCOL, V26, P1517
   O'Byrne KJ, 2000, BRIT J CANCER, V82, P1427, DOI 10.1054/bjoc.1999.1129
   Oida Y, 2006, ONCOL REP, V16, P457
   Oshika Y, 2000, EUR J CANCER, V36, P2390, DOI 10.1016/S0959-8049(00)00343-9
   Oshika Y, 1998, INT J ONCOL, V12, P541
   Oshika Y, 1998, CLIN CANCER RES, V4, P1785
   PARK JE, 1993, MOL BIOL CELL, V4, P1317, DOI 10.1091/mbc.4.12.1317
   Poltorak Z, 1997, J BIOL CHEM, V272, P7151, DOI 10.1074/jbc.272.11.7151
   Schafer BW, 1996, TRENDS BIOCHEM SCI, V21, P134, DOI 10.1016/0968-0004(96)10020-7
   Stefanou D, 2004, HISTOL HISTOPATHOL, V19, P37, DOI 10.14670/HH-19.37
   Streit M, 1999, P NATL ACAD SCI USA, V96, P14888, DOI 10.1073/pnas.96.26.14888
   TAKEICHI M, 1991, SCIENCE, V251, P1451, DOI 10.1126/science.2006419
   Takenaga K, 1997, ONCOGENE, V14, P331, DOI 10.1038/sj.onc.1200820
   Tokunaga T, 1998, BRIT J CANCER, V77, P998, DOI 10.1038/bjc.1998.164
   Tokunaga T, 1999, BRIT J CANCER, V79, P354, DOI 10.1038/sj.bjc.6690056
   TOLSMA SS, 1993, J CELL BIOL, V122, P497, DOI 10.1083/jcb.122.2.497
   Tomii Y, 2002, INT J ONCOL, V21, P1251
   Tomisawa M, 1999, EUR J CANCER, V35, P133, DOI 10.1016/S0959-8049(98)00278-0
   Van Trappen PO, 2002, BRIT J CANCER, V87, P537, DOI 10.1038/sj.bjc.6600471
   Veikkola T, 1999, SEMIN CANCER BIOL, V9, P211, DOI 10.1006/scbi.1998.0091
   Werb Z, 1999, APMIS, V107, P11, DOI 10.1111/j.1699-0463.1999.tb01521.x
   WHEELOCK MJ, 1992, J CELL BIOL, V117, P415, DOI 10.1083/jcb.117.2.415
   Yancopoulos GD, 2000, NATURE, V407, P242, DOI 10.1038/35025215
   Yuan A, 2001, J CLIN ONCOL, V19, P432, DOI 10.1200/JCO.2001.19.2.432
NR 48
TC 13
Z9 16
U1 0
U2 5
PU SPANDIDOS PUBL LTD
PI ATHENS
PA POB 18179, ATHENS, 116 10, GREECE
SN 1021-335X
EI 1791-2431
J9 ONCOL REP
JI Oncol. Rep.
PD DEC
PY 2009
VL 22
IS 6
BP 1407
EP 1413
DI 10.3892/or_00000582
PG 7
WC Oncology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Oncology
GA 518YN
UT WOS:000271732300020
PM 19885594
OA Bronze
DA 2025-04-10
ER

PT J
AU Fukuda, N
   Granzier, HL
   Ishiwata, S
   Kurihara, S
AF Fukuda, Norio
   Granzier, Henk L.
   Ishiwata, Shin'ichi
   Kurihara, Satoshi
TI Physiological functions of the giant elastic protein titin in mammalian
   striated muscle
SO JOURNAL OF PHYSIOLOGICAL SCIENCES
LA English
DT Review
DE skinned muscle; cardiac muscle; skeletal muscle; Ca2(+); connectin
ID FRANK-STARLING MECHANISM; SKINNED CARDIAC-MUSCLE; LENGTH-DEPENDENT
   ACTIVATION; BETA-ADRENERGIC STIMULATION; RAT VENTRICULAR MUSCLE; FAILING
   HUMAN HEART; SKELETAL-MUSCLE; PASSIVE TENSION; THICK FILAMENTS;
   TROPONIN-I
AB The striated muscle sarcomere contains the third filament comprising the giant elastic protein titin, in addition to thick and thin filaments. Titin is the primary source of nonactomyosin-based passive force in both skeletal and cardiac muscles, within the physiological sarcomere length range. Titin's force repositions the thick filaments in the center of the sarcomere after contraction or stretch and thus maintains sarcomere length and structural integrity. In the heart, titin determines myocardial wall stiffness, thereby regulating ventricular filling. Recent studies have revealed the mechanisms involved in the fine tuning of titin-based passive force via alternative splicing or posttranslational modification. It has also been discovered that titin performs roles that go beyond passive force generation, such as a regulation of the Frank-Starling mechanism of the heart. In this review, we discuss how titin regulates passive and active properties of striated muscle during normal muscle function and during disease.
C1 [Fukuda, Norio] Jikei Univ, Sch Med, Dept Cell Physiol, Minato Ku, Tokyo 1058461, Japan.
   [Granzier, Henk L.] Univ Arizona, Dept Mol & Cellular Biol, Tucson, AZ 85724 USA.
   [Ishiwata, Shin'ichi] Waseda Univ, Dept Phys, Tokyo 1698555, Japan.
C3 Jikei University; University of Arizona; Waseda University
RP Fukuda, N (corresponding author), Jikei Univ, Sch Med, Dept Cell Physiol, Minato Ku, 3-25-8 Nishi Shinbashi, Tokyo 1058461, Japan.
EM noriof@jikei.ac.jp
CR ALLEN DG, 1982, J PHYSIOL-LONDON, V327, P79, DOI 10.1113/jphysiol.1982.sp014221
   Altman P.L., 1974, BIOL DATA BOOK
   Arteaga GM, 2000, J PHYSIOL-LONDON, V526, P541, DOI 10.1111/j.1469-7793.2000.t01-1-00541.x
   Bers D. M., 2001, EXCITATION CONTRACTI
   Bodine SC, 2001, SCIENCE, V294, P1704, DOI 10.1126/science.1065874
   Cazorla O, 1999, J MOL CELL CARDIOL, V31, P1215, DOI 10.1006/jmcc.1999.0954
   Cazorla O, 2000, CIRC RES, V86, P59, DOI 10.1161/01.RES.86.1.59
   Cazorla O, 2001, CIRC RES, V88, P1028, DOI 10.1161/hh1001.090876
   Cohen MV, 2000, ANNU REV PHYSIOL, V62, P79, DOI 10.1146/annurev.physiol.62.1.79
   ENDOH M, 1995, GEN PHARMACOL, V26, P1, DOI 10.1016/0306-3623(94)00144-C
   ENDOH M, 1988, CIRC RES, V62, P247, DOI 10.1161/01.RES.62.2.247
   Fitts RH, 2000, J APPL PHYSIOL, V89, P823, DOI 10.1152/jappl.2000.89.2.823
   Fukuda N, 2005, J GEN PHYSIOL, V125, P257, DOI 10.1085/jgp.200409177
   Fukuda N, 2003, J PHYSIOL-LONDON, V553, P147, DOI 10.1113/jphysiol.2003.049759
   Fukuda N, 2001, J PHYSIOL-LONDON, V536, P153, DOI 10.1111/j.1469-7793.2001.00153.x
   Fukuda N, 2001, CIRCULATION, V104, P1639, DOI 10.1161/hc3901.095898
   Fukuda N, 1998, J MUSCLE RES CELL M, V19, P909, DOI 10.1023/A:1005437517287
   Fukuda N, 2000, CIRC RES, V86, pE1
   FUKUDA N, 2005, PFLUGERS ARCH, V44, P449
   Fukuda N, 2008, CIRC RES, V102, P148, DOI 10.1161/CIRCRESAHA.107.170266
   Fukuda N, 2005, J MUSCLE RES CELL M, V26, P319, DOI 10.1007/s10974-005-9038-1
   Fukuda N, 2004, CURR VASC PHARMACOL, V2, P135, DOI 10.2174/1570161043476357
   FUNATSU T, 1993, J CELL BIOL, V120, P711, DOI 10.1083/jcb.120.3.711
   FUNATSU T, 1990, J CELL BIOL, V110, P53, DOI 10.1083/jcb.110.1.53
   Glass DJ, 2003, NAT CELL BIOL, V5, P87, DOI 10.1038/ncb0203-87
   Goto K, 2003, J APPL PHYSIOL, V94, P897, DOI 10.1152/japplphysiol.00408.2002
   Granzier H, 2005, HEART FAIL REV, V10, P211, DOI 10.1007/s10741-005-5251-7
   Granzier H, 2002, J PHYSIOL-LONDON, V541, P335, DOI 10.1113/jphysiol.2001.014381
   Granzier H, 2007, MUSCLE NERVE, V36, P740, DOI 10.1002/mus.20886
   GRANZIER HL, 1995, BIOPHYS J, V68, P1027, DOI 10.1016/S0006-3495(95)80278-X
   Granzier HL, 2004, CIRC RES, V94, P284, DOI 10.1161/01.RES.0000117769.88862.F8
   Gregorio CC, 1999, CURR OPIN CELL BIOL, V11, P18, DOI 10.1016/S0955-0674(99)80003-9
   HANSON J, 1953, NATURE, V172, P530, DOI 10.1038/172530b0
   Helmes M, 2003, J GEN PHYSIOL, V121, P97, DOI 10.1085/jgp.20028652
   Helmes M, 1999, CIRC RES, V84, P1339, DOI 10.1161/01.RES.84.11.1339
   Helmes M, 1996, CIRC RES, V79, P619, DOI 10.1161/01.RES.79.3.619
   HIBBERD MG, 1982, J PHYSIOL-LONDON, V329, P527, DOI 10.1113/jphysiol.1982.sp014317
   HIDALGO HG, 2008, BIOPHYS J S, V94, P1436
   HIGUCHI H, 1986, BIOPHYS J, V50, P385, DOI 10.1016/S0006-3495(86)83474-9
   HOROWITS R, 1987, J CELL BIOL, V105, P2217, DOI 10.1083/jcb.105.5.2217
   HOROWITS R, 1986, NATURE, V323, P160, DOI 10.1038/323160a0
   HUXLEY AF, 1957, PROG BIOPHYS MOL BIO, V7, P255, DOI 10.1016/S0096-4174(18)30128-8
   HUXLEY AF, 1961, J PHYSIOL-LONDON, V156, P150, DOI 10.1113/jphysiol.1961.sp006665
   HUXLEY AF, 1954, NATURE, V173, P971, DOI 10.1038/173971a0
   HUXLEY HE, 1969, SCIENCE, V164, P1356, DOI 10.1126/science.164.3886.1356
   Jackman RW, 2004, AM J PHYSIOL-CELL PH, V287, pC834, DOI 10.1152/ajpcell.00579.2003
   Katz AM, 2002, CIRCULATION, V106, P2986, DOI 10.1161/01.CIR.0000040594.96123.55
   Kellermayer MSZ, 1997, SCIENCE, V276, P1112, DOI 10.1126/science.276.5315.1112
   KENTISH JC, 1986, CIRC RES, V58, P755, DOI 10.1161/01.RES.58.6.755
   Konhilas JP, 2002, CIRC RES, V90, P59, DOI 10.1161/hh0102.102269
   Krüger M, 2006, J MUSCLE RES CELL M, V27, P435, DOI 10.1007/s10974-006-9090-5
   Kulke M, 2001, CIRC RES, V89, P874, DOI 10.1161/hh2201.099453
   KURIHARA S, 1987, PFLUG ARCH EUR J PHY, V409, P427, DOI 10.1007/BF00583798
   LABEIT S, 1992, EMBO J, V11, P1711, DOI 10.1002/j.1460-2075.1992.tb05222.x
   LABEIT S, 1995, SCIENCE, V270, P293, DOI 10.1126/science.270.5234.293
   Lange S, 2005, SCIENCE, V308, P1599, DOI 10.1126/science.1110463
   Li HB, 2002, NATURE, V418, P998, DOI 10.1038/nature00938
   Li L, 2000, AM J PHYSIOL-HEART C, V278, pH769, DOI 10.1152/ajpheart.2000.278.3.H769
   Linke WA, 1999, J CELL BIOL, V146, P631, DOI 10.1083/jcb.146.3.631
   Linke WA, 2008, CARDIOVASC RES, V77, P637, DOI 10.1016/j.cardiores.2007.03.029
   Littlefield R, 1998, ANNU REV CELL DEV BI, V14, P487, DOI 10.1146/annurev.cellbio.14.1.487
   LOCKER RH, 1976, MEAT SCI, V1, P87
   Lynch GS, 2006, PHARMACOL THERAPEUT, V113, P461
   MARUYAMA K, 1985, J CELL BIOL, V101, P2167, DOI 10.1083/jcb.101.6.2167
   MARUYAMA K, 1976, J BIOCHEM, V80, P405, DOI 10.1093/oxfordjournals.jbchem.a131291
   MARUYAMA K, 1976, NATURE, V262, P58, DOI 10.1038/262058a0
   Mayans O, 1998, NATURE, V395, P863, DOI 10.1038/27603
   MORANO I, 1994, J MOL CELL CARDIOL, V26, P361, DOI 10.1006/jmcc.1994.1045
   Muhle-Goll C, 2001, J MOL BIOL, V313, P431, DOI 10.1006/jmbi.2001.5017
   NAGATA K, 1995, J AM COLL CARDIOL, V25, P295, DOI 10.1016/0735-1097(94)00369-2
   Nagueh SF, 2004, CIRCULATION, V110, P155, DOI 10.1161/01.CIR.0000135591.37759.AF
   NAIR P, 2005, J MUSCLE RES CELL M, V26, P307
   Neagoe C, 2002, CIRCULATION, V106, P1333, DOI 10.1161/01.CIR.0000029803.93022.93
   Ono Y, 2004, J BIOL CHEM, V279, P2761, DOI 10.1074/jbc.M308789200
   PARKER JD, 1991, CIRCULATION, V84, P1040, DOI 10.1161/01.CIR.84.3.1040
   Rief M, 1997, SCIENCE, V276, P1109, DOI 10.1126/science.276.5315.1109
   SALYERS AK, 1988, J PHARMACOL METHOD, V19, P267, DOI 10.1016/0160-5402(88)90029-0
   SCHWINGER RHG, 1994, CIRC RES, V74, P959, DOI 10.1161/01.RES.74.5.959
   SUGDEN PH, 1995, CARDIOVASC RES, V30, P478, DOI 10.1016/0008-6363(95)00096-8
   Tachampa K, 2007, CIRC RES, V101, P1081, DOI 10.1161/CIRCRESAHA.107.165258
   Terui T, 2008, J GEN PHYSIOL, V131, P275, DOI 10.1085/jgp.200709895
   Toursel T, 2002, J APPL PHYSIOL, V92, P1465, DOI 10.1152/japplphysiol.00621.2001
   TRINICK J, 1994, TRENDS BIOCHEM SCI, V19, P405, DOI 10.1016/0968-0004(94)90088-4
   Trombitás K, 1999, BIOPHYS J, V77, P3189, DOI 10.1016/S0006-3495(99)77149-3
   Trombitas K, 1997, AM J PHYSIOL-CELL PH, V273, pC662, DOI 10.1152/ajpcell.1997.273.2.C662
   Trombitás K, 2003, BIOPHYS J, V85, P3142, DOI 10.1016/S0006-3495(03)74732-8
   Tskhovrebova L, 1997, NATURE, V387, P308, DOI 10.1038/387308a0
   Udaka J, 2008, J GEN PHYSIOL, V131, P33, DOI 10.1085/jgp.200709888
   UDELSON JE, 1989, CIRCULATION, V79, P371, DOI 10.1161/01.CIR.79.2.371
   van der Ven PFM, 2000, J CELL SCI, V113, P1405
   WAKABAYASHI K, 1994, BIOPHYS J, V67, P2422, DOI 10.1016/S0006-3495(94)80729-5
   WANG K, 1979, P NATL ACAD SCI USA, V76, P3698, DOI 10.1073/pnas.76.8.3698
   Warren CM, 2003, CARDIOVASC RES, V59, P86, DOI 10.1016/S0008-6363(03)00328-6
   WHITING A, 1989, J MOL BIOL, V205, P263, DOI 10.1016/0022-2836(89)90381-1
   Witt SH, 2005, J MOL BIOL, V350, P713, DOI 10.1016/j.jmb.2005.05.021
   Wu YM, 2002, CIRCULATION, V106, P1384, DOI 10.1161/01.CIR.0000029804.61510.02
   Wu YM, 2000, J MOL CELL CARDIOL, V32, P2151, DOI 10.1006/jmcc.2000.1281
   Yamasaki R, 2002, CIRC RES, V90, P1181, DOI 10.1161/01.RES.0000021115.24712.99
NR 98
TC 73
Z9 90
U1 0
U2 12
PU SPRINGER JAPAN KK
PI TOKYO
PA CHIYODA FIRST BLDG EAST, 3-8-1 NISHI-KANDA, CHIYODA-KU, TOKYO, 101-0065,
   JAPAN
SN 1880-6546
EI 1880-6562
J9 J PHYSIOL SCI
JI J. Physiol. Sci.
PD JUN
PY 2008
VL 58
IS 3
BP 151
EP 159
DI 10.2170/physiolsci.RV005408
PG 9
WC Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Physiology
GA 320XB
UT WOS:000257267400001
PM 18477421
OA gold
DA 2025-04-10
ER

PT J
AU Miranda, ER
   Mey, JT
   Blackburn, BK
   Chaves, AB
   Fuller, KNZ
   Perkins, RK
   Ludlow, AT
   Haus, JM
AF Miranda, Edwin R.
   Mey, Jacob T.
   Blackburn, Brian K.
   Chaves, Alec B.
   Fuller, Kelly N. Z.
   Perkins, Ryan K.
   Ludlow, Andrew T.
   Haus, Jacob M.
TI Soluble RAGE and skeletal muscle tissue RAGE expression profiles in lean
   and obese young adults across differential aerobic exercise intensities
SO JOURNAL OF APPLIED PHYSIOLOGY
LA English
DT Article
DE advanced glycation endproducts; exerkines; inflammation
ID GLYCATION END-PRODUCTS; MEDICAL WEIGHT MANAGEMENT;
   CORONARY-ARTERY-DISEASE; DIABETIC-NEPHROPATHY; CARBOXYMETHYL-LYSINE;
   SERUM-LEVELS; CARDIOVASCULAR-DISEASE; DEGRADATION-PRODUCTS;
   INSULIN-RESISTANCE; METABOLIC SYNDROME
AB Nearly 40% of Americans have obesity and are at increased risk for developing type 2 diabetes. Skeletal muscle is responsible for >80% of insulin-stimulated glucose uptake that is attenuated by the inflammatory milieu of obesity and augmented by aerobic exercise. The receptor for advanced glycation endproducts (RAGE) is an inflammatory receptor directly linking metabolic dysfunction with inflammation. Circulating soluble isoforms of RAGE (sRAGE) formed either by proteolytic cleavage (cRAGE) or alternative splicing (esRAGE) act as decoys for RAGE ligands, thereby counteracting RAGE-mediated inflammation. We aimed to determine if RAGE expression or alternative splicing of RAGE is altered by obesity in muscle, and whether acute aerobic exercise (AE) modifies RAGE and sRAGE. Young (20-34 yr) participants without [n = 17; body mass index (BMI): 22.6 +/- 2.6 kg/m(2)] and with obesity (n = 7; BMI: 32.8 +/- 2.9 kg/m(2)) performed acute aerobic exercise (AE) at 40%, 65%, or 80% of maximal aerobic capacity (Vo(2max); mL/kg/min) on separate visits. Blood was taken before and 30 min after each AE bout. Muscle biopsy samples were taken before, 30 min, and 3 h after the 80% Vo(2max) AE bout. Individuals with obesity had higher total RAGE and esRAGE mRNA and RAGE protein (P < 0.0001). In addition, RAGE and esRAGE transcripts correlated to transcripts of the NF-kappa B subunit P65 (P < 0.05). There was no effect of AE on total RAGE or esRAGE transcripts, or RAGE protein (P > 0.05), and AE tended to decrease circulating sRAGE in particular at lower intensities of exercise. RAGE expression is exacerbated in skeletal muscle with obesity, which may contribute to muscle inflammation via NF-kappa B. Future work should investigate the consequences of increased skeletal muscle RAGE on the development of obesity-related metabolic dysfunction and potential mitigating strategies.
C1 [Miranda, Edwin R.; Ludlow, Andrew T.; Haus, Jacob M.] Univ Michigan, Sch Kinesiol, Ann Arbor, MI 48109 USA.
   [Haus, Jacob M.] Univ Illinois, Appl Hlth Sci, Chicago, IL 60607 USA.
   [Miranda, Edwin R.] Univ Utah, Dept Nutr & Integrat Physiol, Salt Lake City, UT USA.
   [Mey, Jacob T.] Pennington Biomed Res Ctr, Integrated Physiol & Mol Metab, Baton Rouge, LA USA.
   [Blackburn, Brian K.] Humboldt State Univ, Appl Hlth Sci & Kinesiol, Arcata, CA USA.
   [Chaves, Alec B.] Duke Univ, Duke Mol Physiol Inst, Sarah W Stedman Nutr & Metab Ctr, Durham, NC USA.
   [Fuller, Kelly N. Z.] Univ Colorado, Dept Pediat, Div Endocrinol, Anschutz Med Campus, Aurora, CO USA.
   [Perkins, Ryan K.] Calif State Univ, Dept Kinesiol, Chico, CA USA.
C3 University of Michigan System; University of Michigan; University of
   Illinois System; University of Illinois Chicago; University of Illinois
   Chicago Hospital; Utah System of Higher Education; University of Utah;
   Louisiana State University System; Louisiana State University;
   Pennington Biomedical Research Center; California State University
   System; California State Polytechnic University, Humboldt; Duke
   University; University of Colorado System; University of Colorado
   Anschutz Medical Campus
RP Haus, JM (corresponding author), Univ Michigan, Sch Kinesiol, Ann Arbor, MI 48109 USA.; Haus, JM (corresponding author), Univ Illinois, Appl Hlth Sci, Chicago, IL 60607 USA.
EM jmhaus@umich.edu
OI Perkins, Ryan/0000-0002-2546-4085; Chaves, Alec/0000-0002-3117-9256;
   Mey, Jacob/0000-0001-6826-7762
FU American Diabetes AssociationJunior Faculty Award [1-14-JF-32]; NIH [R01
   DK109948]
FX This work was supported by an American Diabetes AssociationJunior
   Faculty Award 1-14-JF-32 (J.M.H.) and NIH R01 DK109948 (J.M.H.).
CR Ahmed N, 2005, DIABETES CARE, V28, P2465, DOI 10.2337/diacare.28.10.2465
   Ahmed N, 2005, DIABETOLOGIA, V48, P1590, DOI 10.1007/s00125-005-1810-7
   Ahmed N, 2005, DIABETES RES CLIN PR, V67, P3, DOI 10.1016/j.diabres.2004.09.004
   Basta G, 2006, J CLIN ENDOCR METAB, V91, P4628, DOI 10.1210/jc.2005-2559
   Beisswenger PJ, 2013, DIABETES CARE, V36, P3234, DOI 10.2337/dc12-2689
   BEISSWENGER PJ, 1995, DIABETES, V44, P824, DOI 10.2337/diabetes.44.7.824
   Chaves AB, 2022, J APPL PHYSIOL, V132, P357, DOI 10.1152/japplphysiol.00229.2021
   Choi KM, 2012, J CLIN ENDOCR METAB, V97, P3751, DOI 10.1210/jc.2012-1951
   Coughlan MT, 2011, AM J NEPHROL, V34, P347, DOI 10.1159/000331064
   Dalal M, 2009, J GERONTOL A-BIOL, V64, P132, DOI 10.1093/gerona/gln018
   Danzig V, 2010, PHYSIOL RES, V59, P385, DOI 10.33549/physiolres.931764
   DeFronzo RA, 2009, DIABETES, V58, P773, DOI 10.2337/db09-9028
   DeGroot J, 2001, ARTHRITIS RHEUM, V44, P2562, DOI 10.1002/1529-0131(200111)44:11<2562::AID-ART437>3.0.CO;2-1
   del Pozo CH, 2019, CELL REP, V28, P773, DOI 10.1016/j.celrep.2019.06.061
   Di Pino A, 2016, J CLIN ENDOCR METAB, V101, P1701, DOI 10.1210/jc.2015-4069
   DILL DB, 1974, J APPL PHYSIOL, V37, P247, DOI 10.1152/jappl.1974.37.2.247
   Ding T, 2017, CELL PHYSIOL BIOCHEM, V41, P1035, DOI 10.1159/000461483
   Dorneles GP, 2017, OXID MED CELL LONGEV, V2017, DOI 10.1155/2017/1530230
   Dozio E, 2017, EUR J NUTR, V56, P2557, DOI 10.1007/s00394-016-1291-0
   DUNN JA, 1989, BIOCHEMISTRY-US, V28, P9464, DOI 10.1021/bi00450a033
   DUNN JA, 1991, BIOCHEMISTRY-US, V30, P1205, DOI 10.1021/bi00219a007
   DYER DG, 1993, J CLIN INVEST, V91, P2463, DOI 10.1172/JCI116481
   Villegas-Rodríguez ME, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0159175
   Falcone C, 2005, ARTERIOSCL THROM VAS, V25, P1032, DOI 10.1161/01.ATV.0000160342.20342.00
   Feng ZQ, 2021, CELL DEATH DISCOV, V7, DOI 10.1038/s41420-021-00711-w
   Fuller KNZ, 2018, PHYSIOL REP, V6, DOI 10.14814/phy2.13811
   Gaens KHJ, 2014, ARTERIOSCL THROM VAS, V34, P1199, DOI 10.1161/ATVBAHA.113.302281
   Gurecká R, 2016, GLYCOCONJUGATE J, V33, P599, DOI 10.1007/s10719-016-9696-9
   Haus JM, 2007, J APPL PHYSIOL, V103, P2068, DOI 10.1152/japplphysiol.00670.2007
   Horwitz D, 2016, SURG OBES RELAT DIS, V12, P1337, DOI 10.1016/j.soard.2016.01.016
   Hudson BI, 2008, FASEB J, V22, P1572, DOI 10.1096/fj.07-9909com
   Humpert PM, 2006, DIABETES CARE, V29, P1111, DOI 10.2337/dc05-2478
   Inman CK, 2017, J CLIN TRANSL ENDOCR, V10, P1, DOI 10.1016/j.jcte.2017.08.001
   Kanikowska D, 2022, J PHYSIOL PHARMACOL, V73, P531, DOI 10.26402/jpp.2022.4.06
   Katakami N, 2005, DIABETES CARE, V28, P2716, DOI 10.2337/diacare.28.11.2716
   Klein R, 2017, DIABETES CARE, V40, pE117, DOI 10.2337/dc17-0421
   Koska J, 2018, DIABETES CARE, V41, P570, DOI 10.2337/dc17-1740
   Kotani Kazuhiko, 2011, J Clin Med Res, V3, P252, DOI 10.4021/jocmr704w
   Koyama H, 2005, ARTERIOSCL THROM VAS, V25, P2587, DOI 10.1161/01.ATV.0000190660.32863.cd
   Larson C, 2020, INT J ENV RES PUB HE, V17, DOI 10.3390/ijerph17165740
   Legaard GE, 2022, FREE RADICAL BIO MED, V188, P328, DOI 10.1016/j.freeradbiomed.2022.06.013
   López-Díez R, 2017, ARTERIOSCL THROM VAS, V37, P1536, DOI 10.1161/ATVBAHA.117.309714
   Maessen DE, 2016, DIABETES, V65, P956, DOI 10.2337/db15-1390
   Maessen DE, 2015, DIABETES CARE, V38, P913, DOI 10.2337/dc14-2605
   Martínez-Redondo V, 2015, DIABETOLOGIA, V58, P1969, DOI 10.1007/s00125-015-3671-z
   Mazo Corey E, 2022, Brain Plast, V8, P5, DOI 10.3233/BPL-220137
   Metz VV, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0041823
   Miranda ER, 2018, NUTR METAB CARDIOVAS, V28, P1155, DOI 10.1016/j.numecd.2018.07.009
   Miranda ER, 2017, AM J PHYSIOL-ENDOC M, V313, pE631, DOI 10.1152/ajpendo.00146.2017
   Miranda ER, 2017, FASEB J, V31
   Motawi TM, 2013, BMC ENDOCR DISORD, V13, DOI 10.1186/1472-6823-13-32
   Nakamura K, 2007, MOL MED, V13, P185, DOI 10.2119/2006-00090.Nakamura
   Nielsen TB, 2017, MBIO, V8, DOI 10.1128/mBio.00818-17
   Nin JWM, 2009, DIABETOLOGIA, V52, P705, DOI 10.1007/s00125-009-1263-5
   Olekson MP, 2016, ADV WOUND CARE, V5, P527, DOI 10.1089/wound.2015.0674
   Parikh M, 2014, ANN SURG, V260, P617, DOI 10.1097/SLA.0000000000000919
   Park GB, 2017, MOL CELL BIOCHEM, V425, P191, DOI 10.1007/s11010-016-2873-0
   Perkins BA, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0035655
   Perkins RK, 2020, J APPL PHYSIOL, V129, P1483, DOI 10.1152/japplphysiol.00615.2020
   Perkins RK, 2019, NUTRIENTS, V11, DOI 10.3390/nu11030532
   Petersen AMW, 2005, J APPL PHYSIOL, V98, P1154, DOI 10.1152/japplphysiol.00164.2004
   Popp CJ, 2022, CURR DEV NUTR, V6, DOI 10.1093/cdn/nzac046
   Rabbani N, 2019, ANTIOXID REDOX SIGN, V30, P354, DOI 10.1089/ars.2017.7424
   Raffield LM, 2021, J AM HEART ASSOC, V10, DOI 10.1161/JAHA.121.019946
   Raucci A, 2008, FASEB J, V22, P3716, DOI 10.1096/fj.08-109033
   Riuzzi F, 2018, J CACHEXIA SARCOPENI, V9, P1213, DOI 10.1002/jcsm.12350
   Riuzzi F, 2012, J CELL SCI, V125, P1440, DOI 10.1242/jcs.092163
   Ruiz HH, 2021, INT J OBESITY, V45, P2083, DOI 10.1038/s41366-021-00878-3
   Sagheddu R, 2018, HUM MOL GENET, V27, P3734, DOI 10.1093/hmg/ddy288
   Santilli F, 2013, THROMB HAEMOSTASIS, V110, P1232, DOI 10.1160/TH13-04-0295
   Sayed ME, 2019, J BIOL CHEM, V294, P11579, DOI 10.1074/jbc.RA118.007234
   SCHMIDT AM, 1994, ARTERIOSCLER THROMB, V14, P1521, DOI 10.1161/01.ATV.14.10.1521
   SCHMIDT AM, 1995, J CLIN INVEST, V96, P1395, DOI 10.1172/JCI118175
   Schmidt AM, 2001, J CLIN INVEST, V108, P949, DOI 10.1172/JCI14002
   Semba RD, 2015, J HYPERTENS, V33, P797, DOI 10.1097/HJH.0000000000000460
   Semba RD, 2009, J AM GERIATR SOC, V57, P1874, DOI 10.1111/j.1532-5415.2009.02438.x
   Slusher AL, 2022, MED SCI SPORT EXER, V54, P931, DOI 10.1249/MSS.0000000000002868
   Song F, 2014, DIABETES, V63, P1948, DOI 10.2337/db13-1636
   Su XD, 2011, ARCH MED RES, V42, P596, DOI 10.1016/j.arcmed.2011.11.001
   Tam XHL, 2011, CLIN SCI, V120, P81, DOI 10.1042/CS20100256
   Tan KCB, 2006, DIABETOLOGIA, V49, P2756, DOI 10.1007/s00125-006-0394-1
   Van den Eynde MDG, 2021, CLIN NUTR, V40, P2654, DOI 10.1016/j.clnu.2021.03.042
   Wang YJ, 2010, J IMMUNOL, V185, P1822, DOI 10.4049/jimmunol.0903398
   Wautier MP, 2001, AM J PHYSIOL-ENDOC M, V280, pE685, DOI 10.1152/ajpendo.2001.280.5.E685
   Wendt T, 2006, ATHEROSCLEROSIS, V185, P70, DOI 10.1016/j.atherosclerosis.2005.06.013
   Wu HZ, 2017, J CLIN INVEST, V127, P43, DOI [10.1172/JCI88880, 10.1172/jci88880]
   Yao DC, 2010, DIABETES, V59, P249, DOI 10.2337/db09-0801
   Yonekura H, 2003, BIOCHEM J, V370, P1097, DOI 10.1042/BJ20021371
   Zaki M, 2017, EXCLI J, V16, P973, DOI 10.17179/excli2017-275
   Zhang L, 2008, J BIOL CHEM, V283, P35507, DOI 10.1074/jbc.M806948200
   Zhang T, 2014, J GERONTOL A-BIOL, V69, P1437, DOI 10.1093/gerona/glt204
NR 91
TC 6
Z9 6
U1 4
U2 5
PU AMER PHYSIOLOGICAL SOC
PI Rockville
PA 6120 Executive Blvd, Suite 600, Rockville, MD, UNITED STATES
SN 8750-7587
EI 1522-1601
J9 J APPL PHYSIOL
JI J. Appl. Physiol.
PD OCT 7
PY 2023
VL 135
IS 4
BP 849
EP 862
DI 10.1152/japplphysiol.00748.2022
PG 14
WC Physiology; Sport Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Physiology; Sport Sciences
GA FD2G6
UT WOS:001143747400002
PM 37675469
OA Green Published
DA 2025-04-10
ER

PT J
AU Cunha, SR
   Mohler, PJ
AF Cunha, Shane R.
   Mohler, Peter J.
TI Obscurin Targets Ankyrin-B and Protein Phosphatase 2A to the Cardiac
   M-line
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID HUMAN ERYTHROCYTE ANKYRIN; AXON INITIAL SEGMENTS; C-TERMINAL DOMAIN;
   SARCOPLASMIC-RETICULUM; NEONATAL CARDIOMYOCYTES; SKELETAL-MUSCLE;
   INOSITOL 1,4,5-TRISPHOSPHATE; SPECTRIN CYTOSKELETON; ISOFORM
   SPECIFICITY; RYANODINE RECEPTOR
AB Ankyrin-B targets ion channels and transporters in excitable cells. Dysfunction in ankyrin-B-based pathways results in defects in cardiac physiology. Despite a wealth of knowledge regarding the role of ankyrin-B for cardiac function, little is known regarding the mechanisms underlying ankyrin-B regulation. Moreover, the pathways underlying ankyrin-B targeting in heart are unclear. We report that alternative splicing regulates ankyrin-B localization and function in cardiomyocytes. Specifically, we identify a novel exon (exon 43') in the ankyrin-B regulatory domain that mediates interaction with the Rho-GEF obscurin. Ankyrin-B transcripts harboring exon 43' represent the primary cardiac isoform in human and mouse. We demonstrate that ankyrin-B and obscurin are co-localized at the M-line of myocytes and co-immunoprecipitate from heart. We define the structural requirements for ankyrin-B/obscurin interaction to two motifs in the ankyrin-B regulatory domain and demonstrate that both are critical for obscurin/ankyrin-B interaction. In addition, we demonstrate that interaction with obscurin is required for ankyrin-B M-line targeting. Specifically, both obscurin-binding motifs are required for the M-line targeting of a GFP-ankyrin-B regulatory domain. Moreover, this construct acts as a dominant-negative by competing with endogenous ankyrin-B for obscurin-binding at the M-line, thus providing a powerful new tool to evaluate the function of obscurin/ankyrin-B interactions. With this new tool, we demonstrate that the obscurin/ankyrin-B interaction is critical for recruitment of PP2A to the cardiac M-line. Together, these data provide the first evidence for the molecular basis of ankyrin-B and PP2A targeting and function at the cardiac M-line. Finally, we report that ankyrin-B R1788W is localized adjacent to the ankyrin-B obscurin-binding motif and increases binding activity for obscurin. In summary, our new findings demonstrate that ANK2 is subject to alternative splicing that gives rise to unique polypeptides with diverse roles in cardiac function.
C1 [Cunha, Shane R.; Mohler, Peter J.] Univ Iowa, Carver Coll Med, Dept Internal Med, Iowa City, IA 52242 USA.
   [Mohler, Peter J.] Univ Iowa, Carver Coll Med, Dept Mol Physiol & Biophys, Iowa City, IA 52242 USA.
C3 University of Iowa; University of Iowa
RP Cunha, SR (corresponding author), 285 Newton Rd,CBRB 2283, Iowa City, IA 52242 USA.
EM shane-cunha@uiowa.edu
FU National Institutes of Health [HL084583, HL083422]; Pew Scholars Trust
FX This work was supported, in whole or in part, by National Institutes of
   Health Grants HL084583 and HL083422 (to P. J. M.). This work was also
   supported by Pew Scholars Trust (to P. J. M.). The costs of publication
   of this article were defrayed in part by the payment of page charges.
   This article must therefore be hereby marked "advertisement" in
   accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
CR Abdi KM, 2006, J BIOL CHEM, V281, P5741, DOI 10.1074/jbc.M506697200
   Armani A, 2006, EXP CELL RES, V312, P3546, DOI 10.1016/j.yexcr.2006.07.027
   Bagnato P, 2003, J CELL BIOL, V160, P245, DOI 10.1083/jcb.200208109
   Beck KA, 1997, J CELL SCI, V110, P1239
   Benian GM, 1996, J CELL BIOL, V132, P835, DOI 10.1083/jcb.132.5.835
   Bhasin N, 2007, AM J PHYSIOL-HEART C, V293, pH109, DOI 10.1152/ajpheart.00059.2007
   Birkenmeier CS, 1998, GENOMICS, V50, P79, DOI 10.1006/geno.1998.5305
   BIRKENMEIER CS, 1993, J BIOL CHEM, V268, P9533
   Borisov AB, 2006, HISTOCHEM CELL BIOL, V125, P227, DOI 10.1007/s00418-005-0069-x
   Borisov AB, 2004, J HISTOCHEM CYTOCHEM, V52, P1117, DOI 10.1369/jhc.3A6183.2004
   Borzok MA, 2007, J BIOL CHEM, V282, P32384, DOI 10.1074/jbc.M704089200
   Bowman AL, 2007, FEBS LETT, V581, P1549, DOI 10.1016/j.febslet.2007.03.011
   Brewis N, 2000, AM J PHYSIOL-HEART C, V279, pH1307, DOI 10.1152/ajpheart.2000.279.3.H1307
   Cartegni L, 2002, NAT REV GENET, V3, P285, DOI 10.1038/nrg775
   Cunha SR, 2007, J BIOL CHEM, V282, P4875, DOI 10.1074/jbc.M607096200
   Das A, 2006, J CELL BIOL, V175, P325, DOI 10.1083/jcb.200602095
   Davare MA, 2000, J BIOL CHEM, V275, P39710, DOI 10.1074/jbc.M005462200
   Davare MA, 2001, SCIENCE, V293, P98, DOI 10.1126/science.293.5527.98
   DAVIS JQ, 1994, J BIOL CHEM, V269, P27163
   DAVIS LH, 1992, J BIOL CHEM, V267, P18966
   Devarajan P, 1996, J CELL BIOL, V133, P819, DOI 10.1083/jcb.133.4.819
   DRENCKHAHN D, 1987, EUR J CELL BIOL, V43, P479
   Dubreuil RR, 2006, J MEMBRANE BIOL, V211, P151, DOI 10.1007/s00232-006-0863-y
   Dzhashiashvili Y, 2007, J CELL BIOL, V177, P857, DOI 10.1083/jcb.200612012
   Fukuzawa A, 2005, J MUSCLE RES CELL M, V26, P427, DOI 10.1007/s10974-005-9025-6
   Gagelin C, 2002, J BIOL CHEM, V277, P12978, DOI 10.1074/jbc.M111299200
   Gallagher PG, 1998, J BIOL CHEM, V273, P1339, DOI 10.1074/jbc.273.3.1339
   Gergs U, 2004, J BIOL CHEM, V279, P40827, DOI 10.1074/jbc.M405770200
   Gotthardt M, 2003, J BIOL CHEM, V278, P6059, DOI 10.1074/jbc.M211723200
   Hall DD, 2006, BIOCHEMISTRY-US, V45, P3448, DOI 10.1021/bi051593z
   HALL TG, 1987, J BIOL CHEM, V262, P10537
   Hopitzan AA, 2006, MOL BIOL EVOL, V23, P46, DOI 10.1093/molbev/msj004
   Hopitzan AA, 2005, EXP CELL RES, V309, P86, DOI 10.1016/j.yexcr.2005.04.013
   Kizhatil K, 2007, J BIOL CHEM, V282, P2029, DOI 10.1074/jbc.M608921200
   Kontrogianni-Konstantopoulos A, 2004, AM J PHYSIOL-CELL PH, V287, pC209, DOI 10.1152/ajpcell.00497.2003
   Kontrogianni-Konstantopoulos A, 2003, MOL BIOL CELL, V14, P1138, DOI 10.1091/mbc.E02-07-0411
   Kontrogianni-Konstantopoulos A, 2003, J BIOL CHEM, V278, P3985, DOI 10.1074/jbc.M209012200
   Kontrogianni-Konstantopoulos A, 2006, FASEB J, V20, P2102, DOI 10.1096/fj.06-5761com
   Koticha D, 2006, DEV BIOL, V293, P1, DOI 10.1016/j.ydbio.2005.05.028
   Lacas-Gervais S, 2004, J CELL BIOL, V166, P983, DOI 10.1083/jcb.200408007
   LAMBERT S, 1990, P NATL ACAD SCI USA, V87, P1730, DOI 10.1073/pnas.87.5.1730
   LAMBERT S, 1993, J NEUROSCI, V13, P3725
   Lange S, 2005, SCIENCE, V308, P1599, DOI 10.1126/science.1110463
   Lowe JS, 2008, J CELL BIOL, V180, P173, DOI 10.1083/jcb.200710107
   Lustig M, 2001, CURR BIOL, V11, P1864, DOI 10.1016/S0960-9822(01)00586-3
   LUX SE, 1990, NATURE, V344, P36, DOI 10.1038/344036a0
   Marx SO, 2000, CELL, V101, P365, DOI 10.1016/S0092-8674(00)80847-8
   Marx SO, 2002, SCIENCE, V295, P496, DOI 10.1126/science.1066843
   Mayans O, 1998, NATURE, V395, P863, DOI 10.1038/27603
   Mohler PJ, 2007, CIRCULATION, V115, P432, DOI 10.1161/CIRCULATIONAHA.106.656512
   Mohler PJ, 2005, PLOS BIOL, V3, P2158, DOI 10.1371/journal.pbio.0030423
   Mohler PJ, 2004, P NATL ACAD SCI USA, V101, P17533, DOI 10.1073/pnas.0403711101
   Mohler PJ, 2004, J BIOL CHEM, V279, P40185, DOI 10.1074/jbc.M406018200
   Mohler PJ, 2004, P NATL ACAD SCI USA, V101, P9137, DOI 10.1073/pnas.0402546101
   Mohler PJ, 2004, J BIOL CHEM, V279, P25798, DOI 10.1074/jbc.M401296200
   Mohler PJ, 2004, J BIOL CHEM, V279, P12980, DOI 10.1074/jbc.M313979200
   Mohler PJ, 2003, NATURE, V421, P634, DOI 10.1038/nature01335
   Mohler PJ, 2002, J BIOL CHEM, V277, P10599, DOI 10.1074/jbc.M110958200
   MUMBY MC, 1993, PHYSIOL REV, V73, P673, DOI 10.1152/physrev.1993.73.4.673
   Musa H, 2006, J CELL SCI, V119, P4322, DOI 10.1242/jcs.03198
   Neumann J, 1997, J MOL CELL CARDIOL, V29, P265, DOI 10.1006/jmcc.1996.0271
   Ogawa Y, 2006, J NEUROSCI, V26, P5230, DOI 10.1523/JNEUROSCI.0425-06.2006
   Peng J, 2007, CIRCULATION, V115, P743, DOI 10.1161/CIRCULATIONAHA.106.645499
   PETERS LL, 1991, J CELL BIOL, V114, P1233, DOI 10.1083/jcb.114.6.1233
   Raeker MÖ, 2006, DEV DYNAM, V235, P2018, DOI 10.1002/dvdy.20812
   Scotland P, 1998, J CELL BIOL, V143, P1305, DOI 10.1083/jcb.143.5.1305
   Sherman J, 2005, HEART RHYTHM, V2, P1218, DOI 10.1016/j.hrthm.2005.07.026
   Vandenbroucke I I, 2001, Nucleic Acids Res, V29, pE68, DOI 10.1093/nar/29.13.e68
   Weinert S, 2006, J CELL BIOL, V173, P559, DOI 10.1083/jcb.200601014
   Yang Y, 2004, J NEUROSCI, V24, P7230, DOI 10.1523/JNEUROSCI.2125-04.2004
   Young P, 2001, J CELL BIOL, V154, P123, DOI 10.1083/jcb.200102110
   Zhang X, 1998, J CELL BIOL, V142, P1571, DOI 10.1083/jcb.142.6.1571
   Zhou DX, 1997, J CELL BIOL, V136, P621, DOI 10.1083/jcb.136.3.621
NR 73
TC 65
Z9 77
U1 0
U2 2
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD NOV 14
PY 2008
VL 283
IS 46
BP 31968
EP 31980
DI 10.1074/jbc.M806050200
PG 13
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 370KJ
UT WOS:000260760800079
PM 18782775
OA hybrid, Green Published
DA 2025-04-10
ER

PT J
AU Sajish, M
   Schimmel, P
AF Sajish, Mathew
   Schimmel, Paul
TI A human tRNA synthetase is a potent PARP1-activating effector target for
   resveratrol
SO NATURE
LA English
DT Article
ID SMALL-MOLECULE ACTIVATORS; HISTONE ACETYLTRANSFERASE; CRYSTAL-STRUCTURE;
   TUMOR-SUPPRESSOR; DNA-DAMAGE; HEAT-SHOCK; LIFE-SPAN; KAPPA-B; STRESS;
   POLY(ADP-RIBOSE)
AB Resveratrol is reported to extend lifespan(1,2) and provide cardioneuro-protective(3), anti-diabetic(4), and anti-cancer effects(3,5) by initiating a stress response(2) that induces survival genes. Because human tyrosyl transfer-RNA(tRNA) synthetase (TyrRS) translocates to the nucleus under stress conditions(6), we considered the possibility that the tyrosine-like phenolic ring of resveratrol might fit into the active site pocket to effect a nuclear role. Here we present a 2.1 angstrom co-crystal structure of resveratrol bound to the active site of TyrRS. Resveratrol nullifies the catalytic activity and redirects TyrRS to a nuclear function, stimulating NAD(+)-dependent auto-poly-ADP-ribosylation of poly(ADP-ribose) polymerase 1 (PARP1). Downstream activation of key stress signalling pathways are causally connected to TyrRS-PARP1-NAD(+) collaboration. This collaborationis also demonstrated in the mouse, and is specifically blocked in vivo by a resveratrol-displacing tyrosyl adenylate analogue. In contrast to functionally diverse tRNA synthetase catalytic nulls created by alternative splicing events that ablate active sites(7), here a non-spliced TyrRS catalytic null reveals a new PARP1- and NAD(+)-dependent dimension to the physiological mechanism of resveratrol.
C1 [Sajish, Mathew; Schimmel, Paul] Scripps Res Inst, Dept Mol & Cell Biol, Scripps Labs TRNA Synthetase Res, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA.
   [Schimmel, Paul] Scripps Florida Res Inst, Jupiter, FL 33458 USA.
C3 Scripps Research Institute; State University System of Florida;
   University of Florida; Herbert Wertheim UF Scripps Institute for
   Biomedical Innovation & Technology
RP Schimmel, P (corresponding author), Scripps Res Inst, Dept Mol & Cell Biol, Scripps Labs TRNA Synthetase Res, Skaggs Inst Chem Biol, 10550 North Torrey Pines Rd, La Jolla, CA 92037 USA.
EM schimmel@scripps.edu
RI Thekkel, Sajish/AAM-3548-2021
OI Mathew, Sajish/0000-0001-6715-5953
FU National Cancer Institute [CA92577]; National Foundation for Cancer
   Research; aTyr Pharma; Scripps Research Institute
FX This work was supported in part the National Cancer Institute grant
   CA92577, by a fellowship from the National Foundation for Cancer
   Research, and by aTyr Pharma through an agreement with The Scripps
   Research Institute. We thank the The Scripps Research Institute mouse
   facility for their efforts for this project. We also thank P. Chang for
   the ZZ-PARP1 clone, and the PARG and PARG-MT proteins, and Y. Shi for
   independently repeating some of the key experiments. We thank P. Chang,
   J. H. Chung, L. Guarente, L. Krauss, D. Sinclair, and C. Westphal for
   comments and suggestions on this work.
CR Bastide B, 2002, BIOCHEM BIOPH RES CO, V296, P1267, DOI 10.1016/S0006-291X(02)02073-9
   Baur JA, 2006, NATURE, V444, P337, DOI 10.1038/nature05354
   Bitterman KJ, 2002, J BIOL CHEM, V277, P45099, DOI 10.1074/jbc.M205670200
   Budanov AV, 2008, CELL, V134, P451, DOI 10.1016/j.cell.2008.06.028
   Bungard D, 2010, SCIENCE, V329, P1201, DOI 10.1126/science.1191241
   Butin-Israeli V, 2010, J VIROL, V84, P3431, DOI 10.1128/JVI.01735-09
   Chen WM, 2009, MOL CELL, V34, P663, DOI 10.1016/j.molcel.2009.04.029
   Cohen-Armon M, 2007, MOL CELL, V25, P297, DOI 10.1016/j.molcel.2006.12.012
   Dasgupta B, 2007, P NATL ACAD SCI USA, V104, P7217, DOI 10.1073/pnas.0610068104
   Formentini L, 2009, J BIOL CHEM, V284, P17668, DOI 10.1074/jbc.M109.002931
   Fu GS, 2012, J BIOL CHEM, V287, P9330, DOI 10.1074/jbc.C111.325902
   Fulco M, 2008, DEV CELL, V14, P661, DOI 10.1016/j.devcel.2008.02.004
   Guo M, 2013, NAT CHEM BIOL, V9, P145, DOI [10.1038/nchembio.1158, 10.1038/NCHEMBIO.1158]
   Haigis MC, 2006, GENE DEV, V20, P2913, DOI 10.1101/gad.1467506
   Hawley SA, 2010, CELL METAB, V11, P554, DOI 10.1016/j.cmet.2010.04.001
   Hegan DC, 2010, P NATL ACAD SCI USA, V107, P2201, DOI 10.1073/pnas.0904783107
   Howitz KT, 2008, CELL, V133, P387, DOI 10.1016/j.cell.2008.04.019
   Howitz KT, 2003, NATURE, V425, P191, DOI 10.1038/nature01960
   Jang MS, 1997, SCIENCE, V275, P218, DOI 10.1126/science.275.5297.218
   Kapoor M, 2009, CHEM BIOL, V16, P531, DOI 10.1016/j.chembiol.2009.03.006
   Lambert PF, 1998, J BIOL CHEM, V273, P33048, DOI 10.1074/jbc.273.49.33048
   Lee PS, 2012, J BIOL CHEM, V287, P20504, DOI 10.1074/jbc.C112.369439
   Lo WS, 2014, SCIENCE, V345, P328, DOI 10.1126/science.1252943
   Luo X, 2012, GENE DEV, V26, P417, DOI 10.1101/gad.183509.111
   Mao ZY, 2011, SCIENCE, V332, P1443, DOI 10.1126/science.1202723
   Martin N, 2009, EMBO J, V28, P3534, DOI 10.1038/emboj.2009.279
   Matheny CJ, 2013, CHEM BIOL, V20, P1352, DOI 10.1016/j.chembiol.2013.09.014
   Michishita E, 2008, NATURE, V452, P492, DOI 10.1038/nature06736
   Milne JC, 2007, NATURE, V450, P712, DOI 10.1038/nature06261
   Nemoto S, 2004, SCIENCE, V306, P2105, DOI 10.1126/science.1101731
   Nwachukwu JC, 2014, ELIFE, V3, DOI 10.7554/eLife.02057
   Orlando G, 2014, NUCLEIC ACIDS RES, V42, P2320, DOI 10.1093/nar/gkt1185
   Park SJ, 2012, CELL, V148, P421, DOI 10.1016/j.cell.2012.01.017
   Perraud AL, 2001, NATURE, V411, P595, DOI 10.1038/35079100
   Petesch SJ, 2012, MOL CELL, V45, P64, DOI 10.1016/j.molcel.2011.11.015
   Rajamohan SB, 2009, MOL CELL BIOL, V29, P4116, DOI 10.1128/MCB.00121-09
   Ramsey KM, 2009, SCIENCE, V324, P651, DOI 10.1126/science.1171641
   Renault VM, 2011, ONCOGENE, V30, P3207, DOI 10.1038/onc.2011.35
   Sajish M, 2012, NAT CHEM BIOL, V8, P547, DOI [10.1038/NCHEMBIO.937, 10.1038/nchembio.937]
   Shin SM, 2009, MOL PHARMACOL, V76, P884, DOI 10.1124/mol.109.058479
   Sinclair DA, 2014, ANNU REV PHARMACOL, V54, P363, DOI 10.1146/annurev-pharmtox-010611-134657
   Smith BC, 2009, ANAL BIOCHEM, V394, P101, DOI 10.1016/j.ab.2009.07.019
   Stilmann M, 2009, MOL CELL, V36, P365, DOI 10.1016/j.molcel.2009.09.032
   Sun YL, 2005, P NATL ACAD SCI USA, V102, P13182, DOI 10.1073/pnas.0504211102
   Tang Y, 2008, CELL, V133, P612, DOI 10.1016/j.cell.2008.03.025
   Viswanathan M, 2005, DEV CELL, V9, P605, DOI 10.1016/j.devcel.2005.09.017
   Vyas S, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms5426
   Vyas S, 2013, MOL CELL, V49, P1, DOI 10.1016/j.molcel.2012.12.017
   Wakasugi K, 1999, SCIENCE, V284, P147, DOI 10.1126/science.284.5411.147
   Wang JD, 2010, J BIOL CHEM, V285, P11458, DOI 10.1074/jbc.M109.087585
   Yang XL, 2003, HELV CHIM ACTA, V86, P1246, DOI 10.1002/hlca.200390107
   Yang XL, 2002, P NATL ACAD SCI USA, V99, P15369, DOI 10.1073/pnas.242611799
   Yang YB, 2011, MOL CELL BIOL, V31, P2774, DOI 10.1128/MCB.01139-10
   Zhang P, 2014, P NATL ACAD SCI USA, V111, P10684, DOI 10.1073/pnas.1411026111
NR 54
TC 121
Z9 143
U1 1
U2 98
PU NATURE PUBLISHING GROUP
PI LONDON
PA MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
SN 0028-0836
EI 1476-4687
J9 NATURE
JI Nature
PD MAR 19
PY 2015
VL 519
IS 7543
BP 370
EP +
DI 10.1038/nature14028
PG 16
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA CD6AY
UT WOS:000351171900045
PM 25533949
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Gurianova, V
   Stroy, D
   Ciccocioppo, R
   Gasparova, I
   Petrovic, D
   Soucek, M
   Dosenko, V
   Kruzliak, P
AF Gurianova, Veronika
   Stroy, Dmytro
   Ciccocioppo, Rachele
   Gasparova, Iveta
   Petrovic, Daniel
   Soucek, Miroslav
   Dosenko, Victor
   Kruzliak, Peter
TI Stress response factors as hub-regulators of microRNA biogenesis:
   implication to the diseased heart
SO CELL BIOCHEMISTRY AND FUNCTION
LA English
DT Article
DE miRNAs biogenesis; stress response; hub-mechanisms; cardiac
   pathophysiology
ID ENDOPLASMIC-RETICULUM STRESS; UBIQUITIN-PROTEASOME SYSTEM;
   ISCHEMIA-REPERFUSION INJURY; MYOTONIC-DYSTROPHY; BINDING-PROTEIN;
   MYOCARDIAL-INFARCTION; OXIDATIVE STRESS; TRANSLATIONAL REPRESSION;
   HISTONE DEACETYLASES; CHROMOSOMAL-PROTEIN
AB MicroRNAs (miRNAs) are important regulators of heart function and then an intriguing therapeutic target for plenty of diseases. The problem raised is that many data in this area are contradictory, thus limiting the use of miRNA-based therapy. The goal of this review is to describe the hub-mechanisms regulating the biogenesis and function of miRNAs, which could help in clarifying some contradictions in the miRNA world. With this scope, we analyse an array of factors, including several known agents of stress response, mediators of epigenetic changes, regulators of alternative splicing, RNA editing, protein synthesis and folding and proteolytic systems. All these factors are important in cardiovascular function and most of them regulate miRNA biogenesis, but their influence on miRNAs was shown for non-cardiac cells or some specific cardiac pathologies. Finally, we consider that studying the stress response factors, which are upstream regulators of miRNA biogenesis, in the diseased heart could help in (1) explaining some contradictions concerning miRNAs in heart pathology, (2) making the role of miRNAs in pathogenesis of cardiovascular disease more clear, and therefore, (3) getting powerful targets for its molecular therapy. Copyright (C) 2015 John Wiley & Sons, Ltd.
C1 [Gurianova, Veronika; Stroy, Dmytro; Dosenko, Victor] Natl Acad Sci Ukraine, Bogomoletz Inst Physiol, Kiev, Ukraine.
   [Ciccocioppo, Rachele] Univ Pavia, Clin Med 1, Fdn IRCCS Policlin San Matteo, I-27100 Pavia, Italy.
   [Gasparova, Iveta] Comenius Univ, Fac Med, Inst Biol Genet & Med Genet, Bratislava, Slovakia.
   [Gasparova, Iveta] Univ Hosp, Bratislava, Slovakia.
   [Petrovic, Daniel] Univ Ljubljana, Fac Med, Inst Histol & Embryol, Ljubljana, Slovenia.
   [Soucek, Miroslav; Kruzliak, Peter] St Annes Univ Hosp, Dept Internal Med 2, Brno 65691, Czech Republic.
   [Soucek, Miroslav; Kruzliak, Peter] Masaryk Univ, Brno, Czech Republic.
   [Kruzliak, Peter] Comenius Univ, Fac Pharm, Dept Pharmacol & Toxicol, Bratislava, Slovakia.
   [Kruzliak, Peter] Univ Vet & Pharmaceut Sci, Fac Pharm, Lab Struct Biol & Prote, Brno, Czech Republic.
C3 National Academy of Sciences Ukraine; A.A. Bogomoletz Institute of
   Physiology; University of Pavia; IRCCS Fondazione San Matteo; Comenius
   University Bratislava; Slovak Medical University Bratislava; University
   of Ljubljana; St. Anne's University Hospital Brno (FNUSA); Masaryk
   University Brno; Comenius University Bratislava; University of
   Veterinary Sciences Brno
RP Kruzliak, P (corresponding author), St Annes Univ Hosp, Dept Internal Med 2, Pekarska 53, Brno 65691, Czech Republic.
EM kruzliakpeter@gmail.com
RI Romero, Veronika/G-1116-2018
OI Romero, Veronika/0000-0001-6720-8592; Dosenko,
   Victor/0000-0002-6919-7724
CR Acampa M, 2006, ARCH DIS CHILD, V91, P440, DOI 10.1136/adc.2005.090290
   Adam O, 2012, BASIC RES CARDIOL, V107, DOI 10.1007/s00395-012-0278-0
   Alvarez-Saavedra M, 2010, HUM MOL GENET, V19, P2177, DOI 10.1093/hmg/ddq096
   Aune SE, 2014, J MOL CELL CARDIOL, V72, P138, DOI 10.1016/j.yjmcc.2014.03.005
   Azfer A, 2006, AM J PHYSIOL-HEART C, V291, pH1411, DOI 10.1152/ajpheart.01378.2005
   Ballut L, 2003, BBA-PROTEINS PROTEOM, V1645, P30, DOI 10.1016/S1570-9639(02)00500-9
   Bandara V, 2014, BMC CANCER, V14, DOI 10.1186/1471-2407-14-533
   Barr I, 2012, P NATL ACAD SCI USA, V109, P1919, DOI 10.1073/pnas.1114514109
   Bauersachs J, 2011, CIRC RES, V109, P334, DOI 10.1161/CIRCRESAHA.110.228676
   Bernstein E, 2001, NATURE, V409, P363, DOI 10.1038/35053110
   Bhattacharyya SN, 2006, CELL, V125, P1111, DOI 10.1016/j.cell.2006.04.031
   Botta A, 2013, GENES-BASEL, V4, P275, DOI 10.3390/genes4020275
   Bracaglia G, 2009, EMBO REP, V10, P1327, DOI 10.1038/embor.2009.217
   Calise J, 2013, AM J PHYSIOL-HEART C, V304, pH337, DOI 10.1152/ajpheart.00604.2012
   Cao DJ, 2011, P NATL ACAD SCI USA, V108, P4123, DOI 10.1073/pnas.1015081108
   Cardin S, 2012, CIRC-ARRHYTHMIA ELEC, V5, P1027, DOI 10.1161/CIRCEP.112.973214
   Chahrour M, 2007, NEURON, V56, P422, DOI 10.1016/j.neuron.2007.10.001
   Chen JF, 2008, P NATL ACAD SCI USA, V105, P2111, DOI 10.1073/pnas.0710228105
   Cheng TL, 2014, DEV CELL, V28, P547, DOI 10.1016/j.devcel.2014.01.032
   Cheng YH, 2010, CARDIOVASC RES, V87, P431, DOI 10.1093/cvr/cvq082
   Cifuentes RA, 2010, CLIN CHIM ACTA, V411, P1862, DOI 10.1016/j.cca.2010.08.033
   Collino M, 2013, DIS MODEL MECH, V6, P1012, DOI 10.1242/dmm.011528
   de León-Guerrero SD, 2011, EUR J NEUROSCI, V33, P1563, DOI 10.1111/j.1460-9568.2011.07658.x
   Dincbas-Renqvist V, 2009, BBA-GENE REGUL MECH, V1789, P99, DOI 10.1016/j.bbagrm.2008.10.002
   Dong SM, 2009, J BIOL CHEM, V284, P29514, DOI 10.1074/jbc.M109.027896
   Drews O, 2014, ANTIOXID REDOX SIGN, V21, P2322, DOI 10.1089/ars.2013.5823
   Dutta D, 2013, AUTOPHAGY, V9, P328, DOI 10.4161/auto.22971
   Faller M, 2007, NAT STRUCT MOL BIOL, V14, P23, DOI 10.1038/nsmb1182
   Fiedler J, 2013, ARTERIOSCL THROM VAS, V33, P201, DOI 10.1161/ATVBAHA.112.300137
   Finnegan EF, 2013, CRIT REV BIOCHEM MOL, V48, P51, DOI 10.3109/10409238.2012.738643
   Foresti R, 2001, AM J PHYSIOL-HEART C, V281, pH1976, DOI 10.1152/ajpheart.2001.281.5.H1976
   Ghodgaonkar MM, 2009, CELL DEATH DIFFER, V16, P858, DOI 10.1038/cdd.2009.15
   Gibbings D, 2013, AUTOPHAGY, V9, P781, DOI 10.4161/auto.23694
   Gibbings D, 2012, NAT CELL BIOL, V14, P1314, DOI 10.1038/ncb2611
   Giudice J, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms4603
   Gommans WM, 2012, SEMIN CELL DEV BIOL, V23, P251, DOI 10.1016/j.semcdb.2011.09.018
   Gong M, 2012, PROTEIN SCI, V21, P797, DOI 10.1002/pro.2062
   Granger A, 2008, FASEB J, V22, P3549, DOI 10.1096/fj.08-108548
   Gregory RI, 2004, NATURE, V432, P235, DOI 10.1038/nature03120
   Groenendyk J, 2010, CIRC RES, V107, P1185, DOI 10.1161/CIRCRESAHA.110.227033
   Gurianova V, 2015, MOL CELL BIOCHEM, V404, P45, DOI 10.1007/s11010-015-2365-7
   Haberland M, 2009, NAT REV GENET, V10, P32, DOI 10.1038/nrg2485
   Hagan JP, 2009, NAT STRUCT MOL BIOL, V16, P1021, DOI 10.1038/nsmb.1676
   Han JJ, 2004, GENE DEV, V18, P3016, DOI 10.1101/gad.1262504
   Hassler J, 2012, DEV CELL, V23, P921, DOI 10.1016/j.devcel.2012.10.025
   He B, 2011, J BIOMED SCI, V18, DOI 10.1186/1423-0127-18-22
   Heo I, 2009, CELL, V138, P696, DOI 10.1016/j.cell.2009.08.002
   Ho JJD, 2012, J BIOL CHEM, V287, P29003, DOI 10.1074/jbc.M112.373365
   Ho TH, 2004, EMBO J, V23, P3103, DOI 10.1038/sj.emboj.7600300
   Hoxha E, 2012, STEM CELLS, V30, P2412, DOI 10.1002/stem.1209
   Huntzinger E, 2011, NAT REV GENET, V12, P99, DOI 10.1038/nrg2936
   Ikezoe K, 2007, ACTA NEUROPATHOL, V114, P527, DOI 10.1007/s00401-007-0267-9
   Ishiura S, 2005, Acta Myol, V24, P74
   Jarrousse AS, 1999, J BIOL CHEM, V274, P5925, DOI 10.1074/jbc.274.9.5925
   Johnston M, 2010, MOL BIOL CELL, V21, P1462, DOI 10.1091/mbc.E09-10-0885
   Kalsotra A, 2008, P NATL ACAD SCI USA, V105, P20333, DOI 10.1073/pnas.0809045105
   Kanamori H, 2011, AM J PHYSIOL-HEART C, V300, pH2261, DOI 10.1152/ajpheart.01056.2010
   Kang SJ, 2014, ANN MED, V46, P138, DOI 10.3109/07853890.2014.895588
   Khalil PN, 2005, EUR J PHARMACOL, V528, P124, DOI 10.1016/j.ejphar.2005.10.032
   Kim SH, 2002, CIRC J, V66, P959, DOI 10.1253/circj.66.959
   Koshelev M, 2010, HUM MOL GENET, V19, P1066, DOI 10.1093/hmg/ddp570
   Kozakowska M, 2012, ANTIOXID REDOX SIGN, V16, P113, DOI 10.1089/ars.2011.3964
   Kruzliak P, 2014, CYTOKINE GROWTH F R, V25, P67, DOI 10.1016/j.cytogfr.2014.01.005
   Kukreja RC, 2011, MOL PHARMACOL, V80, P558, DOI 10.1124/mol.111.073528
   Kulichkova VA, 2010, CELL CYCLE, V9, P840, DOI 10.4161/cc.9.4.10829
   Lakkisto P, 2009, SCAND J CLIN LAB INV, V69, P209, DOI 10.1080/00365510802474392
   Latchman DS, 2001, CARDIOVASC RES, V51, P637, DOI 10.1016/S0008-6363(01)00354-6
   Lee Y, 2003, NATURE, V425, P415, DOI 10.1038/nature01957
   Lee Y, 2002, EMBO J, V21, P4663, DOI 10.1093/emboj/cdf476
   LEWIS JD, 1992, CELL, V69, P905, DOI 10.1016/0092-8674(92)90610-O
   Liang JA, 2010, J EXP MED, V207, P2959, DOI 10.1084/jem.20092641
   Lin XY, 2006, HUM MOL GENET, V15, P2087, DOI 10.1093/hmg/ddl132
   Lisovyy OO, 2009, ACTA BIOCHIM POL, V56, P687
   Lorenzen JM, 2013, FREE RADICAL BIO MED, V64, P78, DOI 10.1016/j.freeradbiomed.2013.06.044
   Lu YJ, 2009, CARDIOVASC RES, V84, P434, DOI 10.1093/cvr/cvp232
   Luciano DJ, 2004, RNA, V10, P1174, DOI 10.1261/rna.7350304
   Lugli G, 2005, J NEUROCHEM, V94, P896, DOI 10.1111/j.1471-4159.2005.03224.x
   Lund E, 2004, SCIENCE, V303, P95, DOI 10.1126/science.1090599
   Ma XC, 2012, CIRCULATION, V125, P3170, DOI 10.1161/CIRCULATIONAHA.111.041814
   Martinez NJ, 2013, RNA, V19, P605, DOI 10.1261/rna.036434.112
   Martins PADC, 2008, CIRCULATION, V118, P1567, DOI 10.1161/CIRCULATIONAHA.108.769984
   Matskevich AA, 2008, BIOCHEM J, V412, P527, DOI 10.1042/BJ20071461
   Maunakea AK, 2013, CELL RES, V23, P1256, DOI 10.1038/cr.2013.110
   Mayr F, 2013, INT J MOL SCI, V14, P16532, DOI 10.3390/ijms140816532
   McCauley MD, 2011, SCI TRANSL MED, V3, DOI 10.1126/scitranslmed.3002982
   Memczak S, 2013, NATURE, V495, P333, DOI 10.1038/nature11928
   Mendell JT, 2012, CELL, V148, P1172, DOI 10.1016/j.cell.2012.02.005
   Minamino T, 2010, CIRC RES, V107, P1071, DOI 10.1161/CIRCRESAHA.110.227819
   Minamino T, 2010, J MOL CELL CARDIOL, V48, P1105, DOI 10.1016/j.yjmcc.2009.10.026
   Montgomery RL, 2007, GENE DEV, V21, P1790, DOI 10.1101/gad.1563807
   Mukhopadhyay P, 2012, J CELL MOL MED, V16, P2504, DOI 10.1111/j.1582-4934.2011.01480.x
   Mukhopadhyay P, 2010, PLOS ONE, V5, DOI 10.1371/journal.pone.0015705
   Nakai A, 2007, NAT MED, V13, P619, DOI 10.1038/nm1574
   Nallamshetty S, 2013, FREE RADICAL BIO MED, V64, P20, DOI 10.1016/j.freeradbiomed.2013.05.022
   NAN XS, 1993, NUCLEIC ACIDS RES, V21, P4886, DOI 10.1093/nar/21.21.4886
   Nan XS, 1998, NATURE, V393, P386, DOI 10.1038/30764
   Newman MA, 2008, RNA, V14, P1539, DOI 10.1261/rna.1155108
   Novák J, 2014, THERANOSTICS, V4, P119, DOI 10.7150/thno.7552
   Olson EN, 2014, SCI TRANSL MED, V6, DOI 10.1126/scitranslmed.3009008
   Onishi H, 2008, J NEUROSCI RES, V86, P1994, DOI 10.1002/jnr.21655
   Pan Z., 2012, J STAT COMPUTATION S, P1
   Parameswaran S, 2014, BIOCHEM BIOPH RES CO, V443, P604, DOI 10.1016/j.bbrc.2013.12.019
   Pare JM, 2009, MOL BIOL CELL, V20, P3273, DOI 10.1091/mbc.E09-01-0082
   Pascual M, 2006, DIFFERENTIATION, V74, P65, DOI 10.1111/j.1432-0436.2006.00060.x
   Pasquinelli AE, 2012, NAT REV GENET, V13, P271, DOI 10.1038/nrg3162
   Patrick DM, 2010, J CLIN INVEST, V120, P3912, DOI 10.1172/JCI43604
   Petit F, 1997, MOL BIOL REP, V24, P113, DOI 10.1023/A:1006886911852
   Petit F, 1997, BIOCHEM J, V326, P93, DOI 10.1042/bj3260093
   Poliseno L, 2010, NATURE, V465, P1033, DOI 10.1038/nature09144
   Port JD, 2011, PHYSIOL GENOMICS, V43, P1087, DOI 10.1152/physiolgenomics.00074.2011
   Powell SR, 2012, PROG MOL BIOL TRANSL, V109, P295, DOI 10.1016/B978-0-12-397863-9.00009-2
   Qi DF, 2011, J BIOL CHEM, V286, P41692, DOI 10.1074/jbc.M111.276006
   Qian L, 2011, J EXP MED, V208, P549, DOI 10.1084/jem.20101547
   Rao PK, 2009, CIRC RES, V105, P585, DOI 10.1161/CIRCRESAHA.109.200451
   Rau F, 2011, NAT STRUCT MOL BIOL, V18, P840, DOI 10.1038/nsmb.2067
   Roy A, 2012, CELL SIGNAL, V24, P2123, DOI 10.1016/j.cellsig.2012.07.014
   Salloum FN, 2010, J CARDIOVASC PHARM, V56, P581, DOI 10.1097/FJC.0b013e3181f581ba
   Salmena L, 2011, CELL, V146, P353, DOI 10.1016/j.cell.2011.07.014
   SCHMID HP, 1995, MOL BIOL REP, V21, P43, DOI 10.1007/BF00990969
   Senturia R, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0039688
   Skommer J, 2014, CELL DEATH DIS, V5, DOI 10.1038/cddis.2014.287
   Small EM, 2011, NATURE, V469, P336, DOI 10.1038/nature09783
   Smibert P, 2013, NAT STRUCT MOL BIOL, V20, P789, DOI 10.1038/nsmb.2606
   Smith RM, 2015, CLIN EXP PHARMACOL P, V42, P860, DOI 10.1111/1440-1681.12427
   Suh N, 2010, CURR BIOL, V20, P271, DOI 10.1016/j.cub.2009.12.044
   Suzuki HI, 2011, MOL CELL, V44, P424, DOI 10.1016/j.molcel.2011.09.012
   Takemura G, 2009, AUTOPHAGY, V5, P1034, DOI 10.4161/auto.5.7.9297
   Takeshita D, 2013, J PHYSIOL SCI, V63, P113, DOI 10.1007/s12576-012-0243-6
   Tang XL, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0072503
   Thomson JM, 2006, GENE DEV, V20, P2202, DOI 10.1101/gad.1444406
   Timchenko NA, 2004, J BIOL CHEM, V279, P13129, DOI 10.1074/jbc.M312923200
   Tsimokha AS, 2014, ONCOTARGET, V5, P3555, DOI 10.18632/oncotarget.1957
   Upton JP, 2012, SCIENCE, V338, P818, DOI 10.1126/science.1226191
   van Rooij E, 2008, P NATL ACAD SCI USA, V105, P13027, DOI 10.1073/pnas.0805038105
   Viswanathan SR, 2008, SCIENCE, V320, P97, DOI 10.1126/science.1154040
   Wada T, 2012, EMBO REP, V13, P142, DOI 10.1038/embor.2011.247
   Wang J, 2012, J CELL MOL MED, V16, P2150, DOI 10.1111/j.1582-4934.2012.01523.x
   Wang QD, 2004, J BIOL CHEM, V279, P4952, DOI 10.1074/jbc.M310162200
   Wang XJ, 2014, J MOL CELL CARDIOL, V71, P16, DOI 10.1016/j.yjmcc.2013.11.006
   Warf MB, 2007, RNA, V13, P2238, DOI 10.1261/rna.610607
   Weissbach R, 2012, RNA, V18, P462, DOI 10.1261/rna.027656.111
   Weitz SH, 2014, P NATL ACAD SCI USA, V111, P1861, DOI 10.1073/pnas.1309915111
   Whitesell L, 2003, CURR CANCER DRUG TAR, V3, P349, DOI 10.2174/1568009033481787
   Wiesen JL, 2009, MOL IMMUNOL, V46, P1222, DOI 10.1016/j.molimm.2008.11.012
   Xie M, 2014, CIRCULATION, V129, P1139, DOI 10.1161/CIRCULATIONAHA.113.002416
   Yang BF, 2007, NAT MED, V13, P486, DOI 10.1038/nm1569
   Yang WD, 2006, NAT STRUCT MOL BIOL, V13, P13, DOI 10.1038/nsmb1041
   Ye YM, 2011, PHYSIOL GENOMICS, V43, P534, DOI 10.1152/physiolgenomics.00130.2010
   Ye YM, 2010, CARDIOVASC RES, V87, P535, DOI 10.1093/cvr/cvq053
   Yeom KH, 2006, NUCLEIC ACIDS RES, V34, P4622, DOI 10.1093/nar/gkl458
   Yi R, 2003, GENE DEV, V17, P3011, DOI 10.1101/gad.1158803
   Younce C, 2012, CELL PHYSIOL BIOCHEM, V30, P307, DOI 10.1159/000339066
   Younce CW, 2010, CARDIOVASC RES, V87, P665, DOI 10.1093/cvr/cvq102
   Young JI, 2005, P NATL ACAD SCI USA, V102, P17551, DOI 10.1073/pnas.0507856102
   Yu SY, 2010, J CARDIOVASC TRANSL, V3, P241, DOI 10.1007/s12265-010-9168-8
   Zhang YM, 2014, CIRCULATION, V129, P1088, DOI 10.1161/CIRCULATIONAHA.113.008115
   Zhao YQ, 2010, TOXICOL APPL PHARM, V248, P20, DOI 10.1016/j.taap.2010.07.007
   Zhu HX, 2007, J CLIN INVEST, V117, P1782, DOI 10.1172/JCI27523
   Zhu HY, 2012, CARDIOVASC RES, V94, P284, DOI 10.1093/cvr/cvr291
NR 159
TC 3
Z9 3
U1 0
U2 12
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0263-6484
EI 1099-0844
J9 CELL BIOCHEM FUNCT
JI Cell Biochem. Funct.
PD DEC
PY 2015
VL 33
IS 8
BP 509
EP 518
DI 10.1002/cbf.3151
PG 10
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA DA6MV
UT WOS:000367919800001
PM 26659949
DA 2025-04-10
ER

PT J
AU Rioux, AV
   Nsimba-Batomene, TR
   Slimani, S
   Bergeron, NAD
   Gravel, MAM
   Schreiber, SV
   Fiola, MJ
   Haydock, L
   Garneau, AP
   Isenring, P
AF Rioux, A. V.
   Nsimba-Batomene, T. R.
   Slimani, S.
   Bergeron, N. A. D.
   Gravel, M. A. M.
   Schreiber, S. V.
   Fiola, M. J.
   Haydock, L.
   Garneau, A. P.
   Isenring, P.
TI Navigating the multifaceted intricacies of the
   Na<SUP>+</SUP>-Cl<SUP>-</SUP> cotransporter, a highly regulated key
   effector in the control of hydromineral homeostasis
SO PHYSIOLOGICAL REVIEWS
LA English
DT Review
DE cation-Cl- cotransporter; distal tubule; Gitelman syndrome; Na+-Cl-
   cotransporter
ID SODIUM-CHLORIDE COTRANSPORTER; DISTAL CONVOLUTED TUBULE; SENSITIVE
   NACL-COTRANSPORTER; FAMILIAL HYPERKALEMIC HYPERTENSION;
   PSEUDOHYPOALDOSTERONISM TYPE-II; THICK ASCENDING LIMB; CALCIUM-SENSING
   RECEPTOR; KELCH-LIKE 3; THIAZIDE DIURETIC RECEPTORS; ALTERNATIVE SPLICE
   VARIANT
AB The Na+-Cl- cotransporter (NCC; SLC12A3) is a highly regulated integral membrane protein that is known to exist as three splice variants in primates. Its primary role in the kidney is to mediate the cosymport of Na+ and Cl- across the apical membrane of the distal convoluted tubule. Through this role and the involvement of other ion transport systems, NCC allows the systemic circulation to reclaim a fraction of the ultrafiltered Na+, K+, Cl-, and Mg+ loads in exchange for Ca2+ and HCO3-. The physiological relevance of the Na+-Cl- cotransport mechanism in humans is illustrated by several abnormalities that result from NCC inactivation through the administration of thiazides or in the setting of hereditary disorders. The purpose of the present review is to discuss the molecular mechanisms and overall roles of Na+-Cl(- )cotransport as the main topics of interest. On reading the narrative proposed, one will realize that the knowledge gained in regard to these themes will continue to progress unrelentingly no matter how refined it has now become.
C1 [Rioux, A. V.; Nsimba-Batomene, T. R.; Slimani, S.; Bergeron, N. A. D.; Gravel, M. A. M.; Schreiber, S. V.; Fiola, M. J.; Haydock, L.; Garneau, A. P.; Isenring, P.] Laval Univ, Dept Med, Nephrol Res Grp, Quebec City, PQ, Canada.
   [Haydock, L.; Garneau, A. P.] Univ Paris Cite, Hop Necker Enfants Malad, AP HP, Serv Nephrol Transplantat Renale Adultes,INSERM U1, Paris, France.
C3 Laval University; Institut National de la Sante et de la Recherche
   Medicale (Inserm); Assistance Publique Hopitaux Paris (APHP); Universite
   Paris Cite; Hopital Universitaire Necker-Enfants Malades - APHP
RP Isenring, P (corresponding author), Laval Univ, Dept Med, Nephrol Res Grp, Quebec City, PQ, Canada.
EM paul.isenring@crhdq.ulaval.ca
FU Kidney Foundation of Canada; Canadian Institute of Health Research
FX This work was funded by the Kidney Foundation of Canada and the Canadian
   Institute of Health Research
CR Akella R, 2021, MOL BIOL CELL, V32, P1614, DOI 10.1091/mbc.E20-01-0089
   Akella R, 2020, BIOCHEMISTRY-US, V59, P1747, DOI 10.1021/acs.biochem.0c00146
   Al-Qusairi L, 2017, J AM SOC NEPHROL, V28, P2431, DOI 10.1681/ASN.2016070732
   Al-Qusairi L, 2016, AM J PHYSIOL-RENAL, V311, pF330, DOI 10.1152/ajprenal.00002.2016
   Alnahas Z, 2022, CASE REP ENDOCRINOL, V2022, DOI 10.1155/2022/1098222
   Alothaid H, 2021, SAUDI J BIOL SCI, V28, P116, DOI 10.1016/j.sjbs.2020.08.042
   An CY, 2016, KIDNEY BLOOD PRESS R, V41, P18, DOI 10.1159/000368543
   Arjona FJ, 2013, PFLUG ARCH EUR J PHY, V465, P1409, DOI 10.1007/s00424-013-1275-3
   Arystarkhova E, 2014, PHYSIOL REP, V2, DOI 10.14814/phy2.12226
   Athimulam S, 2019, ENDOCRIN METAB CLIN, V48, P701, DOI 10.1016/j.ecl.2019.08.003
   Azlan NFM, 2021, ACTA PHARM SIN B, V11, P1117, DOI 10.1016/j.apsb.2020.09.009
   Banki E, 2021, KIDNEY INT, V100, P850, DOI 10.1016/j.kint.2021.06.030
   Bao MH, 2019, CLIN EXP HYPERTENS, V41, P381, DOI 10.1080/10641963.2018.1489547
   Barat A, 2016, COMP BIOCHEM PHYS B, V200, P54, DOI 10.1016/j.cbpb.2016.06.003
   Bazúa-Valenti S, 2018, J AM SOC NEPHROL, V29, P1838, DOI 10.1681/ASN.2017111155
   Bazúa-Valenti S, 2015, J AM SOC NEPHROL, V26, P1781, DOI 10.1681/ASN.2014050470
   Bazzini C, 2005, J BIOL CHEM, V280, P19902, DOI 10.1074/jbc.M411961200
   BEAUMONT K, 1989, J PHARMACOL EXP THER, V250, P414
   BEAUMONT K, 1990, CLIN EXP HYPERTENS A, V12, P215, DOI 10.3109/10641969009074730
   BEAUMONT K, 1988, P NATL ACAD SCI USA, V85, P2311, DOI 10.1073/pnas.85.7.2311
   Benos D J, 1985, Soc Gen Physiol Ser, V39, P211
   BENOS DJ, 1983, J PHYSIOL-LONDON, V342, P23, DOI 10.1113/jphysiol.1983.sp014837
   Bergeron MJ, 2003, AM J PHYSIOL-RENAL, V285, pF68, DOI 10.1152/ajprenal.00032.2003
   BETTINELLI A, 1992, J PEDIATR-US, V120, P38, DOI 10.1016/S0022-3476(05)80594-3
   BEYER KH, 1993, HYPERTENSION, V22, P388, DOI 10.1161/01.HYP.22.3.388
   BEYER KH, 1982, BRIT J CLIN PHARMACO, V13, P15
   Bhalla V, 2006, AM J PHYSIOL-RENAL, V291, pF714, DOI 10.1152/ajprenal.00061.2006
   Bickel CA, 2001, AM J PHYSIOL-RENAL, V281, pF639, DOI 10.1152/ajprenal.2001.281.4.F639
   BIEMESDERFER D, 1992, AM J PHYSIOL, V263, pF833, DOI 10.1152/ajprenal.1992.263.5.F833
   BINDELS RJM, 1992, PFLUG ARCH EUR J PHY, V420, P566, DOI 10.1007/BF00374634
   Blanchard A, 2019, J AM SOC NEPHROL, V30, P1533, DOI 10.1681/ASN.2019010031
   Blanchard A, 2017, KIDNEY INT, V91, P24, DOI 10.1016/j.kint.2016.09.046
   Bockenhauer D, 2009, NEW ENGL J MED, V360, P1960, DOI 10.1056/NEJMoa0810276
   Boscardin E, 2018, J AM SOC NEPHROL, V29, P977, DOI [10.1681/ASN.2017030345, 10.1681/asn.2017030345]
   Bostonjoglo M, 1998, J AM SOC NEPHROL, V9, P1347
   Bosu DR, 2008, CELL DIV, V3, DOI 10.1186/1747-1028-3-7
   Boyd-Shiwarski CR, 2018, MOL BIOL CELL, V29, P499, DOI 10.1091/mbc.E17-08-0529
   Boyden LM, 2012, NATURE, V482, P98, DOI 10.1038/nature10814
   BROOKS CS, 1977, CLIN PHARMACOL THER, V22, P14
   Brooks HL, 2002, HYPERTENSION, V39, P470, DOI 10.1161/hy02t2.102959
   BURCKHARDT BC, 1992, PFLUG ARCH EUR J PHY, V420, P78, DOI 10.1007/BF00378644
   Câmpean V, 2001, AM J PHYSIOL-RENAL, V281, pF1028, DOI 10.1152/ajprenal.0148.2001
   Canonica J, 2016, PFLUG ARCH EUR J PHY, V468, P895, DOI 10.1007/s00424-015-1785-2
   Mrad FCC, 2021, WORLD J PEDIATR, V17, P31, DOI 10.1007/s12519-020-00370-4
   Castagna A, 2015, PROTEOM CLIN APPL, V9, P623, DOI 10.1002/prca.201400198
   Castañeda-Bueno M, 2017, P NATL ACAD SCI USA, V114, pE879, DOI 10.1073/pnas.1620315114
   Castañeda-Bueno M, 2012, P NATL ACAD SCI USA, V109, P7929, DOI 10.1073/pnas.1200947109
   Castañeda-Bueno M, 2010, AM J PHYSIOL-RENAL, V299, pF1111, DOI 10.1152/ajprenal.00412.2010
   Chambrey R, 2001, AM J PHYSIOL-RENAL, V281, pF707, DOI 10.1152/ajprenal.2001.281.4.F707
   Chang HG, 1999, AM J PHYSIOL-RENAL, V276, pF952, DOI 10.1152/ajprenal.1999.276.6.F952
   Chávez-Canales M, 2014, HYPERTENSION, V64, P1047, DOI 10.1161/HYPERTENSIONAHA.114.04036
   Chávez-Canales M, 2013, J HYPERTENS, V31, P303, DOI 10.1097/HJH.0b013e32835bbb83
   Chen JC, 2019, P NATL ACAD SCI USA, V116, P4502, DOI 10.1073/pnas.1817220116
   Chen SY, 1999, P NATL ACAD SCI USA, V96, P2514, DOI 10.1073/pnas.96.5.2514
   CHEN ZF, 1994, J AM SOC NEPHROL, V5, P1112
   CHEN ZF, 1990, J AM SOC NEPHROL, V1, P91
   Cheng CJ, 2011, J AM SOC NEPHROL, V22, P460, DOI 10.1681/ASN.2010060681
   Cheng L, 2019, J AM SOC NEPHROL, V30, P1453, DOI 10.1681/ASN.2018101025
   Cheng L, 2018, DRUG DES DEV THER, V12, P3929, DOI 10.2147/DDDT.S179568
   Cheng L, 2015, SCI REP-UK, V5, DOI 10.1038/srep12829
   Chew TA, 2019, NATURE, V572, P488, DOI 10.1038/s41586-019-1438-2
   Chi GM, 2021, EMBO J, V40, DOI 10.15252/embj.2020107294
   Chi XM, 2021, CELL RES, V31, P482, DOI 10.1038/s41422-020-00437-x
   Chiga M, 2008, KIDNEY INT, V74, P1403, DOI 10.1038/ki.2008.451
   Chiga M, 2011, J CELL SCI, V124, P1391, DOI 10.1242/jcs.084111
   Chobanian AV, 2003, HYPERTENSION, V42, P1206, DOI 10.1161/01.HYP.0000107251.49515.c2
   Chotard E, 2022, RHEUMATOLOGY, V61, P2494, DOI 10.1093/rheumatology/keab578
   Chowdhury JA, 2013, CLIN SCI, V124, P701, DOI 10.1042/CS20120430
   COLLINS R, 1985, BMJ-BRIT MED J, V290, P17, DOI 10.1136/bmj.290.6461.17
   COSTANZO LS, 1985, AM J PHYSIOL, V248, pF527, DOI 10.1152/ajprenal.1985.248.4.F527
   COSTANZO LS, 1976, AM J PHYSIOL, V230, P67, DOI 10.1152/ajplegacy.1976.230.1.67
   COSTANZO LS, 1984, AM J PHYSIOL, V246, pF937, DOI 10.1152/ajprenal.1984.246.6.F937
   Crawford RM, 2001, FASEB J, V15, P102, DOI 10.1096/fj.01-0446fje
   CREMASCHI D, 1983, J MEMBRANE BIOL, V73, P227, DOI 10.1007/BF01870537
   CREMASCHI D, 1987, J MEMBRANE BIOL, V95, P219, DOI 10.1007/BF01869484
   Cruz DN, 2001, KIDNEY INT, V59, P710, DOI 10.1046/j.1523-1755.2001.059002710.x
   Cuevas CA, 2017, J AM SOC NEPHROL, V28, P1814, DOI 10.1681/ASN.2016090935
   Cutler CP, 2001, COMP BIOCHEM PHYS A, V130, P551, DOI 10.1016/S1095-6433(01)00435-4
   Czogalla J, 2016, PFLUG ARCH EUR J PHY, V468, P849, DOI 10.1007/s00424-016-1798-5
   DAHL LK, 1972, J EXP MED, V136, P318, DOI 10.1084/jem.136.2.318
   Daigle ND, 2009, J CELL PHYSIOL, V220, P680, DOI 10.1002/jcp.21814
   Darman RB, 2001, J BIOL CHEM, V276, P34359, DOI 10.1074/jbc.C100368200
   de Baaij JHF, 2012, J BIOL CHEM, V287, P13644, DOI 10.1074/jbc.M112.342204
   de Jong JC, 2003, J BIOL CHEM, V278, P24302, DOI 10.1074/jbc.M303101200
   Delaloy C, 2003, MOL CELL BIOL, V23, P9208, DOI 10.1128/MCB.23.24.9208-9221.2003
   Delpire E, 2007, PHYSIOL GENOMICS, V28, P223, DOI 10.1152/physiolgenomics.00173.2006
   Delpire E, 2009, PFLUG ARCH EUR J PHY, V458, P953, DOI 10.1007/s00424-009-0674-y
   DIAMOND JM, 1962, J PHYSIOL-LONDON, V161, P474, DOI 10.1113/jphysiol.1962.sp006899
   DIENGOTT D, 1953, Harefuah, V44, P227
   Disse-Nicodème S, 2000, AM J HUM GENET, V67, P302, DOI 10.1086/303020
   Duan XP, 2019, HYPERTENSION, V73, P112, DOI 10.1161/HYPERTENSIONAHA.118.11621
   DUFFEY ME, 1979, J MEMBRANE BIOL, V50, P331, DOI 10.1007/BF01868896
   DUFFEY ME, 1984, FED PROC, V43, P444
   Dutta P, 2023, AM J PHYSIOL-RENAL, V324, P274, DOI 10.1152/ajprenal.00296.2022
   Dvorak MM, 2007, J AM SOC NEPHROL, V18, P2509, DOI 10.1681/ASN.2007030348
   EARLEY LE, 1961, J CLIN INVEST, V40, P857, DOI 10.1172/JCI104320
   Ecelbarger CA, 2001, EXP NEUROL, V171, P227, DOI 10.1006/exnr.2001.7775
   Eknoyan G, 1997, KIDNEY INT, pS118
   Elkjær ML, 2002, AM J PHYSIOL-RENAL, V283, pF1376, DOI 10.1152/ajprenal.00186.2002
   Ellison DH, 2009, HYPERTENSION, V54, P196, DOI 10.1161/HYPERTENSIONAHA.109.129171
   ELLISON DH, 1987, MINER ELECTROL METAB, V13, P422
   ELLISON DH, 1987, AM J PHYSIOL, V253, pF546, DOI 10.1152/ajprenal.1987.253.3.F546
   Ellison DH, 2000, AM J PHYSIOL-RENAL, V279, pF616, DOI 10.1152/ajprenal.2000.279.4.F616
   Ellison DH, 1993, GENEREVIEWS
   Elzwawi A, 2020, BIOCHEM BIOPH RES CO, V532, P88, DOI 10.1016/j.bbrc.2020.07.143
   Ernst ME, 2022, AM J HYPERTENS, V35, P573, DOI 10.1093/ajh/hpac048
   Estévez R, 2001, NATURE, V414, P558, DOI 10.1038/35107099
   FANESTIL DD, 1992, SEMIN NEPHROL, V12, P18
   Fanestil DD, 1997, AM J PHYSIOL-REG I, V272, pR2004, DOI 10.1152/ajpregu.1997.272.6.R2004
   Farouk SS, 2020, ADV CHRONIC KIDNEY D, V27, P56, DOI 10.1053/j.ackd.2019.08.006
   Fejes-Tóth G, 2008, AM J PHYSIOL-RENAL, V294, pF1298, DOI 10.1152/ajprenal.00579.2007
   Ferdaus MZ, 2017, JCI INSIGHT, V2, DOI 10.1172/jci.insight.96700
   Ferdaus MZ, 2016, J PHYSIOL-LONDON, V594, P4945, DOI 10.1113/JP272311
   Feric M, 2011, AM J PHYSIOL-CELL PH, V300, pC755, DOI 10.1152/ajpcell.00360.2010
   Ferreira-Martins D, 2016, CONSERV PHYSIOL, V4, DOI 10.1093/conphys/cov064
   Fezai Myriam, 2015, Neurosignals, V23, P20, DOI 10.1159/000442601
   Filippi BM, 2011, EMBO J, V30, P1730, DOI 10.1038/emboj.2011.78
   Flagg TP, 2010, PHYSIOL REV, V90, P799, DOI 10.1152/physrev.00027.2009
   Flatman PW, 2008, CURR OPIN NEPHROL HY, V17, P186, DOI 10.1097/MNH.0b013e3282f5244e
   Frame AA, 2019, AM J PHYSIOL-RENAL, V317, pF1623, DOI 10.1152/ajprenal.00264.2019
   Fraser SA, 2007, BIOCHEM J, V405, P85, DOI 10.1042/BJ20061850
   Frindt G, 2017, AM J PHYSIOL-RENAL, V313, pF62, DOI 10.1152/ajprenal.00668.2016
   Frindt G, 2010, AM J PHYSIOL-RENAL, V299, pF890, DOI 10.1152/ajprenal.00323.2010
   Frizzell RA, 2012, CSH PERSPECT MED, V2, DOI 10.1101/cshperspect.a009563
   Furgeson SB, 2010, J AM SOC NEPHROL, V21, P1842, DOI 10.1681/ASN.2010050457
   Furusho T, 2020, HYPERTENS RES, V43, P733, DOI 10.1038/s41440-020-0437-x
   Furusho T, 2020, KIDNEY INT, V97, P713, DOI 10.1016/j.kint.2019.11.021
   Gagnon É, 2002, AM J PHYSIOL-RENAL, V283, pF1046, DOI 10.1152/ajprenal.00107.2002
   Gagnon KB, 2012, PHYSIOL REV, V92, P1577, DOI 10.1152/physrev.00009.2012
   Gallafassi EA, 2023, BRAZ J MED BIOL RES, V56, DOI [10.1590/1414-431X2023e12392, 10.1590/1414-431x2023e12392]
   GAMBA G, 1993, P NATL ACAD SCI USA, V90, P2749, DOI 10.1073/pnas.90.7.2749
   Gamba G, 2005, PHYSIOL REV, V85, P423, DOI 10.1152/physrev.00011.2004
   Gamba G, 2005, AM J PHYSIOL-RENAL, V288, pF245, DOI 10.1152/ajprenal.00311.2004
   GAMBA G, 1994, J BIOL CHEM, V269, P17713
   Gamba G, 2009, AM J PHYSIOL-RENAL, V297, pF838, DOI 10.1152/ajprenal.00159.2009
   Gao X, 2010, NATURE, V463, P828, DOI 10.1038/nature08741
   Garneau AP, 2020, PHYSIOLOGY, V35, P415, DOI 10.1152/physiol.00012.2020
   Garneau AP, 2019, J HEMATOL ONCOL, V12, DOI 10.1186/s13045-019-0766-x
   Garneau AP, 2019, J PHYSIOL-LONDON, V597, P1451, DOI 10.1113/JP276807
   Garneau AP, 2017, AM J PHYSIOL-CELL PH, V313, pC516, DOI 10.1152/ajpcell.00106.2017
   Garneau AP, 2022, J CELL PHYSIOL, V237, P4356, DOI 10.1002/jcp.30879
   GECK P, 1980, BIOCHIM BIOPHYS ACTA, V600, P432, DOI 10.1016/0005-2736(80)90446-0
   Gerelsaikhan T, 2006, BIOCHEMISTRY-US, V45, P12060, DOI 10.1021/bi061126x
   GESEK FA, 1992, J CLIN INVEST, V90, P429, DOI 10.1172/JCI115878
   GESEK FA, 1992, J CLIN INVEST, V90, P749, DOI 10.1172/JCI115947
   Gillen CM, 1996, J BIOL CHEM, V271, P16237, DOI 10.1074/jbc.271.27.16237
   Giménez I, 2002, J BIOL CHEM, V277, P8767, DOI 10.1074/jbc.C200021200
   Giménez I, 2007, J BIOL CHEM, V282, P6540, DOI 10.1074/jbc.M610780200
   Gitelman H J, 1966, Trans Assoc Am Physicians, V79, P221
   Gitelman Syndrome Collaborative Study Group, 2017, Zhonghua Nei Ke Za Zhi, V56, P712, DOI 10.3760/cma.j.issn.0578-1426.2017.09.021
   Glover M, 2014, CLIN SCI, V126, P721, DOI 10.1042/CS20130326
   Glover M, 2010, CAN J PHYSIOL PHARM, V88, P986, DOI [10.1139/Y10-080, 10.1139/y10-080]
   Glover M, 2009, J AM SOC NEPHROL, V20, P1314, DOI 10.1681/ASN.2008050542
   Goel P, 2015, GENE, V557, P1, DOI 10.1016/j.gene.2014.11.051
   GOOD DW, 1984, AM J PHYSIOL, V246, pF609, DOI 10.1152/ajprenal.1984.246.5.F609
   GORDON RD, 1970, AUSTRALAS ANN MED, V19, P287
   Graca JAZ, 2016, AM J PHYSIOL-RENAL, V310, pF518, DOI 10.1152/ajprenal.00208.2015
   Grimm PR, 2017, J AM SOC NEPHROL, V28, P2598, DOI 10.1681/ASN.2016090948
   Grimm PR, 2012, J BIOL CHEM, V287, DOI 10.1074/jbc.M112.402800
   Gunaratne R, 2010, P NATL ACAD SCI USA, V107, P15653, DOI 10.1073/pnas.1007424107
   GUNNELLS JC, 1975, ANNU REV MED, V26, P259, DOI 10.1146/annurev.me.26.020175.001355
   GUPTA AK, 1992, HYPERTENSION, V19, pI78, DOI 10.1161/01.HYP.19.1_Suppl.I78
   HAAS M, 1983, AM J PHYSIOL, V245, pC235, DOI 10.1152/ajpcell.1983.245.3.C235
   Hadchouel J, 2016, ANNU REV PHYSIOL, V78, P367, DOI 10.1146/annurev-physiol-021115-105431
   Hadchouel J, 2010, P NATL ACAD SCI USA, V107, P18109, DOI 10.1073/pnas.1006128107
   Hamann S, 2005, J PHYSIOL-LONDON, V568, P123, DOI 10.1113/jphysiol.2005.093526
   Hamann S, 2010, J PHYSIOL-LONDON, V588, P4089, DOI 10.1113/jphysiol.2010.194738
   Han YF, 2011, CLIN BIOCHEM, V44, P1045, DOI 10.1016/j.clinbiochem.2011.06.008
   Hanna RM, 2022, FRONT ENDOCRINOL, V12, DOI 10.3389/fendo.2021.762130
   HANSEN LL, 1981, PFLUG ARCH EUR J PHY, V389, P121, DOI 10.1007/BF00582101
   Hennings JC, 2017, J AM SOC NEPHROL, V28, P209, DOI 10.1681/ASN.2016010085
   Hiki K, 1999, J BIOL CHEM, V274, P10661, DOI 10.1074/jbc.274.15.10661
   Hix JK, 2011, SEMIN NEPHROL, V31, P553, DOI 10.1016/j.semnephrol.2011.09.010
   Hoorn EJ, 2020, PHYSIOL REV, V100, P321, DOI 10.1152/physrev.00044.2018
   Hoorn EJ, 2012, J NEPHROL, V25, P269, DOI 10.5301/jn.5000174
   Hoorn EJ, 2011, NAT MED, V17, P1304, DOI 10.1038/nm.2497
   Hoorn EJ, 2011, J AM SOC NEPHROL, V22, P605, DOI 10.1681/ASN.2010080827
   Hoover RS, 2016, AM J PHYSIOL-RENAL, V310, pF144, DOI 10.1152/ajprenal.00323.2015
   Hoover RS, 2003, J AM SOC NEPHROL, V14, P271, DOI 10.1097/01.ASN.0000043903.93452.D0
   Horita S, 2011, INT J HYPERTENS, V2011, DOI 10.4061/2011/391762
   HOWELL SL, 1968, BIOCHEM J, V108, P17, DOI 10.1042/bj1080017
   Hsu YJ, 2015, J BONE MINER RES, V30, P116, DOI 10.1002/jbmr.2306
   Huang CF, 2007, AM J PHYSIOL-RENAL, V292, pF1073, DOI 10.1152/ajprenal.00269.2006
   Huang LF, 2015, BMC SYST BIOL, V9, DOI 10.1186/s12918-015-0157-z
   Huttlin EL, 2010, CELL, V143, P1174, DOI 10.1016/j.cell.2010.12.001
   Hwang Kyu Sig, 2010, Electrolyte Blood Press, V8, P51, DOI 10.5049/EBP.2010.8.1.51
   IKEHARA T, 1993, J MEMBRANE BIOL, V132, P115
   Imaseki I, 2019, J EXP BIOL, V222, DOI 10.1242/jeb.201780
   ISENRING P, 1992, HYPERTENSION, V19, P371, DOI 10.1161/01.HYP.19.4.371
   Isenring P, 1998, J GEN PHYSIOL, V112, P549, DOI 10.1085/jgp.112.5.549
   Isenring P, 1998, P NATL ACAD SCI USA, V95, P7179, DOI 10.1073/pnas.95.12.7179
   Isenring P, 1997, J BIOL CHEM, V272, P24556, DOI 10.1074/jbc.272.39.24556
   Isenring P, 2001, COMP BIOCHEM PHYS A, V130, P487, DOI 10.1016/S1095-6433(01)00420-2
   Ishizawa K, 2019, P NATL ACAD SCI USA, V116, P3155, DOI 10.1073/pnas.1817281116
   Ishizawa K, 2016, BIOCHEM BIOPH RES CO, V480, P745, DOI 10.1016/j.bbrc.2016.10.127
   Itoh K, 2014, BIOCHEM BIOPH RES CO, V453, P356, DOI 10.1016/j.bbrc.2014.09.089
   Ivy JR, 2016, HYPERTENSION, V67, P1029, DOI 10.1161/HYPERTENSIONAHA.115.06977
   Ivy JR, 2019, AM J PHYSIOL-RENAL, V317, pF1536, DOI 10.1152/ajprenal.00372.2019
   Jacoby SC, 1999, AM J PHYSIOL-CELL PH, V277, pC684, DOI 10.1152/ajpcell.1999.277.4.C684
   Jensen IS, 2016, ACTA PHYSIOL, V218, P49, DOI 10.1111/apha.12707
   Johnson AD, 2011, HYPERTENSION, V57, P903, DOI 10.1161/HYPERTENSIONAHA.110.158667
   Kato A, 2011, AM J PHYSIOL-REG I, V300, pR284, DOI 10.1152/ajpregu.00725.2009
   Khan O, 2005, AM J PHYSIOL-RENAL, V289, pF442, DOI 10.1152/ajprenal.00335.2004
   Kim GH, 1998, P NATL ACAD SCI USA, V95, P14552, DOI 10.1073/pnas.95.24.14552
   KINNE R, 1986, PFLUG ARCH EUR J PHY, V407, pS168, DOI 10.1007/BF00584947
   Knoers NVAM, 2008, ORPHANET J RARE DIS, V3, DOI 10.1186/1750-1172-3-22
   Ko B, 2015, AM J PHYSIOL-RENAL, V308, pF720, DOI 10.1152/ajprenal.00465.2014
   Ko B, 2013, AM J PHYSIOL-RENAL, V305, pF645, DOI 10.1152/ajprenal.00053.2013
   Ko B, 2011, TRANSL RES, V158, P282, DOI 10.1016/j.trsl.2011.07.005
   Ko B, 2009, CURR OPIN NEPHROL HY, V18, P421, DOI 10.1097/MNH.0b013e32832f2fcb
   Kobayashi K, 2001, J AM SOC NEPHROL, V12, P1327, DOI 10.1681/ASN.V1271327
   Kokubo Y, 2004, J HUM GENET, V49, P507, DOI 10.1007/s10038-004-0181-0
   Komers R, 2012, CLIN SCI, V123, P635, DOI 10.1042/CS20120003
   Kondo A, 2021, SCI REP-UK, V11, DOI 10.1038/s41598-021-95521-6
   Krämer BK, 2008, NAT CLIN PRACT NEPHR, V4, P38, DOI 10.1038/ncpneph0689
   KRISHNA GG, 1989, NEW ENGL J MED, V320, P1177, DOI 10.1056/NEJM198905043201804
   Kumar GN, 2004, DRUG METAB DISPOS, V32, P1491, DOI 10.1124/dmd.104.000604
   KUNAU RT, 1975, J CLIN INVEST, V56, P401, DOI 10.1172/JCI108105
   Lai JG, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0106129
   Lang F, 2006, PHYSIOL REV, V86, P1151, DOI 10.1152/physrev.00050.2005
   Lang F, 2009, EXPERT OPIN THER TAR, V13, P1303, DOI 10.1517/14728220903260807
   Lang H, 1995, Diuretics
   Larkins N, 2014, CLIN KIDNEY J, V7, DOI 10.1093/ckj/sfu029
   Lee CT, 2004, AM J PHYSIOL-RENAL, V287, pF1164, DOI 10.1152/ajprenal.00437.2003
   LEVY RI, 1958, J CLIN INVEST, V37, P1016, DOI 10.1172/JCI103682
   Lewis D S, 1920, Can Med Assoc J, V10, P578
   Lewis S, 2021, AM J PHYSIOL-CELL PH, V321, pC507, DOI 10.1152/ajpcell.00197.2021
   Lin DH, 2012, AM J PHYSIOL-RENAL, V303, pF110, DOI 10.1152/ajprenal.00676.2011
   Lin SH, 2011, P NATL ACAD SCI USA, V108, P17538, DOI 10.1073/pnas.1107452108
   Liu S, 2019, SCIENCE, V366, P505, DOI 10.1126/science.aay3129
   Liu Z, 2011, HUM MOL GENET, V20, P855, DOI 10.1093/hmg/ddq525
   Loffing J, 2006, ANNU REV PHYSIOL, V68, P461, DOI 10.1146/annurev.physiol.68.040104.131654
   Loffing J, 2004, J AM SOC NEPHROL, V15, P2276, DOI 10.1097/01.ASN.0000138234.18569.63
   Loffing J, 2001, AM J PHYSIOL-RENAL, V281, pF1021, DOI 10.1152/ajprenal.0085.2001
   Long WT, 2018, METHODS MOL BIOL, V1713, P45, DOI 10.1007/978-1-4939-7507-5_4
   Louis-Dit-Picard H, 2020, J CLIN INVEST, V130, P6379, DOI 10.1172/JCI94171
   Louis-Dit-Picard H, 2012, NAT GENET, V44, P456, DOI 10.1038/ng.2218
   Loureiro CA, 2019, ARCH BIOCHEM BIOPHYS, V669, P61, DOI 10.1016/j.abb.2019.05.022
   Lytle C, 1998, AM J PHYSIOL-CELL PH, V274, pC299, DOI 10.1152/ajpcell.1998.274.2.C299
   Pleinis JM, 2021, AM J PHYSIOL-CELL PH, V320, pC703, DOI 10.1152/ajpcell.00456.2020
   Mabillard H, 2019, GENES-BASEL, V10, DOI 10.3390/genes10120986
   MACLEAN D, 1983, BRIT MED J, V286, P1419, DOI 10.1136/bmj.286.6375.1419
   Maeoka Y, 2022, AM J PHYSIOL-RENAL, V323, pF564, DOI 10.1152/ajprenal.00153.2022
   Maeoka Y, 2020, AM J PHYSIOL-RENAL, V319, pF1043, DOI 10.1152/ajprenal.00463.2020
   Mamalis D, 2020, SAUDI J KIDNEY DIS T, V31, P259, DOI 10.4103/1319-2442.279949
   Marcoux AA, 2017, BBA-GEN SUBJECTS, V1861, P3154, DOI 10.1016/j.bbagen.2017.09.007
   Marcoux AA, 2021, J CELL PHYSIOL, V236, P1712, DOI 10.1002/jcp.29997
   Marcoux AA, 2019, AM J PHYSIOL-CELL PH, V317, pC20, DOI 10.1152/ajpcell.00041.2019
   Markkanen M, 2017, BRAIN RES, V1675, P87, DOI 10.1016/j.brainres.2017.08.034
   MARUMO F, 1982, PHARMACOLOGY, V24, P175, DOI 10.1159/000137593
   Mastroianni N, 1996, GENOMICS, V35, P486, DOI 10.1006/geno.1996.0388
   Mayan H, 2002, J CLIN ENDOCR METAB, V87, P3248, DOI 10.1210/jc.87.7.3248
   Mayan H, 2018, PHYSIOL REP, V6, DOI 10.14814/phy2.13843
   McCormick JA, 2015, COMPR PHYSIOL, V5, P45, DOI 10.1002/cphy.c140002
   McCormick JA, 2014, J CLIN INVEST, V124, P4723, DOI 10.1172/JCI76126
   McCormick JA, 2011, CELL METAB, V14, P352, DOI 10.1016/j.cmet.2011.07.009
   McCormick JA, 2011, PHYSIOL REV, V91, P177, DOI 10.1152/physrev.00017.2010
   McKee JA, 2000, J AM SOC NEPHROL, V11, P2128, DOI 10.1681/ASN.V11112128
   Mehellou Y, 2018, BIOCHEM BIOPH RES CO, V503, P1868, DOI 10.1016/j.bbrc.2018.07.128
   Mein CA, 2004, HUM MOL GENET, V13, pR169, DOI 10.1093/hmg/ddh078
   Melander O, 2000, HYPERTENSION, V36, P389, DOI 10.1161/01.HYP.36.3.389
   Melnikov S, 2011, EUR J CLIN INVEST, V41, P1113, DOI 10.1111/j.1365-2362.2011.02517.x
   MENEELY GR, 1958, AM J MED, V25, P713, DOI 10.1016/0002-9343(58)90009-3
   Mente A, 2014, NEW ENGL J MED, V371, P601, DOI 10.1056/NEJMoa1311989
   MIYAMOTO H, 1986, J MEMBRANE BIOL, V92, P135, DOI 10.1007/BF01870703
   Moes AD, 2014, PFLUG ARCH EUR J PHY, V466, P107, DOI 10.1007/s00424-013-1407-9
   Monnens L, 1998, NEPHROL DIAL TRANSPL, V13, P1617, DOI 10.1093/ndt/13.7.1617
   Monroy A, 2000, AM J PHYSIOL-RENAL, V279, pF161, DOI 10.1152/ajprenal.2000.279.1.F161
   MOORE ML, 1995, BIOCHEM J, V309, P637, DOI 10.1042/bj3090637
   Moore-Hoon ML, 2000, BIOCHEMISTRY-US, V39, P3718, DOI 10.1021/bi992301v
   Moreno E, 2004, J BIOL CHEM, V279, P16553, DOI 10.1074/jbc.M400602200
   Moreno E, 2023, FRONT PHYSIOL, V14, DOI 10.3389/fphys.2023.1118706
   Moreno E, 2022, AM J PHYSIOL-CELL PH, V323, pC385, DOI 10.1152/ajpcell.00213.2022
   Moreno E, 2006, J BIOL CHEM, V281, P17266, DOI 10.1074/jbc.M602614200
   Moreno E, 2016, J BIOL CHEM, V291, P22472, DOI 10.1074/jbc.M116.742783
   Moriguchi T, 2005, J BIOL CHEM, V280, P42685, DOI 10.1074/jbc.M510042200
   Moseng MA, 2022, SCI ADV, V8, DOI 10.1126/sciadv.abq0952
   Motoshima T, 2023, PHYSIOL GENOMICS, V55, P113, DOI 10.1152/physiolgenomics.00143.2022
   Mount DB, 2014, CLIN J AM SOC NEPHRO, V9, P1974, DOI 10.2215/CJN.04480413
   Mount DB, 1999, J BIOL CHEM, V274, P16355, DOI 10.1074/jbc.274.23.16355
   Mu S, 2011, NAT MED, V17, P573, DOI 10.1038/nm.2337
   MULLINS MM, 1983, AM J PHYSIOL, V244, pH652, DOI 10.1152/ajpheart.1983.244.5.H652
   Murthy M, 2017, CELL MOL LIFE SCI, V74, P1261, DOI 10.1007/s00018-016-2402-z
   Mutig K, 2007, AM J PHYSIOL-RENAL, V293, pF1166, DOI 10.1152/ajprenal.00196.2007
   Mutig K, 2010, AM J PHYSIOL-RENAL, V298, pF502, DOI 10.1152/ajprenal.00476.2009
   Mutig K, 2016, AM J PHYSIOL-RENAL, V311, pF411, DOI 10.1152/ajprenal.00126.2016
   Na T, 2013, AM J PHYSIOL-RENAL, V304, pF8, DOI 10.1152/ajprenal.00284.2012
   Nan J, 2022, SCI ADV, V8, DOI 10.1126/sciadv.add7176
   Newhouse SJ, 2005, HUM MOL GENET, V14, P1805, DOI 10.1093/hmg/ddi187
   Ng HY, 2021, NUTRIENTS, V13, DOI 10.3390/nu13114088
   Nicolet-Barousse L, 2005, J BONE MINER RES, V20, P799, DOI 10.1359/JBMR.041238
   Nielsen J, 2002, AM J PHYSIOL-RENAL, V283, pF923, DOI 10.1152/ajprenal.00015.2002
   Nijenhuis T, 2005, J CLIN INVEST, V115, P1651, DOI 10.1172/JCI24134
   Nishida H, 2012, HYPERTENSION, V60, P981, DOI 10.1161/HYPERTENSIONAHA.112.201509
   Nissant A, 2006, AM J PHYSIOL-RENAL, V290, pF1421, DOI 10.1152/ajprenal.00274.2005
   Nomura N, 2019, CLIN EXP NEPHROL, V23, P1175, DOI 10.1007/s10157-019-01766-x
   Nomura N, 2018, BIOSCIENCE REP, V38, DOI 10.1042/BSR20171243
   Norn Svend, 2008, Dan Medicinhist Arbog, V36, P21
   O'Reilly M, 2003, J AM SOC NEPHROL, V14, P2447, DOI 10.1097/01.ASN.0000089830.97681.3B
   O'Shaughnessy KM, 2015, PEDIATR NEPHROL, V30, P1903, DOI 10.1007/s00467-014-2956-7
   Obermuller N, 1995, AM J PHYSIOL-RENAL, V269, pF900, DOI 10.1152/ajprenal.1995.269.6.F900
   Ohta A, 2013, BIOCHEM J, V451, P111, DOI 10.1042/BJ20121903
   Ohta A, 2009, HUM MOL GENET, V18, P3978, DOI 10.1093/hmg/ddp344
   Hanhof CJAO, 2021, TISSUE ENG PART C-ME, V27, P200, DOI [10.1089/ten.tec.2020.0345, 10.1089/ten.TEC.2020.0345]
   OLESEN OV, 1982, J PHARMACOL EXP THER, V220, P178
   Osada Y, 2009, J HUM GENET, V54, P474, DOI 10.1038/jhg.2009.64
   Ostroverkhova DS, 2020, CELLS-BASEL, V9, DOI 10.3390/cells9071644
   Ott C, 2022, KIDNEY INT, V101, P36, DOI 10.1016/j.kint.2021.09.026
   Arroyo JP, 2011, J AM SOC NEPHROL, V22, P1707, DOI 10.1681/ASN.2011020132
   Pacheco-Alvarez D, 2006, J BIOL CHEM, V281, P28755, DOI 10.1074/jbc.M603773200
   Pacheco-Alvarez D, 2020, AM J PHYSIOL-CELL PH, V319, pC371, DOI 10.1152/ajpcell.00488.2019
   Padhi D, 2009, CLIN PHARMACOKINET, V48, P303, DOI 10.2165/00003088-200948050-00002
   Palmer BF, 2015, CLIN J AM SOC NEPHRO, V10, P1050, DOI 10.2215/CJN.08580813
   Palygin O, 2017, ACTA PHYSIOL, V219, P260, DOI 10.1111/apha.12703
   Pandya C, 2014, J BIOL CHEM, V289, P30229, DOI 10.1074/jbc.R114.572990
   Bahena-Lopez JP, 2023, J AM SOC NEPHROL, V34, P55, DOI 10.1681/ASN.2021121544
   Pathare G, 2013, AM J PHYSIOL-RENAL, V305, pF1513, DOI 10.1152/ajprenal.00440.2013
   Paulais M, 2011, P NATL ACAD SCI USA, V108, P10361, DOI 10.1073/pnas.1101400108
   Pearce D, 2003, CELL PHYSIOL BIOCHEM, V13, P13, DOI 10.1159/000070245
   Pedersen NB, 2010, KIDNEY INT, V78, P160, DOI 10.1038/ki.2010.130
   Penton D, 2019, J AM SOC NEPHROL, V30, P737, DOI 10.1681/ASN.2018050540
   Penton D, 2016, J PHYSIOL-LONDON, V594, P6319, DOI 10.1113/JP272504
   Piala AT, 2014, SCI SIGNAL, V7, DOI 10.1126/scisignal.2005050
   Picard N, 2014, J AM SOC NEPHROL, V25, P511, DOI 10.1681/ASN.2012121202
   Pickering TG, 2001, CURR OPIN NEPHROL HY, V10, P611, DOI 10.1097/00041552-200109000-00010
   Piechotta K, 2002, J BIOL CHEM, V277, P50812, DOI 10.1074/jbc.M208108200
   Pike Sharon, 2019, Curr Protoc Plant Biol, V4, pe20087, DOI 10.1002/cppb.20087
   Plotkin MD, 1996, KIDNEY INT, V50, P174, DOI 10.1038/ki.1996.300
   Podymow T, 2011, SEMIN NEPHROL, V31, P70, DOI 10.1016/j.semnephrol.2010.10.007
   Pollak MR, 1996, J AM SOC NEPHROL, V7, P2244
   Ponce-Coria J, 2012, AM J PHYSIOL-CELL PH, V303, pC1198, DOI 10.1152/ajpcell.00284.2012
   Portioli C, 2021, TRENDS CHEM, V3, P832, DOI 10.1016/j.trechm.2021.05.004
   Poulsen SB, 2021, KIDNEY INT, V100, P321, DOI 10.1016/j.kint.2021.04.021
   PRESCOTT LF, 1964, BRIT MED J, V1, P1438, DOI 10.1136/bmj.1.5395.1438
   Quinn SJ, 1998, J BIOL CHEM, V273, P19579, DOI 10.1074/jbc.273.31.19579
   Race JE, 1999, AM J PHYSIOL-CELL PH, V277, pC1210, DOI 10.1152/ajpcell.1999.277.6.C1210
   Murillo-de-Ozores AR, 2018, J BIOL CHEM, V293, P12209, DOI 10.1074/jbc.RA118.003037
   Rafiqi FH, 2010, EMBO MOL MED, V2, P63, DOI 10.1002/emmm.200900058
   Rashmi P, 2017, KIDNEY INT, V91, P1159, DOI 10.1016/j.kint.2016.10.038
   Reiche J, 2010, MOL CELL BIOL, V30, P3027, DOI 10.1128/MCB.01560-09
   Reid MS, 2020, ELIFE, V9, DOI 10.7554/eLife.52505
   Reilly RF, 2011, NAT REV NEPHROL, V7, P669, DOI 10.1038/nrneph.2011.138
   Ren H, 2013, AM J NEPHROL, V37, P152, DOI 10.1159/000346708
   RENFRO JL, 1977, J EXP ZOOL, V199, P383, DOI 10.1002/jez.1401990311
   RENFRO JL, 1975, AM J PHYSIOL, V228, P52, DOI 10.1152/ajplegacy.1975.228.1.52
   Rengarajan S, 2014, AM J PHYSIOL-RENAL, V306, pF1059, DOI 10.1152/ajprenal.00015.2014
   Reungjui S, 2007, KIDNEY INT, V72, P1483, DOI 10.1038/sj.ki.5002564
   Reungjui S, 2007, J AM SOC NEPHROL, V18, P2724, DOI 10.1681/ASN.2007040416
   Reyes JV, 2022, AM J TRANSL RES, V14, P1
   Riccardi D, 2010, AM J PHYSIOL-RENAL, V298, pF485, DOI 10.1152/ajprenal.00608.2009
   Richards J, 2014, J BIOL CHEM, V289, P11791, DOI 10.1074/jbc.M113.531095
   Richardson C, 2008, J CELL SCI, V121, P675, DOI 10.1242/jcs.025312
   Rieg T, 2013, AM J PATHOL, V182, P96, DOI 10.1016/j.ajpath.2012.09.014
   Ring AM, 2007, P NATL ACAD SCI USA, V104, P4025, DOI 10.1073/pnas.0611728104
   Riveira-Munoz E, 2007, J AM SOC NEPHROL, V18, P1271, DOI 10.1681/ASN.2006101095
   Ronzaud C, 2013, J CLIN INVEST, V123, P657, DOI 10.1172/JCI61110
   Rosenbaek LL, 2018, SCI REP-UK, V8, DOI 10.1038/s41598-018-22153-8
   Rosenbaek LL, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-12819-0
   Rosenbaek LL, 2017, AM J PHYSIOL-RENAL, V313, pF495, DOI 10.1152/ajprenal.00088.2017
   ROWE JW, 1980, METABOLISM, V29, P498, DOI 10.1016/0026-0495(80)90074-8
   Roy A, 2015, J CLIN INVEST, V125, P3433, DOI 10.1172/JCI75245
   Rozansky DJ, 2009, J CLIN INVEST, V119, P2601, DOI 10.1172/JCI38323
   Sabath E, 2004, AM J PHYSIOL-RENAL, V287, pF195, DOI 10.1152/ajprenal.00044.2004
   San-Cristobal P, 2008, AM J PHYSIOL-RENAL, V295, pF1199, DOI 10.1152/ajprenal.90396.2008
   San-Cristobal P, 2009, P NATL ACAD SCI USA, V106, P4384, DOI 10.1073/pnas.0813238106
   Sandberg MB, 2007, AM J PHYSIOL-RENAL, V293, pF662, DOI 10.1152/ajprenal.00064.2007
   Saritas T, 2013, J AM SOC NEPHROL, V24, P407, DOI 10.1681/ASN.2012040404
   Schnoz C, 2021, PFLUG ARCH EUR J PHY, V473, P79, DOI 10.1007/s00424-020-02491-1
   Scholl UI, 2009, P NATL ACAD SCI USA, V106, P5842, DOI 10.1073/pnas.0901749106
   Schultheis PJ, 1998, J BIOL CHEM, V273, P29150, DOI 10.1074/jbc.273.44.29150
   Schumacher FR, 2015, EMBO MOL MED, V7, P1285, DOI 10.15252/emmm.201505444
   Sealey JE, 2005, TRENDS ENDOCRIN MET, V16, P86, DOI 10.1016/j.tem.2005.02.006
   Segel IH., 1993, Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and SteadyState Enzyme Systems
   SELDIN DW, 1966, ANN NY ACAD SCI, V139, P328, DOI 10.1111/j.1749-6632.1966.tb41207.x
   Shaer AJ, 2001, AM J MED SCI, V322, P316, DOI 10.1097/00000441-200112000-00004
   Shaffer PL, 2009, SCIENCE, V325, P1010, DOI 10.1126/science.1176088
   Shibata S, 2014, P NATL ACAD SCI USA, V111, P15556, DOI 10.1073/pnas.1418342111
   Shibata S, 2013, P NATL ACAD SCI USA, V110, P7838, DOI 10.1073/pnas.1304592110
   SHIMIZU T, 1991, TOHOKU J EXP MED, V164, P293, DOI 10.1620/tjem.164.293
   SHIRLEY DG, 1987, BRIT J PHARMACOL, V91, P693, DOI 10.1111/j.1476-5381.1987.tb11264.x
   Shoda W, 2017, KIDNEY INT, V91, P402, DOI 10.1016/j.kint.2016.09.001
   Siddiq MA, 2017, CURR OPIN STRUC BIOL, V47, P113, DOI 10.1016/j.sbi.2017.07.003
   Simard CF, 2004, J BIOL CHEM, V279, P40769, DOI 10.1074/jbc.M406458200
   Simon DB, 1996, NAT GENET, V12, P24, DOI 10.1038/ng0196-24
   SKRABAL F, 1981, LANCET, V2, P895
   SMITH JB, 1984, CLIN CHIM ACTA, V137, P169, DOI 10.1016/0009-8981(84)90177-3
   Sneader W, 2005, DRUG DISCOVERY: A HISTORY, P1, DOI 10.1002/0470015535
   Sohara E, 2016, NEPHROL DIAL TRANSPL, V31, P1417, DOI 10.1093/ndt/gfv259
   Sohara E, 2011, PLOS ONE, V6, DOI 10.1371/journal.pone.0024277
   Somasekharan S, 2012, J BIOL CHEM, V287, P17308, DOI 10.1074/jbc.M112.356014
   Song J, 2006, AM J PHYSIOL-RENAL, V290, pF1055, DOI 10.1152/ajprenal.00108.2005
   Song YL, 2001, J HYPERTENS, V19, P1547, DOI 10.1097/00004872-200109000-00005
   Sorensen MV, 2013, KIDNEY INT, V83, P811, DOI 10.1038/ki.2013.14
   STAESSEN JA, 1993, J HYPERTENS, V11, P443, DOI 10.1097/00004872-199304000-00016
   STANTON BA, 1986, J CLIN INVEST, V78, P1612, DOI 10.1172/JCI112754
   STANTON BA, 1981, KIDNEY INT, V19, P36, DOI 10.1038/ki.1981.5
   Steffensen AB, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-04677-9
   STEIN JH, 1975, PHYSIOL REV, V55, P127, DOI 10.1152/physrev.1975.55.1.127
   Stergiou G, 2022, J HYPERTENS, V40, P1847, DOI 10.1097/HJH.0000000000003240
   STOKES JB, 1989, KIDNEY INT, V36, P427, DOI 10.1038/ki.1989.212
   STOKES JB, 1984, J CLIN INVEST, V74, P7, DOI 10.1172/JCI111420
   Stow LR, 2011, J AM SOC NEPHROL, V22, P598, DOI 10.1681/ASN.2010080803
   Su XT, 2019, AM J PHYSIOL-RENAL, V316, pF582, DOI 10.1152/ajprenal.00412.2018
   Su XT, 2016, AM J PHYSIOL-RENAL, V311, pF12, DOI 10.1152/ajprenal.00112.2016
   Subramanya AR, 2006, AM J PHYSIOL-RENAL, V290, pF619, DOI 10.1152/ajprenal.00280.2005
   Subramanya AR, 2014, CLIN J AM SOC NEPHRO, V9, P2147, DOI 10.2215/CJN.05920613
   Suh SH, 2021, NUTRIENTS, V13, DOI 10.3390/nu13124443
   SUKI W, 1965, J CLIN INVEST, V44, P1458, DOI 10.1172/JCI105252
   Sun QF, 2018, J AM SOC NEPHROL, V29, P1449, DOI 10.1681/ASN.2017101091
   Susa K, 2014, HUM MOL GENET, V23, P5052, DOI 10.1093/hmg/ddu217
   Susa K, 2012, BIOCHEM BIOPH RES CO, V427, P743, DOI 10.1016/j.bbrc.2012.09.130
   Takahashi D, 2014, BIOSCIENCE REP, V34, P195, DOI 10.1042/BSR20140047
   Taniyama Y, 2001, J BIOL CHEM, V276, P26260, DOI 10.1074/jbc.M101614200
   Taylor CA, 2018, P NATL ACAD SCI USA, V115, P3840, DOI 10.1073/pnas.1802339115
   Teranishi K, 2013, COMP BIOCHEM PHYS A, V164, P333, DOI 10.1016/j.cbpa.2012.11.011
   Terker AS, 2018, AM J PHYSIOL-RENAL, V315, pF781, DOI 10.1152/ajprenal.00485.2017
   Terker AS, 2016, J AM SOC NEPHROL, V27, P2436, DOI 10.1681/ASN.2015070815
   Terker AS, 2016, KIDNEY INT, V89, P127, DOI 10.1038/ki.2015.289
   Terker AS, 2015, CELL METAB, V21, P39, DOI 10.1016/j.cmet.2014.12.006
   Terker AS, 2014, HYPERTENSION, V64, P178, DOI 10.1161/HYPERTENSIONAHA.114.03335
   Teulon J, 2019, COMPR PHYSIOL, V9, P301, DOI 10.1002/cphy.c180024
   Thastrup JO, 2012, BIOCHEM J, V441, P325, DOI 10.1042/BJ20111879
   Thomson MN, 2019, AM J PHYSIOL-RENAL, V316, pF292, DOI 10.1152/ajprenal.00464.2018
   Toal C B, 1983, J Hypertens, V1, P345, DOI 10.1097/00004872-198312000-00004
   Topala CN, 2009, CELL CALCIUM, V45, P331, DOI 10.1016/j.ceca.2008.12.003
   TRAN JM, 1990, AM J PHYSIOL, V258, pF908, DOI 10.1152/ajprenal.1990.258.4.F908
   Tsuji S, 2013, BMC NEPHROL, V14, DOI 10.1186/1471-2369-14-166
   Tumlin JA, 1997, AM J KIDNEY DIS, V30, P884, DOI 10.1016/S0272-6386(97)90100-1
   TURNER RJ, 1988, J MEMBRANE BIOL, V102, P71, DOI 10.1007/BF01875354
   Tutakhel OAZ, 2018, FASEB J, V32, P4482, DOI 10.1096/fj.201701047R
   Tutakhel OAZ, 2016, AM J PHYSIOL-RENAL, V310, pF204, DOI 10.1152/ajprenal.00429.2015
   Urwin S, 2020, CLIN ENDOCRINOL, V92, P3, DOI 10.1111/cen.14104
   Valdez-Flores MA, 2016, AM J PHYSIOL-RENAL, V311, pF1159, DOI 10.1152/ajprenal.00124.2016
   Vallon V, 2005, AM J PHYSIOL-REG I, V288, pR4, DOI 10.1152/ajpregu.00369.2004
   Vallon V, 2009, AM J PHYSIOL-RENAL, V297, pF704, DOI 10.1152/ajprenal.00030.2009
   van der Lubbe N, 2013, CURR OPIN NEPHROL HY, V22, P120, DOI 10.1097/MNH.0b013e32835b6551
   van der Lubbe N, 2012, PFLUG ARCH EUR J PHY, V463, P853, DOI 10.1007/s00424-012-1104-0
   van der Lubbe N, 2011, KIDNEY INT, V79, P66, DOI 10.1038/ki.2010.290
   Van Laecke S, 2019, ACTA CLIN BELG, V74, P41, DOI 10.1080/17843286.2018.1516173
   van Megen WH, 2018, PHYSIOL REP, V6, DOI 10.14814/phy2.13728
   Vázquez N, 2002, AM J PHYSIOL-RENAL, V282, pF599, DOI 10.1152/ajprenal.00284.2001
   VELAZQUEZ H, 1986, AM J PHYSIOL, V250, P1013, DOI 10.1152/ajprenal.1986.250.6.F1013
   VELAZQUEZ H, 1992, American Journal of Physiology, V262, pF1076
   Velazquez H, 1996, AM J PHYSIOL-RENAL, V270, pF211, DOI 10.1152/ajprenal.1996.270.1.F211
   VELAZQUEZ H, 1984, AM J PHYSIOL, V247, pF904, DOI 10.1152/ajprenal.1984.247.6.F904
   Ventura HO, 2001, J CARD FAIL, V7, P277, DOI 10.1054/jcaf.2001.26564
   Veríssimo F, 2001, ONCOGENE, V20, P5562, DOI 10.1038/sj.onc.1204726
   Verlander JW, 1998, J CLIN INVEST, V101, P1661, DOI 10.1172/JCI601
   Vidal-Petiot E, 2013, P NATL ACAD SCI USA, V110, P14366, DOI 10.1073/pnas.1304230110
   Vidal-Petiot E, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0037751
   Vitari AC, 2006, BIOCHEM J, V397, P223, DOI 10.1042/BJ20060220
   Vitari AC, 2005, BIOCHEM J, V391, P17, DOI 10.1042/BJ20051180
   Vitari AC, 2004, BIOCHEM J, V378, P257, DOI 10.1042/BJ20031692
   Vitzthum H, 2014, J PHYSIOL-LONDON, V592, P1139, DOI 10.1113/jphysiol.2013.266924
   VONDREELE MM, 1988, AM J PHYSIOL, V255, pF953, DOI 10.1152/ajprenal.1988.255.5.F953
   Vormfelde SV, 2007, CLIN PHARMACOL THER, V82, P300, DOI 10.1038/sj.clpt.6100131
   Wade JB, 2015, AM J PHYSIOL-RENAL, V308, pF923, DOI 10.1152/ajprenal.00388.2014
   Wade JB, 2011, AM J PHYSIOL-RENAL, V300, pF1385, DOI 10.1152/ajprenal.00592.2010
   Wagner CA, 2000, CELL PHYSIOL BIOCHEM, V10, P1, DOI 10.1159/000016341
   Wakabayashi M, 2013, CELL REP, V3, P858, DOI 10.1016/j.celrep.2013.02.024
   Wall SM, 2020, PHYSIOL REV, V100, P1119, DOI 10.1152/physrev.00011.2019
   Wang F, 2017, CLIN EXP NEPHROL, V21, P293, DOI 10.1007/s10157-016-1284-6
   Wang LY, 2017, PROTEIN SCI, V26, P163, DOI 10.1002/pro.3063
   Wang MX, 2018, KIDNEY INT, V93, P893, DOI 10.1016/j.kint.2017.10.023
   Wang WH, 2016, CURR OPIN NEPHROL HY, V25, P429, DOI 10.1097/MNH.0000000000000248
   Wang Y, 2009, P NATL ACAD SCI USA, V106, P226, DOI 10.1073/pnas.0808358106
   Weinstein AM, 2005, AM J PHYSIOL-RENAL, V289, pF699, DOI 10.1152/ajprenal.00043.2005
   Welling PA, 2018, J AM SOC NEPHROL, V29, P1347, DOI 10.1681/ASN.2018030318
   WHEELER HO, 1963, AM J PHYSIOL, V205, P427
   WILKINS RW, 1958, ANN NY ACAD SCI, V71, P465, DOI 10.1111/j.1749-6632.1958.tb54621.x
   WILKINSON DJ, 1993, TOXICOL APPL PHARM, V123, P170, DOI 10.1006/taap.1993.1234
   Wilson FH, 2001, SCIENCE, V293, P1107, DOI 10.1126/science.1062844
   Wilson FH, 2003, P NATL ACAD SCI USA, V100, P680, DOI 10.1073/pnas.242735399
   Wingert RA, 2007, PLOS GENET, V3, P1922, DOI 10.1371/journal.pgen.0030189
   Wu AH, 2019, J HUM HYPERTENS, V33, P508, DOI 10.1038/s41371-019-0170-6
   Xi B, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0059584
   Xie Y, 2020, SCI ADV, V6, DOI 10.1126/sciadv.abc5883
   Xu BE, 2005, P NATL ACAD SCI USA, V102, P10315, DOI 10.1073/pnas.0504422102
   Xu BE, 2000, J BIOL CHEM, V275, P16795, DOI 10.1074/jbc.275.22.16795
   Yang CL, 2007, J CLIN INVEST, V117, P3403, DOI 10.1172/JCI32033
   Yang CL, 2005, J CLIN INVEST, V115, P1379, DOI 10.1172/JCI200522452
   Yang CL, 2003, J CLIN INVEST, V111, P1039, DOI 10.1172/JCI200317443
   Yang HL, 2016, SCI REP-UK, V6, DOI 10.1038/srep25290
   Yang SS, 2007, CELL METAB, V5, P331, DOI 10.1016/j.cmet.2007.03.009
   Yang SS, 2010, HUM MUTAT, V31, P1304, DOI 10.1002/humu.21364
   Yang SS, 2010, J AM SOC NEPHROL, V21, P1868, DOI 10.1681/ASN.2009121295
   Yang TX, 1996, AM J PHYSIOL-RENAL, V271, pF931, DOI 10.1152/ajprenal.1996.271.4.F931
   Yang XY, 2020, NAT COMMUN, V11, DOI 10.1038/s41467-020-14790-3
   Yang YS, 2018, AM J PHYSIOL-RENAL, V314, pF999, DOI 10.1152/ajprenal.00177.2017
   Yoshizaki Y, 2015, BIOCHEM BIOPH RES CO, V467, P229, DOI 10.1016/j.bbrc.2015.09.184
   Yu ASL, 2015, J AM SOC NEPHROL, V26, P11, DOI 10.1681/ASN.2014030284
   Zagórska A, 2007, J CELL BIOL, V176, P89, DOI 10.1083/jcb.200605093
   ZEUTHEN T, 1994, J PHYSIOL-LONDON, V478, P203, DOI 10.1113/jphysiol.1994.sp020243
   Zhang C, 2013, CLIN GENET, V83, P545, DOI 10.1111/cge.12008
   Zhang CB, 2017, AM J PHYSIOL-RENAL, V312, pF682, DOI 10.1152/ajprenal.00420.2016
   Zhang CB, 2014, P NATL ACAD SCI USA, V111, P11864, DOI 10.1073/pnas.1411705111
   Zhang SS, 2021, COMMUN BIOL, V4, DOI 10.1038/s42003-021-01750-w
   Zhao XY, 2021, EXP THER MED, V21, DOI 10.3892/etm.2020.9565
   Zhao YX, 2022, P NATL ACAD SCI USA, V119, DOI 10.1073/pnas.2109083119
   ZIYADEH FN, 1987, BIOCHIM BIOPHYS ACTA, V897, P52, DOI 10.1016/0005-2736(87)90314-2
   Abdelhadi O, 2016, RARE DIS, V4, DOI 10.1080/21675511.2016.1195043
   Adalat S, 2019, KIDNEY INT REP, V4, P1304, DOI 10.1016/j.ekir.2019.05.019
   Andrini O, 2015, AM J PHYSIOL-RENAL, V308, pF1324, DOI 10.1152/ajprenal.00004.2015
   Arystarkhova E, 2005, J BIOENERG BIOMEMBR, V37, P381, DOI 10.1007/s10863-005-9475-y
   Arystarkhova E, 1999, J BIOL CHEM, V274, P33183, DOI 10.1074/jbc.274.47.33183
   Bignon Y, 2020, KIDNEY INT, V97, P304, DOI 10.1016/j.kint.2019.09.028
   Biondo ED, 2021, AM J PHYSIOL-CELL PH, V321, pC394, DOI 10.1152/ajpcell.00059.2021
   Blostein R, 2003, ANN NY ACAD SCI, V986, P420, DOI 10.1111/j.1749-6632.2003.tb07224.x
   Bockenhauer D, 2016, PEDIATR NEPHROL, V31, P707, DOI 10.1007/s00467-015-3142-2
   Bokhari SRA, 2023, Bartter Syndrome
   Cairo ER, 2009, J MEMBRANE BIOL, V231, P117, DOI 10.1007/s00232-009-9210-4
   Celmina M, 2019, CLIN GENET, V95, P63, DOI 10.1111/cge.13374
   Clausen MV, 2017, FRONT PHYSIOL, V8, DOI 10.3389/fphys.2017.00371
   Clissold RL, 2015, NAT REV NEPHROL, V11, P102, DOI 10.1038/nrneph.2014.232
   Cunha TD, 2018, INT J NEPHROL RENOV, V11, P291, DOI 10.2147/IJNRD.S155397
   de Baaij JHF, 2015, NEPHROL DIAL TRANSPL, V30, P952, DOI 10.1093/ndt/gfv014
   Farman N, 2003, ANN NY ACAD SCI, V986, P428, DOI 10.1111/j.1749-6632.2003.tb07225.x
   Ferrè S, 2011, BIOCHEM BIOPH RES CO, V404, P284, DOI 10.1016/j.bbrc.2010.11.108
   Fukuyama S, 2004, J CLIN ENDOCR METAB, V89, P5847, DOI 10.1210/jc.2004-0775
   Garty H, 2006, ANNU REV PHYSIOL, V68, P431, DOI 10.1146/annurev.physiol.68.040104.131852
   GEVEN WB, 1987, KIDNEY INT, V31, P1140, DOI 10.1038/ki.1987.120
   de la F CLG, 2019, REV CHIL PEDIATR-CHI, V90, P437, DOI 10.32641/rchped.v90i4.932
   Hansell P, 2013, CLIN EXP PHARMACOL P, V40, P123, DOI 10.1111/1440-1681.12034
   Heliot C, 2013, DEVELOPMENT, V140, P873, DOI 10.1242/dev.086538
   Jeck N, 2000, PEDIATR RES, V48, P754, DOI 10.1203/00006450-200012000-00009
   Kikuchi R, 2007, MOL PHARMACOL, V72, P1619, DOI 10.1124/mol.107.039701
   Kompatscher A, 2018, AM J PHYSIOL-RENAL, V315, pF27, DOI 10.1152/ajprenal.00601.2017
   LAPOINTE N, 1981, PROSTAG LEUKOTR ESS, V6, P647, DOI 10.1016/0161-4630(81)90127-0
   Lin DH, 2022, CURR OPIN NEPHROL HY, V31, P479, DOI 10.1097/MNH.0000000000000817
   Lo JCY, 2022, FRONT PHYSIOL, V13, DOI 10.3389/fphys.2022.852674
   Lokmane L, 2010, DEVELOPMENT, V137, P347, DOI 10.1242/dev.042226
   Massa F, 2013, DEVELOPMENT, V140, P886, DOI 10.1242/dev.086546
   Matsunoshita N, 2016, GENET MED, V18, P180, DOI 10.1038/gim.2015.56
   Meij IC, 2000, NAT GENET, V26, P265, DOI 10.1038/81543
   Minor NT, 1998, P NATL ACAD SCI USA, V95, P6521, DOI 10.1073/pnas.95.11.6521
   Mir A, 2019, BRAIN DEV-JPN, V41, P706, DOI 10.1016/j.braindev.2019.03.009
   Naylor RW, 2014, PEDIATR NEPHROL, V29, P659, DOI 10.1007/s00467-013-2662-x
   Nitte CM, 2023, FRONT PEDIATR, V11, DOI 10.3389/fped.2023.1149875
   Nozu K, 2020, PEDIATR INT, V62, P428, DOI 10.1111/ped.14089
   Pihakaski-Maunsbach K, 2006, AM J PHYSIOL-RENAL, V291, pF1033, DOI 10.1152/ajprenal.00086.2006
   Riazuddin S, 2009, AM J HUM GENET, V85, P273, DOI 10.1016/j.ajhg.2009.07.003
   Sakalli H, 2012, AM J CASE REP, V13, P230, DOI 10.12659/AJCR.883446
   Schlingmann KP, 2021, J AM SOC NEPHROL, V32, P1498, DOI 10.1681/ASN.2020111587
   Schlingmann KP, 2022, CURR OPIN NEPHROL HY, V31, P508, DOI 10.1097/MNH.0000000000000818
   Schlingmann KP, 2018, AM J HUM GENET, V103, P808, DOI 10.1016/j.ajhg.2018.10.004
   Scholl UI, 2012, PEDIATR NEPHROL, V27, P2081, DOI 10.1007/s00467-012-2219-4
   Sha Q, 2008, AM J PHYSIOL-RENAL, V295, pF91, DOI 10.1152/ajprenal.00519.2007
   Therien AG, 2001, J BIOENERG BIOMEMBR, V33, P407, DOI 10.1023/A:1010619623841
   Tholen LE, 2022, PFLUG ARCH EUR J PHY, V474, P901, DOI 10.1007/s00424-022-02697-5
   Viering D, 2022, J AM SOC NEPHROL, V33, P305, DOI 10.1681/ASN.2021050596
   Wang WH, 2022, AM J PHYSIOL-CELL PH, V323, pC277, DOI 10.1152/ajpcell.00096.2022
   Webb BD, 2021, EUR J HUM GENET, V29, P1566, DOI 10.1038/s41431-021-00883-0
   Wilson FH, 2004, SCIENCE, V306, P1190, DOI 10.1126/science.1102521
   Zhang JH, 2021, GENES DIS, V8, P272, DOI 10.1016/j.gendis.2020.03.006
NR 554
TC 1
Z9 1
U1 3
U2 4
PU AMER PHYSIOLOGICAL SOC
PI Rockville
PA 6120 Executive Blvd, Suite 600, Rockville, MD, UNITED STATES
SN 0031-9333
EI 1522-1210
J9 PHYSIOL REV
JI Physiol. Rev.
PD JUL 8
PY 2024
VL 104
IS 3
DI 10.1152/physrev.00027.2023
PG 59
WC Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Physiology
GA A0H0O
UT WOS:001279424700001
PM 38329422
OA Green Published
DA 2025-04-10
ER

PT J
AU Acharya, D
   Nera, B
   Milstone, ZJ
   Bourke, L
   Yoon, Y
   Rivera-Pérez, JA
   Trivedi, CM
   Fazzio, TG
AF Acharya, Diwash
   Nera, Bernadette
   Milstone, Zachary J.
   Bourke, Lauren
   Yoon, Yeonsoo
   Rivera-Perez, Jaime A.
   Trivedi, Chinmay M.
   Fazzio, Thomas G.
TI TIP55, a splice isoform of the KAT5 acetyltransferase, is essential for
   developmental gene regulation and organogenesis
SO SCIENTIFIC REPORTS
LA English
DT Article
ID HISTONE ACETYLTRANSFERASE; TIP60; ACETYLATION; IDENTIFICATION;
   ACTIVATION; MECHANISMS; BINDING; GROWTH; FORM
AB Regulation of chromatin structure is critical for cell type-specific gene expression. Many chromatin regulatory complexes exist in several different forms, due to alternative splicing and differential incorporation of accessory subunits. However, in vivo studies often utilize mutations that eliminate multiple forms of complexes, preventing assessment of the specific roles of each. Here we examined the developmental roles of the TIP55 isoform of the KAT5 histone acetyltransferase. In contrast to the pre-implantation lethal phenotype of mice lacking all four Kat5 transcripts, mice specifically deficient for Tip55 die around embryonic day 11.5 (E11.5). Prior to developmental arrest, defects in heart and neural tube were evident in Tip55 mutant embryos. Specification of cardiac and neural cell fates appeared normal in Tip55 mutants. However, cell division and survival were impaired in heart and neural tube, respectively, revealing a role for TIP55 in cellular proliferation. Consistent with these findings, transcriptome profiling revealed perturbations in genes that function in multiple cell types and developmental pathways. These findings show that Tip55 is dispensable for the pre- and early post-implantation roles of KatS, but is essential during organogenesis. Our results raise the possibility that isoform-specific functions of other chromatin regulatory proteins may play important roles in development.
C1 [Acharya, Diwash; Nera, Bernadette; Trivedi, Chinmay M.; Fazzio, Thomas G.] Univ Massachusetts, Sch Med, Dept Mol Cell & Canc Biol, Worcester, MA 01605 USA.
   [Milstone, Zachary J.; Bourke, Lauren; Trivedi, Chinmay M.] Univ Massachusetts, Sch Med, Div Cardiovasc Med, Worcester, MA 01605 USA.
   [Milstone, Zachary J.; Bourke, Lauren; Trivedi, Chinmay M.] Univ Massachusetts, Sch Med, Dept Med, Worcester, MA 01605 USA.
   [Yoon, Yeonsoo; Rivera-Perez, Jaime A.] Univ Massachusetts, Sch Med, Dept Pediat, Div Genes & Dev, Worcester, MA 01605 USA.
C3 University of Massachusetts System; University of Massachusetts
   Worcester; University of Massachusetts System; University of
   Massachusetts Worcester; University of Massachusetts System; University
   of Massachusetts Worcester; University of Massachusetts System;
   University of Massachusetts Worcester
RP Fazzio, TG (corresponding author), Univ Massachusetts, Sch Med, Dept Mol Cell & Canc Biol, Worcester, MA 01605 USA.
EM thomas.fazzio@umassmed.edu
RI Trivedi, Chinmay/ABA-4097-2021
OI Milstone, Zachary/0000-0003-0344-5550; Rivera-Perez,
   Jaime/0000-0001-5776-6291; Bourke, Lauren/0000-0003-4391-0074; Trivedi,
   Chinmay/0000-0002-3544-0474
FU National Institutes of Health [R01HD072122, R01HL118100, R01HD083311];
   American Cancer Society [RSG-14-220-01]; Translationtional Cancer
   Biology Postdoctoral training grant from the NIH [T32CA130807]
FX We thank K. McCannell, T. Wu, and J. Benanti for critical comments on
   the manuscript. This work was supported by the National Institutes of
   Health [R01HD072122 to T.G.F.; R01HL118100 to C.M.T.; and R01HD083311 to
   J. A. R.-P.] and the American Cancer Society [RSG-14-220-01] to T.G.F.
   B.N. was supported by a Translationtional Cancer Biology Postdoctoral
   training grant from the NIH (T32CA130807). T.G.F. is a Leukemia and
   Lymphoma Society Scholar.
CR Acharya D, 2017, CELL REP, V19, P671, DOI 10.1016/j.celrep.2017.04.001
   Barak O, 2004, J BIOL CHEM, V279, P45130, DOI 10.1074/jbc.M406212200
   Börner K, 2016, DEVELOPMENT, V143, P3154, DOI 10.1242/dev.139634
   Chen PB, 2013, ELIFE, V2, DOI 10.7554/eLife.01557
   Fazzio TG, 2008, CELL, V134, P162, DOI 10.1016/j.cell.2008.05.031
   Gonzalez-Sandoval A, 2016, TRENDS GENET, V32, P485, DOI 10.1016/j.tig.2016.05.004
   Guertin MJ, 2013, CURR OPIN GENET DEV, V23, P116, DOI 10.1016/j.gde.2012.11.008
   Hu YF, 2009, DEV DYNAM, V238, P2912, DOI 10.1002/dvdy.22110
   Huang W, 2011, BMC BIOINFORMATICS, V12, DOI 10.1186/1471-2105-12-1
   Ikura T, 2000, CELL, V102, P463, DOI 10.1016/S0092-8674(00)00051-9
   Kim MS, 2006, J BIOL CHEM, V281, P15082, DOI 10.1074/jbc.M513593200
   Kusch T, 2004, SCIENCE, V306, P2084, DOI 10.1126/science.1103455
   Legube G, 2004, J BIOL CHEM, V279, P44825, DOI 10.1074/jbc.M407478200
   Legube G, 2003, GENE, V310, P161, DOI 10.1016/S0378-1119(03)00547-X
   Leng N, 2013, BIOINFORMATICS, V29, P1035, DOI 10.1093/bioinformatics/btt087
   Milstone ZJ, 2017, DEV DYNAM, V246, P1015, DOI [10.1002/DVDY.24563, 10.1002/dvdy.24563]
   Mirabella AC, 2016, CHROMOSOMA, V125, P75, DOI 10.1007/s00412-015-0530-0
   Ran QT, 2000, GENE, V258, P141, DOI 10.1016/S0378-1119(00)00410-8
   Rivera-Pérez JA, 2005, DEV BIOL, V288, P363, DOI 10.1016/j.ydbio.2005.09.012
   Squatrito M, 2006, TRENDS CELL BIOL, V16, P433, DOI 10.1016/j.tcb.2006.07.007
   Sun YL, 2005, P NATL ACAD SCI USA, V102, P13182, DOI 10.1073/pnas.0504211102
   Sykes SM, 2006, MOL CELL, V24, P841, DOI 10.1016/j.molcel.2006.11.026
   Tang Y, 2006, MOL CELL, V24, P827, DOI 10.1016/j.molcel.2006.11.021
   TODARO GJ, 1963, J CELL BIOL, V17, P299, DOI 10.1083/jcb.17.2.299
   Tripathi S, 2015, CELL HOST MICROBE, V18, P723, DOI 10.1016/j.chom.2015.11.002
   Villar D, 2014, NAT REV GENET, V15, P221, DOI 10.1038/nrg3481
   Yamamoto T, 1997, J BIOL CHEM, V272, P30595, DOI 10.1074/jbc.272.49.30595
   Zibetti C, 2010, J NEUROSCI, V30, P2521, DOI 10.1523/JNEUROSCI.5500-09.2010
NR 28
TC 2
Z9 4
U1 0
U2 6
PU NATURE PORTFOLIO
PI BERLIN
PA HEIDELBERGER PLATZ 3, BERLIN, 14197, GERMANY
SN 2045-2322
J9 SCI REP-UK
JI Sci Rep
PD OCT 8
PY 2018
VL 8
AR 14908
DI 10.1038/s41598-018-33213-4
PG 9
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA GW0RP
UT WOS:000446577100010
PM 30297694
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Uddman, R
   Möller, S
   Nilsson, T
   Nyström, S
   Ekstrand, J
   Edvinsson, L
AF Uddman, R
   Möller, S
   Nilsson, T
   Nyström, S
   Ekstrand, J
   Edvinsson, L
TI Neuropeptide YY1 and neuropeptide YY2 receptors in
   human cardiovascular tissues
SO PEPTIDES
LA English
DT Article
DE neuropeptide Y receptors; autonomic nervous system; blood vessels;
   RT-PCR
ID CEREBRAL BLOOD-VESSELS; PEPTIDE-YY; FUNCTIONAL EXPRESSION;
   PANCREATIC-POLYPEPTIDE; Y2 RECEPTOR; 2 ISOFORMS; CLONING; NORADRENALINE;
   LOCALIZATION; ACTIVATION
AB mRNA encoding the human NPY Y-1 and NPY Y-2 receptors were detected in cerebral, meningeal, and coronary arteries using reverse transcriptase-polymerase chain reaction (RT-PCR). In addition, the trigeminal and superior cervical ganglia were positive for both receptors. In some arteries and in SK-N-MC cells only mRNA encoding the NPY Y-1 was detected. Besides the expected NPY Y-1 PCR products, an additional 97 bp longer amplicon originating from an alternative splicing event was found in most tissues studied. Antibodies directed against the NPY Y-1 receptor revealed immunostaining mainly in the smooth muscle layer of blood vessels whereas antibodies against the NPY Y-2 receptor showed immunostaining in nerve cell bodies. (C) 2002 Elsevier Science Inc. All rights reserved.
C1 Univ Hosp, Dept Otorhinolaryngol, S-20502 Malmo, Sweden.
   Lund Univ, Dept Internal Med, Div Expt Vasc Res, Lund, Sweden.
   AstraZeneca R&D, Dept Biol Mol, Umea, Sweden.
C3 Lund University; Skane University Hospital; Lund University; AstraZeneca
RP Uddman, R (corresponding author), Univ Hosp, Dept Otorhinolaryngol, S-20502 Malmo, Sweden.
OI Edvinsson, Lars/0000-0002-1805-1346
CR Abounader R, 1999, J CEREBR BLOOD F MET, V19, P155, DOI 10.1097/00004647-199902000-00007
   BALL HJ, 1995, J BIOL CHEM, V270, P27272, DOI 10.1074/jbc.270.45.27272
   Bao L, 1997, P NATL ACAD SCI USA, V94, P12661, DOI 10.1073/pnas.94.23.12661
   BARD JA, 1995, J BIOL CHEM, V270, P26762, DOI 10.1074/jbc.270.45.26762
   Bergdahl A, 1996, EUR J PHARMACOL, V316, P59, DOI 10.1016/S0014-2999(96)00636-X
   DAHLOF C, 1985, EUR J PHARMACOL, V109, P289, DOI 10.1016/0014-2999(85)90433-9
   EDVINSSON L, 1987, TRENDS PHARMACOL SCI, V8, P231, DOI 10.1016/0165-6147(87)90069-1
   FRIED G, 1985, J NEUROSCI, V5, P450
   GARCIAVILLALON AL, 1991, J PHARMACOL EXP THER, V258, P304
   GERALD C, 1995, J BIOL CHEM, V270, P26758, DOI 10.1074/jbc.270.45.26758
   Gullestad L, 1998, J AUTONOM NERV SYST, V70, P84, DOI 10.1016/S0165-1838(98)00032-0
   HERZOG H, 1992, P NATL ACAD SCI USA, V89, P5794, DOI 10.1073/pnas.89.13.5794
   LARHAMMAR D, 1992, J BIOL CHEM, V267, P10935
   LUNDBERG JM, 1984, ACTA PHYSIOL SCAND, V120, P477, DOI 10.1111/j.1748-1716.1984.tb07410.x
   LUNDBERG JM, 1986, ACTA PHYSIOL SCAND, V126, P231, DOI 10.1111/j.1748-1716.1986.tb07810.x
   Marklund U, 2002, MOL CELL ENDOCRINOL, V188, P85, DOI 10.1016/S0303-7207(01)00738-9
   Michel MC, 1998, PHARMACOL REV, V50, P143
   MODIN A, 1991, EUR J PHARMACOL, V203, P165, DOI 10.1016/0014-2999(91)90711-X
   MONSMA FJ, 1989, NATURE, V342, P926, DOI 10.1038/342926a0
   NAKAMURA M, 1995, J BIOL CHEM, V270, P30102, DOI 10.1074/jbc.270.50.30102
   Naveilhan P, 1999, NAT MED, V5, P1188, DOI 10.1038/13514
   Naveilhan P, 2001, NATURE, V409, P513, DOI 10.1038/35054063
   Nilsson Torun, 1996, Blood Pressure, V5, P164, DOI 10.3109/08037059609062125
   PERNOW J, 1987, LIFE SCI, V40, P47, DOI 10.1016/0024-3205(87)90251-7
   ROSE PM, 1995, J BIOL CHEM, V270, P22661, DOI 10.1074/jbc.270.39.22661
   TATEMOTO K, 1982, NATURE, V296, P659, DOI 10.1038/296659a0
   VANETTI M, 1993, FEBS LETT, V331, P260, DOI 10.1016/0014-5793(93)80349-Y
   WAHLESTEDT C, 1993, ANN REV PHARM TOXICO, V32, P309
   WEINBERG DH, 1996, J BIOL CHEM, V271, P16485
   You JP, 2001, J CEREBR BLOOD F MET, V21, P77, DOI 10.1097/00004647-200101000-00010
   Zhang X, 1997, P NATL ACAD SCI USA, V94, P729, DOI 10.1073/pnas.94.2.729
NR 31
TC 26
Z9 32
U1 1
U2 3
PU ELSEVIER SCIENCE INC
PI NEW YORK
PA 360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA
SN 0196-9781
J9 PEPTIDES
JI Peptides
PD MAY
PY 2002
VL 23
IS 5
BP 927
EP 934
AR PII S0196-9781(02)00003-7
DI 10.1016/S0196-9781(02)00003-7
PG 8
WC Biochemistry & Molecular Biology; Endocrinology & Metabolism;
   Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Endocrinology & Metabolism;
   Pharmacology & Pharmacy
GA 583ZV
UT WOS:000177442800014
PM 12084524
DA 2025-04-10
ER

PT J
AU Wright, SM
   Jensen, SL
   Cockriel, KL
   Davis, B
   Tschanz, JT
   Munger, RG
   Corcoran, CD
   Kauwe, JSK
AF Wright, Sage M.
   Jensen, Samantha L.
   Cockriel, Kristen L.
   Davis, Brian
   Tschanz, JoAnn T.
   Munger, Ronald G.
   Corcoran, Christopher D.
   Kauwe, John S. K.
TI Association study of rs3846662 with Alzheimer's disease in a
   population-based cohort: the Cache County Study
SO NEUROBIOLOGY OF AGING
LA English
DT Article
DE HMGCR; Alzheimer's disease; APOE; Cholesterol synthesis; Genetics;
   Association
ID LIPOPROTEIN CHOLESTEROL RESPONSE; COENZYME-A REDUCTASE; LIPID-LEVELS;
   HMGCR; RISK; ONSET; CRITERIA; LOCI; GENE; AGE
AB 3-Hydroxy-3-methylglutaryl coenzyme A reductase is associated with monitoring cholesterol levels. The presence of the single-nucleotide polymorphism rs3846662 introduces alternative splicing at exon 13; the exclusion of this exon leads to a reduction in total cholesterol levels. Lower cholesterol levels are linked to a reduction in Alzheimer's disease (AD) risk. The major allele of rs3846662, which encourages the splicing of exon 13, has recently been shown to act as a preventative allele for AD, especially in women. The purpose of our research was to replicate and confirm this finding. Using logistic regressions and survival curves, we found a significant association between AD and rs3846662, with a stronger association in individuals who carry the APOE e4 allele, supporting previously published work. The effect of rs3846662 on women is insignificant in our cohort. We confirmed that rs3846662 is associated with reduced risk for AD without gender differences; however, we failed to detect association between rs3846662 and delayed mild cognitive impairment conversion to AD for either of the APOE e4 allelic groups. (C) 2019 Elsevier Inc. All rights reserved.
C1 [Wright, Sage M.; Jensen, Samantha L.; Cockriel, Kristen L.; Davis, Brian; Kauwe, John S. K.] Brigham Young Univ, Dept Biol, 4101A LSB, Provo, UT 84602 USA.
   [Tschanz, JoAnn T.] Utah State Univ, Dept Psychol, Logan, UT 84322 USA.
   [Munger, Ronald G.] Utah State Univ, Dept Nutr Dietet & Food Sci, Logan, UT 84322 USA.
   [Corcoran, Christopher D.] Utah State Univ, Dept Math & Stat, Logan, UT 84322 USA.
C3 Brigham Young University; Utah System of Higher Education; Utah State
   University; Utah System of Higher Education; Utah State University; Utah
   System of Higher Education; Utah State University
RP Kauwe, JSK (corresponding author), Brigham Young Univ, Dept Biol, 4101A LSB, Provo, UT 84602 USA.
EM kauwe@byu.edu
RI Kauwe, John/AAC-6646-2021
OI Jensen, Samantha L./0000-0002-4090-304X; Wright,
   Sage/0000-0002-0735-5504
FU National Institutes of Health, United States [R01AG11380, R01AG21136,
   R01AG31272, R01AG042611, RF1AG054052]
FX This work was supported by the National Institutes of Health, United
   States (R01AG11380, R01AG21136, R01AG31272, R01AG042611, RF1AG054052).
   The funders had no role in study design, data collection and analysis,
   decision to publish, or preparation of the article.
CR Adlard PA, 2004, NEUROBIOL AGING, V25, P725, DOI 10.1016/j.neurobiolaging.2003.12.016
   Armstrong R A, 2011, Int J Alzheimers Dis, V2011, P630865, DOI 10.4061/2011/630865
   Aulchenko YS, 2009, NAT GENET, V41, P47, DOI 10.1038/ng.269
   Bertram L, 2007, NAT GENET, V39, P17, DOI 10.1038/ng1934
   BLAND JM, 1994, BRIT MED J, V309, P248, DOI 10.1136/bmj.309.6949.248
   Breitner JCS, 1999, NEUROLOGY, V53, P321, DOI 10.1212/WNL.53.2.321
   Burkhardt R, 2008, ARTERIOSCL THROM VAS, V28, P2078, DOI 10.1161/ATVBAHA.108.172288
   Cano-Corres R, 2018, J CLIN LAB ANAL, V32, DOI 10.1002/jcla.22566
   Chang XL, 2016, ONCOTARGET, V7, P22746, DOI 10.18632/oncotarget.8176
   CORDER EH, 1993, SCIENCE, V261, P921, DOI 10.1126/science.8346443
   HARDY JA, 1992, SCIENCE, V256, P184, DOI 10.1126/science.1566067
   Istvan ES, 2000, EMBO J, V19, P819, DOI 10.1093/emboj/19.5.819
   Kathiresan S, 2008, NEW ENGL J MED, V358, P1240, DOI 10.1056/NEJMoa0706728
   KIMMEL HD, 1957, PSYCHOL BULL, V54, P351, DOI 10.1037/h0046737
   Krauss RM, 2008, CIRCULATION, V117, P1537, DOI 10.1161/CIRCULATIONAHA.107.708388
   Lambert JC, 2013, NAT GENET, V45, P1452, DOI 10.1038/ng.2802
   Leduc V, 2015, MOL PSYCHIATR, V20, P867, DOI 10.1038/mp.2014.81
   Leduc V, 2016, PHARMACOGENET GENOM, V26, P1, DOI 10.1097/FPC.0000000000000178
   Medina MW, 2010, DISCOV MED, V9, P495
   Medina MW, 2008, CIRCULATION, V118, P355, DOI 10.1161/CIRCULATIONAHA.108.773267
   Medina MW, 2009, TRENDS CARDIOVAS MED, V19, P173, DOI 10.1016/j.tcm.2009.10.003
   Newell KL, 1999, J NEUROPATH EXP NEUR, V58, P1147, DOI 10.1097/00005072-199911000-00004
   Ridge PG, 2013, BIOMED RES INT, V2013, DOI 10.1155/2013/254954
   Rodríguez-Rodríguez E, 2009, BRAIN RES, V1280, P166, DOI 10.1016/j.brainres.2009.05.019
   Ruxton GD, 2010, METHODS ECOL EVOL, V1, P114, DOI 10.1111/j.2041-210X.2010.00014.x
   Sharp AR, 2014, BMC BIOINFORMATICS, V15, DOI 10.1186/1471-2105-15-S7-S8
   Simmons CR, 2011, MOL NEURODEGENER, V6, DOI 10.1186/1750-1326-6-62
   Simons M, 1998, P NATL ACAD SCI USA, V95, P6460, DOI 10.1073/pnas.95.11.6460
   Skol AD, 2006, NAT GENET, V38, P209, DOI 10.1038/ng1706
   Swerdlow RH, 2004, MED HYPOTHESES, V63, P8, DOI 10.1016/j.mehy.2003.12.045
   Team RC, 2016, R LANG ENV STAT COMP
   Tschanz JT, 2002, NEUROPSY NEUROPSY BE, V15, P28
NR 32
TC 6
Z9 6
U1 0
U2 1
PU ELSEVIER SCIENCE INC
PI NEW YORK
PA STE 800, 230 PARK AVE, NEW YORK, NY 10169 USA
SN 0197-4580
EI 1558-1497
J9 NEUROBIOL AGING
JI Neurobiol. Aging
PD DEC
PY 2019
VL 84
DI 10.1016/j.neurobiolaging.2019.03.004
PG 6
WC Geriatrics & Gerontology; Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Geriatrics & Gerontology; Neurosciences & Neurology
GA JU3LE
UT WOS:000501576800047
PM 30975575
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Wang, J
   Thurston, H
   Essandoh, E
   Otoo, M
   Han, MD
   Rajan, A
   Dube, S
   Zajdel, RW
   Sanger, JM
   Linask, KK
   Dube, DK
   Sanger, JW
AF Wang, Jushuo
   Thurston, Harold
   Essandoh, Eugene
   Otoo, Mary
   Han, Mingda
   Rajan, Arun
   Dube, Syamalima
   Zajdel, Robert W.
   Sanger, Jean M.
   Linask, Kersti K.
   Dube, Dipak K.
   Sanger, Joseph W.
TI Tropomyosin expression and dynamics in developing avian embryonic
   muscles
SO CELL MOTILITY AND THE CYTOSKELETON
LA English
DT Article
DE tropomyosin isoforms; alternative splicing; myofibrillogenesis;
   fluorescence recovery after photobleaching; hearts
ID FETAL SKELETAL-MUSCLE; ALPHA-TROPOMYOSIN; CARDIAC TROPOMYOSIN;
   STRIATED-MUSCLE; HEART DEVELOPMENT; BETA-TROPOMYOSIN; GENE-EXPRESSION;
   CHICK-EMBRYO; ISOFORM; CELLS
AB The expression of striated muscle proteins occurs early in the developing embryo in the somites and forming heart. A major component of the assembling rnyofibrils is the actin-binding protein tropomyosin. In vertebrates, there are four genes for tropomyosin (TM), each of which can be alternatively spliced. TPM1 can generate at least 10 different isoforms including the striated muscle-specific TPM1 alpha and TPM1 kappa. We have undertaken a detailed study of the expression of various TM isoforms in 2-day-old (stage HH 10-12; 33 h) heart and somites, the progenitor of future skeletal muscles. Both TPM1 alpha and TPM1 kappa are expressed transiently in embryonic heart while TPM1 alpha is expressed in somites. Both RT-PCR and in situ hybridization data suggest that TPM1 kappa is expressed in embryonic heart whereas TPM1 alpha is expressed in embryonic heart, and also in the branchial arch region of somites, and in the somites. Photobleaching studies of Yellow Fluorescent Protein-TPM1 alpha and -TPM1 kappa expressed in cultured avian cardiornyocytes revealed that the dynamics of the two probes was the same in both premyofibrils and in mature myofibrils. This was in sharp contrast to skeletal muscle cells in which the fluorescent proteins were more dynamic in premyofibrils. We speculate that the differences in the two muscles is due to the appearance of nebulin in the skeletal myocytes premyofibrils transform into mature myofibrils. Cell Motil.
C1 [Wang, Jushuo; Thurston, Harold; Zajdel, Robert W.; Sanger, Jean M.; Dube, Dipak K.; Sanger, Joseph W.] SUNY Upstate Med Univ, Dept Cell & Dev Biol, Syracuse, NY 13210 USA.
   [Thurston, Harold; Essandoh, Eugene; Otoo, Mary; Rajan, Arun; Dube, Syamalima; Dube, Dipak K.] SUNY Upstate Med Univ, Dept Med, Syracuse, NY 13210 USA.
   [Han, Mingda; Linask, Kersti K.] Univ S Florida, Childrens Res Inst, Dept Pediat, St Petersburg, FL 33701 USA.
C3 State University of New York (SUNY) System; State University of New York
   (SUNY) Upstate Medical Center; State University of New York (SUNY)
   System; State University of New York (SUNY) Upstate Medical Center;
   State University System of Florida; University of South Florida
RP Sanger, JW (corresponding author), SUNY Upstate Med Univ, Dept Cell & Dev Biol, 750 E Adams St, Syracuse, NY 13210 USA.
EM angerjo@upstate.edu
FU NHLBI NIH HHS [HL 48954, HL 80426, HL 67306] Funding Source: Medline;
   NIAMS NIH HHS [AR 46481] Funding Source: Medline
CR BAHLER M, 1985, DEV BIOL, V112, P345, DOI 10.1016/0012-1606(85)90405-1
   Bang ML, 2006, J CELL BIOL, V173, P905, DOI 10.1083/jcb.200603119
   BARTON PJR, 1985, J MUSCLE RES CELL M, V6, P461, DOI 10.1007/BF00712583
   Dabiri GA, 1999, METHOD ENZYMOL, V302, P171, DOI 10.1016/S0076-6879(99)02017-0
   Denz CR, 2004, BIOCHEM BIOPH RES CO, V320, P1291, DOI 10.1016/j.bbrc.2004.06.084
   FLEENOR DE, 1992, J MUSCLE RES CELL M, V13, P55, DOI 10.1007/BF01738428
   Fock U, 2002, J MUSCLE RES CELL M, V23, P205, DOI 10.1023/A:1020909902462
   FORRYSCHAUDIES S, 1990, CELL GROWTH DIFFER, V1, P473
   Gunning PW, 2005, TRENDS CELL BIOL, V15, P333, DOI 10.1016/j.tcb.2005.04.007
   HAMBURGER V, 1951, J MORPHOL, V88, P49, DOI 10.1002/jmor.1050880104
   HARDY S, 1995, GENE, V156, P265, DOI 10.1016/0378-1119(94)00929-M
   HIRUMA T, 1985, ANAT EMBRYOL, V172, P325, DOI 10.1007/BF00318980
   Jagatheesan G, 2003, J BIOL CHEM, V278, P23204, DOI 10.1074/jbc.M303073200
   LEESMILLER JP, 1991, BIOESSAYS, V13, P429, DOI 10.1002/bies.950130902
   LEMONNIER M, 1991, GENE, V107, P229, DOI 10.1016/0378-1119(91)90323-4
   Linask KK, 1997, DEV BIOL, V185, P148, DOI 10.1006/dbio.1997.8570
   Linask KK, 2001, DEV DYNAM, V221, P249, DOI 10.1002/dvdy.1131
   LINDQUESTER GJ, 1989, NUCLEIC ACIDS RES, V17, P2099, DOI 10.1093/nar/17.5.2099
   Luque EA, 1997, GENE, V185, P175, DOI 10.1016/S0378-1119(96)00606-3
   MANASEK FJ, 1968, J MORPHOL, V125, P329, DOI 10.1002/jmor.1051250306
   MCLACHLAN AD, 1975, J MOL BIOL, V98, P293, DOI 10.1016/S0022-2836(75)80119-7
   MCLACHLAN AD, 1975, J MOL BIOL, V98, P281, DOI 10.1016/S0022-2836(75)80118-5
   MINTY AJ, 1982, CELL, V30, P185, DOI 10.1016/0092-8674(82)90024-1
   MONCMAN CL, 1995, CELL MOTIL CYTOSKEL, V32, P205, DOI 10.1002/cm.970320305
   Muthuchamy M, 1998, J MOL CELL CARDIOL, V30, P1545, DOI 10.1006/jmcc.1998.0720
   MUTHUCHAMY M, 1993, MOL CELL BIOL, V13, P3311, DOI 10.1128/MCB.13.6.3311
   Muthuchamy M, 1997, TRENDS CARDIOVAS MED, V7, P124, DOI 10.1016/S1050-1738(97)00004-2
   Muthuchamy M, 1995, J BIOL CHEM, V270, P30593, DOI 10.1074/jbc.270.51.30593
   Narshi A, 2005, CARDIOVASC TOXICOL, V5, P1, DOI 10.1385/CT:5:1:001
   Ogut O, 2003, J BIOL CHEM, V278, P3089, DOI 10.1074/jbc.M205853200
   ORDAHL CP, 1986, DEV BIOL, V117, P488, DOI 10.1016/0012-1606(86)90315-5
   Perry SV, 2001, J MUSCLE RES CELL M, V22, P5, DOI 10.1023/A:1010303732441
   RHEE D, 1994, CELL MOTIL CYTOSKEL, V28, P1, DOI 10.1002/cm.970280102
   Romanoff A.L., 1960, THE AVIAN EMBRYO
   Sanger JW, 2005, J MUSCLE RES CELL M, V26, P343, DOI 10.1007/s10974-005-9016-7
   TOYOTA N, 1983, CELL, V33, P297, DOI 10.1016/0092-8674(83)90358-6
   Varga AE, 2005, ONCOGENE, V24, P5043, DOI 10.1038/sj.onc.1208688
   Vlahovich N, 2008, CELL MOTIL CYTOSKEL, V65, P73, DOI 10.1002/cm.20245
   Wang Da-Zhi, 1996, Frontiers in Bioscience (online), V1, pA1
   Wang J, 2005, CELL MOTIL CYTOSKEL, V61, P34, DOI 10.1002/cm.20063
   Wang J, 2007, CELL MOTIL CYTOSKEL, V64, P767, DOI 10.1002/cm.20221
   WIECZOREK DF, 1988, MOL CELL BIOL, V8, P679, DOI 10.1128/MCB.8.2.679
   Zajdel RW, 2003, J CELL BIOCHEM, V89, P427, DOI 10.1002/jcb.10504
NR 43
TC 23
Z9 24
U1 0
U2 5
PU WILEY-LISS
PI HOBOKEN
PA DIV JOHN WILEY & SONS INC, 111 RIVER ST, HOBOKEN, NJ 07030 USA
SN 0886-1544
J9 CELL MOTIL CYTOSKEL
JI Cell Motil. Cytoskeleton
PD MAY
PY 2008
VL 65
IS 5
BP 379
EP 392
DI 10.1002/cm.20267
PG 14
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA 300FC
UT WOS:000255808700003
PM 18302173
DA 2025-04-10
ER

PT J
AU Ziober, BL
   Chen, YQ
   Kramer, RH
AF Ziober, BL
   Chen, YQ
   Kramer, RH
TI The laminin-binding activity of the alpha 7 integrin receptor is defined
   by developmentally regulated splicing in the extracellular domain
SO MOLECULAR BIOLOGY OF THE CELL
LA English
DT Article
ID CYTOPLASMIC DOMAIN; SKELETAL-MUSCLE; LIGAND-BINDING; CELL-ADHESION;
   MESSENGER-RNA; SUBUNIT; EXPRESSION; BETA-1; ISOFORM; FORMS
AB The expression pattern of the laminin-binding alpha 7 beta 1 integrin is developmentally regulated in skeletal, cardiac, and smooth muscle. The X1/X2 alternative splicing in the extracellular domain of alpha 7 is found in the variable region between conserved alpha-chain homology repeat domains III and IV, a site implicated in ligand binding. To assess differences in X1/X2 isoform activity, we generated MCF-7 cell lines transfected with alpha 7-X1/X2 cDNAs. Transfectants expressing the alpha 7-X2 variant adhered rapidly to laminin 1, whereas those expressing alpha 7-X1 failed to attach. That alpha 7-X1 exists in an inactive state was established in assays using an activating beta 1 antibody that induced X1-dependent cell adhesion and spreading. Furthermore, the activation of alpha 7-X1 was cell type specific, and when expressed in HT1080 cells, the integrin was converted into a fully functional receptor capable of promoting adhesion. Thus, the expression of the alpha 7-X1/X2 integrin is a novel mechanism that regulates receptor affinity states in a cell-specific context and may modulate integrin-dependent events during muscle development and repair.
C1 UNIV CALIF SAN FRANCISCO, DEPT STOMATOL, SAN FRANCISCO, CA 94143 USA.
   UNIV CALIF SAN FRANCISCO, DEPT ANAT, SAN FRANCISCO, CA 94143 USA.
C3 University of California System; University of California San Francisco;
   University of California System; University of California San Francisco
FU NIDCR NIH HHS [DE-10306] Funding Source: Medline
CR ARROYO AG, 1992, J CELL BIOL, V117, P659, DOI 10.1083/jcb.117.3.659
   BAZZONI G, 1995, J BIOL CHEM, V270, P25570, DOI 10.1074/jbc.270.43.25570
   Belkin AM, 1996, J CELL BIOL, V132, P211, DOI 10.1083/jcb.132.1.211
   BROWN NH, 1989, CELL, V59, P185, DOI 10.1016/0092-8674(89)90880-5
   CHAN BMC, 1993, J CELL BIOL, V120, P537, DOI 10.1083/jcb.120.2.537
   COLLO G, 1993, J BIOL CHEM, V268, P19019
   COOPER HM, 1991, J CELL BIOL, V115, P843, DOI 10.1083/jcb.115.3.843
   Crawley S. C., 1996, Molecular Biology of the Cell, V7, p67A
   DELWEL GO, 1995, CELL ADHES COMMUN, V3, P143, DOI 10.3109/15419069509081283
   DELWEL GO, 1993, J BIOL CHEM, V268, P25865
   DIAMOND MS, 1994, CURR BIOL, V4, P506, DOI 10.1016/S0960-9822(00)00111-1
   DJAFFAR I, 1994, BIOCHEM J, V300, P69, DOI 10.1042/bj3000069
   FAULL RJ, 1993, J CELL BIOL, V121, P155, DOI 10.1083/jcb.121.1.155
   FORNARO M, 1995, J BIOL CHEM, V270, P24666, DOI 10.1074/jbc.270.42.24666
   GEHLSEN KR, 1989, J BIOL CHEM, V264, P19034
   GRINBLAT Y, 1994, DEVELOPMENT, V120, P91
   GU MJ, 1994, J CELL SCI, V107, P175
   Hemler M.E, 1994, INTEGRINS BIOL PROBL, P1
   HOGERVORST F, 1991, EUR J BIOCHEM, V199, P425, DOI 10.1111/j.1432-1033.1991.tb16140.x
   Hughes PE, 1997, CELL, V88, P521, DOI 10.1016/S0092-8674(00)81892-9
   Humphries MJ, 1996, CURR OPIN CELL BIOL, V8, P632, DOI 10.1016/S0955-0674(96)80104-9
   HYNES RO, 1992, CELL, V69, P11, DOI 10.1016/0092-8674(92)90115-S
   IRIE A, 1995, EMBO J, V14, P5550, DOI 10.1002/j.1460-2075.1995.tb00242.x
   KAMATA T, 1995, BIOCHEM J, V305, P945, DOI 10.1042/bj3050945
   KAWAGUCHI S, 1993, J BIOL CHEM, V268, P16279
   KRAMER RH, 1991, CELL REGUL, V2, P805, DOI 10.1091/mbc.2.10.805
   KRAMER RH, 1994, METHOD ENZYMOL, V245, P129
   LANGUINO LR, 1992, J BIOL CHEM, V267, P7116
   LIN CS, 1993, CANCER RES, V53, P2950
   Martin PT, 1996, DEV BIOL, V174, P125, DOI 10.1006/dbio.1996.0057
   MATTER ML, 1994, J CELL BIOL, V124, P1083, DOI 10.1083/jcb.124.6.1083
   MEREDITH J, 1995, SCIENCE, V269, P1570, DOI 10.1126/science.7545312
   Mould AP, 1996, J CELL SCI, V109, P2613
   PICKER LJ, 1993, EUR J IMMUNOL, V23, P2751, DOI 10.1002/eji.1830231105
   PuzonMcLaughlin W, 1996, J BIOL CHEM, V271, P16580, DOI 10.1074/jbc.271.28.16580
   Roote CE, 1996, DEVELOPMENT, V122, P1985
   SanchezMateos P, 1996, SEMIN CANCER BIOL, V7, P99, DOI 10.1006/scbi.1996.0015
   Schwartz MA, 1995, ANNU REV CELL DEV BI, V11, P549, DOI 10.1146/annurev.cellbio.11.1.549
   SHIMIZU Y, 1990, NATURE, V345, P250, DOI 10.1038/345250a0
   SONG WK, 1993, J CELL SCI, V106, P1139
   SONG WK, 1992, J CELL BIOL, V117, P643, DOI 10.1083/jcb.117.3.643
   SUZUKI S, 1990, EMBO J, V9, P757, DOI 10.1002/j.1460-2075.1990.tb08170.x
   TAKADA Y, 1993, J BIOL CHEM, V268, P17597
   TAMURA RN, 1991, P NATL ACAD SCI USA, V88, P10183, DOI 10.1073/pnas.88.22.10183
   TENNENBAUM T, 1995, P NATL ACAD SCI USA, V92, P7041, DOI 10.1073/pnas.92.15.7041
   TUCKWELL DS, 1994, CELL ADHES COMMUN, V2, P385, DOI 10.3109/15419069409004450
   VANDERFLIER A, 1995, FEBS LETT, V369, P340, DOI 10.1016/0014-5793(95)00814-P
   VANKUPPEVELT THMSM, 1989, P NATL ACAD SCI USA, V86, P5415
   WANG WW, 1995, GENOMICS, V26, P563, DOI 10.1016/0888-7543(95)80176-M
   WEITZMAN JB, 1993, J BIOL CHEM, V268, P8651
   Yao CC, 1997, J CELL SCI, V110, P1477
   Yao CC, 1996, J CELL SCI, V109, P3139
   Yao CC, 1996, J BIOL CHEM, V271, P25598, DOI 10.1074/jbc.271.41.25598
   ZAVORTINK M, 1993, CELL ADHES COMMUN, V1, P251, DOI 10.3109/15419069309097258
   ZHIDKOVA NI, 1995, BIOCHEM BIOPH RES CO, V214, P279, DOI 10.1006/bbrc.1995.2285
   ZIOBER BL, 1993, J BIOL CHEM, V268, P26773
NR 56
TC 45
Z9 51
U1 0
U2 0
PU AMER SOC CELL BIOLOGY
PI BETHESDA
PA 8120 WOODMONT AVE, STE 750, BETHESDA, MD 20814-2755 USA
SN 1059-1524
EI 1939-4586
J9 MOL BIOL CELL
JI Mol. Biol. Cell
PD SEP
PY 1997
VL 8
IS 9
BP 1723
EP 1734
DI 10.1091/mbc.8.9.1723
PG 12
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA XW993
UT WOS:A1997XW99300007
PM 9307969
OA Green Published
DA 2025-04-10
ER

PT J
AU Xiong, YG
   Soumillon, M
   Wu, J
   Hansen, J
   Hu, B
   van Hasselt, JGC
   Jayaraman, G
   Lim, R
   Bouhaddou, M
   Ornelas, L
   Bochicchio, J
   Lenaeus, L
   Stocksdale, J
   Shim, J
   Gomez, E
   Sareen, D
   Svendsen, C
   Thompson, LM
   Mahajan, M
   Iyengar, R
   Sobie, EA
   Azeloglu, EU
   Birtwistle, MR
AF Xiong, Yuguang
   Soumillon, Magali
   Wu, Jie
   Hansen, Jens
   Hu, Bin
   van Hasselt, Johan G. C.
   Jayaraman, Gomathi
   Lim, Ryan
   Bouhaddou, Mehdi
   Ornelas, Loren
   Bochicchio, Jim
   Lenaeus, Lindsay
   Stocksdale, Jennifer
   Shim, Jaehee
   Gomez, Emilda
   Sareen, Dhruv
   Svendsen, Clive
   Thompson, Leslie M.
   Mahajan, Milind
   Iyengar, Ravi
   Sobie, Eric A.
   Azeloglu, Evren U.
   Birtwistle, Marc R.
TI A Comparison of mRNA Sequencing with Random Primed and 3′-Directed
   Libraries
SO SCIENTIFIC REPORTS
LA English
DT Article
ID DIFFERENTIAL EXPRESSION; SEQ; TRANSCRIPTOME
AB Creating a cDNA library for deep mRNA sequencing (mRNAseq) is generally done by random priming, creating multiple sequencing fragments along each transcript. A 3'-end-focused library approach cannot detect differential splicing, but has potentially higher throughput at a lower cost, along with the ability to improve quantification by using transcript molecule counting with unique molecular identifiers (UMI) that correct PCR bias. Here, we compare an implementation of such a 3'-digital gene expression (3'-DGE) approach with "conventional" random primed mRNAseq. Given our particular datasets on cultured human cardiomyocyte cell lines, we find that, while conventional mRNAseq detects similar to 15% more genes and needs similar to 500,000 fewer reads per sample for equivalent statistical power, the resulting differentially expressed genes, biological conclusions, and gene signatures are highly concordant between two techniques. We also find good quantitative agreement at the level of individual genes between two techniques for both read counts and fold changes between given conditions. We conclude that, for high-throughput applications, the potential cost savings associated with 3'-DGE approach are likely a reasonable tradeoff for modest reduction in sensitivity and inability to observe alternative splicing, and should enable many larger scale studies focusing on not only differential expression analysis, but also quantitative transcriptome profiling.
C1 [Xiong, Yuguang; Hansen, Jens; Hu, Bin; van Hasselt, Johan G. C.; Jayaraman, Gomathi; Bouhaddou, Mehdi; Shim, Jaehee; Iyengar, Ravi; Sobie, Eric A.; Azeloglu, Evren U.; Birtwistle, Marc R.] Icahn Sch Med Mt Sinai, Dept Pharmacol Sci, New York, NY 10029 USA.
   [Xiong, Yuguang; Hansen, Jens; Hu, Bin; van Hasselt, Johan G. C.; Jayaraman, Gomathi; Bouhaddou, Mehdi; Shim, Jaehee; Iyengar, Ravi; Sobie, Eric A.; Azeloglu, Evren U.; Birtwistle, Marc R.] Icahn Sch Med Mt Sinai, DToxS LINCS Ctr, New York, NY 10029 USA.
   [Soumillon, Magali; Bochicchio, Jim] Broad Inst MIT & Harvard, Cambridge, MA USA.
   [Wu, Jie; Lim, Ryan; Thompson, Leslie M.] Univ Calif Irvine, Dept Biol Chem, Irvine, CA 92717 USA.
   [Wu, Jie; Lim, Ryan; Stocksdale, Jennifer; Thompson, Leslie M.] Univ Calif Irvine, UCI MIND, Irvine, CA USA.
   [Ornelas, Loren; Lenaeus, Lindsay; Gomez, Emilda; Sareen, Dhruv; Svendsen, Clive] Cedars Sinai Med Ctr, Board Governors Regenerat Med Inst, Los Angeles, CA 90048 USA.
   [Ornelas, Loren; Lenaeus, Lindsay; Gomez, Emilda; Sareen, Dhruv; Svendsen, Clive] David & Janet Polak Fdn, Stem Cell Core Lab, iPSC Core, Los Angeles, CA USA.
   [Sareen, Dhruv; Svendsen, Clive] Cedars Sinai Med Ctr, Dept Biomed Sci, Los Angeles, CA 90048 USA.
   [Thompson, Leslie M.] Univ Calif Irvine, Dept Psychiat & Human Behav, Neurobiol & Behav, Irvine, CA USA.
   [Mahajan, Milind] Icahn Sch Med Mt Sinai, Dept Genet, New York, NY 10029 USA.
   [Soumillon, Magali] Berkeley Lights Inc, 5858 Horton St, Emeryville, CA 94608 USA.
   [Birtwistle, Marc R.] Clemson Univ, Dept Chem & Biomol Engn, Clemson, SC 29634 USA.
C3 Icahn School of Medicine at Mount Sinai; Icahn School of Medicine at
   Mount Sinai; Harvard University; Massachusetts Institute of Technology
   (MIT); Broad Institute; University of California System; University of
   California Irvine; University of California System; University of
   California Irvine; Cedars Sinai Medical Center; Cedars Sinai Medical
   Center; University of California System; University of California
   Irvine; Icahn School of Medicine at Mount Sinai; Clemson University
RP Azeloglu, EU; Birtwistle, MR (corresponding author), Icahn Sch Med Mt Sinai, Dept Pharmacol Sci, New York, NY 10029 USA.; Azeloglu, EU; Birtwistle, MR (corresponding author), Icahn Sch Med Mt Sinai, DToxS LINCS Ctr, New York, NY 10029 USA.; Birtwistle, MR (corresponding author), Clemson Univ, Dept Chem & Biomol Engn, Clemson, SC 29634 USA.
EM evren.azeloglu@mssm.edu; marc.birtwistle@mssm.edu
RI van Hasselt, Coen/H-5593-2019; Hansen, Jens/ABD-5213-2022
OI Hansen, Jens/0000-0002-1362-6534; Lim, Ryan/0000-0001-6388-5158;
   Azeloglu, Evren/0000-0001-6137-109X; Sareen, Dhruv/0000-0002-0898-9656;
   van Hasselt, J.G.C./0000-0002-1664-7314; Xiong,
   Yuguang/0000-0001-5221-6266
FU NIH Grant [P50GM071558, U54NS091046]; NIGMS [T32GM062754]; 
   [R01GM104184];  [U54HG008098]
FX We acknowledge R01GM104184 (MRB) and U54HG008098 (LINCS Center), the NIH
   Grant P50GM071558 (Systems Biology Center New York) (MRB and RI), and
   the NIH Grant U54NS091046 (NeuroLINCS-LMT). MB was supported by a
   NIGMS-funded Integrated Pharmacological Sciences Training Program grant
   (T32GM062754). We also thank Marc Hafner for helpful discussions and
   facilitating our work with the Broad Institute team.
CR Ardlie KG, 2015, SCIENCE, V348, P648, DOI 10.1126/science.1262110
   Byron SA, 2016, NAT REV GENET, V17, P257, DOI 10.1038/nrg.2016.10
   Chen YS, 2014, FRONT PROBAB STAT SC, P51, DOI 10.1007/978-3-319-07212-8_3
   Conesa A, 2016, GENOME BIOL, V17, DOI 10.1186/s13059-016-0881-8
   DeLaughter D. M., 2016, DEV CELL, P163
   Fuller HR, 2016, FRONT CELL NEUROSCI, V9, DOI 10.3389/fncel.2015.00506
   Islam S, 2014, NAT METHODS, V11, P163, DOI [10.1038/NMETH.2772, 10.1038/nmeth.2772]
   Kivioja T, 2012, NAT METHODS, V9, P72, DOI [10.1038/NMETH.1778, 10.1038/nmeth.1778]
   La Manno G, 2016, CELL, V167, P566, DOI 10.1016/j.cell.2016.09.027
   Li S, 2014, NAT BIOTECHNOL, V32, P888, DOI 10.1038/nbt.3000
   Li S, 2014, NAT BIOTECHNOL, V32, P915, DOI 10.1038/nbt.2972
   Liu YC, 2013, BIOINFORMATICS, V29, P308, DOI [10.1093/bioinformatics/btt688, 10.1093/bioinformatics/bts690]
   Melé M, 2015, SCIENCE, V348, P660, DOI 10.1126/science.aaa0355
   Mortazavi A, 2008, NAT METHODS, V5, P621, DOI 10.1038/nmeth.1226
   Olsson A, 2016, NATURE, V537, P698, DOI 10.1038/nature19348
   Parekh S, 2016, SCI REP-UK, V6, DOI 10.1038/srep25533
   Plaisier SB, 2010, NUCLEIC ACIDS RES, V38, DOI 10.1093/nar/gkq636
   Risso D, 2014, NAT BIOTECHNOL, V32, P896, DOI 10.1038/nbt.2931
   Rivas MA, 2015, SCIENCE, V348, P666, DOI 10.1126/science.1261877
   Robinson MD, 2008, BIOSTATISTICS, V9, P321, DOI 10.1093/biostatistics/kxm030
   Robinson MD, 2010, GENOME BIOL, V11, DOI 10.1186/gb-2010-11-3-r25
   Robinson MD, 2010, BIOINFORMATICS, V26, P139, DOI 10.1093/bioinformatics/btp616
   Sareen D, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0039113
   Smith G. R., 2016, PLOS ONE, V11
   Soumillon M., 2014, 3236 BIORXIV
   Su ZQ, 2014, NAT BIOTECHNOL, V32, P903, DOI 10.1038/nbt.2957
   Tarazona S, 2011, GENOME RES, V21, P2213, DOI 10.1101/gr.124321.111
   Trapnell C, 2013, NAT BIOTECHNOL, V31, P46, DOI 10.1038/nbt.2450
   Trapnell C, 2010, NAT BIOTECHNOL, V28, P511, DOI 10.1038/nbt.1621
   Trapnell C, 2009, BIOINFORMATICS, V25, P1105, DOI 10.1093/bioinformatics/btp120
   Wagner A., 2016, NAT PUBL GR, V34, P1
   Wang C, 2014, NAT BIOTECHNOL, V32, P926, DOI 10.1038/nbt.3001
   Ziegenhain C, 2017, MOL CELL, V65, P631, DOI 10.1016/j.molcel.2017.01.023
NR 33
TC 36
Z9 41
U1 0
U2 4
PU NATURE PORTFOLIO
PI BERLIN
PA HEIDELBERGER PLATZ 3, BERLIN, 14197, GERMANY
SN 2045-2322
J9 SCI REP-UK
JI Sci Rep
PD NOV 7
PY 2017
VL 7
AR 14626
DI 10.1038/s41598-017-14892-x
PG 12
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA FL9IA
UT WOS:000414565700006
PM 29116112
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Li, MY
   Jia, C
   Kazmierkiewicz, KL
   Bowman, AS
   Tian, LF
   Liu, YC
   Gupta, NA
   Gudiseva, HV
   Yee, SS
   Kim, M
   Dentchev, T
   Kimble, JA
   Parker, JS
   Messinger, JD
   Hakonarson, H
   Curcio, CA
   Stambolian, D
AF Li, Mingyao
   Jia, Cheng
   Kazmierkiewicz, Krista L.
   Bowman, Anita S.
   Tian, Lifeng
   Liu, Yichuan
   Gupta, Neel A.
   Gudiseva, Harini V.
   Yee, Stephanie S.
   Kim, Mijin
   Dentchev, Tzvete
   Kimble, James A.
   Parker, John S.
   Messinger, Jeffrey D.
   Hakonarson, Hakon
   Curcio, Christine A.
   Stambolian, Dwight
TI Comprehensive analysis of gene expression in human retina and supporting
   tissues
SO HUMAN MOLECULAR GENETICS
LA English
DT Article
ID PIGMENT EPITHELIUM; GEOGRAPHIC ATROPHY; BRUCHS MEMBRANE; GANGLION-CELLS;
   OPTIC-NERVE; AGE; DISEASE; RNA; TOPOGRAPHY; MACULA
AB Understanding the influence of gene expression on the molecular mechanisms underpinning human phenotypic diversity is fundamental to being able to predict health outcomes and treat disease. We have carried out whole transcriptome expression analysis on a series of eight normal human postmortem eyes by RNA sequencing. Here we present data showing that similar to 80% of the transcriptome is expressed in the posterior layers of the eye and that there is significant differential expression not only between the layers of the posterior part of the eye but also between locations of a tissue layer. These differences in expression also extend to alternative splicing and splicing factors. Differentially expressed genes are enriched for genes associated with psychiatric, immune and cardiovascular disorders. Enrichment categories for gene ontology included ion transport, synaptic transmission and visual and sensory perception. Lastly, allele-specific expression was found to be significant for CFH, C3 and CFB, which are known risk genes for age-related macular degeneration. These expression differences should be useful in determining the underlying biology of associations with common diseases of the human retina, retinal pigment epithelium and choroid and in guiding the analysis of the genomic regions involved in the control of normal gene expression.
C1 [Li, Mingyao; Jia, Cheng; Liu, Yichuan] Univ Penn, Perelman Sch Med, Dept Biostat & Epidemiol, Philadelphia, PA 19104 USA.
   [Kazmierkiewicz, Krista L.; Bowman, Anita S.; Gudiseva, Harini V.; Yee, Stephanie S.; Kim, Mijin; Stambolian, Dwight] Univ Penn, Perelman Sch Med, Dept Ophthalmol, Philadelphia, PA 19104 USA.
   [Dentchev, Tzvete] Univ Penn, Perelman Sch Med, Dept Dermatol, Philadelphia, PA 19104 USA.
   [Hakonarson, Hakon] Univ Penn, Perelman Sch Med, Dept Pediat, Philadelphia, PA 19104 USA.
   [Tian, Lifeng; Hakonarson, Hakon] Childrens Hosp Philadelphia, Ctr Appl Genom, Philadelphia, PA 19104 USA.
   [Hakonarson, Hakon] Childrens Hosp Philadelphia, Div Pulm Med, Philadelphia, PA 19104 USA.
   [Gupta, Neel A.] Drexel Univ, Coll Med, Philadelphia, PA 19104 USA.
   [Kimble, James A.] Retina Specialists Alabama, Birmingham, AL 35294 USA.
   [Kimble, James A.; Parker, John S.; Messinger, Jeffrey D.; Curcio, Christine A.] Univ Alabama Sch Med, Dept Ophthalmol, Birmingham, AL 35294 USA.
C3 University of Pennsylvania; University of Pennsylvania; University of
   Pennsylvania; University of Pennsylvania; University of Pennsylvania;
   Pennsylvania Medicine; Childrens Hospital of Philadelphia; University of
   Pennsylvania; Pennsylvania Medicine; Childrens Hospital of Philadelphia;
   Drexel University
RP Stambolian, D (corresponding author), Univ Penn, Perelman Sch Med, Dept Ophthalmol, Philadelphia, PA 19104 USA.
EM stamboli@mail.med.upenn.edu; stamboli@mail.med.upenn.edu
RI Parker, John/H-5751-2019; Liu, Yichuan/AAF-3893-2021; Hakonarson,
   Hakon/ABZ-4865-2022
OI Bowman, Anita S./0000-0002-8651-5317; LIU, YICHUAN/0000-0003-2023-072X
FU Arnold and Mabel Beckman Initiative for Macular Research
FX The Arnold and Mabel Beckman Initiative for Macular Research.
CR Anders S, 2010, GENOME BIOL, V11, DOI 10.1186/gb-2010-11-10-r106
   Bailey JNC, 2013, HUM MOL GENET, V22, pR59, DOI 10.1093/hmg/ddt396
   BARONDES M, 1990, BRIT J OPHTHALMOL, V74, P180, DOI 10.1136/bjo.74.3.180
   Bellmann C, 2002, ARCH OPHTHALMOL-CHIC, V120, P579, DOI 10.1001/archopht.120.5.579
   Berisha F, 2007, INVEST OPHTH VIS SCI, V48, P2285, DOI 10.1167/iovs.06-1029
   Cai H, 2012, FRONT AGING NEUROSCI, V4, DOI 10.3389/fnagi.2012.00008
   Chung TS, 2012, J CLIN PSYCHOPHARM, V32, P394, DOI 10.1097/JCP.0b013e31825370f4
   Curcio CA, 2001, EYE, V15, P376, DOI 10.1038/eye.2001.140
   Curcio CA, 2001, INVEST OPHTH VIS SCI, V42, P265
   CURCIO CA, 1990, J COMP NEUROL, V292, P497, DOI 10.1002/cne.902920402
   CURCIO CA, 1990, J COMP NEUROL, V300, P5, DOI 10.1002/cne.903000103
   Curcio CA, 2013, RETINA-J RET VIT DIS, V33, P265, DOI 10.1097/IAE.0b013e31827e25e0
   Curcio CA, 2011, INVEST OPHTH VIS SCI, V52, P3943, DOI 10.1167/iovs.10-6377
   DACEY DM, 1993, J NEUROSCI, V13, P5334, DOI 10.1523/JNEUROSCI.13-12-05334.1993
   DeLuca DS, 2012, BIOINFORMATICS, V28, P1530, DOI 10.1093/bioinformatics/bts196
   Dennis G, 2003, GENOME BIOL, V4, DOI 10.1186/gb-2003-4-9-r60
   Drasdo N, 2007, VISION RES, V47, P2901, DOI 10.1016/j.visres.2007.01.007
   Fleckenstein M, 2010, INVEST OPHTH VIS SCI, V51, P637, DOI 10.1167/iovs.09-3547
   Freedman ML, 2011, NAT GENET, V43, P513, DOI 10.1038/ng.840
   Freund KB, 2010, RETINA-J RET VIT DIS, V30, P1333, DOI 10.1097/IAE.0b013e3181e7976b
   Fritsche LG, 2013, NAT GENET, V45, P433, DOI 10.1038/ng.2578
   Geiss GK, 2008, NAT BIOTECHNOL, V26, P317, DOI 10.1038/nbt1385
   Göring HHH, 2007, NAT GENET, V39, P1208, DOI 10.1038/ng2119
   Hirano AA, 2011, J COMP NEUROL, V519, P972, DOI 10.1002/cne.22562
   Hornan DM, 2007, INVEST OPHTH VIS SCI, V48, P5388, DOI 10.1167/iovs.07-0355
   Huang DW, 2009, NAT PROTOC, V4, P44, DOI 10.1038/nprot.2008.211
   Kamei M, 1999, INVEST OPHTH VIS SCI, V40, P2367
   KATZ B, 1989, SURV OPHTHALMOL, V34, P31, DOI 10.1016/0039-6257(89)90127-6
   KATZ B, 1989, ANN NEUROL, V26, P221, DOI 10.1002/ana.410260207
   Kirwan RP, 2012, INVEST OPHTH VIS SCI, V53, P2243, DOI 10.1167/iovs.11-6729
   Klein RJ, 2005, SCIENCE, V308, P385, DOI 10.1126/science.1109557
   Li CM, 2005, J LIPID RES, V46, P628, DOI 10.1194/jlr.M400428-JLR200
   Li J, 2002, INVEST OPHTH VIS SCI, V43, P573
   LUTTY GA, 1993, INVEST OPHTH VIS SCI, V34, P477
   Malik KF, 2003, INVEST OPHTH VIS SCI, V44, P2730, DOI 10.1167/iovs.02-1120
   Morley M, 2004, NATURE, V430, P743, DOI 10.1038/nature02797
   Moschos MM, 2012, CURR ALZHEIMER RES, V9, P782
   Mrejen S, 2013, SURV OPHTHALMOL, V58, P387, DOI 10.1016/j.survophthal.2012.12.001
   Neumann S, 2013, J COMP NEUROL, V521, P709, DOI 10.1002/cne.23201
   Nickla DL, 2010, PROG RETIN EYE RES, V29, P144, DOI 10.1016/j.preteyeres.2009.12.002
   Nicolae DL, 2010, PLOS GENET, V6, DOI 10.1371/journal.pgen.1000888
   Nishikawa S, 2001, CURR EYE RES, V22, P34, DOI 10.1076/ceyr.22.1.34.6979
   Oak A. S. W., 2014, RETINA
   Polyak SL., 1941, RETINA-J RET VIT DIS
   Rickman CB, 2006, INVEST OPHTH VIS SCI, V47, P2305, DOI 10.1167/iovs.05-1437
   Robinson MD, 2010, BIOINFORMATICS, V26, P139, DOI 10.1093/bioinformatics/btp616
   Rodieck R. W., 1999, 1 STEPS SEEING
   Ruiz A, 1996, BIOCHEM BIOPH RES CO, V226, P467, DOI 10.1006/bbrc.1996.1379
   Schaub MA, 2012, GENOME RES, V22, P1748, DOI 10.1101/gr.136127.111
   Sharon D, 2002, P NATL ACAD SCI USA, V99, P315, DOI 10.1073/pnas.012582799
   Shen SH, 2012, NUCLEIC ACIDS RES, V40, DOI 10.1093/nar/gkr1291
   Spraul CW, 1996, INVEST OPHTH VIS SCI, V37, P2724
   Stambolian D, 2013, CLIN GENET, V84, P102, DOI 10.1111/cge.12180
   Trapnell C, 2013, NAT BIOTECHNOL, V31, P46, DOI 10.1038/nbt.2450
   Trapnell C, 2010, NAT BIOTECHNOL, V28, P511, DOI 10.1038/nbt.1621
   Twine NA, 2011, PLOS ONE, V6, DOI 10.1371/journal.pone.0016266
   Verhoeven VJM, 2013, NAT GENET, V45, P314, DOI 10.1038/ng.2554
   Vogt SD, 2006, EXP EYE RES, V83, P834, DOI 10.1016/j.exer.2006.04.002
   Vogt SD, 2011, EXP EYE RES, V93, P413, DOI 10.1016/j.exer.2011.06.002
   Wagner AH, 2013, EXP EYE RES, V111, P105, DOI 10.1016/j.exer.2013.03.004
   Wang JJ, 1998, BRIT J OPHTHALMOL, V82, P743, DOI 10.1136/bjo.82.7.743
   Wang L, 2010, PLOS ONE, V5, DOI 10.1371/journal.pone.0010329
   WEITER JJ, 1986, INVEST OPHTH VIS SCI, V27, P145
   Wiggs JL, 2012, PLOS GENET, V8, P413, DOI 10.1371/journal.pgen.1002654
   Wu TD, 2005, BIOINFORMATICS, V21, P1859, DOI 10.1093/bioinformatics/bti310
   Yoshida S, 2002, INVEST OPHTH VIS SCI, V43, P2554
   Zheng WC, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0037926
   Zweifel SA, 2010, OPHTHALMOLOGY, V117, P303, DOI 10.1016/j.ophtha.2009.07.014
NR 68
TC 93
Z9 101
U1 1
U2 12
PU OXFORD UNIV PRESS
PI OXFORD
PA GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND
SN 0964-6906
EI 1460-2083
J9 HUM MOL GENET
JI Hum. Mol. Genet.
PD AUG 1
PY 2014
VL 23
IS 15
BP 4001
EP 4014
DI 10.1093/hmg/ddu114
PG 14
WC Biochemistry & Molecular Biology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Genetics & Heredity
GA AM2GV
UT WOS:000339669200007
PM 24634144
OA Green Submitted, hybrid, Green Published
DA 2025-04-10
ER

PT J
AU Stoodley, J
   Vallejo-Bedia, F
   Seone-Miraz, D
   Debasa-Mouce, M
   Wood, MJA
   Varela, MA
AF Stoodley, Jessica
   Vallejo-Bedia, Francisco
   Seone-Miraz, David
   Debasa-Mouce, Manuel
   Wood, Matthew J. A.
   Varela, Miguel A.
TI Application of Antisense Conjugates for the Treatment of Myotonic
   Dystrophy Type 1
SO INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
LA English
DT Review
DE antibody; bridged nucleic acids; cell-penetrating peptide; lipids;
   muscle; myotonic dystrophy; oligonucleotides; splicing
ID 3 UNTRANSLATED REGION; LOCKED NUCLEIC-ACIDS; OLIGONUCLEOTIDE THERAPY;
   TRINUCLEOTIDE REPEAT; MOUSE MODEL; SPLICING REGULATION; TARGETING DMPK;
   RNA TOXICITY; CTG REPEAT; IN-VIVO
AB Myotonic dystrophy type 1 (DM1) is one of the most common muscular dystrophies and can be potentially treated with antisense therapy decreasing mutant DMPK, targeting miRNAs or their binding sites or via a blocking mechanism for MBNL1 displacement from the repeats. Unconjugated antisense molecules are able to correct the disease phenotype in mouse models, but they show poor muscle penetration upon systemic delivery in DM1 patients. In order to overcome this challenge, research has focused on the improvement of the therapeutic window and biodistribution of antisense therapy using bioconjugation to lipids, cell penetrating peptides or antibodies. Antisense conjugates are able to induce the long-lasting correction of DM1 pathology at both molecular and functional levels and also efficiently penetrate hard-to-reach tissues such as cardiac muscle. Delivery to the CNS at clinically relevant levels remains challenging and the use of alternative administration routes may be necessary to ameliorate some of the symptoms experienced by DM1 patients. With several antisense therapies currently in clinical trials, the outlook for achieving a clinically approved treatment for patients has never looked more promising.
C1 [Stoodley, Jessica; Vallejo-Bedia, Francisco; Seone-Miraz, David; Debasa-Mouce, Manuel; Wood, Matthew J. A.; Varela, Miguel A.] Univ Oxford, Inst Dev & Regenerat Med IDRM, Dept Paediat, Roosevelt Dr, Oxford OX3 7TY, England.
   [Stoodley, Jessica; Vallejo-Bedia, Francisco; Seone-Miraz, David; Debasa-Mouce, Manuel; Wood, Matthew J. A.; Varela, Miguel A.] MDUK Oxford Neuromuscular Ctr, Oxford OX3 7TY, England.
C3 University of Oxford
RP Varela, MA (corresponding author), Univ Oxford, Inst Dev & Regenerat Med IDRM, Dept Paediat, Roosevelt Dr, Oxford OX3 7TY, England.; Varela, MA (corresponding author), MDUK Oxford Neuromuscular Ctr, Oxford OX3 7TY, England.
EM miguel.varela@paediatrics.ox.ac.uk
RI Wood, Matthew/HDN-1469-2022
OI Varela Muino, Miguel Angel/0000-0003-4376-9381; Debasa-Mouce,
   Manuel/0000-0001-9511-7399; Stoodley, Jessica/0000-0003-4406-9002
FU Medical Research Council (MRC) [MRW0147421, MRP01741X1]; John Fell Fund
   [0007895]
FX This work was supported by Medical Research Council (MRC) grants
   (MRW0147421 and MRP01741X1) and by John Fell Fund (0007895).
CR Aartsma-Rus A, 2017, NUCLEIC ACID THER, V27, P251, DOI 10.1089/nat.2017.0682
   Batra R, 2014, MOL CELL, V56, P311, DOI 10.1016/j.molcel.2014.08.027
   Benichou SA, 2022, GENE THER, V29, DOI 10.1038/s41434-022-00316-7
   Betts CA, 2015, SCI REP-UK, V5, DOI 10.1038/srep08986
   BROOK JD, 1992, CELL, V68, P799, DOI 10.1016/0092-8674(92)90154-5
   Cerro-Herreros E, 2021, MOL THER-NUCL ACIDS, V26, P174, DOI 10.1016/j.omtn.2021.07.017
   Cerro-Herreros E, 2020, MOL THER NUCL ACIDS, V21, P837, DOI 10.1016/j.omtn.2020.07.021
   Cerro-Herreros E, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-04892-4
   Corey DR, 2017, NAT NEUROSCI, V20, P497, DOI 10.1038/nn.4508
   Crooke ST, 2017, NUCLEIC ACID THER, V27, P70, DOI 10.1089/nat.2016.0656
   Davis BM, 1997, P NATL ACAD SCI USA, V94, P7388, DOI 10.1073/pnas.94.14.7388
   DOMINSKI Z, 1993, P NATL ACAD SCI USA, V90, P8673, DOI 10.1073/pnas.90.18.8673
   Douniol M, 2012, DEV MED CHILD NEUROL, V54, P905, DOI 10.1111/j.1469-8749.2012.04379.x
   Dugal-Tessier J, 2021, J CLIN MED, V10, DOI 10.3390/jcm10040838
   Echenne B, 2013, HAND CLINIC, V113, P1387, DOI 10.1016/B978-0-444-59565-2.00009-5
   Eckstein F, 2014, NUCLEIC ACID THER, V24, P374, DOI 10.1089/nat.2014.0506
   Eder P S, 1991, Antisense Res Dev, V1, P141
   Fortune MT, 2000, HUM MOL GENET, V9, P439, DOI 10.1093/hmg/9.3.439
   Freyermuth F, 2016, NAT COMMUN, V7, DOI 10.1038/ncomms11067
   Fugier C, 2011, NAT MED, V17, P720, DOI 10.1038/nm.2374
   Gao XJ, 2014, MOL THER, V22, P1333, DOI 10.1038/mt.2014.63
   Goodkey K, 2018, METHODS MOL BIOL, V1828, P69, DOI 10.1007/978-1-4939-8651-4_4
   Hamm S, 2010, IMMUNOBIOLOGY, V215, P559, DOI 10.1016/j.imbio.2009.09.003
   Hammond SM, 2021, bioRxiv, DOI [10.1101/2021.07.29.454272, 10.1101/2021.07.29.454272, DOI 10.1101/2021.07.29.454272]
   Hammond SM, 2021, EMBO MOL MED, V13, DOI 10.15252/emmm.202013243
   Hammond SM, 2016, P NATL ACAD SCI USA, V113, P10962, DOI 10.1073/pnas.1605731113
   Huguet A, 2012, PLOS GENET, V8, DOI 10.1371/journal.pgen.1003043
   Ionis Pharmaceuticals Reports, DMPKRX PHAS 1 2 TRIA
   Ivanova GD, 2008, NUCLEIC ACIDS RES, V36, P6418, DOI 10.1093/nar/gkn671
   Jauvin D, 2017, MOL THER-NUCL ACIDS, V7, P465, DOI 10.1016/j.omtn.2017.05.007
   Jeong W, 2014, CANCER CHEMOTH PHARM, V73, P343, DOI 10.1007/s00280-013-2362-z
   Johnsen KB, 2019, PROG NEUROBIOL, V181, DOI 10.1016/j.pneurobio.2019.101665
   Johnson N., 2022, APPL ENVIRON MICROB, V98, P2711
   Johnson NE, 2021, NEUROLOGY, V96, pE1045, DOI 10.1212/WNL.0000000000011425
   Kanadia RN, 2006, P NATL ACAD SCI USA, V103, P11748, DOI 10.1073/pnas.0604970103
   Kanadia RN, 2003, GENE EXPR PATTERNS, V3, P459, DOI 10.1016/S1567-133X(03)00064-4
   Khan T, 2016, MOL THER-NUCL ACIDS, V5, DOI 10.1038/mtna.2016.55
   King M, 1997, EUR J PHARMACOL, V331, pR5, DOI 10.1016/S0014-2999(97)01064-9
   Klein AF, 2019, J CLIN INVEST, V129, P4739, DOI 10.1172/JCI128205
   Konieczny P, 2014, NUCLEIC ACIDS RES, V42, P10873, DOI 10.1093/nar/gku767
   Koshkin AA, 1998, TETRAHEDRON, V54, P3607, DOI 10.1016/S0040-4020(98)00094-5
   Krützfeldt J, 2005, NATURE, V438, P685, DOI 10.1038/nature04303
   Kuyumcu-Martinez NM, 2007, MOL CELL, V28, P68, DOI 10.1016/j.molcel.2007.07.027
   Ladd AN, 2013, MOL CELL NEUROSCI, V56, P456, DOI 10.1016/j.mcn.2012.12.003
   Larsen HJ, 1999, BBA-GENE STRUCT EXPR, V1489, P159, DOI 10.1016/S0167-4781(99)00145-1
   Larsen Maja Thim, 2016, Mol Cell Ther, V4, P3
   Lee JE, 2012, P NATL ACAD SCI USA, V109, P4221, DOI 10.1073/pnas.1117019109
   Lee KY, 2013, EMBO MOL MED, V5, P1887, DOI 10.1002/emmm.201303275
   Leger AJ, 2013, NUCLEIC ACID THER, V23, P109, DOI 10.1089/nat.2012.0404
   Leventhal L, 1996, BRAIN RES, V719, P78, DOI 10.1016/0006-8993(96)00089-3
   López-Martínez A, 2020, GENES-BASEL, V11, DOI 10.3390/genes11091109
   Lueck JD, 2007, J GEN PHYSIOL, V129, P79, DOI 10.1085/jgp.200609635
   MAHADEVAN M, 1992, SCIENCE, V255, P1253, DOI 10.1126/science.1546325
   Mankodi A, 2000, SCIENCE, V289, P1769, DOI 10.1126/science.289.5485.1769
   Manoharan M, 1999, BBA-GENE STRUCT EXPR, V1489, P117, DOI 10.1016/S0167-4781(99)00138-4
   Miller JW, 2000, EMBO J, V19, P4439, DOI 10.1093/emboj/19.17.4439
   MONIA BP, 1993, J BIOL CHEM, V268, P14514
   Morita K, 2002, BIOORG MED CHEM LETT, V12, P73, DOI 10.1016/S0960-894X(01)00683-7
   Mulders SAM, 2009, P NATL ACAD SCI USA, V106, P13915, DOI 10.1073/pnas.0905780106
   Nagata T, 2021, NAT BIOTECHNOL, V39, P1529, DOI 10.1038/s41587-021-00972-x
   Norwood FLM, 2009, BRAIN, V132, P3175, DOI 10.1093/brain/awp236
   Obika S, 2001, BIOORGAN MED CHEM, V9, P1001, DOI 10.1016/S0968-0896(00)00325-4
   Obika S, 2001, CHEM COMMUN, P1992, DOI 10.1039/b105640a
   Ostergaard ME, 2019, NUCLEIC ACIDS RES, V47, P6045, DOI 10.1093/nar/gkz360
   Overby SJ, 2022, MOL THER-NUCL ACIDS, V27, P1146, DOI 10.1016/j.omtn.2022.02.003
   Pandey SK, 2015, J PHARMACOL EXP THER, V355, P329, DOI 10.1124/jpet.115.226969
   Pascual-Gilabert M, 2021, DRUG DISCOV TODAY, V26, P1765, DOI [10.1016/j.drudis.2021.03.024This, 10.1016/j.drudis.2021.03.024]
   Paterson Judy, 2016, Drug Discov Today Technol, V20, P49, DOI 10.1016/j.ddtec.2016.07.009
   Prakash TP, 2019, NUCLEIC ACIDS RES, V47, P6029, DOI 10.1093/nar/gkz354
   Rao AN, 2021, JCI INSIGHT, V6, DOI 10.1172/jci.insight.143465
   Rau F, 2015, NAT COMMUN, V6, DOI 10.1038/ncomms8205
   Relizani K, 2022, NUCLEIC ACIDS RES, V50, P17, DOI 10.1093/nar/gkab1199
   Rifai A, 1996, AM J PATHOL, V149, P717
   Roberts TC, 2020, NAT REV DRUG DISCOV, V19, P673, DOI 10.1038/s41573-020-0075-7
   Rossi G, 1994, Life Sci, V54, pPL375, DOI 10.1016/0024-3205(94)90038-8
   Saarbach J, 2019, CURR OPIN CHEM BIOL, V52, P112, DOI 10.1016/j.cbpa.2019.06.006
   Savkur RS, 2001, NAT GENET, V29, P40, DOI 10.1038/ng704
   Seth PP, 2019, J CLIN INVEST, V129, P915, DOI 10.1172/JCI125228
   Siciliano G, 2001, CLIN GENET, V59, P344, DOI 10.1034/j.1399-0004.2001.590508.x
   Sievers EL, 2013, ANNU REV MED, V64, P15, DOI 10.1146/annurev-med-050311-201823
   Singh RN, 2018, ADV NEUROBIOL, V20, P31, DOI 10.1007/978-3-319-89689-2_2
   Sonoda H, 2018, MOL THER, V26, P1366, DOI 10.1016/j.ymthe.2018.02.032
   Summerton J, 1997, ANTISENSE NUCLEIC A, V7, P187, DOI 10.1089/oli.1.1997.7.187
   Tabrizi SJ, 2019, NEW ENGL J MED, V380, P2307, DOI 10.1056/NEJMoa1900907
   TANEJA KL, 1995, J CELL BIOL, V128, P995, DOI 10.1083/jcb.128.6.995
   TSILFIDIS C, 1992, NAT GENET, V1, P192, DOI 10.1038/ng0692-192
   Veedu RN, 2009, RNA BIOL, V6, P321, DOI 10.4161/rna.6.3.8807
   Vester B, 2004, BIOCHEMISTRY-US, V43, P13233, DOI 10.1021/bi0485732
   Wang ET, 2012, CELL, V150, P710, DOI 10.1016/j.cell.2012.06.041
   Wang SY, 2019, NUCLEIC ACID THER, V29, P245, DOI 10.1089/nat.2019.0794
   Ward AJ, 2010, HUM MOL GENET, V19, P3614, DOI 10.1093/hmg/ddq277
   Watanabe TA, 2006, OLIGONUCLEOTIDES, V16, P169, DOI 10.1089/oli.2006.16.169
   Weaving G, 2016, ANN CLIN BIOCHEM, V53, P106, DOI 10.1177/0004563215593561
   Webster CI, 2017, PAIN, V158, P660, DOI 10.1097/j.pain.0000000000000810
   Weijs R, 2021, NEUROPATHOLOGY, V41, P3, DOI 10.1111/neup.12721
   Wheeler TM, 2012, NATURE, V488, P111, DOI 10.1038/nature11362
   Wheeler TM, 2009, SCIENCE, V325, P336, DOI 10.1126/science.1173110
   Wojtkowiak-Szlachcic A, 2015, NUCLEIC ACIDS RES, V43, P3318, DOI 10.1093/nar/gkv163
   Wu HJ, 2004, J BIOL CHEM, V279, P17181, DOI 10.1074/jbc.M311683200
   Yadava RS, 2020, HUM MOL GENET, V29, P1440, DOI 10.1093/hmg/ddaa060
   Yang JL, 2021, NEUROBIOL DIS, V148, DOI 10.1016/j.nbd.2020.105218
   Yin H, 2008, HUM MOL GENET, V17, P3909, DOI 10.1093/hmg/ddn293
NR 102
TC 7
Z9 7
U1 0
U2 6
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
SN 1661-6596
EI 1422-0067
J9 INT J MOL SCI
JI Int. J. Mol. Sci.
PD FEB
PY 2023
VL 24
IS 3
AR 2697
DI 10.3390/ijms24032697
PG 13
WC Biochemistry & Molecular Biology; Chemistry, Multidisciplinary
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Chemistry
GA 8V6JR
UT WOS:000930735900001
PM 36769018
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Giacomello, M
   De Mario, A
   Scarlatti, C
   Primerano, S
   Carafoli, E
AF Giacomello, Marta
   De Mario, Agnese
   Scarlatti, Chiara
   Primerano, Simona
   Carafoli, Ernesto
TI Plasma membrane calcium ATPases and related disorders
SO INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
LA English
DT Review
DE Ca2+ pumps; Ca2+ homeostasis; Embryonic development; Genetic deafness;
   Cerebellar ataxia
ID CA2+ PUMP; CA2+-ATPASE PMCA; HAIR-CELLS; RAT-BRAIN; ISOFORM 4;
   EXPRESSION; CALMODULIN; LOCALIZATION; MUTATION; SITE
AB The plasma membrane Ca2+ ATPases (PMCA pumps) cooperate with other transport systems in the plasma membrane and in the organelles in the regulation of cell Ca2+. They have high Ca2+ affinity and are thus the fine tuners of cytosolic Ca2+. They belong to the superfamily of P-type ATPases: their four basic isoforms share the essential properties of the reaction cycle and the general membrane topography motif of 10 transmembrane domains and three large cytosolic units. However they also differ in other important properties, e.g., tissue distribution and regulatory mechanisms. Their chief regulator is calmodulin, that removes their C-terminal cytosolic tail from autoinhibitory binding sites next to the active site of the pump, restoring activity. The number of pump isoforms is increased to over 30 by alternative splicing of the transcripts at a N-terminal site (site A) and at site C within the C-terminal calmodulin binding domain: the splice variants are tissue specific and developmentally regulated.
   The importance of PMCAs in the maintenance of cellular Ca2+ homeostasis is underlined by the disease phenotypes, genetic or acquired, caused by their malfunction. Non-genetic PMCA deficiencies have long been considered possible causative factors in disease conditions as important as cancer, hypertension, or neurodegeneration. Those of genetic origin are better characterized: some have now been discovered in humans as well. They concern all four PMCA isoforms, and range from cardiac dysfunctions, to deafness, to hypertension, to cerebellar ataxia. (c) 2012 Elsevier Ltd. All rights reserved.
C1 [Giacomello, Marta; De Mario, Agnese; Scarlatti, Chiara; Primerano, Simona; Carafoli, Ernesto] Univ Padua, Venetian Inst Mol Med, Padua, Italy.
C3 Veneto Institute Molecular Medicine; University of Padua
RP Carafoli, E (corresponding author), Univ Padua, Venetian Inst Mol Med, Padua, Italy.
EM ernesto.carafoli@unipd.it
RI GIACOMELLO, MARTA/HGB-1486-2022; Carafoli, Ernesto/K-5192-2016
OI Carafoli, Ernesto/0000-0002-7826-0094; Giacomello,
   Marta/0000-0002-0290-6602; De Mario, Agnese/0000-0001-5129-4780
CR Aartsen WM, 2009, MOL CELL NEUROSCI, V41, P156, DOI 10.1016/j.mcn.2009.02.003
   Arking DE, 2006, NAT GENET, V38, P644, DOI 10.1038/ng1790
   Aung CS, 2007, BIOCHEM BIOPH RES CO, V355, P932, DOI 10.1016/j.bbrc.2007.02.050
   Axelsen KB, 1998, J MOL EVOL, V101, P46
   Beurg M, 2010, J NEUROPHYSIOL, V104, P18, DOI 10.1152/jn.00019.2010
   BRANDT P, 1992, J BIOL CHEM, V267, P4376
   Brini M, 2003, J BIOL CHEM, V278, P24500, DOI 10.1074/jbc.M300784200
   Brini M, 2012, METAL IONS LIFE SCI, V12
   Brown CS, 2007, PLATELETS, V18, P207, DOI 10.1080/09537100600954037
   Carafoli E, 2003, NAT REV MOL CELL BIO, V4, P326, DOI 10.1038/nrm1073
   CARAFOLI E, 1991, PHYSIOL REV, V71, P129, DOI 10.1152/physrev.1991.71.1.129
   CARAFOLI E, 1994, FASEB J, V8, P993, DOI 10.1096/fasebj.8.13.7926378
   CARAFOLI E, 1974, J MOL CELL CARDIOL, V6, P361, DOI 10.1016/0022-2828(74)90077-7
   Carafoli E, 2010, BBA-BIOENERGETICS, V1797, P595, DOI 10.1016/j.bbabio.2010.03.024
   Caride AJ, 1999, KIDNEY INT, V56, P1818, DOI 10.1046/j.1523-1755.1999.00736.x
   Caride AJ, 1999, J BIOL CHEM, V274, P35227, DOI 10.1074/jbc.274.49.35227
   Cartwright EJ, 2007, ANN NY ACAD SCI, V1099, P247, DOI 10.1196/annals.1387.007
   Chang KC, 2008, P NATL ACAD SCI USA, V105, P4477, DOI 10.1073/pnas.0709118105
   Cho YS, 2009, NAT GENET, V41, P527, DOI 10.1038/ng.357
   Duncan JL, 2006, J NEUROSCI, V26, P7201, DOI 10.1523/JNEUROSCI.5230-05.2006
   EAKIN TJ, 1995, MOL BRAIN RES, V29, P71, DOI 10.1016/0169-328X(94)00231-3
   Elwess NL, 1997, J BIOL CHEM, V272, P17981, DOI 10.1074/jbc.272.29.17981
   Empson RM, 2010, FUNCT NEUROL, V25, P153
   ENYEDI A, 1994, J BIOL CHEM, V269, P41
   FALCHETTO R, 1992, PROTEIN SCI, V1, P1613, DOI 10.1002/pro.5560011209
   FALCHETTO R, 1991, J BIOL CHEM, V266, P2930
   Ficarella R, 2007, P NATL ACAD SCI USA, V104, P1516, DOI 10.1073/pnas.0609775104
   Filoteo AG, 1997, J BIOL CHEM, V272, P23741, DOI 10.1074/jbc.272.38.23741
   FUJIMOTO T, 1993, J CELL BIOL, V120, P1147, DOI 10.1083/jcb.120.5.1147
   Giacomello M, 2012, INT J BIOCHEM CELL B, V44, P679, DOI 10.1016/j.biocel.2012.02.006
   Giacomello M, 2011, CELL CALCIUM, V50, P569, DOI 10.1016/j.ceca.2011.09.004
   Grati M, 2006, J CELL SCI, V119, P2995, DOI 10.1242/jcs.03030
   Guerini D, 2000, J BIOL CHEM, V275, P3706, DOI 10.1074/jbc.275.5.3706
   Guerini D, 2003, J BIOL CHEM, V278, P38141, DOI 10.1074/jbc.M302400200
   Guerini D, 1999, J BIOL CHEM, V274, P1667, DOI 10.1074/jbc.274.3.1667
   Gunaratne HJ, 2006, J CELL PHYSIOL, V207, P413, DOI 10.1002/jcp.20575
   HILFIKER H, 1994, J BIOL CHEM, V269, P26178
   Holton Mary Louisa, 2010, World J Biol Chem, V1, P201, DOI 10.4331/wjbc.v1.i6.201
   Hong KW, 2010, J HUM HYPERTENS, V24, P367, DOI 10.1038/jhh.2009.86
   INOUE Y, 1993, NEUROSCI RES, V16, P39, DOI 10.1016/0168-0102(93)90007-D
   JAMES PH, 1989, BIOCHEMISTRY-US, V28, P4253, DOI 10.1021/bi00436a020
   Johnson JE, 2007, MOL VIS, V13, P887
   Jones S, 2008, SCIENCE, V321, P1801, DOI 10.1126/science.1164368
   Kamagate A, 2000, CELL CALCIUM, V27, P231, DOI 10.1054/ceca.2000.0116
   Krebs J, 2003, HELV CHIM ACTA, V86, P3875, DOI 10.1002/hlca.200390325
   Lee WJ, 2005, BIOCHEM BIOPH RES CO, V337, P779, DOI 10.1016/j.bbrc.2005.09.119
   Lehotsky J, 1999, NEUROCHEM INT, V35, P221, DOI 10.1016/S0197-0186(99)00062-5
   Mohamed TMA, 2011, J BIOL CHEM, V286, P41520, DOI 10.1074/jbc.M111.290411
   Morgans CW, 1998, J NEUROSCI, V18, P2467
   Oceandy D, 2007, BIOCHEM SOC T, V35, P927, DOI 10.1042/BST0350927
   Okunande GW, 2004, J BIOL CHEM, V279, P33742, DOI 10.1074/jbc.M404628200
   Palty R, 2010, P NATL ACAD SCI USA, V107, P436, DOI 10.1073/pnas.0908099107
   PEDERSEN PL, 1987, TRENDS BIOCHEM SCI, V12, P146, DOI 10.1016/0968-0004(87)90071-5
   Penniston J T, 1980, Ann N Y Acad Sci, V356, P245, DOI 10.1111/j.1749-6632.1980.tb29615.x
   Philipson KD, 1999, CALCIUM AS A CELLULAR REGULATOR, P279
   Reinhardt T.A., 1999, Am. J. Physiol, V276, P796
   Reinhardt TA, 2004, J BIOL CHEM, V279, P42369, DOI 10.1074/jbc.M407788200
   Ricci AJ, 1998, J PHYSIOL-LONDON, V506, P159, DOI 10.1111/j.1469-7793.1998.159bx.x
   Roberts-Thomson Sarah J, 2010, World J Biol Chem, V1, P248, DOI 10.4331/wjbc.v1.i8.248
   SALAMINO F, 1994, CELL CALCIUM, V15, P28, DOI 10.1016/0143-4160(94)90101-5
   SCHNITZER JE, 1995, P NATL ACAD SCI USA, V92, P1759, DOI 10.1073/pnas.92.5.1759
   Schuh K, 2001, J CELL BIOL, V155, P201, DOI 10.1083/jcb.200104131
   Schultz JM, 2005, NEW ENGL J MED, V352, P1557, DOI 10.1056/NEJMoa043899
   Schwede T, 2003, NUCLEIC ACIDS RES, V31, P3381, DOI 10.1093/nar/gkg520
   Sepúlveda MR, 2006, J BIOL CHEM, V281, P447, DOI 10.1074/jbc.M506950200
   Silverstein RS, 2006, NEUROSCIENCE, V141, P245, DOI 10.1016/j.neuroscience.2006.03.036
   STAHL WL, 1992, ANN NY ACAD SCI, V671, P433, DOI 10.1111/j.1749-6632.1992.tb43821.x
   Stahl WL, 1996, NEUROSCI LETT, V178, P267
   STAUFFER TP, 1993, J BIOL CHEM, V268, P25993
   STAUFFER TP, 1995, J BIOL CHEM, V270, P12184, DOI 10.1074/jbc.270.20.12184
   Street VA, 1998, NAT GENET, V19, P390, DOI 10.1038/1284
   Strehler EE, 2004, CURR MOL MED, V4, P323, DOI 10.2174/1566524043360735
   Strehler EE, 2001, PHYSIOL REV, V81, P21, DOI 10.1152/physrev.2001.81.1.21
   THOMPSON JD, 1994, NUCLEIC ACIDS RES, V22, P4673, DOI 10.1093/nar/22.22.4673
   Tidow H, 2012, NATURE, V491, P468, DOI 10.1038/nature11539
   Toyoshima C, 2000, NATURE, V405, P647, DOI 10.1038/35015017
   Toyoshima C, 2002, NATURE, V418, P605, DOI 10.1038/nature00944
   Toyoshima C, 2008, ARCH BIOCHEM BIOPHYS, V476, P3, DOI 10.1016/j.abb.2008.04.017
   Ueda K, 2008, P NATL ACAD SCI USA, V105, P9355, DOI 10.1073/pnas.0801294105
   VanHouten J, 2010, P NATL ACAD SCI USA, V107, P11405, DOI 10.1073/pnas.0911186107
   Yang J, 2007, HUM MOL GENET, V16, P1017, DOI 10.1093/hmg/ddm047
   Zacharias DA, 1999, BBA-GEN SUBJECTS, V1428, P397, DOI 10.1016/S0304-4165(99)00058-6
   Zanni G, 2012, P NATL ACAD SCI USA, V109, P14514, DOI 10.1073/pnas.1207488109
NR 83
TC 25
Z9 29
U1 0
U2 33
PU PERGAMON-ELSEVIER SCIENCE LTD
PI OXFORD
PA THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND
SN 1357-2725
EI 1878-5875
J9 INT J BIOCHEM CELL B
JI Int. J. Biochem. Cell Biol.
PD MAR
PY 2013
VL 45
IS 3
BP 753
EP 762
DI 10.1016/j.biocel.2012.09.016
PG 10
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA 098HL
UT WOS:000315539900029
PM 23041476
DA 2025-04-10
ER

PT J
AU Lin, JC
AF Lin, Jung-Chun
TI RBM4-MEF2C network constitutes a feed-forward circuit that facilitates
   the differentiation of brown adipocytes
SO RNA BIOLOGY
LA English
DT Article
DE alternative splicing; brown adipocytes; MEF2C; miR-1; RBM4
ID MUSCLE-SPECIFIC MICRORNAS; LONG NONCODING RNA; MESSENGER-RNA;
   TRANSCRIPTIONAL CONTROL; GENE-EXPRESSION; ADIPOSE-TISSUE; MEF2 GENE;
   ADIPOGENESIS; RBM4; PHOSPHORYLATION
AB Myocyte enhancer factor 2c (MEF2C) is the MADS-box type transcription factor involved in the differentiation of cardiac and skeletal muscle and synaptic formation. Alternatively spliced transcripts of the MEF2C gene were proven to encode isoforms which exert distinct functions in transcriptional regulation. During the differentiation of brown adipocytes, upregulated RBM4 enhanced skipping of the MEF2C gamma region which functions as a transcriptional repressor. The presence of an overexpressed MEF2C gamma- isoform in turn induced transcriptional activity of the RBM4 promoter, constituting a positive feedback circuit in differentiating brown adipocytes. The RBM4-MEF2C gamma- network induced the expression of "myogenic" miR-1 to a greater extent than did PRDM17, BMP7 C/EBP beta, or UCP1 transcripts in C3H10T1/2 cells. Overexpression of miR-1 independently exerted the same activity as RBM4 and the MEF2C gamma- isoform of upregulating brown adipocyte-specific factors in C3H10T1/2 cells, which suggests a potential effect of miR-1 on brown adipocytes. These results indicated that the RBM4-MEF2C-miR-1 network constitutes a novel mechanism which programs the gene expression profile toward the development of brown adipocytes.
C1 Taipei Med Univ, Coll Med Sci & Technol, Sch Med Lab Sci & Biotechnol, Taipei, Taiwan.
C3 Taipei Medical University
RP Lin, JC (corresponding author), Taipei Med Univ, Coll Med Sci & Technol, Sch Med Lab Sci & Biotechnol, Taipei, Taiwan.
EM lin2511@tmu.edu.tw
FU National Science Council [NSC102-2320-B-038-045]; Ministry of Science
   and Technology of Taiwan [MOST103-2320-B-038-047-MY2]
FX This work was supported by grants (NSC102-2320-B-038-045) from the
   National Science Council and (MOST103-2320-B-038-047-MY2) from the
   Ministry of Science and Technology of Taiwan.
CR Ab Hakim NH, 2010, GENES CELLS, V15, P255, DOI 10.1111/j.1365-2443.2009.01378.x
   Bachinski LL, 2010, MUSCLE NERVE, V42, P856, DOI 10.1002/mus.21789
   Black BL, 1998, ANNU REV CELL DEV BI, V14, P167, DOI 10.1146/annurev.cellbio.14.1.167
   Cacchiarelli D, 2010, CELL METAB, V12, P341, DOI 10.1016/j.cmet.2010.07.008
   Cannon B, 2004, PHYSIOL REV, V84, P277, DOI 10.1152/physrev.00015.2003
   Cesana M, 2011, CELL, V147, P358, DOI 10.1016/j.cell.2011.09.028
   Chen JF, 2006, NAT GENET, V38, P228, DOI 10.1038/ng1725
   Conte I, 2014, NUCLEIC ACIDS RES, V42, P7793, DOI 10.1093/nar/gku498
   COUSIN B, 1992, J CELL SCI, V103, P931
   Devakanmalai GS, 2013, BIOL OPEN, V2, P505, DOI 10.1242/bio.20132550
   EDMONDSON DG, 1994, DEVELOPMENT, V120, P1251
   Entingh AJ, 2003, J BIOL CHEM, V278, P33377, DOI 10.1074/jbc.M303056200
   Gagan J, 2012, J BIOL CHEM, V287, P40360, DOI 10.1074/jbc.M112.378414
   Ganassi M, 2014, BBA-GENE REGUL MECH, V1839, P559, DOI 10.1016/j.bbagrm.2014.05.003
   Giordano A, 2014, EUR J ENDOCRINOL, V170, pR159, DOI 10.1530/EJE-13-0945
   Gonçalves V, 2014, RNA, V20, P474, DOI 10.1261/rna.041376.113
   Hinits Y, 2009, DEVELOPMENT, V136, P403, DOI 10.1242/dev.028019
   Karbiener M, 2014, STEM CELLS, V32, P1578, DOI 10.1002/stem.1603
   Legnini I, 2014, MOL CELL, V53, P506, DOI 10.1016/j.molcel.2013.12.012
   LEIFER D, 1993, P NATL ACAD SCI USA, V90, P1546, DOI 10.1073/pnas.90.4.1546
   Lin JC, 2005, MOL CELL BIOL, V25, P10111, DOI 10.1128/MCB.25.22.10111-10121.2005
   Lin JC, 2014, RNA, V20, P1621, DOI 10.1261/rna.045583.114
   Lin JC, 2014, BBA-MOL CELL RES, V1843, P769, DOI 10.1016/j.bbamcr.2013.12.018
   Lin JC, 2013, MOL CELL BIOL, V33, P319, DOI 10.1128/MCB.01266-12
   Lin JC, 2011, J CELL BIOL, V193, P509, DOI 10.1083/jcb.201007131
   Lin JC, 2009, J BIOL CHEM, V284, P34658, DOI 10.1074/jbc.M109.032946
   Liu N, 2007, P NATL ACAD SCI USA, V104, P20844, DOI 10.1073/pnas.0710558105
   Liu N, 2014, P NATL ACAD SCI USA, V111, P4109, DOI 10.1073/pnas.1401732111
   LYONS GE, 1995, J NEUROSCI, V15, P5727, DOI 10.1523/jneurosci.15-08-05727.1995
   MARTIN JF, 1994, MOL CELL BIOL, V14, P1647, DOI 10.1128/MCB.14.3.1647
   Penn BH, 2004, GENE DEV, V18, P2348, DOI 10.1101/gad.1234304
   Rosen ED, 2006, NAT REV MOL CELL BIO, V7, P885, DOI 10.1038/nrm2066
   Seale P, 2008, NATURE, V454, P961, DOI 10.1038/nature07182
   Seale P, 2009, GENE DEV, V23, P788, DOI 10.1101/gad.1779209
   Sharma G, 2005, MOL CELL ENDOCRINOL, V245, P93, DOI 10.1016/j.mce.2005.10.027
   Sun SY, 2010, NAT STRUCT MOL BIOL, V17, P306, DOI 10.1038/nsmb.1750
   Sweetman D, 2008, DEV BIOL, V321, P491, DOI 10.1016/j.ydbio.2008.06.019
   Trajkovski M, 2012, NAT CELL BIOL, V14, P1330, DOI 10.1038/ncb2612
   Tseng YH, 2008, NATURE, V454, P1000, DOI 10.1038/nature07221
   Walden TB, 2009, J CELL PHYSIOL, V218, P444, DOI 10.1002/jcp.21621
   Wu J, 2013, GENE DEV, V27, P234, DOI 10.1101/gad.211649.112
   Zhu BM, 2005, J BIOL CHEM, V280, P28749, DOI 10.1074/jbc.M502491200
   Zhu BM, 2004, MOL CELL BIOL, V24, P8264, DOI 10.1128/MCB.24.18.8264-8275.2004
NR 43
TC 19
Z9 20
U1 0
U2 5
PU TAYLOR & FRANCIS INC
PI PHILADELPHIA
PA 530 WALNUT STREET, STE 850, PHILADELPHIA, PA 19106 USA
SN 1547-6286
EI 1555-8584
J9 RNA BIOL
JI RNA Biol.
PY 2015
VL 12
IS 2
BP 208
EP 220
DI 10.1080/15476286.2015.1017213
PG 13
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA CF0MT
UT WOS:000352238900011
PM 25826570
OA Green Published, Bronze
DA 2025-04-10
ER

PT J
AU Antonetti, DA
   Algenstaedt, P
   Kahn, CR
AF Antonetti, DA
   Algenstaedt, P
   Kahn, CR
TI Insulin receptor substrate 1 binds two novel splice variants of the
   regulatory subunit of phosphatidylinositol 3-kinase in muscle and brain
SO MOLECULAR AND CELLULAR BIOLOGY
LA English
DT Article
ID GROWTH-FACTOR RECEPTORS; TYROSINE KINASES; SH2 DOMAINS; PI3-KINASE;
   ASSOCIATE; PROTEINS; CLONING; CDNA; GENE; P85
AB We have identified two novel alternatively spliced forms of the p85 alpha regulatory subunit of phosphatidylinositol (PI) 3-kinase by expression screening of a human skeletal muscle library with phosphorylated baculovirus-produced human insulin receptor substrate 1, One form is identical to p85 alpha throughout the region which encodes both Src homology 2 (SH2) domains and the inter-SH2 domain/p110 binding region but diverges in sequence from p85 alpha on the 5' side of nucleotide 953, where the entire break point cluster gene and SH3 regions are replaced by a unique 34-amino-acid N terminus, This form has an estimated molecular mass of similar to 53 M)a and has been termed p85/AS53. The second form is identical to p85 and p85/AS53 except for a 24-nucleotide insert between the SH2 domains that results in a replacement of aspartic acid 605 with nine amino acids, adding two potential serine phosphorylation sites in the vicinity of the known serine autophosphorylation site (Ser-608), Northern (RNA) analyses reveal a wide tissue distribution of p85 alpha, whereas p85/AS53 is dominant in skeletal muscle and brain, and the insert isoforms are restricted to cardiac muscle and skeletal muscle. Western blot (immunoblot) analyses using an anti-p85 polyclonal antibody and a specific anti-p85/AS53 antibody confirmed the tissue distribution of p85/AS53 protein and indicate a similar to 7-fold higher expression of p85/AS53 protein than of p85 in skeletal muscle, Both p85 and p85/AS53 bind to p110 in coprecipitation experiments, but p85 alpha itself appears to have preferential binding to insulin receptor substrate 1 following insulin stimulation, These data indicate that the gene for the p85 alpha regulatory subunit of PI 3-kinase can undergo tissue-specific alternative splicing. Two novel splice variants of the regulatory subunit of PI 3-kinase are present in skeletal muscle, cardiac muscle, and brain; these variants may have important functional differences in activity and may play a role in tissue-specific signals such as insulin-stimulated glucose transport or control of neurotransmitter secretion or action.
C1 HARVARD UNIV,SCH MED,JOSLIN DIABET CTR,DIV RES,BOSTON,MA 02215.
   HARVARD UNIV,SCH MED,DEPT MED,BOSTON,MA 02215.
C3 Harvard University; Harvard Medical School; Harvard University Medical
   Affiliates; Joslin Diabetes Center, Inc.; Harvard University; Harvard
   Medical School
RI Kahn, Ronald/AAY-2435-2021
OI antonetti, david/0000-0003-1130-6577
FU NIDDK NIH HHS [DK33201, DK45935] Funding Source: Medline
CR AHN AH, 1993, NAT GENET, V3, P283, DOI 10.1038/ng0493-283
   ARAKI E, 1993, DIABETES, V42, P1041, DOI 10.2337/diabetes.42.7.1041
   ARAKI E, 1994, NATURE, V372, P186, DOI 10.1038/372186a0
   Ausubel F.M., 1993, CURRENT PROTOCOLS MO
   BALTENSPERGER K, 1994, J BIOL CHEM, V269, P28937
   CHEATHAM B, 1995, ENDOCR REV, V16, P117, DOI 10.1210/er.16.2.117
   DHAND R, 1994, EMBO J, V13, P511, DOI 10.1002/j.1460-2075.1994.tb06289.x
   DHAND R, 1994, EMBO J, V13, P522, DOI 10.1002/j.1460-2075.1994.tb06290.x
   DIVECHA N, 1995, CELL, V80, P269, DOI 10.1016/0092-8674(95)90409-3
   ESCOBEDO JA, 1991, CELL, V65, P75, DOI 10.1016/0092-8674(91)90409-R
   HU P, 1992, MOL CELL BIOL, V12, P981, DOI 10.1128/MCB.12.3.981
   HU QJ, 1995, SCIENCE, V268, P100, DOI 10.1126/science.7701328
   KASUYA J, 1995, J BIOL CHEM, V270, P14305, DOI 10.1074/jbc.270.24.14305
   KENNELLY PJ, 1991, J BIOL CHEM, V266, P15555
   KLIPPEL A, 1994, MOL CELL BIOL, V14, P2675, DOI 10.1128/MCB.14.4.2675
   LAM K, 1994, J BIOL CHEM, V269, P20648
   LAMPHERE L, 1994, AM J PHYSIOL, V266, pE486, DOI 10.1152/ajpendo.1994.266.3.E486
   LEE AD, 1995, GROWTH REGULAT, V361, P51
   LING LE, 1992, J VIROL, V66, P1702, DOI 10.1128/JVI.66.3.1702-1708.1992
   MCGLADE CJ, 1992, MOL CELL BIOL, V12, P991, DOI 10.1128/MCB.12.3.991
   OKADA T, 1994, J BIOL CHEM, V269, P3568
   OTSU M, 1991, CELL, V65, P91, DOI 10.1016/0092-8674(91)90411-Q
   PONS S, 1995, MOL CELL BIOL, V15, P4453
   ROCHE S, 1994, P NATL ACAD SCI USA, V91, P9185, DOI 10.1073/pnas.91.19.9185
   Sambrook J, 1989, MOL CLONING LAB MANU
   SHEPHERD PR, 1995, BIOCHEM J, V305, P25, DOI 10.1042/bj3050025
   SIMS RE, 1987, SOUTHERN MED J, V80, P903, DOI 10.1097/00007611-198707000-00023
   SKOLNIK EY, 1991, CELL, V65, P83, DOI 10.1016/0092-8674(91)90410-Z
   STOYANOV B, 1995, SCIENCE, V269, P690, DOI 10.1126/science.7624799
   SUN XJ, 1993, MOL CELL BIOL, V13, P7418, DOI 10.1128/MCB.13.12.7418
   TANIZAWA Y, 1992, MOL ENDOCRINOL, V6, P1070, DOI 10.1210/me.6.7.1070
   VARTICOVSKI L, 1994, BBA-MOL BASIS DIS, V1226, P1, DOI 10.1016/0925-4439(94)90051-5
   WANG J, 1995, J BIOL CHEM, V270, P12774, DOI 10.1074/jbc.270.21.12774
   WHITE M, COMMUNICATION
   WHITE MF, 1994, CURR OPIN GENET DEV, V4, P47, DOI 10.1016/0959-437X(94)90090-6
   WHITE MF, 1994, J BIOL CHEM, V269, P1
   WHITE MF, 1988, J BIOL CHEM, V263, P2969
   WHITE MF, 1990, PEPTIDE HORMONE ACTI, P223
   YEH JI, 1995, J BIOL CHEM, V270, P2107, DOI 10.1074/jbc.270.5.2107
   ZANCA DM, 1986, NATURE, V319, P743
   ZHENG Y, 1994, J BIOL CHEM, V269, P18727
   Zhu JH, 1996, J BIOL CHEM, V271, P768, DOI 10.1074/jbc.271.2.768
NR 42
TC 112
Z9 124
U1 0
U2 6
PU AMER SOC MICROBIOLOGY
PI WASHINGTON
PA 1325 MASSACHUSETTS AVENUE, NW, WASHINGTON, DC 20005-4171
SN 0270-7306
J9 MOL CELL BIOL
JI Mol. Cell. Biol.
PD MAY
PY 1996
VL 16
IS 5
BP 2195
EP 2203
PG 9
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA UG299
UT WOS:A1996UG29900033
PM 8628286
DA 2025-04-10
ER

PT J
AU Appukuttan, B
   McFarland, TJ
   Davies, MH
   Atchaneeyasakul, LO
   Zhang, Y
   Babra, B
   Pan, YZ
   Rosenbaum, JT
   Acott, T
   Powers, MR
   Stout, JT
AF Appukuttan, Binoy
   McFarland, Trevor J.
   Davies, Michael H.
   Atchaneeyasakul, La-ongsri
   Zhang, Yi
   Babra, Bobby
   Pan, Yuzhen
   Rosenbaum, James T.
   Acott, Ted
   Powers, Michael R.
   Stout, J. Timothy
TI Identification of novel alternatively spliced isoforms of RTEF-1 within
   human ocular vascular endothelial cells and murine retina
SO INVESTIGATIVE OPHTHALMOLOGY & VISUAL SCIENCE
LA English
DT Article
ID TRANSCRIPTION FACTOR RTEF-1; OXYGEN-INDUCED RETINOPATHY; GROWTH-FACTOR
   GENE; PROXIMAL PROMOTER; CARDIAC MYOCYTES; FACTOR TEF-1; DNA-BINDING;
   EXPRESSION; ENHANCER; FAMILY
AB PURPOSE. Identification of transcription factors that regulate the transcription of the vascular endothelial growth factor ( VEGF) gene may facilitate understanding of the etiology and progression of ocular neovascular diseases. The purpose of this study was to determine whether transcriptional enhancer factor 1-related (RTEF-1) was present within ocular vascular endothelial cells and whether it played a role in the control of the transcription of the VEGF gene.
   METHODS. Primary cultures of human retinal vascular endothelial cells (RVECs) were maintained under normoxic or hypoxic conditions before isolation of mRNA. RT-PCR was performed to detect RTEF-1 transcripts. Amplified products were cloned into an expression plasmid. Human VEGF promoter and deletion constructs were cloned into a pSEAP reporter vector. Various RTEF-1 isoforms and VEGF promoter constructs were coelectroporated into human cells, and reporter expression levels were determined. Retinal tissue from a mouse model of retinopathy of prematurity (ROP) was analyzed by RT-PCR for the presence of RTEF-1 transcripts.
   RESULTS. Full-length 1305-bp and novel 936-bp RTEF-1 transcripts were identified in cultured human RVECs under normoxic conditions. A novel 447-bp isoform was present in cells maintained in a hypoxic environment. Four of the 11 translated exons predicted to code for the 1305-bp product were spliced out of the 936-bp transcript. The 1305-bp product enhanced expression from the VEGF promoter 4-fold greater than background, whereas the 936-bp and the 447-bp isoforms enhanced expression 3X and 12X, respectively. Analysis with deletion promoter constructs determined that all isoforms required the presence of Sp1 elements for efficient activation and that the hypoxia response element (HRE) was not essential for enhancement. Transcripts for novel RTEF-1 isoforms were also identified in neural retinal tissue of mice. Different murinespecific isoforms were present at different stages of postnatal development.
   CONCLUSIONS. Novel RTEF-1 transcripts are present within human ocular vascular endothelial cells and mouse neural retina during normal and ROP development, and alternatively spliced products are produced under hyperoxic and hypoxic conditions. Alternative spliced variants of human RTEF-1 transcripts are able to potentiate expression from the VEGF 5' proximal promoter region.
C1 Oregon Hlth & Sci Univ, Casey Eye Inst, Portland, OR 97239 USA.
C3 Oregon Health & Science University
RP Stout, JT (corresponding author), Oregon Hlth & Sci Univ, Casey Eye Inst, 3375 SW Terwilliger Blvd, Portland, OR 97239 USA.
EM stoutt@ohsu.edu
RI Atchaneeyasakul, La-ongsri/B-2901-2012; Pan, JX/GVS-2269-2022
FU NEI NIH HHS [EY008247, EY003279, EY011548, R01 EY019042, EY010572]
   Funding Source: Medline
CR Davies MH, 2003, INVEST OPHTH VIS SCI, V44, P3202, DOI 10.1167/iovs.03-0050
   DAVIS RJ, 1993, J BIOL CHEM, V268, P14553
   Donahue ML, 1996, CURR EYE RES, V15, P175, DOI 10.3109/02713689608997411
   Farrance IKG, 1996, J BIOL CHEM, V271, P8266, DOI 10.1074/jbc.271.14.8266
   Finkenzeller G, 1997, ONCOGENE, V15, P669, DOI 10.1038/sj.onc.1201219
   Forsythe JA, 1996, MOL CELL BIOL, V16, P4604
   FRIGERIO JM, 1995, HUM MOL GENET, V4, P37, DOI 10.1093/hmg/4.1.37
   Jacquemin P, 1996, J BIOL CHEM, V271, P21775, DOI 10.1074/jbc.271.36.21775
   Jiang SW, 2000, BIOCHEMISTRY-US, V39, P3505, DOI 10.1021/bi991048w
   Kanda K, 1998, ENDOTHELIUM-J ENDOTH, V6, P33, DOI 10.3109/10623329809053403
   Kaneko KJ, 1998, DEV GENET, V22, P43, DOI 10.1002/(SICI)1520-6408(1998)22:1<43::AID-DVG5>3.0.CO;2-7
   Lashkari K, 2000, AM J PATHOL, V156, P1337, DOI 10.1016/S0002-9440(10)65004-3
   Miller JW, 1997, AM J PATHOL, V151, P13
   PEER J, 1995, LAB INVEST, V72, P638
   Pierce EA, 1996, ARCH OPHTHALMOL-CHIC, V114, P1219, DOI 10.1001/archopht.1996.01100140419009
   SEIPEL K, 1992, EMBO J, V11, P4961, DOI 10.1002/j.1460-2075.1992.tb05603.x
   Shie JL, 2004, J BIOL CHEM, V279, P25010, DOI 10.1074/jbc.M403103200
   Silverman MD, 2005, MICROVASC RES, V70, P32, DOI 10.1016/j.mvr.2005.07.001
   SMITH LEH, 1994, INVEST OPHTH VIS SCI, V35, P101
   Stewart AFR, 1996, GENOMICS, V37, P68, DOI 10.1006/geno.1996.0522
   Stewart AFR, 1998, CIRC RES, V83, P43, DOI 10.1161/01.RES.83.1.43
   THEILL LE, 1989, NATURE, V342, P945, DOI 10.1038/342945a0
   Ueyama T, 2000, J BIOL CHEM, V275, P17476, DOI 10.1074/jbc.M001970200
   Vannay A, 2005, PEDIATR RES, V57, P396, DOI 10.1203/01.PDR.0000153867.80238.E0
   XIAO JH, 1991, CELL, V65, P551, DOI 10.1016/0092-8674(91)90088-G
   Yasunami M, 1996, BIOCHEM BIOPH RES CO, V228, P365, DOI 10.1006/bbrc.1996.1667
   Yockey CE, 1996, J BIOL CHEM, V271, P3727, DOI 10.1074/jbc.271.7.3727
   Young T L, 1997, J AAPOS, V1, P105, DOI 10.1016/S1091-8531(97)90008-2
   Zuzarte PC, 2000, BBA-GENE STRUCT EXPR, V1517, P82, DOI 10.1016/S0167-4781(00)00261-X
NR 29
TC 14
Z9 22
U1 0
U2 4
PU ASSOC RESEARCH VISION OPHTHALMOLOGY INC
PI ROCKVILLE
PA 12300 TWINBROOK PARKWAY, ROCKVILLE, MD 20852-1606 USA
SN 0146-0404
J9 INVEST OPHTH VIS SCI
JI Invest. Ophthalmol. Vis. Sci.
PD AUG
PY 2007
VL 48
IS 8
BP 3775
EP 3782
DI 10.1167/iovs.06-1172
PG 8
WC Ophthalmology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Ophthalmology
GA 199VF
UT WOS:000248722600045
PM 17652751
DA 2025-04-10
ER

PT J
AU Pusceddu, I
   Dieplinger, B
   Mueller, T
AF Pusceddu, Irene
   Dieplinger, Benjamin
   Mueller, Thomas
TI ST2 and the ST2/IL-33 signalling pathway-biochemistry and
   pathophysiology in animal models and humans
SO CLINICA CHIMICA ACTA
LA English
DT Review
DE Biomarkers; Diagnosis; Inflammation; Interleukin; Prognosis
ID EMERGENCY-DEPARTMENT PATIENTS; RECEPTOR ACCESSORY PROTEIN; SOLUBLE ST2;
   HEART-FAILURE; NUCLEAR IL-33; EXPRESSION; CELLS; CYTOKINE; GENE;
   TUMORIGENICITY-2
AB ST2 is an interleukin (IL)-1 receptor family member with transmembrane (ST2L) and soluble (sST2) isoforms. Structurally, the ST2 gene products are very similar in mice and humans. In humans and in mice, alternative promoter activation and splicing produce ST2L and sST2. ST2L represents the longest transcript, whereas sST2 is the truncated, soluble isoform. ST2L is the biological receptor for IL-33, a member of the IL-1 family. IL-33 is the functional ligand of ST2L and signals the presence of tissue damage to local immune cells. IL-33/ST2L signalling leads to the production of inflammatory cytokines/chemokines and to the induction of the immune response. Conversely, sST2 functions as a decoy receptor for IL-33, inhibiting the effects of IL-33/ST2L signalling. Animal studies have allowed the investigation of ST2 and the IL-33/ST2L signalling pathway at multiple levels. However, clinical studies have mainly focused on the determination of sST2 in the circulation. In humans, plasma concentrations of sST2 increase in several diseases, such as heart disease, pulmonary disease, burn injury and graft-versus-host disease. Consequently, increased plasma concentrations of sST2 are not specific for a single disorder in humans and are thus of limited value for diagnostic purposes. However, increased plasma concentrations of sST2 have been linked to a worse prognosis in numerous diseases. Nevertheless, the major source of circulating sST2 in healthy and diseased humans is currently not fully established. In addition, whether the downregulation of sST2 can improve the outcome of patients in the clinical setting has not been elucidated. The aim of the present review was to provide an update on the findings regarding the biochemistry and pathophysiology of ST2 and the sST2 signalling pathway in humans and experimental models.
C1 [Pusceddu, Irene; Mueller, Thomas] Hosp Bolzano, Dept Clin Pathol, Via Lorenz Boehler 5, I-39100 Bolzano, Italy.
   [Dieplinger, Benjamin] Konventhosp Barntherzige Brueder Linz, Dept Lab Med, Linz, Austria.
C3 Krankenhaus Bozen
RP Mueller, T (corresponding author), Hosp Bolzano, Dept Clin Pathol, Via Lorenz Boehler 5, I-39100 Bolzano, Italy.
EM thomas.mueller@sabes.it
OI Mueller, Thomas/0000-0002-5095-3964
CR Abdullahi M, 2016, IRAN J IMMUNOL, V13, P27, DOI IJIv13i1A4
   Aimo A, 2017, JACC-HEART FAIL, V5, P287, DOI 10.1016/j.jchf.2016.12.016
   Aimo A, 2017, JACC-HEART FAIL, V5, P280, DOI 10.1016/j.jchf.2016.09.010
   Ali M, 2009, TISSUE ANTIGENS, V73, P206, DOI 10.1111/j.1399-0039.2008.01185.x
   Ali S, 2007, P NATL ACAD SCI USA, V104, P18660, DOI 10.1073/pnas.0705939104
   Baekkevold ES, 2003, AM J PATHOL, V163, P69, DOI 10.1016/S0002-9440(10)63631-0
   Bajwa EK, 2015, AM J CARDIOL, V115, p44B, DOI 10.1016/j.amjcard.2015.01.040
   Bandara G, 2015, EUR J IMMUNOL, V45, P3034, DOI 10.1002/eji.201545501
   Bartunek J, 2008, J AM COLL CARDIOL, V52, P2166, DOI 10.1016/j.jacc.2008.09.027
   Benoit JL, 2013, ACAD EMERG MED, V20, P1207, DOI 10.1111/acem.12250
   Brunner SM, 2011, TRANSPL INT, V24, P1027, DOI 10.1111/j.1432-2277.2011.01306.x
   Carriere V, 2007, P NATL ACAD SCI USA, V104, P282, DOI 10.1073/pnas.0606854104
   Cayrol C, 2009, P NATL ACAD SCI USA, V106, P9021, DOI 10.1073/pnas.0812690106
   Chan WL, 2003, IMMUNOL LETT, V85, P159, DOI 10.1016/S0165-2478(02)00223-7
   Chen B, 2018, J INTERF CYTOK RES, V38, P137, DOI 10.1089/jir.2017.0067
   Choi YS, 2012, BIOCHEM BIOPH RES CO, V421, P305, DOI 10.1016/j.bbrc.2012.04.005
   Curinier C, 2018, CONTEMP CLIN TRIALS, V66, P45, DOI 10.1016/j.cct.2018.01.007
   De Grove KC, 2018, CLIN EXP ALLERGY, V48, P1665, DOI 10.1111/cea.13261
   De la Fuente M, 2015, CYTOKINE GROWTH F R, V26, P615, DOI 10.1016/j.cytogfr.2015.07.017
   Demyanets S, 2013, J MOL CELL CARDIOL, V60, P16, DOI 10.1016/j.yjmcc.2013.03.020
   Dieplinger B, 2015, CLIN CHIM ACTA, V451, P310, DOI 10.1016/j.cca.2015.10.015
   Du WJ, 2018, THERANOSTICS, V8, P4155, DOI 10.7150/thno.26055
   Funakoshi-Tago M, 2008, CELL SIGNAL, V20, P1679, DOI 10.1016/j.cellsig.2008.05.013
   Gachter T, 1996, J BIOL CHEM, V271, P124
   Glück J, 2012, INFLAMM RES, V61, P547, DOI 10.1007/s00011-012-0443-9
   Griesenauer B, 2017, FRONT IMMUNOL, V8, DOI 10.3389/fimmu.2017.00475
   Hacker S, 2018, CLIN CHEM LAB MED, V56, P2079, DOI 10.1515/cclm-2018-0042
   Haider T, 2018, CLIN CHEM LAB MED, V56, P810, DOI 10.1515/cclm-2017-0762
   Hartopo AB, 2018, CARDIOL RES PRACT, V2018, DOI 10.1155/2018/3048941
   Hayakawa H, 2007, J BIOL CHEM, V282, P26369, DOI 10.1074/jbc.M704916200
   He B, 2017, CELL MOL BIOL, V63, P73, DOI 10.14715/cmb/2017.63.3.14
   Ho JE, 2013, J CLIN INVEST, V123, P4208, DOI 10.1172/JCI67119
   Iwahana H, 1999, EUR J BIOCHEM, V264, P397, DOI 10.1046/j.1432-1327.1999.00615.x
   Jamil MO, 2015, INT J HEMATOL, V101, P452, DOI 10.1007/s12185-015-1785-1
   Kamekura R, 2012, CLIN EXP ALLERGY, V42, P218, DOI 10.1111/j.1365-2222.2011.03867.x
   Kurowska-Stolarska M, 2009, J IMMUNOL, V183, P6469, DOI 10.4049/jimmunol.0901575
   Lefrançais E, 2012, P NATL ACAD SCI USA, V109, P1673, DOI 10.1073/pnas.1115884109
   Lei Y, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0133774
   Lingel A, 2009, STRUCTURE, V17, P1398, DOI 10.1016/j.str.2009.08.009
   Löhning M, 1998, P NATL ACAD SCI USA, V95, P6930, DOI 10.1073/pnas.95.12.6930
   Lüthi AU, 2009, IMMUNITY, V31, P84, DOI 10.1016/j.immuni.2009.05.007
   Lupón J, 2018, EUR J HEART FAIL, V20, P938, DOI 10.1002/ejhf.949
   Ma X, 2018, CLIN CHIM ACTA, V480, P138, DOI 10.1016/j.cca.2018.02.005
   Maneechotesuwan K, 2007, J IMMUNOL, V178, P2491, DOI 10.4049/jimmunol.178.4.2491
   Martínez-Martínez E, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0079176
   Martinez-Rumayor A, 2008, AM J CLIN PATHOL, V130, P578, DOI 10.1309/WMG2BFRC97MKKQKP
   Marzullo A, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0156315
   Mildner M, 2010, CARDIOVASC RES, V87, P769, DOI 10.1093/cvr/cvq104
   Miller AM, 2008, J EXP MED, V205, P339, DOI 10.1084/jem.20071868
   Mitchell PD, 2018, INT ARCH ALLERGY IMM, V176, P133, DOI 10.1159/000488015
   Mueller Thomas, 2016, EJIFCC, V27, P224
   Mueller T, 2015, AM J CARDIOL, V115, p8B, DOI 10.1016/j.amjcard.2015.01.035
   Ni YM, 2015, INT J MOL SCI, V16, P27956, DOI 10.3390/ijms161126063
   O'Donnell C, 2016, BRIT J CANCER, V114, P37, DOI 10.1038/bjc.2015.433
   O'Meara E, 2018, CIRC-HEART FAIL, V11, DOI 10.1161/CIRCHEARTFAILURE.117.004446
   O'Neill LAJ, 2008, IMMUNOL REV, V226, P10, DOI 10.1111/j.1600-065X.2008.00701.x
   Ohto-Ozaki H, 2010, EUR J IMMUNOL, V40, P2632, DOI 10.1002/eji.200940291
   Oshikawa K, 2002, CLIN EXP ALLERGY, V32, P1520, DOI 10.1046/j.1365-2745.2002.01494.x
   Oshikawa K, 2001, AM J RESP CRIT CARE, V164, P277, DOI 10.1164/ajrccm.164.2.2008120
   Oshikawa K, 2001, RESP MED, V95, P532, DOI 10.1053/rmed.2001.1080
   Palmer G, 2008, CYTOKINE, V42, P358, DOI 10.1016/j.cyto.2008.03.008
   Pascual-Figal DA, 2018, CIRC-HEART FAIL, V11, DOI 10.1161/CIRCHEARTFAILURE.118.005488
   Pascual-Figal DA, 2015, AM J CARDIOL, V115, p3B, DOI 10.1016/j.amjcard.2015.01.034
   Pascual-Figal DA, 2011, ANN THORAC SURG, V92, P2118, DOI 10.1016/j.athoracsur.2011.07.048
   Pérez-Martínez MT, 2018, J AM COLL CARDIOL, V72, P1429, DOI 10.1016/j.jacc.2018.06.062
   Ponikowski P, 2016, EUR HEART J, V37, P2129, DOI 10.1093/eurheartj/ehw128
   Ramadan AM, 2018, JCI INSIGHT, V3, DOI 10.1172/jci.insight.99208
   Reichenbach DK, 2015, BLOOD, V125, P3183, DOI 10.1182/blood-2014-10-606830
   ROSSLER U, 1995, DEV BIOL, V168, P86, DOI 10.1006/dbio.1995.1063
   Roussel L, 2008, EMBO REP, V9, P1006, DOI 10.1038/embor.2008.145
   Ruiz-Castilla M, 2019, SHOCK, V51, P194, DOI 10.1097/SHK.0000000000001155
   Sanada S, 2007, J CLIN INVEST, V117, P1538, DOI 10.1172/JCI30634
   Schiering C, 2014, NATURE, V513, P564, DOI 10.1038/nature13577
   Schmitz J, 2005, IMMUNITY, V23, P479, DOI 10.1016/j.immuni.2005.09.015
   Seki K, 2009, CIRC-HEART FAIL, V2, P684, DOI 10.1161/CIRCHEARTFAILURE.109.873240
   Shao DM, 2014, BIOCHEM BIOPH RES CO, V451, P8, DOI 10.1016/j.bbrc.2014.06.111
   Tago K, 2001, BIOCHEM BIOPH RES CO, V285, P1377, DOI 10.1006/bbrc.2001.5306
   Tomaniga S., 1999, BIOCHEM BIOPH RES CO, V264, P14
   TOMINAGA S, 1992, BIOCHIM BIOPHYS ACTA, V1171, P215, DOI 10.1016/0167-4781(92)90125-J
   TOMINAGA S, 1989, FEBS LETT, V258, P301, DOI 10.1016/0014-5793(89)81679-5
   Tominaga S, 1996, HUM GENET, V97, P561
   Traister RS, 2015, J ALLERGY CLIN IMMUN, V135, P92, DOI 10.1016/j.jaci.2014.06.023
   Tseng CCS, 2018, J CARDIOVASC TRANSL, V11, P15, DOI 10.1007/s12265-017-9775-8
   Vander Lugt MT, 2013, NEW ENGL J MED, V369, P529, DOI 10.1056/NEJMoa1213299
   Veeraveedu PT, 2017, BIOCHEM PHARMACOL, V138, P73, DOI 10.1016/j.bcp.2017.04.022
   Vocca L, 2015, IMMUNOBIOLOGY, V220, P954, DOI 10.1016/j.imbio.2015.02.005
   Wasserman A, 2012, ISR MED ASSOC J, V14, P620
   Weinberg EO, 2002, CIRCULATION, V106, P2961, DOI 10.1161/01.CIR.0000038705.69871.D9
   Xu D, 1998, J EXP MED, V187, P787, DOI 10.1084/jem.187.5.787
   Yamamoto K, 1998, J BIOL CHEM, V273, P11862, DOI 10.1074/jbc.273.19.11862
   Yancy CW, 2017, CIRCULATION, V136, pE137, DOI [10.1161/CIR.0000000000000509, 10.1016/j.cardfail.2017.04.014]
   Zhang JL, 2015, SCI TRANSL MED, V7, DOI 10.1126/scitranslmed.aab0166
   Zile MR, 2016, CIRC-HEART FAIL, V9, DOI 10.1161/CIRCHEARTFAILURE.115.002551
   Zou SC, 2018, EUR REV MED PHARMACO, V22, P1758, DOI 10.26355/eurrev_201803_14593
NR 94
TC 49
Z9 59
U1 4
U2 21
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
SN 0009-8981
EI 1873-3492
J9 CLIN CHIM ACTA
JI Clin. Chim. Acta
PD AUG
PY 2019
VL 495
BP 493
EP 500
DI 10.1016/j.cca.2019.05.023
PG 8
WC Medical Laboratory Technology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Medical Laboratory Technology
GA IL0CR
UT WOS:000476964200074
PM 31136737
DA 2025-04-10
ER

PT J
AU Snyders, DJ
AF Snyders, DJ
TI Structure and function of cardiac potassium channels
SO CARDIOVASCULAR RESEARCH
LA English
DT Review
ID TRANSIENT OUTWARD CURRENT; RECTIFIER K+ CURRENT; HUMAN ATRIAL MYOCYTES;
   HUMAN VENTRICULAR MYOCYTES; HUMAN INWARD RECTIFIER; DELAYED RECTIFIER;
   BETA-SUBUNIT; HEART-FAILURE; RAT VENTRICLE; MOLECULAR-CLONING
AB Recent advances in molecular biology have had a major impact on our understanding of the biophysical and molecular properties of ion channels. This review is focused on cardiac potassium channels which, in general, serve to control and limit cardiac excitability. Approximately 60 K+ channel subunits have been cloned to date. The (evolutionary) oldest potassium channel subunits consist of two transmembrane (Tm) segments with an intervening pore-loop (P). Channels formed by four 2Tm-IP subunits generally function as inwardly rectifying K+-selective channels (KirX.Y): they conduct: substantial current near the resting potential but carry little or no current at depolarized potentials. The inward rectifier I-K1 and the ligand-gated K-ATP and K-ACh channels are composed of such subunits. The second major class of K+ channel subunits consists of six transmembrane segments (S1-S6). The S5-P-S6 section resembles the 2Tm-1P subunit, and the additional membrane-spanning segments (especially the charged S4 segment) endow these 6Tm-1P channels with voltage-dependent gating. For both major families, four subunits assemble into a homo- or heterotetrameric channel, subject to specific subunit-subunit interactions. The 6Tm-1P channels are closed at the resting potential, but activate at different rates upon depolarization to carry sustained or transient outward currents (the latter due to inactivation by different mechanisms). Cardiac cells typically display at least one transient outward current and several delayed rectifiers to control the duration of the action potential. The molecular basis for each of these currents is formed by subunits that belong to different Kvx.y subfamilies and alternative splicing can contribute further to the diversity in native cells. These subunits display distinct pharmacological properties and drug-binding sites have been identified. Additional subunits have evolved by concatenation of two 2Tm-1P subunits (4Tm-2P); dimers of such subunits yield voltage-independent leak channels. A special class of 6Tm-1P subunits encodes the 'funny' pacemaker current which activates upon hyperpolarization and carries both Na+ and K+ ions. The regional heterogeneity of K+ currents and action potential duration is explained by the heterogeneity of subunit expression, and significant changes in expression occur in cardiac disease, most frequently a reduction. This electrical remodelling may also be important for novel antiarrhythmic therapeutic strategies. The recent crystallization of a 2Tm-IP channel enhances the outlook for more refined molecular approaches. (C) 1999 Elsevier Science B.V. All rights reserved.
C1 Univ Instelling Antwerp VIB, Dept Biochem, Dept Mol Biophys Physiol & Pharmacol, B-2610 Antwerp, Belgium.
C3 University of Antwerp; Flanders Institute for Biotechnology (VIB)
RP Snyders, DJ (corresponding author), Univ Instelling Antwerp VIB, Dept Biochem, Dept Mol Biophys Physiol & Pharmacol, Univ Plein 1,T4-21, B-2610 Antwerp, Belgium.
EM dsnyders@uia.ua.ac.be
RI Snyders, Dirk/A-2713-2013
OI Snyders, Dirk/0000-0001-7142-6672
FU NHLBI NIH HHS [HL59689] Funding Source: Medline
CR Accili EA, 1997, J BIOL CHEM, V272, P25824, DOI 10.1074/jbc.272.41.25824
   AGUILARBRYAN L, 1995, SCIENCE, V268, P423, DOI 10.1126/science.7716547
   ATTALI B, 1993, NATURE, V365, P850, DOI 10.1038/365850a0
   BACKX PH, 1993, CIRC RES, V72, P890, DOI 10.1161/01.RES.72.4.890
   BALSER JR, 1990, J GEN PHYSIOL, V96, P835, DOI 10.1085/jgp.96.4.835
   Barhanin J, 1996, NATURE, V384, P78, DOI 10.1038/384078a0
   BARRY DM, 1995, CIRC RES, V77, P361, DOI 10.1161/01.RES.77.2.361
   Barry DM, 1996, ANNU REV PHYSIOL, V58, P363, DOI 10.1146/annurev.ph.58.030196.002051
   BEUCKELMANN DJ, 1993, CIRC RES, V73, P379, DOI 10.1161/01.RES.73.2.379
   Bezanilla F, 1998, METHOD ENZYMOL, V293, P331
   CARMELIET E, 1992, J PHARMACOL EXP THER, V262, P809
   Cha A, 1997, NEURON, V19, P1127, DOI 10.1016/S0896-6273(00)80403-1
   CHOI KL, 1993, NEURON, V10, P533, DOI 10.1016/0896-6273(93)90340-W
   Clapham DE, 1997, ANNU REV PHARMACOL, V37, P167, DOI 10.1146/annurev.pharmtox.37.1.167
   CLARK RB, 1993, CARDIOVASC RES, V27, P1795, DOI 10.1093/cvr/27.10.1795
   Corey S, 1998, J BIOL CHEM, V273, P5271, DOI 10.1074/jbc.273.9.5271
   CURRAN ME, 1995, CELL, V80, P795, DOI 10.1016/0092-8674(95)90358-5
   Daram P, 1997, EMBO J, V16, P3455, DOI 10.1093/emboj/16.12.3455
   Deal KK, 1996, PHYSIOL REV, V76, P49, DOI 10.1152/physrev.1996.76.1.49
   Demolombe S, 1998, J BIOL CHEM, V273, P6837, DOI 10.1074/jbc.273.12.6837
   DIFRANCESCO D, 1993, ANNU REV PHYSIOL, V55, P455, DOI 10.1146/annurev.physiol.55.1.455
   Dixon JE, 1996, CIRC RES, V79, P659, DOI 10.1161/01.RES.79.4.659
   DIXON JE, 1994, CIRC RES, V75, P252, DOI 10.1161/01.RES.75.2.252
   Doupnik CA, 1997, P NATL ACAD SCI USA, V94, P10461, DOI 10.1073/pnas.94.19.10461
   Doyle DA, 1998, SCIENCE, V280, P69, DOI 10.1126/science.280.5360.69
   Duprat F, 1997, EMBO J, V16, P5464, DOI 10.1093/emboj/16.17.5464
   ENGLAND SK, 1995, J BIOL CHEM, V270, P28531, DOI 10.1074/jbc.270.48.28531
   ENGLAND SK, 1995, P NATL ACAD SCI USA, V92, P6309, DOI 10.1073/pnas.92.14.6309
   Feng JL, 1997, CIRC RES, V80, P572, DOI 10.1161/01.RES.80.4.572
   Fink M, 1996, J BIOL CHEM, V271, P26341, DOI 10.1074/jbc.271.42.26341
   Fiset C, 1997, J PHYSIOL-LONDON, V500, P51, DOI 10.1113/jphysiol.1997.sp021998
   Franqueza L, 1997, CIRC RES, V81, P1053
   Franqueza L, 1999, CARDIOVASC RES, V41, P212, DOI 10.1016/S0008-6363(98)00220-X
   Gauss R, 1998, NATURE, V393, P583, DOI 10.1038/31248
   GOLDSTEIN SAN, 1991, NEURON, V7, P403, DOI 10.1016/0896-6273(91)90292-8
   Hille B., 1991, IONIC CHANNELS EXCIT
   Holmes TC, 1996, SCIENCE, V274, P2089, DOI 10.1126/science.274.5295.2089
   HOSHI T, 1990, SCIENCE, V250, P533, DOI 10.1126/science.2122519
   HOSHI T, 1991, NEURON, V7, P547, DOI 10.1016/0896-6273(91)90367-9
   INAGAKI N, 1995, SCIENCE, V270, P1166, DOI 10.1126/science.270.5239.1166
   Jan LY, 1997, J PHYSIOL-LONDON, V505, P267, DOI 10.1111/j.1469-7793.1997.267bb.x
   Jegla T, 1997, J NEUROSCI, V17, P32, DOI 10.1523/JNEUROSCI.17-01-00032.1997
   Ji S, 1998, J BIOL CHEM, V273, P1324, DOI 10.1074/jbc.273.3.1324
   Johns DC, 1997, J BIOL CHEM, V272, P31598, DOI 10.1074/jbc.272.50.31598
   Kaab S, 1996, CIRC RES, V78, P262, DOI 10.1161/01.RES.78.2.262
   KASS RS, 1993, TRENDS CARDIOVAS MED, V3, P149, DOI 10.1016/1050-1738(93)90016-Y
   Keating MT, 1996, CURR OPIN GENET DEV, V6, P326, DOI 10.1016/S0959-437X(96)80010-4
   KETCHUM KA, 1995, NATURE, V376, P690, DOI 10.1038/376690a0
   Kiehn J, 1996, MOL PHARMACOL, V50, P380
   Kim E, 1996, NEUROPHARMACOLOGY, V35, P993, DOI 10.1016/0028-3908(96)00093-7
   KRAPIVINSKY G, 1995, NATURE, V374, P135, DOI 10.1038/374135a0
   Kupershmidt S, 1999, CIRC RES, V84, P146, DOI 10.1161/01.RES.84.2.146
   Kupershmidt S, 1998, J BIOL CHEM, V273, P27231, DOI 10.1074/jbc.273.42.27231
   LeesMiller JP, 1997, CIRC RES, V81, P719
   Lesage F, 1996, EMBO J, V15, P1004, DOI 10.1002/j.1460-2075.1996.tb00437.x
   LI M, 1992, SCIENCE, V257, P1225, DOI 10.1126/science.1519059
   Liu Y, 1996, NEURON, V16, P859, DOI 10.1016/S0896-6273(00)80106-3
   London B, 1997, CIRC RES, V81, P870
   LOPATIN AN, 1994, NATURE, V372, P366, DOI 10.1038/372366a0
   Ludwig A, 1998, NATURE, V393, P587, DOI 10.1038/31255
   Ludwig J, 1997, EMBO J, V16, P6337, DOI 10.1093/emboj/16.21.6337
   MACKINNON R, 1995, NEURON, V14, P889, DOI 10.1016/0896-6273(95)90327-5
   MAJUMDER K, 1995, FEBS LETT, V361, P13, DOI 10.1016/0014-5793(95)00120-X
   Mannuzzu LM, 1996, SCIENCE, V271, P213, DOI 10.1126/science.271.5246.213
   MAYS DJ, 1995, J CLIN INVEST, V96, P282, DOI 10.1172/JCI118032
   McDonald TV, 1997, NATURE, V388, P289, DOI 10.1038/40882
   MORALES MJ, 1995, J BIOL CHEM, V270, P6272, DOI 10.1074/jbc.270.11.6272
   Nabauer M, 1998, CARDIOVASC RES, V37, P324, DOI 10.1016/S0008-6363(97)00274-5
   Nabauer M, 1996, CIRCULATION, V93, P168, DOI 10.1161/01.CIR.93.1.168
   Nakamura TY, 1997, AM J PHYSIOL-HEART C, V273, pH1775, DOI 10.1152/ajpheart.1997.273.4.H1775
   Nuss HB, 1996, GENE THER, V3, P900
   Ohya S, 1997, FEBS LETT, V420, P47, DOI 10.1016/S0014-5793(97)01483-X
   Papazian DM, 1997, NEWS PHYSIOL SCI, V12, P203
   RETTIG J, 1994, NATURE, V369, P289, DOI 10.1038/369289a0
   Salata JJ, 1998, MOL PHARMACOL, V54, P220, DOI 10.1124/mol.54.1.220
   Salinas M, 1997, J BIOL CHEM, V272, P24371, DOI 10.1074/jbc.272.39.24371
   SANGUINETTI MC, 1995, CELL, V81, P299, DOI 10.1016/0092-8674(95)90340-2
   Sanguinetti MC, 1996, NATURE, V384, P80, DOI 10.1038/384080a0
   SANGUINETTI MC, 1990, J GEN PHYSIOL, V96, P195, DOI 10.1085/jgp.96.1.195
   Santoro B, 1998, CELL, V93, P717, DOI 10.1016/S0092-8674(00)81434-8
   SERODIO P, 1994, J NEUROPHYSIOL, V72, P1516, DOI 10.1152/jn.1994.72.4.1516
   Serodio P, 1996, J NEUROPHYSIOL, V75, P2174, DOI 10.1152/jn.1996.75.5.2174
   Shi WM, 1997, J NEUROSCI, V17, P9423
   SHIBASAKI T, 1987, J PHYSIOL-LONDON, V387, P227, DOI 10.1113/jphysiol.1987.sp016571
   Shimoni Y, 1997, J PHYSIOL-LONDON, V500, P65, DOI 10.1113/jphysiol.1997.sp021999
   SLAWSKY MT, 1994, J PHARMACOL EXP THER, V269, P66
   Smith PL, 1996, NATURE, V379, P833, DOI 10.1038/379833a0
   SNYDERS DJ, 1992, MOL PHARMACOL, V41, P322
   SNYDERS DJ, 1993, J GEN PHYSIOL, V101, P513, DOI 10.1085/jgp.101.4.513
   Snyders DJ, 1996, MOL PHARMACOL, V49, P949
   Spector PS, 1996, CIRC RES, V78, P499, DOI 10.1161/01.RES.78.3.499
   Spector PS, 1996, J GEN PHYSIOL, V107, P611, DOI 10.1085/jgp.107.5.611
   STANFIELD PR, 1994, J PHYSIOL-LONDON, V475, P1
   TAKIMOTO K, 1994, CIRC RES, V75, P1006, DOI 10.1161/01.RES.75.6.1006
   Takimoto K, 1997, CIRC RES, V81, P533, DOI 10.1161/01.RES.81.4.533
   TAMKUN MM, 1991, FASEB J, V5, P331, DOI 10.1096/fasebj.5.3.2001794
   TOMASELLI GF, 1994, CIRCULATION, V90, P2534, DOI 10.1161/01.CIR.90.5.2534
   TRUDEAU MC, 1995, SCIENCE, V269, P92, DOI 10.1126/science.7604285
   Uebele VN, 1996, J BIOL CHEM, V271, P2406, DOI 10.1074/jbc.271.5.2406
   Uebele VN, 1998, AM J PHYSIOL-CELL PH, V274, pC1485, DOI 10.1152/ajpcell.1998.274.6.C1485
   VanWagoner DR, 1997, CIRC RES, V80, P772
   VARNUM MD, 1993, P NATL ACAD SCI USA, V90, P11528, DOI 10.1073/pnas.90.24.11528
   Vetter DE, 1996, NEURON, V17, P1251, DOI 10.1016/S0896-6273(00)80255-X
   Wallner M, 1995, RECEPTOR CHANNEL, V3, P185
   Wang SM, 1996, FEBS LETT, V389, P167, DOI 10.1016/0014-5793(96)00570-4
   WANG ZG, 1995, J PHARMACOL EXP THER, V272, P184
   WANG ZG, 1993, CIRC RES, V73, P1061, DOI 10.1161/01.RES.73.6.1061
   WETTWER E, 1994, CIRC RES, V75, P473, DOI 10.1161/01.RES.75.3.473
   Wible BA, 1998, J BIOL CHEM, V273, P11745, DOI 10.1074/jbc.273.19.11745
   Wickenden AD, 1997, J PHYSIOL-LONDON, V504, P271, DOI 10.1111/j.1469-7793.1997.271be.x
   Wickman K, 1998, NEURON, V20, P103, DOI 10.1016/S0896-6273(00)80438-9
   Yeola SW, 1996, CIRC RES, V78, P1105, DOI 10.1161/01.RES.78.6.1105
   Yeola SW, 1997, CARDIOVASC RES, V33, P540, DOI 10.1016/S0008-6363(96)00221-0
   YUE DT, 1988, PFLUG ARCH EUR J PHY, V413, P127, DOI 10.1007/BF00582522
NR 114
TC 152
Z9 178
U1 0
U2 18
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 0008-6363
J9 CARDIOVASC RES
JI Cardiovasc. Res.
PD MAY
PY 1999
VL 42
IS 2
BP 377
EP 390
DI 10.1016/S0008-6363(99)00071-1
PG 14
WC Cardiac & Cardiovascular Systems
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology
GA 200ZV
UT WOS:000080570900011
PM 10533574
OA Bronze
DA 2025-04-10
ER

PT J
AU Unruh, D
   Turner, K
   Srinivasan, R
   Kocatürk, B
   Qi, XY
   Chu, ZT
   Aronow, BJ
   Plas, DR
   Gallo, CA
   Kalthoff, H
   Kirchhofer, D
   Ruf, W
   Ahmad, SA
   Lucas, FV
   Versteeg, HH
   Bogdanov, VY
AF Unruh, Dusten
   Turner, Kevin
   Srinivasan, Ramprasad
   Kocaturk, Begum
   Qi, Xiaoyang
   Chu, Zhengtao
   Aronow, Bruce J.
   Plas, David R.
   Gallo, Catherine A.
   Kalthoff, Holger
   Kirchhofer, Daniel
   Ruf, Wolfram
   Ahmad, Syed A.
   Lucas, Fred V.
   Versteeg, Henri H.
   Bogdanov, Vladimir Y.
TI Alternatively spliced tissue factor contributes to tumor spread and
   activation of coagulation in pancreatic ductal adenocarcinoma
SO INTERNATIONAL JOURNAL OF CANCER
LA English
DT Article
DE pancreatic ductal adenocarcinoma; metastasis; molecular mechanisms of
   angiogenesis; tissue factor; alternative splicing
ID FACTOR EXPRESSION; CANCER-CELLS; GROWTH; ANGIOGENESIS; PROGRESSION;
   MICROPARTICLES; THROMBOSIS; RECEPTOR; MODEL
AB Alternatively spliced tissue factor (asTF) promotes neovascularization and monocyte recruitment via integrin ligation. While asTF mRNA has been detected in some pancreatic ductal adenocarcinoma (PDAC) cell lines and increased asTF expression can promote PDAC growth in a subcutaneous model, the expression of asTF protein in bona fide PDAC lesions and/or its role in metastatic spread are yet to be ascertained. We here report that asTF protein is abundant in lesional and stromal compartments of the five studied types of carcinoma including PDAC. Analysis of 29 specimens of PDAC revealed detectable asTF in >90% of the lesions with a range of staining intensities. asTF levels in PDAC lesions positively correlated with the degree of monocyte infiltration. In an orthotopic model, asTF-overexpressing high-grade PDAC cell line Pt45P1/asTF+ produced metastases to distal lymph nodes, which stained positive for asTF. PDAC cells stimulated with and/or overexpressing asTF exhibited upregulation of genes implicated in PDAC progression and metastatic spread. Pt45P1/asTF+ cells displayed higher coagulant activity compared to Pt45P1 cells; the same effect was observed for cell-derived microparticles (MPs). Our findings demonstrate that asTF is expressed in PDAC and lymph node metastases and potentiates PDAC spread in vivo. asTF elicits global changes in gene expression likely involved in tumor progression and metastatic dissemination, and it also enhances the procoagulant potential of PDAC cells and cell-derived MPs. Thus, asTF may comprise a novel therapeutic target to treat PDAC and, possibly, its thrombotic complications.
   What's new? Alternatively spliced tissue factor (asTF) triggers the growth of new blood vessels and is present at elevated levels in certain cancers, indicating that it could play an important role in tumor growth and metastasis. Here, asTF was found to be abundant in human pancreatic ductal adenocarcinoma (PDAC) lesions and stromal monocytes, and its overexpression potentiated PDAC metastasis in vivo. Furthermore, asTF augmented EGFR-linked signaling pathways in PDAC cells and contributed to the coagulant activity of PDAC cells and cell-derived microparticles. The findings suggest that asTF may be a key target for stemming metastatic spread and complications in PDAC.
C1 [Unruh, Dusten; Srinivasan, Ramprasad; Qi, Xiaoyang; Chu, Zhengtao; Bogdanov, Vladimir Y.] Univ Cincinnati, Coll Med, Div Hematol Oncol, Cincinnati, OH 45267 USA.
   [Turner, Kevin; Lucas, Fred V.] Univ Cincinnati, Coll Med, Dept Pathol & Lab Med, Cincinnati, OH 45267 USA.
   [Kocaturk, Begum; Versteeg, Henri H.] Leiden Univ, Med Ctr, Einthoven Lab Expt Vasc Med, Leiden, Netherlands.
   [Aronow, Bruce J.] Cincinnati Childrens Hosp & Med Ctr, Dept Biomed Informat & Dev Biol, Cincinnati, OH USA.
   [Plas, David R.; Gallo, Catherine A.] Univ Cincinnati, Coll Med, Dept Canc Biol, Cincinnati, OH 45267 USA.
   [Kalthoff, Holger] Univ Hosp Schleswig Holstein, Inst Expt Canc Res, Kiel, Germany.
   [Kirchhofer, Daniel] Genentech Inc, Dept Early Discovery Biochem, San Francisco, CA 94080 USA.
   [Ruf, Wolfram] Scripps Res Inst, Dept Immunol & Microbial Sci, La Jolla, CA 92037 USA.
   Univ Cincinnati, Coll Med, Dept Surg, Cincinnati, OH 45267 USA.
C3 University System of Ohio; University of Cincinnati; University System
   of Ohio; University of Cincinnati; Leiden University; Leiden University
   Medical Center (LUMC); Leiden University - Excl LUMC; Cincinnati
   Children's Hospital Medical Center; University System of Ohio;
   University of Cincinnati; University of Kiel; Schleswig Holstein
   University Hospital; Roche Holding; Roche Holding USA; Genentech;
   Scripps Research Institute; University System of Ohio; University of
   Cincinnati
RP Bogdanov, VY (corresponding author), Univ Cincinnati, Coll Med, Div Hematol Oncol, 3125 Eden Ave, Cincinnati, OH 45267 USA.
EM vladimir.bogdanov@uc.edu
RI Kalthoff, Holger/B-1618-2010; Aronow, Bruce/F-8438-2012; Versteeg,
   Henri/G-1783-2018
OI Turner, Kevin/0000-0001-6954-1153; Qi, Xiaoyang/0000-0001-5363-1760;
   Unruh, Dusten/0000-0003-1027-1982; Ruf, Wolfram/0000-0002-6064-2166;
   Kocaturk, Begum/0000-0003-3657-6055; Bogdanov,
   Vladimir/0000-0003-4968-1129; Versteeg, Henri/0000-0003-4294-175X
FU NIH/NCI [1R21CA160293-01A1]
FX Grant sponsor: NIH/NCI; Grant number: 1R21CA160293-01A1
CR Balanis N, 2011, MOL BIOL CELL, V22, P4288, DOI 10.1091/mbc.E10-08-0700
   Bogdanov VY, 2003, NAT MED, V9, P458, DOI 10.1038/nm841
   Camaj P, 2009, BIOL CHEM, V390, P1293, DOI 10.1515/BC.2009.140
   Ettelaie C, 2013, THROMB HAEMOSTASIS, V109, P61, DOI 10.1160/TH12-05-0279
   Garnier D, 2012, J BIOL CHEM, V287, P43565, DOI 10.1074/jbc.M112.401760
   Goldin-Lang P, 2008, ONCOL REP, V20, P123
   Haas SL, 2006, WORLD J GASTROENTERO, V12, P4843
   Hobbs JE, 2007, THROMB RES, V120, pS13, DOI 10.1016/S0049-3848(07)70126-3
   Jemal A, 2008, CA-CANCER J CLIN, V58, P71, DOI 10.3322/CA.2007.0010
   Khorana AA, 2007, CLIN CANCER RES, V13, P2870, DOI 10.1158/1078-0432.CCR-06-2351
   Kirchhofer D, 2000, THROMB HAEMOSTASIS, V84, P1072
   Mizukami Y, 2012, J GASTROEN HEPATOL, V27, P23, DOI 10.1111/j.1440-1746.2011.07012.x
   Morello V, 2011, ONCOGENE, V30, P4087, DOI 10.1038/onc.2011.107
   Olive KP, 2009, SCIENCE, V324, P1457, DOI 10.1126/science.1171362
   Qi XY, 2009, CLIN CANCER RES, V15, P5840, DOI 10.1158/1078-0432.CCR-08-3285
   Rak J, 2006, CANCER RES, V66, P10643, DOI 10.1158/0008-5472.CAN-06-2350
   Rollin J, 2010, J THROMB HAEMOST, V8, P607, DOI 10.1111/j.1538-7836.2009.03713.x
   Sawai H, 2006, BMC CELL BIOL, V7, DOI 10.1186/1471-2121-7-8
   Schoppmann SF, 2002, AM J PATHOL, V161, P947, DOI 10.1016/S0002-9440(10)64255-1
   Seeliger H, 2009, MOL CANCER RES, V7, P189, DOI 10.1158/1541-7786.MCR-08-0132
   Sipos B, 2003, VIRCHOWS ARCH, V442, P444, DOI 10.1007/s00428-003-0784-4
   Srinivasan R, 2011, J THROMB HAEMOST, V9, P2087, DOI 10.1111/j.1538-7836.2011.04454.x
   Tardos JG, 2008, J THROMB HAEMOST, V6, P877, DOI 10.1111/j.1538-7836.2008.02946.x
   Tesselaar MET, 2007, J THROMB HAEMOST, V5, P520, DOI 10.1111/j.1538-7836.2007.02369.x
   Thaler J, 2012, J THROMB HAEMOST, V10, P1363, DOI 10.1111/j.1538-7836.2012.04754.x
   Thomas GM, 2009, J EXP MED, V206, P1913, DOI 10.1084/jem.20082297
   van den Berg YW, 2009, P NATL ACAD SCI USA, V106, P19497, DOI 10.1073/pnas.0905325106
   van den Berg YW, 2012, BLOOD, V119, P924, DOI 10.1182/blood-2011-06-317685
   Wang JG, 2012, BLOOD, V119, P5543, DOI 10.1182/blood-2012-01-402156
   Yotsumoto F, 2010, CANCER SCI, V101, P2351, DOI 10.1111/j.1349-7006.2010.01671.x
   Yu JL, 2005, BLOOD, V105, P1734, DOI 10.1182/blood-2004-05-2042
   Zwicker JI, 2009, CLIN CANCER RES, V15, P6830, DOI 10.1158/1078-0432.CCR-09-0371
NR 32
TC 41
Z9 47
U1 0
U2 29
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0020-7136
EI 1097-0215
J9 INT J CANCER
JI Int. J. Cancer
PD JAN 1
PY 2014
VL 134
IS 1
BP 9
EP 20
DI 10.1002/ijc.28327
PG 12
WC Oncology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Oncology
GA 238WI
UT WOS:000325982000002
PM 23754313
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Hong, CS
   Kwon, SJ
   Kim, DH
AF Hong, Chang-Soo
   Kwon, Soon-Jae
   Kim, Do Han
TI Multiple functions of junctin and junctate, two distinct isoforms of
   aspartyl beta-hydroxylase
SO BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
LA English
DT Review
DE Ryanodine receptor; calsequestrin; triadin; striated muscle;
   excitation-con traction coupling; calcium signaling
ID MICE OVEREXPRESSING JUNCTIN; CALCIUM-BINDING PROTEIN; J-J LOCUS;
   SARCOPLASMIC-RETICULUM; TRANSGENIC MICE; CARDIAC CALSEQUESTRIN; IMPAIRED
   RELAXATION; RYANODINE RECEPTOR; MOLECULAR-CLONING; CDNA CLONING
AB The single genomic locus, A beta H-J-J, encodes three functionally distinct proteins aspartyl beta-hydroxylase, junctin and junctate by alternative splicing. Among these three proteins, junctin and junctate could play important roles in the regulation of intracellular Ca2+ by regulating either Ca2+ release from intracellular Ca2+ stores or Ca2+ influx in various biological processes. Here we review recent findings concerning the expressional regulations and the proposed functions of junctin and junctate. (c) 2007 Elsevier Inc. All rights reserved.
C1 Gwangju Inst Sci & Technol, Dept Life Sci, Kwangju 500712, South Korea.
   Univ Penn, Sch Vet Med, Dept Anim Biol, Philadelphia, PA 19104 USA.
C3 Gwangju Institute of Science & Technology (GIST); University of
   Pennsylvania
RP Kim, DH (corresponding author), Gwangju Inst Sci & Technol, Dept Life Sci, 1 Oryong-dong, Kwangju 500712, South Korea.
EM dhkim@gist.ac.kr
CR Dinchuk JE, 2000, J BIOL CHEM, V275, P39543, DOI 10.1074/jbc.M006753200
   DIVET A, IN PRESS J CELL PHYS
   Fan GC, 2007, BIOCHEM BIOPH RES CO, V352, P617, DOI 10.1016/j.bbrc.2006.11.093
   Feriotto G, 2005, MOL CELL BIOL, V25, P3261, DOI 10.1128/MCB.25.8.3261-3275.2005
   Feriotto G, 2006, ANN NY ACAD SCI, V1091, P184, DOI 10.1196/annals.1378.065
   GERGS U, 2007, AM J PHYSL HEART CIR
   Gregory KN, 2006, J MOL CELL CARDIOL, V40, P653, DOI 10.1016/j.yjmcc.2006.02.003
   Györke I, 2004, BIOPHYS J, V86, P2121, DOI 10.1016/S0006-3495(04)74271-X
   Hong CS, 2002, FASEB J, V16, P1310, DOI 10.1096/fj.01-0908fje
   Hong CS, 2001, BIOCHEM BIOPH RES CO, V289, P882, DOI 10.1006/bbrc.2001.6056
   Jaehnig EJ, 2006, MOL CELL BIOL, V26, P9315, DOI 10.1128/MCB.00482-06
   JIA S, 1992, J BIOL CHEM, V267, P14322
   Jones LR, 1998, J CLIN INVEST, V101, P1385, DOI 10.1172/JCI1362
   Jones LR, 1995, J BIOL CHEM, V270, P30787, DOI 10.1074/jbc.270.51.30787
   Kirchhefer U, 2006, CELL CALCIUM, V39, P131, DOI 10.1016/j.ceca.2005.10.004
   Kirchhefer U, 2004, AM J PHYSIOL-HEART C, V287, pH2216, DOI 10.1152/ajpheart.00137.2004
   Kirchhefer U, 2004, CARDIOVASC RES, V62, P122, DOI 10.1016/j.cardiores.2004.01.005
   Kirchhefer U, 2003, CARDIOVASC RES, V59, P369, DOI 10.1016/S0008-6363(03)00432-2
   Kirchhefer U, 2001, J BIOL CHEM, V276, P4142, DOI 10.1074/jbc.M006443200
   Knollmann BC, 2006, J CLIN INVEST, V116, P2510, DOI 10.1172/JCI29128
   KORIOTH F, 1994, GENE, V150, P395, DOI 10.1016/0378-1119(94)90460-X
   Lim KY, 2000, GENE, V255, P35, DOI 10.1016/S0378-1119(00)00299-7
   Miller SLW, 2005, CARDIOVASC RES, V67, P667, DOI 10.1016/j.cardiores.2005.04.023
   MITCHELL RD, 1988, J BIOL CHEM, V263, P1376
   Sato Y, 1998, J BIOL CHEM, V273, P28470, DOI 10.1074/jbc.273.43.28470
   Stamboulian S, 2005, DEV BIOL, V286, P326, DOI 10.1016/j.ydbio.2005.08.006
   Terentyev D, 2003, P NATL ACAD SCI USA, V100, P11759, DOI 10.1073/pnas.1932318100
   Treves S, 2004, J CELL BIOL, V166, P537, DOI 10.1083/jcb.200404079
   Treves S, 2000, J BIOL CHEM, V275, P39555, DOI 10.1074/jbc.M005473200
   WANG QP, 1991, J BIOL CHEM, V266, P14004
   Yuan QQ, 2007, CIRCULATION, V115, P300, DOI 10.1161/CIRCULATIONAHA.106.654699
   Zhang L, 1997, J BIOL CHEM, V272, P23389, DOI 10.1074/jbc.272.37.23389
   Zhang L, 2001, J MOL CELL CARDIOL, V33, P233, DOI 10.1006/jmcc.2000.1295
NR 33
TC 20
Z9 24
U1 0
U2 4
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0006-291X
EI 1090-2104
J9 BIOCHEM BIOPH RES CO
JI Biochem. Biophys. Res. Commun.
PD OCT 12
PY 2007
VL 362
IS 1
BP 1
EP 4
DI 10.1016/j.bbrc.2007.07.166
PG 4
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA 208ZK
UT WOS:000249357700001
PM 17706594
DA 2025-04-10
ER

PT J
AU Jossin, Y
   Bar, I
   Ignatova, N
   Tissir, F
   de Rouvroit, CL
   Goffinet, AM
AF Jossin, Y
   Bar, I
   Ignatova, N
   Tissir, F
   de Rouvroit, CL
   Goffinet, AM
TI The Reelin signaling pathway: Some recent developments
SO CEREBRAL CORTEX
LA English
DT Article
ID BRAIN-DEVELOPMENT; TYROSINE PHOSPHORYLATION; NEURONAL MIGRATION; VLDL
   RECEPTOR; MUTANT MICE; DISABLED-1; PROTEINS; BINDING; SITES; FORM
AB The Reelin signaling pathway plays a key role in the architectonic development of the central nervous system. Extracellular Reelin binds to receptors of the lipoprotein receptor family and induces tyrosine phosphorylation of the adaptor Dab1. In this paper, we discuss three recent developments. First, we show that the central part of Reelin is involved in receptor binding and signal activation as reflected in Dab1 phosphorylation. Second, we examine the genomic organization, alternative splicing and promoter use of the NO gene, which hint at a particularly complex regulation. Third, we present preliminary studies by in situ hybridization that demonstrate regulated expression of Reelin receptors and Dab1 by radial precursors in the ventricular zone.
C1 UCL GEDE 7382, Dev Genet Unit, B-1200 Brussels, Belgium.
   Fac Univ Notre Dame Paix, Sch Med, Neurobiol Unit 2853, B-5000 Namur, Belgium.
C3 Universite Catholique Louvain; Cliniques Universitaires Saint-Luc;
   University of Namur
RP Goffinet, AM (corresponding author), UCL GEDE 7382, Dev Genet Unit, 73 Ave E Mounier, B-1200 Brussels, Belgium.
RI bar, isabelle/AAQ-7795-2020
OI BAR, ISABELLE/0000-0002-6091-9137; Jossin, Yves/0000-0001-8466-7432;
   Tissir, Fadel/0000-0002-9292-6622
CR Bernier B, 2000, J COMP NEUROL, V422, P448
   D'Arcangelo G, 1999, NEURON, V24, P471, DOI 10.1016/S0896-6273(00)80860-0
   DARCANGELO G, 1995, NATURE, V374, P719, DOI 10.1038/374719a0
   de Bergeyck V, 1998, J NEUROSCI METH, V82, P17, DOI 10.1016/S0165-0270(98)00024-7
   de Rouvroit CL, 1999, EXP NEUROL, V156, P214, DOI 10.1006/exnr.1998.7007
   Dulabon L, 2000, NEURON, V27, P33, DOI 10.1016/S0896-6273(00)00007-6
   HACK I, 2002, FENS ABSTR, V1, P506
   Herrick TM, 2002, DEVELOPMENT, V129, P787
   Hiesberger T, 1999, NEURON, V24, P481, DOI 10.1016/S0896-6273(00)80861-2
   Hong SE, 2000, NAT GENET, V26, P93, DOI 10.1038/79246
   Howe S, 1999, STAND MAG, V1, P19
   Howell BW, 1999, GENE DEV, V13, P643, DOI 10.1101/gad.13.6.643
   Howell BW, 2000, CURR BIOL, V10, P877, DOI 10.1016/S0960-9822(00)00608-4
   Howell BW, 1997, EMBO J, V16, P121, DOI 10.1093/emboj/16.1.121
   Howell BW, 1997, NATURE, V389, P733, DOI 10.1038/39607
   Keshvara L, 2002, J NEUROSCI, V22, P4869, DOI 10.1523/JNEUROSCI.22-12-04869.2002
   Keshvara L, 2001, J BIOL CHEM, V276, P16008, DOI 10.1074/jbc.M101422200
   Kubo K, 2002, NEUROSCI RES, V43, P381, DOI 10.1016/S0168-0102(02)00068-8
   Lambert de Rouvroit C, 1998, Adv Anat Embryol Cell Biol, V150, P1
   MEYER G, 2002, FENS ABSTR, V1, P506
   Rice DS, 2001, ANNU REV NEUROSCI, V24, P1005, DOI 10.1146/annurev.neuro.24.1.1005
   Senzaki K, 1999, CELL, V99, P635, DOI 10.1016/S0092-8674(00)81552-4
   Trommsdorff M, 1999, CELL, V97, P689, DOI 10.1016/S0092-8674(00)80782-5
   Utsunomiya-Tate N, 2000, P NATL ACAD SCI USA, V97, P9729, DOI 10.1073/pnas.160272497
NR 24
TC 38
Z9 42
U1 0
U2 1
PU OXFORD UNIV PRESS INC
PI CARY
PA JOURNALS DEPT, 2001 EVANS RD, CARY, NC 27513 USA
SN 1047-3211
J9 CEREB CORTEX
JI Cereb. Cortex
PD JUN
PY 2003
VL 13
IS 6
BP 627
EP 633
DI 10.1093/cercor/13.6.627
PG 7
WC Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA 681CL
UT WOS:000183019300013
PM 12764038
DA 2025-04-10
ER

PT J
AU Granatosky, EA
   DiPrimio, N
   Pickering, JRE
   Stevens, DC
   Perlstein, EO
   Taylor, RE
AF Granatosky, Eve A.
   DiPrimio, Nina
   Pickering, Jarred R. E.
   Stevens, D. Cole
   Perlstein, Ethan O.
   Taylor, Richard E.
TI GEX1A, a Polyketide from Streptomyces chromofuscus, Corrects the
   Cellular Defects Associated with Niemann-Pick Type C1 in Human
   Fibroblasts
SO JOURNAL OF NATURAL PRODUCTS
LA English
DT Article
ID DISEASE TYPE-C; HERBOXIDIENE BIOSYNTHESIS; CHOLESTEROL; NPC1;
   IDENTIFICATION; EXPRESSION; PHENOTYPE; PROTEIN; TARGET; CELLS
AB We report the first evidence of GEX1A, a polyketide known to modulate alternative pre-mRNA splicing, as a potential treatment for Niemann-Pick type C disease. GEX1A was isolated from its producing organism, Streptomyces chromofuscus, and screened in NPC1 mutant cells alongside several semisynthetic analogues. We found that GEX1A and analogues are capable of restoring cholesterol trafficking in NPC1 mutant fibroblasts, as well as altering the expression of NPC1 isoforms detected by Western blot. These results, along with the compound's favorable pharmacokinetic properties, highlight the potential of spliceosome-targeting scaffolds such as GEX1A for the treatment of genetic diseases.
C1 [Granatosky, Eve A.; Pickering, Jarred R. E.; Stevens, D. Cole; Taylor, Richard E.] Univ Notre Dame, Dept Chem & Biochem, Notre Dame, IN 46556 USA.
   [DiPrimio, Nina; Perlstein, Ethan O.] Perlara PBC, San Francisco, CA 94080 USA.
   [Stevens, D. Cole] Univ Mississippi, Dept Biomol Sci, University, MS 38677 USA.
C3 University of Notre Dame; University of Mississippi
RP Taylor, RE (corresponding author), Univ Notre Dame, Dept Chem & Biochem, Notre Dame, IN 46556 USA.
EM rtaylor@nd.edu
OI Stevens, David Cole/0000-0001-6668-9419; Taylor,
   Richard/0000-0003-1146-7493; Granatosky, Eve/0000-0002-7533-2646
FU Ara Parseghian Medical Research Foundation;
   Chemistry-Biochemistry-Biology Interface (CBBI) Program at the
   University of Notre Dame from the National Institute of General Medical
   Sciences [T32GM075762]
FX We would like to thank V. Raksakulthai, field application scientist at
   Molecular Devices, who greatly assisted with the development of a
   MetaXpress analysis tool for the quantification of filipin stain per
   cell. This work was supported in part by the Ara Parseghian Medical
   Research Foundation. E.A.G. acknowledges support from the
   Chemistry-Biochemistry-Biology Interface (CBBI) Program at the
   University of Notre Dame, training grant T32GM075762, from the National
   Institute of General Medical Sciences.
CR Banwell M, 2000, PURE APPL CHEM, V72, P1631, DOI 10.1351/pac200072091631
   Fan LY, 2011, ACS CHEM BIOL, V6, P582, DOI 10.1021/cb100356k
   Gelsthorpe ME, 2008, J BIOL CHEM, V283, P8229, DOI 10.1074/jbc.M708735200
   Ghosh AK, 2011, ORG LETT, V13, P66, DOI 10.1021/ol102549a
   Han CC, 2013, CELL SIGNAL, V25, P144, DOI 10.1016/j.cellsig.2012.09.023
   Hasegawa M, 2011, ACS CHEM BIOL, V6, P229, DOI 10.1021/cb100248e
   ISAAC BG, 1992, J ORG CHEM, V57, P7220, DOI 10.1021/jo00052a042
   Kaida D, 2007, NAT CHEM BIOL, V3, P576, DOI 10.1038/nchembio.2007.18
   Kirkegaard T, 2016, SCI TRANSL MED, V8, DOI 10.1126/scitranslmed.aad9823
   Koguchi Y, 1997, J ANTIBIOT, V50, P970, DOI 10.7164/antibiotics.50.970
   Kotake Y, 2007, NAT CHEM BIOL, V3, P570, DOI 10.1038/nchembio.2007.16
   Kwon HJ, 2009, CELL, V137, P1213, DOI 10.1016/j.cell.2009.03.049
   Liu JY, 2010, J BIOL CHEM, V285, P26058, DOI 10.1074/jbc.M110.100271
   Lyseng-Williamson KA, 2014, DRUGS, V74, P61, DOI 10.1007/s40265-013-0164-6
   Meng FK, 2014, NATURE, V513, P367, DOI 10.1038/nature13735
   Millat G, 1999, AM J HUM GENET, V65, P1321, DOI 10.1086/302626
   Murray TJ, 2008, ORG LETT, V10, P3429, DOI 10.1021/ol800902g
   Nagral A, 2014, J CLIN EXP HEPATOL, V4, P37, DOI 10.1016/j.jceh.2014.02.005
   Naryshkin NA, 2014, SCIENCE, V345, P688, DOI 10.1126/science.1250127
   OHTSUKA K, 1993, BIOCHEM BIOPH RES CO, V197, P235, DOI 10.1006/bbrc.1993.2466
   Palacino J, 2015, NAT CHEM BIOL, V11, P511, DOI [10.1038/NCHEMBIO.1837, 10.1038/nchembio.1837]
   Park WD, 2003, HUM MUTAT, V22, P313, DOI 10.1002/humu.10255
   Pellicena M, 2011, ORG LETT, V13, P5350, DOI 10.1021/ol202210k
   Pham D, 2016, NAT PROD REP, V33, P637, DOI 10.1039/c5np00110b
   Pipalia NH, 2017, J LIPID RES, V58, P695, DOI 10.1194/jlr.M072140
   Pipalia NH, 2011, P NATL ACAD SCI USA, V108, P5620, DOI 10.1073/pnas.1014890108
   Rauniyar N, 2015, MOL CELL PROTEOMICS, V14, P1734, DOI 10.1074/mcp.M114.045609
   Rohrs TM, 2017, ANGEW CHEM INT EDIT, V56, P10900, DOI 10.1002/anie.201705924
   Sakai Y, 2002, J ANTIBIOT, V55, P855, DOI 10.7164/antibiotics.55.855
   Shao L, 2012, APPL ENVIRON MICROB, V78, P2034, DOI 10.1128/AEM.06904-11
   Soccio RE, 2003, J BIOL CHEM, V278, P22183, DOI 10.1074/jbc.R300003200
   Subramanian K, 2017, MOL CELL PROTEOMICS, V16, P1938, DOI 10.1074/mcp.M116.064949
   Vanier MT, 2015, J INHERIT METAB DIS, V38, P187, DOI 10.1007/s10545-014-9794-4
   Wehrmann ZT, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0048561
   Yadav JS, 2014, EUR J ORG CHEM, V2014, P4389, DOI 10.1002/ejoc.201402235
   Yu DY, 2014, BIOORG MED CHEM LETT, V24, P4511, DOI 10.1016/j.bmcl.2014.07.078
   Yu DY, 2013, BIOORG MED CHEM LETT, V23, P5667, DOI 10.1016/j.bmcl.2013.08.023
   Yun Z., 2007, ORGANIC LETT, V9, P3141
NR 38
TC 4
Z9 8
U1 0
U2 13
PU AMER CHEMICAL SOC
PI WASHINGTON
PA 1155 16TH ST, NW, WASHINGTON, DC 20036 USA
SN 0163-3864
EI 1520-6025
J9 J NAT PROD
JI J. Nat. Prod.
PD SEP
PY 2018
VL 81
IS 9
BP 2018
EP 2025
DI 10.1021/acs.jnatprod.8b00314
PG 8
WC Plant Sciences; Chemistry, Medicinal; Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED); Index Chemicus (IC)
SC Plant Sciences; Pharmacology & Pharmacy
GA GV7BM
UT WOS:000446276600013
PM 30188717
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Sun, XY
   Deng, KY
   Zang, YH
   Zhang, ZY
   Zhao, BX
   Fan, JY
   Huang, LJ
AF Sun, Xueyuan
   Deng, Kaiyuan
   Zang, Yunhui
   Zhang, Zhiyong
   Zhao, Boxin
   Fan, Jingyao
   Huang, Lijuan
TI Exploring the regulatory roles of circular RNAs in the pathogenesis of
   atherosclerosis
SO VASCULAR PHARMACOLOGY
LA English
DT Review
DE Circular RNAs; Biogenesis; Atherosclerosis; Transcription
ID SMOOTH-MUSCLE-CELL; VASCULAR ENDOTHELIAL-CELLS; TOLL-LIKE RECEPTORS;
   OXIDATIVE STRESS; NITRIC-OXIDE; LOW-DENSITY; CHOLESTEROL ACCUMULATION;
   INFLAMMATORY RESPONSE; CIRCRNA BIOGENESIS; SIGNALING PATHWAY
AB Circular RNAs (circRNAs) are a class of noncoding RNAs with a covalently closed loop structure. Recent evidence has shown that circRNAs can regulate gene transcription, alternative splicing, microRNA (miRNA) "molecular sponges", RNA-binding proteins and protein translation. Atherosclerosis is one of the leading causes of death worldwide, and more studies have indicated that circRNAs are related to atherosclerosis pathogenesis, including vascular endothelial cells, vascular smooth muscle cells, inflammation and lipid metabolism. In this review, we systematically summarize the biogenesis, characteristics and functions of circRNAs with a focus on their roles in the pathogenesis of atherosclerosis.
C1 [Sun, Xueyuan; Deng, Kaiyuan; Zang, Yunhui; Zhang, Zhiyong; Zhao, Boxin; Fan, Jingyao; Huang, Lijuan] Harbin Med Univ, Dept Clin Lab, Affiliated Hosp 2, Harbin 150086, Peoples R China.
C3 Harbin Medical University
RP Huang, LJ (corresponding author), Harbin Med Univ, Dept Clin Lab, Affiliated Hosp 2, Harbin 150086, Peoples R China.
EM hebhlj@sina.com
RI Zhang, Yuyao/KEH-7175-2024; Zhang, Yifei/GRO-3001-2022
CR Abdelmohsen K, 2017, RNA BIOL, V14, P361, DOI 10.1080/15476286.2017.1279788
   Akkoca M, 2017, CLIN HEMORHEOL MICRO, V65, P151, DOI 10.3233/CH-16143
   Allahverdian S, 2014, CIRCULATION, V129, P1551, DOI 10.1161/CIRCULATIONAHA.113.005015
   ARNBERG AC, 1980, CELL, V19, P313, DOI 10.1016/0092-8674(80)90505-X
   Ashwal-Fluss R, 2014, MOL CELL, V56, P55, DOI 10.1016/j.molcel.2014.08.019
   Aubart FC, 2009, MOL THER, V17, P455, DOI 10.1038/mt.2008.291
   Badimon L, 2014, J INTERN MED, V276, P618, DOI 10.1111/joim.12296
   Balzan S, 2018, LIFE SCI, V198, P79, DOI 10.1016/j.lfs.2018.02.024
   Baumer Y, 2017, ATHEROSCLEROSIS, V256, P105, DOI 10.1016/j.atherosclerosis.2016.11.017
   Bazan HA, 2017, CIRC-CARDIOVASC GENE, V10, DOI 10.1161/CIRCGENETICS.117.001720
   Begum S, 2018, ONCOGENE, V37, P4055, DOI 10.1038/s41388-018-0230-3
   Boeckel JN, 2015, CIRC RES, V117, P884, DOI 10.1161/CIRCRESAHA.115.306319
   Borran S, 2020, PATHOL RES PRACT, V216, DOI 10.1016/j.prp.2020.153217
   Burd CE, 2010, PLOS GENET, V6, DOI 10.1371/journal.pgen.1001233
   Buttery LDK, 1996, LAB INVEST, V75, P77
   Cao Y, 2018, BIOCHEM BIOPH RES CO, V507, P362, DOI 10.1016/j.bbrc.2018.11.041
   CAPEL B, 1993, CELL, V73, P1019, DOI 10.1016/0092-8674(93)90279-Y
   Chen JJ, 2017, BIOCHEM BIOPH RES CO, V494, P126, DOI 10.1016/j.bbrc.2017.10.068
   Chen YH, 2016, J MED GENET, V53, P359, DOI 10.1136/jmedgenet-2016-103758
   Cheng J, 2019, GENE, V709, P1, DOI 10.1016/j.gene.2019.05.012
   Choromanska B, 2017, ADV CLIN EXP MED, V26, P717, DOI 10.17219/acem/62325
   Choy JC, 2001, J MOL CELL CARDIOL, V33, P1673, DOI 10.1006/jmcc.2001.1419
   COCQUERELLE C, 1992, EMBO J, V11, P1095, DOI 10.1002/j.1460-2075.1992.tb05148.x
   Conn SJ, 2015, CELL, V160, P1125, DOI 10.1016/j.cell.2015.02.014
   Cui M, 2020, J BIOCHEM MOL TOXIC, V34, DOI 10.1002/jbt.22468
   Cui YM, 2018, BIOMED PHARMACOTHER, V108, P1081, DOI 10.1016/j.biopha.2018.09.095
   CYBULSKY MI, 1991, SCIENCE, V251, P788, DOI 10.1126/science.1990440
   Danan M, 2012, NUCLEIC ACIDS RES, V40, P3131, DOI 10.1093/nar/gkr1009
   Dang RY, 2017, BIOCHEM BIOPH RES CO, V490, P104, DOI 10.1016/j.bbrc.2017.05.164
   Deng T, 2017, MOL MED REP, V16, P9367, DOI 10.3892/mmr.2017.7779
   Dong YZ, 2017, DIABETES VASC DIS RE, V14, P14, DOI 10.1177/1479164116666762
   Du WW, 2016, NUCLEIC ACIDS RES, V44, P2846, DOI 10.1093/nar/gkw027
   Eriksson EE, 2001, J EXP MED, V194, P205, DOI 10.1084/jem.194.2.205
   Faure E, 2001, J IMMUNOL, V166, P2018, DOI 10.4049/jimmunol.166.3.2018
   Feinberg MW, 2016, CIRC RES, V118, P703, DOI 10.1161/CIRCRESAHA.115.306300
   Fernandez S, 2001, CELL IMMUNOL, V209, P140, DOI 10.1006/cimm.2001.1795
   Firouzi SS, 2018, NEUROL RES, V40, P624, DOI 10.1080/01616412.2018.1458813
   Förstermann U, 2017, CIRC RES, V120, P713, DOI 10.1161/CIRCRESAHA.116.309326
   Forouzanfar MH, 2016, LANCET, V388, P1659, DOI 10.1016/S0140-6736(16)31679-8
   Frostegård J, 2013, BMC MED, V11, DOI 10.1186/1741-7015-11-117
   Gharavi NM, 2007, J BIOL CHEM, V282, P31460, DOI 10.1074/jbc.M704267200
   Giannotti KC, 2019, MOLECULES, V24, DOI 10.3390/molecules24183244
   Gimbrone MA, 2016, CIRC RES, V118, P620, DOI 10.1161/CIRCRESAHA.115.306301
   Goedeke L, 2015, NAT MED, V21, P1280, DOI 10.1038/nm.3949
   Gorenne I, 2013, CIRCULATION, V127, P386, DOI 10.1161/CIRCULATIONAHA.112.124404
   Grote K, 2005, VASC PHARMACOL, V43, P357, DOI 10.1016/j.vph.2005.08.021
   Guo JU, 2014, GENOME BIOL, V15, DOI 10.1186/s13059-014-0409-z
   Guo RW, 2012, CARDIOVASC RES, V93, P360, DOI 10.1093/cvr/cvr307
   Guo XY, 2018, WORLD J GASTROENTERO, V24, P323, DOI 10.3748/wjg.v24.i3.323
   Guo XY, 2017, OXID MED CELL LONGEV, V2017, DOI 10.1155/2017/3960197
   Gwon WG, 2017, INT IMMUNOPHARMACOL, V42, P81, DOI 10.1016/j.intimp.2016.11.014
   Hall IF, 2019, CIRC RES, V124, P498, DOI 10.1161/CIRCRESAHA.118.314240
   Hanefeld M, 2011, CARDIOVASC DIABETOL, V10, DOI 10.1186/1475-2840-10-65
   Hansen TB, 2013, NATURE, V495, P384, DOI 10.1038/nature11993
   Hashemian SM, 2020, MOL THER-NUCL ACIDS, V21, P51, DOI 10.1016/j.omtn.2020.05.012
   Holdt LM, 2016, NAT COMMUN, V7, DOI 10.1038/ncomms12429
   Huang AQ, 2020, THERANOSTICS, V10, P3503, DOI 10.7150/thno.42174
   Huang C, 2015, TRANSCR-AUSTIN, V6, P61, DOI 10.1080/21541264.2015.1071301
   Huang HS, 2020, BIOCHEM BIOPH RES CO, V525, P512, DOI 10.1016/j.bbrc.2020.02.109
   Indolfi C, 2019, VASC PHARMACOL, V114, P49, DOI 10.1016/j.vph.2018.10.006
   Ivanov A, 2015, CELL REP, V10, P170, DOI 10.1016/j.celrep.2014.12.019
   Jeck WR, 2014, NAT BIOTECHNOL, V32, P453, DOI 10.1038/nbt.2890
   Jeck WR, 2013, RNA, V19, P141, DOI 10.1261/rna.035667.112
   Kanters E, 2003, J CLIN INVEST, V112, P1176, DOI 10.1172/JCI18580
   Kassi E, 2011, BMC MED, V9, DOI 10.1186/1741-7015-9-48
   Khan MA, 2020, J TRANSL MED, V18, DOI 10.1186/s12967-020-02305-z
   Khan MAF, 2016, CIRC RES, V119, P996, DOI 10.1161/CIRCRESAHA.116.309568
   Kim NY, 2020, INT J MOL MED, V46, P449, DOI 10.3892/ijmm.2020.4582
   Kong P, 2019, NUCLEIC ACIDS RES, V47, P3580, DOI 10.1093/nar/gkz141
   Lacolley P, 2012, CARDIOVASC RES, V95, P194, DOI 10.1093/cvr/cvs135
   Legnini I, 2017, MOL CELL, V66, P22, DOI 10.1016/j.molcel.2017.02.017
   Lemmens K, 2007, CIRCULATION, V116, P954, DOI 10.1161/CIRCULATIONAHA.107.690487
   Li A, 2018, CELL PHYSIOL BIOCHEM, V47, P2458, DOI 10.1159/000491619
   Li CY, 2017, BIOMED PHARMACOTHER, V95, P1514, DOI 10.1016/j.biopha.2017.09.064
   Li H, 2020, ECOTOX ENVIRON SAFE, V192, DOI 10.1016/j.ecoenv.2020.110267
   Li HM, 2019, WIRES RNA, V10, DOI 10.1002/wrna.1538
   Li MY, 2018, FEBS J, V285, P220, DOI 10.1111/febs.14191
   Li QD, 2019, CELL METAB, V30, P157, DOI 10.1016/j.cmet.2019.05.009
   Li QG, 2020, CELL CYCLE, V19, P1466, DOI 10.1080/15384101.2020.1754561
   Li R, 2020, CELL MOL LIFE SCI, V77, P1661, DOI 10.1007/s00018-019-03345-5
   Li X, 2007, MOL CELL, V28, P91, DOI 10.1016/j.molcel.2007.07.032
   Li YS, 2017, EBIOMEDICINE, V24, P137, DOI 10.1016/j.ebiom.2017.09.015
   Li ZY, 2015, NAT STRUCT MOL BIOL, V22, P256, DOI 10.1038/nsmb.2959
   Libby P, 2002, NATURE, V420, P868, DOI [10.1038/nature01323, 10.1161/ATVBAHA.108.179705]
   Libby P, 2011, NATURE, V473, P317, DOI 10.1038/nature10146
   Lin HJ, 2016, SEMIN OPHTHALMOL, V31, P1, DOI 10.3109/08820538.2015.1114865
   Lin S., 2019, SILENCING HSA CIRC 0
   Liu C, 2017, THERANOSTICS, V7, P2863, DOI 10.7150/thno.19353
   Lusis AJ, 2000, NATURE, V407, P233, DOI 10.1038/35025203
   Mao YY, 2018, BIOCHEM BIOPH RES CO, V505, P119, DOI 10.1016/j.bbrc.2018.09.069
   Marszalek RJ, 2019, PFLUG ARCH EUR J PHY, V471, P769, DOI 10.1007/s00424-018-2224-y
   Medzhitov R, 2001, NAT REV IMMUNOL, V1, P135, DOI 10.1038/35100529
   Memczak S, 2013, NATURE, V495, P333, DOI 10.1038/nature11928
   Millen AE, 2017, J NUTR HEALTH AGING, V21, P772, DOI 10.1007/s12603-016-0827-6
   Mirzaei H, 2020, MOL THER-ONCOLYTICS, V19, P218, DOI 10.1016/j.omto.2020.10.003
   Moore KJ, 2013, NAT REV IMMUNOL, V13, P709, DOI 10.1038/nri3520
   Morton DJ, 2018, RNA, V24, P127, DOI 10.1261/rna.064626.117
   Naeli P, 2020, CRIT REV ONCOL HEMAT, V145, DOI 10.1016/j.critrevonc.2019.102854
   Nahand JS, 2020, FRONT MICROBIOL, V11, DOI 10.3389/fmicb.2020.01853
   Najafi-Shoushtari SH, 2010, SCIENCE, V328, P1566, DOI 10.1126/science.1189123
   Ng WL, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-12550-w
   Ng WL, 2016, RNA BIOL, V13, P861, DOI 10.1080/15476286.2016.1207036
   NIGRO JM, 1991, CELL, V64, P607, DOI 10.1016/0092-8674(91)90244-S
   O'Shea JJ, 2004, NAT REV DRUG DISCOV, V3, P555, DOI 10.1038/nrd1441
   Owens GK, 2004, PHYSIOL REV, V84, P767, DOI 10.1152/physrev.00041.2003
   Pamudurti NR, 2017, MOL CELL, V66, P9, DOI 10.1016/j.molcel.2017.02.021
   Pan L, 2018, INT J MOL MED, V42, P597, DOI 10.3892/ijmm.2018.3625
   Pentikäinen MO, 2000, J INTERN MED, V247, P359, DOI 10.1046/j.1365-2796.2000.00655.x
   Ping SN, 2017, CELL DEATH DIS, V8, DOI 10.1038/cddis.2017.213
   Ping SN, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0141375
   Pirillo A, 2013, MEDIAT INFLAMM, V2013, DOI 10.1155/2013/152786
   Pisoschi AM, 2015, EUR J MED CHEM, V97, P55, DOI 10.1016/j.ejmech.2015.04.040
   Ponting CP, 2009, CELL, V136, P629, DOI 10.1016/j.cell.2009.02.006
   Qiu JH, 2011, ANN BIOMED ENG, V39, P2869, DOI 10.1007/s10439-011-0382-6
   Qu SB, 2017, RNA BIOL, V14, P992, DOI 10.1080/15476286.2016.1220473
   Rahman S, 2007, DIABETES OBES METAB, V9, P767, DOI 10.1111/j.1463-1326.2006.00655.x
   Rayner KJ, 2010, SCIENCE, V328, P1570, DOI 10.1126/science.1189862
   Rong ZH, 2019, MOL THER-NUCL ACIDS, V18, P999, DOI 10.1016/j.omtn.2019.10.023
   Ross R, 1999, NEW ENGL J MED, V340, P115, DOI 10.1056/NEJM199901143400207
   SANGER HL, 1976, P NATL ACAD SCI USA, V73, P3852, DOI 10.1073/pnas.73.11.3852
   Seo HH, 2017, BIOL RES, V50, DOI 10.1186/s40659-016-0106-3
   Shabaninejad Z, 2019, J OVARIAN RES, V12, DOI 10.1186/s13048-019-0558-5
   Shan K, 2017, CIRCULATION, V136, P1629, DOI 10.1161/CIRCULATIONAHA.117.029004
   Shang LL, 2019, GENE, V711, DOI 10.1016/j.gene.2019.143948
   Shankman LS, 2015, NAT MED, V21, P628, DOI 10.1038/nm.3866
   Shen L, 2019, MOL MED REP, V19, P3923, DOI 10.3892/mmr.2019.10011
   Solly EL, 2019, J CLIN MED, V8, DOI 10.3390/jcm8122199
   Song CL, 2017, CELL PHYSIOL BIOCHEM, V42, P1202, DOI 10.1159/000478918
   STEPANOV SS, 1985, TSITOLOGIYA+, V27, P1235
   Sugiyama S, 2001, AM J PATHOL, V158, P879, DOI 10.1016/S0002-9440(10)64036-9
   Sun JG, 2019, BIOCHEM CELL BIOL, V97, P709, DOI 10.1139/bcb-2019-0031
   Sun XH, 2013, CURR ATHEROSCLER REP, V15, DOI 10.1007/s11883-013-0372-2
   Sun Y, 2019, CELL DEATH DIS, V10, DOI 10.1038/s41419-019-1590-5
   Sun Y, 2017, CIRC RES, V121, P628, DOI 10.1161/CIRCRESAHA.117.311441
   Suzuki H, 2014, INT J MOL SCI, V15, P9331, DOI 10.3390/ijms15069331
   Tan WLW, 2017, CARDIOVASC RES, V113, P298, DOI 10.1093/cvr/cvw250
   Tang Q, 2020, ONCOTARGETS THER, V13, P2067, DOI 10.2147/OTT.S233672
   Tay Y, 2014, NATURE, V505, P344, DOI 10.1038/nature12986
   Tousoulis D, 2016, EUR HEART J, V37, P1723, DOI 10.1093/eurheartj/ehv759
   Vausort M, 2016, J AM COLL CARDIOL, V68, P1247, DOI 10.1016/j.jacc.2016.06.040
   Vilades D, 2020, FASEB J, V34, P4403, DOI 10.1096/fj.201902507R
   Violi F, 2017, ANTIOXID REDOX SIGN, V27, P1083, DOI 10.1089/ars.2016.6963
   Wang HH, 2009, GLIA, V57, P24, DOI 10.1002/glia.20732
   Wang LY, 2019, ATHEROSCLEROSIS, V286, P88, DOI 10.1016/j.atherosclerosis.2019.05.006
   Wang LB, 2019, DNA CELL BIOL, V38, P1499, DOI 10.1089/dna.2019.4865
   Wang PL, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0090859
   Wang R, 2016, SCI REP-UK, V6, DOI 10.1038/srep36790
   Wang Y, 2020, EUR REV MED PHARMACO, V24, P3476, DOI 10.26355/eurrev_202004_20806
   Wang Y, 2019, OXID MED CELL LONGEV, V2019, DOI 10.1155/2019/7954657
   Weinert S, 2013, CARDIOVASC RES, V97, P544, DOI 10.1093/cvr/cvs367
   Weiser-Evans MCM, 2017, CIRC RES, V121, P591, DOI 10.1161/CIRCRESAHA.117.311722
   Werfel S, 2016, J MOL CELL CARDIOL, V98, P103, DOI 10.1016/j.yjmcc.2016.07.007
   Williams JW, 2019, IMMUNITY, V50, P941, DOI 10.1016/j.immuni.2019.03.007
   Wilusz JE, 2018, WIRES RNA, V9, DOI 10.1002/wrna.1478
   Xia X, 2019, MOL CANCER, V18, DOI 10.1186/s12943-019-1056-5
   Xiang Q, 2020, EBIOMEDICINE, V53, DOI 10.1016/j.ebiom.2020.102679
   Xiao ZP, 2018, CELL PHYSIOL BIOCHEM, V46, P1779, DOI 10.1159/000489364
   Xu G, 2009, CIRC RES, V105, P500, DOI 10.1161/CIRCRESAHA.109.193870
   Xu JY, 2019, FASEB J, V33, P2659, DOI 10.1096/fj.201800243RRR
   Xu S, 2018, PEERJ, V6, DOI 10.7717/peerj.5503
   Yan XD, 2018, CELL PHYSIOL BIOCHEM, V48, P1245, DOI 10.1159/000492010
   Yang L, 2019, MOL THER-NUCL ACIDS, V16, P434, DOI 10.1016/j.omtn.2019.02.028
   Yang MH, 2014, J LIPID RES, V55, P226, DOI 10.1194/jlr.M041335
   Yang YB, 2018, JNCI-J NATL CANCER I, V110, DOI 10.1093/jnci/djx166
   Yang Y, 2017, CELL RES, V27, P626, DOI 10.1038/cr.2017.31
   Yao QP, 2020, J CELL PHYSIOL, V235, P6831, DOI 10.1002/jcp.29577
   Yousefi F, 2020, CELL COMMUN SIGNAL, V18, DOI 10.1186/s12964-020-00555-4
   Yvan-Charvet L, 2008, CIRCULATION, V118, P1837, DOI 10.1161/CIRCULATIONAHA.108.793869
   Zaiou Mohamed, 2018, Diseases, V6, DOI 10.3390/diseases6020034
   Zaphiropoulos PG, 1996, P NATL ACAD SCI USA, V93, P6536, DOI 10.1073/pnas.93.13.6536
   Zhang CZ, 2020, SIGNAL TRANSDUCT TAR, V5, DOI 10.1038/s41392-020-0105-2
   Zhang F, 2018, AGING-US, V10, P2266, DOI 10.18632/aging.101541
   Zhang J, 2018, EXP THER MED, V16, P265, DOI 10.3892/etm.2018.6170
   Zhang ML, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-06862-2
   Zhang ML, 2018, ONCOGENE, V37, P1805, DOI 10.1038/s41388-017-0019-9
   Zhang SC, 2020, J BIOMED SCI, V27, DOI 10.1186/s12929-019-0595-9
   Zhang XO, 2016, GENOME RES, V26, P1277, DOI 10.1101/gr.202895.115
   Zhang XS, 2016, NUTR RES, V36, P964, DOI 10.1016/j.nutres.2016.06.004
   Zhang Y, 2013, MOL CELL, V51, P792, DOI 10.1016/j.molcel.2013.08.017
   Zhao ZZ, 2017, SCI REP-UK, V7, DOI 10.1038/srep39918
   Zheng CF, 2015, MOL MED REP, V12, P6656, DOI 10.3892/mmr.2015.4264
   Zhou P, 2017, FRONT PHARMACOL, V8, DOI 10.3389/fphar.2017.00464
   Zhou WP, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0121823
   Zhu K, 2019, EBIOMEDICINE, V49, P341, DOI 10.1016/j.ebiom.2019.10.004
   Zhu YY, 2020, EXP CELL RES, V387, DOI 10.1016/j.yexcr.2019.111753
NR 185
TC 14
Z9 14
U1 1
U2 10
PU ELSEVIER SCIENCE INC
PI NEW YORK
PA STE 800, 230 PARK AVE, NEW YORK, NY 10169 USA
SN 1537-1891
EI 1879-3649
J9 VASC PHARMACOL
JI Vasc. Pharmacol.
PD DEC
PY 2021
VL 141
AR 106898
DI 10.1016/j.vph.2021.106898
EA NOV 2021
PG 16
WC Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Pharmacology & Pharmacy
GA ZA3PJ
UT WOS:000756079500001
PM 34302990
DA 2025-04-10
ER

PT J
AU Yu, L
   Heere-Ress, E
   Boucher, B
   Defesche, JC
   Kastelein, J
   Lavoie, MA
   Genest, J
AF Yu, L
   Heere-Ress, E
   Boucher, B
   Defesche, JC
   Kastelein, J
   Lavoie, MA
   Genest, J
TI Familial hypercholesterolemia.: Acceptor splice site (G → C) mutation in
   intron 7 of the LDL-R gene:: alternate RNA editing causes exon 8
   skipping or a premature stop codon in exon 8.:
   LDL-RHonduras-1 [LDL-R1061(-1) G→C]
SO ATHEROSCLEROSIS
LA English
DT Article
DE familial hypercholesterolemia; low density lipoprotein receptor; reverse
   transcriptase PCR amplification
ID DENSITY-LIPOPROTEIN-RECEPTOR; FRENCH-CANADIAN MUTATION; CORONARY-ARTERY
   DISEASE; CONSEQUENCES; CHOLESTEROL; DELETION
AB Familial hypercholesterolemia (FH) is an autosomal dominant lipoprotein disorder caused by defects in the low density lipoprotein (LDL) receptor (R) gene. We report a novel mutation of the LDL-R gene in a 38-year-old man with homozygous FH from the province of Trujilo in Northern Honduras. The patient presented with tendinous xanthomas over the extensor tendons as well as xanthelasmas at sites of surgical scars. He was diagnosed with severe coronary artery disease requiring revascularization at age 29. After an unsuccessful course of treatment with simvastatin, the patient has been treated with plasma apheresis and macromolecular plasma filtration bi-monthly. Haplotyping of the LDL-R gene revealed homozygosity for the rare 'J' allele and a loss of the EcoRV restriction cleavage site in exon 8. Single stranded conformational polymorphism of exons 3, 6, 7, 9, 10 and 8 reveals an abnormal migration pattern in exon 8. Direct sequencing of the promoter region, exons 1, 4, 8 and 13 revealed two RFLP's and a novel mutation in intron 7. This mutation consists of G --> C transposition at the acceptor splice site of exon 8 at the last nucleotide of intron 7 [LDL-R1061(-1)G --> C]. Reverse transcriptase (RT) PCR amplification of RNA from monocytes obtained from the patient reveals a decrease in LDL-R mRNA (52% of control) and skipping of exon 8 (approximately 38%, as assessed by densitometric scanning of the amplified fragments) to form a new RNA transcript that includes exons 7 and 9 without frameshift. Alternative RNA editing leads to a new cryptic acceptor splice site 17 bp downstream in exon 8 producing a frameshift mutation and a predicted premature stop codon 1138 bp from the transcriptional start site (approximately 62%). Western blotting analysis using a monoclonal antibody (C7) directed at the amino terminus of the LDL-R protein reveals a marked reduction in LDL-R protein expressed in monocytes obtained from the patient. We conclude that LDL-R1061(-1)G -->C is a novel mutation of the LDL-R gene that results in marked decrease in LDL-R mRNA levels and protein expression by two alternate RNA editing mechanisms, that cause skipping of exon 8 or the use of a novel cryptic acceptor splice site in exon 8 with a frameshift and premature stop codon. The patient continues to do well on selective plasma filtration but developed bilateral severe carotid artery disease requiring surgical intervention. (C) 1999 Elsevier Science Ireland Ltd. All rights reserved.
C1 Clin Res Inst Montreal, Cardiovasc Genet Lab, Montreal, PQ H2W 1R7, Canada.
   Univ Vienna, Dept Clin Pharmacol, Vienna, Austria.
   Univ Amsterdam, Acad Med Ctr, Dept Vasc Med, NL-1105 AZ Amsterdam, Netherlands.
   Montreal Heart Inst, Montreal, PQ H1T 1C8, Canada.
   Univ Montreal, Ctr Hosp, Serv Cardiol, Montreal, PQ, Canada.
C3 Universite de Montreal; Institut de Recherche Clinique de Montreal
   (IRCM); University of Vienna; University of Amsterdam; Academic Medical
   Center Amsterdam; Universite de Montreal; Universite de Montreal
RP Genest, J (corresponding author), Clin Res Inst Montreal, Cardiovasc Genet Lab, 110 Pine Ave W, Montreal, PQ H2W 1R7, Canada.
RI Kastelein, John/AEK-0200-2022
CR ALLOISIO N, 1993, BLOOD, V81, P2791
   BETARD C, 1992, HUM GENET, V88, P529, DOI 10.1007/BF00219339
   BOYUM A, 1968, SCAND J CLIN LAB INV, VS 21, P77
   DAVIS CG, 1987, NATURE, V326, P760, DOI 10.1038/326760a0
   FISCHER SG, 1980, P NATL ACAD SCI-BIOL, V77, P4420, DOI 10.1073/pnas.77.8.4420
   GENEST JJ, 1992, CIRCULATION, V85, P2025, DOI 10.1161/01.CIR.85.6.2025
   Goldstein J.L., 1989, METABOLIC BASIS INHE, P1215
   Hobbs Helen H., 1992, Human Mutation, V1, P445, DOI 10.1002/humu.1380010602
   KARAYAN L, 1994, ARTERIOSCLER THROMB, V14, P1258, DOI 10.1161/01.ATV.14.8.1258
   KRAWCZAK M, 1992, HUM GENET, V90, P41
   LEITERSDORF E, 1990, J CLIN INVEST, V85, P1014, DOI 10.1172/JCI114531
   LOMBARDI P, 1993, ATHEROSCLEROSIS, V104, P117, DOI 10.1016/0021-9150(93)90182-T
   MOORJANI S, 1993, LANCET, V341, P1303, DOI 10.1016/0140-6736(93)90815-X
   ROGERS J, 1980, P NATL ACAD SCI-BIOL, V77, P1877, DOI 10.1073/pnas.77.4.1877
   SASS C, 1995, J BIOL CHEM, V270, P25166, DOI 10.1074/jbc.270.42.25166
   SUDHOF TC, 1985, SCIENCE, V228, P815, DOI 10.1126/science.2988123
   Weber M, 1997, CAN J CARDIOL, V13, P253
   Yu L, 1996, ATHEROSCLEROSIS, V124, P103, DOI 10.1016/0021-9150(96)05828-5
NR 18
TC 22
Z9 24
U1 0
U2 0
PU ELSEVIER SCI IRELAND LTD
PI CLARE
PA CUSTOMER RELATIONS MANAGER, BAY 15, SHANNON INDUSTRIAL ESTATE CO, CLARE,
   IRELAND
SN 0021-9150
J9 ATHEROSCLEROSIS
JI Atherosclerosis
PD SEP
PY 1999
VL 146
IS 1
BP 125
EP 131
DI 10.1016/S0021-9150(99)00109-4
PG 7
WC Cardiac & Cardiovascular Systems; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology
GA 230NU
UT WOS:000082257900016
PM 10487495
DA 2025-04-10
ER

PT J
AU Tran, P
   Leclerc, D
   Chan, M
   Pai, A
   Hiou-Tim, F
   Wu, Q
   Goyette, P
   Artigas, C
   Milos, R
   Rozen, R
AF Tran, P
   Leclerc, D
   Chan, M
   Pai, A
   Hiou-Tim, F
   Wu, Q
   Goyette, P
   Artigas, C
   Milos, R
   Rozen, R
TI Multiple transcription start sites and alternative splicing in the
   methylenetetrahydrofolate reductase gene result in two enzyme isoforms
SO MAMMALIAN GENOME
LA English
DT Article
ID MESSENGER-RNA; COMMON MUTATION; ACUTE-LEUKEMIA; MTHFR; RISK;
   HOMOCYSTEINE; IDENTIFICATION; POLYMORPHISMS; TRANSLATION; ASSOCIATION
AB Methylenetetrahydrofolate reductase (MTHFR) reduces 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, the major carbon donor in the remethylation of homocysteine to methionine. Mild MTHFR deficiency, due to a common variant at nucleotide 677, has been reported to alter risk for several disorders including cardiovascular disease, neural tube defects, pregnancy complications, and certain cancers. Little is known about MTHFR regulation, since the complete cDNA and gene sequences have not been determined. In earlier work, we isolated and expressed a 2.2-kb human cDNA comprised of 11 coding exons, and we demonstrated that it encoded an active 70-kDa isoform. However, transcript sizes of approximately 7.5 kb and 9.5 kb and the presence of a second isoform of 77 kDa on Western blots suggested that cDNA sequences were incomplete. In this report, we characterized the complete cDNA and gene structure in human and mouse. Variable 5' and 3' UTR regions were identified, resulting in transcript heterogeneity. The 5' and 3' termini of the MTHFR cDNA were found to overlap with the 5' terminus of a chloride ion channel gene (CLCN-6) and the 3' terminus of an unidentified gene, respectively; this finding has resulted in finer mapping of MTHFR on Chromosome (Chr) 1p36.3. Ribonuclease protection assays identified clusters of transcriptional start sites, suggesting the existence of multiple promoters. MTHFR has several polyadenylation sites creating 3'UTR lengths of 0.2 kb-5.0 kb or 0.6 kb-4.0 kb in human and mouse, respectively. In both species, the previously reported exon 1 was redefined to approximately 3.0 kb in length and shown to be alternatively spliced. An important splice variant contains novel coding sequences; this cDNA was expressed and shown to encode the isozyme of 77 kDa. Our results, which suggest intricate regulation of MTHFR, will facilitate additional regulatory and functional studies of the different isoforms.
C1 McGill Univ, Montreal Childrens Hosp, Dept Human Genet, Montreal, PQ H3H 1P3, Canada.
   McGill Univ, Montreal Childrens Hosp, Dept Pediat, Montreal, PQ H3H 1P3, Canada.
   McGill Univ, Montreal Childrens Hosp, Dept Biol, Montreal, PQ H3H 1P3, Canada.
C3 McGill University; McGill University; McGill University
RP Rozen, R (corresponding author), McGill Univ, Montreal Childrens Hosp, Res Inst, 4060 St Catherine St W,Room 200, Montreal, PQ H3Z 2Z3, Canada.
RI Leclerc, Daniel/B-6375-2012; Rozen, Rima/AAE-9294-2020
OI Leclerc, Daniel/0000-0002-9766-8941
CR [Anonymous], MOL CLONING LAB MANU
   Bezold G, 2001, NEW ENGL J MED, V344, P1172, DOI 10.1056/NEJM200104123441517
   Botto LD, 2000, AM J EPIDEMIOL, V151, P862
   Chan M, 1999, FASEB J, V13, pA1375
   CROSS SH, 1994, NAT GENET, V6, P236, DOI 10.1038/ng0394-236
   DAUBNER SC, 1982, J BIOL CHEM, V257, P140
   Dell'Api M, 2001, BIOL REPROD, V64, P218
   Frosst P, 1996, MAMM GENOME, V7, P864, DOI 10.1007/s003359900255
   FROSST P, 1995, NAT GENET, V10, P111, DOI 10.1038/ng0595-111
   Gaughan DJ, 2000, GENE, V257, P279, DOI 10.1016/S0378-1119(00)00392-9
   Goyette P, 1998, MAMM GENOME, V9, P652, DOI 10.1007/s003359900838
   GOYETTE P, 1994, NAT GENET, V7, P195, DOI 10.1038/ng0694-195
   GUALERZI CO, 1990, BIOCHEMISTRY-US, V29, P5881, DOI 10.1021/bi00477a001
   Guenther BD, 1999, NAT STRUCT BIOL, V6, P359, DOI 10.1038/7594
   Higuchi R., 1990, PCR PROTOCOLS GUIDE, P177
   Homberger A, 2000, EUR J HUM GENET, V8, P725, DOI 10.1038/sj.ejhg.5200522
   Jacques PF, 1996, CIRCULATION, V93, P7, DOI 10.1161/01.CIR.93.1.7
   James SJ, 1999, AM J CLIN NUTR, V70, P495
   Kashiwabara S, 2000, DEV BIOL, V228, P106, DOI 10.1006/dbio.2000.9894
   Kupferminc MJ, 1999, NEW ENGL J MED, V340, P9, DOI 10.1056/NEJM199901073400102
   Leclerc D, 1998, P NATL ACAD SCI USA, V95, P3059, DOI 10.1073/pnas.95.6.3059
   Ma J, 1997, CANCER RES, V57, P1098
   Mills JL, 1999, AM J MED GENET, V86, P71, DOI 10.1002/(SICI)1096-8628(19990903)86:1<71::AID-AJMG14>3.0.CO;2-Y
   Schwahn B, 2001, Am J Pharmacogenomics, V1, P189, DOI 10.2165/00129785-200101030-00004
   Skibola CF, 1999, P NATL ACAD SCI USA, V96, P12810, DOI 10.1073/pnas.96.22.12810
   Speek M, 1996, HUM MOL GENET, V5, P1749, DOI 10.1093/hmg/5.11.1749
   Ueland PM, 2000, AM J CLIN NUTR, V72, P324
   van der Velden AW, 1999, INT J BIOCHEM CELL B, V31, P87, DOI 10.1016/S1357-2725(98)00134-4
   Weisberg IS, 2001, ATHEROSCLEROSIS, V156, P409, DOI 10.1016/S0021-9150(00)00671-7
   Wenstrom KD, 2001, AM J OBSTET GYNECOL, V184, P806, DOI 10.1067/mob.2001.113845
   Wiemels JL, 2001, P NATL ACAD SCI USA, V98, P4004, DOI 10.1073/pnas.061408298
   Yamada K, 2001, P NATL ACAD SCI USA, V98, P14853, DOI 10.1073/pnas.261469998
NR 32
TC 41
Z9 52
U1 0
U2 2
PU SPRINGER-VERLAG
PI NEW YORK
PA 175 FIFTH AVE, NEW YORK, NY 10010 USA
SN 0938-8990
J9 MAMM GENOME
JI Mamm. Genome
PD SEP
PY 2002
VL 13
IS 9
BP 483
EP 492
DI 10.1007/s00335-002-2167-6
PG 10
WC Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology;
   Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology;
   Genetics & Heredity
GA 586YN
UT WOS:000177613900002
PM 12370778
DA 2025-04-10
ER

PT J
AU Miljus, N
   Massih, B
   Weis, MA
   Rison, JV
   Bonnas, CB
   Sillaber, I
   Ehrenreich, H
   Geurten, BRH
   Heinrich, R
AF Miljus, Natasa
   Massih, Bita
   Weis, Marissa A.
   Rison, Jan Vincent
   Bonnas, Christel B.
   Sillaber, Inge
   Ehrenreich, Hannelore
   Geurten, Bart R. H.
   Heinrich, Ralf
TI Neuroprotection and endocytosis: erythropoietin receptors in insect
   nervous systems
SO JOURNAL OF NEUROCHEMISTRY
LA English
DT Article
DE endocytosis; erythropoietin; erythropoietin receptor; insect;
   neuroprotection; non-erythropoietic Epo variant
ID DIFFERENTIATED NEUROBLASTOMA SH-SY5Y; CEREBRAL-ISCHEMIA;
   CORTICAL-NEURONS; IN-VITRO; BRAIN; REGENERATION; HIPPOCAMPAL;
   ACTIVATION; CYTOKINE; IDENTIFICATION
AB Erythropoietin (Epo) plays a dual role as an erythropoiesis-stimulating hormone and a locally produced cytoprotectant in various vertebrate tissues. Splice variants and engineered derivatives of Epo that mediate neuroprotection but do not stimulate erythropoiesis suggest that alternative receptors, different from the classical' homodimeric receptor involved in haematopoiesis, mediate neuroprotective Epo functions. Previous studies on grasshoppers demonstrated neuroprotective and neuroregenerative effects of Epo that involved similar transduction pathways as in mammals. To advance the characterization of yet unidentified neuroprotective Epo receptors, we studied the neuroprotective potency of the human non-erythropoietic Epo splice variant EV-3 in primary cultured locust brain neurons. We demonstrate that EV-3, like Epo, protects locust neurons from hypoxia-induced apoptotic death through activation of the Janus kinase/signal transducer and activator of transcription transduction pathway. Using the fluorescent dye FM1-43 to quantify endocytotic activity we show that both Epo and EV-3 increase the number of fluorescently labelled endocytotic vesicles. This reveals that binding of Epo to its neuroprotective receptor induces endocytosis, as it has been described for the mammalian homodimeric Epo-receptor expressed by erythroid progenitors. Reduction in Epo-stimulated endocytotic activity following pre-exposure to EV-3 indicated that both Epo and its splice variant bind to the same receptor on locust neurons. The shared neuroprotective potency of Epo and EV-3 in insect and mammalian neurons, in the absence of erythropoietic effects of EV-3 in mammals, suggests a greater similarity of the unidentified nervous Epo receptors (or receptor complexes) across phyla than between mammalian haematopoietic and neuroprotective receptors. Insects may serve as suitable models to evaluate the specific protective mechanisms mediated by Epo and its variants in non-erythropoietic mammalian tissues.
C1 [Miljus, Natasa; Massih, Bita; Weis, Marissa A.; Rison, Jan Vincent; Geurten, Bart R. H.; Heinrich, Ralf] Univ Goettingen, Inst Zool, Dept Cellular Neurobiol, Gottingen, Germany.
   [Bonnas, Christel B.; Sillaber, Inge] Epomedics GmbH, Gottingen, Germany.
   [Ehrenreich, Hannelore] Max Planck Inst Expt Med, Clin Neurosci, Gottingen, Germany.
   [Ehrenreich, Hannelore] DFG Ctr Nanoscale Microscopy & Mol Physiol Brain, Gottingen, Germany.
C3 University of Gottingen; Max Planck Society
RP Heinrich, R (corresponding author), Univ Goettingen, Inst Zool & Anthropol, Dept Cellular Neurobiol, Julia Lermontowa Weg 3, D-37077 Gottingen, Germany.
EM rheinri1@gwdg.de
RI Ehrenreich, Hannelore/AAS-6079-2020; Geurten, Bart/I-2037-2019
OI Geurten, Bart/0000-0002-1816-3241; Ehrenreich,
   Hannelore/0000-0001-8371-5711; Hambrecht, Bita/0009-0005-7908-2305
CR Adamcio B, 2008, BMC BIOL, V6, DOI 10.1186/1741-7007-6-37
   Alnaeeli Mawadda, 2012, Anat Res Int, V2012, P953264, DOI 10.1155/2012/953264
   [Anonymous], INT C COMP TOOL 2005
   [Anonymous], 2009, IDENTIFICATION ERYTH
   [Anonymous], 2013, Morphological Image Analysis: Principles and Applications
   Arbouzova NI, 2006, DEVELOPMENT, V133, P2605, DOI 10.1242/dev.02411
   Becker V, 2010, SCIENCE, V328, P1404, DOI 10.1126/science.1184913
   Beckman DL, 1999, BLOOD, V94, P2667, DOI 10.1182/blood.V94.8.2667.420k27_2667_2675
   BENJAMINI Y, 1995, J R STAT SOC B, V57, P289, DOI 10.1111/j.2517-6161.1995.tb02031.x
   Bernaudin M, 1999, J CEREBR BLOOD F MET, V19, P643, DOI 10.1097/00004647-199906000-00007
   Bond WS, 2014, FRONT IMMUNOL, V5, DOI 10.3389/fimmu.2014.00523
   Brines M, 2005, NAT REV NEUROSCI, V6, P484, DOI 10.1038/nrn1687
   Brines M, 2008, P NATL ACAD SCI USA, V105, P10925, DOI 10.1073/pnas.0805594105
   Buchmann K, 2014, FRONT IMMUNOL, V5, DOI 10.3389/fimmu.2014.00459
   Bulut GB, 2011, J BIOL CHEM, V286, P6449, DOI 10.1074/jbc.M110.186890
   Campana WM, 1998, INT J MOL MED, V1, P235
   Celik M, 2002, P NATL ACAD SCI USA, V99, P2258, DOI 10.1073/pnas.042693799
   Chateauvieux S, 2011, BIOCHEM PHARMACOL, V82, P1291, DOI 10.1016/j.bcp.2011.06.045
   Chu CY, 2008, CELL MOL LIFE SCI, V65, P3545, DOI 10.1007/s00018-008-8231-y
   Collino M, 2015, PHARMACOL THERAPEUT, V151, P32, DOI 10.1016/j.pharmthera.2015.02.005
   Constantinescu SN, 1999, TRENDS ENDOCRIN MET, V10, P18, DOI 10.1016/S1043-2760(98)00101-5
   Ehrenreich H, 2007, MOL PSYCHIATR, V12, P206, DOI 10.1038/sj.mp.4001907
   El-Kordi A, 2009, BMC BIOL, V7, DOI 10.1186/1741-7007-7-37
   Elliott S, 2006, BLOOD, V107, P1892, DOI 10.1182/blood-2005-10-4066
   Elliott S, 2014, ANN HEMATOL, V93, P181, DOI 10.1007/s00277-013-1947-2
   Erbayraktar S, 2003, P NATL ACAD SCI USA, V100, P6741, DOI 10.1073/pnas.1031753100
   Ernst MD, 2004, STAT SCI, V19, P676, DOI 10.1214/088342304000000396
   Fisher R A., 1970, Breakthroughs in Statistics: Methodology and Distribution, P66, DOI DOI 10.1007/978-1-4612-4380-96
   Gan Y, 2012, STROKE, V43, P3071, DOI 10.1161/STROKEAHA.112.663120
   Genc S, 2004, BRAIN RES, V1000, P19, DOI 10.1016/j.brainres.2003.12.037
   Gerber S, 2007, ISJ-INVERT SURVIV J, V4, P95
   Ghezzi P, 2004, CELL DEATH DIFFER, V11, pS37, DOI 10.1038/sj.cdd.4401450
   Ghezzi Pietro, 2013, Methods Mol Biol, V982, P43, DOI 10.1007/978-1-62703-308-4_3
   Gocht D, 2009, MICROSC RES TECHNIQ, V72, P385, DOI 10.1002/jemt.20683
   Groppe DM, 2011, PSYCHOPHYSIOLOGY, V48, P1711, DOI 10.1111/j.1469-8986.2011.01273.x
   Jelkmann W, 1996, ANN ANAT, V178, P391, DOI 10.1016/S0940-9602(96)80124-5
   Juul SE, 1998, PEDIATR RES, V43, P40, DOI 10.1203/00006450-199801000-00007
   King CE, 2007, EXP NEUROL, V205, P48, DOI 10.1016/j.expneurol.2007.01.017
   Kirkeby A, 2007, J NEUROSCI METH, V164, P50, DOI 10.1016/j.jneumeth.2007.03.026
   Kretz A, 2005, MOL CELL NEUROSCI, V29, P569, DOI 10.1016/j.mcn.2005.04.009
   Kuhn H. W., 1956, Nav. Res. Logist. Q, V3, P253, DOI [10.1002/nav.3800030404, DOI 10.1002/NAV.3800030404]
   Kuhn HW, 2005, NAV RES LOG, V52, P7, DOI 10.1002/nav.20053
   Leist M, 2004, SCIENCE, V305, P239, DOI 10.1126/science.1098313
   Levin I, 1998, FEBS LETT, V427, P164, DOI 10.1016/S0014-5793(98)00414-1
   Liongue C, 2007, BMC EVOL BIOL, V7, DOI 10.1186/1471-2148-7-120
   Lundby C, 2011, J PHYSIOL-LONDON, V589, P1265, DOI 10.1113/jphysiol.2010.195917
   MASUDA S, 1993, J BIOL CHEM, V268, P11208
   Miljus N, 2014, NEUROSCIENCE, V258, P218, DOI 10.1016/j.neuroscience.2013.11.020
   Miskowiak KW, 2014, J CLIN PSYCHIAT, V75, P1347, DOI 10.4088/JCP.13m08839
   Mitkovski M, 2015, J CEREBR BLOOD F MET, V35, P1233, DOI 10.1038/jcbfm.2015.100
   Morishita E, 1997, NEUROSCIENCE, V76, P105, DOI 10.1016/s0306-4522(96)00306-5
   Mukhopadhyay P, 2015, PATTERN RECOGN, V48, P993, DOI 10.1016/j.patcog.2014.08.027
   Nogawa-Kosaka N, 2010, EXP HEMATOL, V38, P363, DOI 10.1016/j.exphem.2010.02.009
   Ostrowski D, 2011, NEUROSCIENCE, V188, P95, DOI 10.1016/j.neuroscience.2011.05.018
   Ott C, 2015, MOL MED, V21, P803, DOI 10.2119/molmed.2015.00192
   Pankratova S, 2012, J NEUROCHEM, V121, P915, DOI 10.1111/j.1471-4159.2012.07751.x
   Sanchez PE, 2009, J COMP NEUROL, V514, P403, DOI 10.1002/cne.22020
   SAWYER ST, 1987, J BIOL CHEM, V262, P5554
   Schober ME, 2014, J NEUROTRAUM, V31, P358, DOI 10.1089/neu.2013.2922
   Shein NA, 2005, J CEREBR BLOOD F MET, V25, P1456, DOI 10.1038/sj.jcbfm.9600142
   Sinor AD, 2000, NEUROSCI LETT, V290, P213, DOI 10.1016/S0304-3940(00)01361-6
   Sirén AL, 2001, P NATL ACAD SCI USA, V98, P4044, DOI 10.1073/pnas.051606598
   Toth C, 2008, NEUROSCIENCE, V154, P767, DOI 10.1016/j.neuroscience.2008.03.052
   Um M, 2006, J BIOL CHEM, V281, P5648, DOI 10.1074/jbc.M510943200
   Um M, 2007, CELL SIGNAL, V19, P634, DOI 10.1016/j.cellsig.2006.08.014
   van der Kooij MA, 2008, BRAIN RES REV, V59, P22, DOI 10.1016/j.brainresrev.2008.04.007
   Villa P, 2003, J EXP MED, V198, P971, DOI 10.1084/jem.20021067
   Villa P, 2007, J CEREBR BLOOD F MET, V27, P552, DOI 10.1038/sj.jcbfm.9600370
   Wang L, 2014, INT J BIOL SCI, V10, P921, DOI 10.7150/ijbs.9518
   Wyder S, 2007, GENOME BIOL, V8, DOI 10.1186/gb-2007-8-11-r242
   Yin ZS, 2010, AM J NEURORADIOL, V31, P509, DOI 10.3174/ajnr.A1820
   Yu XB, 2002, DEVELOPMENT, V129, P505
   Zhang W, 2009, J CLIN NEUROSCI, V16, P554, DOI 10.1016/j.jocn.2008.06.013
NR 73
TC 10
Z9 12
U1 0
U2 11
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0022-3042
EI 1471-4159
J9 J NEUROCHEM
JI J. Neurochem.
PD APR
PY 2017
VL 141
IS 1
BP 63
EP 74
DI 10.1111/jnc.13967
PG 12
WC Biochemistry & Molecular Biology; Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Neurosciences & Neurology
GA EP6PW
UT WOS:000397502400006
PM 28142212
OA Bronze
DA 2025-04-10
ER

PT J
AU Hanson, J
   Reynaud, D
   Qiao, N
   Devel, P
   Moray, AL
   Renard, JF
   Kelley, LP
   Winum, JY
   Montero, JL
   Kinsella, BT
   Pirotte, B
   Pace-Asciak, CR
   Dogné, JM
AF Hanson, Julien
   Reynaud, Denis
   Qiao, Na
   Devel, Philippe
   Moray, Anne-Lise
   Renard, Jean-Francois
   Kelley, Leanne P.
   Winum, Jean-Yves
   Montero, Jean-Louis
   Kinsella, B. Therese
   Pirotte, Bernard
   Pace-Asciak, Cecil R.
   Dogne, Jean-Michel
TI Synthesis and pharmacological evaluation of novel nitrobenzenic
   thromboxane modulators as antiplatelet agents acting on both the alpha
   and beta isoforms of the human thromboxane receptor
SO JOURNAL OF MEDICINAL CHEMISTRY
LA English
DT Article
ID A(2) RECEPTOR; SYNTHASE INHIBITOR; TP-ALPHA; MEDIATED DESENSITIZATION;
   BLOOD PLATELETS; IN-VIVO; ANTAGONIST; PROSTACYCLIN; EXPRESSION; TARGET
AB Thromboxane A(2) ( TXA(2)) is an arachidonic acid metabolite involved in pathologies such as stroke, myocardial infarction, and atherosclerosis. Consequently, the design of TXA2 receptor ( TP) antagonists remains of great interest in cardiovascular medicine. The actions of TXA2 are mediated by its specific G-protein coupled receptor of which two alternative spliced isoforms, TP alpha and TP beta, have been described in humans. In this study, we report the synthesis of a series of original N-alkyl-N'-[2-( cycloalkyl, alkylaryl)-5-nitrobenzenesulfonyl] urea and N-alkyl-N'-[ 2-( alkylaryl)-5-nitrobenzenesulfonyl]-N"-cyanoguanidines and outline their pharmacological evaluation using the individual TP alpha and TP beta isoforms. Among compounds analyzed, several of them exhibited greater affinity and/or functional activity for either TP alpha or TP beta. The most promising molecules were also found to be antiplatelet agents. From the present results, structural features involved in isoform selectivity can be proposed, and thereby several lead compounds have been identified for the further development of selective TP isoform antagonists.
C1 Univ Liege, Nat & Synth Drugs Res Ctr, Dept Pharm, Lab Med Chem, B-4000 Liege, Belgium.
   Hosp Sick Children, Inst Res, Program Integrat Biol, Toronto, ON M5G 1X8, Canada.
   Univ Coll Dublin, Sch Biomol & Biomed Sci, Conway Inst Biomol & Biomed Res, Dublin 2, Ireland.
   Univ Namur, FUNDP, Dept Pharm, B-5000 Namur, Belgium.
   Univ Montpellier 2, Ecole Normale Super Chim Montpellier, UMR 5032, Lab Chim Biomol, F-34296 Montpellier, France.
C3 University of Liege; University of Toronto; Hospital for Sick Children
   (SickKids); University College Dublin; University of Namur; Ecole
   nationale superieure de chimie de Montpellier; Universite de Montpellier
RP Hanson, J (corresponding author), Univ Liege, Nat & Synth Drugs Res Ctr, Dept Pharm, Lab Med Chem, 1 Av Hop, B-4000 Liege, Belgium.
EM J.hanson@ulg.ac.be
RI Dogné, Jean-Michel/AAD-5773-2021; WINUM, Jean-Yves/AAC-9578-2019;
   Hanson, Julien/A-8242-2008; Pirotte, Bernard/AEO-1620-2022; WINUM,
   Jean-Yves/P-3387-2016
OI Pace-Asciak, Cecil/0009-0003-1392-4923; Hanson,
   Julien/0000-0001-7063-7590; WINUM, Jean-Yves/0000-0003-3197-3414;
   Kinsella, B. Therese/0000-0003-3072-941X
FU Wellcome Trust Funding Source: Medline
CR Ashton AW, 2004, CIRC RES, V95, P372, DOI 10.1161/01.RES.0000138300.41642.15
   BORN GVR, 1963, J PHYSIOL-LONDON, V168, P178, DOI 10.1113/jphysiol.1963.sp007185
   Cheng Y, 2002, SCIENCE, V296, P539, DOI 10.1126/science.1068711
   COLEMAN RA, 1994, PHARMACOL REV, V46, P205
   Coyle AT, 2005, FEBS J, V272, P4754, DOI 10.1111/j.1742-4658.2005.04890.x
   Coyle AT, 2005, FEBS J, V272, P1036, DOI 10.1111/j.1742-4658.2004.04538.x
   Dogné JM, 2000, PROSTAG LEUKOTR ESS, V62, P311, DOI 10.1054/plef.2000.0160
   Dogné JM, 2005, J MED CHEM, V48, P2251, DOI 10.1021/jm0402059
   Dogné JM, 2004, J PHARMACOL EXP THER, V309, P498, DOI 10.1124/jpet.103.063610
   Dogné JM, 2004, CURR MED CHEM, V11, P1223, DOI 10.2174/0929867043365260
   Dogné JM, 2001, J PHARM PHARMACOL, V53, P669, DOI 10.1211/0022357011775992
   Egan KM, 2005, CIRCULATION, V111, P334, DOI 10.1161/01.CIR.0000153386.95356.78
   Ghuysen A, 2004, J PHARMACOL EXP THER, V310, P964, DOI 10.1124/jpet.104.066852
   Habib A, 1999, J BIOL CHEM, V274, P2645, DOI 10.1074/jbc.274.5.2645
   HAMBERG M, 1975, P NATL ACAD SCI USA, V72, P2994, DOI 10.1073/pnas.72.8.2994
   Hanson J, 2005, J PHARMACOL EXP THER, V313, P293, DOI 10.1124/jpet.104.079301
   HARRIS DN, 1979, J CYCLIC NUCL PROT, V5, P125
   HIRATA M, 1991, NATURE, V349, P617, DOI 10.1038/349617a0
   Kinsella BT, 1997, J PHARMACOL EXP THER, V281, P957
   Lin KD, 1999, BIOTECHNIQUES, V26, P318, DOI 10.2144/99262rr02
   MAIS DE, 1985, J PHARMACOL EXP THER, V233, P418
   MEERWEIN H, 1957, CHEM BER-RECL, V90, P841, DOI 10.1002/cber.19570900602
   Moncada S, 1978, Adv Prostaglandin Thromboxane Res, V5, P211
   Parent JL, 1999, J BIOL CHEM, V274, P8941, DOI 10.1074/jbc.274.13.8941
   Qiao N, 2003, J PHARMACOL EXP THER, V307, P1142, DOI 10.1124/jpet.103.056705
   RAYCHOWDHURY MK, 1994, J BIOL CHEM, V269, P19256
   Reid HM, 2003, J BIOL CHEM, V278, P51190, DOI 10.1074/jbc.M309314200
   Rolin S, 2003, J PHARMACOL EXP THER, V306, P59, DOI 10.1124/jpet.102.046607
   Tchana-Sato V, 2005, PROSTAG OTH LIPID M, V78, P82, DOI 10.1016/j.prostaglandins.2005.04.001
   WAGNER AW, 1963, CHEM BER-RECL, V96, P1177, DOI 10.1002/cber.19630960433
   Walsh MT, 1998, J PHARMACOL EXP THER, V286, P1026
   Walsh MT, 2000, J BIOL CHEM, V275, P20412, DOI 10.1074/jbc.M907881199
NR 32
TC 10
Z9 14
U1 0
U2 0
PU AMER CHEMICAL SOC
PI WASHINGTON
PA 1155 16TH ST, NW, WASHINGTON, DC 20036 USA
SN 0022-2623
J9 J MED CHEM
JI J. Med. Chem.
PD JUN 15
PY 2006
VL 49
IS 12
BP 3701
EP 3709
DI 10.1021/jm060108a
PG 9
WC Chemistry, Medicinal
WE Science Citation Index Expanded (SCI-EXPANDED); Index Chemicus (IC)
SC Pharmacology & Pharmacy
GA 050UR
UT WOS:000238114700032
PM 16759113
DA 2025-04-10
ER

PT J
AU Leung, E
   Print, CG
   Parry, DA
   Closey, DN
   Lockhart, PJ
   Skinner, SJM
   Batchelor, DC
   Krissansen, GW
AF Leung, E
   Print, CG
   Parry, DA
   Closey, DN
   Lockhart, PJ
   Skinner, SJM
   Batchelor, DC
   Krissansen, GW
TI Cloning of novel kinectin splice variants with alternative C-termini:
   Structure, distribution and evolution of mouse kinectin
SO IMMUNOLOGY AND CELL BIOLOGY
LA English
DT Article
DE cDNA clones; coiled-coil protein; kinectin; microtubule; protein
   variants
ID COILED-COILS; PROTEIN; IDENTIFICATION; DESMOPLAKIN
AB The analysis of cDNA clones encoding novel variant forms of mouse kinectin, an endoplasmic reticulum (ER)-bound receptor for the motor protein kinesin, is reported. Kinesin and cytoplasmic dynein are involved in mediating the anterograde and retrograde movements of intracellular vesicles along the microtubule network. The amino acid sequence deduced from kinectin cDNA isolated from mouse spleen cell and testis libraries revealed a long signal peptide or transmembrane sequence, and a 328 amino acid residue globular N-terminal domain adjacent to a much larger 858-999-residue C-terminal coiled-coil rod domain. The C-terminal domain was composed of 18 coiled-coil regions formed from multiple contiguous heptad repeats which undergo alternative splicing as evidenced by the presence of at least five small (23-33 amino acid residue) insertion sequences scattered throughout. The inserts are present in any one of a number of combinations, generating an array of novel kinectin variants. insert 5 contains a termination codon, producing a C-terminus that is highly homologous to that of human kinectin. Three out of five mouse kinectin clones lack insert 5, generating a novel eleven amino acid C-terminus encoded by sequence that extends past the insertion site. The existence of alternative C-termini may have functional relevance given that the C-termini are exposed for interaction with kinesin, whereas the globular N-terminus is embedded in the ER membrane. Alternative C-termini represent candidate modifications that could determine specificity of binding to kinesin or cytoplasmic dynein, and the switching of directionality of movement. The cDNA hybridized to 4.5 kb transcripts expressed in all mouse cell lines and tissues examined, which provides the first indication that the kinectins are very widely distributed. Mouse kinectin is 42% similar over a 203 amino acid region to the chicken extracellular cardiac morphogen ES/130, whose canine homologue containing an inserted sequence of 10 amino acids repeated 54 times in tandem, is a ribosome receptor expressed on the ER. Mouse kinectin shares 64 and 83% identity, respectively, with its M(r) 160000 chicken and human kinectin homologues, There is a two-fold molar excess of kinectin over kinesin in unextracted vesicles, suggesting that kinectin might be a dimer. The electrostatic properties of the coiled-coil region of mouse kinectin, together with the relative frequencies of residues in particular positions within the heptad repeats support this notion.
C1 UNIV AUCKLAND,SCH MED,DEPT MOL MED,AUCKLAND 1,NEW ZEALAND.
   UNIV AUCKLAND,SCH MED,DEPT PAEDIAT,AUCKLAND 1,NEW ZEALAND.
   MASSEY UNIV,DEPT PHYS,PALMERSTON NORTH,NEW ZEALAND.
   MASSEY UNIV,MOL GENET UNIT,PALMERSTON NORTH,NEW ZEALAND.
C3 University of Auckland; University of Auckland; Massey University;
   Massey University
RI Skinner, Samuel/O-6882-2019; Mackey, David/H-5340-2014; Lockhart,
   Peter/E-6624-2011; Leung, Euphemia/D-2642-2009
OI Leung, Euphemia/0000-0002-6932-3188; Print, Cristin/0000-0001-8345-7812;
   Lockhart, Peter/0000-0002-1862-5688
CR AMOS LA, 1991, MOL CYTOSKELETON, P23
   BLAU HM, 1985, SCIENCE, V230, P758, DOI 10.1126/science.2414846
   CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
   COHEN C, 1990, FUNCTION GENETICS, V7, P1
   CONWAY JF, 1991, INT J BIOL MACROMOL, V13, P14, DOI 10.1016/0141-8130(91)90004-E
   FELSENSTEIN J, 1993, PHYLIP 3 5 MANUAL
   FUTTERER A, 1995, MOL BIOL CELL, V6, P161
   GREEN KJ, 1992, INT J BIOL MACROMOL, V14, P145, DOI 10.1016/S0141-8130(05)80004-2
   GREENWALT DE, 1992, BLOOD, V80, P1105
   HARBURY PB, 1994, NATURE, V371, P80, DOI 10.1038/371080a0
   HARBURY PB, 1993, SCIENCE, V262, P1401, DOI 10.1126/science.8248779
   JACKSON MR, 1990, EMBO J, V9, P3153, DOI 10.1002/j.1460-2075.1990.tb07513.x
   KOZAK M, 1993, MICROBIOL REV, V47, P1
   KUMAR J, 1995, SCIENCE, V267, P1834, DOI 10.1126/science.7892610
   MJAATVEDT CH, 1991, DEV BIOL, V145, P219, DOI 10.1016/0012-1606(91)90121-I
   MONERA OD, 1994, BIOCHEMISTRY-US, V33, P3862, DOI 10.1021/bi00179a010
   NAORA H, 1982, P NATL ACAD SCI-BIOL, V79, P6196, DOI 10.1073/pnas.79.20.6196
   Nomura N, 1994, DNA Res, V1, P27, DOI 10.1093/dnares/1.1.27
   OSHEA EK, 1992, CELL, V68, P699, DOI 10.1016/0092-8674(92)90145-3
   Parry D.A. N., 1991, AIP C P 226, P367
   PRINT CG, 1994, GENE, V144, P221, DOI 10.1016/0378-1119(94)90381-6
   PRINT CG, 1995, GENE, V153, P293, DOI 10.1016/0378-1119(95)00702-8
   PRINT CG, 1995, THESIS U AUCKLAND NZ
   REZAEE M, 1993, J BIOL CHEM, V268, P14404
   TOYOSHIMA I, 1992, J CELL BIOL, V118, P1121, DOI 10.1083/jcb.118.5.1121
   VIRATA MLA, 1992, P NATL ACAD SCI USA, V89, P544, DOI 10.1073/pnas.89.2.544
   WANKER EE, 1995, J CELL BIOL, V130, P29, DOI 10.1083/jcb.130.1.29
   YU H, 1995, GENE, V153, P293
NR 28
TC 25
Z9 29
U1 0
U2 1
PU BLACKWELL SCIENCE
PI CARLTON
PA 54 UNIVERSITY ST, P O BOX 378, CARLTON VICTORIA 3053, AUSTRALIA
SN 0818-9641
J9 IMMUNOL CELL BIOL
JI Immunol. Cell Biol.
PD OCT
PY 1996
VL 74
IS 5
BP 421
EP 433
DI 10.1038/icb.1996.72
PG 13
WC Cell Biology; Immunology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Immunology
GA VQ232
UT WOS:A1996VQ23200006
PM 8912005
DA 2025-04-10
ER

PT J
AU Sang, LJ
   Vieira, DCO
   Yue, DT
   Ben-Johny, M
   Dick, IE
AF Sang, Lingjie
   Vieira, Daiana C. O.
   Yue, David T.
   Ben-Johny, Manu
   Dick, Ivy E.
TI The molecular basis of the inhibition of CaV1
   calcium-dependent inactivation by the distal carboxy tail
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID C-TERMINUS; CA2+-DEPENDENT INACTIVATION; FLUORESCENT PROTEIN;
   SKELETAL-MUSCLE; CA2+ REGULATION; STAC PROTEINS; IQ DOMAIN; CHANNEL;
   CALMODULIN; BINDING
AB Ca2+/calmodulin-dependent inactivation (CDI) of Ca-V channels is a critical regulatory process that tunes the kinetics of Ca2+ entry for different cell types and physiologic responses. CDI is mediated by calmodulin (CaM), which is bound to the IQ domain of the Ca-V carboxy tail. This modulatory process is tailored by alternative splicing such that select splice variants of Ca(V)1.3 and Ca(V)1.4 contain a long distal carboxy tail (DCT). The DCT harbors an inhibitor of CDI (ICDI) module that competitively displaces CaM from the IQ domain, thereby diminishing CDI. While this overall mechanism is now well described, the detailed interactions required for ICDI binding to the IQ domain are yet to be elucidated. Here, we perform alanine-scanning mutagenesis of the IQ and ICDI domains and evaluate the contribution of neighboring regions to CDI inhibition. Through FRET binding analysis, we identify functionally relevant residues within the Ca(V)1.3 IQ domain and the Ca(V)1.4 ICDI and nearby A region, which are required for high-affinity IQ/ICDI binding. Importantly, patch-clamp recordings demonstrate that disruption of this interaction commensurately diminishes ICDI function resulting in the re-emergence of CDI in mutant channels. Furthermore, Ca(V)1.2 channels harbor a homologous DCT; however, the ICDI region of this channel does not appear to appreciably modulate Ca(V)1.2 CDI. Yet coexpression of Ca(V)1.2 ICDI with select Ca(V)1.3 splice variants significantly disrupts CDI, implicating a cross-channel modulatory scheme in cells expressing both channel subtypes. In all, these findings provide new insights into a molecular rheostat that fine-tunes Ca2+-entry and supports normal neuronal and cardiac function.
C1 [Sang, Lingjie; Yue, David T.; Ben-Johny, Manu; Dick, Ivy E.] Johns Hopkins Univ, Sch Med, Dept Biomed Engn, Baltimore, MD 21205 USA.
   [Vieira, Daiana C. O.; Dick, Ivy E.] Univ Maryland, Sch Med, Dept Physiol, Baltimore, MD 21201 USA.
   [Ben-Johny, Manu] Columbia Univ, Dept Physiol & Cellular Biophys, New York, NY USA.
C3 Johns Hopkins University; University System of Maryland; University of
   Maryland Baltimore; Columbia University
RP Dick, IE (corresponding author), Johns Hopkins Univ, Sch Med, Dept Biomed Engn, Baltimore, MD 21205 USA.; Dick, IE (corresponding author), Univ Maryland, Sch Med, Dept Physiol, Baltimore, MD 21201 USA.
EM ied@som.umaryand.edu
RI Vieira, Daiana/LTF-7395-2024
OI Dick, Ivy/0000-0002-7253-6846
FU NIH/NINDS [5R01NS085074]; NIH/NHLBI [1R01HL149926]
FX This grant was supported by an NIH/NINDS grant 5R01NS085074 and by an
   NIH/NHLBI grant 1R01HL149926. The content is solely the responsibility
   of the authors and does not necessarily represent the official views of
   the National Institutes of Health.
CR Adams PJ, 2014, CELL, V159, P608, DOI 10.1016/j.cell.2014.09.047
   Alseikhan BA, 2002, P NATL ACAD SCI USA, V99, P17185, DOI 10.1073/pnas.262372999
   Bazzazi H, 2013, CELL REP, V5, P367, DOI 10.1016/j.celrep.2013.09.006
   Bezprozvanny I, 2009, TRENDS MOL MED, V15, P89, DOI 10.1016/j.molmed.2009.01.001
   Bock G, 2011, J BIOL CHEM, V286, P42736, DOI 10.1074/jbc.M111.269951
   Campiglio M, 2018, P NATL ACAD SCI USA, V115, P1376, DOI 10.1073/pnas.1715997115
   Chaudhuri D, 2007, J GEN PHYSIOL, V129, P385, DOI 10.1085/jgp.200709749
   Christel CJ, 2012, J PHYSIOL-LONDON, V590, DOI 10.1113/jphysiol.2012.239954
   Doering CJ, 2005, BIOPHYS J, V89, P3042, DOI 10.1529/biophysj.105.067124
   Erickson MG, 2001, NEURON, V31, P973, DOI 10.1016/S0896-6273(01)00438-X
   Erickson MG, 2003, NEURON, V39, P97, DOI 10.1016/S0896-6273(03)00395-7
   Fuller MD, 2010, SCI SIGNAL, V3, DOI 10.1126/scisignal.2001152
   Gao TY, 2000, J BIOL CHEM, V275, P25436, DOI 10.1074/jbc.M003465200
   Gerhardstein BL, 2000, J BIOL CHEM, V275, P8556, DOI 10.1074/jbc.275.12.8556
   Ghosh D, 2017, Adv Pharmacol, V78, P49, DOI 10.1016/bs.apha.2016.08.002
   Gomez-Ospina N, 2006, CELL, V127, P591, DOI 10.1016/j.cell.2006.10.017
   Griessmeier K, 2009, J BIOL CHEM, V284, P29809, DOI 10.1074/jbc.M109.048082
   GUTIERREZ LM, 1991, J BIOL CHEM, V266, P16387
   Haeseleer F, 2016, J BIOL CHEM, V291, P15663, DOI 10.1074/jbc.M116.731737
   Harvey RD, 2013, J MOL CELL CARDIOL, V58, P143, DOI 10.1016/j.yjmcc.2012.12.006
   Hoda JC, 2005, J NEUROSCI, V25, P252, DOI 10.1523/JNEUROSCI.3054-04.2005
   Huang H, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms5481
   Huang H, 2012, NEURON, V73, P304, DOI 10.1016/j.neuron.2011.11.022
   Hulme JT, 2006, J PHYSIOL-LONDON, V576, P87, DOI 10.1113/jphysiol.2006.111799
   Hulme JT, 2005, P NATL ACAD SCI USA, V102, P5274, DOI 10.1073/pnas.0409885102
   Hurley MJ, 2013, BRAIN, V136, P2077, DOI 10.1093/brain/awt134
   Johny MB, 2013, NAT COMMUN, V4, DOI 10.1038/ncomms2727
   Kim J, 2004, NEURON, V41, P745, DOI 10.1016/S0896-6273(04)00081-9
   Lee A, 2003, P NATL ACAD SCI USA, V100, P16059, DOI 10.1073/pnas.2237000100
   Liang HY, 2003, NEURON, V39, P951, DOI 10.1016/S0896-6273(03)00560-9
   Lieb A, 2012, CHANNELS, V6, P197, DOI 10.4161/chan.21002
   Lipscombe D, 2004, J NEUROPHYSIOL, V92, P2633, DOI 10.1152/jn.00486.2004
   Liu N, 2017, ELIFE, V6, DOI 10.7554/eLife.21989
   Liu XD, 2010, NATURE, V463, P968, DOI 10.1038/nature08766
   Mangoni ME, 2003, P NATL ACAD SCI USA, V100, P5543, DOI 10.1073/pnas.0935295100
   MCDONALD TF, 1994, PHYSIOL REV, V74, P365, DOI 10.1152/physrev.1994.74.2.365
   Nagai T, 2002, NAT BIOTECHNOL, V20, P87, DOI 10.1038/nbt0102-87
   Niu J, 2018, ELIFE, V7, DOI 10.7554/eLife.35222
   Peterson BZ, 1999, NEURON, V22, P549, DOI 10.1016/S0896-6273(00)80709-6
   Pitt GS, 2001, J BIOL CHEM, V276, P30794, DOI 10.1074/jbc.M104959200
   Polster E, 2018, J NEUROSCI, V38, P9215, DOI 10.1523/JNEUROSCI.0695-18.2018
   Rizzo MA, 2004, NAT BIOTECHNOL, V22, P445, DOI 10.1038/nbt945
   Sang LJ, 2016, NAT COMMUN, V7, DOI 10.1038/ncomms12239
   Schroder E, 2009, CIRC RES, V104, P1373, DOI 10.1161/CIRCRESAHA.108.191387
   Shaltiel L, 2012, J BIOL CHEM, V287, P36312, DOI 10.1074/jbc.M112.392811
   Singh A, 2008, J BIOL CHEM, V283, P20733, DOI 10.1074/jbc.M802254200
   Singh A, 2006, NAT NEUROSCI, V9, P1108, DOI 10.1038/nn1751
   Splawski I, 2004, CELL, V119, P19, DOI 10.1016/j.cell.2004.09.011
   Splawski I, 2005, P NATL ACAD SCI USA, V102, P8089, DOI 10.1073/pnas.0502506102
   Striessnig J, 2006, BIOCHEM SOC T, V34, P903, DOI 10.1042/BST0340903
   Striessnig J, 2015, CURR MOL PHARMACOL, V8, P110, DOI 10.2174/1874467208666150507105845
   Strom TM, 1998, NAT GENET, V19, P260, DOI 10.1038/940
   Tan GMY, 2012, J BIOL CHEM, V287, P832, DOI 10.1074/jbc.M111.268722
   Wahl-Schott C, 2006, P NATL ACAD SCI USA, V103, P15657, DOI 10.1073/pnas.0604621103
   WEI XY, 1991, J BIOL CHEM, V266, P21943
   Xu WF, 2001, J NEUROSCI, V21, P5944, DOI 10.1523/JNEUROSCI.21-16-05944.2001
   Yang PS, 2006, J NEUROSCI, V26, P10677, DOI 10.1523/JNEUROSCI.3236-06.2006
   Yang PS, 2014, NAT CHEM BIOL, V10, P231, DOI [10.1038/nchembio.1436, 10.1038/NCHEMBIO.1436]
   Yuen SMWK, 2017, P NATL ACAD SCI USA, V114, pE9520, DOI 10.1073/pnas.1708852114
   Zühlke RD, 1999, NATURE, V399, P159, DOI 10.1038/20200
NR 60
TC 10
Z9 11
U1 1
U2 1
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD JAN-JUN
PY 2021
VL 296
AR 100502
DI 10.1016/j.jbc.2021.100502
PG 12
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA TI5TQ
UT WOS:000672866400476
PM 33667546
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Mammen, AL
   Mahoney, JA
   St Germain, A
   Badders, N
   Taylor, JP
   Rosen, A
   Spinette, S
AF Mammen, Andrew L.
   Mahoney, James A.
   St Germain, Amanda
   Badders, Nisha
   Taylor, J. Paul
   Rosen, Antony
   Spinette, Sarah
TI A Novel Conserved Isoform of the Ubiquitin Ligase UFD2a/UBE4B Is
   Expressed Exclusively in Mature Striated Muscle Cells
SO PLOS ONE
LA English
DT Article
ID CAENORHABDITIS-ELEGANS; PROTEIN-DEGRADATION; PROTEASOME PATHWAY; UNC-45
   CHAPERONE; U-BOX; MYOSIN; DIFFERENTIATION; MAINTENANCE; DOMAIN; HEART
AB Yeast Ufd2p was the first identified E4 multiubiquitin chain assembly factor. Its vertebrate homologues later referred to as UFD2a, UBE4B or E4B were also shown to have E3 ubiquitin ligase activity. UFD2a function in the brain has been well established in vivo, and in vitro studies have shown that its activity is essential for proper condensation and segregation of chromosomes during mitosis. Here we show that 2 alternative splice forms of UFD2a, UFD2a-7 and -7/7a, are expressed sequentially during myoblast differentiation of C2C12 cell cultures and during cardiotoxin-induced regeneration of skeletal muscle in mice. UFD2a-7 contains an alternate exon 7, and UFD2a-7/7a, the larger of the 2 isoforms, contains an additional novel exon 7a. Analysis of protein or mRNA expression in mice and zebrafish revealed that a similar pattern of isoform switching occurs during developmental myogenesis of cardiac and skeletal muscle. In vertebrates (humans, rodents, zebrafish), UFD2a-7/7a is expressed only in mature striated muscle. This unique tissue specificity is further validated by the conserved presence of 2 muscle-specific splicing regulatory motifs located in the 3' introns of exons 7 and 7a. UFD2a interacts with VCP/p97, an AAA-type ATPase implicated in processes whose functions appear to be regulated, in part, through their interaction with one or more of 15 previously identified cofactors. UFD2a-7/7a did not interact with VCP/p97 in yeast 2-hybrid experiments, which may allow the ATPase to bind cofactors that facilitate its muscle-specific functions. We conclude that the regulated expression of these UFD2a isoforms most likely imparts divergent functions that are important for myogenisis.
C1 [Mammen, Andrew L.; Mahoney, James A.; Rosen, Antony] Johns Hopkins Univ, Sch Med, Dept Med, Div Rheumatol, Baltimore, MD 21205 USA.
   [Mammen, Andrew L.] Johns Hopkins Univ, Sch Med, Dept Neurol, Baltimore, MD 21205 USA.
   [Badders, Nisha; Taylor, J. Paul] St Jude Childrens Hosp, Dept Dev Neurobiol, Memphis, TN USA.
   [St Germain, Amanda; Spinette, Sarah] Rhode Isl Coll, Dept Biol, Providence, RI 02908 USA.
C3 Johns Hopkins University; Johns Hopkins University; St Jude Children's
   Research Hospital; Rhode Island College
RP Mammen, AL (corresponding author), Johns Hopkins Univ, Sch Med, Dept Med, Div Rheumatol, Baltimore, MD 21205 USA.
EM sspinette@ric.edu
RI Mammen, Andrew/AAF-2885-2021; Taylor, J Paul/N-2482-2018
OI Taylor, J Paul/0000-0002-5794-0349
FU National Institutes of Health [P01HL056091, R37DE012354, R01AR044684,
   R01 AG031587]; National Center for Research Resources (NCRR), a
   component of the National Institutes of Health (NIH) [P20RR016457];
   Office Of The Director; Office of Integrative Activities [1004057]
   Funding Source: National Science Foundation
FX This work was supported by National Institutes of Health grants
   P01HL056091, R37DE012354, R01AR044684, R01 AG031587 and RI-INBRE Grant #
   P20RR016457 from the National Center for Research Resources (NCRR
   http://ncrr.nih.gov/), a component of the National Institutes of Health
   (NIH http://www.nih.gov/). The funders had no role in study design, data
   collection and analysis, decision to publish, or preparation of the
   manuscript.
CR Abu Hatoum O, 1998, MOL CELL BIOL, V18, P5670, DOI 10.1128/MCB.18.10.5670
   Aravind L, 2000, CURR BIOL, V10, pR132, DOI 10.1016/S0960-9822(00)00398-5
   Ardley HC, 2005, ESSAYS BIOCHEM, V41, P15, DOI 10.1042/EB0410015
   Barral JM, 2002, SCIENCE, V295, P669, DOI 10.1126/science.1066648
   Bazzaro M, 2007, AM J PATHOL, V171, P1640, DOI 10.2353/ajpath.2007.070325
   BENIRSCHKE RC, STRUCTURE, V18, P955
   BERNICK EP, BMC CELL BIOL, V11, P70
   Bland CS, 2010, NUCLEIC ACIDS RES, V38, P7651, DOI 10.1093/nar/gkq614
   Brand-Saberi B, 2005, ANN ANAT, V187, P199, DOI 10.1016/j.aanat.2004.12.018
   Campos Y, 2010, PLOS ONE, V5, DOI 10.1371/journal.pone.0009866
   Cao K, 2003, CELL, V115, P355, DOI 10.1016/S0092-8674(03)00815-8
   Cao PR, 2005, INT J BIOCHEM CELL B, V37, P2088, DOI 10.1016/j.biocel.2004.11.010
   Castle JC, 2008, NAT GENET, V40, P1416, DOI 10.1038/ng.264
   COUTEAUX R, 1988, BIOL CELL, V62, P171, DOI 10.1016/0248-4900(88)90034-2
   CUSTER SK, HUM MOL GENET, V19
   Etheridge L, 2002, DEV DYNAM, V224, P457, DOI 10.1002/dvdy.10123
   Guinto JB, 2007, ACTA NEUROPATHOL, V114, P55, DOI 10.1007/s00401-007-0224-7
   Heuze ML, 2008, BLOOD, V112, P5130, DOI 10.1182/blood-2007-12-128744
   Higgins D G, 1994, Methods Mol Biol, V25, P307
   Hoppe T, 2004, CELL, V118, P337, DOI 10.1016/j.cell.2004.07.014
   Hutagalung AH, 2002, J CELL SCI, V115, P3983, DOI 10.1242/jcs.00107
   Janiesch PC, 2007, NAT CELL BIOL, V9, P379, DOI 10.1038/ncb1554
   Johnson JM, 2003, SCIENCE, V302, P2141, DOI 10.1126/science.1090100
   Ju JS., 2010, Human Molecular Genetics, V19, pR38
   Kachur T, 2004, J CELL SCI, V117, P5313, DOI 10.1242/jcs.01389
   Kachur TM, 2008, INT J MOL SCI, V9, P1863, DOI 10.3390/ijms9091863
   Kalsotra A, 2008, P NATL ACAD SCI USA, V105, P20333, DOI 10.1073/pnas.0809045105
   Kaneko C, 2003, BIOCHEM BIOPH RES CO, V300, P297, DOI 10.1016/S0006-291X(02)02834-6
   Kaneko-Oshikawa C, 2005, MOL CELL BIOL, V25, P10953, DOI 10.1128/MCB.25.24.10953-10964.2005
   Kimura K, 2006, GENOME RES, V16, P55, DOI 10.1101/gr.4039406
   Kuang S, 2008, TRENDS MOL MED, V14, P82, DOI 10.1016/j.molmed.2007.12.004
   Kuang S, 2008, CELL STEM CELL, V2, P22, DOI 10.1016/j.stem.2007.12.012
   Ladd AN, 2005, DEV DYNAM, V233, P783, DOI 10.1002/dvdy.20382
   Landsverk ML, 2007, J CELL BIOL, V177, P205, DOI 10.1083/jcb.200607084
   Lecker SH, 2006, J AM SOC NEPHROL, V17, P1807, DOI 10.1681/ASN.2006010083
   Li WQ, 2007, FASEB J, V21, P3606, DOI 10.1096/fj.07-8159com
   Lindon C, 1998, J CELL BIOL, V140, P111, DOI 10.1083/jcb.140.1.111
   Mahoney JA, 2002, BIOCHEM J, V361, P587, DOI 10.1042/0264-6021:3610587
   Matsumoto M, 2004, EMBO J, V23, P659, DOI 10.1038/sj.emboj.7600081
   MCAULIFFE JJ, 1990, CIRC RES, V66, P1204, DOI 10.1161/01.RES.66.5.1204
   McElhinny AS, 2004, J CELL SCI, V117, P3175, DOI 10.1242/jcs.01158
   Ni WM, 2011, J CELL SCI, V124, P3164, DOI 10.1242/jcs.087320
   NORDQUIST KA, BIOCHEMISTRY, V49, P347
   Péault B, 2007, MOL THER, V15, P867, DOI 10.1038/mt.sj.6300145
   Price MG, 2002, J CELL SCI, V115, P4013, DOI 10.1242/jcs.00108
   Ramadan K, 2007, NATURE, V450, P1258, DOI 10.1038/nature06388
   Samson T, 2007, J BIOL CHEM, V282, P15730, DOI 10.1074/jbc.M611197200
   Solomon V, 1996, J BIOL CHEM, V271, P26690, DOI 10.1074/jbc.271.43.26690
   Sorokin AV, 2009, BIOCHEMISTRY-MOSCOW+, V74, P1411, DOI 10.1134/S000629790913001X
   Spinette S, 2004, CELL CYCLE, V3, P1638
   Spinette S, 2006, BIOCHEM BIOPH RES CO, V347, P1103, DOI 10.1016/j.bbrc.2006.06.194
   Srikakulam R, 2008, PLOS ONE, V3, DOI 10.1371/journal.pone.0002137
   Sugnet CW, 2006, PLOS COMPUT BIOL, V2, P22, DOI 10.1371/journal.pcbi.0020004
   Sun L, 2007, ONCOGENE, V26, P441, DOI 10.1038/sj.onc.1209793
   Sun LP, 2005, J BIOL CHEM, V280, P26448, DOI 10.1074/jbc.M500373200
   THOMPSON JD, 1994, NUCLEIC ACIDS RES, V22, P4673, DOI 10.1093/nar/22.22.4673
   TOWNSEND PJ, 1995, J MOL CELL CARDIOL, V27, P2223, DOI 10.1016/S0022-2828(95)91587-7
   Vesa J, 2009, NEUROMUSCULAR DISORD, V19, P766, DOI 10.1016/j.nmd.2009.08.003
   Wang ET, 2008, NATURE, V456, P470, DOI 10.1038/nature07509
   Warren CM, 2004, MECH DEVELOP, V121, P1301, DOI 10.1016/j.mod.2004.07.003
   YAFFE D, 1977, NATURE, V270, P725, DOI 10.1038/270725a0
   YAFFE D, 1977, DIFFERENTIATION, V7, P159, DOI 10.1111/j.1432-0436.1977.tb01507.x
NR 62
TC 10
Z9 12
U1 1
U2 4
PU PUBLIC LIBRARY SCIENCE
PI SAN FRANCISCO
PA 185 BERRY ST, STE 1300, SAN FRANCISCO, CA 94107 USA
SN 1932-6203
J9 PLOS ONE
JI PLoS One
PD DEC 9
PY 2011
VL 6
IS 12
AR e28861
DI 10.1371/journal.pone.0028861
PG 14
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA 866FK
UT WOS:000298365700079
PM 22174917
OA Green Published, Green Submitted, gold
DA 2025-04-10
ER

PT J
AU Sinard, JH
   Stewart, GW
   Stabach, PR
   Argent, AC
   Gilligan, DM
   Morrow, JS
AF Sinard, JH
   Stewart, GW
   Stabach, PR
   Argent, AC
   Gilligan, DM
   Morrow, JS
TI Utilization of an 86 bp exon generates a novel adducin isoform (β4)
   lacking the MARCKS homology domain
SO BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION
LA English
DT Article
DE cytoskeleton; alternative mRNA splicing; actin binding protein; gene
   structure; intron; exon
ID PROTEIN-KINASE-C; CALMODULIN-BINDING DOMAIN; ERYTHROCYTE ADDUCIN;
   ALPHA-ADDUCIN; HYPERTENSIVE RATS; MILAN STRAIN; SPECTRIN; CLONING; GENE;
   PHOSPHORYLATION
AB A novel isoform of P-adducin has been amplified and characterized from a human bone marrow cDNA library (GenBank #U43959). This isoform arises from the insertion of an 86 bp alternatively spliced and previously unrecognized exon (now termed exon 15) within codon 581 of the human red blood cell beta-adducin sequence. This results in an insertion of 28 novel amino acids. The remainder of the red cell beta-adducin mRNA is then translated in a different reading frame, adding an additional 35 novel amino acids prior to the stop codon. This new isoform, thus, replaces beta 1-adducin sequence after residue 580 with a total of 63 new amino acids. Sequences from genomic clones of the human beta-adducin gene show that this alternate exon is flanked by splice consensus sequences and is appropriately located in the genomic map between exons encoding up-stream and down-stream sequences, thus defining a new exon. The COOH-terminus of this new isoform, which we designate beta 4, lacks a 22 amino acid lysine-rich sequence common to both the human red cell alpha- and beta-adducin subunits and homologous to a highly conserved region in MARCKS, a filamentous actin-cross linking protein regulated by protein kinase C and calcium/calmodulin. beta 4-adducin preserves a previously identified calmodulin binding domain. PCR analysis indicates that this new beta-adducin isoform is expressed in fetal brain and liver, bone marrow, and NT-2 (neuroepithelial) cells, but is not detected in several other tissues. We anticipate that this new beta 4 isoform of beta-adducin will display unique and tissue-specific functional properties. (C) 1998 Elsevier Science B.V.
C1 Yale Univ, Sch Med, Dept Pathol, New Haven, CT 06510 USA.
   Univ London Univ Coll, Sch Med, Dept Med, London WC1E 6JJ, England.
   Yale Univ, Sch Med, Dept Internal Med, New Haven, CT 06510 USA.
C3 Yale University; University of London; University College London; UCL
   Medical School; Yale University
RP Morrow, JS (corresponding author), Yale Univ, Sch Med, Dept Pathol, New Haven, CT 06510 USA.
RI Argent, Andrew/J-1605-2019; Stabach, Paul/KMX-3962-2024
OI Stewart, Gordon W/0000-0002-6110-3949
FU Wellcome Trust Funding Source: Medline
CR ADEREM A, 1992, TRENDS BIOCHEM SCI, V17, P438, DOI 10.1016/0968-0004(92)90016-3
   BIANCHI G, 1994, P NATL ACAD SCI USA, V91, P3999, DOI 10.1073/pnas.91.9.3999
   BIANCHI G, 1989, AM J HYPERTENS, V2
   BIANCHI G, 1995, CLIN EXP PHARM PHYSL, V1, pS7
   CASARI G, 1995, HYPERTENSION, V25, P320, DOI 10.1161/01.HYP.25.3.320
   COLEMAN TR, 1989, CELL MOTIL CYTOSKEL, V12, P248, DOI 10.1002/cm.970120406
   DING D, 1993, P NATL ACAD SCI USA, V90, P2512, DOI 10.1073/pnas.90.6.2512
   DONG LQ, 1995, J BIOL CHEM, V270, P25534, DOI 10.1074/jbc.270.43.25534
   GARDNER K, 1987, NATURE, V328, P359, DOI 10.1038/328359a0
   GARDNER K, 1986, J BIOL CHEM, V261, P1339
   GILLIGAN D M, 1991, Journal of Cell Biology, V115, p42A
   GILLIGAN DM, 1997, UNPUB
   GILLIGAN DM, 1994, MOL BIOL CELL, V5, P421
   Goldberg Y. P., 1992, Human Molecular Genetics, V1, P669, DOI 10.1093/hmg/1.9.669
   GRUMONT RJ, 1994, P NATL ACAD SCI USA, V91, P4367, DOI 10.1073/pnas.91.10.4367
   HARTWIG JH, 1992, NATURE, V356, P618, DOI 10.1038/356618a0
   HUGHES CA, 1995, J BIOL CHEM, V270, P18990, DOI 10.1074/jbc.270.32.18990
   JOSHI R, 1990, J BIOL CHEM, V265, P13130
   JOSHI R, 1991, J CELL BIOL, V115, P665, DOI 10.1083/jcb.115.3.665
   KAISER HW, 1989, J CELL BIOL, V109, P557, DOI 10.1083/jcb.109.2.557
   KENNEDY SP, 1991, J CELL BIOL, V115, P267, DOI 10.1083/jcb.115.1.267
   Kuhlman PA, 1996, J BIOL CHEM, V271, P7986, DOI 10.1074/jbc.271.14.7986
   Matsuoka Y, 1996, J BIOL CHEM, V271, P25157, DOI 10.1074/jbc.271.41.25157
   Matsuoka Y., 1995, Molecular Biology of the Cell, V6, p269A
   MISCHE SM, 1987, J CELL BIOL, V105, P2837, DOI 10.1083/jcb.105.6.2837
   MORROW JS, 1997, HDB PHYSIOL 14, P485
   NEGRINI C, 1995, BBA-BIOMEMBRANES, V1236, P207, DOI 10.1016/0005-2736(95)00081-D
   PALFREY HC, 1985, J BIOL CHEM, V260, P6021
   PINTOCORREIA C, 1991, DEV BIOL, V146, P301, DOI 10.1016/0012-1606(91)90232-R
   RINFRET A, 1993, MOL IMMUNOL, V30, P1307, DOI 10.1016/0161-5890(93)90047-F
   SALARDI S, 1989, AM J HYPERTENS, V2, P229, DOI 10.1093/ajh/2.4.229
   SALARDI S, 1988, J HYPERTENS, V64, pS196
   SCARAMUZZINO DA, 1993, P NATL ACAD SCI USA, V90, P3398, DOI 10.1073/pnas.90.8.3398
   Sinard J. H., 1995, Molecular Biology of the Cell, V6, p269A
   SINARD JH, 1994, MOL BIOL CELL S421A, V5
   TAYLOR SAM, 1992, NAT GENET, V2, P223, DOI 10.1038/ng1192-223
   Tisminetzky S, 1995, GENE, V167, P313, DOI 10.1016/0378-1119(95)00591-9
   TRIPODI G, 1991, BIOCHEM BIOPH RES CO, V177, P939, DOI 10.1016/0006-291X(91)90629-L
   WASEEM A, 1988, EUR J BIOCHEM, V178, P563, DOI 10.1111/j.1432-1033.1988.tb14483.x
   YAN GC, 1993, BIOCHEM BIOPH RES CO, V194, P512, DOI 10.1006/bbrc.1993.1849
NR 40
TC 9
Z9 10
U1 0
U2 0
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 0167-4781
J9 BBA-GENE STRUCT EXPR
JI Biochim. Biophys. Acta-Gene Struct. Expression
PD MAR 4
PY 1998
VL 1396
IS 1
BP 57
EP 66
DI 10.1016/S0167-4781(97)00167-X
PG 10
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA ZA346
UT WOS:000072354300010
PM 9524222
OA hybrid
DA 2025-04-10
ER

PT J
AU Zhang, H
   Wang, D
   Li, M
   Plecitá-Hlavatá, L
   D'Alessandro, A
   Tauber, J
   Riddle, S
   Kumar, S
   Flockton, A
   McKeon, BA
   Frid, MG
   Reisz, JA
   Caruso, P
   El Kasmi, KC
   Jezek, P
   Morrell, NW
   Hu, CJ
   Stenmark, KR
AF Zhang, Hui
   Wang, Daren
   Li, Min
   Plecita-Hlavata, Lydie
   D'Alessandro, Angelo
   Tauber, Jan
   Riddle, Suzette
   Kumar, Sushil
   Flockton, Amanda
   McKeon, B. Alexandre
   Frid, Maria G.
   Reisz, Julie A.
   Caruso, Paola
   El Kasmi, Karim C.
   Jezek, Petr
   Morrell, Nicholas W.
   Hu, Cheng-Jun
   Stenmark, Kurt R.
TI Metabolic and Proliferative State of Vascular Adventitial Fibroblasts in
   Pulmonary Hypertension Is Regulated Through a MicroRNA-124/PTBP1
   (Polypyrimidine Tract Binding Protein 1)/Pyruvate Kinase Muscle Axis
SO CIRCULATION
LA English
DT Article
DE hypoxia; metabolism; mitochondria; pyruvate kinase; shikonin; splicing
   factors; TEEP-46
ID CANCER-CELL-GROWTH; PYRUVATE-KINASE; ARTERIAL-HYPERTENSION; INFLAMMATORY
   PHENOTYPE; ISOFORM EXPRESSION; COLORECTAL-CANCER; ROS PRODUCTION;
   COLON-CANCER; INHIBITION; DYSFUNCTION
AB BACKGROUND: An emerging metabolic theory of pulmonary hypertension (PH) suggests that cellular and mitochondrial metabolic dysfunction underlies the pathology of this disease. We and others have previously demonstrated the existence of hyperproliferative, apoptosis-resistant, proinflammatory adventitial fibroblasts from human and bovine hypertensive pulmonary arterial walls (PHFibs) that exhibit constitutive reprogramming of glycolytic and mitochondrial metabolism, accompanied by an increased ratio of glucose catabolism through glycolysis versus the tricarboxylic acid cycle. However, the mechanisms responsible for these metabolic alterations in PH-Fibs remain unknown. We hypothesized that in PH-Fibs microRNA-124 (miR-124) regulates PTBP1 (polypyrimidine tract binding protein 1) expression to control alternative splicing of pyruvate kinase muscle (PKM) isoforms 1 and 2, resulting in an increased PKM2/PKM1 ratio, which promotes glycolysis and proliferation even in aerobic environments.
   METHODS: Pulmonary adventitial fibroblasts were isolated from calves and humans with severe PH (PH-Fibs) and from normal subjects. PTBP1 gene knockdown was achieved via PTBP1-siRNA; restoration of miR-124 was performed with miR-124 mimic. TEPP-46 and shikonin were used to manipulate PKM2 glycolytic function. Histone deacetylase inhibitors were used to treat cells. Metabolic products were determined by mass spectrometry-based metabolomics analyses, and mitochondrial function was analyzed by confocal microscopy and spectrofluorometry.
   RESULTS: We detected an increased PKM2/PKM1 ratio in PH-Fibs compared with normal subjects. PKM2 inhibition reversed the glycolytic status of PH-Fibs, decreased their cell proliferation, and attenuated macrophage interleukin-1 beta expression. Furthermore, normalizing the PKM2/PKM1 ratio in PH-Fibs by miR-124 overexpression or PTBP1 knockdown reversed the glycolytic phenotype (decreased the production of glycolytic intermediates and byproducts, ie, lactate), rescued mitochondrial reprogramming, and decreased cell proliferation. Pharmacological manipulation of PKM2 activity with TEPP-46 and shikonin or treatment with histone deacetylase inhibitors produced similar results.
   CONCLUSIONS: In PH, miR-124, through the alternative splicing factor PTBP1, regulates the PKM2/PKM1 ratio, the overall metabolic, proliferative, and inflammatory state of cells. This PH phenotype can be rescued with interventions at various levels of the metabolic cascade. These findings suggest a more integrated view of vascular cell metabolism, which may open unique therapeutic prospects in targeting the dynamic glycolytic and mitochondrial interactions and between mesenchymal inflammatory cells in PH.
C1 [Zhang, Hui; Wang, Daren; Li, Min; Riddle, Suzette; Kumar, Sushil; Flockton, Amanda; McKeon, B. Alexandre; Frid, Maria G.; Stenmark, Kurt R.] Univ Colorado, Cardiovasc Pulm Res Labs, Dept Pediat, Anschutz Med Campus, Aurora, CO USA.
   [Zhang, Hui; Wang, Daren; Li, Min; Riddle, Suzette; Kumar, Sushil; Flockton, Amanda; McKeon, B. Alexandre; Frid, Maria G.; Stenmark, Kurt R.] Univ Colorado, Cardiovasc Pulm Res Labs, Dept Med, Anschutz Med Campus, Aurora, CO USA.
   [D'Alessandro, Angelo; Reisz, Julie A.] Univ Colorado, Dept Biochem & Mol Genet & Biol Mass Spectrometry, Anschutz Med Campus, Aurora, CO USA.
   [El Kasmi, Karim C.] Univ Colorado, Dept Pediat, Div Gastroenterol Hepatol & Nutr, Anschutz Med Campus, Aurora, CO USA.
   [Hu, Cheng-Jun] Univ Colorado, Dept Craniofacial Biol, Sch Dent Med, Anschutz Med Campus, Aurora, CO USA.
   [Plecita-Hlavata, Lydie; Tauber, Jan; Jezek, Petr] Czech Acad Sci, Dept Mitochondrial Physiol, Inst Physiol, Prague, Czech Republic.
   [Caruso, Paola; Morrell, Nicholas W.] Univ Cambridge, Div Resp Med, Dept Med, Sch Clin Med,Addenbrookes Hosp, Cambridge, England.
C3 University of Colorado System; University of Colorado Anschutz Medical
   Campus; University of Colorado System; University of Colorado Anschutz
   Medical Campus; University of Colorado System; University of Colorado
   Anschutz Medical Campus; University of Colorado System; University of
   Colorado Anschutz Medical Campus; University of Colorado System;
   University of Colorado Anschutz Medical Campus; Czech Academy of
   Sciences; Institute of Physiology of the Czech Academy of Sciences;
   Cambridge University Hospitals NHS Foundation Trust; Addenbrooke's
   Hospital; University of Cambridge
RP Stenmark, KR (corresponding author), Univ Colorado, Pediat, Res 2, Anschutz Med Campus,Campus Box B131, Aurora, CO 80045 USA.
EM kurt.stenmark@ucdenver.edu
RI D'Alessandro, Angelo/AAA-4695-2019; stenmark, kurt/AFI-6776-2022; Jezek,
   Petr/B-9264-2012; Plecita-Hlavata, Lydie/C-1028-2012; Tauber,
   Jan/H-9066-2013
OI Morrell, Nicholas/0000-0001-5700-9792; Jezek, Petr/0000-0002-2720-9395;
   Hu, Cheng-Jun/0000-0003-0985-1285; Plecita-Hlavata,
   Lydie/0000-0003-0759-1731; D'Alessandro, Angelo/0000-0002-2258-6490;
   Tauber, Jan/0000-0002-4711-5716
FU National Institutes of Health [NHLBI P01HL014985, NHLBI T32HL007171,
   NHLBI R01HL114887]; Department of Defense [DoD W81XWH-15-1-0280];
   KONTAKT Czech Ministry of Education [LH11055, LH15071]; Grant Agency of
   Czech Republic [16-04788S]
FX This work was supported in part by National Institutes of Health grants
   NHLBI P01HL014985, NHLBI T32HL007171, and NHLBI R01HL114887; Department
   of Defense grant DoD W81XWH-15-1-0280; KONTAKT grant, LH11055, and
   LH15071 from Czech Ministry of Education; and Grant Agency of Czech
   Republic, No. 16-04788S.
CR Akamata K, 2016, ONCOTARGET, V7, P69321, DOI 10.18632/oncotarget.12504
   Anastasiou D, 2012, NAT CHEM BIOL, V8, P839, DOI 10.1038/NCHEMBIO.1060
   Brown RD, 2013, AM J PHYSIOL-HEART C, V304, pH269, DOI 10.1152/ajpheart.00158.2012
   Caruso P, 2017, CIRCULATION, V136, P2451, DOI 10.1161/CIRCULATIONAHA.117.028034
   Cavasin MA, 2012, CIRC RES, V110, P739, DOI 10.1161/CIRCRESAHA.111.258426
   Chen F, 2016, FREE RADICAL BIO MED, V99, P167, DOI 10.1016/j.freeradbiomed.2016.08.003
   Chen M, 2012, NAT STRUCT MOL BIOL, V19, P346, DOI 10.1038/nsmb.2219
   Chiaradonna F, 2015, ANTIOXID REDOX SIGN, V23, P30, DOI 10.1089/ars.2014.5854
   Christofk HR, 2008, NATURE, V452, P230, DOI 10.1038/nature06734
   Clower CV, 2010, P NATL ACAD SCI USA, V107, P1894, DOI 10.1073/pnas.0914845107
   Cottrill KA, 2013, EUR J CLIN INVEST, V43, P855, DOI 10.1111/eci.12104
   D'Alessandro A, 2018, ANTIOXID REDOX SIGN, V28, P230, DOI 10.1089/ars.2017.7217
   D'Alessandro A, 2015, TRANSFUSION, V55, P1155, DOI 10.1111/trf.12975
   Dayton TL, 2016, EMBO REP, V17, P1721, DOI 10.15252/embr.201643300
   Dlasková A, 2008, INT J BIOCHEM CELL B, V40, P2098, DOI 10.1016/j.biocel.2008.02.007
   El Kasmi KC, 2014, J IMMUNOL, V193, P597, DOI 10.4049/jimmunol.1303048
   Freund-Michel V, 2014, INT J BIOCHEM CELL B, V55, P93, DOI 10.1016/j.biocel.2014.08.012
   Frid MG, 2009, AM J PHYSIOL-LUNG C, V297, pL1059, DOI 10.1152/ajplung.90611.2008
   Frid MG, 2006, AM J PATHOL, V168, P659, DOI 10.2353/ajpath.2006.050599
   Galié N, 2004, CARDIOVASC RES, V61, P227, DOI 10.1016/j.cardiores.2003.11.026
   Galiè N, 2013, J AM COLL CARDIOL, V62, pD60, DOI 10.1016/j.jacc.2013.10.031
   Guzy RD, 2005, CELL METAB, V1, P401, DOI 10.1016/j.cmet.2005.05.001
   Heiden MGV, 2009, SCIENCE, V324, P1029, DOI 10.1126/science.1160809
   Humbert M, 2014, CIRCULATION, V130, P2189, DOI 10.1161/CIRCULATIONAHA.114.006974
   Israelsen WJ, 2015, SEMIN CELL DEV BIOL, V43, P43, DOI 10.1016/j.semcdb.2015.08.004
   Kang K, 2013, J BIOL CHEM, V288, P25414, DOI 10.1074/jbc.M113.460287
   Lemons JMS, 2010, PLOS BIOL, V8, DOI 10.1371/journal.pbio.1000514
   Leopold JA, 2016, INT J MOL SCI, V17, DOI 10.3390/ijms17050761
   Li M, 2016, CIRCULATION, V134, P1105, DOI 10.1161/CIRCULATIONAHA.116.023171
   Li M, 2011, J IMMUNOL, V187, P2711, DOI 10.4049/jimmunol.1100479
   Lunt SY, 2015, MOL CELL, V57, P95, DOI 10.1016/j.molcel.2014.10.027
   Maiellaro K, 2007, CARDIOVASC RES, V75, P640, DOI 10.1016/j.cardiores.2007.06.023
   Majesky MW, 2015, ARTERIOSCL THROM VAS, V35, pE31, DOI 10.1161/ATVBAHA.115.306088
   Meyrick B, J IMMUNOL
   Nemkov T, 2017, RAPID COMMUN MASS SP, V31, P663, DOI 10.1002/rcm.7834
   Olson KA, 2016, TRENDS BIOCHEM SCI, V41, P219, DOI 10.1016/j.tibs.2016.01.002
   Palsson-McDermott EM, 2015, CELL METAB, V21, P65, DOI [10.1016/j.cmet.2014.12.005, 10.1016/j.cmet.2015.01.017]
   Paulin R, 2014, CELL METAB, V20, P827, DOI 10.1016/j.cmet.2014.08.011
   Paulin R, 2014, CIRC RES, V115, P148, DOI 10.1161/CIRCRESAHA.115.301130
   Plecitá-Hlavatá L, 2016, AM J RESP CELL MOL, V55, P47, DOI 10.1165/rcmb.2015-0142OC
   Pullamsettit SS, 2017, AM J RESP CRIT CARE, V195, P425, DOI 10.1164/rccm.201606-1226PP
   Qi W, 2017, NAT MED, V23, P753, DOI 10.1038/nm.4328
   Rafikova O, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0150480
   Schell JC, 2014, MOL CELL, V56, P400, DOI 10.1016/j.molcel.2014.09.026
   Singh Pankaj K, 2011, Mol Cell Pharmacol, V3, P125
   Sprowl-Tanio S, 2016, CANCER METAB, V4, DOI 10.1186/s40170-016-0159-3
   STENMARK KR, 1987, J APPL PHYSIOL, V62, P821, DOI 10.1152/jappl.1987.62.2.821
   Stenmark KR, 2015, J APPL PHYSIOL, V119, P1164, DOI 10.1152/japplphysiol.00283.2015
   Stenmark KR, 2013, ANNU REV PHYSIOL, V75, P23, DOI 10.1146/annurev-physiol-030212-183802
   Sun Y, 2012, ONCOL REP, V28, P1346, DOI 10.3892/or.2012.1958
   Tamada M, 2012, CLIN CANCER RES, V18, P5554, DOI 10.1158/1078-0432.CCR-12-0859
   Taniguchi K, 2015, CANCER LETT, V363, P17, DOI 10.1016/j.canlet.2015.03.026
   Tantini B, 2005, BASIC RES CARDIOL, V100, P131, DOI 10.1007/s00395-004-0504-5
   Wang DR, 2014, CIRC RES, V114, P67, DOI 10.1161/CIRCRESAHA.114.301633
   WARBURG O, 1956, SCIENCE, V123, P309, DOI 10.1126/science.123.3191.309
   West AC, 2014, J CLIN INVEST, V124, P30, DOI 10.1172/JCI69738
   Xie M, 2016, NAT COMMUN, V7, DOI 10.1038/ncomms13280
   Xu WL, 2011, COMPR PHYSIOL, V1, P357, DOI 10.1002/cphy.c090005
   Yang HJ, 2009, INT J CANCER, V124, P2450, DOI 10.1002/ijc.24195
   Zhao L, 2013, CIRCULATION, V128, P1214, DOI 10.1161/CIRCULATIONAHA.113.004136
   Zhao L, 2012, CIRCULATION, V126, P455, DOI 10.1161/CIRCULATIONAHA.112.103176
NR 61
TC 174
Z9 191
U1 1
U2 45
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA TWO COMMERCE SQ, 2001 MARKET ST, PHILADELPHIA, PA 19103 USA
SN 0009-7322
EI 1524-4539
J9 CIRCULATION
JI Circulation
PD DEC 19
PY 2017
VL 136
IS 25
BP 2468
EP +
DI 10.1161/CIRCULATIONAHA.117.028069
PG 41
WC Cardiac & Cardiovascular Systems; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology
GA FR2KW
UT WOS:000418896900012
PM 28972001
OA Green Accepted, Bronze
DA 2025-04-10
ER

PT J
AU Mably, JD
   Mohideen, MAPK
   Burns, CG
   Chen, JN
   Fishman, MC
AF Mably, JD
   Mohideen, MAPK
   Burns, CG
   Chen, JN
   Fishman, MC
TI Heart of glass regulates the concentric growth of the heart in
   zebrafish
SO CURRENT BIOLOGY
LA English
DT Article
ID DANIO-RERIO; CARDIOVASCULAR-SYSTEM; GENE CLOCHE; MUTATION; PROTEIN;
   IDENTIFICATION; TRANSCRIPTION; GASTRULATION; PREDICTION; INDUCTION
AB Background: Patterned growth of vertebrate organs is essential for normal physiological function, but the underlying pathways that govern organotypic growth are not clearly understood. Heart function is critically dependent upon the concentric thickening of the ventricular wall generated by the addition of cells to the myocardium along the axis from the endocardium (inside) to the outside of the chamber. In heart of glass mutant embryos, the number of cells in the myocardium is normal, but they are not added in the concentric direction. As a consequence, the chambers are huge and dysfunctional, and the myocardium remains a single layer.
   Results: To begin to define the factors controlling the concentric growth of cells in the myocardium, we used positional cloning to identify the heart of glass (heg) gene. heg encodes a protein of previously undescribed function, expressed in the endocardial layer of the heart. By alternative splicing, three distinct isoforms are generated, one of which is predicted to be transmembrane and two other secreted. By selective morpholino perturbation, we demonstrate that the transmembrane form is critical for the normal pattern of growth.
   Conclusions: heart of glass encodes a previously uncharacterized endocardial signal that is vital for patterning concentric growth of the heart. Growth of the heart requires addition of myocardial cells along the endocardial-to-myocardial axis. This axis of patterning is driven by heg, a novel transmembrane protein expressed in the endocardium.
C1 Massachusetts Gen Hosp, Cardiovasc Res Ctr, Boston, MA 02129 USA.
   Harvard Univ, Sch Med, Dept Med, Boston, MA 02129 USA.
   Univ Calif Los Angeles, Dept Mol Cell & Dev Biol, Los Angeles, CA 90095 USA.
   Novartis Inst Biomed Res, Cambridge, MA 02139 USA.
C3 Harvard University; Harvard University Medical Affiliates; Massachusetts
   General Hospital; Harvard University; Harvard Medical School; University
   of California System; University of California Los Angeles; Novartis;
   Novartis USA
RP Fishman, MC (corresponding author), Massachusetts Gen Hosp, Cardiovasc Res Ctr, 149 13th St, Boston, MA 02129 USA.
RI Chen, Jau-Nian/AAM-7808-2020
OI Chen, Jau-Nian/0000-0001-8807-3607
FU NHLBI NIH HHS [5R01 HL 49579, 5R01 HL 63206-04, T32 HL007208] Funding
   Source: Medline; NIDDK NIH HHS [5R01 DK 55383] Funding Source: Medline
CR Alexander J, 1998, DEV GENET, V22, P288, DOI 10.1002/(SICI)1520-6408(1998)22:3<288::AID-DVG10>3.3.CO;2-T
   Amsterdam A, 1999, GENE DEV, V13, P2713, DOI 10.1101/gad.13.20.2713
   Chen JN, 1996, DEVELOPMENT, V123, P293
   Draper BW, 2001, GENESIS, V30, P154, DOI 10.1002/gene.1053
   Driever W, 1996, DEVELOPMENT, V123, P37
   Ekker SC, 2000, YEAST, V17, P302, DOI 10.1002/1097-0061(200012)17:4<302::AID-YEA53>3.0.CO;2-#
   Erokhina E L, 1968, Tsitologiia, V10, P1391
   Ewing B, 1998, GENOME RES, V8, P186, DOI 10.1101/gr.8.3.186
   Ewing B, 1998, GENOME RES, V8, P175, DOI 10.1101/gr.8.3.175
   Garrity DM, 2002, DEVELOPMENT, V129, P4635
   Gilmour Darren T., 2002, P121
   Gordon D, 1998, GENOME RES, V8, P195, DOI 10.1101/gr.8.3.195
   Haffter P, 1996, DEVELOPMENT, V123, P1
   Hammerschmidt M, 1996, DEVELOPMENT, V123, P143
   Hansen JE, 1998, GLYCOCONJUGATE J, V15, P115, DOI 10.1023/A:1006960004440
   HOFMANN K, 1993, BIOL CHEM HOPPESEYLE, V347, P166
   Horne-Badovinac S, 2001, CURR BIOL, V11, P1492, DOI 10.1016/S0960-9822(01)00458-4
   Hu N, 2000, ANAT REC, V260, P148, DOI 10.1002/1097-0185(20001001)260:2<148::AID-AR50>3.0.CO;2-X
   JOWETT T, 1994, TRENDS GENET, V10, P73, DOI 10.1016/0168-9525(94)90220-8
   Keegan BR, 2002, DEVELOPMENT, V129, P1623
   Kikuchi Y, 2000, GENE DEV, V14, P1279
   Kikuchi Y, 2001, GENE DEV, V15, P1493, DOI 10.1101/gad.892301
   Kikuno R, 2002, NUCLEIC ACIDS RES, V30, P166, DOI 10.1093/nar/30.1.166
   Knapik EW, 1996, DEVELOPMENT, V123, P451
   Kupperman E, 2000, NATURE, V406, P192, DOI 10.1038/35018092
   Li FQ, 1996, J MOL CELL CARDIOL, V28, P1737, DOI 10.1006/jmcc.1996.0163
   Liao W, 1997, DEVELOPMENT, V124, P381
   MEYER D, 1995, NATURE, V378, P386, DOI 10.1038/378386a0
   MICHELMORE RW, 1991, P NATL ACAD SCI USA, V88, P9828, DOI 10.1073/pnas.88.21.9828
   Nielsen H, 1999, PROTEIN ENG, V12, P3, DOI 10.1093/protein/12.1.3
   Parker L, 1999, DEVELOPMENT, V126, P2643
   Peterson RT, 2001, CURR BIOL, V11, P1481, DOI 10.1016/S0960-9822(01)00482-1
   Ramsdell AF, 1997, DEV BIOL, V188, P64, DOI 10.1006/dbio.1997.8637
   RANDALL DJ, 2002, NAT MED, V8, P850
   Reifers F, 1998, DEVELOPMENT, V125, P2381
   Rottbauer W, 2002, CELL, V111, P661, DOI 10.1016/S0092-8674(02)01112-1
   Rottbauer W, 2001, DEV CELL, V1, P265, DOI 10.1016/S1534-5807(01)00023-5
   RYCHTEROVA V, 1978, Folia Morphologica (Prague), V26, P131
   RYCHTEROVA V, 1971, Folia Morphologica (Prague), V19, P262
   Sehnert AJ, 2002, NAT GENET, V31, P106, DOI 10.1038/ng875
   SHU X, 2003, IN PRESS DEVELOPMENT
   Soonpaa MH, 1996, AM J PHYSIOL-HEART C, V271, pH2183
   Stainier DYR, 1996, DEVELOPMENT, V123, P285
   THOMPSON JD, 1994, NUCLEIC ACIDS RES, V22, P4673, DOI 10.1093/nar/22.22.4673
   Walsh EC, 2001, SCIENCE, V293, P1670, DOI 10.1126/science.293.5535.1670
   WARGA RM, 1990, DEVELOPMENT, V108, P569
   Xu XL, 2002, NAT GENET, V30, P205, DOI 10.1038/ng816
   Yelon D, 2000, DEVELOPMENT, V127, P2573
   Yelon D, 1999, DEV BIOL, V214, P23, DOI 10.1006/dbio.1999.9406
   Zhong TP, 2000, SCIENCE, V287, P1820, DOI 10.1126/science.287.5459.1820
NR 50
TC 210
Z9 251
U1 0
U2 15
PU CELL PRESS
PI CAMBRIDGE
PA 1100 MASSACHUSETTS AVE, CAMBRIDGE, MA 02138 USA
SN 0960-9822
J9 CURR BIOL
JI Curr. Biol.
PD DEC 16
PY 2003
VL 13
IS 24
BP 2138
EP 2147
DI 10.1016/j.cub.2003.11.055
PG 10
WC Biochemistry & Molecular Biology; Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Life Sciences & Biomedicine - Other
   Topics; Cell Biology
GA 756GB
UT WOS:000187456500020
PM 14680629
OA Bronze
DA 2025-04-10
ER

PT J
AU Fang, XF
   Poulsen, R
   Zhao, L
   Wang, JJ
   Rivkees, SA
   Wendler, CC
AF Fang, Xiefan
   Poulsen, Ryan
   Zhao, Lu
   Wang, Jingjing
   Rivkees, Scott A.
   Wendler, Christopher C.
TI Knockdown of DNA methyltransferase 1 reduces DNA methylation and alters
   expression patterns of cardiac genes in embryonic cardiomyocytes
SO FEBS OPEN BIO
LA English
DT Article
DE DNA methylation; DNMT1; embryonic cardiomyocyte; gene expression
ID ZEBRAFISH; CELLS; EPIGENETICS; INHIBITION; EXPOSURE; STAGE
AB We previously found that DNA methyltransferase 3a (DNMT3a) plays an important role in regulating embryonic cardiomyocyte gene expression, morphology, and function. In this study, we investigated the role of the most abundant DNMT in mammalian cells, DNMT1, in these processes. It is known that DNMT1 is essential for embryonic development, during which it is involved in regulating cardiomyocyte DNA methylation and gene expression. We used siRNA to knock down DNMT1 expression in primary cultures of mouse embryonic cardiomyocytes. Immunofluorescence staining and multielectrode array were, respectively, utilized to evaluate cardiomyocyte growth and electrophysiology. RNA sequencing (RNA-Seq) and multiplex bisulfite sequencing were, respectively, performed to examine gene expression and promoter methylation. At 72 h post-transfection, reduction of DNMT1 expression decreased the number and increased the size of embryonic cardiomyocytes. Beat frequency and the amplitude of field action potentials were decreased by DNMT1 siRNA. RNA-Seq analysis identified 801 up-regulated genes and 494 down-regulated genes in the DNMT1 knockdown cells when compared to controls. Pathway analysis of the differentially expressed genes revealed pathways that were associated with cell death and survival, cell morphology, cardiac function, and cardiac disease. Alternative splicing analysis identified 929 differentially expressed exons, including 583 up-regulated exons and 308 down-regulated exons. Moreover, decreased methylation levels were found in the promoters of cardiac genes Myh6, Myh7, Myh7b, Tnnc1, Tnni3, Tnnt2, Nppa, Nppb, mef2c, mef2d, Camta2, Cdkn1A, and Cdkn1C. Of these 13 genes, 6 (Myh6, Tnnc1, Tnni3, Tnnt2, Nppa, Nppb) and 1 (Cdkn1C) had increased or decreased gene expression, respectively. Altogether, these data show that DNMT1 is important in embryonic cardiomyocytes by regulating DNA methylation, gene expression, gene splicing, and cell function.
C1 [Fang, Xiefan; Poulsen, Ryan; Rivkees, Scott A.; Wendler, Christopher C.] Univ Florida, Child Hlth Res Inst, Dept Pediat, Coll Med, Gainesville, FL USA.
   [Fang, Xiefan; Zhao, Lu; Wang, Jingjing] Charles River Labs Inc, 6995 Longley Lane, Reno, NV 89511 USA.
C3 State University System of Florida; University of Florida; Charles River
   Laboratories
RP Fang, XF (corresponding author), Charles River Labs Inc, 6995 Longley Lane, Reno, NV 89511 USA.
EM xiefan.fang@crl.com
RI wendler, chris/KHW-6239-2024
FU Children's Miracle Network
FX We thank John Wang-Hu for technical assistance and Children's Miracle
   Network for funding.
CR Akalin A, 2012, GENOME BIOL, V13, DOI [10.1186/gb-2012-13-10-R87, 10.1186/gb-2012-13-10-r87]
   Anders S, 2015, BIOINFORMATICS, V31, P166, DOI 10.1093/bioinformatics/btu638
   Anders S, 2012, GENOME RES, V22, P2008, DOI 10.1101/gr.133744.111
   Chang CP, 2012, ANNU REV PHYSIOL, V74, P41, DOI 10.1146/annurev-physiol-020911-153242
   Denis H, 2011, EMBO REP, V12, P647, DOI 10.1038/embor.2011.110
   Doyle MJ, 2015, STEM CELL REV REP, V11, P710, DOI 10.1007/s12015-015-9596-6
   Du L, 2018, HUM EXP TOXICOL, V37, P475, DOI 10.1177/0960327117710535
   Evans SM, 2010, CIRC RES, V107, P1428, DOI 10.1161/CIRCRESAHA.110.227405
   Fang XF, 2016, FASEB J, V30, P3238, DOI 10.1096/fj.201600346R
   Fang XF, 2015, TOXICOL SCI, V146, P395, DOI 10.1093/toxsci/kfv105
   Fang XF, 2014, AM J PHYSIOL-REG I, V307, pR1471, DOI 10.1152/ajpregu.00307.2014
   Fang XF, 2013, ENVIRON TOXICOL PHAR, V36, P40, DOI 10.1016/j.etap.2013.02.014
   Faulk C, 2011, EPIGENETICS-US, V6, P791, DOI 10.4161/epi.6.7.16209
   Flores K, 2012, BMC GENOMICS, V13, DOI 10.1186/1471-2164-13-480
   Gilsbach R, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms6288
   Gu Y, 2014, PROTEIN CELL, V5, P59, DOI 10.1007/s13238-013-0016-x
   Guerrero-Bosagna C, 2012, MOL CELL ENDOCRINOL, V354, P3, DOI 10.1016/j.mce.2011.10.004
   Haas J, 2013, EMBO MOL MED, V5, P413, DOI 10.1002/emmm.201201553
   Huang DW, 2009, NAT PROTOC, V4, P44, DOI 10.1038/nprot.2008.211
   Huang MH, 2019, PHARMACOL RES, V139, P50, DOI 10.1016/j.phrs.2018.10.015
   Inoue A, 2011, SCIENCE, V334, P194, DOI 10.1126/science.1212483
   Kao YH, 2013, CLIN EXP PHARMACOL P, V40, P379, DOI 10.1111/1440-1681.12089
   Kass SU, 1997, TRENDS GENET, V13, P444, DOI 10.1016/S0168-9525(97)01268-7
   Koczor CA, 2013, PHYSIOL GENOMICS, V45, P597, DOI 10.1152/physiolgenomics.00013.2013
   Krueger F, 2011, BIOINFORMATICS, V27, P1571, DOI 10.1093/bioinformatics/btr167
   Lei H, 1996, DEVELOPMENT, V122, P3195
   Lin NN, 2014, FEBS J, V281, P2088, DOI 10.1111/febs.12764
   Love MI, 2014, GENOME BIOL, V15, DOI 10.1186/s13059-014-0550-8
   McCulley DJ, 2012, CURR TOP DEV BIOL, V100, P253, DOI 10.1016/B978-0-12-387786-4.00008-7
   Movassagh M, 2011, CIRCULATION, V124, P2411, DOI 10.1161/CIRCULATIONAHA.111.040071
   Movassagh M, 2010, PLOS ONE, V5, DOI 10.1371/journal.pone.0008564
   Nilsson E, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0036129
   O'Neill KM, 2018, EPIGENET CHROMATIN, V11, DOI 10.1186/s13072-018-0182-4
   Okano M, 1999, CELL, V99, P247, DOI 10.1016/S0092-8674(00)81656-6
   Ordovás JM, 2010, NAT REV CARDIOL, V7, P510, DOI 10.1038/nrcardio.2010.104
   Parfett CL, 2017, INT J MOL SCI, V18, DOI 10.3390/ijms18061179
   Robinson MD, 2010, BIOINFORMATICS, V26, P139, DOI 10.1093/bioinformatics/btp616
   Santos MS, 2012, BEST PRACT RES CL EN, V26, P581, DOI 10.1016/j.beem.2012.03.003
   Senyildiz M, 2017, TOXICOL IN VITRO, V44, P313, DOI 10.1016/j.tiv.2017.07.028
   Sharma P, 2008, DNA CELL BIOL, V27, P357, DOI 10.1089/dna.2007.0694
   Sharma P, 2014, GENE, V541, P31, DOI 10.1016/j.gene.2014.02.034
   Shukla S, 2011, NATURE, V479, P74, DOI 10.1038/nature10442
   Siedner S, 2003, J PHYSIOL-LONDON, V548, P493, DOI 10.1113/JPHYSIOL.2002.036509
   Sim CB, 2015, FASEB J, V29, P1329, DOI 10.1096/fj.14-264093
   Skinner MK, 2012, GENOME BIOL, V13, DOI [10.1186/gb-2012-13-10-R91, 10.1186/gb-2012-13-10-r91]
   Stenzig J, 2018, J MOL CELL CARDIOL, V120, P53, DOI 10.1016/j.yjmcc.2018.05.012
   Sun C, 2018, CURR OPIN PHYSIOL, V1, P123, DOI 10.1016/j.cophys.2017.09.002
   Szyf M, 2011, EPIGENETICS-US, V6, P971, DOI 10.4161/epi.6.8.16793
   Szyf M, 2011, TOXICOL SCI, V120, P235, DOI 10.1093/toxsci/kfr024
   Wamstad JA, 2012, CELL, V151, P206, DOI 10.1016/j.cell.2012.07.035
   Wu TT, 2020, LAB INVEST, V100, P974, DOI 10.1038/s41374-020-0402-y
   Xu SH, 2014, CURR PHARM DESIGN, V20, P1881, DOI 10.2174/13816128113199990527
   Ying AK, 2000, CARDIOVASC RES, V46, P172, DOI 10.1016/S0008-6363(00)00004-3
   Yun Y, 2019, SCI TOTAL ENVIRON, V660, P1602, DOI 10.1016/j.scitotenv.2018.12.476
   Zhou YP, 2012, BMC GENOMICS, V13, DOI 10.1186/1471-2164-13-123
NR 55
TC 8
Z9 8
U1 0
U2 10
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 2211-5463
J9 FEBS OPEN BIO
JI FEBS Open Bio
PD AUG
PY 2021
VL 11
IS 8
BP 2364
EP 2382
DI 10.1002/2211-5463.13252
EA JUL 2021
PG 19
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA TT5VV
UT WOS:000677220300001
PM 34235895
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Carrier, L
   Mearini, G
   Stathopoulou, K
   Cuello, F
AF Carrier, Lucie
   Mearini, Giulia
   Stathopoulou, Konstantina
   Cuello, Friederike
TI Cardiac myosin-binding protein C (MYBPC3) in cardiac
   pathophysiology
SO GENE
LA English
DT Review
DE MYBPC3; Cardiac myosin-binding protein C; Cardiomyopathies; Hypertrophy
   postranslational modifications; Gene therapy
ID FAMILIAL HYPERTROPHIC CARDIOMYOPATHY; UBIQUITIN-PROTEASOME SYSTEM;
   LEFT-VENTRICULAR NONCOMPACTION; MESSENGER-RNA DECAY; SPLICE DONOR SITE;
   KINASE-A; CMYBP-C; SARCOMERIC CARDIOMYOPATHIES; DIASTOLIC DYSFUNCTION;
   SUDDEN-DEATH
AB More than 350 individual MYPBC3 mutations have been identified in patients with inherited hypertrophic cardiomyopathy (HCM), thus representing 40-50% of all HCM mutations, making it the most frequently mutated gene in HCM. HCM is considered a disease of the sarcomere and is characterized by left ventricular hypertrophy, myocyte disarray and diastolic dysfunction. MYBPC3 encodes for the thick filament associated protein cardiac myosin-binding protein C (cMyBP-C), a signaling node in cardiac myocytes that contributes to the maintenance of sarcomeric structure and regulation of contraction and relaxation.
   This review aims to provide a succinct overview of how mutations in MYBPC3 are considered to affect the physiological function of cMyBP-C, thus causing the deleterious consequences observed in HCM patients. Importantly, recent advances to causally treat HCM by repairing MYBPC3 mutations by gene therapy are discussed here, providing a promising alternative to heart transplantation for patients with a fatal form of neonatal cardiomyopathy due to bi-allelic truncating MYBPC3 mutations. (C) 2015 Elsevier B.V. All rights reserved.
C1 Univ Med Ctr Hamburg Eppendorf, Dept Expt Pharmacol & Toxicol, Cardiovasc Res Ctr, D-20246 Hamburg, Germany.
   DZHK German Ctr Cardiovasc Res, Hamburg, Germany.
C3 Berlin Institute of Health; Free University of Berlin; Humboldt
   University of Berlin; Charite Universitatsmedizin Berlin; University of
   Hamburg; University Medical Center Hamburg-Eppendorf; German Centre for
   Cardiovascular Research
RP Carrier, L (corresponding author), Univ Med Ctr Hamburg Eppendorf, Dept Expt Pharmacol & Toxicol, Martinistr 52, D-20246 Hamburg, Germany.
EM l.carrier@uke.de
RI Mearini, Giulia/KCL-3068-2024; Cuello, Friederike/A-9642-2016; Carrier,
   Lucie/HLX-3022-2023; Stathopoulou, Konstantina/H-5684-2019
OI Stathopoulou, Konstantina/0000-0002-3746-3055; Cuello,
   Friederike/0000-0003-1612-1715
FU National Institutes of Health [GM089820]; Elsevier, the publisher of
   GENE; DZHK (German Center for Cardiovascular Research); German Ministry
   of Research and Education (BMBF); Association Institut de Myologie
   (Paris); Deutsche Forschungsgemeinschaft [CU 53/2-1]
FX This review and the corresponding Gene Wiki article are written as part
   of the Gene Wiki. Review series-a series resulting from a collaboration
   between the journal GENE and the Gene Wiki Initiative. The Gene Wiki
   Initiative is supported by the National Institutes of Health (GM089820).
   Additional support for Gene Wiki Reviews is provided by Elsevier, the
   publisher of GENE. This work was supported by the DZHK (German Center
   for Cardiovascular Research), the German Ministry of Research and
   Education (BMBF), the Association Institut de Myologie (Paris), a grant
   awarded to F. Cuello by the Deutsche Forschungsgemeinschaft (CU 53/2-1).
   The authors apologize that they have not been able to mention every
   important study in this field due to space constraints.
CR Ababou A, 2007, J BIOL CHEM, V282, P9204, DOI 10.1074/jbc.M610899200
   Adalsteinsdottir B, 2014, CIRCULATION, V130, P1158, DOI 10.1161/CIRCULATIONAHA.114.011207
   Aryal B, 2014, P NATL ACAD SCI USA, V111, P2011, DOI 10.1073/pnas.1321783111
   Bahrudin U, 2008, J MOL BIOL, V384, P896, DOI 10.1016/j.jmb.2008.09.070
   Bardswell SC, 2012, J MUSCLE RES CELL M, V33, P53, DOI 10.1007/s10974-011-9276-3
   Bardswell SC, 2010, J BIOL CHEM, V285, P5674, DOI 10.1074/jbc.M109.066456
   Barefield D, 2015, J MOL CELL CARDIOL, V79, P234, DOI 10.1016/j.yjmcc.2014.11.018
   Barefield D, 2010, J MOL CELL CARDIOL, V48, P866, DOI 10.1016/j.yjmcc.2009.11.014
   Behrens-Gawlik V, 2014, PFLUG ARCH EUR J PHY, V466, P215, DOI 10.1007/s00424-013-1409-7
   BONNE G, 1995, NAT GENET, V11, P438, DOI 10.1038/ng1295-438
   Brennan JP, 2006, J BIOL CHEM, V281, P21827, DOI 10.1074/jbc.M603952200
   Brickson S, 2007, AM J PHYSIOL-HEART C, V292, pH1747, DOI 10.1152/ajpheart.01037.2006
   Calore C, 2015, J MED GENET, V52, P338, DOI 10.1136/jmedgenet-2014-102923
   Carrier L, 1998, TRENDS CARDIOVAS MED, V8, P151, DOI 10.1016/S1050-1738(97)00144-8
   CARRIER L, 1993, NAT GENET, V4, P311, DOI 10.1038/ng0793-311
   Carrier L, 2004, CARDIOVASC RES, V63, P293, DOI 10.1016/j.cardiores.2004.04.009
   Carrier L, 1997, CIRC RES, V80, P427, DOI 10.1161/01.res.0000435859.24609.b3
   Carrier L, 2010, CARDIOVASC RES, V85, P330, DOI 10.1093/cvr/cvp247
   Cazorla O, 2006, CARDIOVASC RES, V69, P370, DOI 10.1016/j.cardiores.2005.11.009
   Chen PP, 2010, J GEN PHYSIOL, V136, P615, DOI 10.1085/jgp.201010448
   Christiaans I, 2010, NETH HEART J, V18, P248, DOI 10.1007/BF03091771
   Copeland O, 2010, J MOL CELL CARDIOL, V49, P1003, DOI 10.1016/j.yjmcc.2010.09.007
   Cuello F, 2011, J BIOL CHEM, V286, P5300, DOI 10.1074/jbc.M110.202713
   Dalle-Donne I, 2008, ANTIOXID REDOX SIGN, V10, P445, DOI 10.1089/ars.2007.1716
   Dellefave LM, 2009, CIRC-CARDIOVASC GENE, V2, P442, DOI 10.1161/CIRCGENETICS.109.861955
   Deprez RHL, 2006, J MED GENET, V43, P829, DOI 10.1136/jmg.2005.040329
   Dhandapany PS, 2009, NAT GENET, V41, P187, DOI 10.1038/ng.309
   Ding QR, 2014, CIRC RES, V115, P488, DOI 10.1161/CIRCRESAHA.115.304351
   Dirkx E, 2012, AM J PHYSIOL-HEART C, V303, pH323, DOI 10.1152/ajpheart.00749.2011
   Doudna JA, 2014, SCIENCE, V346, P1077, DOI 10.1126/science.1258096
   Duncker D J., 2015, Cardiovascular research
   El-Armouche A, 2007, J MOL CELL CARDIOL, V43, P223, DOI 10.1016/j.yjmcc.2007.05.003
   Elliott PM, 2014, EUR HEART J, V35, P2733, DOI 10.1093/eurheartj/ehu284
   Eschenhagen T, 2015, CARDIOVASC RES, V105, P424, DOI 10.1093/cvr/cvv017
   Fert-Bober J, 2014, PROTEOM CLIN APPL, V8, P522, DOI 10.1002/prca.201400013
   Flashman E, 2004, CIRC RES, V94, P1279, DOI 10.1161/01.RES.0000127175.21818.C2
   Fougerousse F, 1998, CIRC RES, V82, P130
   Fraysse B, 2012, J MOL CELL CARDIOL, V52, P1299, DOI 10.1016/j.yjmcc.2012.03.009
   García-Castro M, 2005, INT J CARDIOL, V102, P501, DOI 10.1016/j.ijcard.2004.05.060
   GAUTEL M, 1995, EMBO J, V14, P1952, DOI 10.1002/j.1460-2075.1995.tb07187.x
   Ge Y, 2009, P NATL ACAD SCI USA, V106, P12658, DOI 10.1073/pnas.0813369106
   Gedicke-Hornung C, 2013, EMBO MOL MED, V5, P1128, DOI 10.1002/emmm.201202168
   GEISTERFERLOWRANCE AAT, 1990, CELL, V62, P999, DOI 10.1016/0092-8674(90)90274-I
   Girolami F, 2006, J CARDIOVASC MED, V7, P601, DOI 10.2459/01.JCM.0000237908.26377.d6
   Govindan S, 2012, J MUSCLE RES CELL M, V33, P17, DOI 10.1007/s10974-012-9292-y
   Goyenvalle A, 2004, SCIENCE, V306, P1796, DOI 10.1126/science.1104297
   Gruen M, 1999, J MOL BIOL, V286, P933, DOI 10.1006/jmbi.1998.2522
   Gupta MK, 2014, PFLUG ARCH EUR J PHY, V466, P231, DOI 10.1007/s00424-013-1377-y
   Haas J., 2014, Eur Heart J
   Hammond SM, 2011, TRENDS GENET, V27, P196, DOI 10.1016/j.tig.2011.02.004
   Han L, 2014, CARDIOVASC RES, V104, P258, DOI 10.1093/cvr/cvu205
   Harris SP, 2004, CIRC RES, V95, P930, DOI 10.1161/01.RES.0000147312.02673.56
   Harris SP, 2002, CIRC RES, V90, P594, DOI 10.1161/01.RES.0000012222.70819.64
   HARTZELL HC, 1984, J BIOL CHEM, V259, P5587
   HARTZELL HC, 1982, J BIOL CHEM, V257, P2111
   Haworth RS, 2004, CIRC RES, V95, P1091, DOI 10.1161/01.RES.0000149299.34793.3c
   Ho CY, 2015, CARDIOVASC RES, V105, P397, DOI 10.1093/cvr/cvv025
   Ho CY, 2009, CIRC-CARDIOVASC GENE, V2, P314, DOI 10.1161/CIRCGENETICS.109.862128
   Hoedemaekers YM, 2010, CIRC-CARDIOVASC GENE, V3, P232, DOI 10.1161/CIRCGENETICS.109.903898
   HOFMANN PA, 1991, J GEN PHYSIOL, V97, P1141, DOI 10.1085/jgp.97.6.1141
   Hsu PD, 2014, CELL, V157, P1262, DOI 10.1016/j.cell.2014.05.010
   Ingles J, 2005, J MED GENET, V42, DOI 10.1136/jmg.2005.033886
   Jääskeläinen P, 2004, ANN MED, V36, P23, DOI 10.1080/07853890310017161
   Jeong EM, 2013, J MOL CELL CARDIOL, V56, P44, DOI 10.1016/j.yjmcc.2012.12.003
   Kampourakis T, 2014, P NATL ACAD SCI USA, V111, P18763, DOI 10.1073/pnas.1413922112
   Kohr MJ, 2011, AM J PHYSIOL-HEART C, V300, pH1327, DOI 10.1152/ajpheart.00997.2010
   Korte FS, 2003, CIRC RES, V93, P752, DOI 10.1161/01.RES.0000096363.85588.9A
   Kubo T, 2005, J AM COLL CARDIOL, V46, P1737, DOI 10.1016/j.jacc.2005.05.087
   Kulikovskaya I, 2003, J GEN PHYSIOL, V122, P761, DOI 10.1085/jgp.200308941
   Kunst G, 2000, CIRC RES, V86, P51, DOI 10.1161/01.RES.86.1.51
   Kuster DWD, 2013, CIRC RES, V112, P633, DOI 10.1161/CIRCRESAHA.112.275602
   Lan F, 2013, CELL STEM CELL, V12, P101, DOI 10.1016/j.stem.2012.10.010
   Long CZ, 2014, SCIENCE, V345, P1184, DOI 10.1126/science.1254445
   Lovelock JD, 2012, CIRC RES, V110, P841, DOI 10.1161/CIRCRESAHA.111.258251
   Luther PK, 2008, J MOL BIOL, V384, P60, DOI 10.1016/j.jmb.2008.09.013
   Luther PK, 2011, P NATL ACAD SCI USA, V108, P11423, DOI 10.1073/pnas.1103216108
   Maron BJ, 2012, HEART RHYTHM, V9, P57, DOI 10.1016/j.hrthm.2011.08.009
   MARON BJ, 1995, CIRCULATION, V92, P785, DOI 10.1161/01.CIR.92.4.785
   Marston S, 2012, J MUSCLE RES CELL M, V33, P75, DOI 10.1007/s10974-011-9268-3
   Marston S, 2009, CIRC RES, V105, P219, DOI 10.1161/CIRCRESAHA.109.202440
   Marziliano N, 2012, NEONATOLOGY, V102, P254, DOI 10.1159/000339847
   McClellan G, 2001, BIOPHYS J, V81, P1083, DOI 10.1016/S0006-3495(01)75765-7
   Mearini G, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms6515
   Mearini G, 2013, MOL THER-NUCL ACIDS, V2, DOI 10.1038/mtna.2013.31
   Mearini G, 2008, BBA-MOL BASIS DIS, V1782, P749, DOI 10.1016/j.bbadis.2008.06.009
   Meurs KM, 2005, HUM MOL GENET, V14, P3587, DOI 10.1093/hmg/ddi386
   Michels M, 2009, JACC-CARDIOVASC IMAG, V2, P58, DOI 10.1016/j.jcmg.2008.08.003
   Mohamed AS, 1998, ARCH BIOCHEM BIOPHYS, V358, P313, DOI 10.1006/abbi.1998.0857
   Moolman JA, 2000, CIRCULATION, V101, P1396, DOI 10.1161/01.CIR.101.12.1396
   Morita H, 2008, NEW ENGL J MED, V358, P1899, DOI 10.1056/NEJMoa075463
   Moss RL, 2015, CIRC RES, V116, P183, DOI 10.1161/CIRCRESAHA.116.300561
   Mun JY, 2014, P NATL ACAD SCI USA, V111, P2170, DOI 10.1073/pnas.1316001111
   Mun JY, 2011, J MOL BIOL, V410, P214, DOI 10.1016/j.jmb.2011.05.010
   Nanni L, 2003, BIOCHEM BIOPH RES CO, V309, P391, DOI 10.1016/j.bbrc.2003.08.014
   Niimura H, 1998, NEW ENGL J MED, V338, P1248, DOI 10.1056/NEJM199804303381802
   Olivotto I, 2015, CARDIOVASC RES, V105, P409, DOI 10.1093/cvr/cvv024
   Ortiz MF, 2009, REV ESP CARDIOL, V62, P572, DOI 10.1016/S0300-8932(09)71039-5
   Otsuka H, 2012, CIRC J, V76, P453, DOI 10.1253/circj.CJ-11-0876
   Patel BG, 2013, FRONT PHYSIOL, V4, DOI 10.3389/fphys.2013.00336
   Pfuhl M, 2012, J MUSCLE RES CELL M, V33, P83, DOI 10.1007/s10974-012-9291-z
   Pohlmann L, 2007, CIRC RES, V101, P928, DOI 10.1161/CIRCRESAHA.107.158774
   Predmore JM, 2010, CIRCULATION, V121, P997, DOI 10.1161/CIRCULATIONAHA.109.904557
   Previs MJ, 2015, SCI ADV, V1, DOI 10.1126/sciadv.1400205
   Probst S, 2011, CIRC-CARDIOVASC GENE, V4, P367, DOI 10.1161/CIRCGENETICS.110.959270
   Ran FA, 2013, NAT PROTOC, V8, P2281, DOI 10.1038/nprot.2013.143
   Razumova MV, 2006, J BIOL CHEM, V281, P35846, DOI 10.1074/jbc.M606949200
   Richard P, 2003, CIRCULATION, V107, P2227, DOI 10.1161/01.CIR.0000066323.15244.54
   Rottbauer W, 1997, J CLIN INVEST, V100, P475, DOI 10.1172/JCI119555
   Rybakova IN, 2011, J BIOL CHEM, V286, P2008, DOI 10.1074/jbc.M110.170605
   Sadayappan S, 2005, CIRC RES, V97, P1156, DOI 10.1161/01.RES.0000190605.79013.4d
   Sadayappan S, 2006, P NATL ACAD SCI USA, V103, P16918, DOI 10.1073/pnas.0607069103
   Sadayappan Sakthivel, 2012, Biophys Rev, V4, P93, DOI 10.1007/s12551-012-0067-x
   Sadayappan S, 2011, CIRC RES, V109, P141, DOI 10.1161/CIRCRESAHA.111.242560
   Saltzman AJ, 2010, CIRC RES, V106, P1549, DOI 10.1161/CIRCRESAHA.109.216291
   Sarikas A, 2005, CARDIOVASC RES, V66, P33, DOI 10.1016/j.cardiores.2005.01.004
   Schaefer E, 2014, EUR J MED GENET, V57, P129, DOI 10.1016/j.ejmg.2014.02.015
   Schlossarek S, 2014, J MOL CELL CARDIOL, V71, P25, DOI 10.1016/j.yjmcc.2013.12.016
   Schlossarek S, 2012, J MUSCLE RES CELL M, V33, P5, DOI 10.1007/s10974-011-9273-6
   Schlossarek S, 2012, BASIC RES CARDIOL, V107, DOI 10.1007/s00395-011-0235-3
   Schlossarek S, 2011, J MOL CELL CARDIOL, V50, P613, DOI 10.1016/j.yjmcc.2011.01.014
   Sequeira V, 2013, CIRC RES, V112, P1491, DOI 10.1161/CIRCRESAHA.111.300436
   Stelzer JE, 2006, CIRC RES, V98, P1212, DOI 10.1161/01.RES.0000219863.94390.ce
   Stelzer JE, 2006, BIOPHYS J, V90, P4119, DOI 10.1529/biophysj.105.078147
   Stöhr A, 2013, J MOL CELL CARDIOL, V63, P189, DOI 10.1016/j.yjmcc.2013.07.011
   Sun N, 2012, SCI TRANSL MED, V4, DOI 10.1126/scitranslmed.3003552
   Tajsharghi H, 2010, J MED GENET, V47, P575, DOI 10.1136/jmg.2009.072710
   Tanaka A, 2014, J AM HEART ASSOC, V3, DOI 10.1161/JAHA.114.001263
   Teirlinck CH, 2012, BMC MED GENET, V13, DOI 10.1186/1471-2350-13-105
   THIERFELDER L, 1994, CELL, V77, P701, DOI 10.1016/0092-8674(94)90054-X
   Thottakara T., 2015, J MOL CELL CARDIOL
   van der Velden J, 2015, CARDIOVASC RES, V105, P449, DOI 10.1093/cvr/cvv019
   van Dijk SJ, 2012, CIRC-HEART FAIL, V5, P36, DOI 10.1161/CIRCHEARTFAILURE.111.963702
   van Dijk SJ, 2009, CIRCULATION, V119, P1473, DOI 10.1161/CIRCULATIONAHA.108.838672
   Van Driest SL, 2004, J AM COLL CARDIOL, V44, P1903, DOI 10.1016/j.jacc.2004.07.045
   Vignier N, 2009, CIRC RES, V105, P239, DOI 10.1161/CIRCRESAHA.109.201251
   Waldmüller S, 2003, J MOL CELL CARDIOL, V35, P623, DOI 10.1016/S0022-2828(03)00050-6
   Wally V, 2012, J INVEST DERMATOL, V132, P1959, DOI 10.1038/jid.2012.101
   WATKINS H, 1995, NAT GENET, V11, P434, DOI 10.1038/ng1295-434
   Weith A, 2012, J MOL CELL CARDIOL, V52, P219, DOI 10.1016/j.yjmcc.2011.09.019
   Wessels M. W., 2014, EUR J HUM GENET
   Witayavanitkul N, 2014, J BIOL CHEM, V289, P8818, DOI 10.1074/jbc.M113.541128
   Witt CC, 2001, J BIOL CHEM, V276, P5353, DOI 10.1074/jbc.M008691200
   Woodley Louise, 2002, Briefings in Functional Genomics & Proteomics, V1, P266, DOI 10.1093/bfgp/1.3.266
   Xin B, 2007, AM J MED GENET A, V143A, P2662, DOI 10.1002/ajmg.a.31981
   Zacchigna S, 2014, CIRC RES, V114, P1827, DOI 10.1161/CIRCRESAHA.114.302331
   Zahka K, 2008, HEART, V94, P1326, DOI 10.1136/hrt.2007.127241
   Zoghbi ME, 2008, P NATL ACAD SCI USA, V105, P2386, DOI 10.1073/pnas.0708912105
NR 147
TC 153
Z9 176
U1 1
U2 43
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
SN 0378-1119
EI 1879-0038
J9 GENE
JI Gene
PD DEC 1
PY 2015
VL 573
IS 2
BP 188
EP 197
DI 10.1016/j.gene.2015.09.008
PG 10
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA CS7ZH
UT WOS:000362305000002
PM 26358504
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Rodríguez-Pérez, JM
   Blachman-Braun, R
   Pomerantz, A
   Vargas-Alarcón, G
   Posadas-Sánchez, R
   Pérez-Hernández, N
AF Rodriguez-Perez, Jose Manuel
   Blachman-Braun, Ruben
   Pomerantz, Alan
   Vargas-Alarcon, Gilberto
   Posadas-Sanchez, Rosalinda
   Perez-Hernandez, Nonanzit
TI Possible role of intronic polymorphisms in the PHACTR1 gene on
   the development of cardiovascular disease
SO MEDICAL HYPOTHESES
LA English
DT Article
DE PHACTR1 gene; Cardiovascular disease; Genomic variants; Intron;
   Alternative splicing
ID CORONARY-ARTERY-DISEASE; GENOME-WIDE ASSOCIATION; INDEPENDENT
   RISK-FACTOR; MYOCARDIAL-INFARCTION; SUSCEPTIBILITY LOCI; FAMILY-HISTORY;
   HEART-DISEASE; NITRIC-OXIDE; STEM-CELLS; VARIANTS
AB Cardiovascular disease (CVD) is a complex multifactorial and polygenetic disease in which the interaction of numerous genes, genetic variants, and environmental factors plays a major role in its development. In an attempt to demonstrate the association between certain genetic variants and CVD, researchers have run large genomic wild association studies (GWAS) in recent decades. These studies have correlated several genomic variants with the presence of CVD. Recently, certain polymorphisms in the phosphatase and actin regulator 1 (PHACTR1) gene have been shown to be associated with CVD (i.e., coronary artery disease, coronary artery calcification, early onset myocardial infarction, cervical artery dissection and hypertension) in different ethnic groups. It is important to state that all of the described PHACTR1 genetic variants associated with CVD are located in non-translating gene regions known as introns. Thus, the purpose of this article is to hypothesize the effect of certain intronic polymorphisms in the PHACTR1 gene on pathological processes in the cardiovascular system. In addition, we present compelling evidence that supports this hypothesis as well as a methodology that could be used to assess the allelic effect using in vitro and in vivo models, which will ultimately demonstrate the pathophysiological contribution of PHACTR1 intronic polymorphisms to the development of CVD. (C) 2016 Elsevier Ltd. All rights reserved.
C1 [Rodriguez-Perez, Jose Manuel; Blachman-Braun, Ruben; Vargas-Alarcon, Gilberto; Perez-Hernandez, Nonanzit] Natl Inst Cardiol Ignacio Chavez, Dept Mol Biol, Juan Badiano 1,Col Secc 16, Mexico City 14080, DF, Mexico.
   [Pomerantz, Alan] Natl Inst Med Sci & Nutr Salvador Zubiran, Dept Hematol & Oncol, Mexico City 14080, DF, Mexico.
   [Posadas-Sanchez, Rosalinda] Natl Inst Cardiol Ignacio Chavez, Dept Endocrinol, Mexico City 14080, DF, Mexico.
C3 National Institute of Cardiology - Mexico; National Institute of
   Cardiology - Mexico
RP Pérez-Hernández, N (corresponding author), Natl Inst Cardiol Ignacio Chavez, Dept Mol Biol, Juan Badiano 1,Col Secc 16, Mexico City 14080, DF, Mexico.
EM unicanona@yahoo.com.mx
RI Vargas-Alarcon, Gilberto/AEW-0446-2022; Blachman-Braun,
   Ruben/AFH-0498-2022
OI Vargas-Alarcon, Gilberto/0000-0001-7916-5163; Blachman-Braun,
   Ruben/0000-0001-9700-0805
FU Consejo Nacional de Ciencia y Tecnologia (CONACyT) [233402, 261741]
FX This article was partially supported by grants from Consejo Nacional de
   Ciencia y Tecnologia (CONACyT), with the project number 233402 and
   261741.
CR Allain B, 2012, CELL SIGNAL, V24, P214, DOI 10.1016/j.cellsig.2011.09.003
   Allen PB, 2004, P NATL ACAD SCI USA, V101, P7187, DOI 10.1073/pnas.0401673101
   Alonso A, 2004, CELL, V117, P699, DOI 10.1016/j.cell.2004.05.018
   [Anonymous], PHACTR1 PHOSPH ACT R
   Arbour L, 2015, CAN J CARDIOL, V31, P1094, DOI 10.1016/j.cjca.2015.07.005
   Beaudoin M, 2015, ARTERIOSCL THROM VAS, V35, P1472, DOI 10.1161/ATVBAHA.115.305534
   Bevan S, 2012, STROKE, V43, P3161, DOI 10.1161/STROKEAHA.112.665760
   Bowman MAH, 2012, TRENDS CARDIOVAS MED, V22, P93, DOI 10.1016/j.tcm.2012.07.002
   Cao Y, 2005, BIOCHEM BIOPH RES CO, V332, P370, DOI 10.1016/j.bbrc.2005.04.135
   Chen YY, 2007, CELL METAB, V6, P164, DOI 10.1016/j.cmet.2007.07.001
   Companioni O, 2011, REV ESP CARDIOL, V64, P509, DOI [10.1016/j.rec.2011.01.011, 10.1016/j.recesp.2011.01.010]
   Debette S, 2015, NAT GENET, V47, P78, DOI 10.1038/ng.3154
   Deloukas P, 2013, NAT GENET, V45, P25, DOI 10.1038/ng.2480
   Fils-Aimé N, 2013, J BIOL CHEM, V288, P11807, DOI 10.1074/jbc.M112.430934
   Freilinger T, 2012, NAT GENET, V44, P777, DOI 10.1038/ng.2307
   FRIEDLANDER Y, 1985, BRIT HEART J, V53, P382
   Fujimaki T, 2015, BIOMED REP, V3, P118, DOI 10.3892/br.2014.371
   Goff DC Jr, 2014, CIRCULATION, V129, pS49, DOI [10.1161/01.cir.0000437741.48606.98, 10.1016/j.jacc.2013.11.005]
   Hager J, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0038663
   Han X, 2014, INT J MOL SCI, V15, P14058, DOI 10.3390/ijms150814058
   Harada N, 2008, AM J PHYSIOL-ENDOC M, V294, pE61, DOI 10.1152/ajpendo.00358.2007
   Hughes-Large JM, 2016, DATA BRIEF, V6, P899, DOI 10.1016/j.dib.2016.01.039
   Jansen H, 2015, ATHEROSCLEROSIS, V241, P419, DOI 10.1016/j.atherosclerosis.2015.05.033
   Jarray R, 2015, BIOCHIMIE, V118, P151, DOI 10.1016/j.biochi.2015.09.008
   Jarray R, 2011, BIOCHIMIE, V93, P1668, DOI 10.1016/j.biochi.2011.07.010
   Kathiresan S, 2009, NAT GENET, V41, P334, DOI 10.1038/ng.327
   Kelemen O, 2013, GENE, V514, P1, DOI 10.1016/j.gene.2012.07.083
   Kelloniemi A, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0130502
   Knight JC, 2005, J MOL MED, V83, P97, DOI 10.1007/s00109-004-0603-7
   Laslett LJ, 2012, J AM COLL CARDIOL, V60, pS1, DOI 10.1016/j.jacc.2012.11.002
   Lee JY, 2013, J HUM GENET, V58, P120, DOI 10.1038/jhg.2012.124
   Lee MS, 2016, J INVASIVE CARDIOL, V28, P160
   Li HG, 2014, ATHEROSCLEROSIS, V237, P208, DOI 10.1016/j.atherosclerosis.2014.09.001
   Lozano R, 2012, LANCET, V380, P2095, DOI 10.1016/S0140-6736(12)61728-0
   Lu XF, 2012, NAT GENET, V44, P890, DOI 10.1038/ng.2337
   Mount PF, 2007, J MOL CELL CARDIOL, V42, P271, DOI 10.1016/j.yjmcc.2006.05.023
   Nichols M, 2014, EUR HEART J, V35, P2950, DOI 10.1093/eurheartj/ehu299
   Niu PP, 2014, J TRANSL MED, V12, DOI 10.1186/1479-5876-12-170
   O'Donnell CJ, 2011, CIRCULATION, V124, P2855, DOI 10.1161/CIRCULATIONAHA.110.974899
   Oswald J, 2004, STEM CELLS, V22, P377, DOI 10.1634/stemcells.22-3-377
   Pechlivanis S, 2013, BMC MED GENET, V14, DOI 10.1186/1471-2350-14-23
   Peden JF, 2011, NAT GENET, V43, P339, DOI 10.1038/ng.782
   Peng YP, 2014, BMC CANCER, V14, DOI 10.1186/1471-2407-14-738
   Pérez-Hernández N, 2016, INT J ENV RES PUB HE, V13, DOI 10.3390/ijerph13080803
   Pérez-Hernández N, 2013, GAC MED MEX, V149, P655
   Peti W, 2013, FEBS J, V280, P596, DOI 10.1111/j.1742-4658.2012.08509.x
   Polat SB, 2016, ARCH ENDOCRIN METAB, V60, P117, DOI 10.1590/2359-3997000000116
   Polonsky TS, 2010, JAMA-J AM MED ASSOC, V303, P1610, DOI 10.1001/jama.2010.461
   Pon JR, 2016, ONCOTARGET, V7, P2297, DOI 10.18632/oncotarget.6223
   Potthoff MJ, 2007, DEVELOPMENT, V134, P4131, DOI 10.1242/dev.008367
   Qi L, 2011, J AM COLL CARDIOL, V58, P2675, DOI 10.1016/j.jacc.2011.08.054
   Ramírez-Bello J, 2013, GAC MED MEX, V149, P220
   ROSE G, 1964, BRIT J PREV SOC MED, V18, P75
   Sharma RK, 2010, VASC HEALTH RISK MAN, V6, P603
   SHEA S, 1984, J AM COLL CARDIOL, V4, P793, DOI 10.1016/S0735-1097(84)80408-8
   Soutar AK, 2007, NAT CLIN PRACT CARD, V4, P214, DOI 10.1038/ncpcardio0836
   Szpakowicz A, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0129820
   Tousoulis D, 2012, CURR VASC PHARMACOL, V10, P4, DOI 10.2174/157016112798829760
   van Setten J, 2013, ATHEROSCLEROSIS, V228, P400, DOI 10.1016/j.atherosclerosis.2013.02.039
   Vargas JD, 2016, ATHEROSCLEROSIS, V245, P230, DOI 10.1016/j.atherosclerosis.2015.11.034
   Wiezlak M, 2012, J CELL SCI, V125, P5860, DOI 10.1242/jcs.112078
   Xu J, 2014, J NEUROSCI, V34, P11048, DOI 10.1523/JNEUROSCI.3986-13.2014
   Yan MS, 2015, ARTERIOSCL THROM VAS, V35, P2297, DOI 10.1161/ATVBAHA.115.305043
   Zhang ZZ, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0046495
NR 64
TC 9
Z9 10
U1 0
U2 13
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
SN 0306-9877
EI 1532-2777
J9 MED HYPOTHESES
JI Med. Hypotheses
PD DEC
PY 2016
VL 97
BP 64
EP 70
DI 10.1016/j.mehy.2016.10.012
PG 7
WC Medicine, Research & Experimental
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Research & Experimental Medicine
GA ED9CD
UT WOS:000389166900014
PM 27876132
DA 2025-04-10
ER

PT J
AU Maeda, M
   Holder, E
   Lowes, B
   Valent, S
   Bies, RD
AF Maeda, M
   Holder, E
   Lowes, B
   Valent, S
   Bies, RD
TI Dilated cardiomyopathy associated with deficiency of the cytoskeletal
   protein metavinculin
SO CIRCULATION
LA English
DT Article
DE cardiomyopathy; cytoskeleton; molecular biology; vinculin; disk,
   intercalated
ID EXPRESSION; LOCALIZATION; DYSTROPHIN; MYOCARDIUM; VINCULIN
AB Background The cytoskeleton plays an important role in maintaining cell structure and integrity. Defects in cytoskeletal proteins can cripple cell strength and may cause cardiomyopathy. We analyzed heart tissues from subjects with dilated cardiomyopathy for abnormalities in the cardiac cytoskeleton. Metavinculin, a cardiac isoform of the cytoskeletal protein vinculin, connects actin microfilaments to the intercalated disk and membrane costameres of the heart.
   Methods and Results Metavinculin and vinculin transcripts and protein were analyzed by polymerase chain reaction (PCR) and Western blotting. Thirty-three human heart specimens were studied, including 5 normal controls, 4 subjects with ischemic cardiomyopathy, 1 with X-linked cardiomyopathy, and 23 with idiopathic dilated cardiomyopathy (IDC). PCR of cardiac cDNA detected absence of the metavinculin transcript in cardiac tissue from a subject with IDC. PCR of genomic DNA showed that the metavinculin exon was present but not utilized in the cardiac transcript. Western blot analysis demonstrated absence of metavinculin protein in the heart from this subject. Immunostaining of cardiac vinculin in this heart showed disorganized intercalated disk structures. Metavinculin deficiency was associated with normal cardiac expression of the cytoskeletal proteins vinculin, alpha-actinin, and dystrophin. Normal metavinculin expression in the other heart specimens suggests that the defect is specific in the IDC subject identified.
   Conclusions These results demonstrate an association between metavinculin deficiency and dilated cardiomyopathy due to a defect in alternative mRNA splicing.
C1 UNIV COLORADO,HLTH SCI CTR,DIV CARDIOL,DENVER,CO 80262.
   VET AFFAIRS MED CTR,DENVER,CO 80262.
C3 University of Colorado System; University of Colorado Denver; University
   of Colorado Anschutz Medical Campus; US Department of Veterans Affairs;
   Veterans Health Administration (VHA)
RI Lowes, Brian/M-9020-2017
OI Lowes, Brian/0000-0002-5919-2540
CR Alberts B., 1994, Molecular biology of the cell, P787
   BEIKIN AM, 1988, J CELL BIOL, V107, P545
   BIES RD, 1992, CIRCULATION, V86, P147, DOI 10.1161/01.CIR.86.1.147
   BIES RD, 1995, J AM COLL CARDIO FEB, pA277
   CHIRGWIN JM, 1979, BIOCHEMISTRY-US, V13, P2633
   FADIG R, DEFICIENCY DYSTROPHI
   GOLDSTEIN J, 1988, HEART DIS, P1633
   GONCHAROVA EJ, 1992, DEVELOPMENT, V114, P173
   KOTELIANSKY VE, 1992, EUR J BIOCHEM, V204, P767, DOI 10.1111/j.1432-1033.1992.tb16692.x
   MAEDA M, 1995, J BIOL CHEM, V270, P20246, DOI 10.1074/jbc.270.35.20246
   MICHELS VV, 1992, NEW ENGL J MED, V326, P77, DOI 10.1056/NEJM199201093260201
   MUNTONI F, 1993, NEW ENGL J MED, V329, P921, DOI 10.1056/NEJM199309233291304
   PETERS NS, 1994, CIRCULATION, V90, P713, DOI 10.1161/01.CIR.90.2.713
   SCHAPER J, 1991, CIRCULATION, V83, P504, DOI 10.1161/01.CIR.83.2.504
   Seidman JG., 2003, Current protocols in molecular biology (Vol. 2003)
   STRASSER P, 1993, FEBS LETT, V317, P189, DOI 10.1016/0014-5793(93)81274-4
   TSUTSUI H, 1993, SCIENCE, V260, P682, DOI 10.1126/science.8097594
   WANG N, 1993, SCIENCE, V260, P1124, DOI 10.1126/science.7684161
NR 18
TC 117
Z9 128
U1 0
U2 5
PU AMER HEART ASSOC
PI DALLAS
PA 7272 GREENVILLE AVENUE, DALLAS, TX 75231-4596
SN 0009-7322
J9 CIRCULATION
JI Circulation
PD JAN 7
PY 1997
VL 95
IS 1
BP 17
EP 20
DI 10.1161/01.CIR.95.1.17
PG 4
WC Cardiac & Cardiovascular Systems; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology
GA WB307
UT WOS:A1997WB30700017
PM 8994410
DA 2025-04-10
ER

PT J
AU Zhang, XH
   Kanika, ND
   Melman, A
   DiSanto, ME
AF Zhang, Xinhua
   Kanika, Nirmala D.
   Melman, Arnold
   DiSanto, Michael E.
TI Smooth muscle myosin expression, isoform composition, and functional
   activities in rat corpus cavernosum altered by the
   streptozotocin-induced type 1 diabetes
SO AMERICAN JOURNAL OF PHYSIOLOGY-ENDOCRINOLOGY AND METABOLISM
LA English
DT Article
DE blebbistatin; cross-bridge cycling; erectile dysfunction; smooth muscle
   relaxation
ID INDUCED ERECTILE DYSFUNCTION; DISTINCT ANIMAL-MODELS; NITRIC-OXIDE
   SYNTHASE; IN-VIVO RELAXATION; LIGHT-CHAIN; SHORTENING VELOCITY;
   URINARY-BLADDER; II INHIBITOR; HEAVY-CHAIN; SINGLE-GENE
AB Zhang X, Kanika ND, Melman A, DiSanto ME. Smooth muscle myosin expression, isoform composition, and functional activities in rat corpus cavernosum altered by the streptozotocin-induced type 1 diabetes. Am J Physiol Endocrinol Metab 302: E32-E42, 2012. First published September 13, 2011; doi:10.1152/ajpendo.00231.2011.-Diabetes mellitus (DM) is a quite common chronic disease, and the prevalence of erectile dysfunction (ED) is three times higher in this large population. Although diabetes-related ED has been studied extensively, the actin-myosin contractile apparatus was not examined. The mRNAs encoding smooth muscle myosin (SMM) heavy chains (MHC) and essential light chains (LC17) exist as several different alternatively spliced isoforms with distinct contractile properties. Recently, we provided novel data that blebbistatin (BLEB), a specific myosin II inhibitor, potently relaxed corpus cavernosum smooth muscle (CCSM). In this study, we examine whether diabetes alters SMM expression, alternative splicing, and/or functional activities, including sensitivity to BLEB. By using streptozotocin (STZ)-induced 2-mo diabetic rats, functional activities were tested in vivo by intracavernous pressure (ICP) recording during cavernous nerve stimulation and in vitro via organ bath contractility studies. SMM isoform composition was analyzed by competitive RT-PCR and total SMM, myocardin, and embryonic SMM (SMemb) expression by real-time RT-PCR. Results revealed that the blood glucose level of STZ rats was 407.0 vs. 129.5 mg/dl (control). STZ rats exhibited ED confirmed by significantly increased CCSM contractile response to phenylephrine and decreased ICP response. For STZ rats, SM-B, LC17a and SM2 isoforms, total SMM, and myocardin expression increased, whereas SM-A, LC17b, and SM1 isoforms were decreased, with SMemb unchanged. BLEB was significantly more effective in relaxing STZ CCSM both in vitro and in vivo. Thus we demonstrated a novel diabetes-specific effect on alternative splicing of the SMM heavy chain and essential light chain genes to a SMM isoform composition favoring a heightened contractility and ED. A switch to a more contractile phenotype was supported further by total SMM expression increase. Moreover, the change in CCSM phenotype was associated with an increased sensitivity to BLEB, which may serve as a novel pharmacotherapy for ED.
C1 [Zhang, Xinhua; DiSanto, Michael E.] Rowan Univ, Cooper Med Sch, Div Urol, Dept Surg, Camden, NJ USA.
   [Zhang, Xinhua; Kanika, Nirmala D.; Melman, Arnold; DiSanto, Michael E.] Albert Einstein Coll Med, Dept Urol, Bronx, NY 10467 USA.
C3 Rowan University; Cooper Medical School of Rowan University; Yeshiva
   University; Montefiore Medical Center; Albert Einstein College of
   Medicine
RP DiSanto, ME (corresponding author), Cooper Univ Hosp, 3 Cooper Plaza, Camden, NJ 08103 USA.
EM disanto-michael@cooperhealth.edu
FU National Institute of Diabetes and Digestive and Kidney Diseases
   [5-R01-DK-077116]
FX This study was supported by National Institute of Diabetes and Digestive
   and Kidney Diseases Grant 5-R01-DK-077116.
CR ADELSTEIN RS, 1980, ANNU REV BIOCHEM, V49, P921, DOI 10.1146/annurev.bi.49.070180.004421
   ANDERSSON KE, 1995, PHYSIOL REV, V75, P191, DOI 10.1152/physrev.1995.75.1.191
   Arner A, 2003, J MUSCLE RES CELL M, V24, P165, DOI 10.1023/A:1026001513928
   BABIJ P, 1989, J MOL BIOL, V210, P673, DOI 10.1016/0022-2836(89)90142-3
   BABIJ P, 1991, P NATL ACAD SCI USA, V88, P10676, DOI 10.1073/pnas.88.23.10676
   Babu GJ, 2001, NAT CELL BIOL, V3, P1025, DOI 10.1038/ncb1101-1025
   Beck J, 2000, ACTA NEUROBIOL EXP, V60, P29, DOI 10.55782/ane-2000-1322
   Bivalacqua TJ, 2004, P NATL ACAD SCI USA, V101, P9121, DOI 10.1073/pnas.0400520101
   Christ GJ, 2006, BJU INT, V97, P1076, DOI 10.1111/j.1464-410X.2006.06058.x
   Chua RG, 2009, MOL CELL ENDOCRINOL, V303, P67, DOI 10.1016/j.mce.2009.02.001
   Costabile RA, 2003, J UROLOGY, V170, pS35, DOI 10.1097/01.ju.0000077448.31995.99
   DiSanto ME, 1998, AM J PHYSIOL-CELL PH, V275, pC976, DOI 10.1152/ajpcell.1998.275.4.C976
   DiSanto ME, 2003, AM J PHYSIOL-CELL PH, V285, pC1397, DOI 10.1152/ajpcell.00513.2002
   DiSanto ME, 1997, AM J PHYSIOL-CELL PH, V272, pC1532, DOI 10.1152/ajpcell.1997.272.5.C1532
   Dunsmuir WD, 1996, DIABETIC MED, V13, P700, DOI 10.1002/(SICI)1096-9136(199608)13:8<700::AID-DIA174>3.3.CO;2-#
   Eddinger TJ, 2007, J PHARMACOL EXP THER, V320, P865, DOI 10.1124/jpet.106.109363
   FELDMAN HA, 1994, J UROLOGY, V151, P54, DOI 10.1016/S0022-5347(17)34871-1
   Hashitani H, 2004, BRIT J PHARMACOL, V141, P183, DOI 10.1038/sj.bjp.0705602
   Huang QQ, 1999, J BIOL CHEM, V274, P35095, DOI 10.1074/jbc.274.49.35095
   Hypolite JA, 2001, AM J PHYSIOL-CELL PH, V280, pC254, DOI 10.1152/ajpcell.2001.280.2.C254
   KELLEY CA, 1993, J BIOL CHEM, V268, P12848
   Koi PT, 2007, INT J IMPOT RES, V19, P62, DOI 10.1038/sj.ijir.3901503
   Kosova B, 2011, UROLOGY, V77, DOI 10.1016/j.urology.2010.04.052
   LENZ S, 1989, J BIOL CHEM, V264, P9009
   Limouze J, 2004, J MUSCLE RES CELL M, V25, P337, DOI 10.1007/s10974-004-6060-7
   Livak KJ, 2001, METHODS, V25, P402, DOI 10.1006/meth.2001.1262
   Mallick C, 2007, BIOL PHARM BULL, V30, P84, DOI 10.1248/bpb.30.84
   MALMQVIST U, 1991, PFLUG ARCH EUR J PHY, V418, P523, DOI 10.1007/BF00370566
   Matthew JD, 1998, J BIOL CHEM, V273, P31289, DOI 10.1074/jbc.273.47.31289
   MCCULLOCH DK, 1984, DIABETOLOGIA, V26, P437
   MCCULLOCH DK, 1980, DIABETOLOGIA, V18, P279
   Melman A, 2008, GENE THER, V15, P364, DOI 10.1038/sj.gt.3303093
   Melman A, 2009, BJU INT, V104, P1292, DOI 10.1111/j.1464-410X.2009.08573.x
   Mitani Y, 2001, EUR RESPIR J, V17, P316, DOI 10.1183/09031936.01.17203160
   Musicki B, 2005, P NATL ACAD SCI USA, V102, P11870, DOI 10.1073/pnas.0502488102
   NABESHIMA Y, 1987, J BIOL CHEM, V262, P10608
   Park K, 2008, EUR UROL, V53, P1282, DOI 10.1016/j.eururo.2008.01.032
   Ren J, 2002, PHARMACOL RES, V45, P195, DOI 10.1006/phrs.2002.0947
   Rhee AY, 2006, PFLUG ARCH EUR J PHY, V452, P766, DOI 10.1007/s00424-006-0091-4
   Shaw JE, 2010, DIABETES RES CLIN PR, V87, P4, DOI 10.1016/j.diabres.2009.10.007
   Siegman MJ, 1997, AM J PHYSIOL-GASTR L, V272, pG1571, DOI 10.1152/ajpgi.1997.272.6.G1571
   Somlyo AV, 1998, ACTA PHYSIOL SCAND, V164, P381, DOI 10.1111/j.1365-201X.1998.tb10695.x
   Straight AF, 2003, SCIENCE, V299, P1743, DOI 10.1126/science.1081412
   Vickers MA, 2002, INT J IMPOT RES, V14, P466, DOI 10.1038/sj.ijir.3900910
   Vignozzi L, 2007, J SEX MED, V4, P620, DOI 10.1111/j.1743-6109.2007.00440.x
   Wang ZG, 2003, P NATL ACAD SCI USA, V100, P7129, DOI 10.1073/pnas.1232341100
   YAMAMOTO M, 1992, P NATL ACAD SCI USA, V89, P5326, DOI 10.1073/pnas.89.12.5326
   Yamanaka M, 2003, J UROLOGY, V170, P291, DOI 10.1097/01.ju.0000060564.31122.2a
   Yousif MHM, 2007, VASC PHARMACOL, V47, P281, DOI 10.1016/j.vph.2007.08.002
   Zhang XH, 2006, J SEX MED, V3, P253, DOI 10.1111/j.1743-6109.2006.00207.x
   Zhang XH, 2005, EUR UROL, V47, P409, DOI 10.1016/j.eururo.2004.10.021
   Zhang XH, 2009, J SEX MED, V6, P2661, DOI 10.1111/j.1743-6109.2009.01424.x
   Zhang XH, 2011, BJU INT, V107, P310, DOI 10.1111/j.1464-410X.2010.09366.x
NR 53
TC 13
Z9 20
U1 6
U2 22
PU AMER PHYSIOLOGICAL SOC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA
SN 0193-1849
EI 1522-1555
J9 AM J PHYSIOL-ENDOC M
JI Am. J. Physiol.-Endocrinol. Metab.
PD JAN
PY 2012
VL 302
IS 1
BP E32
EP E42
DI 10.1152/ajpendo.00231.2011
PG 11
WC Endocrinology & Metabolism; Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism; Physiology
GA 866JU
UT WOS:000298377600004
PM 21917637
OA Green Published, Green Accepted
DA 2025-04-10
ER

PT J
AU Misquitta, CM
   Mwanjewe, J
   Nie, L
   Grover, AK
AF Misquitta, CM
   Mwanjewe, J
   Nie, L
   Grover, AK
TI Sarcoplasmic reticulum Ca<SUP>2+</SUP> pump mRNA stability in cardiac
   and smooth muscle:: role of the 3′-untranslated region
SO AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY
LA English
DT Article
DE mRNA stability; calcium; adenosinetriphosphatase; transcription; 3
   '-untranslated region; translation
ID MESSENGER-RNA; EXPRESSION; EXCHANGE; ATPASE; HEART; PHOSPHORYLATION;
   PHOSPHOLAMBAN; PROTEINS; ISOFORMS; STOMACH
AB Stomach smooth muscle (SSM) and left ventricular muscle (LVM) express the sarco(endo) plasmic reticulum Ca2+-ATPase (SERCA) pump gene SERCA2. Alternative splicing yields two major isoforms, SERCA2a in LVM and slow twitch muscle and SERCA2b in SSM and most other tissues. The splices have different 3'-untranslated regions (UTR) and also encode proteins that differ slightly in their COOH-terminal domains. SERCA2 transcription rates are similar in the two tissues, yet LVM has a much higher level of SERCA2 mRNA than SSM. To understand the control of SERCA2 RNA expression, we inhibited transcription and showed that the half-life of SERCA2 mRNA is significantly longer (P < 0.05) in primary cultures of LVM cells than in SSM cells. Nuclear SERCA2 mRNA levels were also higher in LVM than in SSM. In vitro decay assays using synthetic RNA corresponding to the 3'-UTR of SERCA2a and -2b showed that nuclear extracts produced a faster decay of SERCA2 RNA than cytoplasmic extracts and that nuclear extracts produced a faster decay of SERCA2b than -2a. This was also true when the full-length native mRNA was used instead of the 3'-UTR RNA, and SERCA2b decay by cytoplasmic extracts was faster for LVM than for SSM. We propose that nuclear decay is an initial step in the control of SERCA2 RNA abundance and that this control is maintained or modulated in the cytoplasm. We discuss how these control mechanisms may be part of a control switch in cardiac development and pathophysiology.
C1 McMaster Univ, Dept Med, Hamilton, ON L8N 3Z5, Canada.
   McMaster Univ, Dept Biol, Hamilton, ON L8N 3Z5, Canada.
C3 McMaster University; McMaster University
RP McMaster Univ, Dept Med, HSC 4N41,1200 Main St W, Hamilton, ON L8N 3Z5, Canada.
EM groverak@mcmaster.ca
CR BERGER LC, 1992, EUR J BIOCHEM, V204, P733, DOI 10.1111/j.1432-1033.1992.tb16688.x
   Bhogal MS, 1998, P NATL ACAD SCI USA, V95, P1484, DOI 10.1073/pnas.95.4.1484
   Blaxall BC, 2000, J BIOL CHEM, V275, P4290, DOI 10.1074/jbc.275.6.4290
   BOHELER KR, 1992, J BIOL CHEM, V267, P12979
   Brewer G, 1998, J BIOL CHEM, V273, P34770, DOI 10.1074/jbc.273.52.34770
   Clement JQ, 2000, J MOL BIOL, V299, P1179, DOI 10.1006/jmbi.2000.3745
   EGGERMONT JA, 1990, BIOCHEM J, V266, P901
   Hryshko LV, 1997, BASIC RES CARDIOL, V92, P45, DOI 10.1007/BF00794067
   KHAN I, 1990, BIOCHEM J, V268, P415, DOI 10.1042/bj2680415
   KHAN I, 1990, NUCLEIC ACIDS RES, V18, P4026, DOI 10.1093/nar/18.13.4026
   Loflin P, 1999, GENE DEV, V13, P1884, DOI 10.1101/gad.13.14.1884
   LYTTON J, 1988, J BIOL CHEM, V263, P15024
   Maxwell K, 1999, AM J PHYSIOL-HEART C, V277, pH2212, DOI 10.1152/ajpheart.1999.277.6.H2212
   Misquitta CM, 1999, CELL CALCIUM, V25, P277, DOI 10.1054/ceca.1999.0032
   Misquitta CM, 1999, BIOCHEM J, V338, P167, DOI 10.1042/0264-6021:3380167
   MOVSESIAN MA, 1994, CIRCULATION, V90, P653, DOI 10.1161/01.CIR.90.2.653
   Pande A, 1996, J BIOL CHEM, V271, P8493, DOI 10.1074/jbc.271.14.8493
   PORT JD, 1992, J BIOL CHEM, V267, P24103
   Qi M, 1996, AM J PHYSIOL-HEART C, V271, pH1031, DOI 10.1152/ajpheart.1996.271.3.H1031
   Ross J, 1996, TRENDS GENET, V12, P171, DOI 10.1016/0168-9525(96)10016-0
   TAMM I, 1976, J CELL BIOL, V69, P229, DOI 10.1083/jcb.69.2.229
   Terracciano CMN, 1998, J PHYSIOL-LONDON, V512, P651, DOI 10.1111/j.1469-7793.1998.651bd.x
   VETTER R, 1995, J MOL CELL CARDIOL, V27, P1689, DOI 10.1016/S0022-2828(95)90788-2
   Wagner BJ, 1998, GENOMICS, V48, P195, DOI 10.1006/geno.1997.5142
   WEIL D, 1990, MOL CELL BIOL, V10, P5865, DOI 10.1128/MCB.10.11.5865
   Wilson GM, 1999, MOL CELL BIOL, V19, P4056
   Wu KD, 2001, AM J PHYSIOL-CELL PH, V280, pC843, DOI 10.1152/ajpcell.2001.280.4.C843
   XU A, 1993, J BIOL CHEM, V268, P8394
   ZarainHerzberg A, 1996, MOL CELL BIOCHEM, V164, P285, DOI 10.1007/BF00408669
NR 29
TC 21
Z9 22
U1 0
U2 1
PU AMER PHYSIOLOGICAL SOC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA
SN 0363-6143
EI 1522-1563
J9 AM J PHYSIOL-CELL PH
JI Am. J. Physiol.-Cell Physiol.
PD AUG
PY 2002
VL 283
IS 2
BP C560
EP C568
DI 10.1152/ajpcell.00527.2001
PG 9
WC Cell Biology; Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Physiology
GA 571FD
UT WOS:000176704900021
PM 12107066
DA 2025-04-10
ER

PT J
AU Azma, T
   Sugimoto, Y
   Kinoshita, H
   Ito, T
   Tsukamoto, M
   Hoshijima, H
   Nakao, M
   Kikuchi, H
AF Azma, Toshiharu
   Sugimoto, Yuki
   Kinoshita, Hiroyuki
   Ito, Taishin
   Tsukamoto, Masanori
   Hoshijima, Hiroshi
   Nakao, Masakazu
   Kikuchi, Hirosato
TI Detection of the full-length transcript variant for neurokinin-1
   receptor in human whole blood associated with enhanced reinforcement of
   clot by substance-P
SO JOURNAL OF THROMBOSIS AND THROMBOLYSIS
LA English
DT Article
DE Substance-P; Neurokinin-1 receptor; Transcript variant; Splice isoform;
   Clot formation; Leukocytes
ID CHROMOSOME LOCALIZATION; TACHYKININS; EXPRESSION; CDNA; GENE; MICE
AB We have recently reported that a neurotransmitter for pain, substance-P (SP), promotes platelet-dependent clot formation through neurokinin-1 receptors (NK1Rs), in which leukocytes appear to be involved (J Thromb Thrombolysis 2009;27:280-6). Two naturally occurring splice isoforms of NK1R with different signal transduction potency, namely the full-length and the truncated NK1Rs are identified. It is known that human leukocytes express truncated NK1Rs, while in vivo expression of the full-length NK1R has not yet been fully clarified. Modulatory effects of alternative splicing for NK1Rs on clot formation also remain to be evaluated. Expression of the transcript variant mRNA for NK1Rs in human whole blood (n = 20) was evaluated by real-time reverse transcription polymerase chain reaction (RT-PCR). A 15 min time series of the strength of clot, formed after reloading of calcium in citrated whole blood with or without SP (10 nM) and a NK1R antagonist Spantide (1 mu M), was measured by using oscillating-probe viscoelastometry. The full-length transcript variant was detected in 5 samples among 20. SP significantly increased the clot strength while Spantide suppressed the SP-derived change. The extent of modulation by SP/NK1R pathway in a subgroup with expression of the full-length transcript variant was three times as potent as those in another subgroup without expression. We conclude that expression of the full-length transcript variant for NK1R can be detected in human whole blood and that such expression is associated with the enhanced reinforcement of clot by SP. Further study is required to nominate this mRNA as a biomarker for prothrombotic risks in painful conditions such as perioperative period.
C1 [Azma, Toshiharu; Ito, Taishin; Tsukamoto, Masanori; Hoshijima, Hiroshi; Kikuchi, Hirosato] Saitama Med Univ, Dept Anesthesiol, Fac Med, Saitama 3500495, Japan.
   [Sugimoto, Yuki] Hiroshima Univ Hosp, Dept Anesthesiol, Hiroshima, Japan.
   [Kinoshita, Hiroyuki] Wakayama Med Univ, Dept Anesthesiol, Wakayama, Japan.
   [Nakao, Masakazu] Hiroshima Gen Hosp, Dept Anesthesiol, Hatsukaichi, Hiroshima, Japan.
C3 Saitama Medical University; Hiroshima University; Wakayama Medical
   University
RP Azma, T (corresponding author), Saitama Med Univ, Dept Anesthesiol, Fac Med, Saitama 3500495, Japan.
EM azmacci@nifty.com
RI Kinoshita, Hiroyuki/AFC-8806-2022; Yoshimoto, Yuki/MBG-4223-2025
OI Azma, Toshiharu/0000-0001-9183-0840; Tsukamoto,
   Masanori/0000-0001-6848-0870
FU Ministry of Education, Culture, Sports, Science and Technology in Japan
   [22791453, 22791454, 22591748]; Grants-in-Aid for Scientific Research
   [22791454, 22791453, 22591748] Funding Source: KAKEN
FX This study was supported in part by Grants-in-aid for Scientific
   Research from the Ministry of Education, Culture, Sports, Science and
   Technology in Japan (No. 22791453, 22791454, and 22591748).
CR Azma T, 2009, J THROMB THROMBOLYS, V27, P280, DOI 10.1007/s11239-008-0215-0
   Benson DA, 2003, NUCLEIC ACIDS RES, V31, P23, DOI 10.1093/nar/gkg057
   Cao YQ, 1998, NATURE, V392, P390, DOI 10.1038/32897
   Chernova I, 2009, J LEUKOCYTE BIOL, V85, P154, DOI 10.1189/jlb.0408260
   De Felipe C, 1998, NATURE, V392, P394, DOI 10.1038/32904
   Eular US, 1931, J PHYSL, V72, P74
   FONG TM, 1992, MOL PHARMACOL, V41, P24
   Gaddum J H, 1934, J Physiol, V83, P1
   Ganter MT, 2008, ANESTH ANALG, V106, P1366, DOI 10.1213/ane.0b013e318168b367
   Geerts WH, 2008, CHEST, V133, p381S, DOI 10.1378/chest.08-0656
   GERARD NP, 1991, BIOCHEMISTRY-US, V30, P10640, DOI 10.1021/bi00108a006
   GERARD NP, 1990, J BIOL CHEM, V265, P20455
   Graham GJ, 2004, BLOOD, V104, P1058, DOI 10.1182/blood-2003-11-3979
   Harrison S, 2001, INT J BIOCHEM CELL B, V33, P555, DOI 10.1016/S1357-2725(01)00031-0
   HETT DA, 1995, BRIT J ANAESTH, V75, P771, DOI 10.1093/bja/75.6.771
   HUANG RRC, 1992, BIOCHEM BIOPH RES CO, V184, P966, DOI 10.1016/0006-291X(92)90685-E
   Jones S, 2008, BLOOD, V111, P605, DOI 10.1182/blood-2007-07-103424
   Lai JP, 2006, P NATL ACAD SCI USA, V103, P7771, DOI 10.1073/pnas.0602563103
   Manak MM, 2010, AIDS, V24, P2789, DOI 10.1097/QAD.0b013e3283405c33
   Monaco-Shawver L, 2011, J LEUKOCYTE BIOL, V89, P113, DOI 10.1189/jlb.0410200
   Reed KL, 2004, P NATL ACAD SCI USA, V101, P9115, DOI 10.1073/pnas.0403210101
   Rozen S, 2000, Methods Mol Biol, V132, P365
   SALEEM A, 1983, ANN CLIN LAB SCI, V13, P115
   Shantsila E, 2009, THROMB HAEMOSTASIS, V102, P916, DOI 10.1160/TH09-01-0023
   Tuluc F, 2009, TRENDS IMMUNOL, V30, P271, DOI 10.1016/j.it.2009.03.006
   Zimmer A, 1998, P NATL ACAD SCI USA, V95, P2630, DOI 10.1073/pnas.95.5.2630
NR 26
TC 4
Z9 5
U1 0
U2 3
PU SPRINGER
PI DORDRECHT
PA VAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDS
SN 0929-5305
J9 J THROMB THROMBOLYS
JI J. Thromb. Thrombolysis
PD MAY
PY 2012
VL 33
IS 4
SI SI
BP 329
EP 337
DI 10.1007/s11239-011-0650-1
PG 9
WC Cardiac & Cardiovascular Systems; Hematology; Peripheral Vascular
   Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology; Hematology
GA 935HB
UT WOS:000303508600005
PM 22057425
DA 2025-04-10
ER

PT J
AU Ouhtit, A
   Matrougui, K
   Bengrine, A
   Koochekpour, S
   Zerfaoui, M
   Yousief, Z
AF Ouhtit, Allal
   Matrougui, Khalid
   Bengrine, Abderrahmane
   Koochekpour, Shahriar
   Zerfaoui, Mourad
   Yousief, Zakaria
TI Survivin is not only a death encounter but also a survival protein for
   invading tumor cells
SO FRONTIERS IN BIOSCIENCE-LANDMARK
LA English
DT Article
DE SVV; apoptosis; cell cycle; carcinogenesis; angiogenesis; tumor
   invasion; therapeutic strategies; review
ID ANTI-APOPTOSIS GENE; SPINDLE CHECKPOINT; SPLICE VARIANTS; EXPRESSION;
   CANCER; INHIBITOR; CYCLE; PHOSPHORYLATION; SUPPRESSION; ACTIVATION
AB Cell proliferation and cell death pathways meet at a pivotal crossroad, crucial to maintain normal homeostasis and to eliminate dangerous cells before they start dividing. Survivin ( SVV) is an intriguing and fascinating protein at this crossroad that interfaces life and death, through its dual role in facilitating cell division and encountering apoptosis. SVV's prominent expression in essentially all human malignancies, and low or no expression in most normal tissues, suggests that it would be an ideal target for cancer-directed therapy. However, SVV has been recently described as a target for fine tuning by alternative splicing mechanism generating five defined splice variants and a number of other uncharacterized/bizarre isoforms. This diversity indicates that SVV, in addition to its known functions in tumorogenesis, angiogenesis and cardiovascular diseases, might be associated with other unknown functions. Intriguingly, new accumulating evidence from our own work and others, suggest a novel role for SVV in the mechanisms of tumor invasion and metastasis. The SVV pathway has now provided tangible opportunities for targeted, rational cancer therapy. It is therefore an attractive and promising therapeutic target not only for cancer but also for other diseases. Although a number of studies utilizing SVV as an anti-cancer strategy are well underway, further investigation into the exact molecular interactions underpinning its functions is critical for the success of such trials. Impeding development of safe and effective SVV antagonists for clinical use is due to a lack of understanding the molecular mechanisms by which SVV differentially affects apoptosis and cell division in both normal and malignant cells. In this report, in addition to reviewing the SVV known functions, we discuss the newly proposed mechanisms by which SVV might serve as a survival tool for invading tumor cells.
C1 Louisiana State Univ, Hlth Sci Ctr, Dept Pathol, Stanley Scott Canc Ctr, New Orleans, LA 70112 USA.
   Louisiana State Univ, Hlth Sci Ctr, Dept Pharmacol, New Orleans, LA 70112 USA.
   Louisiana State Univ, Hlth Sci Ctr, Dept Microbiol Immunol & Parasitol, New Orleans, LA 70112 USA.
   Louisiana State Univ, Hlth Sci Ctr, Neurosci Ctr Excellence, New Orleans, LA 70112 USA.
   Louisiana State Univ, Hlth Sci Ctr, Dept Biochem & Mol Biol, New Orleans, LA 70112 USA.
   SUNY Buffalo, Dept Physiol & Biophys, Buffalo, NY 14214 USA.
C3 Louisiana State University System; Louisiana State University Health
   Sciences Center New Orleans; Louisiana State University System;
   Louisiana State University Health Sciences Center New Orleans; Louisiana
   State University System; Louisiana State University Health Sciences
   Center New Orleans; Louisiana State University System; Louisiana State
   University Health Sciences Center New Orleans; Louisiana State
   University System; Louisiana State University Health Sciences Center New
   Orleans; State University of New York (SUNY) System; University at
   Buffalo, SUNY
RP Ouhtit, A (corresponding author), Louisiana State Univ, Hlth Sci Ctr, Dept Pathol, Stanley Scott Canc Ctr, New Orleans, LA 70112 USA.
EM aouhti@lsuhsc.edu
RI Abd Elmageed, Zakaria/O-3456-2018
OI Abd Elmageed, Zakaria/0000-0003-4031-0348
CR Adida C, 1998, AM J PATHOL, V152, P43
   Allen SM, 2003, CANCER RES, V63, P567
   Altieri DC, 2003, NAT REV CANCER, V3, P46, DOI 10.1038/nrc968
   Altieri DC, 2001, TRENDS MOL MED, V7, P542, DOI 10.1016/S1471-4914(01)02243-2
   Ambrosini G, 1997, NAT MED, V3, P917, DOI 10.1038/nm0897-917
   Caldas H, 2005, MOL CANCER, V4, DOI 10.1186/1476-4598-4-11
   Choy JC, 2001, J MOL CELL CARDIOL, V33, P1673, DOI 10.1006/jmcc.2001.1419
   Chu ZL, 1997, P NATL ACAD SCI USA, V94, P10057, DOI 10.1073/pnas.94.19.10057
   Deng H, 2006, WORLD J GASTROENTERO, V12, P1013, DOI 10.3748/wjg.v12.i7.1013
   Deveraux QL, 1999, GENE DEV, V13, P239, DOI 10.1101/gad.13.3.239
   Fangusaro JR, 2005, BRIT J CANCER, V92, P359, DOI 10.1038/sj.bjc.6602317
   Fornaro M, 2003, J BIOL CHEM, V278, P50402, DOI 10.1074/jbc.M307627200
   Fortugno P, 2002, J CELL SCI, V115, P575
   Ghatak S, 2002, J BIOL CHEM, V277, P38013, DOI 10.1074/jbc.M202404200
   Grabowski P, 2003, BRIT J CANCER, V88, P115, DOI 10.1038/sj.bjc.6600696
   Gritsko T, 2006, CLIN CANCER RES, V12, P11, DOI 10.1158/1078-0432.CCR-04-1752
   Grossman D, 1999, J INVEST DERMATOL, V113, P1076, DOI 10.1046/j.1523-1747.1999.00776.x
   Hattori M, 2001, CANCER LETT, V169, P155, DOI 10.1016/S0304-3835(01)00499-2
   Hoffman WH, 2002, J BIOL CHEM, V277, P3247, DOI 10.1074/jbc.M106643200
   Huang P, 2001, TRENDS CELL BIOL, V11, P343, DOI 10.1016/S0962-8924(01)02063-3
   Islam A, 2000, ONCOGENE, V19, P617, DOI 10.1038/sj.onc.1203358
   Jiang YY, 2004, J BIOL CHEM, V279, P40511, DOI 10.1074/jbc.M404496200
   Kato J, 2001, INT J CANCER, V95, P92
   Katoh M, 2003, J NEURO-ONCOL, V64, P71, DOI 10.1007/BF02700022
   Kawasaki H, 1998, CANCER RES, V58, P5071
   Krieg A, 2002, BRIT J CANCER, V86, P737, DOI 10.1038/sj.bjc.6600153
   Lens SMA, 2003, EMBO J, V22, P2934, DOI 10.1093/emboj/cdg307
   Li F, 2005, BRIT J CANCER, V92, P212, DOI 10.1038/sj.bjc.6602340
   LI F, 2006, J CELL PHYSL
   Li FZ, 2003, J CELL PHYSIOL, V197, P8, DOI 10.1002/jcp.10327
   Li FZ, 1999, BIOCHEM J, V344, P305, DOI 10.1042/0264-6021:3440305
   Li FZ, 2005, INT J CANCER, V114, P509, DOI 10.1002/ijc.20768
   Li FZ, 1998, NATURE, V396, P580, DOI 10.1038/25141
   Lin YH, 2001, J BIOL CHEM, V276, P46024, DOI 10.1074/jbc.M105132200
   Mahotka C, 1999, CANCER RES, V59, P6097
   Mahotka C, 2002, CELL DEATH DIFFER, V9, P1334, DOI 10.1038/sj.cdd.4401091
   Mirza A, 2002, ONCOGENE, V21, P2613, DOI 10.1038/sj.onc.1205353
   Monaghan M, 2000, J PATHOL, V192, P519
   O'Connor DS, 2000, P NATL ACAD SCI USA, V97, P13103, DOI 10.1073/pnas.240390697
   Papapetropoulos A, 2000, J BIOL CHEM, V275, P9102, DOI 10.1074/jbc.275.13.9102
   Reed JC, 2001, J CLIN INVEST, V108, P965, DOI 10.1172/JCI14123
   Ross JS, 2001, ANN NY ACAD SCI, V947, P271
   Shin S, 2001, BIOCHEMISTRY-US, V40, P1117, DOI 10.1021/bi001603q
   Skoufias DA, 2000, J CELL BIOL, V151, P1575, DOI 10.1083/jcb.151.7.1575
   Sommer KW, 2003, ONCOGENE, V22, P4266, DOI 10.1038/sj.onc.1206509
   SPAN PN, 2006, BREAST CANC RES 0316
   Suzuki A, 2000, ONCOGENE, V19, P1346, DOI 10.1038/sj.onc.1203429
   Tran J, 2002, P NATL ACAD SCI USA, V99, P4349, DOI 10.1073/pnas.072586399
   Tran J, 1999, BIOCHEM BIOPH RES CO, V264, P781, DOI 10.1006/bbrc.1999.1589
   Ueda M, 2002, J CLIN ENDOCR METAB, V87, P3452, DOI 10.1210/jc.87.7.3452
   Uren AG, 2000, CURR BIOL, V10, P1319, DOI 10.1016/S0960-9822(00)00769-7
   Wall NR, 2003, CANCER RES, V63, P230
   Wang HW, 2002, EMBO J, V21, P2602, DOI 10.1093/emboj/21.11.2602
   Wheatley SP, 2001, CURR BIOL, V11, P886, DOI 10.1016/S0960-9822(01)00238-X
   Xia WL, 2006, CANCER RES, V66, P1640, DOI 10.1158/0008-5472.CAN-05-2000
   Yamasaki T, 2001, NDT&E INT, V34, P207, DOI 10.1016/S0963-8695(00)00060-8
   Yoshida H, 2001, INT J ONCOL, V19, P537
   Zhang T, 2001, CANCER RES, V61, P8664
   Zhao J, 2000, J CELL SCI, V113, P4363
   Zhou MX, 2002, J PHARMACOL EXP THER, V303, P124, DOI 10.1124/jpet.102.037192
   ZHU DE, 2006, CANCER GENE THER, V13, P1
NR 61
TC 25
Z9 28
U1 0
U2 5
PU FRONTIERS IN BIOSCIENCE INC
PI IRVINE
PA 16471 SCIENTIFIC WAY, IRVINE, CA 92618 USA
SN 1093-9946
EI 1093-4715
J9 FRONT BIOSCI-LANDMRK
JI Front. Biosci.
PD JAN 1
PY 2007
VL 12
BP 1260
EP 1270
DI 10.2741/2144
PG 11
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA 129QS
UT WOS:000243745000101
PM 17127378
OA Bronze
DA 2025-04-10
ER

PT J
AU Machuca-Tzili, L
   Thorpe, H
   Robinson, TE
   Sewry, C
   Brook, JD
AF Machuca-Tzili, Laura
   Thorpe, Helena
   Robinson, Thelma E.
   Sewry, Caroline
   Brook, J. David
TI Flies deficient in Muscleblind protein model features of myotonic
   dystrophy with altered splice forms of Z-band associated transcripts
SO HUMAN GENETICS
LA English
DT Article
ID EXPANDED-REPEAT TRANSCRIPTS; CUG-BINDING PROTEIN; PRE-MESSENGER-RNA;
   SKELETAL-MUSCLE; ALPHA-ACTININ; NUCLEAR FOCI; DILATED CARDIOMYOPATHY;
   TRINUCLEOTIDE REPEAT; UNTRANSLATED REGION; MUSCULAR-DYSTROPHY
AB Myotonic dystrophy (DM) is a dominantly inherited neuromuscular disorder characterised by muscle weakness and wasting. There are two forms of DM; both of which are caused by the expansion of repeated DNA sequences. DM1 is associated with a CTG repeat located in the 3' untranslated region of a gene, DMPK and DM2 with a tetranucleotide repeat expansion, CCTG, located in the first intron of a different gene, ZNF9. Recent data suggest a dominant RNA gain-of-function mechanism underlying DM, as transcripts containing either CUG or CCUG repeat expansions accumulate as foci in the nuclei of DM1 and DM2 cells respectively, where they exert a toxic effect, sequestering specific RNA binding proteins such as Muscleblind, which leads to splicing defects and the disruption of normal cellular functions. Z-band disruption is a well-known histological feature of DM1 muscle, which has also been reported in Muscleblind deficient flies. In order to determine whether there is a common molecular basis for this abnormality we have examined the alternative splicing pattern of transcripts that encode proteins associated with the Z-band in both organisms. Our results demonstrate that the missplicing of ZASP/LDB3 leads to the expression of an isoform in DM1 patient muscle, which is not present in normal controls, nor in other myopathies. Furthermore the Drosophila homologue, CG30084, is also misspliced, in Muscleblind deficient flies. Another Z-band transcript, alpha actinin, is misspliced in mbl mutant flies, but not in DM1 patient samples. These results point to similarities but subtle differences in the molecular breakdown of Z-band structures in flies and DM patients and emphasise the relevance of Muscleblind proteins in DM pathophysiology.
C1 Univ Nottingham, Inst Genet, Queens Med Ctr, Nottingham NG7 2UH, England.
   Robert Jones & Agnes Hunt Orthopaed Hosp, Ctr Inherited Neuromuscular Dis, Oswestry SY10 7AG, Shrops, England.
C3 University of Nottingham; Keele University
RP Brook, JD (corresponding author), Univ Nottingham, Inst Genet, Queens Med Ctr, Nottingham NG7 2UH, England.
EM David.Brook@nottingham.ac.uk
OI Brook, John David/0000-0002-5946-6740
CR [Anonymous], 2000, Drosophila Protocols
   Arimura T, 2004, J BIOL CHEM, V279, P6746, DOI 10.1074/jbc.M311849200
   Artero R, 1998, DEV BIOL, V195, P131, DOI 10.1006/dbio.1997.8833
   Begemann G, 1997, DEVELOPMENT, V124, P4321
   BEGGS AH, 1992, J BIOL CHEM, V267, P9281
   BROOK, 1992, CELL, V69, P385
   BROOK JD, 1992, CELL, V68, P799, DOI 10.1016/0092-8674(92)90154-5
   Buj-Bello A, 2002, HUM MOL GENET, V11, P2297, DOI 10.1093/hmg/11.19.2297
   Casso D, 1999, MECH DEVELOP, V88, P229, DOI 10.1016/S0925-4773(99)00174-4
   Charlet-B N, 2002, MOL CELL, V10, P45, DOI 10.1016/S1097-2765(02)00572-5
   Davis BM, 1997, P NATL ACAD SCI USA, V94, P7388, DOI 10.1073/pnas.94.14.7388
   Fardaei M, 2002, HUM MOL GENET, V11, P805, DOI 10.1093/hmg/11.7.805
   Fardaei M, 2001, NUCLEIC ACIDS RES, V29, P2766, DOI 10.1093/nar/29.13.2766
   Faulkner G, 1999, J CELL BIOL, V146, P465, DOI 10.1083/jcb.146.2.465
   Fomenkov A, 2003, J BIOL CHEM, V278, P23906, DOI 10.1074/jbc.M300746200
   FU YH, 1992, SCIENCE, V255, P1256, DOI 10.1126/science.1546326
   GEORGE AL, 1993, NAT GENET, V3, P305, DOI 10.1038/ng0493-305
   GOLDSTEIN MA, 1988, J GEN PHYSIOL, V92, P113, DOI 10.1085/jgp.92.1.113
   GOLDSTEIN MA, 1987, FASEB J, V1, P133, DOI 10.1096/fasebj.1.2.3609610
   Hamshere MG, 1997, P NATL ACAD SCI USA, V94, P7394, DOI 10.1073/pnas.94.14.7394
   Harper P.S. Monckton., 2001, MYOTONIC DYSTROPHY, V3e
   Ho TH, 2004, EMBO J, V23, P3103, DOI 10.1038/sj.emboj.7600300
   Jiang H, 2004, HUM MOL GENET, V13, P3079, DOI 10.1093/hmg/ddh327
   Kanadia RN, 2003, SCIENCE, V302, P1978, DOI 10.1126/science.1088583
   KENNEDY MB, 1995, TRENDS BIOCHEM SCI, V20, P350, DOI 10.1016/S0968-0004(00)89074-X
   Kimura T, 2005, HUM MOL GENET, V14, P2189, DOI 10.1093/hmg/ddi223
   Klaavuniemi T, 2006, EXP CELL RES, V312, P1299, DOI 10.1016/j.yexcr.2005.12.036
   Klaavuniemi T, 2004, J BIOL CHEM, V279, P26402, DOI 10.1074/jbc.M401871200
   KLINKERFUSS GH, 1967, ARCH NEUROL-CHICAGO, V16, P181, DOI 10.1001/archneur.1967.00470200069006
   Ladd AN, 2005, DEV DYNAM, V233, P783, DOI 10.1002/dvdy.20382
   Ladd AN, 2001, MOL CELL BIOL, V21, P1285, DOI 10.1128/MCB.21.4.1285-1296.2001
   Le Ber I, 2004, BRAIN, V127, P1979, DOI 10.1093/brain/awh216
   Liquori CL, 2001, SCIENCE, V293, P864, DOI 10.1126/science.1062125
   LUDATSCHER RM, 1978, J CLIN PATHOL, V31, P1057, DOI 10.1136/jcp.31.11.1057
   Luther PK, 2003, J MOL BIOL, V332, P161, DOI 10.1016/S0022-2836(03)00883-0
   Machuca-Tzili LE, 2003, AM J HUM GENET, V73, P576
   MAHADEVAN M, 1992, SCIENCE, V255, P1253, DOI 10.1126/science.1546325
   Mankodi A, 2002, MOL CELL, V10, P35, DOI 10.1016/S1097-2765(02)00563-4
   Mankodi A, 2001, HUM MOL GENET, V10, P2165, DOI 10.1093/hmg/10.19.2165
   Michalowski S, 1999, NUCLEIC ACIDS RES, V27, P3534, DOI 10.1093/nar/27.17.3534
   Miller JW, 2000, EMBO J, V19, P4439, DOI 10.1093/emboj/19.17.4439
   Monferrer L, 2006, J HERED, V97, P67, DOI 10.1093/jhered/esj003
   Pascual M, 2006, DIFFERENTIATION, V74, P65, DOI 10.1111/j.1432-0436.2006.00060.x
   Philips AV, 1998, SCIENCE, V280, P737, DOI 10.1126/science.280.5364.737
   Ranum LPW, 1998, NAT GENET, V19, P196, DOI 10.1038/570
   Savkur RS, 2004, AM J HUM GENET, V74, P1309, DOI 10.1086/421528
   Savkur RS, 2001, NAT GENET, V29, P40, DOI 10.1038/ng704
   Selcen D, 2005, ANN NEUROL, V57, P269, DOI 10.1002/ana.20376
   Sergeant N, 2001, HUM MOL GENET, V10, P2143, DOI 10.1093/hmg/10.19.2143
   Staden R, 1996, MOL BIOTECHNOL, V5, P233, DOI 10.1007/BF02900361
   TANEJA KL, 1995, J CELL BIOL, V128, P995, DOI 10.1083/jcb.128.6.995
   Tiso N, 1999, BIOCHEM BIOPH RES CO, V265, P256, DOI 10.1006/bbrc.1999.1661
   Vatta M, 2003, J AM COLL CARDIOL, V42, P2014, DOI 10.1016/j.jacc.2003.10.021
   Xing YL, 2006, MOL GENET METAB, V88, P71, DOI 10.1016/j.ymgme.2005.11.009
   Zhou Q, 2001, J CELL BIOL, V155, P605, DOI 10.1083/jcb.200107092
NR 55
TC 33
Z9 39
U1 0
U2 3
PU SPRINGER
PI NEW YORK
PA 233 SPRING ST, NEW YORK, NY 10013 USA
SN 0340-6717
EI 1432-1203
J9 HUM GENET
JI Hum. Genet.
PD NOV
PY 2006
VL 120
IS 4
BP 487
EP 499
DI 10.1007/s00439-006-0228-8
PG 13
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA 102DT
UT WOS:000241791900004
PM 16927100
DA 2025-04-10
ER

PT J
AU Bahouth, SW
   Nooh, MM
   Mancarella, S
AF Bahouth, Suleiman W.
   Nooh, Mohammed M.
   Mancarella, Salvatore
TI Involvement of SAP97 anchored multiprotein complexes in regulating
   cardiorenal signaling and trafficking networks
SO BIOCHEMICAL PHARMACOLOGY
LA English
DT Review
DE MAGUK; SAP97; ?1-adrenergic receptor; AQP2; AKAP5; PKA; Voltage gated
   cardiac channels; Knockout mice
ID SYNAPSE-ASSOCIATED PROTEIN; GUANYLATE KINASE DOMAINS; DISCS-LARGE;
   PDZ-DOMAIN; PLASMA-MEMBRANE; BETA-1-ADRENERGIC RECEPTOR; SCAFFOLDING
   PROTEINS; FUNCTIONAL-ANALYSIS; CHANNEL EXPRESSION; PROTEOMIC ANALYSIS
AB SAP97 is a member of the MAGUK family of proteins, but unlike other MAGUK proteins that are selectively expressed in the CNS, SAP97 is also expressed in peripheral organs, like the heart and kidneys. SAP97 has several protein binding cassettes, and this review will describe their involvement in creating SAP97-anchored multi -protein networks. SAP97-anchored networks localized at the inner leaflet of the cell membrane play a major role in trafficking and targeting of membrane G protein-coupled receptors (GPCR), channels, and structural proteins. SAP97 plays a major role in compartmentalizing voltage gated sodium and potassium channels to specific cellular compartments of heart cells. SAP97 undergoes extensive alternative splicing. These splice variants give rise to different SAP97 isoforms that alter its cellular localization, networking, signaling and trafficking effects. Regarding GPCR, SAP97 binds to the beta 1-adrenergic receptor and recruits AKAP5/PKA and PDE4D8 to create a multiprotein complex that regulates trafficking and signaling of cardiac beta 1-AR. In the kidneys, SAP97 anchored networks played a role in trafficking of aquaporin-2 water channels. Cardiac specific ablation of SAP97 (SAP97-cKO) resulted in cardiac hypertrophy and failure in aging mice. Similarly, instituting transverse aortic constriction (TAC) in young SAP97 c-KO mice exacerbated TAC-induced cardiac remodeling and dysfunction. These findings highlight a critical role for SAP97 in the pathophysiology of a number of cardiac and renal dis-eases, suggesting that SAP97 is a relevant target for drug discovery.
C1 [Bahouth, Suleiman W.] Univ Tennessee, Hlth Sci Ctr, Dept Pharmacol Addict Sci & Toxicol, Memphis, TN 38163 USA.
   [Nooh, Mohammed M.] Cairo Univ, Dept Biochem, Fac Pharm, Cairo, Egypt.
   [Nooh, Mohammed M.] October 6 Univ, Fac Pharm, Biochem Dept, Giza, Egypt.
   [Mancarella, Salvatore] Univ Tennessee, Hlth Sci Ctr, Dept Physiol, Memphis, TN USA.
C3 University of Tennessee System; University of Tennessee Health Science
   Center; Egyptian Knowledge Bank (EKB); Cairo University; Egyptian
   Knowledge Bank (EKB); October 6 University (O6U); University of
   Tennessee System; University of Tennessee Health Science Center
RP Bahouth, SW (corresponding author), Univ Tennessee, Hlth Sci Ctr, Dept Pharmacol Addict Sci & Toxicol, Memphis, TN 38163 USA.
EM sbahouth@uthsc.edu
OI Nooh, Mohammed/0000-0001-9794-4099
FU National Heart, Lung, and Blood Institute Grant [HL-085848]; Bridge
   Funding support from the College of Medicine at the University of
   Tennessee Health Sciences Center
FX This work was supported by National Heart, Lung, and Blood Institute
   Grant HL-085848 and by Bridge Funding support from the College of
   Medicine at the University of Tennessee Health Sciences Center.
CR Ahn SY, 2013, J AM SOC NEPHROL, V24, P1127, DOI 10.1681/ASN.2012111074
   Albesa M, 2011, CARDIOVASC RES, V89, P320, DOI 10.1093/cvr/cvq326
   Anderson JM, 1996, CURR BIOL, V6, P382, DOI 10.1016/S0960-9822(02)00501-8
   Asimaki A, 2014, SCI TRANSL MED, V6, DOI 10.1126/scitranslmed.3008008
   Atasoy D, 2007, P NATL ACAD SCI USA, V104, P2525, DOI 10.1073/pnas.0611003104
   Bahouth SW, 2017, CELL SIGNAL, V36, P42, DOI 10.1016/j.cellsig.2017.04.015
   Baines AJ, 2014, BBA-BIOMEMBRANES, V1838, P605, DOI 10.1016/j.bbamem.2013.05.030
   Bassand P, 1999, EUR J NEUROSCI, V11, P2031, DOI 10.1046/j.1460-9568.1999.00611.x
   Beuriot A, 2020, HEART RHYTHM, V17, P786, DOI 10.1016/j.hrthm.2019.12.019
   Bhat HF, 2013, CELL MOL LIFE SCI, V70, P2533, DOI 10.1007/s00018-012-1233-9
   Bissen D, 2019, CELL MOL LIFE SCI, V76, P2133, DOI 10.1007/s00018-019-03068-7
   Boucrot E, 2015, NATURE, V517, P460, DOI 10.1038/nature14067
   Broselid S, 2014, J BIOL CHEM, V289, P22117, DOI 10.1074/jbc.M114.566893
   Cai CL, 2006, J BIOL CHEM, V281, P4267, DOI 10.1074/jbc.M505886200
   Caruana G, 2002, INT J DEV BIOL, V46, P511
   Caruana G, 2001, MOL CELL BIOL, V21, P1475, DOI 10.1128/MCB.21.5.1475-1483.2001
   Chishti AH, 1998, TRENDS BIOCHEM SCI, V23, P281, DOI 10.1016/S0968-0004(98)01237-7
   Christensen NR, 2019, ADV THER-GERMANY, V2, DOI 10.1002/adtp.201800143
   Cohen AR, 1998, J CELL BIOL, V142, P129, DOI 10.1083/jcb.142.1.129
   Colledge M, 2000, NEURON, V27, P107, DOI 10.1016/S0896-6273(00)00013-1
   Craven SE, 1998, CELL, V93, P495, DOI 10.1016/S0092-8674(00)81179-4
   Cunha SR, 2011, SEMIN CELL DEV BIOL, V22, P166, DOI 10.1016/j.semcdb.2010.09.013
   Dimitratos SD, 1999, BIOESSAYS, V21, P912, DOI 10.1002/(SICI)1521-1878(199911)21:11<912::AID-BIES3>3.0.CO;2-Z
   Doerks T, 2000, TRENDS BIOCHEM SCI, V25, P317, DOI 10.1016/S0968-0004(00)01599-1
   Dunn HA, 2015, MOL PHARMACOL, V88, P624, DOI 10.1124/mol.115.098509
   Eichel CA, 2016, CIRC RES, V119, P544, DOI 10.1161/CIRCRESAHA.116.309254
   El-Haou S, 2009, CIRC RES, V104, P758, DOI 10.1161/CIRCRESAHA.108.191007
   Feng W, 2004, NAT STRUCT MOL BIOL, V11, P475, DOI 10.1038/nsmb751
   Folco EJ, 2004, AM J PHYSIOL-HEART C, V287, pH681, DOI 10.1152/ajpheart.00152.2004
   Fourie C, 2014, BBA-BIOMEMBRANES, V1838, P589, DOI 10.1016/j.bbamem.2013.03.015
   Frese KK, 2006, EMBO J, V25, P1406, DOI 10.1038/sj.emboj.7601030
   Fu Q, 2014, J BIOL CHEM, V289, P14771, DOI 10.1074/jbc.M113.542589
   Fujita A, 2000, BIOCHEM BIOPH RES CO, V269, P1, DOI 10.1006/bbrc.1999.1893
   Funke L, 2005, ANNU REV BIOCHEM, V74, P219, DOI 10.1146/annurev.biochem.74.082803.133339
   Gardner LA, 2004, J BIOL CHEM, V279, P21135, DOI 10.1074/jbc.M313652200
   Gardner LA, 2007, J BIOL CHEM, V282, P5085, DOI 10.1074/jbc.M608871200
   Gardner LA, 2006, J BIOL CHEM, V281, P33537, DOI 10.1074/jbc.M601809200
   Gillet L, 2015, HEART RHYTHM, V12, P181, DOI 10.1016/j.hrthm.2014.09.057
   Godreau D, 2003, J BIOL CHEM, V278, P47046, DOI 10.1074/jbc.M308463200
   Gonzalez-Mariscal L, 2000, KIDNEY INT, V57, P2386, DOI 10.1046/j.1523-1755.2000.00098.x
   Goto T, 2013, CELL SIGNAL, V25, P690, DOI 10.1016/j.cellsig.2012.11.020
   Hanada T, 2003, J BIOL CHEM, V278, P34445, DOI 10.1074/jbc.M305209200
   He JQ, 2006, J BIOL CHEM, V281, P2820, DOI 10.1074/jbc.M509503200
   He JQ, 2004, J BIOL CHEM, V279, P50190, DOI 10.1074/jbc.M404876200
   Hoover KB, 2000, CURR OPIN CELL BIOL, V12, P229, DOI 10.1016/S0955-0674(99)00080-0
   Hough CD, 1997, GENE DEV, V11, P3242, DOI 10.1101/gad.11.23.3242
   Hsueh YP, 1998, J CELL BIOL, V142, P139, DOI 10.1083/jcb.142.1.139
   Humbert P, 2003, BIOESSAYS, V25, P542, DOI 10.1002/bies.10286
   Humbert PO, 2008, ONCOGENE, V27, P6888, DOI 10.1038/onc.2008.341
   Iizuka-Kogo A, 2007, DEVELOPMENT, V134, P1799, DOI 10.1242/dev.02830
   Jemth P, 2007, BIOCHEMISTRY-US, V46, P8701, DOI 10.1021/bi7008618
   Jeyifous O, 2009, NAT NEUROSCI, V12, P1011, DOI 10.1038/nn.2362
   Karnak D, 2002, J BIOL CHEM, V277, P46730, DOI 10.1074/jbc.M208781200
   Katsura T, 1997, AM J PHYSIOL-RENAL, V272, pF816
   Kim E, 1997, J CELL BIOL, V136, P669, DOI 10.1083/jcb.136.3.669
   Koliwer J, 2015, J BIOL CHEM, V290, P6120, DOI 10.1074/jbc.M114.605725
   Kuhlendahl S, 1998, EUR J BIOCHEM, V252, P305, DOI 10.1046/j.1432-1327.1998.2520305.x
   Kuwahara M, 2001, AM J HUM GENET, V69, P738, DOI 10.1086/323643
   Le SS, 1997, P NATL ACAD SCI USA, V94, P6670, DOI 10.1073/pnas.94.13.6670
   Lee S, 2002, MOL CELL BIOL, V22, P1778, DOI 10.1128/MCB.22.6.1778-1791.2002
   Leonard AS, 1998, J BIOL CHEM, V273, P19518, DOI 10.1074/jbc.273.31.19518
   Leonoudakis D, 2004, J BIOL CHEM, V279, P22331, DOI 10.1074/jbc.M400285200
   Leonoudakis D, 2001, J CELL SCI, V114, P987
   Li JD, 2010, J BIOL CHEM, V285, P28723, DOI 10.1074/jbc.M110.147868
   Li X, 2014, CARDIOVASC RES, V104, P270, DOI 10.1093/cvr/cvu209
   Li X, 2013, J BIOL CHEM, V288, P33797, DOI 10.1074/jbc.M113.470559
   Li YH, 2004, EMBO J, V23, P2723, DOI 10.1038/sj.emboj.7600294
   Liu Y, 2007, BIOCHEMISTRY-US, V46, P10864, DOI 10.1021/bi700879k
   LUE RA, 1994, P NATL ACAD SCI USA, V91, P9818, DOI 10.1073/pnas.91.21.9818
   Mahoney ZX, 2006, P NATL ACAD SCI USA, V103, P19872, DOI 10.1073/pnas.0609326103
   Makara MA, 2018, JACC-BASIC TRANSL SC, V3, P675, DOI 10.1016/j.jacbts.2018.07.008
   Mangmool S, 2010, J CELL BIOL, V189, P573, DOI 10.1083/jcb.200911047
   MARFATIA SM, 1995, J BIOL CHEM, V270, P715, DOI 10.1074/jbc.270.2.715
   Matamoros M, 2016, CARDIOVASC RES, V110, P279, DOI 10.1093/cvr/cvw009
   McGee AW, 2001, MOL CELL, V8, P1291, DOI 10.1016/S1097-2765(01)00411-7
   McLaughlin M, 2002, J BIOL CHEM, V277, P6406, DOI 10.1074/jbc.M108724200
   Milstein ML, 2012, P NATL ACAD SCI USA, V109, pE2134, DOI 10.1073/pnas.1109370109
   Mohler PJ, 2004, P NATL ACAD SCI USA, V101, P17533, DOI 10.1073/pnas.0403711101
   Mori K, 1998, J HUM GENET, V43, P123, DOI 10.1007/s100380050052
   Mori S, 2013, BIOCHEM BIOPH RES CO, V435, P334, DOI 10.1016/j.bbrc.2013.04.056
   MULLER BM, 1995, J NEUROSCI, V15, P2354, DOI 10.1523/JNEUROSCI.15-03-02354.1995
   Musa H, 2020, AM J PHYSIOL-HEART C, V318, pH1357, DOI 10.1152/ajpheart.00481.2019
   Mustroph J, 2021, CIRC RES, V128, P1139, DOI 10.1161/CIRCRESAHA.120.318170
   Naim E, 2005, KIDNEY INT, V68, P955, DOI 10.1111/j.1523-1755.2005.00489.x
   Nakagawa T, 2004, NEURON, V44, P453, DOI 10.1016/j.neuron.2004.10.012
   Nguyen MM, 2003, MOL CELL BIOL, V23, P8970, DOI 10.1128/MCB.23.24.8970-8981.2003
   Nichols CB, 2010, CIRC RES, V107, P747, DOI 10.1161/CIRCRESAHA.109.216127
   Nikandrova YA, 2010, J BIOL CHEM, V285, P923, DOI 10.1074/jbc.M109.033985
   Nix SL, 2000, J BIOL CHEM, V275, P41192, DOI 10.1074/jbc.M002078200
   Noda Y, 2004, FEBS LETT, V568, P139, DOI 10.1016/j.febslet.2004.05.021
   Nooh MM, 2019, AM J PHYSIOL-RENAL, V317, pF375, DOI 10.1152/ajprenal.00228.2018
   Nooh MM, 2018, MOL PHARMACOL, V94, P862, DOI 10.1124/mol.118.112045
   Nooh MM, 2014, J BIOL CHEM, V289, P2277, DOI 10.1074/jbc.M113.513481
   Nooh MM, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0063379
   O'Neill AK, 2011, J BIOL CHEM, V286, P43559, DOI 10.1074/jbc.M111.294603
   Olesen ETB, 2021, NAT REV NEPHROL, V17, P765, DOI 10.1038/s41581-021-00447-x
   Olsen O, 2003, J BIOL CHEM, V278, P6873, DOI 10.1074/jbc.M210165200
   Omar MH, 2022, CELL REP, V40, DOI 10.1016/j.celrep.2022.111073
   Omar MH, 2020, TRENDS PHARMACOL SCI, V41, P933, DOI 10.1016/j.tips.2020.09.007
   Oxford EM, 2007, CIRC RES, V101, P703, DOI 10.1161/CIRCRESAHA.107.154252
   Paarmann I, 2002, J BIOL CHEM, V277, P40832, DOI 10.1074/jbc.M205618200
   Paarmann I, 2008, PROTEIN SCI, V17, P1946, DOI 10.1110/ps.035550.108
   Peters CJ, 2009, J MOL CELL CARDIOL, V46, P636, DOI 10.1016/j.yjmcc.2009.01.010
   Petitprez S, 2011, CIRC RES, V108, P294, DOI 10.1161/CIRCRESAHA.110.228312
   Reilly L, 2021, HEART RHYTHM, V18, P1423, DOI 10.1016/j.hrthm.2021.04.008
   Rivera C, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0054410
   Roskoski R Jr, 2021, PHARMACOL RES, V168, DOI 10.1016/j.phrs.2021.105579
   Saras J, 1996, TRENDS BIOCHEM SCI, V21, P455, DOI 10.1016/S0968-0004(96)30044-3
   Schlüter OM, 2006, NEURON, V51, P99, DOI 10.1016/j.neuron.2006.05.016
   Setou M, 2000, SCIENCE, V288, P1796, DOI 10.1126/science.288.5472.1796
   Shcherbakova OG, 2007, J CELL BIOL, V176, P521, DOI 10.1083/jcb.200604167
   Shen L, 2000, J NEUROSCI, V20, P7932
   Sheng M, 2001, ANNU REV NEUROSCI, V24, P1, DOI 10.1146/annurev.neuro.24.1.1
   Sheng M, 2011, CSH PERSPECT BIOL, V3, DOI 10.1101/cshperspect.a005678
   Shin SM, 2012, NAT NEUROSCI, V15, P1655, DOI 10.1038/nn.3259
   Shy D, 2014, CIRCULATION, V130, P147, DOI 10.1161/CIRCULATIONAHA.113.007852
   Songyang Z, 1997, SCIENCE, V275, P73, DOI 10.1126/science.275.5296.73
   Takeuchi M, 1997, J BIOL CHEM, V272, P11943, DOI 10.1074/jbc.272.18.11943
   Tang YT, 1999, P NATL ACAD SCI USA, V96, P12559, DOI 10.1073/pnas.96.22.12559
   Toyooka K, 2002, J NEUROCHEM, V83, P797, DOI 10.1046/j.1471-4159.2002.01181.x
   Tully MD, 2012, BIOCHEMISTRY-US, V51, P899, DOI 10.1021/bi201178v
   Valenti G, 2005, ENDOCRINOLOGY, V146, P5063, DOI 10.1210/en.2005-0868
   Veerman CC, 2015, GENE, V573, P177, DOI 10.1016/j.gene.2015.08.062
   von Ossowski I, 2006, FEBS J, V273, P5219, DOI 10.1111/j.1742-4658.2006.05521.x
   Vukicevic T, 2016, FRONT PHARMACOL, V7, DOI 10.3389/fphar.2016.00023
   Waites CL, 2009, J NEUROSCI, V29, P4332, DOI 10.1523/JNEUROSCI.4431-08.2009
   Won S, 2017, CURR OPIN NEUROBIOL, V43, P94, DOI 10.1016/j.conb.2017.01.006
   Wu HJ, 2000, EMBO J, V19, P5740, DOI 10.1093/emboj/19.21.5740
   Wu HJ, 1998, J CELL SCI, V111, P2365
   Xiang Y, 2002, J BIOL CHEM, V277, P33783, DOI 10.1074/jbc.M204136200
   Xu B, 2020, CIRC RES, V127, P796, DOI 10.1161/CIRCRESAHA.119.316319
   Ye F, 2018, CURR OPIN STRUC BIOL, V48, P6, DOI 10.1016/j.sbi.2017.08.006
   Zhang L, 2015, MOL CELL NEUROSCI, V65, P31, DOI 10.1016/j.mcn.2015.02.011
   Zhang SS, 2014, CELL COMMUN ADHES, V21, P43, DOI 10.3109/15419061.2013.876014
   Zhou WG, 2008, J NEUROSCI, V28, P10220, DOI 10.1523/JNEUROSCI.3434-08.2008
   Zhu JW, 2016, NAT REV NEUROSCI, V17, P209, DOI 10.1038/nrn.2016.18
   Zhu JW, 2011, EMBO J, V30, P4986, DOI 10.1038/emboj.2011.428
NR 137
TC 2
Z9 2
U1 1
U2 4
PU PERGAMON-ELSEVIER SCIENCE LTD
PI OXFORD
PA THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND
SN 0006-2952
EI 1873-2968
J9 BIOCHEM PHARMACOL
JI Biochem. Pharmacol.
PD FEB
PY 2023
VL 208
AR 115406
DI 10.1016/j.bcp.2022.115406
EA JAN 2023
PG 14
WC Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Pharmacology & Pharmacy
GA 8I1HU
UT WOS:000921479900001
PM 36596415
OA Bronze
DA 2025-04-10
ER

PT J
AU Gao, C
   Wang, YB
AF Gao, Chen
   Wang, Yibin
TI mRNA METABOLISM IN CARDIAC DEVELOPMENT AND DISEASE: LIFE AFTER
   TRANSCRIPTION
SO PHYSIOLOGICAL REVIEWS
LA English
DT Review
DE development; gene regulation; heart diseases; mRNA;
   post-transcriptional; RNA binding protein; RNA processing
ID TRACT BINDING-PROTEIN; POSTTRANSCRIPTIONAL REGULATION; GENE-EXPRESSION;
   MYOTONIC-DYSTROPHY; QUALITY-CONTROL; DILATED CARDIOMYOPATHY; DYNAMIC
   ANTAGONISM; SPLICING FACTORS; NONCODING RNAS; EMERGING ROLES
AB The central dogma of molecular biology illustrates the importance of mRNAs as critical mediators between genetic information encoded at the DNA level and proteomes/metabolomes that determine the diverse functional outcome at the cellular and organ levels. Although the total number of protein-producing (coding) genes in the mammalian genome is similar to 20,000, it is evident that the intricate processes of cardiac development and the highly regulated physiological regulation in the normal heart, as well as the complex manifestation of pathological remodeling in a diseased heart, would require a much higher degree of complexity at the transcriptome level and beyond. Indeed, in addition to an extensive regulatory scheme implemented at the level of transcription, the complexity of transcript processing following transcription is dramatically increased. RNA processing includes post-transcriptional modification, alternative splicing, editing and transportation, ribosomal loading, and degradation. While transcriptional control of cardiac genes has been a major focus of investigation in recent decades, a great deal of progress has recently been made in our understanding of how post-transcriptional regulation of mRNA contributes to transcriptome complexity. In this review, we highlight some of the key molecular processes and major players in RNA maturation and post-transcriptional regulation. In addition, we provide an update to the recent progress made in the discovery of RNA processing regulators implicated in cardiac development and disease. While post-transcriptional modulation is a complex and challenging problem to study, recent technological advancements are paving the way for a new era of exciting discoveries and potential clinical translation in the context of cardiac biology and heart disease.
C1 Univ Calif Los Angeles, David Geffen Sch Med, Dept Anesthesiol, Los Angeles, CA 90095 USA.
   Univ Calif Los Angeles, David Geffen Sch Med, Dept Med, Los Angeles, CA 90095 USA.
   Univ Calif Los Angeles, David Geffen Sch Med, Dept Physiol, Los Angeles, CA 90095 USA.
C3 University of California System; University of California Los Angeles;
   University of California Los Angeles Medical Center; David Geffen School
   of Medicine at UCLA; University of California System; University of
   California Los Angeles; University of California Los Angeles Medical
   Center; David Geffen School of Medicine at UCLA; University of
   California System; University of California Los Angeles; University of
   California Los Angeles Medical Center; David Geffen School of Medicine
   at UCLA
RP Wang, YB (corresponding author), 650 Charles E Young St,Room CHS 37200J, Los Angeles, CA 90095 USA.
RI Gao, Chen/KZU-1046-2024
FU National Institutes of Health (NIH); American Heart Association; NIH;
   Department of Defense
FX The work is in part supported by a K99 Award from the National
   Institutes of Health (NIH) and a postdoctoral fel-lowship award and
   Career Development Award from American Heart Association (to C. Gao) and
   grants from NIH and the Department of Defense (to Y. Wang).
CR Abdelmohsen K, 2008, BIOL CHEM, V389, P243, DOI 10.1515/BC.2008.022
   Adhikari S, 2016, RNA BIOL, V13, P756, DOI 10.1080/15476286.2016.1201628
   Agirre E, 2015, BMC BIOL, V13, DOI 10.1186/s12915-015-0141-5
   Aguado A, 2016, J HYPERTENS, V34, P253, DOI 10.1097/HJH.0000000000000801
   Anderson P, 2015, BBA-GENE REGUL MECH, V1849, P861, DOI 10.1016/j.bbagrm.2014.11.009
   Andreassi C, 2018, FRONT MOL NEUROSCI, V11, DOI 10.3389/fnmol.2018.00304
   Andreev DE, 2017, NUCLEIC ACIDS RES, V45, P513, DOI 10.1093/nar/gkw1190
   [Anonymous], BIOCH BIOPHYS ACTA G
   [Anonymous], 2017, RNA BIOL, DOI DOI 10.1080/15476286.2016.1267096
   Auboeuf D, 2018, TRANSCR-AUSTIN, V9, P75, DOI 10.1080/21541264.2017.1373891
   Balacco DL, 2019, BIOCHEMISTRY-US, V58, P363, DOI 10.1021/acs.biochem.8b01166
   Baralle D, 2017, CLIN SCI, V131, P355, DOI 10.1042/CS20160211
   Baralle FE, 2017, NAT REV MOL CELL BIO, V18, P437, DOI 10.1038/nrm.2017.27
   Barreau C, 2005, NUCLEIC ACIDS RES, V33, P7138, DOI 10.1093/nar/gki1012
   Bartling B, 1999, CIRCULATION, V100, P216
   Batista PJ, 2017, GENOM PROTEOM BIOINF, V15, P154, DOI 10.1016/j.gpb.2017.03.002
   Beermann J, 2016, PHYSIOL REV, V96, P1297, DOI 10.1152/physrev.00041.2015
   Beqqali A, 2018, Biophys Rev, V10, P1061, DOI 10.1007/s12551-018-0439-y
   Beqqali A, 2016, CARDIOVASC RES, V112, P452, DOI 10.1093/cvr/cvw192
   Bielli P, 2014, NUCLEIC ACIDS RES, V42, P12070, DOI 10.1093/nar/gku922
   Blackinton JG, 2016, NUCLEIC ACIDS RES, V44, P426, DOI 10.1093/nar/gkv1066
   BOISE LH, 1993, CELL, V74, P597, DOI 10.1016/0092-8674(93)90508-N
   Brinegar AE, 2016, BRAIN RES, V1647, P1, DOI 10.1016/j.brainres.2016.02.050
   Buszczak M, 2014, CELL, V159, P242, DOI 10.1016/j.cell.2014.09.016
   Cadar AG, 2014, BIOCHEM BIOPH RES CO, V453, P185, DOI 10.1016/j.bbrc.2014.09.085
   Cao GC, 2016, OPEN BIOL, V6, DOI 10.1098/rsob.160003
   Cao T, 2018, TRENDS CARDIOVAS MED, V28, P81, DOI 10.1016/j.tcm.2017.08.002
   Carey KT, 2018, TRENDS GENET, V34, P279, DOI 10.1016/j.tig.2017.12.012
   Cazorla O, 2000, CIRC RES, V86, P59, DOI 10.1161/01.RES.86.1.59
   Chandola U, 2015, BRIEF FUNCT GENOMICS, V14, P169, DOI 10.1093/bfgp/elu039
   Chang KT, 2017, CIRC RES, V121, P1140, DOI 10.1161/CIRCRESAHA.117.311281
   Chang SH, 2014, P NATL ACAD SCI USA, V111, P18309, DOI 10.1073/pnas.1412172111
   Charlet-B N, 2002, MOL CELL, V9, P649, DOI 10.1016/S1097-2765(02)00479-3
   Chen Q, 2017, CURR OPIN GENET DEV, V46, P15, DOI 10.1016/j.gde.2017.06.010
   Chen Y, 2016, NUCLEIC ACIDS RES, V44, P4381, DOI 10.1093/nar/gkw177
   Chopra P, 2010, PLOS ONE, V5, DOI 10.1371/journal.pone.0014305
   Chorghade S, 2017, ELIFE, V6, DOI 10.7554/eLife.24139
   Chung CZ, 2017, BBA-GEN SUBJECTS, V1861, P2971, DOI 10.1016/j.bbagen.2017.05.003
   Churko JM, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-07333-4
   Coller JM, 1998, GENE DEV, V12, P3226, DOI 10.1101/gad.12.20.3226
   COOPER TA, 1988, NUCLEIC ACIDS RES, V16, P8443, DOI 10.1093/nar/16.17.8443
   COOPER TA, 1989, NUCLEIC ACIDS RES, V17, P7905, DOI 10.1093/nar/17.19.7905
   COOPER TA, 1985, J BIOL CHEM, V260, P1140
   Corbett AH, 2018, CURR OPIN CELL BIOL, V52, P96, DOI 10.1016/j.ceb.2018.02.011
   Covelo-Molares H, 2018, WIRES RNA, V9, DOI 10.1002/wrna.1489
   Cui XYA, 2014, WIRES RNA, V5, P481, DOI 10.1002/wrna.1225
   da Costa PJ, 2017, INT J BIOCHEM CELL B, V91, P168, DOI 10.1016/j.biocel.2017.07.013
   Dai DJ, 2018, CELL DEATH DIS, V9, DOI 10.1038/s41419-017-0129-x
   Damianov A, 2010, RNA, V16, P405, DOI 10.1261/rna.1838210
   Dasgupta T, 2012, WIRES RNA, V3, P104, DOI 10.1002/wrna.107
   De Almeida C, 2018, WIRES RNA, V9, DOI 10.1002/wrna.1440
   de Bruin RG, 2017, EUR HEART J, V38, P1380, DOI 10.1093/eurheartj/ehw567
   Decker CJ, 2012, CSH PERSPECT BIOL, V4, DOI 10.1101/cshperspect.a012286
   Deniaud A, 2015, NUCLEIC ACIDS RES, V43, P7600, DOI 10.1093/nar/gkv668
   Ding JH, 2004, EMBO J, V23, P885, DOI 10.1038/sj.emboj.7600054
   Dorn LE, 2019, CIRCULATION, V139, P533, DOI 10.1161/CIRCULATIONAHA.118.036146
   Duan HC, 2019, WIRES RNA, V10, DOI 10.1002/wrna.1507
   Dyle MC, 2020, WIRES RNA, V11, DOI 10.1002/wrna.1560
   Erson-Bensan Ayse Elif, 2017, Microrna, V6, P97, DOI 10.2174/2211536606666170511102219
   Escayola DA, 2018, BIOCHEMISTRY-US, V57, P2462, DOI 10.1021/acs.biochem.7b01262
   Fan C, 2009, J BIOL CHEM, V284, P25653, DOI 10.1074/jbc.M109.041368
   Feng HZ, 2014, PHYSIOL REP, V2, DOI 10.14814/phy2.12139
   Fonseca BD, 2018, WIRES RNA, V9, DOI 10.1002/wrna.1480
   Frese KS, 2015, J CELL SCI, V128, P3030, DOI 10.1242/jcs.166850
   Freyermuth F, 2016, NAT COMMUN, V7, DOI 10.1038/ncomms11067
   Frye M, 2018, SCIENCE, V361, P1346, DOI 10.1126/science.aau1646
   Gallagher TL, 2011, DEV BIOL, V359, P251, DOI 10.1016/j.ydbio.2011.08.025
   Galloway A, 2019, BBA-GENE REGUL MECH, V1862, P270, DOI 10.1016/j.bbagrm.2018.09.011
   Gandal MJ, 2018, SCIENCE, V362, P1265, DOI 10.1126/science.aat8127
   Gao C, 2016, J CLIN INVEST, V126, P195, DOI 10.1172/JCI84015
   GARLICK PJ, 1980, BIOCHEM J, V192, P719, DOI 10.1042/bj1920719
   Gerbracht JV, 2018, BIOCHEM SOC T, V46, P153, DOI 10.1042/BST20170059
   Gerstberger S, 2014, NAT REV GENET, V15, P829, DOI 10.1038/nrg3813
   Geuens T, 2016, HUM GENET, V135, P851, DOI 10.1007/s00439-016-1683-5
   Giudice J, 2016, SCI REP-UK, V6, DOI 10.1038/srep35550
   Giudice J, 2014, ADV EXP MED BIOL, V825, P389, DOI 10.1007/978-1-4939-1221-6_11
   Giulietti M, 2013, NUCLEIC ACIDS RES, V41, pD125, DOI 10.1093/nar/gks997
   Golani-Armon A, 2016, BIOCHEMISTRY-MOSCOW+, V81, P1038, DOI 10.1134/S0006297916100023
   Greenleaf AL, 2019, TRANSCR-AUSTIN, V10, P91, DOI 10.1080/21541264.2018.1535211
   Gripp KW, 2011, AM J MED GENET A, V155A, P2516, DOI 10.1002/ajmg.a.34190
   Gunning PW, 2015, J CELL SCI, V128, P2965, DOI 10.1242/jcs.172502
   Guo WG, 2014, J MOL CELL CARDIOL, V75, P131, DOI 10.1016/j.yjmcc.2014.07.010
   Guo W, 2012, NAT MED, V18, P766, DOI 10.1038/nm.2693
   Guzikowski AR, 2019, WIRES RNA, V10, DOI 10.1002/wrna.1524
   Harvey R, 2017, BIOCHEM SOC T, V45, P1007, DOI 10.1042/BST20160364
   Hasin-Brumshtein Y, 2016, ELIFE, V5, DOI 10.7554/eLife.15614
   Hautbergue GM, 2017, ADV EXP MED BIOL, V1007, P89, DOI 10.1007/978-3-319-60733-7_6
   Herzel L, 2017, NAT REV MOL CELL BIO, V18, P637, DOI 10.1038/nrm.2017.63
   Hinkle ER, 2019, TRANSCR-AUSTIN, V10, P1, DOI 10.1080/21541264.2018.1558677
   Hinze F, 2016, J MOL MED, V94, P1349, DOI 10.1007/s00109-016-1483-3
   Hitchcock-DeGregori SE, 2017, SUBCELL BIOCHEM, V82, P253, DOI 10.1007/978-3-319-49674-0_9
   Houston DW, 2013, INT REV CEL MOL BIO, V306, P127, DOI 10.1016/B978-0-12-407694-5.00004-3
   Hu J, 2019, P NATL ACAD SCI USA, V116, P6172, DOI 10.1073/pnas.1822176116
   Hu ZY, 2017, GENES-BASEL, V8, DOI 10.3390/genes8120344
   Huang C, 2010, INT J BIOL SCI, V6, P396
   Hug N, 2016, NUCLEIC ACIDS RES, V44, P1483, DOI 10.1093/nar/gkw010
   Iakova P, 2004, EMBO J, V23, P406, DOI 10.1038/sj.emboj.7600052
   Jansen RP, 2014, TRENDS GENET, V30, P408, DOI 10.1016/j.tig.2014.07.002
   Jia WY, 2017, LIFE SCI, V186, P1, DOI 10.1016/j.lfs.2017.07.025
   Kahvejian A, 2005, GENE DEV, V19, P104, DOI 10.1101/gad.1262905
   Kalsotra A, 2008, P NATL ACAD SCI USA, V105, P20333, DOI 10.1073/pnas.0809045105
   Karam CN, 2011, J MUSCLE RES CELL M, V31, P315, DOI 10.1007/s10974-010-9237-2
   Kargapolova Y, 2017, NUCLEIC ACIDS RES, V45, P6074, DOI 10.1093/nar/gkx152
   Kasprowicz-Maluski A, 2016, ACTA BIOCHIM POL, V63, P693, DOI 10.18388/abp.2016_1359
   Kishor A, 2019, WIRES RNA, V10, DOI 10.1002/wrna.1548
   Klein AF, 2015, CURR GENE THER, V15, P329, DOI 10.2174/1566523215666150630120537
   Kong SW, 2010, CIRC-CARDIOVASC GENE, V3, P138, DOI 10.1161/CIRCGENETICS.109.904698
   Koshelev M, 2010, HUM MOL GENET, V19, P1066, DOI 10.1093/hmg/ddp570
   Kurosaki T, 2019, NAT REV MOL CELL BIO, V20, P406, DOI 10.1038/s41580-019-0126-2
   Kurosaki T, 2016, J CELL SCI, V129, P461, DOI 10.1242/jcs.181008
   Kuroyanagi H, 2006, NAT METHODS, V3, P909, DOI 10.1038/NMETH944
   Kuyumcu-Martinez NM, 2007, MOL CELL, V28, P68, DOI 10.1016/j.molcel.2007.07.027
   Ladd AN, 2016, INT REV CEL MOL BIO, V324, P125, DOI 10.1016/bs.ircmb.2015.12.009
   Ladd AN, 2005, DEV DYNAM, V233, P783, DOI 10.1002/dvdy.20382
   Lee BH, 2016, MOL CELLS, V39, P841, DOI 10.14348/molcells.2016.0277
   Lee JH, 2011, CIRC RES, V109, P1332, DOI 10.1161/CIRCRESAHA.111.249433
   Lee JA, 2016, NEURON, V89, P113, DOI 10.1016/j.neuron.2015.11.025
   Lee JA, 2009, GENE DEV, V23, P2284, DOI 10.1101/gad.1837009
   Lee JE, 2009, BIOCHEM SOC T, V37, P1281, DOI 10.1042/BST0371281
   Lee M, 2014, CELL, V158, P980, DOI 10.1016/j.cell.2014.08.005
   Lee Y, 2015, ANNU REV BIOCHEM, V84, P291, DOI 10.1146/annurev-biochem-060614-034316
   Lejeune F, 2017, BMB REP, V50, P175, DOI 10.5483/BMBRep.2017.50.4.015
   Lesnik C, 2015, RNA BIOL, V12, P801, DOI 10.1080/15476286.2015.1058686
   Lewis CJT, 2017, NAT REV MOL CELL BIO, V18, P202, DOI 10.1038/nrm.2016.163
   LEWIS SEM, 1984, BIOCHEM J, V217, P517, DOI 10.1042/bj2170517
   Li SJ, 2013, NUCLEIC ACIDS RES, V41, P2659, DOI 10.1093/nar/gks1362
   Linder B, 2015, NAT METHODS, V12, P767, DOI [10.1038/nmeth.3453, 10.1038/NMETH.3453]
   Liu J, 2019, PROTEIN CELL, V10, P405, DOI 10.1007/s13238-018-0578-8
   Liu N, 2010, DEV CELL, V18, P510, DOI 10.1016/j.devcel.2010.03.010
   Liu TY, 2017, OPEN BIOL, V7, DOI 10.1098/rsob.160303
   Liu Y, 2019, BBA-GENE REGUL MECH, V1862, P209, DOI 10.1016/j.bbagrm.2018.11.006
   Loiselle JJ, 2014, IN VITRO CELL DEV-AN, V50, P331, DOI 10.1007/s11626-013-9708-z
   López-Morató M, 2018, FRONT NEUROL, V9, DOI 10.3389/fneur.2018.00349
   Lu S, 2016, BIOCHEM BIOPH RES CO, V473, P993, DOI 10.1016/j.bbrc.2016.04.004
   Luo Y, 2018, BIOCHEMISTRY-US, V57, P2424, DOI 10.1021/acs.biochem.7b01162
   Lykke-Andersen S, 2015, NAT REV MOL CELL BIO, V16, P665, DOI 10.1038/nrm4063
   MacNicol MC, 2015, BIOMOLECULES, V5, P1580, DOI 10.3390/biom5031580
   Makeyev AV, 2002, RNA, V8, P265, DOI 10.1017/S1355838202024627
   Man SM, 2015, IMMUNOL REV, V265, P6, DOI 10.1111/imr.12296
   Martinez NM, 2018, QUANT BIOL, V6, P210, DOI 10.1007/s40484-018-0147-4
   Mathiyalagan P, 2019, CIRCULATION, V139, P518, DOI 10.1161/CIRCULATIONAHA.118.033794
   Matoulkova E, 2012, RNA BIOL, V9, P563, DOI 10.4161/rna.20231
   Medioni C, 2018, METHODS MOL BIOL, V1649, P1, DOI 10.1007/978-1-4939-7213-5_1
   Meier UT, 2017, RNA BIOL, V14, P693, DOI 10.1080/15476286.2016.1249091
   Miller JW, 2000, EMBO J, V19, P4439, DOI 10.1093/emboj/19.17.4439
   Mohan N, 2018, CELL REP, V24, P3539, DOI 10.1016/j.celrep.2018.08.077
   Mohanty BK, 2019, METHODS, V155, P124, DOI 10.1016/j.ymeth.2018.11.006
   Morton DJ, 2018, RNA, V24, P127, DOI 10.1261/rna.064626.117
   Moujaber O, 2018, GERONTOLOGY, V64, P485, DOI 10.1159/000488759
   Mukhopadhyay D, 2003, MOL CELL, V11, P113, DOI 10.1016/S1097-2765(03)00012-1
   MULLIGAN GJ, 1992, J BIOL CHEM, V267, P25480
   Munoz-Tello P, 2015, BIOMED RES INT, V2015, DOI 10.1155/2015/968127
   Murmu N, 2004, P NATL ACAD SCI USA, V101, P13873, DOI 10.1073/pnas.0406066101
   Nagel RJ, 1998, RNA, V4, P11
   Nakahata S, 2005, NUCLEIC ACIDS RES, V33, P2078, DOI 10.1093/nar/gki338
   Nakka K, 2018, SKELET MUSCLE, V8, DOI 10.1186/s13395-018-0152-3
   Nasif S, 2018, SEMIN CELL DEV BIOL, V75, P78, DOI 10.1016/j.semcdb.2017.08.053
   Nishida K, 2015, J MOL CELL CARDIOL, V84, P212, DOI 10.1016/j.yjmcc.2015.05.004
   Nishida K, 2017, INT J MOL SCI, V18, DOI 10.3390/ijms18071341
   Nutter CA, 2016, CELL REP, V15, P2200, DOI 10.1016/j.celrep.2016.05.002
   Oerum S, 2017, BIOMOLECULES, V7, DOI 10.3390/biom7010020
   Ogorodnikov A, 2016, PFLUG ARCH EUR J PHY, V468, P993, DOI 10.1007/s00424-016-1828-3
   Opitz CA, 2004, CIRC RES, V94, P967, DOI 10.1161/01.RES.0000124301.48193.E1
   Park C, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-11651-w
   Park JY, 2011, PLOS ONE, V6, DOI 10.1371/journal.pone.0022391
   Parker R, 2007, MOL CELL, V25, P635, DOI 10.1016/j.molcel.2007.02.011
   Patange Simona, 2018, Curr Opin Syst Biol, V8, P7, DOI 10.1016/j.coisb.2017.11.011
   Peake JM, 2015, EXERC IMMUNOL REV, V21, P8
   Peck SA, 2019, WIRES RNA, V10, DOI 10.1002/wrna.1529
   Peer E, 2017, CURR OPIN CHEM BIOL, V41, P93, DOI 10.1016/j.cbpa.2017.10.008
   Perez I, 1997, RNA, V3, P764
   Philippe L, 2018, NUCLEIC ACIDS RES, V46, P1457, DOI 10.1093/nar/gkx1237
   Poon KL, 2012, CARDIOVASC RES, V94, P418, DOI 10.1093/cvr/cvs095
   Pratt CA, 2013, CURR OPIN CELL BIOL, V25, P99, DOI 10.1016/j.ceb.2012.08.015
   Rajan S, 2010, CIRCULATION, V121, P410, DOI 10.1161/CIRCULATIONAHA.109.889725
   Ramanathan A, 2016, NUCLEIC ACIDS RES, V44, P7511, DOI 10.1093/nar/gkw551
   Ramanouskaya TV, 2017, MOL GENET GENOMICS, V292, P1175, DOI 10.1007/s00438-017-1350-0
   Ratnadiwakara M, 2018, SEMIN CELL DEV BIOL, V79, P113, DOI 10.1016/j.semcdb.2017.10.008
   Rattenbacher B, 2010, MOL CELL BIOL, V30, P3970, DOI 10.1128/MCB.00624-10
   Ray D, 2013, NATURE, V499, P172, DOI 10.1038/nature12311
   Rohrbach S, 2005, J MOL CELL CARDIOL, V38, P485, DOI 10.1016/j.yjmcc.2004.12.013
   Roundtree IA, 2017, CELL, V169, P1187, DOI 10.1016/j.cell.2017.05.045
   Ryder PV, 2018, TRAFFIC, V19, P496, DOI 10.1111/tra.12571
   Saldi T, 2016, J MOL BIOL, V428, P2623, DOI 10.1016/j.jmb.2016.04.017
   Shepard PJ, 2009, GENOME BIOL, V10, DOI 10.1186/gb-2009-10-10-242
   Shukla S, 2011, NATURE, V479, P74, DOI 10.1038/nature10442
   Simms C. L., 2017, RNA, V8, pe1366
   Singer-Krüger B, 2014, RNA BIOL, V11, P1031, DOI 10.4161/rna.29945
   Singh H, 2013, P NATL ACAD SCI USA, V110, P10836, DOI 10.1073/pnas.1302028110
   Small EM, 2010, CIRCULATION, V121, P1022, DOI 10.1161/CIRCULATIONAHA.109.889048
   STJOHNSTON D, 1995, CELL, V81, P161, DOI 10.1016/0092-8674(95)90324-0
   Stoecklin G, 2013, ADV EXP MED BIOL, V768, P197, DOI 10.1007/978-1-4614-5107-5_12
   Strässer K, 2002, NATURE, V417, P304, DOI 10.1038/nature746
   Subramaniam D, 2008, AM J PHYSIOL-GASTR L, V294, pG1025, DOI 10.1152/ajpgi.00602.2007
   Susor A, 2017, RESULTS PROBL CELL D, V63, P257, DOI 10.1007/978-3-319-60855-6_12
   Tang ZZ, 2012, HUM MOL GENET, V21, P1312, DOI 10.1093/hmg/ddr568
   Timchenko NA, 2001, J BIOL CHEM, V276, P7820, DOI 10.1074/jbc.M005960200
   Timchenko NA, 2001, MOL CELL BIOL, V21, P6927, DOI 10.1128/MCB.21.20.6927-6938.2001
   Tong JY, 2018, FRONT MED-PRC, V12, P481, DOI 10.1007/s11684-018-0654-8
   Trotman JB, 2019, WIRES RNA, V10, DOI 10.1002/wrna.1504
   Tsekrekou M, 2017, INT J MOL SCI, V18, DOI 10.3390/ijms18071411
   Ulianov SV, 2015, INT REV CEL MOL BIO, V315, P183, DOI 10.1016/bs.ircmb.2014.11.004
   van den Hoogenhof MMG, 2017, PLOS ONE, V12, DOI 10.1371/journal.pone.0184093
   van den Hoogenhof MMG, 2016, CIRC RES, V118, P454, DOI 10.1161/CIRCRESAHA.115.307872
   Verma SK, 2016, SCI REP-UK, V6, DOI 10.1038/srep30896
   Verma SK, 2013, J BIOL CHEM, V288, P35372, DOI 10.1074/jbc.M113.507426
   Vhuiyan MI, 2017, J BIOCHEM, V162, P17, DOI 10.1093/jb/mvw102
   Viereck J, 2017, CIRC RES, V120, P262, DOI 10.1161/CIRCRESAHA.116.310174
   Visvanathan A, 2018, BIOESSAYS, V40, DOI 10.1002/bies.201700093
   Vlasova IA, 2008, RNA BIOL, V5, P201, DOI 10.4161/rna.7056
   Vuong CK, 2018, NEURON, V98, P127, DOI 10.1016/j.neuron.2018.03.008
   Walters R, 2014, J CELL BIOL, V204, P862, DOI 10.1083/jcb.201401059
   Wang ET, 2015, GENOME RES, V25, P858, DOI 10.1101/gr.184390.114
   Wang GS, 2007, J CLIN INVEST, V117, P2802, DOI 10.1172/JCI32308
   Wang JJ, 2018, CHANNELS, V12, P51, DOI 10.1080/19336950.2017.1381805
   Wang WG, 2014, SCI CHINA LIFE SCI, V57, P863, DOI 10.1007/s11427-014-4706-2
   WANG YC, 1992, J BIOL CHEM, V267, P12004
   Wang YB, 2013, EMBO MOL MED, V5, P1431, DOI 10.1002/emmm.201302663
   Ward AJ, 2010, HUM MOL GENET, V19, P3614, DOI 10.1093/hmg/ddq277
   Warf MB, 2007, RNA, V13, P2238, DOI 10.1261/rna.610607
   Warren CM, 2004, MECH DEVELOP, V121, P1301, DOI 10.1016/j.mod.2004.07.003
   Watanabe T, 2018, FRONT MOL BIOSCI, V5, DOI 10.3389/fmolb.2018.00105
   Wei CL, 2016, MOL CELL, V62, P875, DOI 10.1016/j.molcel.2016.04.013
   Wei CL, 2015, CELL REP, V10, P1521, DOI 10.1016/j.celrep.2015.02.013
   Wells QS, 2013, CIRC-CARDIOVASC GENE, V6, P317, DOI 10.1161/CIRCGENETICS.113.000011
   Wheeler EC, 2018, WIRES RNA, V9, DOI 10.1002/wrna.1436
   Wu K, 2018, GENOM PROTEOM BIOINF, V16, P120, DOI 10.1016/j.gpb.2017.09.004
   Wu PD, 2018, 2018 6TH INTERNATIONAL CONFERENCE ON MECHANICAL, AUTOMOTIVE AND MATERIALS ENGINEERING (CMAME), P37, DOI 10.1109/CMAME.2018.8592233
   Xu XD, 2005, CELL, V120, P59, DOI 10.1016/j.cell.2004.11.036
   Yablonovitch AL, 2017, PLOS GENET, V13, DOI 10.1371/journal.pgen.1007064
   Ye B, 2009, CIRC RES, V105, P1083, DOI 10.1161/CIRCRESAHA.109.195040
   Ye JM, 2013, J CELL SCI, V126, P1682, DOI 10.1242/jcs.121384
   Ye JQ, 2015, P NATL ACAD SCI USA, V112, pE3020, DOI 10.1073/pnas.1508461112
   Yin ZY, 2015, BBA-MOL BASIS DIS, V1852, P47, DOI 10.1016/j.bbadis.2014.11.003
   Zander G, 2017, RNA BIOL, V14, P1642, DOI 10.1080/15476286.2017.1345835
   Zhai LT, 2014, J ZHEJIANG UNIV-SC B, V15, P438, DOI 10.1631/jzus.B1400070
   Zhang B, 2020, CURR GENET, V66, P73, DOI 10.1007/s00294-019-01016-3
   Zhang J, 2009, CELL DEATH DIFFER, V16, P1460, DOI 10.1038/cdd.2009.87
   Zhang M, 2018, CELL DEATH DIFFER, V25, P1118, DOI 10.1038/s41418-017-0029-8
   Zhang T, 2016, STEM CELLS, V34, P1776, DOI 10.1002/stem.2366
   Zhang XQ, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-05887-9
   Zhang YJ, 2015, BIOCHEM BIOPH RES CO, V464, P679, DOI 10.1016/j.bbrc.2015.06.139
   Zhou A, 2018, J AM HEART ASSOC, V7, DOI 10.1161/JAHA.117.007802
   Zhou AY, 2018, HEART RHYTHM, V15, P1072, DOI 10.1016/j.hrthm.2018.02.018
   Zhou BY, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-01628-0
   Zigácková D, 2018, PHILOS T R SOC B, V373, DOI 10.1098/rstb.2018.0171
NR 246
TC 27
Z9 31
U1 1
U2 17
PU AMER PHYSIOLOGICAL SOC
PI Rockville
PA 6120 Executive Blvd, Suite 600, Rockville, MD, UNITED STATES
SN 0031-9333
EI 1522-1210
J9 PHYSIOL REV
JI Physiol. Rev.
PD APR
PY 2020
VL 100
IS 2
BP 673
EP 694
DI 10.1152/physrev.00007.2019
PG 22
WC Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Physiology
GA KW8DZ
UT WOS:000521415100006
PM 31751167
OA Green Published
DA 2025-04-10
ER

PT J
AU Marsters, P
   Kendall, NR
   Campbell, BK
AF Marsters, P.
   Kendall, N. R.
   Campbell, B. K.
TI Pre-translational regulation of luteinizing hormone receptor in
   follicular somatic cells of cattle
SO ANIMAL REPRODUCTION SCIENCE
LA English
DT Article
DE Luteinizing hormone receptor; Pre-translational regulation; Follicle;
   Granulosa cells; Theca cells; Variable deletion site
ID MESSENGER-RIBONUCLEIC-ACID; BOVINE GRANULOSA-CELLS; RNA-BINDING-PROTEIN;
   LH RECEPTOR; STIMULATING-HORMONE; GONADOTROPIN RECEPTORS; DOMINANT
   FOLLICLE; SPLICE VARIANTS; GENE-EXPRESSION; THECA CELLS
AB Differential regulation of LHR in theca cells (TC) and granulosa cells (GC) is important for normal follicular development. Unlike TC, GC only acquire LH-responsiveness during the later stages of antral follicle development. This study tested the hypothesis that differential LH-responsiveness in these two cell types may be due, in part, to shifts in cellular patterns of alternatively spliced LHR mRNA transcripts which may not be obvious from analysis of total LHR gene expression. It also further explored the role of translation inhibition by an LHR binding protein (LHBP), normally associated with the production of endogenous cholesterol. LHR mRNA variation arises as a result of the alternative splicing of two variable deletion sites (VDS) designated 5' VDS and 3' VDS, and it was proposed that differences in cell sensitivity to LH may be (due in part to variations in the pattern of the mRNA expression of the receptor variants. The outcomes of the present study support a dynamic multi-facetted regulation of LHR during pre-translation. Not only did the ratio between variants change during antral follicle growth and in vitro cell differentiation but also between TC and GC. Regulation could also be linked to LH concentration feedback mechanisms as the absence of LH caused cultured TC to markedly up-regulate amounts of LHR mRNA. In both TC and GC, LHR mRNA was greatly reduced after treatment to block mevalonate production in the de nova cholesterol pathway, adding further support for a regulatory mechanism linked to enriched cellular amounts of mevalonate kinase. (C) 2015 The Authors. Published by Elsevier B.V.
C1 [Marsters, P.; Campbell, B. K.] Univ Nottingham, Div Child Hlth Obstet & Gynaecol, Queens Med Ctr, Nottingham NG7 2UH, England.
   [Kendall, N. R.] Univ Nottingham, Sch Vet Med & Sci, Loughborough LE12 5RD, Leics, England.
C3 University of Nottingham; University of Nottingham
RP Marsters, P (corresponding author), Univ Nottingham, Div Child Hlth Obstet & Gynaecol, Queens Med Ctr, D Floor,East Block, Nottingham NG7 2UH, England.
EM peter.marsters@nottingham.ac.uk
RI Kendall, Nigel/F-6485-2011
OI Kendall, Nigel/0000-0002-2572-2531
FU Biotechnology and Biological Sciences Research Council (BBSRC) [S20230];
   University of Nottingham; EPSRC [EP/H004424/1] Funding Source: UKRI
FX This work was supported by the Biotechnology and Biological Sciences
   Research Council (BBSRC Grant Reference No. S20230) and the University
   of Nottingham. We thank Mrs. Catherine Pincott-Allen, for skilled
   technical assistance, the NIH for provision of purified ovine
   gonadotrophins and Dr. Anne Kelly from the Glasgow Royal Infirmary for
   provision of reagents for the radioimmunoassay of A4.
CR Abdennebi L, 2002, REPRODUCTION, V123, P819, DOI 10.1530/rep.0.1230819
   Bacich DJ, 1999, MOL CELL ENDOCRINOL, V147, P113, DOI 10.1016/S0303-7207(98)00216-0
   Bao B, 1997, BIOL REPROD, V56, P1158, DOI 10.1095/biolreprod56.5.1158
   BERNARD MP, 1990, MOL CELL ENDOCRINOL, V71, pR19, DOI 10.1016/0303-7207(90)90034-6
   Campbell BK, 1998, J REPROD FERTIL, V112, P69, DOI 10.1530/jrf.0.1120069
   Campbell BK, 2003, REPRODUCTION, P429
   Campbell BK, 2001, J ENDOCRINOL, V169, P333, DOI 10.1677/joe.0.1690333
   Campbell BK, 1996, J REPROD FERTIL, V106, P7, DOI 10.1530/jrf.0.1060007
   CARSON RS, 1979, BIOL REPROD, V21, P75, DOI 10.1095/biolreprod21.1.75
   CONLEY AJ, 1995, BIOL REPROD, V52, P1081, DOI 10.1095/biolreprod52.5.1081
   ERICKSON GF, 1982, MOL CELL ENDOCRINOL, V27, P17, DOI 10.1016/0303-7207(82)90059-4
   Evans ACO, 1997, ENDOCRINOLOGY, V138, P2963, DOI 10.1210/en.138.7.2963
   Forni M, 2003, REPROD NUTR DEV, V43, P517, DOI 10.1051/rnd:2004006
   Gutierrez CG, 1997, BIOL REPROD, V56, P608, DOI 10.1095/biolreprod56.3.608
   Hampton JH, 2004, REPRODUCTION, V127, P695, DOI 10.1530/rep.1.00015
   Izquierdo D, 2004, FERTIL STERIL, V82, P1193, DOI 10.1016/j.fertnstert.2004.03.037
   JI IH, 1991, ENDOCRINOLOGY, V128, P2648, DOI 10.1210/endo-128-5-2648
   Karlsson AB, 2010, MOL ENDOCRINOL, V24, P1765, DOI 10.1210/me.2009-0487
   Kash JC, 1999, BIOCHEMISTRY-US, V38, P16889, DOI 10.1021/bi9915770
   Kawate N, 1998, MOL REPROD DEV, V51, P66, DOI 10.1002/(SICI)1098-2795(199809)51:1<66::AID-MRD8>3.0.CO;2-U
   Kwintkiewicz J, 2006, FERTIL STERIL, V86, P1053, DOI 10.1016/j.fertnstert.2006.04.020
   LABARBERA AR, 1981, ENDOCRINOLOGY, V108, P1561, DOI 10.1210/endo-108-4-1561
   LOOSFELT H, 1989, SCIENCE, V245, P525, DOI 10.1126/science.2502844
   LYDON JP, 1995, GENE DEV, V9, P2266, DOI 10.1101/gad.9.18.2266
   Marsters P, 2003, MOL CELL ENDOCRINOL, V203, P117, DOI 10.1016/S0303-7207(03)00093-5
   McNatty K.P., 1999, J REPROD FERTIL S, V54
   MCNATTY KP, 1984, J REPROD FERTIL, V72, P39, DOI 10.1530/jrf.0.0720039
   Menon B, 2009, BBA-MOL CELL RES, V1793, P1787, DOI 10.1016/j.bbamcr.2009.08.009
   Nair AK, 2005, J BIOL CHEM, V280, P42809, DOI 10.1074/jbc.M503154200
   Nair AK, 2008, FEBS J, V275, P3397, DOI 10.1111/j.1742-4658.2008.06490.x
   Niswender GD, 2002, REPRODUCTION, V123, P333, DOI 10.1530/rep.0.1230333
   Nogueira MFG, 2007, MOL REPROD DEV, V74, P680, DOI 10.1002/mrd.20656
   PENG XR, 1991, ENDOCRINOLOGY, V129, P3200, DOI 10.1210/endo-129-6-3200
   Reinholz MM, 2000, GYNECOL ONCOL, V79, P264, DOI 10.1006/gyno.2000.5946
   Remy JJ, 1996, MOL CELL ENDOCRINOL, V125, P79, DOI 10.1016/S0303-7207(96)03955-X
   RICHARDS JS, 1994, ENDOCR REV, V15, P725, DOI 10.1210/er.15.6.725
   Robert C, 2003, REPRODUCTION, V125, P437, DOI 10.1530/rep.0.1250437
   Simoes RAL, 2012, THERIOGENOLOGY, V77, P139, DOI 10.1016/j.theriogenology.2011.07.027
   TILLY JL, 1992, ENDOCRINOLOGY, V130, P1296, DOI 10.1210/en.130.3.1296
   Wang L, 2007, MOL ENDOCRINOL, V21, P2233, DOI 10.1210/me.2007-0102
   Webb R, 1999, J REPROD FERTIL, P33
   WEBB R, 1982, J REPROD FERTIL, V66, P169, DOI 10.1530/jrf.0.0660169
   West A. P., 1992, Biochemical Society Transactions, V20, p320S
   XU ZZ, 1995, BIOL REPROD, V53, P951, DOI 10.1095/biolreprod53.4.951
   Zeleznik AJ, 2003, ENDOCRINOLOGY, V144, P3985, DOI 10.1210/en.2003-0293
   ZHANG R, 1995, J BIOL CHEM, V270, P21722, DOI 10.1074/jbc.270.37.21722
NR 46
TC 3
Z9 5
U1 0
U2 9
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 0378-4320
EI 1873-2232
J9 ANIM REPROD SCI
JI Anim. Reprod. Sci.
PD DEC
PY 2015
VL 163
BP 63
EP 74
DI 10.1016/j.anireprosci.2015.09.019
PG 12
WC Agriculture, Dairy & Animal Science; Reproductive Biology; Veterinary
   Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Agriculture; Reproductive Biology; Veterinary Sciences
GA CZ0EM
UT WOS:000366777900009
PM 26507944
OA hybrid, Green Published
DA 2025-04-10
ER

PT J
AU Magnussen, AL
   Rennel, ES
   Hua, J
   Bevan, HS
   Beazley Long, N
   Lehrling, C
   Gammons, M
   Floege, J
   Harper, SJ
   Agostini, HT
   Bates, DO
   Churchill, AJ
AF Magnussen, Anette L.
   Rennel, Emma S.
   Hua, Jing
   Bevan, Heather S.
   Beazley Long, Nicholas
   Lehrling, Christina
   Gammons, Melissa
   Floege, Juergen
   Harper, Steven J.
   Agostini, Hansjuergen T.
   Bates, David O.
   Churchill, Amanda J.
TI VEGF-A165b Is Cytoprotective and Antiangiogenic in the Retina
SO INVESTIGATIVE OPHTHALMOLOGY & VISUAL SCIENCE
LA English
DT Article
ID ENDOTHELIAL GROWTH-FACTOR; SPLICE VARIANT; DIABETIC-RETINOPATHY;
   ANGIOGENIC ISOFORMS; TUMOR-GROWTH; VEGF; VEGF(165)B; BEVACIZUMAB; CELLS;
   NEOVASCULARIZATION
AB PURPOSE. A number of key ocular diseases, including diabetic retinopathy and age-related macular degeneration, are characterized by localized areas of epithelial or endothelial damage, which can ultimately result in the growth of fragile new blood vessels, vitreous hemorrhage, and retinal detachment. VEGF-A(165), the principal neovascular agent in ocular angiogenic conditions, is formed by proximal splice site selection in its terminal exon 8. Alternative splicing of this exon results in an antiangiogenic isoform, VEGF-A(165)b, which is downregulated in diabetic retinopathy. Here the authors investigate the antiangiogenic activity of VEGF(165)b and its effect on retinal epithelial and endothelial cell survival.
   METHODS. VEGF-A(165)b was injected intraocularly in a mouse model of retinal neovascularization (oxygen-induced retinopathy [OIR]). Cytotoxicity and cell migration assays were used to determine the effect of VEGF-A(165)b.
   RESULTS. VEGF-A(165)b dose dependently inhibited angiogenesis (IC50, 12.6 pg/eye) and retinal endothelial migration induced by 1 nM VEGF-A(165) across monolayers in culture (IC50, 1 nM). However, it also acts as a survival factor for endothelial cells and retinal epithelial cells through VEGFR2 and can stimulate downstream signaling. Furthermore, VEGF-A(165)b injection, while inhibiting neovascular proliferation in the eye, reduced the ischemic insult in OIR (IC50, 2.6 pg/eye). Unlike bevacizumab, pegaptanib did not interact directly with VEGF-A(165)b. CONCLUSIONS. The survival effects of VEGF-A(165)b signaling can protect the retina from ischemic damage. These results suggest that VEGF-A(165)b may be a useful therapeutic agent in ischemia-induced angiogenesis and a cytoprotective agent for retinal pigment epithelial cells. (Invest Ophthalmol Vis Sci. 2010; 51:4273-4281) DOI:10.1167/iovs.09-4296
C1 [Magnussen, Anette L.; Rennel, Emma S.; Hua, Jing; Bevan, Heather S.; Beazley Long, Nicholas; Gammons, Melissa; Harper, Steven J.; Bates, David O.] Univ Bristol, Sch Vet Sci, Dept Physiol & Pharmacol, Microvasc Res Labs,Bristol Heart Inst, Bristol BS2 8EJ, Avon, England.
   [Lehrling, Christina; Agostini, Hansjuergen T.] Univ Freiburg, Univ Eye Hosp, Freiburg, Germany.
   [Floege, Juergen] Rhein Westfal TH Aachen, Univ Hosp, Div Nephrol & Clin Immunol, Achen, Germany.
   [Churchill, Amanda J.] Univ Bristol, Bristol Eye Hosp, Unit Ophthalmol, Bristol BS1 2LX, Avon, England.
C3 University of Bristol; University of Freiburg; RWTH Aachen University;
   Bristol Eye Hospital; University of Bristol
RP Bates, DO (corresponding author), Univ Bristol, Sch Vet Sci, Dept Physiol & Pharmacol, Microvasc Res Labs,Bristol Heart Inst, Southwell St, Bristol BS2 8EJ, Avon, England.
EM dave.bates@bris.ac.uk; a.j.churchill@bristol.ac.uk
RI Beazley-Long, Nicholas/I-7131-2019
OI Beazley-long, Nicholas/0000-0001-7342-2771; Bates,
   David/0000-0003-4850-2360; gammons, melissa/0000-0001-9661-9331
FU Fight for Sight; National Eye Research Centre; Richard Bright VEGF
   Research Trust; North Bristol NHS Trust Adrian Wright Bequest into
   Disability in the Elderly; Skin Cancer Research Fund; Wellcome Trust
   [79736, 69029]; British Heart Foundation [BS/06/005]; Academy of Finland
   (AKA) [79736] Funding Source: Academy of Finland (AKA)
FX Supported by Fight for Sight (ER), the National Eye Research Centre, the
   Richard Bright VEGF Research Trust and the North Bristol NHS Trust
   Adrian Wright Bequest into Disability in the Elderly (AM), the Skin
   Cancer Research Fund (MG), Wellcome Trust Grants 79736 (JH, NBL) and
   69029 (HSB), and British Heart Foundation Grant BS/06/005 (DOB).
CR ADAMIS AP, 1994, AM J OPHTHALMOL, V118, P445, DOI 10.1016/S0002-9394(14)75794-0
   Anderson HR, 1995, BRIT J OPHTHALMOL, V79, P1120, DOI 10.1136/bjo.79.12.1120
   Baffert F, 2006, AM J PHYSIOL-HEART C, V290, pH547, DOI 10.1152/ajpheart.00616.2005
   Bates DO, 2002, CANCER RES, V62, P4123
   Benest AV, 2009, NATURE, V458, P41, DOI 10.1038/458041a
   Bevan HS, 2008, NEPHRON PHYSIOL, V110, P57, DOI 10.1159/000177614
   Bogaert E, 2006, MUSCLE NERVE, V34, P391, DOI 10.1002/mus.20609
   ChanLing T, 1997, MICROSC RES TECHNIQ, V36, P1
   Eremina V, 2008, NEW ENGL J MED, V358, P1129, DOI 10.1056/NEJMoa0707330
   Ergorul C, 2008, MOL VIS, V14, P1517
   Gaudreault J, 2005, INVEST OPHTH VIS SCI, V46, P726, DOI 10.1167/iovs.04-0601
   Gerhardt H, 2003, J CELL BIOL, V161, P1163, DOI 10.1083/jcb.200302047
   Hamdollah Zadeh MA, 2008, MICROCIRCULATION, V15, P605, DOI 10.1080/10739680802220323
   Holz FG, 2004, AM J OPHTHALMOL, V137, P504, DOI 10.1016/j.ajo.2003.11.026
   Hua J, 2010, INVEST OPHTH VIS SCI, V51, P4282, DOI 10.1167/iovs.09-4360
   Hurwitz H, 2004, NEW ENGL J MED, V350, P2335, DOI 10.1056/NEJMoa032691
   JAUREGUI HO, 1981, IN VITRO CELL DEV B, V17, P1100
   Joussen AM, 2001, AM J PATHOL, V158, P147, DOI 10.1016/S0002-9440(10)63952-1
   Kabbinavar F, 2003, J CLIN ONCOL, V21, P60, DOI 10.1200/JCO.2003.10.066
   Kawamura H, 2008, CANCER RES, V68, P4683, DOI 10.1158/0008-5472.CAN-07-6577
   Kinose F, 2005, MOL VIS, V11, P366
   Konopatskaya O, 2006, MOL VIS, V12, P626
   Krohne TU, 2009, BRIT J OPHTHALMOL, V93, P91, DOI 10.1136/bjo.2008.145102
   Lee S, 2007, CELL, V130, P691, DOI 10.1016/j.cell.2007.06.054
   Mazzone M, 2009, CELL, V136, P839, DOI 10.1016/j.cell.2009.01.020
   Mizutani M, 1996, J CLIN INVEST, V97, P2883, DOI 10.1172/JCI118746
   Nishijima K, 2007, AM J PATHOL, V171, P53, DOI 10.2353/ajpath.2007.061237
   Nowak DG, 2008, J CELL SCI, V121, P3487, DOI 10.1242/jcs.016410
   Nowak DG, 2010, J BIOL CHEM, V285, P5532, DOI 10.1074/jbc.M109.074930
   Ong JM, 2003, NEUROCHEM RES, V28, P883, DOI 10.1023/A:1023223409798
   Oosthuyse B, 2001, NAT GENET, V28, P131, DOI 10.1038/88842
   Ostendorf T, 1999, J CLIN INVEST, V104, P913, DOI 10.1172/JCI6740
   Perrin RM, 2005, DIABETOLOGIA, V48, P2422, DOI 10.1007/s00125-005-1951-8
   Peters S, 2007, AM J OPHTHALMOL, V143, P995, DOI 10.1016/j.ajo.2007.03.007
   Qiu Y, 2008, FASEB J, V22, P1104, DOI 10.1096/fj.07-9718com
   Rennel ES, 2008, BRIT J CANCER, V98, P1250, DOI 10.1038/sj.bjc.6604309
   Rennel ES, 2009, BRIT J CANCER, V101, P1183, DOI 10.1038/sj.bjc.6605249
   Rennel ES, 2008, EUR J CANCER, V44, P1883, DOI 10.1016/j.ejca.2008.05.027
   Rosenfeld PJ, 2006, NEW ENGL J MED, V355, P1419, DOI 10.1056/NEJMoa054481
   Roth F, 2004, GRAEF ARCH CLIN EXP, V242, P710, DOI 10.1007/s00417-004-0976-x
   Saint-Geniez M, 2008, PLOS ONE, V3, DOI 10.1371/journal.pone.0003554
   SHIMA DT, 1995, MOL MED, V1, P182, DOI 10.1007/BF03401566
   SHWEIKI D, 1992, NATURE, V359, P843, DOI 10.1038/359843a0
   Slomiany MG, 2004, AM J PHYSIOL-CELL PH, V287, pC746, DOI 10.1152/ajpcell.00568.2003
   SMITH LEH, 1994, INVEST OPHTH VIS SCI, V35, P101
   Spitzer MS, 2006, BRIT J OPHTHALMOL, V90, P1316, DOI 10.1136/bjo.2006.095190
   STITT AW, 1995, BRIT J OPHTHALMOL, V79, P362, DOI 10.1136/bjo.79.4.362
   Suarez SC, 2006, CELL MOL LIFE SCI, V63, P2067, DOI 10.1007/s00018-006-6254-9
   Sun HW, 2007, BIOCHEM BIOPH RES CO, V353, P152, DOI 10.1016/j.bbrc.2006.12.002
   Tolentino MJ, 1996, OPHTHALMOLOGY, V103, P1820, DOI 10.1016/S0161-6420(96)30420-X
   Tolosa L, 2008, J NEUROCHEM, V105, P1080, DOI 10.1111/j.1471-4159.2007.05206.x
   Varey AHR, 2008, BRIT J CANCER, V98, P1366, DOI 10.1038/sj.bjc.6604308
   Whittles CE, 2002, MICROCIRCULATION, V9, P513, DOI 10.1038/sj.mn.7800164
   Woolard J, 2004, CANCER RES, V64, P7822, DOI 10.1158/0008-5472.CAN-04-0934
NR 54
TC 67
Z9 79
U1 2
U2 9
PU ASSOC RESEARCH VISION OPHTHALMOLOGY INC
PI ROCKVILLE
PA 12300 TWINBROOK PARKWAY, ROCKVILLE, MD 20852-1606 USA
SN 0146-0404
EI 1552-5783
J9 INVEST OPHTH VIS SCI
JI Invest. Ophthalmol. Vis. Sci.
PD AUG
PY 2010
VL 51
IS 8
BP 4273
EP 4281
DI 10.1167/iovs.09-4296
PG 9
WC Ophthalmology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Ophthalmology
GA 629JT
UT WOS:000280194100061
PM 20237249
OA Green Published
DA 2025-04-10
ER

PT J
AU Sarkar, A
   Caamano, S
   Fernandez, JM
AF Sarkar, A
   Caamano, S
   Fernandez, JM
TI The elasticity of individual titin PEVK exons measured by single
   molecule atomic force microscopy
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID GIANT PROTEIN TITIN; ISOFORM EXPRESSION; PASSIVE STIFFNESS;
   MUSCLE-STIFFNESS; SPRING ELEMENTS; SKELETAL-MUSCLE; STRIATED-MUSCLE;
   CARDIAC TITIN; DIVERSITY; MECHANICS
AB The I-band region of the giant muscle protein titin contains a large domain enriched for the amino acids proline, glutamate, valine, and lysine and is denoted the PEVK domain. The PEVK domain of titin encodes a random coil shown to be an important factor in the passive elasticity of titin. Muscle-specific splicing of 116 PEVK exons encodes this domain. It has been proposed that proline contents determine the elasticity of the PEVK polypeptide, where the individual exons code for "flexibility cassettes." To test this hypothesis, we have measured the elasticity of three distinct polypeptides encoded by individual PEVK exons (161, 120 and 184) that varied greatly in their proline contents (7, 14, and 37% respectively) and total PEVK contents (55, 70, and 87%). We used single molecule atomic force microscopy techniques to measure the persistence length, p, of the engineered PEVK proteins. Surprisingly, all three exons 161, 120, and 184 coded for proteins with similar values of persistence length, p = 0.92 0.38, 0.89 0.42, and 0.98 0.4 nm, respectively. We conclude that the PEVK exons encode polypeptides of similar elastic properties, unrelated to their total PEVK contents. Hence, alternative splicing solely adjusts the length of the PEVK domain of titin.
C1 Columbia Univ, Dept Biol Sci, Fairchild Ctr 1011A, New York, NY 10027 USA.
   Mayo Clin, Coll Med, Dept Neurol Surg, Rochester, MN 55905 USA.
C3 Columbia University; Mayo Clinic
RP Columbia Univ, Dept Biol Sci, Fairchild Ctr 1011A, 1212 Amsterdam Ave,MC 2449, New York, NY 10027 USA.
EM jfernandez@columbia.edu
CR Bang ML, 2001, CIRC RES, V89, P1065, DOI 10.1161/hh2301.100981
   Carrion-Vazquez M, 1999, P NATL ACAD SCI USA, V96, P11288, DOI 10.1073/pnas.96.20.11288
   Carrion-Vazquez M, 1999, P NATL ACAD SCI USA, V96, P3694, DOI 10.1073/pnas.96.7.3694
   Freiburg A, 2000, CIRC RES, V86, P1114
   FURST DO, 1995, J MOL CELL CARDIOL, V27, P951, DOI 10.1016/0022-2828(95)90064-0
   Granzier H, 2002, J PHYSIOL-LONDON, V541, P335, DOI 10.1113/jphysiol.2001.014381
   Granzier HL, 2004, CIRC RES, V94, P284, DOI 10.1161/01.RES.0000117769.88862.F8
   Improta S, 1998, J MOL BIOL, V284, P761, DOI 10.1006/jmbi.1998.2028
   Labeit D, 2003, P NATL ACAD SCI USA, V100, P13716, DOI 10.1073/pnas.2235652100
   LABEIT S, 1995, SCIENCE, V270, P293, DOI 10.1126/science.270.5234.293
   Lahmers S, 2004, CIRC RES, V94, P505, DOI 10.1161/01.RES.0000115522.52554.86
   Li HB, 2000, P NATL ACAD SCI USA, V97, P6527, DOI 10.1073/pnas.120048697
   Li HB, 2002, NATURE, V418, P998, DOI 10.1038/nature00938
   Li HB, 2001, P NATL ACAD SCI USA, V98, P10682, DOI 10.1073/pnas.191189098
   Linke WA, 1998, P NATL ACAD SCI USA, V95, P8052, DOI 10.1073/pnas.95.14.8052
   Linke WA, 2000, HISTOL HISTOPATHOL, V15, P799, DOI 10.14670/HH-15.799
   Nelson P, 1999, P NATL ACAD SCI USA, V96, P14342, DOI 10.1073/pnas.96.25.14342
   Oberhauser AF, 1999, NAT STRUCT BIOL, V6, P1025
   Rief M, 1997, SCIENCE, V276, P1109, DOI 10.1126/science.276.5315.1109
   SCHIMMEL PR, 1967, P NATL ACAD SCI USA, V58, P52, DOI 10.1073/pnas.58.1.52
   Schlierf M, 2004, P NATL ACAD SCI USA, V101, P7299, DOI 10.1073/pnas.0400033101
   Trombitás K, 2000, BIOPHYS J, V79, P3226, DOI 10.1016/S0006-3495(00)76555-6
   WANG K, 1979, P NATL ACAD SCI USA, V76, P3698, DOI 10.1073/pnas.76.8.3698
   WANG K, 1991, P NATL ACAD SCI USA, V88, P7101, DOI 10.1073/pnas.88.16.7101
   Watanabe K, 2002, J BIOL CHEM, V277, P11549, DOI 10.1074/jbc.M200356200
   Wu YM, 2002, CIRCULATION, V106, P1384, DOI 10.1161/01.CIR.0000029804.61510.02
NR 26
TC 47
Z9 56
U1 0
U2 6
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
SN 0021-9258
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD FEB 25
PY 2005
VL 280
IS 8
BP 6261
EP 6264
DI 10.1074/jbc.C400573200
PG 4
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 902DT
UT WOS:000227332700004
PM 15632200
OA hybrid
DA 2025-04-10
ER

PT J
AU Barresi, R
   Di Blasi, C
   Negri, T
   Brugnoni, R
   Vitali, A
   Felisari, G
   Salandi, A
   Daniel, S
   Cornelio, F
   Morandi, L
   Mora, M
AF Barresi, R
   Di Blasi, C
   Negri, T
   Brugnoni, R
   Vitali, A
   Felisari, G
   Salandi, A
   Daniel, S
   Cornelio, F
   Morandi, L
   Mora, M
TI Disruption of heart sarcoglycan complex and severe cardiomyopathy caused
   by β sarcoglycan mutations
SO JOURNAL OF MEDICAL GENETICS
LA English
DT Article
DE limb-girdle muscular dystrophy; sarcoglycans; dystrophin associated
   proteins; cardiomyopathy
ID GIRDLE MUSCULAR-DYSTROPHY; PRIMARY ADHALINOPATHY; MISSENSE MUTATIONS;
   CLINICAL ASPECTS; LGMD 2E; GENE; GLYCOPROTEIN; IDENTIFICATION;
   DEFICIENCY; PROTEINS
AB Two young males with limb-girdle muscular dystrophy (LGMD) resulting from sarcoglycan deficiency died at 27 (patient 1) and 18 years (patient 2) of severe cardiomyopathy. Genetic analysis showed that they were compound heterozygotes for mutations in the beta sarcoglycan gene, One of these mutations, an 8 bp duplication in exon 3, was common to both patients. The second mutation in patient 2 was a 4 bp deletion at the splice donor site of intron 2, not reported previously. Patient 2 had more severe heart and skeletal muscle defects with faster deterioration; no sarcoglycans were detected in his skeletal muscle. The second mutation in patient 1, inferred because the unaffected father carries the 8 bp duplication, was not found. in patient I,both heart and skeletal muscle were analysed and showed reduction of all sarcoglycans in both tissues and incorrect localisation of alpha and gamma sarcoglycans ire heart. Therefore mutations in one sarcoglycan gene can disrupt the entire sarcoglycan complex in both skeletal and cardiac muscle. Differing expression patterns of sarcoglycan components in heart and skeletal muscle could be the result of alternatively spliced transcripts in these tissues. By sequencing an alternative transcript, highly expressed in the heart and skeletal muscle of patient 1, we found an 87 bp cryptic exon not previously reported. Although cardiomyopathy earn result from mutations in alpha and gamma sarcoglycans, we show for the first time that the condition can also be caused by mutations in the beta sarcoglycan gene. This report therefore expands the phenotype of sarcoglycanopathies and suggests that cardiac function in LGMD patients with defective sarcoglycan expression should be monitored.
C1 Ist Nazl Neurol Carlo Besta, Dept Neuromuscular Dis, I-20133 Milan, Italy.
   Osped Gen Moriggia Pelascini, Dept Rehabil Cardiol, Como, Italy.
   Ist Sci Eugenio Medea, Lecce, Italy.
C3 Fondazione IRCCS Istituto Neurologico Carlo Besta; IRCCS Eugenio Medea
RP Mora, M (corresponding author), Ist Nazl Neurol Carlo Besta, Dept Neuromuscular Dis, Via Celoria 11, I-20133 Milan, Italy.
RI Salandi, Antonio/AAA-5239-2020; Barresi, Rita/AAB-9569-2022; Pane,
   Marika/K-1818-2017; Mora, Marina/J-2883-2018; Brugnoni,
   Raffaella/AAN-8039-2021
OI Mora, Marina/0000-0002-5765-2320; Brugnoni,
   Raffaella/0000-0003-1365-4508; Negri, Tiziana/0000-0002-3528-7115
CR Barresi R, 1997, ACTA NEUROPATHOL, V94, P28, DOI 10.1007/s004010050668
   BenHamida M, 1996, NEUROMUSCULAR DISORD, V6, P493, DOI 10.1016/S0960-8966(96)00395-1
   Bönnemann CG, 1998, NEUROMUSCULAR DISORD, V8, P193, DOI 10.1016/S0960-8966(98)00014-5
   Bonnemann CG, 1996, HUM MOL GENET, V5, P1953, DOI 10.1093/hmg/5.12.1953
   BONNEMANN CG, 1995, NAT GENET, V11, P266, DOI 10.1038/ng1195-266
   BUSHBY KMD, 1995, NEUROMUSCULAR DISORD, V5, P337, DOI 10.1016/0960-8966(95)00005-8
   CAMPBELL KP, 1989, NATURE, V338, P259, DOI 10.1038/338259a0
   Duclos F, 1998, NEUROMUSCULAR DISORD, V8, P30, DOI 10.1016/S0960-8966(97)00135-1
   Duggan DJ, 1997, NEW ENGL J MED, V336, P618, DOI 10.1056/NEJM199702273360904
   Eymard B, 1997, NEUROLOGY, V48, P1227, DOI 10.1212/WNL.48.5.1227
   Fadic R, 1996, NEW ENGL J MED, V334, P362, DOI 10.1056/NEJM199602083340604
   Lim LE, 1998, CURR OPIN NEUROL, V11, P443, DOI 10.1097/00019052-199810000-00006
   LIM LE, 1995, NAT GENET, V11, P257, DOI 10.1038/ng1195-257
   MORANDI L, 1995, J NEUROL SCI, V132, P146, DOI 10.1016/0022-510X(95)00147-T
   MUNTONI F, 1995, J CLIN INVEST, V96, P693, DOI 10.1172/JCI118112
   Nigro V, 1996, HUM MOL GENET, V5, P1179, DOI 10.1093/hmg/5.8.1179
   Nigro V, 1997, HUM MOL GENET, V6, P601, DOI 10.1093/hmg/6.4.601
   Nigro V, 1996, NAT GENET, V14, P195, DOI 10.1038/ng1096-195
   NOGUCHI S, 1995, SCIENCE, V270, P819, DOI 10.1126/science.270.5237.819
   Olson TM, 1998, SCIENCE, V280, P750, DOI 10.1126/science.280.5364.750
   PICCOLO F, 1995, NAT GENET, V10, P243, DOI 10.1038/ng0695-243
   ROBERDS SL, 1994, CELL, V78, P625, DOI 10.1016/0092-8674(94)90527-4
   Towbin JA, 1998, CURR OPIN CELL BIOL, V10, P131, DOI 10.1016/S0955-0674(98)80096-3
   van der Kooi AJ, 1998, HEART, V79, P73, DOI 10.1136/hrt.79.1.73
   YOSHIDA M, 1994, EUR J BIOCHEM, V222, P1055, DOI 10.1111/j.1432-1033.1994.tb18958.x
   YOSHIDA M, 1990, J BIOCHEM, V108, P748, DOI 10.1093/oxfordjournals.jbchem.a123276
NR 26
TC 93
Z9 107
U1 0
U2 2
PU BMJ PUBLISHING GROUP
PI LONDON
PA BRITISH MED ASSOC HOUSE, TAVISTOCK SQUARE, LONDON WC1H 9JR, ENGLAND
SN 0022-2593
J9 J MED GENET
JI J. Med. Genet.
PD FEB
PY 2000
VL 37
IS 2
BP 102
EP 107
DI 10.1136/jmg.37.2.102
PG 6
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA 283ZZ
UT WOS:000085307100005
PM 10662809
OA Green Published, Bronze
DA 2025-04-10
ER

PT J
AU Subramaniam, J
   Yamankurt, G
   Cunha, SR
AF Subramaniam, Janani
   Yamankurt, Gokay
   Cunha, Shane R.
TI Obscurin regulates ankyrin macromolecular complex formation
SO JOURNAL OF MOLECULAR AND CELLULAR CARDIOLOGY
LA English
DT Article
DE Ankyrin; sAnk1.5; AnkG107; Obscurin; Alternative splicing
ID ALTERNATIVELY SPLICED FORMS; C-TERMINAL DOMAIN; SARCOPLASMIC-RETICULUM;
   SKELETAL-MUSCLE; NEUROMUSCULAR-JUNCTION; CA2+ SIGNALS; BINDING;
   ORGANIZATION; MEMBRANE; ISOFORM
AB Obscurin is a large scaffolding protein in striated muscle that maintains sarcolemmal integrity and aligns the sarcoplasmic reticulum with the underlying contractile machinery. Ankyrins are a family of adaptor proteins with some isoforms that interact with obscurin. Previous studies have examined obscurin interacting with individual ankyrins. In this study, we demonstrate that two different ankyrins interact with obscurin's carboxyl terminus via independent ankyrin-binding domains (ABDs). Using in-vitro binding assays, co-precipitation assays, and FLIM-FRET analysis, we show that obscurin interacts with small ankyrin 1.5 (sAnk1.5) and the muscle specific ankyrin-G isoform (AnkG107). While there is no direct interaction between sAnk1.5 and AnkG107, obscurin connects the two ankyrins both in vitro and in cells. Moreover, AnkG107 recruits beta-spectrin to this macromolecular protein complex and mutating obscurin's ABDs disrupts complex formation. To further characterize AnkG107 interaction with obscurin, we measure obscurin-binding to different AnkG107 isoforms expressed in the heart and find that the first obscurin-binding domain in AnkG107 principally mediates this interaction. We also find that AnkG107 does not bind to filamin-C and displays minimal binding to plectin-1 compared to obscurin. Finally, both sAnk1.5-GFP and AnkG107-CTD-RFP are targeted to the M-lines of ventricular cardiomyocytes and mutating their obscurin-binding domains disrupts the M-line localization of these ankyrin constructs. Altogether, these findings support a model in which obscurin can interact via independent binding domains with two different ankyrin protein complexes to target them to the sarcomeric M-line of ventricular cardiomyocytes.
C1 [Subramaniam, Janani; Yamankurt, Gokay; Cunha, Shane R.] Univ Texas, Dept Integrat Biol & Pharmacol, Hlth Sci Ctr Houston, Houston, TX 77030 USA.
C3 University of Texas System; University of Texas Health Science Center
   Houston
RP Cunha, SR (corresponding author), Univ Texas, Dept Integrat Biol & Pharmacol, Hlth Sci Ctr Houston, Houston, TX 77030 USA.
EM shane.r.cunha@uth.tmc.edu
OI Subramaniam, Janani/0000-0002-0533-7687
FU American Heart Association [16GRNT30410011]; American Heart Association
   (AHA) [16GRNT30410011] Funding Source: American Heart Association (AHA)
FX Funding This work was supported by the American Heart Association
   (16GRNT30410011) .
CR Abdi KM, 2006, J BIOL CHEM, V281, P5741, DOI 10.1074/jbc.M506697200
   Ackermann MA, 2011, J CELL SCI, V124, P3619, DOI 10.1242/jcs.085159
   Ackermann MA, 2009, MOL BIOL CELL, V20, P2963, DOI 10.1091/mbc.E08-12-1251
   Armani A, 2006, EXP CELL RES, V312, P3546, DOI 10.1016/j.yexcr.2006.07.027
   Ayalon G, 2008, CELL, V135, P1189, DOI 10.1016/j.cell.2008.10.018
   Bagnato P, 2003, J CELL BIOL, V160, P245, DOI 10.1083/jcb.200208109
   Birkenmeier CS, 1998, GENOMICS, V50, P79, DOI 10.1006/geno.1998.5305
   Blondelle J, 2019, COMMUN BIOL, V2, DOI 10.1038/s42003-019-0405-7
   Borisov AB, 2004, J HISTOCHEM CYTOCHEM, V52, P1117, DOI 10.1369/jhc.3A6183.2004
   Borzok MA, 2007, J BIOL CHEM, V282, P32384, DOI 10.1074/jbc.M704089200
   Busby B, 2011, J MOL BIOL, V408, P321, DOI 10.1016/j.jmb.2011.01.053
   Busby B, 2010, BIOCHEMISTRY-US, V49, P9948, DOI 10.1021/bi101165p
   Carlsson L, 2008, HISTOCHEM CELL BIOL, V130, P91, DOI 10.1007/s00418-008-0413-z
   Cunha SR, 2008, J BIOL CHEM, V283, P31968, DOI 10.1074/jbc.M806050200
   Cunha SR, 2006, CARDIOVASC RES, V71, P22, DOI 10.1016/j.cardiores.2006.03.018
   Cunha SR, 2011, CIRCULATION, V124, P1212, DOI 10.1161/CIRCULATIONAHA.111.023986
   Cunha SR, 2008, J MOL CELL CARDIOL, V45, P724, DOI 10.1016/j.yjmcc.2008.08.005
   Dauber W, 1999, J MUSCLE RES CELL M, V20, P697, DOI 10.1023/A:1005521529855
   Dauber W, 2000, J MUSCLE RES CELL M, V21, P443, DOI 10.1023/A:1005614917564
   DAVIS LH, 1992, J BIOL CHEM, V267, P18966
   Devarajan P, 1996, J CELL BIOL, V133, P819, DOI 10.1083/jcb.133.4.819
   Fukuzawa A, 2005, J MUSCLE RES CELL M, V26, P427, DOI 10.1007/s10974-005-9025-6
   Gagelin C, 2002, J BIOL CHEM, V277, P12978, DOI 10.1074/jbc.M111299200
   Gallagher PG, 1998, J BIOL CHEM, V273, P1339, DOI 10.1074/jbc.273.3.1339
   Giacomello E, 2015, AM J PHYSIOL-CELL PH, V308, pC123, DOI 10.1152/ajpcell.00090.2014
   Gokhin DS, 2011, J CELL BIOL, V194, P105, DOI 10.1083/jcb.201011128
   Goodman SR, 2015, EXP BIOL MED, V240, P1039, DOI 10.1177/1535370215596084
   He M, 2014, J CELL BIOL, V206, P273, DOI 10.1083/jcb.201401016
   He M, 2012, J BIOL CHEM, V287, P43995, DOI 10.1074/jbc.M112.417501
   Hopitzan AA, 2006, MOL BIOL EVOL, V23, P46, DOI 10.1093/molbev/msj004
   Hopitzan AA, 2005, EXP CELL RES, V309, P86, DOI 10.1016/j.yexcr.2005.04.013
   Hu LYR, 2020, FRONT PHYSIOL, V11, DOI 10.3389/fphys.2020.00478
   Hu LYR, 2017, SCI ADV, V3, DOI 10.1126/sciadv.1603081
   Kakhniashvili DG, 2001, BIOCHEMISTRY-US, V40, P11630, DOI 10.1021/bi010176t
   Kaplan MM, 2018, CELL REP, V23, P3891, DOI 10.1016/j.celrep.2018.05.085
   Kontrogianni-Konstantopoulos A, 2004, AM J PHYSIOL-CELL PH, V287, pC209, DOI 10.1152/ajpcell.00497.2003
   Kontrogianni-Konstantopoulos A, 2003, MOL BIOL CELL, V14, P1138, DOI 10.1091/mbc.E02-07-0411
   Kontrogianni-Konstantopoulos A, 2006, FASEB J, V20, P2102, DOI 10.1096/fj.06-5761com
   Kordeli E, 1998, J CELL SCI, V111, P2197
   KORDELI E, 1995, J BIOL CHEM, V270, P2352, DOI 10.1074/jbc.270.5.2352
   Lange S, 2012, MOL BIOL CELL, V23, P2490, DOI 10.1091/mbc.E12-01-0052
   Lange S, 2009, J CELL SCI, V122, P2640, DOI 10.1242/jcs.046193
   Le Scouarnec S, 2008, P NATL ACAD SCI USA, V105, P15617, DOI 10.1073/pnas.0805500105
   Lopes LR, 2015, HEART, V101, P294, DOI 10.1136/heartjnl-2014-306387
   Maiweilidan Y, 2011, EXP CELL RES, V317, P724, DOI 10.1016/j.yexcr.2011.01.002
   Manring Heather R, 2017, Biophys Rev, V9, P245, DOI 10.1007/s12551-017-0254-x
   Marston S, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0138568
   McQuin C, 2018, PLOS BIOL, V16, DOI 10.1371/journal.pbio.2005970
   Mohler PJ, 2004, P NATL ACAD SCI USA, V101, P17533, DOI 10.1073/pnas.0403711101
   Mohler PJ, 2003, NATURE, V421, P634, DOI 10.1038/nature01335
   Mohler PJ, 2002, J BIOL CHEM, V277, P10599, DOI 10.1074/jbc.M110958200
   OTTO E, 1991, J CELL BIOL, V114, P241, DOI 10.1083/jcb.114.2.241
   PETERS LL, 1995, J CELL BIOL, V130, P313, DOI 10.1083/jcb.130.2.313
   Pierantozzi E, 2019, INT J MOL SCI, V20, DOI 10.3390/ijms20133361
   Porter NC, 2005, MOL MEMBR BIOL, V22, P421, DOI 10.1080/09687860500244262
   Powell JA, 2003, J NEUROSCI, V23, P8185
   Raeker MÖ, 2006, DEV DYNAM, V235, P2018, DOI 10.1002/dvdy.20812
   Randazzo D, 2017, AM J PHYSIOL-CELL PH, V312, pC16, DOI 10.1152/ajpcell.00098.2016
   Randazzo D, 2013, J CELL BIOL, V200, P523, DOI 10.1083/jcb.201205118
   Roberts JD, 2019, J CLIN INVEST, V129, P3171, DOI 10.1172/JCI125538
   Rowland TJ, 2016, J AM COLL CARDIOL, V68, P2237, DOI 10.1016/j.jacc.2016.08.052
   Russell MW, 2002, GENE, V282, P237, DOI 10.1016/S0378-1119(01)00795-8
   Stirling DR, 2021, BMC BIOINFORMATICS, V22, DOI 10.1186/s12859-021-04344-9
   Subramaniam J, 2020, J MOL CELL CARDIOL, V139, P225, DOI 10.1016/j.yjmcc.2020.02.001
   Swayne LA, 2017, CIRC-CARDIOVASC GENE, V10, DOI 10.1161/CIRCGENETICS.116.001537
   Willis CD, 2012, MOL MEMBR BIOL, V29, P36, DOI 10.3109/09687688.2012.660709
   Wu HC, 2015, CARDIOVASC RES, V107, P466, DOI 10.1093/cvr/cvv184
   Yamankurt G, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0128177
   Young P, 2001, J CELL BIOL, V154, P123, DOI 10.1083/jcb.200102110
   Zayas R, 2007, CELL CALCIUM, V41, P343, DOI 10.1016/j.ceca.2006.07.007
   Zhou DX, 1997, J CELL BIOL, V136, P621, DOI 10.1083/jcb.136.3.621
   Zhu HP, 2011, J NEUROSCI, V31, P15269, DOI 10.1523/JNEUROSCI.3766-11.2011
NR 72
TC 5
Z9 5
U1 0
U2 2
PU ELSEVIER SCI LTD
PI OXFORD
PA THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND
SN 0022-2828
EI 1095-8584
J9 J MOL CELL CARDIOL
JI J. Mol. Cell. Cardiol.
PD JUL
PY 2022
VL 168
BP 44
EP 57
DI 10.1016/j.yjmcc.2022.04.008
EA APR 2022
PG 14
WC Cardiac & Cardiovascular Systems; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology; Cell Biology
GA 1H5IK
UT WOS:000796577400002
PM 35447147
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Kim, JH
   Cheong, HS
   Kim, LH
   Shin, HJ
   Na, HS
   Chung, MW
   Shin, HD
AF Kim, Jeong-Hyun
   Cheong, Hyun Sub
   Kim, Lyoung Hyo
   Shin, Hee Jung
   Na, Han Sung
   Chung, Myeon Woo
   Shin, Hyoung Doo
TI Direct sequencing for comprehensive screening of LDLR genetic
   polymorphisms among five ethnic populations
SO GENES & GENOMICS
LA English
DT Article
DE LDLR; Single nucleotide polymorphism; Lipoprotein metabolism;
   Pharmacogenetics; Minor allele frequency
ID DENSITY-LIPOPROTEIN-RECEPTOR; CORONARY-ARTERY-DISEASE; FAMILIAL
   HYPERCHOLESTEROLEMIA; CHOLESTEROL HOMEOSTASIS; COMMON POLYMORPHISM;
   SPLICING EFFICIENCY; ALZHEIMERS-DISEASE; LIPID-METABOLISM;
   APOLIPOPROTEIN-E; N-GLYCOSYLATION
AB Low density lipoprotein receptor (LDLR) plays an important role in plasma lipoprotein metabolism and pharmacological responses. Although mutations of LDLR and their functional associations with plasma LDL cholesterol concentrations have been described, no comprehensive comparisons of LDLR variants among populations are established. The aim of this study is to define the distribution of single nucleotide polymorphisms (SNPs) of LDLR and to discover novel variants across population groups. A total of 288 DNAs from 96 Korean, 48 Chinese, 48 Japanese, 48 African-American, and 48 European-American subjects were resequenced. A total of 59 SNPs (18 in the coding regions, 37 in the introns, and 4 in the 3'-untranslated region) were identified, including eight novel variants. Polymorphisms of LDLR showed significantly different distributions in comparisons among ethnic population groups (P < 0.05, Fisher's exact test). Moreover, almost all of these differently distributed SNPs were common variants. Notably, prevalent variations-rs1003723, rs1799898, rs688, rs5925, rs6413504 in Europeans, nonsynonymous rs11669576 (Ala391Thr) in Africans, and rs14158 in Asians-were observed. In further in silico analyses for the novel SNPs, 2 intronic variants (+17716G > A in the intron 5 and +38569A > C in the intron 16) were predicted as potential branch point sites for alternative splicing. Although this study is not free from limitations such as insufficient sample size and no functional studies on the novel SNPs, our findings provides supporting information about LDLR genetic variability among ethnic groups and pharmacogenetics studies for plasma lipoprotein metabolism.
C1 [Kim, Jeong-Hyun; Shin, Hyoung Doo] Sogang Univ, Res Inst Basic Sci, Seoul 121742, South Korea.
   [Cheong, Hyun Sub; Kim, Lyoung Hyo; Shin, Hyoung Doo] SNP Genet Inc, Dept Genet Epidemiol, Seoul, South Korea.
   [Shin, Hee Jung; Na, Han Sung; Chung, Myeon Woo] Natl Inst Food & Drug Safety Evaluat, Dept Toxicol Evaluat & Res, Chungcheongbuk Do, South Korea.
   [Shin, Hyoung Doo] Sogang Univ, Dept Life Sci, Seoul 121742, South Korea.
C3 Sogang University; SNP Genetics; Ministry of Food & Drug Safety (MFDS),
   Republic of Korea; National Institute of Food & Drug Safety Evaluation;
   Sogang University
RP Shin, HD (corresponding author), Sogang Univ, Dept Life Sci, Seoul 121742, South Korea.
EM hdshin@sogang.ac.kr
RI Kim, Sun Jung/AAM-7334-2020; Kim, Hyunkyung/KRL-4586-2024
FU Ministry of Food and Drug Safety [11182MFDS658]
FX This research was supported by a grant (11182MFDS658) from Ministry of
   Food and Drug Safety in 2011.
CR Adeyemo A, 2012, BMC MED GENET, V13, DOI 10.1186/1471-2350-13-88
   AHN YI, 1994, ARTERIOSCLER THROMB, V14, P663, DOI 10.1161/01.ATV.14.5.663
   Albers JJ, 2011, BBA-PROTEINS PROTEOM, V1814, P908, DOI 10.1016/j.bbapap.2011.04.004
   Andreotti G, 2008, CANCER EPIDEM BIOMAR, V17, P525, DOI 10.1158/1055-9965.EPI-07-2704
   Benjannet S, 2012, J BIOL CHEM, V287, P33745, DOI 10.1074/jbc.M112.399725
   Bieghs V, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0030668
   BROWN MS, 1986, SCIENCE, V232, P34, DOI 10.1126/science.3513311
   Cardona A, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0098076
   Chasman DI, 2012, CIRC-CARDIOVASC GENE, V5, P257, DOI 10.1161/CIRCGENETICS.111.961144
   Cheng D, 2005, J MED GENET, V42, P129, DOI 10.1136/jmg.2004.024968
   Cross DS, 2010, BMC GENET, V11, DOI 10.1186/1471-2156-11-51
   DAMMERMAN M, 1995, CIRCULATION, V91, P505, DOI 10.1161/01.CIR.91.2.505
   Davis HR, 2011, ATHEROSCLEROSIS, V215, P266, DOI 10.1016/j.atherosclerosis.2011.02.010
   Di Lello FA, 2013, EUR J CLIN MICROBIOL, V32, P1427, DOI 10.1007/s10096-013-1894-9
   Fouchier SW, 2005, HUM MUTAT, V26, P550, DOI 10.1002/humu.20256
   Gao F, 2013, HUM MOL GENET, V22, P1424, DOI 10.1093/hmg/dds559
   Go Gwang-woong, 2012, Yale Journal of Biology and Medicine, V85, P19
   Guénard F, 2012, OBESITY, V20, P2075, DOI 10.1038/oby.2012.52
   Hobbs Helen H., 1992, Human Mutation, V1, P445, DOI 10.1002/humu.1380010602
   Holla OL, 2009, MOL GENET METAB, V96, P245, DOI 10.1016/j.ymgme.2008.12.014
   HUMPHRIES S, 1991, ARTERIOSCLER THROMB, V11, P509, DOI 10.1161/01.ATV.11.3.509
   ISHIBASHI S, 1993, J CLIN INVEST, V92, P883, DOI 10.1172/JCI116663
   Kathiresan S, 2008, NAT GENET, V40, P189, DOI 10.1038/ng.75
   KLAUSEN IC, 1993, HUM GENET, V91, P193
   Leren TP, 2014, ATHEROSCLEROSIS, V237, P76, DOI 10.1016/j.atherosclerosis.2014.08.038
   Linsel-Nitschke P, 2008, PLOS ONE, V3, DOI 10.1371/journal.pone.0002986
   Mahley RW, 2000, ANNU REV GENOM HUM G, V1, P507, DOI 10.1146/annurev.genom.1.1.507
   Martinelli N, 2010, BLOOD, V116, P5688, DOI 10.1182/blood-2010-03-277079
   Miljkovic I, 2010, J LIPID RES, V51, P1823, DOI 10.1194/jlr.M003897
   Pineda JA, 2011, AIDS, V25, P1415, DOI 10.1097/QAD.0b013e328348a7ac
   Pullinger Clive R, 2003, Expert Rev Cardiovasc Ther, V1, P107, DOI 10.1586/14779072.1.1.107
   Sanna S, 2011, PLOS GENET, V7, DOI 10.1371/journal.pgen.1002198
   Schaefer JR, 2012, CLIN RES CARDIOL S, V7, P2
   Seidelmann SB, 2005, ARTERIOSCL THROM VAS, V25, P204, DOI 10.1161/01.ATV.0000149146.32385.1b
   Skropeta D, 2007, J LIPID RES, V48, P2047, DOI 10.1194/jlr.M700248-JLR200
   Slimani A, 2012, ATHEROSCLEROSIS, V222, P158, DOI 10.1016/j.atherosclerosis.2012.02.018
   Thompson D, 2003, HUM HERED, V56, P48, DOI 10.1159/000073732
   Tishkoff SA, 2002, NAT REV GENET, V3, P611, DOI 10.1038/nrg865
   Wang B, 2009, J NEUROL SCI, V276, P118, DOI 10.1016/j.jns.2008.09.013
   Willer CJ, 2008, NAT GENET, V40, P161, DOI 10.1038/ng.76
   Xue C, 2013, J TRANSL MED, V11, DOI 10.1186/1479-5876-11-67
   Zhang LN, 2013, CLIN BIOCHEM, V46, P727, DOI 10.1016/j.clinbiochem.2013.01.013
   Zhu H, 2007, HUM MOL GENET, V16, P1765, DOI 10.1093/hmg/ddm124
   Zou FG, 2008, HUM MOL GENET, V17, P929, DOI 10.1093/hmg/ddm365
NR 44
TC 1
Z9 1
U1 0
U2 6
PU SPRINGER
PI NEW YORK
PA 233 SPRING ST, NEW YORK, NY 10013 USA
SN 1976-9571
EI 2092-9293
J9 GENES GENOM
JI Genes Genom.
PD MAR
PY 2015
VL 37
IS 3
BP 247
EP 255
DI 10.1007/s13258-014-0244-3
PG 9
WC Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology;
   Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology;
   Genetics & Heredity
GA CC3FZ
UT WOS:000350233200004
DA 2025-04-10
ER

PT J
AU Ma, C
   Wang, XY
   Zhang, LX
   Zhu, XR
   Bai, JE
   He, SY
   Mei, J
   Jiang, JQ
   Guan, XY
   Zheng, XD
   Qu, LH
   Zhu, DL
AF Ma, Cui
   Wang, Xiaoying
   Zhang, Lixin
   Zhu, Xiangrui
   Bai, June
   He, Siyu
   Mei, Jian
   Jiang, Jiaqi
   Guan, Xiaoyu
   Zheng, Xiaodong
   Qu, Lihui
   Zhu, Daling
TI Super Enhancer-Associated Circular RNA-CircKrt4 Regulates Hypoxic
   Pulmonary Artery Endothelial Cell Dysfunction in Mice
SO ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY
LA English
DT Article
DE endothelial cells; hypertension; pulmonary; mitochondria; RNA; circular
ID TO-MESENCHYMAL TRANSITION; BINDING-PROTEIN; GLYCEROL KINASE; PUR-ALPHA;
   CONTRIBUTES; IDENTIFICATION; MITOCHONDRIAL; HYPERTENSION; BIOGENESIS;
   ACTIVATION
AB Background:Circular RNAs (circRNAs) have been implicated in pulmonary hypertension progression through largely unknown mechanisms. Pulmonary artery endothelial cell (PAEC) dysfunction is a hallmark in the pathogenesis of pulmonary hypertension. However, the specific role of circular RNAs in PAEC injury caused by hypoxia remains unclear. Methods:In this study, using the Western blotting, RNA pull down, Dual-luciferase reporter assay, immunohistochemistry, and immunofluorescence, we identified a novel circular RNA derived from alternative splicing of the keratin 4 gene (circKrt4). Results:CircKrt4 was upregulated in lung tissues and plasma and specifically in PAECs under hypoxic conditions. In the nucleus, circKrt4 induces endothelial-to-mesenchymal transition by interacting with the Pura (transcriptional activator protein Pur-alpha) to promote N-cadherin gene activation. In the cytoplasm, increased circKrt4 leads to mitochondrial dysfunction by inhibiting cytoplasmic-mitochondrial shuttling of mitochondrial-bound Glpk (glycerol kinase). Intriguingly, circKrt4 was identified as a super enhancer-associated circular RNA that is transcriptionally activated by a transcription factor, CEBPA (CCAAT enhancer binding protein alpha). Furthermore, RBM25 (RNA-binding-motif protein 25) was found to regulate circKrt4 cyclization by increase the back-splicing of Krt4 gene. Conclusions:These findings demonstrate that a super enhancer-associated circular RNA-circKrt4 modulates PAEC injury to promote pulmonary hypertension by targeting Pura and Glpk.
C1 [Ma, Cui; Wang, Xiaoying; Zhang, Lixin; Zhu, Xiangrui; Bai, June; He, Siyu; Mei, Jian; Guan, Xiaoyu; Zhu, Daling] Harbin Med Univ, Cent Lab, 39 Xinyang Rd, Daqing 163319, Peoples R China.
   [Ma, Cui; Zhang, Lixin; Zhu, Xiangrui; Mei, Jian; Zheng, Xiaodong] Harbin Med Univ, Coll Med Lab Sci & Technol, Daqing, Peoples R China.
   [Jiang, Jiaqi] Harbin Med Univ, Coll Pharm, Daqing, Peoples R China.
   [Qu, Lihui] Harbin Med Univ, Coll Basic Med Sci, Daqing, Peoples R China.
   [Wang, Xiaoying; Bai, June; He, Siyu; Guan, Xiaoyu; Zhu, Daling] Harbin Med Univ, Coll Pharm, Harbin, Peoples R China.
   [Zhu, Daling] Minist Educ, Key Lab Cardiovasc Med Res, Daqing, Peoples R China.
C3 Harbin Medical University; Harbin Medical University; Harbin Medical
   University; Harbin Medical University; Harbin Medical University
RP Zhu, DL (corresponding author), Harbin Med Univ, Cent Lab, 39 Xinyang Rd, Daqing 163319, Peoples R China.
EM zhudaling@hrbmu.edu.cn
RI Zhu, Ling-cheng/AAZ-2510-2021; Zheng, Xiaodong/AAA-4379-2019
OI , Xiangrui Zhu/0009-0009-8123-6480; Zheng, Xiaodong/0000-0002-6103-9836
FU National Natural Science Foundation of China [82170059, 81873412,
   31820103007, 31771276, 31471095]; Heilongjiang Touyan Innovation Team;
   National Natural Science Foundation of Heilongjiang Province
   [LH2020H027]; Construction Project of Scientific Research and Innovation
   Team of Harbin Medical University-Daqing [HD-CXTD-202001]
FX This study was supported by National Natural Science Foundation of China
   (grant numbers 82170059 and 81873412 to C. Ma and 31820103007, 31771276,
   and 31471095 to D. Zhu); Heilongjiang Touyan Innovation Team to DZ
   Pro-gram; National Natural Science Foundation of Heilongjiang Province
   (grant number LH2020H027 to L. Qu); Construction Project of Scientific
   Research and Innovation Team of Harbin Medical University-Daqing (grant
   number HD-CXTD-202001 to C. Ma)
CR Alvarez-Dominguez JR, 2017, CELL REP, V19, P2503, DOI 10.1016/j.celrep.2017.05.082
   Bartoszewski R, 2019, FASEB J, V33, P7929, DOI 10.1096/fj.201802650RR
   Carlson SM, 2017, J BIOL CHEM, V292, P13381, DOI 10.1074/jbc.M117.784371
   Caruso P, 2017, CIRCULATION, V136, P2451, DOI 10.1161/CIRCULATIONAHA.117.028034
   Chen LL, 2020, NAT REV MOL CELL BIO, V21, P475, DOI 10.1038/s41580-020-0243-y
   Chen LL, 2016, NAT REV MOL CELL BIO, V17, P205, DOI 10.1038/nrm.2015.32
   Chen RX, 2019, NAT COMMUN, V10, DOI 10.1038/s41467-019-12651-2
   Di Stefano B, 2016, NAT CELL BIOL, V18, P371, DOI 10.1038/ncb3326
   Earley S, 2002, AM J PHYSIOL-LUNG C, V283, pL86, DOI 10.1152/ajplung.00476.2001
   Evans CE, 2021, EUR RESPIR J, V58, DOI 10.1183/13993003.03957-2020
   Ge XH, 2021, REDOX BIOL, V41, DOI 10.1016/j.redox.2021.101932
   Ge Y, 2019, NAT COMMUN, V10, DOI 10.1038/s41467-018-08076-y
   Good RB, 2015, AM J PATHOL, V185, P1850, DOI 10.1016/j.ajpath.2015.03.019
   Guo WJ, 2017, NAT COMMUN, V8, DOI 10.1038/s41467-017-02351-0
   Hu CJ, 2019, EUR RESPIR J, V54, DOI 10.1183/13993003.00378-2019
   Hua W, 2020, CELL MOL LIFE SCI, V77, P2103, DOI 10.1007/s00018-019-03398-6
   Huang C, 2018, GENE DEV, V32, P639, DOI 10.1101/gad.314856.118
   Huang SL, 2019, CIRCULATION, V139, P2857, DOI 10.1161/CIRCULATIONAHA.118.038361
   Jiang Y, 2021, ARTERIOSCL THROM VAS, V41, P1675, DOI 10.1161/ATVBAHA.120.315525
   Jin X, 2021, MOL THER-NUCL ACIDS, V23, P1007, DOI 10.1016/j.omtn.2020.09.029
   KANEKO M, 1985, ARCH BIOCHEM BIOPHYS, V237, P135, DOI 10.1016/0003-9861(85)90262-0
   Kong TQ, 2007, J IMMUNOL, V179, P1934, DOI 10.4049/jimmunol.179.3.1934
   Krachmarov CP, 1996, P NATL ACAD SCI USA, V93, P14112, DOI 10.1073/pnas.93.24.14112
   Kurakula K, 2021, BIOMEDICINES, V9, DOI 10.3390/biomedicines9010057
   Lahm T, 2016, AM J PHYSIOL-LUNG C, V311, pL375, DOI 10.1152/ajplung.00132.2016
   Lawrie A, 2021, J CLIN INVEST, V131, DOI 10.1172/JCI149721
   Li H, 2020, CARDIOVASC RES, V116, P1323, DOI 10.1093/cvr/cvz215
   Li Y, 2018, NAT REV CARDIOL, V15, P445, DOI 10.1038/s41569-018-0023-y
   Liang WC, 2021, MOL THER-NUCL ACIDS, V26, P1351, DOI 10.1016/j.omtn.2021.10.028
   Ma C, 2022, CELL BIOSCI, V12, DOI 10.1186/s13578-022-00744-3
   Ma C, 2020, MOL THER-NUCL ACIDS, V22, P530, DOI 10.1016/j.omtn.2020.09.018
   Ma C, 2011, HYPERTENSION, V58, P679, DOI 10.1161/HYPERTENSIONAHA.111.171561
   Memczak S, 2013, NATURE, V495, P333, DOI 10.1038/nature11928
   Molitor L, 2021, FRONT GENET, V12, DOI 10.3389/fgene.2021.638217
   Pandey PR, 2020, NUCLEIC ACIDS RES, V48, P3789, DOI 10.1093/nar/gkaa035
   Pu XY, 2021, ARTERIOSCL THROM VAS, V41, P167, DOI 10.1161/ATVBAHA.120.315052
   Rahib L, 2009, MOL GENET METAB, V96, P106, DOI 10.1016/j.ymgme.2008.11.163
   Rol N, 2018, INT J MOL SCI, V19, DOI 10.3390/ijms19092585
   Salzman J, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0030733
   Sánchez-Duffhues G, 2018, DEV DYNAM, V247, P492, DOI 10.1002/dvdy.24589
   Song CH, 2022, CELL DEATH DIFFER, V29, P393, DOI 10.1038/s41418-021-00865-1
   Tang FQ, 2020, NPJ PRECIS ONCOL, V4, DOI 10.1038/s41698-020-0108-z
   Tang HY, 2018, AM J PHYSIOL-LUNG C, V314, pL256, DOI 10.1152/ajplung.00096.2017
   Thandapani P, 2019, PHARMACOL THERAPEUT, V199, P129, DOI 10.1016/j.pharmthera.2019.02.014
   Wang H, 2020, CELL DEATH DIS, V11, DOI 10.1038/s41419-020-03217-y
   Wong BW, 2017, EMBO J, V36, P2187, DOI 10.15252/embj.201696150
   Xie JJ, 2018, GASTROENTEROLOGY, V154, P2137, DOI 10.1053/j.gastro.2018.02.018
   Yang Z, 2019, ONCOGENE, V38, P2516, DOI 10.1038/s41388-018-0602-8
   Yu QJ, 2017, ADV EXP MED BIOL, V967, P373, DOI 10.1007/978-3-319-63245-2_24
   Yuan P, 2021, AM J RESP CRIT CARE, V203, P1579, DOI 10.1164/rccm.202005-2052LE
   Zambrano N, 1997, BIOCHEM J, V328, P293, DOI 10.1042/bj3280293
   Zhang CT, 2021, BRIT J PHARMACOL, V178, P217, DOI 10.1111/bph.15314
   Zhang H, 2017, CIRCULATION, V136, P2468, DOI 10.1161/CIRCULATIONAHA.117.028069
   Zhang JT, 2020, HYPERTENSION, V75, P668, DOI 10.1161/HYPERTENSIONAHA.119.13715
   Zhang WH, 2014, RESP RES, V15, DOI 10.1186/s12931-014-0119-9
   Zhou A, 2008, MOL CELL BIOL, V28, P5924, DOI 10.1128/MCB.00560-08
NR 56
TC 18
Z9 18
U1 1
U2 6
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA TWO COMMERCE SQ, 2001 MARKET ST, PHILADELPHIA, PA 19103 USA
SN 1079-5642
EI 1524-4636
J9 ARTERIOSCL THROM VAS
JI Arterioscler. Thromb. Vasc. Biol.
PD JUL
PY 2023
VL 43
IS 7
BP 1179
EP 1198
DI 10.1161/ATVBAHA.122.318842
PG 20
WC Hematology; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Hematology; Cardiovascular System & Cardiology
GA K2TG2
UT WOS:001015009200015
PM 37139839
DA 2025-04-10
ER

PT J
AU Hsiao, CD
   Tsai, WY
   Horng, LS
   Tsai, HJ
AF Hsiao, CD
   Tsai, WY
   Horng, LS
   Tsai, HJ
TI Molecular structure and developmental expression of three muscle-type
   troponin T genes in zebrafish
SO DEVELOPMENTAL DYNAMICS
LA English
DT Article
DE zebrafish; troponin T; expression pattern; alternative splicing; gene
   structure; molecular evolution
ID FAST SKELETAL-MUSCLE; COMPLETE NUCLEOTIDE-SEQUENCE; TAIL
   STRIATED-MUSCLE; WALL SMOOTH-MUSCLE; REGULATORY ELEMENTS; ADULT
   ISOFORMS; CARDIAC-MUSCLE; FUGU RUBRIPES; MESSENGER-RNA; AXIAL MUSCLE
AB Troponin T (Tnnt), a troponin component, interacts with tropomyosin and is crucial to the regulation of striated muscle contraction. To gain insight into the molecular evolution and developmental regulation of Tnnt gene (Tnnt) in lower vertebrates, zebrafish Tnnt1 (slow Tnnt), Tnnt2 (cardiac Tnnt), and Tnnt3b (fast Tnnt isoform b) were characterized. The polypeptides of zebrafish Tnnt1, Tnnt2, and Tnnt3b were conserved in the central tropomyosin- and C-terminal troponin I-binding domains. However, the N-terminal hypervariable regions were highly extended and rich in glutamic acid in polypeptides of Tnnt1 and Tnnt2, but not Tnnt3b. The Tnnt2 and Tnnt3b contain introns, whereas Tnnt1 is intron-free. During development, large to small, alternatively spliced variants were detected in Tnnt2, but not in Tnnt1 or Tnnt3. Whole-mount in situ hybridization showed zebrafish Tnnt1 and Tnnt2 are activated during early somitogenesis (10 hr postfertilization, hpf) and cardiogenesis (14 hpf), respectively, but Tnnt3b is not activated until middle somitogenesis (18 hpf). Tnnt2 and Tnnt3b expression was cardiac- and fast-muscle specific, but Tnnt1 was expressed in both slow and fast muscles. We propose that three, distinct, muscle-type Tnnt evolved after the divergence of fish and deuterostome invertebrates. In zebrafish, the developmental regulation of Tnnt during somitogenesis and cardiogenesis is more restricted and simpler than in tetrapods. These new findings may provide insight into the developmental regulation and molecular evolution of vertebrate Tnnt. Developmental Dynamics 227: 266-279, 2003. (C) 2003 Wiley-Liss, Inc.
C1 Natl Taiwan Univ, Inst Fisheries Sci, Taipei 10764, Taiwan.
C3 National Taiwan University
RP Tsai, HJ (corresponding author), Natl Taiwan Univ, Inst Fisheries Sci, Taipei 10764, Taiwan.
RI Hsiao, Chung-Der/W-4535-2019
OI Hsiao, Chung-Der/0000-0002-6398-8672
CR Antin PB, 2002, DEV DYNAM, V225, P135, DOI 10.1002/dvdy.10148
   APARICIO S, 1995, P NATL ACAD SCI USA, V92, P1684, DOI 10.1073/pnas.92.5.1684
   Barton PJR, 1999, GENOMICS, V57, P102, DOI 10.1006/geno.1998.5702
   Benoist P, 1998, J BIOL CHEM, V273, P7538, DOI 10.1074/jbc.273.13.7538
   Bolland DJ, 2001, GENE, V271, P43, DOI 10.1016/S0378-1119(01)00504-2
   BREITBART RE, 1986, J MOL BIOL, V188, P313, DOI 10.1016/0022-2836(86)90157-9
   Briggs JP, 2002, AM J PHYSIOL-REG I, V282, pR3, DOI 10.1152/ajpregu.00589.2001
   Bucher EA, 1999, J BIOL CHEM, V274, P17661, DOI 10.1074/jbc.274.25.17661
   Burge C, 1997, J MOL BIOL, V268, P78, DOI 10.1006/jmbi.1997.0951
   Calvo S, 1999, MOL CELL BIOL, V19, P515
   Charlet-B N, 2002, MOL CELL, V9, P649, DOI 10.1016/S1097-2765(02)00479-3
   COOPER TA, 1985, J BIOL CHEM, V260, P1140
   COOPER TA, 1984, SCIENCE, V226, P979, DOI 10.1126/science.6095446
   DHOOT GK, 1986, MUSCLE NERVE, V9, P155, DOI 10.1002/mus.880090209
   Endo T, 1996, J BIOL CHEM, V271, P27855, DOI 10.1074/jbc.271.44.27855
   Endo T, 1997, CELL STRUCT FUNCT, V22, P197, DOI 10.1247/csf.22.197
   Farza H, 1998, J MOL CELL CARDIOL, V30, P1247, DOI 10.1006/jmcc.1998.0698
   Filatov VL, 1999, BIOCHEMISTRY-MOSCOW+, V64, P969
   FITZGIBBON J, 1995, GENE, V164, P273, DOI 10.1016/0378-1119(95)00458-I
   FYRBERG E, 1990, J MOL BIOL, V216, P657, DOI 10.1016/0022-2836(90)90390-8
   GAHLMANN R, 1987, J BIOL CHEM, V262, P16122
   Hirao Chinami, 2001, Development Growth and Differentiation, V43, pS71
   Hsiao CD, 2001, DEV DYNAM, V220, P323, DOI 10.1002/dvdy.1113
   Huang QQ, 1999, GENE, V229, P1, DOI 10.1016/S0378-1119(99)00051-7
   Huang QQ, 1999, J MOL EVOL, V49, P780, DOI 10.1007/PL00006600
   Inoue A, 1996, J BIOCHEM-TOKYO, V120, P834
   Inoue A, 1998, FISHERIES SCI, V64, P459, DOI 10.2331/fishsci.64.459
   JIN JP, 1992, J MOL BIOL, V227, P1269, DOI 10.1016/0022-2836(92)90540-Z
   Jin JP, 2001, J MOL EVOL, V52, P103, DOI 10.1007/s002390010139
   Jin JP, 1996, GENE, V168, P217, DOI 10.1016/0378-1119(95)00803-9
   JIN JP, 1988, J BIOL CHEM, V263, P7305
   Johnston IA, 1997, J EXP BIOL, V200, P849
   Ju BS, 1999, DEV GENET, V25, P158, DOI 10.1002/(SICI)1520-6408(1999)25:2<158::AID-DVG10>3.0.CO;2-6
   Kelly GM, 1997, BIOCHEM CELL BIOL, V75, P623, DOI 10.1139/bcb-75-5-623
   KIMMEL CB, 1995, DEV DYNAM, V203, P253, DOI 10.1002/aja.1002030302
   Koban MU, 2001, MECH DEVELOP, V109, P267, DOI 10.1016/S0925-4773(01)00548-2
   KOUMANS JTM, 1995, COMP BIOCHEM PHYS A, V110, P3, DOI 10.1016/0300-9629(94)00150-R
   Krishan K, 2000, J MUSCLE RES CELL M, V21, P527, DOI 10.1023/A:1026541803317
   Kusakabe R, 1999, INT J DEV BIOL, V43, P541
   Kyprianou P, 1997, BASIC APPL MYOL, V7, P287
   Marden JH, 1999, P NATL ACAD SCI USA, V96, P15304, DOI 10.1073/pnas.96.26.15304
   MESNARD L, 1993, FEBS LETT, V328, P139, DOI 10.1016/0014-5793(93)80981-Y
   Müller F, 2002, BIOESSAYS, V24, P564, DOI 10.1002/bies.10096
   Myers CD, 1996, J CELL BIOL, V132, P1061, DOI 10.1083/jcb.132.6.1061
   Nakada K, 1997, EXP CELL RES, V235, P93, DOI 10.1006/excr.1997.3654
   Nakayama M, 1996, MOL CELL BIOL, V16, P2408
   Ogut O, 1999, AM J PHYSIOL-CELL PH, V276, pC1162, DOI 10.1152/ajpcell.1999.276.5.C1162
   Ogut O, 1998, J BIOL CHEM, V273, P27858, DOI 10.1074/jbc.273.43.27858
   Oota S, 1999, MOL BIOL EVOL, V16, P856, DOI 10.1093/oxfordjournals.molbev.a026170
   PEARLSTONE JR, 1977, J BIOL CHEM, V252, P983
   Pearson WR, 1999, MOL BIOL EVOL, V16, P806, DOI 10.1093/oxfordjournals.molbev.a026165
   Perry SV, 1998, J MUSCLE RES CELL M, V19, P575
   Postlethwait JH, 1998, NAT GENET, V18, P345, DOI 10.1038/ng0498-345
   Reiter JF, 2001, DEV BIOL, V234, P330, DOI 10.1006/dbio.2001.0259
   Ryan KJ, 1996, MOL CELL BIOL, V16, P4014
   SABRY MA, 1991, J MUSCLE RES CELL M, V12, P262, DOI 10.1007/BF01745116
   Schiaffino S, 1996, PHYSIOL REV, V76, P371, DOI 10.1152/physrev.1996.76.2.371
   Schilling TF, 1997, DEVELOPMENT, V124, P2945
   Sehnert AJ, 2002, NAT GENET, V31, P106, DOI 10.1038/ng875
   Shuler CF, 2001, CRIT REV ORAL BIOL M, V12, P3, DOI 10.1177/10454411010120010201
   Stockdale FE, 1997, CELL STRUCT FUNCT, V22, P37, DOI 10.1247/csf.22.37
   Tan XG, 2002, DEV GENES EVOL, V212, P207, DOI 10.1007/s00427-002-0224-5
   Taylor JS, 2001, PHILOS T R SOC B, V356, P1661, DOI 10.1098/rstb.2001.0975
   THISSE C, 1993, DEVELOPMENT, V119, P1203
   THOMPSON JD, 1994, NUCLEIC ACIDS RES, V22, P4673, DOI 10.1093/nar/22.22.4673
   Thys TM, 1998, J EXP BIOL, V201, P2993
   Thys TM, 2001, J EXP BIOL, V204, P4249
   VANSWEARINGEN J, 1995, DEV BIOL, V170, P321, DOI 10.1006/dbio.1995.1218
   Venkatesh B, 2000, FEBS LETT, V476, P3, DOI 10.1016/S0014-5793(00)01659-8
   Wachtler F., 1992, SEMINDEVBIOL, V3, P217
   Waddleton DM, 1999, J MUSCLE RES CELL M, V20, P315, DOI 10.1023/A:1005407807658
   Wang J, 1997, GENE, V193, P105, DOI 10.1016/S0378-1119(97)00100-5
   Wang Q, 2001, ANAT RECORD, V263, P72, DOI 10.1002/ar.1078
   Wang Q, 2000, CIRC RES, V86, P478, DOI 10.1161/01.RES.86.4.478
   Warkman AS, 2002, MECH DEVELOP, V115, P143, DOI 10.1016/S0925-4773(02)00096-5
   WATERMAN RE, 1969, AM J ANAT, V125, P457, DOI 10.1002/aja.1001250406
   WILKINSON JM, 1984, EUR J BIOCHEM, V143, P47, DOI 10.1111/j.1432-1033.1984.tb08337.x
   Xu YF, 1999, DNA CELL BIOL, V18, P85, DOI 10.1089/104454999315655
   Xu YF, 2000, DEV DYNAM, V219, P201, DOI 10.1002/1097-0177(2000)9999:9999<::AID-DVDY1043>3.3.CO;2-9
   YAMANO K, 1991, GEN COMP ENDOCR, V81, P464, DOI 10.1016/0016-6480(91)90174-5
   Yan Z, 2001, J BIOL CHEM, V276, P17361, DOI 10.1074/jbc.M101251200
   Yelon D, 1999, DEV BIOL, V214, P23, DOI 10.1006/dbio.1999.9406
   Yonemura I, 2002, ZOOL SCI, V19, P215, DOI 10.2108/zsj.19.215
   Yonemura I, 2000, J EXP ZOOL, V286, P149, DOI 10.1002/(SICI)1097-010X(20000201)286:2<149::AID-JEZ7>3.0.CO;2-H
NR 84
TC 41
Z9 44
U1 0
U2 17
PU WILEY-LISS
PI NEW YORK
PA DIV JOHN WILEY & SONS INC, 605 THIRD AVE, NEW YORK, NY 10158-0012 USA
SN 1058-8388
J9 DEV DYNAM
JI Dev. Dyn.
PD JUN
PY 2003
VL 227
IS 2
BP 266
EP 279
DI 10.1002/dvdy.10305
PG 14
WC Anatomy & Morphology; Developmental Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Anatomy & Morphology; Developmental Biology
GA 686EH
UT WOS:000183308100011
PM 12761854
OA Bronze
DA 2025-04-10
ER

PT J
AU Gruber, AJ
   Zavolan, M
AF Gruber, Andreas J.
   Zavolan, Mihaela
TI Alternative cleavage and polyadenylation in health and disease
SO NATURE REVIEWS GENETICS
LA English
DT Review
ID PRE-MESSENGER-RNA; POLY(A) TAIL; U1 SNRNP; PROTHROMBIN GENE; VENOUS
   THROMBOSIS; BINDING-PROTEINS; POINT MUTATIONS; SIGNAL MUTATION; FACTOR
   CPSF-73; HELA-CELLS
AB Most human genes have multiple sites at which RNA 3. end cleavage and polyadenylation can occur, enabling the expression of distinct transcript isoforms under different conditions. Novel methods to sequence RNA 3' ends have generated comprehensive catalogues of polyadenylation (poly(A)) sites; their analysis using innovative computational methods has revealed how poly(A) site choice is regulated by core RNA 3. end processing factors, such as cleavage factor I and cleavage and polyadenylation specificity factor, as well as by other RNA-binding proteins, particularly splicing factors. Here, we review the experimental and computational methods that have enabled the global mapping of mRNA and of long non-coding RNA 3. ends, quantification of the resulting isoforms and the discovery of regulators of alternative cleavage and polyadenylation (APA). We highlight the different types of APA-derived isoforms and their functional differences, and illustrate how APA contributes to human diseases, including cancer and haematological, immunological and neurological diseases.
C1 [Gruber, Andreas J.] Univ Oxford, Oxford Big Data Inst, Nuffield Dept Med, Oxford, England.
   [Zavolan, Mihaela] Univ Basel, Biozentrum, Computat & Syst Biol, Basel, Switzerland.
C3 University of Oxford; University of Basel
RP Gruber, AJ (corresponding author), Univ Oxford, Oxford Big Data Inst, Nuffield Dept Med, Oxford, England.; Zavolan, M (corresponding author), Univ Basel, Biozentrum, Computat & Syst Biol, Basel, Switzerland.
EM andreas.gruber@bdi.ox.ac.uk; mihaela.zavolan@unibas.ch
RI Zavolan, Mihaela/JAC-8443-2023; Gruber, Andreas/AAQ-2834-2021
OI Zavolan, Mihaela/0000-0002-8832-2041
CR Almada AE, 2013, NATURE, V499, P360, DOI 10.1038/nature12349
   ALT FW, 1980, CELL, V20, P293, DOI 10.1016/0092-8674(80)90615-7
   An JJ, 2008, CELL, V134, P175, DOI 10.1016/j.cell.2008.05.045
   Andreu N, 2006, J HUM GENET, V51, P92, DOI 10.1007/s10038-005-0328-7
   Arefeen A, 2018, BIOINFORMATICS, V34, P2521, DOI 10.1093/bioinformatics/bty110
   Bacchetta R, 2018, ANN NY ACAD SCI, V1417, P5, DOI 10.1111/nyas.13011
   Bao JQ, 2016, PLOS GENET, V12, DOI 10.1371/journal.pgen.1005863
   Beaudoing E, 2000, GENOME RES, V10, P1001, DOI 10.1101/gr.10.7.1001
   Bennett CL, 2001, IMMUNOGENETICS, V53, P435, DOI 10.1007/s002510100358
   Berg MG, 2012, CELL, V150, P53, DOI 10.1016/j.cell.2012.05.029
   Berkovits BD, 2015, NATURE, V522, P363, DOI 10.1038/nature14321
   Brais B, 1998, NAT GENET, V18, P164, DOI 10.1038/ng0298-164
   Bray NL, 2016, NAT BIOTECHNOL, V34, P888, DOI 10.1038/nbt0816-888d
   Brumbaugh J, 2018, CELL, V172, P106, DOI 10.1016/j.cell.2017.11.023
   Ceelie H, 2004, J THROMB HAEMOST, V2, P119, DOI 10.1111/j.1538-7836.2003.00493.x
   Chan SL, 2014, GENE DEV, V28, P2370, DOI 10.1101/gad.250993.114
   Chang JW, 2018, NUCLEIC ACIDS RES, V46, P5996, DOI 10.1093/nar/gky340
   Chang JW, 2017, ENDOCRINOL METAB, V32, P413, DOI 10.3803/EnM.2017.32.4.413
   Chang JW, 2015, NAT COMMUN, V6, DOI 10.1038/ncomms8218
   Chuvpilo S, 1999, IMMUNITY, V10, P261, DOI 10.1016/S1074-7613(00)80026-6
   Clerici M, 2017, ELIFE, V6, DOI 10.7554/eLife.33111
   Cook KB, 2011, NUCLEIC ACIDS RES, V39, pD301, DOI 10.1093/nar/gkq1069
   Coulon A, 2014, ELIFE, V3, DOI 10.7554/eLife.03939
   Crawford EK, 1997, J BIOL CHEM, V272, P21120, DOI 10.1074/jbc.272.34.21120
   Curinha A, 2014, NUCLEUS-PHILA, V5, P508, DOI 10.4161/nucl.36360
   Dai WJ, 2012, NUCLEIC ACIDS RES, V40, P787, DOI 10.1093/nar/gkr783
   Dantonel JC, 1997, NATURE, V389, P399, DOI 10.1038/38763
   DARNELL JE, 1971, P NATL ACAD SCI USA, V68, P1321, DOI 10.1073/pnas.68.6.1321
   Decorsière A, 2012, CELL CYCLE, V11, P2578, DOI 10.4161/cc.20625
   Derti A, 2012, GENOME RES, V22, P1173, DOI 10.1101/gr.132563.111
   Dominski Z, 2005, CELL, V123, P37, DOI 10.1016/j.cell.2005.08.002
   Eckmann CR, 2011, WIRES RNA, V2, P348, DOI 10.1002/wrna.56
   EDMONDS M, 1971, P NATL ACAD SCI USA, V68, P1336, DOI 10.1073/pnas.68.6.1336
   Elkon R, 2013, NAT REV GENET, V14, P496, DOI 10.1038/nrg3482
   Elkon R, 2012, GENOME BIOL, V13, DOI 10.1186/gb-2012-13-7-r59
   Fanourgakis G, 2016, PLOS GENET, V12, DOI 10.1371/journal.pgen.1005857
   Ferraresi P, 1997, ARTERIOSCL THROM VAS, V17, P2418, DOI 10.1161/01.ATV.17.11.2418
   Floor SN, 2016, ELIFE, V5, DOI 10.7554/eLife.10921
   Fox-Walsh K, 2011, GENOMICS, V98, P266, DOI 10.1016/j.ygeno.2011.04.003
   Fu YG, 2011, GENOME RES, V21, P741, DOI 10.1101/gr.115295.110
   Gaidatzis D, 2007, BMC BIOINFORMATICS, V8, DOI 10.1186/1471-2105-8-69
   Garin I, 2010, P NATL ACAD SCI USA, V107, P3105, DOI 10.1073/pnas.0910533107
   Gehring NH, 2001, NAT GENET, V28, P389, DOI 10.1038/ng578
   Giudice G, 2016, DATABASE-OXFORD, DOI 10.1093/database/baw035
   Goers ES, 2010, NUCLEIC ACIDS RES, V38, P2467, DOI 10.1093/nar/gkp1209
   Graham RR, 2007, P NATL ACAD SCI USA, V104, P6758, DOI 10.1073/pnas.0701266104
   Grassi E, 2016, BMC BIOINFORMATICS, V17, DOI 10.1186/s12859-016-1254-8
   Gruber AJ, 2018, NAT METHODS, V15, P832, DOI 10.1038/s41592-018-0114-z
   Gruber AJ, 2018, GENOME BIOL, V19, DOI 10.1186/s13059-018-1415-3
   Gruber AJ, 2016, GENOME RES, V26, P1145, DOI 10.1101/gr.202432.115
   Gruber AR, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms6465
   Gruber AR, 2014, WIRES RNA, V5, P183, DOI 10.1002/wrna.1206
   Gruber AR, 2012, RNA BIOL, V9, P1405, DOI 10.4161/rna.22570
   Ha KCH, 2018, GENOME BIOL, V19, DOI 10.1186/s13059-018-1414-4
   HARTEVELD CL, 1994, BRIT J HAEMATOL, V87, P139, DOI 10.1111/j.1365-2141.1994.tb04883.x
   Hellquist A, 2007, J MED GENET, V44, P314, DOI 10.1136/jmg.2006.046185
   HIGGS DR, 1983, NATURE, V306, P398, DOI 10.1038/306398a0
   Hill CH, 2019, MOL CELL, V73, P1217, DOI 10.1016/j.molcel.2018.12.023
   Hoffman Y, 2016, PLOS GENET, V12, DOI 10.1371/journal.pgen.1005879
   Hoque M, 2013, NAT METHODS, V10, P133, DOI [10.1038/NMETH.2288, 10.1038/nmeth.2288]
   Hosoda N, 2006, MOL CELL BIOL, V26, P3085, DOI 10.1128/MCB.26.8.3085-3097.2006
   Hwang HW, 2016, CELL REP, V15, P423, DOI 10.1016/j.celrep.2016.03.023
   Izquierdo JM, 2008, J BIOL CHEM, V283, P19077, DOI 10.1074/jbc.M800017200
   Jan CH, 2011, NATURE, V469, P97, DOI 10.1038/nature09616
   Jenal M, 2012, CELL, V149, DOI 10.1016/j.cell.2012.03.022
   Ji XJ, 2016, NUCLEIC ACIDS RES, V44, P2283, DOI 10.1093/nar/gkw088
   Ji XJ, 2013, MOL CELL BIOL, V33, P2560, DOI 10.1128/MCB.01380-12
   Ji Z, 2009, PLOS ONE, V4, DOI 10.1371/journal.pone.0008419
   Kaida D, 2010, NATURE, V468, P664, DOI 10.1038/nature09479
   Kanitz A, 2015, GENOME BIOL, V16, DOI 10.1186/s13059-015-0702-5
   Kaufmann I, 2004, EMBO J, V23, P616, DOI 10.1038/sj.emboj.7600070
   KELLER W, 1991, EMBO J, V10, P4241, DOI 10.1002/j.1460-2075.1991.tb05002.x
   Kühn U, 2009, J BIOL CHEM, V284, P22803, DOI 10.1074/jbc.M109.018226
   Kyburz A, 2006, MOL CELL, V23, P195, DOI 10.1016/j.molcel.2006.05.037
   Lackford B, 2014, EMBO J, V33, P878, DOI 10.1002/embj.201386537
   Lane DA, 2000, BLOOD, V95, P1517, DOI 10.1182/blood.V95.5.1517.005k48_1517_1532
   Lee SH, 2018, NATURE, V561, P127, DOI 10.1038/s41586-018-0465-8
   Leung MKK, 2018, BIOINFORMATICS, V34, P2889, DOI 10.1093/bioinformatics/bty211
   Li WC, 2015, PLOS GENET, V11, DOI 10.1371/journal.pgen.1005166
   Lianoglou S, 2013, GENE DEV, V27, P2380, DOI 10.1101/gad.229328.113
   Lim J, 2016, GENE DEV, V30, P1671, DOI 10.1101/gad.284802.116
   Lima SA, 2017, NAT STRUCT MOL BIOL, V24, P1057, DOI 10.1038/nsmb.3499
   Lou H, 1996, GENE DEV, V10, P208, DOI 10.1101/gad.10.2.208
   Luo WT, 2013, PLOS GENET, V9, DOI 10.1371/journal.pgen.1003613
   Ma WR, 2018, CELL, V175, P1492, DOI 10.1016/j.cell.2018.10.007
   MACDONALD CC, 1994, MOL CELL BIOL, V14, P6647, DOI 10.1128/MCB.14.10.6647
   Makeyev AV, 2002, RNA, V8, P265, DOI 10.1017/S1355838202024627
   Mandel CR, 2006, NATURE, V444, P953, DOI 10.1038/nature05363
   Martin G, 2012, CELL REP, V1, P753, DOI 10.1016/j.celrep.2012.05.003
   Masamha CP, 2014, NATURE, V510, P412, DOI 10.1038/nature13261
   Masuda A, 2015, GENE DEV, V29, P1045, DOI 10.1101/gad.255737.114
   Mattioli CC, 2019, NUCLEIC ACIDS RES, V47, P2560, DOI 10.1093/nar/gky1270
   Mayr C, 2019, CSH PERSPECT BIOL, V11, DOI 10.1101/cshperspect.a034728
   Mayr C, 2016, TRENDS CELL BIOL, V26, P227, DOI 10.1016/j.tcb.2015.10.012
   Mayr C, 2009, CELL, V138, P673, DOI 10.1016/j.cell.2009.06.016
   Millevoi S, 2006, EMBO J, V25, P4854, DOI 10.1038/sj.emboj.7601331
   MURTHY KGK, 1992, J BIOL CHEM, V267, P14804
   Neve J, 2017, RNA BIOL, V14, P865, DOI 10.1080/15476286.2017.1306171
   NIWA M, 1990, GENE DEV, V4, P1552, DOI 10.1101/gad.4.9.1552
   Oh JM, 2017, NAT STRUCT MOL BIOL, V24, P993, DOI 10.1038/nsmb.3473
   ORKIN SH, 1985, EMBO J, V4, P453, DOI 10.1002/j.1460-2075.1985.tb03650.x
   Ozsolak F, 2010, CELL, V143, P1018, DOI 10.1016/j.cell.2010.11.020
   Park JE, 2016, MOL CELL, V62, P462, DOI 10.1016/j.molcel.2016.04.007
   Patro R, 2017, NAT METHODS, V14, P417, DOI 10.1038/nmeth.4197
   PEATTIE DA, 1994, GENE, V150, P251, DOI 10.1016/0378-1119(94)90434-0
   Pelechano V, 2014, NAT PROTOC, V9, P1740, DOI 10.1038/nprot.2014.121
   Pertea M, 2015, NAT BIOTECHNOL, V33, P290, DOI 10.1038/nbt.3122
   Plass M, 2017, PLOS COMPUT BIOL, V13, DOI 10.1371/journal.pcbi.1005460
   Polydorides AD, 2000, P NATL ACAD SCI USA, V97, P6350, DOI 10.1073/pnas.110128397
   Poort SR, 1996, BLOOD, V88, P3698, DOI 10.1182/blood.V88.10.3698.bloodjournal88103698
   PROUDFOOT NJ, 1976, NATURE, V263, P211, DOI 10.1038/263211a0
   Reyes A, 2018, NUCLEIC ACIDS RES, V46, P582, DOI 10.1093/nar/gkx1165
   Ridker PM, 1999, CIRCULATION, V99, P999, DOI 10.1161/01.CIR.99.8.999
   Rot G, 2017, CELL REP, V19, P1056, DOI 10.1016/j.celrep.2017.04.028
   Routh A, 2017, NUCLEIC ACIDS RES, V45, DOI 10.1093/nar/gkx286
   RUND D, 1992, P NATL ACAD SCI USA, V89, P4324, DOI 10.1073/pnas.89.10.4324
   Sandberg R, 2008, SCIENCE, V320, P1643, DOI 10.1126/science.1155390
   Sanfilippo P, 2017, METHODS, V126, P86, DOI 10.1016/j.ymeth.2017.06.003
   Schäfer P, 2018, RNA, V24, P1721, DOI 10.1261/rna.068056.118
   Schönemann L, 2014, GENE DEV, V28, P2381, DOI 10.1101/gad.250985.114
   Schwartz JC, 2015, ANNU REV BIOCHEM, V84, P355, DOI 10.1146/annurev-biochem-060614-034325
   SHEETS MD, 1990, NUCLEIC ACIDS RES, V18, P5799, DOI 10.1093/nar/18.19.5799
   Shepard PJ, 2011, RNA, V17, P761, DOI 10.1261/rna.2581711
   Shi YS, 2009, MOL CELL, V33, P365, DOI 10.1016/j.molcel.2008.12.028
   Shin JH, 2007, GENES IMMUN, V8, P503, DOI 10.1038/sj.gene.6364413
   Singh I, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-04112-z
   Singh P, 2009, CANCER RES, V69, P9422, DOI 10.1158/0008-5472.CAN-09-2236
   SINGH R, 1995, SCIENCE, V268, P1173, DOI 10.1126/science.7761834
   Spies N, 2013, GENOME RES, V23, P2078, DOI 10.1101/gr.156919.113
   Stacey SN, 2011, NAT GENET, V43, P1098, DOI 10.1038/ng.926
   Subtelny AO, 2014, NATURE, V508, P66, DOI 10.1038/nature13007
   Sun YD, 2018, P NATL ACAD SCI USA, V115, pE1419, DOI 10.1073/pnas.1718723115
   Tajnik M, 2015, NUCLEIC ACIDS RES, V43, P10492, DOI 10.1093/nar/gkv956
   Takagaki Y, 1996, CELL, V87, P941, DOI 10.1016/S0092-8674(00)82000-0
   Taliaferro JM, 2016, MOL CELL, V61, P821, DOI 10.1016/j.molcel.2016.01.020
   Tian B, 2005, NUCLEIC ACIDS RES, V33, P201, DOI 10.1093/nar/gki158
   Tian B, 2017, NAT REV MOL CELL BIO, V18, P18, DOI 10.1038/nrm.2016.116
   Ule J, 2006, NATURE, V444, P580, DOI 10.1038/nature05304
   Van Etten JL, 2017, CANCER RES, V77, P5228, DOI 10.1158/0008-5472.CAN-17-0320
   Van Nostrand EL, 2016, NAT METHODS, V13, P508, DOI [10.1038/NMETH.3810, 10.1038/nmeth.3810]
   Venkataraman K, 2005, GENE DEV, V19, P1315, DOI 10.1101/gad.1298605
   Vorlová S, 2011, MOL CELL, V43, P927, DOI 10.1016/j.molcel.2011.08.009
   Wahl MC, 2009, CELL, V136, P701, DOI 10.1016/j.cell.2009.02.009
   Wallace AM, 1999, P NATL ACAD SCI USA, V96, P6763, DOI 10.1073/pnas.96.12.6763
   Wang RJ, 2018, GENOME RES, V28, P1427, DOI 10.1101/gr.237826.118
   Wang RJ, 2018, NUCLEIC ACIDS RES, V46, pD315, DOI 10.1093/nar/gkx1000
   Wang W, 2014, BIOINFORMATICS, V30, P2162, DOI 10.1093/bioinformatics/btu189
   Weinstein JN, 2013, NAT GENET, V45, P1113, DOI 10.1038/ng.2764
   Wiestner A, 2007, BLOOD, V109, P4599, DOI 10.1182/blood-2006-08-039859
   Xia Z, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms6274
   Xue ZY, 2018, BMC GENOMICS, V19, DOI 10.1186/s12864-018-4903-7
   Yang Q, 2011, STRUCTURE, V19, P368, DOI 10.1016/j.str.2010.12.021
   Yang Q, 2010, P NATL ACAD SCI USA, V107, P10062, DOI 10.1073/pnas.1000848107
   Yao CG, 2013, RNA, V19, P1781, DOI 10.1261/rna.042317.113
   Yao CG, 2012, P NATL ACAD SCI USA, V109, P18773, DOI 10.1073/pnas.1211101109
   Ye CT, 2018, BIOINFORMATICS, V34, P1841, DOI 10.1093/bioinformatics/bty029
   Yoon OK, 2010, RNA, V16, P1256, DOI 10.1261/rna.2038810
   You LM, 2015, NUCLEIC ACIDS RES, V43, pD59, DOI 10.1093/nar/gku1076
   Yudin D, 2008, NEURON, V59, P241, DOI 10.1016/j.neuron.2008.05.029
   Zarnack K, 2013, CELL, V152, P453, DOI 10.1016/j.cell.2012.12.023
   Zhao J, 1999, MICROBIOL MOL BIOL R, V63, P405, DOI 10.1128/MMBR.63.2.405-445.1999
   Zheng DH, 2014, ADV EXP MED BIOL, V825, P97, DOI 10.1007/978-1-4939-1221-6_3
   Zhu H, 2007, J BIOL CHEM, V282, P2203, DOI 10.1074/jbc.M609349200
   Zhu Y, 2018, MOL CELL, V69, P62, DOI 10.1016/j.molcel.2017.11.031
NR 164
TC 295
Z9 316
U1 4
U2 77
PU NATURE PUBLISHING GROUP
PI LONDON
PA MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
SN 1471-0056
EI 1471-0064
J9 NAT REV GENET
JI Nat. Rev. Genet.
PD OCT
PY 2019
VL 20
IS 10
BP 599
EP 614
DI 10.1038/s41576-019-0145-z
PG 16
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA IZ7SM
UT WOS:000487297600007
PM 31267064
DA 2025-04-10
ER

PT J
AU Maree, AO
   Vangjeli, C
   Jneid, H
   Ryan, J
   Cox, D
   Cannon, CP
   Shields, DC
   Fitzgerald, DJ
AF Maree, A. O.
   Vangjeli, C.
   Jneid, H.
   Ryan, J.
   Cox, D.
   Cannon, C. P.
   Shields, D. C.
   Fitzgerald, D. J.
TI G-protein β3 subunit polymorphism and bleeding in the orbofiban in
   patients with unstable coronary syndromes-thrombolysis in myocardial
   infarction 16 trial
SO JOURNAL OF THROMBOSIS AND HAEMOSTASIS
LA English
DT Article
DE bleeding; cardiovascular disease; genetics; pharmacology; platelets;
   thrombosis
ID 825T ALLELE; C825T POLYMORPHISM; PLATELET RESPONSE; SEX-DIFFERENCES;
   ASSOCIATION; RISK; ASPIRIN; HERITABILITY; ACTIVATION; VARIANT
AB Background: Variability in platelet response to antiplatelet drugs is heritable. A common single base substitution (825C > T) in the G-protein beta polypeptide 3 (GNB3) gene leads to alternative splicing (41-amino-acid deletion) of the human G-protein beta 3 (G beta 3) subunit. This truncated protein carried by GNB3 T allele carriers is linked to coronary artery disease and implicated as a genetic marker of drug response. Large studies of Caucasians associate T allele carriage with lower platelet reactivity.Objectives: To evaluate whether the GNB3 genotype would predispose to bleeding in patients treated with a GPIIb/IIIa receptor antagonist. Methods: GNB3 genotype distribution was determined in DNA samples from patients in the orbofiban in patients with unstable coronary syndromes-thrombolysis in myocardial infarction (OPUS-TIMI) 16 genetic sub-study. Impact of genotype on the bleeding endpoint and the composite primary endpoint of death, myocardial infarction (MI), re-hospitalization for ischemia and urgent revascularization was estimated in the treatment and placebo arm. Results: Out of 887 patients, 45.1% carried the GNB3 CC genotype, 44.5% CT and 10.4% TT. Interaction between T allele carriership and treatment for bleeding was significant (P = 0.008). This reflects the fact that GNB3 non-T carriers treated with orbofiban had no bleeding effect compared with placebo (RR = 0.92, 95% CI 0.55-1.55) whereas T carriers did (RR = 2.62, 95% CI 1.58-4.35, P < 0.001). Interaction between T allele carriership and treatment was not significant for the primary endpoint (P = 0.18) or MI (P = 0.69). Conclusion: The GNB3 T allele significantly increased bleeding in patients treated with the platelet antagonist orbofiban. Our findings suggest that risk of bleeding associated with an antiplatelet agent is heritable and may be dissociated from risk of thrombosis.
C1 [Maree, A. O.] Waterford Reg Hosp, Cardiol Sect, Waterford, Ireland.
   [Maree, A. O.; Vangjeli, C.; Cox, D.] Royal Coll Surgeons Ireland, Dept Clin Pharmacol, Dublin 2, Ireland.
   [Jneid, H.] Michael E DeBakey VA Med Ctr, Div Cardiol, Houston, TX USA.
   [Jneid, H.] Baylor Coll Med, Houston, TX 77030 USA.
   [Ryan, J.] Univ Chicago, Med Ctr, Div Cardiol, Chicago, IL 60637 USA.
   [Cannon, C. P.] Harvard Univ, Brigham & Womens Hosp, Dept Med, Sch Med, Boston, MA 02115 USA.
   [Shields, D. C.; Fitzgerald, D. J.] Univ Coll Dublin, Mol Med Lab, Conway Inst, Dublin 2, Ireland.
C3 Royal College of Surgeons - Ireland; Baylor College of Medicine; Baylor
   College Medical Hospital; Baylor College of Medicine; University of
   Chicago; University of Chicago Medical Center; Harvard University;
   Harvard University Medical Affiliates; Brigham & Women's Hospital;
   Harvard Medical School; University College Dublin
RP Maree, AO (corresponding author), Waterford Reg Hosp, Cardiol Sect, Waterford, Ireland.
EM andrew.maree@gmail.com
RI Cannon, Christopher/AAY-7644-2020; /B-4329-2010; Maree,
   Andrew/AAO-5313-2021; Ryan, John/B-7632-2012; Cox, Dermot/A-8465-2008
OI Shields, Denis/0000-0003-4015-2474; Cox, Dermot/0000-0003-1365-3396;
   Maree, Andrew/0000-0002-0002-5828
FU GD Searle and company; Irish Heart Foundation; Higher Education
   Authority of Ireland
FX The original OPUS-TIMI 16 trial was sponsored by GD Searle and company.
   Genetic sub-analyses were supported by grants from the Irish Heart
   Foundation and Higher Education Authority of Ireland.
CR Alexander KP, 2006, CIRCULATION, V114, P1380, DOI 10.1161/CIRCULATIONAHA.106.620815
   Becker DM, 2006, JAMA-J AM MED ASSOC, V295, P1420, DOI 10.1001/jama.295.12.1420
   Bray PF, 2007, J THROMB HAEMOST, V5, P1617, DOI 10.1111/j.1538-7836.2007.02618.x
   Cannon CP, 2000, CIRCULATION, V102, P149, DOI 10.1161/01.CIR.102.2.149
   Dobrev D, 2000, CIRCULATION, V102, P692, DOI 10.1161/01.CIR.102.6.692
   Faraday N, 2007, CIRCULATION, V115, P2490, DOI 10.1161/CIRCULATIONAHA.106.667584
   FITZGERALD DJ, 1986, NEW ENGL J MED, V315, P983, DOI 10.1056/NEJM198610163151602
   Frey UH, 2003, THROMB RES, V109, P279, DOI 10.1016/S0049-3848(03)00253-6
   Hauner H, 2003, PHARMACOGENETICS, V13, P453, DOI 10.1097/00008571-200308000-00003
   Klintschar A, 2005, FORENSIC SCI INT, V153, P142, DOI 10.1016/j.forsciint.2004.09.103
   Law DA, 1999, NATURE, V401, P808, DOI 10.1038/44599
   Maree A, 2004, EUR HEART J, V25, P238
   Maree AO, 2007, CIRCULATION, V115, P2196, DOI 10.1161/CIRCULATIONAHA.106.675991
   Maree AO, 2005, J THROMB HAEMOST, V3, P2340, DOI 10.1111/j.1538-7836.2005.01555.x
   MILLER SA, 1988, NUCLEIC ACIDS RES, V16, P1215, DOI 10.1093/nar/16.3.1215
   Naber CK, 2003, PHARMACOGENETICS, V13, P279, DOI 10.1097/00008571-200305000-00007
   O'Connor FF, 2001, BLOOD, V98, P3256, DOI 10.1182/blood.V98.12.3256
   O'Donnell CJ, 2001, CIRCULATION, V103, P3051, DOI 10.1161/01.CIR.103.25.3051
   Richardson M, 1999, J BIOL CHEM, V274, P13525, DOI 10.1074/jbc.274.19.13525
   Schreieck J, 2004, AM HEART J, V148, P545, DOI 10.1016/j.ahj.2004.03.024
   Shields D. C., 2002, Pharmacogenomics Journal, V2, P182, DOI 10.1038/sj.tpj.6500100
   Siffert W, 1999, J AM SOC NEPHROL, V10, P1921
   Siffert W, 1998, NAT GENET, V18, P45, DOI 10.1038/ng0198-45
   Simoons ML, 2001, LANCET, V357, P1915
   Sperling H, 2003, J UROLOGY, V169, P1048, DOI 10.1097/01.ju.0000058369.72348.ba
   Sun AJ, 2005, EUR J HUM GENET, V13, P361, DOI 10.1038/sj.ejhg.5201334
   Topol E, 1998, NEW ENGL J MED, V339, P436
   von Beckerath N, 2003, ATHEROSCLEROSIS, V167, P135, DOI 10.1016/S0021-9150(02)00422-7
   von Beckerath N, 2000, ATHEROSCLEROSIS, V149, P151, DOI 10.1016/S0021-9150(99)00317-2
   Wascher TC, 2003, STROKE, V34, P605, DOI 10.1161/01.STR.0000058159.63950.EA
NR 30
TC 5
Z9 6
U1 0
U2 0
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 1538-7933
EI 1538-7836
J9 J THROMB HAEMOST
JI J. Thromb. Haemost.
PD MAY
PY 2010
VL 8
IS 5
BP 934
EP 941
DI 10.1111/j.1538-7836.2010.03775.x
PG 8
WC Hematology; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Hematology; Cardiovascular System & Cardiology
GA 591TW
UT WOS:000277328600010
PM 20096003
OA Bronze
DA 2025-04-10
ER

PT J
AU Lampasona, AA
   Czaplinski, K
AF Lampasona, Alexa A.
   Czaplinski, Kevin
TI Hnrnpab regulates neural cell motility through transcription of Eps8
SO RNA
LA English
DT Article
DE RNA binding protein; cell motility; regulation of gene expression
ID ACTIN MESSENGER-RNA; GENE-EXPRESSION; BINDING-FACTOR; STEM-CELL; CBF-A;
   PROTEIN BINDS; MICE LACKING; RHO GTPASES; GROWTH; LOCALIZATION
AB Cell migration requires a complicated network of structural and regulatory proteins. Changes in cellular motility can impact migration as a result of cell-type or developmental stage regulated expression of critical motility genes. Hnrnpab is a conserved RNA-binding protein found as two isoforms produced by alternative splicing. Its expression is enriched in the sub-ventricular zone (SVZ) and the rostral migratory stream within the brain, suggesting possible support of the migration of neural progenitor cells in this region. Here we show that the migration of cells from the SVZ of developing Hnrnpab(-/-) mouse brains is impaired. An RNA-seq analysis to identify Hnrnpab-dependent cell motility genes led us to Eps8, and in agreement with the change in cell motility, we show that Eps8 is decreased in Hnrnpab(-/-) SVZ tissue. We scrutinized the motility of Hnrnpab(-/-) cells and confirmed that the decreases in both cell motility and Eps8 are restored by ectopically coexpressing both alternatively spliced Hnrnpab isoforms, therefore these variants are surprisingly nonredundant for cell motility. Our results support a model where both Hnrnpab isoforms work in concert to regulate Eps8 transcription in the mouse SVZ to promote the normal migration of neural cells during CNS development.
C1 [Lampasona, Alexa A.] SUNY Stony Brook, Program Mol & Cellular Pharmacol, Stony Brook, NY 11749 USA.
   [Lampasona, Alexa A.; Czaplinski, Kevin] SUNY Stony Brook, Ctr Mol Med, Stony Brook, NY 11749 USA.
   [Czaplinski, Kevin] SUNY Stony Brook, Dept Anesthesiol, Stony Brook, NY 11749 USA.
C3 State University of New York (SUNY) System; Stony Brook University;
   State University of New York (SUNY) System; Stony Brook University;
   State University of New York (SUNY) System; Stony Brook University
RP Czaplinski, K (corresponding author), SUNY Stony Brook, Ctr Mol Med, Stony Brook, NY 11749 USA.; Czaplinski, K (corresponding author), SUNY Stony Brook, Dept Anesthesiol, Stony Brook, NY 11749 USA.
EM Kevin.Czaplinski@stonybrook.edu
RI Czaplinski, Kevin/AAL-5625-2020
FU National Science Foundation CAREER award [IOS-1254146]
FX This work was supported by research funds supplied by the Stony Brook
   School of Medicine and a National Science Foundation CAREER award
   (IOS-1254146) to K.C.
CR Akindahunsi AA, 2005, COMPUT BIOL CHEM, V29, P13, DOI 10.1016/j.compbiolchem.2004.11.002
   Apostolopoulou M, 2017, STEM CELL REP, V9, P1931, DOI 10.1016/j.stemcr.2017.10.005
   Aranburu A, 2006, EUR J IMMUNOL, V36, P2192, DOI 10.1002/eji.200535659
   Auciello G, 2013, J CELL SCI, V126, P613, DOI 10.1242/jcs.116228
   Baghirova S, 2015, METHODSX, V2, P440, DOI 10.1016/j.mex.2015.11.001
   Baltz AG, 2012, MOL CELL, V46, P674, DOI 10.1016/j.molcel.2012.05.021
   BAZAR L, 1995, J BIOL CHEM, V270, P8241, DOI 10.1074/jbc.270.14.8241
   Briese M, 2018, P NATL ACAD SCI USA, V115, pE2859, DOI 10.1073/pnas.1721670115
   Bunnell TM, 2011, MOL BIOL CELL, V22, P4047, DOI 10.1091/mbc.E11-06-0582
   Burridge K, 2004, CELL, V116, P167, DOI 10.1016/S0092-8674(04)00003-0
   Caric D, 2001, DEVELOPMENT, V128, P4203
   CASTAGNINO P, 1995, ONCOGENE, V10, P723
   Castello A, 2012, CELL, V149, P1393, DOI 10.1016/j.cell.2012.04.031
   CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
   Cléry A, 2008, CURR OPIN STRUC BIOL, V18, P290, DOI 10.1016/j.sbi.2008.04.002
   Condeelis J, 2005, BIOL CELL, V97, P97
   Cooper AR, 2015, NUCLEIC ACIDS RES, V43, P682, DOI 10.1093/nar/gku1312
   Czaplinski K, 2006, RNA, V12, P213, DOI 10.1261/rna.2820106
   Czaplinski K, 2005, DEV CELL, V8, P505, DOI 10.1016/j.devcel.2005.01.012
   Daubner GM, 2013, CURR OPIN STRUC BIOL, V23, P100, DOI 10.1016/j.sbi.2012.11.006
   Dichmann DS, 2008, DEV DYNAM, V237, P1755, DOI 10.1002/dvdy.21590
   Ding JZ, 1999, GENE DEV, V13, P1102, DOI 10.1101/gad.13.9.1102
   Disanza A, 2004, NAT CELL BIOL, V6, P1180, DOI 10.1038/ncb1199
   Disanza A, 2006, NAT CELL BIOL, V8, P1337, DOI 10.1038/ncb1502
   Dizon MLV, 2006, NEUROSCIENCE, V142, P717, DOI 10.1016/j.neuroscience.2006.06.050
   Dormoy-Raclet V, 2007, MOL CELL BIOL, V27, P5365, DOI 10.1128/MCB.00113-07
   Enokizono Y, 2005, J BIOL CHEM, V280, P18862, DOI 10.1074/jbc.M411822200
   FAZIOLI F, 1993, EMBO J, V12, P3799, DOI 10.1002/j.1460-2075.1993.tb06058.x
   Fregnan F, 2011, EXP CELL RES, V317, P757, DOI 10.1016/j.yexcr.2011.01.023
   Frittoli E, 2011, IMMUNITY, V35, P388, DOI 10.1016/j.immuni.2011.07.007
   Funato Y, 2004, CANCER RES, V64, P5237, DOI 10.1158/0008-5472.CAN-04-0327
   Gao CJ, 2004, J BIOL CHEM, V279, P11236, DOI 10.1074/jbc.M313385200
   Gerstberger S, 2014, NAT REV GENET, V15, P829, DOI 10.1038/nrg3813
   Girauda M, 2014, P NATL ACAD SCI USA, V111, P1491, DOI 10.1073/pnas.1323535111
   Gong SC, 2003, NATURE, V425, P917, DOI 10.1038/nature02033
   Gonzalez-Perez O, 2011, BRAIN RES REV, V67, P147, DOI 10.1016/j.brainresrev.2011.01.001
   Hertzog M, 2010, PLOS BIOL, V8, DOI 10.1371/journal.pbio.1000387
   Innocenti M, 2003, J CELL BIOL, V160, P17, DOI 10.1083/jcb.200206079
   Yan CYI, 2009, DEV DYNAM, V238, P204, DOI 10.1002/dvdy.21826
   Jeronimo C, 2007, MOL CELL, V27, P262, DOI 10.1016/j.molcel.2007.06.027
   Kaneko N, 2017, J NEUROCHEM, V141, P835, DOI 10.1111/jnc.14002
   Katz ZB, 2012, GENE DEV, V26, P1885, DOI 10.1101/gad.190413.112
   Kennedy SP, 2016, FRONT CELL DEV BIOL, V4, DOI 10.3389/fcell.2016.00088
   Kislauskis EH, 1997, J CELL BIOL, V136, P1263, DOI 10.1083/jcb.136.6.1263
   Kornblum HI, 1998, J NEUROSCI RES, V53, P697, DOI 10.1002/(SICI)1097-4547(19980915)53:6<697::AID-JNR8>3.0.CO;2-0
   Kroll TT, 2009, MECH DEVELOP, V126, P523, DOI 10.1016/j.mod.2009.03.007
   KUMAR A, 1987, J BIOL CHEM, V262, P17126
   Lanzetti L, 2000, NATURE, V408, P374, DOI 10.1038/35042605
   Lein ES, 2007, NATURE, V445, P168, DOI 10.1038/nature05453
   Lemieux B, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0126654
   Leverrier S, 2000, BIOL CHEM, V381, P1031, DOI 10.1515/BC.2000.127
   Li YH, 2013, FUTURE ONCOL, V9, P1587, DOI 10.2217/fon.13.104
   Liao GN, 2015, WIRES RNA, V6, P1, DOI 10.1002/wrna.1265
   Lim DA, 2016, CSH PERSPECT BIOL, V8, DOI 10.1101/cshperspect.a018820
   Lionnet T, 2011, NAT METHODS, V8, P165, DOI [10.1038/nmeth.1551, 10.1038/NMETH.1551]
   Lu PD, 2004, EMBO J, V23, P169, DOI 10.1038/sj.emboj.7600030
   Mazan-Mamczarz K, 2009, NUCLEIC ACIDS RES, V37, P204, DOI 10.1093/nar/gkn929
   McKee AE, 2005, BMC DEV BIOL, V5, DOI 10.1186/1471-213X-5-14
   McNamara RP, 2013, CELL REP, V5, P1256, DOI 10.1016/j.celrep.2013.11.003
   Meijering E, 2012, METHOD ENZYMOL, V504, P183, DOI 10.1016/B978-0-12-391857-4.00009-4
   Mikheev AM, 2000, NUCLEIC ACIDS RES, V28, P3762, DOI 10.1093/nar/28.19.3762
   Ming GL, 2011, NEURON, V70, P687, DOI 10.1016/j.neuron.2011.05.001
   Mitra S, 2011, J BIOL CHEM, V286, P15287, DOI 10.1074/jbc.M109.094441
   Mizuguchi H, 2000, MOL THER, V1, P376, DOI 10.1006/mthe.2000.0050
   Mostoslavsky G, 2006, P NATL ACAD SCI USA, V103, P16406, DOI 10.1073/pnas.0608130103
   Murali A, 2014, CELL MOL LIFE SCI, V71, P1703, DOI 10.1007/s00018-013-1519-6
   Murgatroyd C, 2004, J NEUROSCI, V24, P7762, DOI 10.1523/JNEUROSCI.1614-04.2004
   Panda AC, 2014, MOL CELL BIOL, V34, P3106, DOI 10.1128/MCB.00423-14
   Pérez-Cañadillas JM, 2006, EMBO J, V25, P3167, DOI 10.1038/sj.emboj.7601190
   Poling BC, 2017, RNA BIOL, V14, P1570, DOI 10.1080/15476286.2017.1334755
   Pont AR, 2012, MOL CELL, V47, P5, DOI 10.1016/j.molcel.2012.04.019
   Quinn LM, 2017, TRANSCR-AUSTIN, V8, P185, DOI 10.1080/21541264.2017.1293595
   Raju CS, 2008, MOL BIOL CELL, V19, P3008, DOI 10.1091/mbc.E07-10-1083
   Raju CS, 2011, MOL BIOL CELL, V22, P1864, DOI 10.1091/mbc.E10-11-0904
   Ridley AJ, 2006, TRENDS CELL BIOL, V16, P522, DOI 10.1016/j.tcb.2006.08.006
   Riquelme PA, 2008, PHILOS T R SOC B, V363, P123, DOI 10.1098/rstb.2006.2016
   Rushlow WJ, 1999, NEUROSCIENCE, V94, P637, DOI 10.1016/S0306-4522(99)00342-5
   Sarig G, 1997, BIOCHEM BIOPH RES CO, V237, P617, DOI 10.1006/bbrc.1997.7198
   Scita G, 1999, NATURE, V401, P290, DOI 10.1038/45822
   Scita G, 2001, J CELL BIOL, V154, P1031, DOI 10.1083/jcb.200103146
   Seibenhener ML, 2012, JOVE-J VIS EXP, DOI 10.3791/3634
   Shaffer SM, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0075120
   Shestakova EA, 2001, P NATL ACAD SCI USA, V98, P7045, DOI 10.1073/pnas.121146098
   Sibilia M, 1998, EMBO J, V17, P719, DOI 10.1093/emboj/17.3.719
   Sinnamon JR, 2012, RNA, V18, P704, DOI 10.1261/rna.030742.111
   SMIDT MP, 1995, NUCLEIC ACIDS RES, V23, P2389, DOI 10.1093/nar/23.13.2389
   Vaggi F, 2011, PLOS COMPUT BIOL, V7, DOI 10.1371/journal.pcbi.1002088
   Wagner B, 2006, EMBO J, V25, P752, DOI 10.1038/sj.emboj.7600988
   Walker TL, 2014, JOVE-J VIS EXP, DOI 10.3791/51225
   Wang D, 1999, J VIROL, V73, P7761, DOI 10.1128/JVI.73.9.7761-7768.1999
   Wang T, 2015, NUCLEIC ACIDS RES, V43, P5263, DOI 10.1093/nar/gkv439
   Wang XH, 2017, MBIO, V8, DOI 10.1128/mBio.00713-17
   Weisman-Shomer P, 2002, NUCLEIC ACIDS RES, V30, P3672, DOI 10.1093/nar/gkf506
   Weiss S, 1996, TRENDS NEUROSCI, V19, P387, DOI 10.1016/S0166-2236(96)10035-7
   Wichterle H, 1997, NEURON, V18, P779, DOI 10.1016/S0896-6273(00)80317-7
   Yabuki T, 2001, GENE, V264, P123, DOI 10.1016/S0378-1119(00)00592-8
   ZHANG GH, 1994, NATURE, V372, P809
   Zhang J, 2013, ONCOGENE, V32, P2907, DOI 10.1038/onc.2012.350
   Zhao CM, 2008, CELL, V132, P645, DOI 10.1016/j.cell.2008.01.033
   Zhou ZJ, 2014, CANCER RES, V74, P2750, DOI 10.1158/0008-5472.CAN-13-2509
NR 100
TC 8
Z9 8
U1 1
U2 4
PU COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
PI COLD SPRING HARBOR
PA 1 BUNGTOWN RD, COLD SPRING HARBOR, NY 11724 USA
SN 1355-8382
EI 1469-9001
J9 RNA
JI RNA
PD JAN
PY 2019
VL 25
IS 1
BP 45
EP 59
DI 10.1261/rna.067413.118
PG 15
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA HE5BN
UT WOS:000453385800005
PM 30314980
OA Green Published, Bronze
DA 2025-04-10
ER

PT J
AU Wali, VB
   Haskins, JW
   Gilmore-Hebert, M
   Platt, JT
   Liu, ZZ
   Stern, DF
AF Wali, Vikram B.
   Haskins, Jonathan W.
   Gilmore-Hebert, Maureen
   Platt, James T.
   Liu, Zongzhi
   Stern, David F.
TI Convergent and Divergent Cellular Responses by ErbB4 Isoforms in Mammary
   Epithelial Cells
SO MOLECULAR CANCER RESEARCH
LA English
DT Article
ID INTRACELLULAR DOMAIN; NUCLEAR-LOCALIZATION; SPLICE VARIANTS;
   GENE-EXPRESSION; GENOME BROWSER; GROWTH-FACTOR; CANCER; RECEPTOR;
   PHOSPHORYLATION; SURVIVAL
AB Associations of ErbB4 (ERBB4/HER4), the fourth member of the EGFR family, with cancer are variable, possibly as a result of structural diversity of this receptor. There are multiple structural isoforms of ERBB4 arising by alternative mRNA splicing, and a subset undergo proteolysis that releases membrane-anchored and soluble isoforms that associate with transcription factors and coregulators to modulate transcription. To compare the differential and common signaling activities of full-length (FL) and soluble intracellular isoforms of ERBB4, four JM-a isoforms (FL and soluble intracellular domain (ICD) CYT-1 and CYT-2) were expressed in isogenic MCF10A cells and their biologic activities were analyzed. Both FL and ICD CYT-2 promoted cell proliferation and invasion, and CYT-1 suppressed cell growth. Transcriptional profiling revealed several new and underexplored ERBB4-regulated transcripts, including: proteases/protease inhibitors (MMP3 and SERPINE2), the YAP/Hippo pathway (CTGF, CYR61, and SPARC), the mevalonate/cholesterol pathway (HMGCR, HMGCS1, LDLR, and DHCR7), and cytokines (IL8, CCL20, and CXCL1). Many of these transcripts were subsequently validated in a luminal breast cancer cell line that normally expresses ERBB4. Furthermore, ChIP-seq experiments identified ADAP1, APOE, SPARC, STMN1, and MXD1 as novel molecular targets of ERBB4. These findings clarify the diverse biologic activities of ERBB4 isoforms, and reveal new and divergent functions. (C) 2014 AACR.
C1 [Wali, Vikram B.; Haskins, Jonathan W.; Gilmore-Hebert, Maureen; Platt, James T.; Liu, Zongzhi; Stern, David F.] Yale Univ, Sch Med, Dept Pathol, New Haven, CT 06511 USA.
C3 Yale University
RP Wali, VB (corresponding author), Yale Univ, Sch Med, 300 George St, New Haven, CT 06511 USA.
EM vikram.wali@yale.edu
RI Liu, Zongzhi/AAE-1856-2022; Wali, Vikram/G-3567-2015
FU National Cancer Institute [R01 CA80065]; NIH [T32GM07223]
FX This work was supported by USPHS grant R01 CA80065 from the National
   Cancer Institute, and NIH training grant T32GM07223 (to J.W. Haskins).
CR Allison JG, 2011, NEUROSCI RES, V70, P155, DOI 10.1016/j.neures.2011.02.009
   Anderson SM, 2007, BREAST CANCER RES, V9, DOI 10.1186/bcr1653
   Aqeilan RI, 2005, CANCER RES, V65, P6764, DOI 10.1158/0008-5472.CAN-05-1150
   Arasada RR, 2005, J BIOL CHEM, V280, P30783, DOI 10.1074/jbc.M506057200
   Barnes NLP, 2005, CLIN CANCER RES, V11, P2163, DOI 10.1158/1078-0432.CCR-04-1633
   Battaglia S, 2010, CARCINOGENESIS, V31, P1650, DOI 10.1093/carcin/bgq086
   Citterio C, 2012, SCI SIGNAL, V5, DOI 10.1126/scisignal.2002962
   Ding L, 2008, NATURE, V455, P1069, DOI 10.1038/nature07423
   Elenius K, 1997, J BIOL CHEM, V272, P26761, DOI 10.1074/jbc.272.42.26761
   Feng SM, 2007, MOL ENDOCRINOL, V21, P1861, DOI 10.1210/me.2006-0101
   Frey MR, 2009, GASTROENTEROLOGY, V136, P217, DOI 10.1053/j.gastro.2008.09.023
   Gallo RM, 2007, GROWTH FACTORS, V25, P329, DOI 10.1080/08977190701804008
   Gilbertson R, 2001, GENE CHROMOSOME CANC, V31, P288, DOI 10.1002/gcc.1146
   Gilmore-Hebert M, 2010, MOL CANCER RES, V8, P1388, DOI 10.1158/1541-7786.MCR-10-0042
   Hilliard VC, 2011, AM J PHYSIOL-GASTR L, V301, pG338, DOI 10.1152/ajpgi.00057.2011
   Hollmén M, 2010, FUTURE ONCOL, V6, P37, DOI 10.2217/fon.09.144
   Jones FE, 1999, J CELL BIOL, V147, P77, DOI 10.1083/jcb.147.1.77
   Kaiser J, 2013, SCIENCE, V342, P1028, DOI 10.1126/science.342.6162.1028
   Kandoth C, 2013, NATURE, V502, P333, DOI 10.1038/nature12634
   Kent WJ, 2002, GENOME RES, V12, P996, DOI 10.1101/gr.229102
   Knowlden JM, 1998, ONCOGENE, V17, P1949, DOI 10.1038/sj.onc.1202107
   Komuro A, 2003, J BIOL CHEM, V278, P33334, DOI 10.1074/jbc.M305597200
   Linggi B, 2006, ONCOGENE, V25, P160, DOI 10.1038/sj.onc.1209003
   Linggi B, 2006, J BIOL CHEM, V281, P25373, DOI 10.1074/jbc.M603998200
   Määttä JA, 2006, MOL BIOL CELL, V17, P67, DOI 10.1091/mbc.E05-05-0402
   Machleidt A, 2013, BMC CANCER, V13, DOI 10.1186/1471-2407-13-437
   Meerbrey KL, 2011, P NATL ACAD SCI USA, V108, P3665, DOI 10.1073/pnas.1019736108
   Meijer IMJ, 2013, CELL SIGNAL, V25, P470, DOI 10.1016/j.cellsig.2012.11.008
   Meyer LR, 2013, NUCLEIC ACIDS RES, V41, pD64, DOI 10.1093/nar/gks1048
   Muraoka-Cook RS, 2008, MOL ENDOCRINOL, V22, P2307, DOI 10.1210/me.2008-0055
   Muraoka-Cook RS, 2006, MOL BIOL CELL, V17, P4118, DOI 10.1091/mbc.E06-02-0101
   Muraoka-Cook RS, 2009, MOL CELL BIOL, V29, P4935, DOI 10.1128/MCB.01705-08
   Naresh A, 2006, CANCER RES, V66, P6412, DOI 10.1158/0008-5472.CAN-05-2368
   Ni CY, 2001, SCIENCE, V294, P2179, DOI 10.1126/science.1065412
   O'Geen H, 2006, BIOTECHNIQUES, V41, P577, DOI 10.2144/000112268
   O'Geen H, 2010, METHODS MOL BIOL, V649, P437, DOI 10.1007/978-1-60761-753-2_27
   Omerovic J, 2007, FASEB J, V21, P2849, DOI 10.1096/fj.06-7925com
   Ontsouka EC, 2014, J MAMMARY GLAND BIOL, V19, P43, DOI 10.1007/s10911-014-9316-x
   Paatero I, 2012, J BIOL CHEM, V287, P9659, DOI 10.1074/jbc.M111.299537
   Prickett TD, 2009, NAT GENET, V41, P1127, DOI 10.1038/ng.438
   Rosenbloom KR, 2012, NUCLEIC ACIDS RES, V40, pD912, DOI 10.1093/nar/gkr1012
   Rozowsky J, 2009, NAT BIOTECHNOL, V27, P66, DOI 10.1038/nbt.1518
   Sardi SP, 2006, CELL, V127, P185, DOI 10.1016/j.cell.2006.07.037
   Sorrentino G, 2014, NAT CELL BIOL, V16, P357, DOI 10.1038/ncb2936
   Sundvall M, 2007, ONCOGENE, V26, P6905, DOI 10.1038/sj.onc.1210501
   Sundvall M, 2010, MOL BIOL CELL, V21, P4275, DOI 10.1091/mbc.E10-04-0332
   Tidcombe H, 2003, P NATL ACAD SCI USA, V100, P8281, DOI 10.1073/pnas.1436402100
   van der Meer DLM, 2010, NUCLEIC ACIDS RES, V38, P2839, DOI 10.1093/nar/gkq012
   Veikkolainen V, 2011, CELL CYCLE, V10, P2647, DOI 10.4161/cc.10.16.17194
   Williams CC, 2004, J CELL BIOL, V167, P469, DOI 10.1083/jcb.200403155
   Wong J, 2009, J BIOL CHEM, V284, P18824, DOI 10.1074/jbc.M109.013243
   Zhang H, 2009, J BIOL CHEM, V284, P13355, DOI 10.1074/jbc.M900843200
NR 52
TC 21
Z9 22
U1 0
U2 2
PU AMER ASSOC CANCER RESEARCH
PI PHILADELPHIA
PA 615 CHESTNUT ST, 17TH FLOOR, PHILADELPHIA, PA 19106-4404 USA
SN 1541-7786
EI 1557-3125
J9 MOL CANCER RES
JI Mol. Cancer Res.
PD AUG
PY 2014
VL 12
IS 8
BP 1140
EP 1155
DI 10.1158/1541-7786.MCR-13-0637
PG 16
WC Oncology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Oncology; Cell Biology
GA AO2FG
UT WOS:000341131000007
PM 24829397
OA Green Submitted, Green Accepted
DA 2025-04-10
ER

PT J
AU Koshelev, M
   Sarma, S
   Price, RE
   Wehrens, XHT
   Cooper, TA
AF Koshelev, Misha
   Sarma, Satyam
   Price, Roger E.
   Wehrens, Xander H. T.
   Cooper, Thomas A.
TI Heart-specific overexpression of CUGBP1 reproduces functional and
   molecular abnormalities of myotonic dystrophy type 1
SO HUMAN MOLECULAR GENETICS
LA English
DT Article
ID BINDING PROTEIN; CARDIAC ABNORMALITIES; GENE-EXPRESSION; TRANSGENIC
   MICE; SUDDEN-DEATH; RNA; DISEASE; INVOLVEMENT; EXPANSION; MUSCLE
AB Myotonic dystrophy type 1 (DM1) is caused by a CTG expansion within the 3'-untranslated region of the DMPK gene. The predominant mechanism of pathogenesis is a toxic gain of function of CUG repeat containing RNA transcribed from the expanded allele. The molecular mechanisms by which the RNA containing expanded repeats produce pathogenic effects include: sequestration of muscleblind-like 1 (MBNL1) protein and up-regulation of CUG binding protein 1 (CUGBP1). MBNL1 and CUGBP1 are RNA binding proteins that regulate alternative splicing transitions during development. Altered functions of these proteins in DM1 lead to misregulated splicing of their target genes, resulting in several features of the disease. The role of MBNL1 depletion in DM1 is well established through a mouse knock-out model that reproduces many disease features. Here we directly test the hypothesis that CUGBP1 up-regulation also contributes to manifestations of DM1. Using tetracycline-inducible CUGBP1 and heart-specific reverse tetracycline trans-activator transgenes, we expressed human CUGBP1 in adult mouse heart. Our results demonstrate that up-regulation of CUGBP1 is sufficient to reproduce molecular, histopathological and functional changes observed in a previously described DM1 mouse model that expresses expanded CUG RNA repeats as well as in individuals with DM1. These results strongly support a role for CUGBP1 up-regulation in DM1 pathogenesis.
C1 [Koshelev, Misha; Cooper, Thomas A.] Baylor Coll Med, Dept Pathol, Houston, TX 77030 USA.
   [Sarma, Satyam; Wehrens, Xander H. T.] Baylor Coll Med, Dept Mol Physiol & Biophys, Houston, TX 77030 USA.
   [Sarma, Satyam; Wehrens, Xander H. T.] Baylor Coll Med, Dept Med Cardiol, Houston, TX 77030 USA.
   [Cooper, Thomas A.] Baylor Coll Med, Dept Mol & Cellular Biol, Houston, TX 77030 USA.
   [Price, Roger E.] Baylor Coll Med, Ctr Comparat Med, Houston, TX 77030 USA.
C3 Baylor College of Medicine; Baylor College of Medicine; Baylor College
   of Medicine; Baylor College of Medicine; Baylor College of Medicine
RP Cooper, TA (corresponding author), Baylor Coll Med, Dept Pathol, Houston, TX 77030 USA.
EM tcooper@bcm.edu
RI Sarma, Satyam/JXW-8015-2024; Wehrens, Xander/AAQ-9574-2020
OI Wehrens, Xander/0000-0001-5044-672X; Sarma, Satyam/0000-0002-0628-4919
FU NIH [F30NS61358-01, R01AR45653, R01GM076493, R01089598, R01091947];
   Baylor Research Advocates for Student Scientists (BRASS) Program;
   Muscular Dystrophy Association; W.M. Keck Foundation Distinguished Young
   Scholars program
FX -This work was supported by NIH predoctoral NSRA fellowship
   F30NS61358-01 (M. V. K.), the Baylor Research Advocates for Student
   Scientists (BRASS) Program (M. V. K.), NIH grants R01AR45653 and
   R01GM076493 (T. A. C.), the Muscular Dystrophy Association (T. A. C.),
   NIH grants R01089598 and R01091947 (X. H. W.), the Muscular Dystrophy
   Association (X. H. W.) and the W.M. Keck Foundation Distinguished Young
   Scholars program (X. H. W.).
CR Bhakta D, 2004, AM HEART J, V147, P224, DOI 10.1016/j.ahj.2003.08.008
   Bielecka-Dabrowa Agata, 2008, Cardiol J, V15, P388
   BULLOCH RT, 1967, ARCH PATHOL, V84, P130
   Bushby K, 2003, NEUROMUSCULAR DISORD, V13, P664, DOI 10.1016/S0960-8966(02)00213-4
   Chelu MG, 2009, J CLIN INVEST, V119, P1940, DOI 10.1172/JCI37059
   Cooper TA, 2009, CELL, V136, P777, DOI 10.1016/j.cell.2009.02.011
   Cudia P, 2009, J NEUROL NEUROSUR PS, V80, P790, DOI 10.1136/jnnp.2008.162594
   Dansithong W, 2005, J BIOL CHEM, V280, P5773, DOI 10.1074/jbc.M410781200
   de Haro M, 2006, HUM MOL GENET, V15, P2138, DOI 10.1093/hmg/ddl137
   Groh WJ, 2008, NEW ENGL J MED, V358, P2688, DOI 10.1056/NEJMoa062800
   Harper P.S. Monckton., 2001, MYOTONIC DYSTROPHY, V3e
   HIROMASA S, 1988, AM HEART J, V115, P914, DOI 10.1016/0002-8703(88)90901-5
   Ho TH, 2005, HUM MOL GENET, V14, P1539, DOI 10.1093/hmg/ddi162
   Kalsotra A, 2008, P NATL ACAD SCI USA, V105, P20333, DOI 10.1073/pnas.0809045105
   Kistner A, 1996, P NATL ACAD SCI USA, V93, P10933, DOI 10.1073/pnas.93.20.10933
   Kuyumcu-Martinez NM, 2007, MOL CELL, V28, P68, DOI 10.1016/j.molcel.2007.07.027
   Ladd AN, 2001, MOL CELL BIOL, V21, P1285, DOI 10.1128/MCB.21.4.1285-1296.2001
   Lin XY, 2006, HUM MOL GENET, V15, P2087, DOI 10.1093/hmg/ddl132
   Liquori CL, 2001, SCIENCE, V293, P864, DOI 10.1126/science.1062125
   LUDATSCHER RM, 1978, J CLIN PATHOL, V31, P1057, DOI 10.1136/jcp.31.11.1057
   MCCAULEY M, J VIS EXP IN PRESS
   Miller JW, 2000, EMBO J, V19, P4439, DOI 10.1093/emboj/19.17.4439
   MOTTA J, 1979, AM J MED, V67, P467, DOI 10.1016/0002-9343(79)90795-2
   Pelargonio G, 2002, HEART, V88, P665, DOI 10.1136/heart.88.6.665
   Philips AV, 1998, SCIENCE, V280, P737, DOI 10.1126/science.280.5364.737
   Phillips MF, 1997, CARDIOVASC RES, V33, P13, DOI 10.1016/S0008-6363(96)00163-0
   Ranum LPW, 2006, ANNU REV NEUROSCI, V29, P259, DOI 10.1146/annurev.neuro.29.051605.113014
   Savkur RS, 2001, NAT GENET, V29, P40, DOI 10.1038/ng704
   Schara Ulrike, 2006, Semin Pediatr Neurol, V13, P71
   Sohal DS, 2001, CIRC RES, V89, P20, DOI 10.1161/hh1301.092687
   Timchenko NA, 2004, J BIOL CHEM, V279, P13129, DOI 10.1074/jbc.M312923200
   Timchenko NA, 2001, J BIOL CHEM, V276, P7820, DOI 10.1074/jbc.M005960200
   TOKGOZOGLU LS, 1995, JAMA-J AM MED ASSOC, V274, P813, DOI 10.1001/jama.274.10.813
   Valencik ML, 2001, TRANSGENIC RES, V10, P269, DOI 10.1023/A:1016601928465
   Wang GS, 2007, J CLIN INVEST, V117, P2802, DOI 10.1172/JCI32308
   Wheeler TM, 2007, CURR OPIN NEUROL, V20, P572, DOI 10.1097/WCO.0b013e3282ef6064
NR 36
TC 119
Z9 139
U1 0
U2 9
PU OXFORD UNIV PRESS
PI OXFORD
PA GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND
SN 0964-6906
EI 1460-2083
J9 HUM MOL GENET
JI Hum. Mol. Genet.
PD MAR 15
PY 2010
VL 19
IS 6
BP 1066
EP 1075
DI 10.1093/hmg/ddp570
PG 10
WC Biochemistry & Molecular Biology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Genetics & Heredity
GA 565BE
UT WOS:000275262500010
PM 20051426
OA Green Published, Bronze
DA 2025-04-10
ER

PT J
AU Syafruddin, SE
   Mohtar, MA
   Nazarie, WFWM
   Low, TY
AF Syafruddin, Saiful E.
   Mohtar, M. Aiman
   Wan Mohamad Nazarie, Wan Fahmi
   Low, Teck Yew
TI Two Sides of the Same Coin: The Roles of KLF6 in Physiology and
   Pathophysiology
SO BIOMOLECULES
LA English
DT Review
DE transcription factor; gene regulation; developmental process;
   inflammation; cancer; KLFs
ID TUMOR-SUPPRESSOR GENE; KRUPPEL-LIKE FACTOR-6; TRANSCRIPTION FACTOR KLF6;
   ZINC-FINGER PROTEIN; EPITHELIAL-MESENCHYMAL TRANSITION; PROMOTER-BINDING
   PROTEIN; HEPATIC STELLATE CELLS; PROSTATE-CANCER; LUNG-CANCER;
   HEPATOCELLULAR-CARCINOMA
AB The Kruppel-like factors (KLFs) family of proteins control several key biological processes that include proliferation, differentiation, metabolism, apoptosis and inflammation. Dysregulation of KLF functions have been shown to disrupt cellular homeostasis and contribute to disease development. KLF6 is a relevant example; a range of functional and expression assays suggested that the dysregulation of KLF6 contributes to the onset of cancer, inflammation-associated diseases as well as cardiovascular diseases. KLF6 expression is either suppressed or elevated depending on the disease, and this is largely due to alternative splicing events producing KLF6 isoforms with specialised functions. Hence, the aim of this review is to discuss the known aspects of KLF6 biology that covers the gene and protein architecture, gene regulation, post-translational modifications and functions of KLF6 in health and diseases. We put special emphasis on the equivocal roles of its full-length and spliced variants. We also deliberate on the therapeutic strategies of KLF6 and its associated signalling pathways. Finally, we provide compelling basic and clinical questions to enhance the knowledge and research on elucidating the roles of KLF6 in physiological and pathophysiological processes.
C1 [Syafruddin, Saiful E.; Mohtar, M. Aiman; Low, Teck Yew] Univ Kebangsaan Malaysia, UKM Med Mol Biol Inst UMBI, Kuala Lumpur 56000, Malaysia.
   [Wan Mohamad Nazarie, Wan Fahmi] Univ Malaysia Sabah, Fac Sci & Nat Resources, Biotechnol Programme, Kota Kinabalu 88400, Sabah, Malaysia.
C3 Universiti Kebangsaan Malaysia; Universiti Malaysia Sabah; Universiti
   Kebangsaan Malaysia
RP Syafruddin, SE (corresponding author), Univ Kebangsaan Malaysia, UKM Med Mol Biol Inst UMBI, Kuala Lumpur 56000, Malaysia.
EM endisy@ppukm.ukm.edu.my; m.aimanmohtar@ppukm.ukm.edu.my;
   wanfahmi@ums.edu.my; lowteckyew@ppukm.ukm.edu.my
RI Low, Teck/Q-5946-2019; Nazarie, Wan/AAM-1166-2020; Syafruddin,
   Saiful/U-9324-2019; Mohtar, M. Aiman/B-8129-2018
OI Mohtar, M. Aiman/0000-0002-9015-9802; Low, Teck Yew/0000-0001-7878-7534;
   Syafruddin, Saiful Effendi/0000-0002-9960-4888; Wan Mohamad Nazarie, Wan
   Fahmi/0000-0001-9569-3839
FU Universiti Kebangsaan Malaysia, Geran Galakan Penyelidik Muda
   [GGPM-2020-035]
FX S.E.S. was supported by the Universiti Kebangsaan Malaysia, Geran
   Galakan Penyelidik Muda, GGPM-2020-035.
CR Agell L, 2008, MODERN PATHOL, V21, P1470, DOI 10.1038/modpathol.2008.145
   Ahronian LG, 2016, ONCOGENE, V35, P4653, DOI 10.1038/onc.2016.2
   Akimov V, 2018, NAT STRUCT MOL BIOL, V25, P631, DOI 10.1038/s41594-018-0084-y
   Andreoli V, 2010, IUBMB LIFE, V62, P896, DOI 10.1002/iub.396
   Anstee QM, 2019, NAT REV GASTRO HEPAT, V16, P411, DOI 10.1038/s41575-019-0145-7
   Anzalone AV, 2019, NATURE, V576, P149, DOI 10.1038/s41586-019-1711-4
   Ao H.-D., 2017, ONCOTARGET, V8, P87174
   Banck MS, 2006, FEBS LETT, V580, P6981, DOI 10.1016/j.febslet.2006.10.077
   Bar-Shira A, 2006, PROSTATE, V66, P1052, DOI 10.1002/pros.20425
   Bates DO, 2017, PHARMACOL REV, V69, P63, DOI 10.1124/pr.115.011239
   Bechmann LP, 2013, J HEPATOL, V58, P1000, DOI 10.1016/j.jhep.2013.01.020
   Bechmann LP, 2012, HEPATOLOGY, V55, P1083, DOI 10.1002/hep.24793
   Benzeno S, 2004, CANCER RES, V64, P3885, DOI 10.1158/0008-5472.CAN-03-2818
   Bi J, 2016, MOL THER-NUCL ACIDS, V5, DOI 10.1038/mtna.2016.71
   Botella LM, 2002, BLOOD, V100, P4001, DOI 10.1182/blood.V100.12.4001
   Boyault S, 2005, HEPATOLOGY, V41, P681, DOI 10.1002/hep.20588
   Britschgi A, 2008, ONCOGENE, V27, P5706, DOI 10.1038/onc.2008.179
   Camacho-Vanegas O, 2007, INT J CANCER, V121, P1390, DOI 10.1002/ijc.22809
   Cerami E, 2012, CANCER DISCOV, V2, P401, DOI 10.1158/2159-8290.CD-12-0095
   Chen H, 2011, GASTRIC CANCER, V14, P339, DOI 10.1007/s10120-011-0049-x
   Chen SG, 2019, EUR REV MED PHARMACO, V23, P8878, DOI 10.26355/eurrev_201910_19283
   Chen WF, 2016, NATURE, V539, P112, DOI 10.1038/nature19796
   Cho H, 2016, NATURE, V539, P107, DOI 10.1038/nature19795
   Cinelli MA, 2020, MED RES REV, V40, P158, DOI 10.1002/med.21599
   D'Astolfo DS, 2008, CELL DEATH DIFFER, V15, P613, DOI 10.1038/sj.cdd.4402299
   Date D, 2014, J BIOL CHEM, V289, P10318, DOI 10.1074/jbc.M113.526749
   De Graeve F, 2003, GENE, V314, P55, DOI 10.1016/S0378-1119(03)00720-0
   de Mendoza A, 2013, P NATL ACAD SCI USA, V110, pE4858, DOI 10.1073/pnas.1311818110
   DeKelver RC, 2013, PLOS GENET, V9, DOI 10.1371/journal.pgen.1003765
   Difeo A, 2008, CANCER RES, V68, P965, DOI 10.1158/0008-5472.CAN-07-2604
   Difeo A, 2006, CLIN CANCER RES, V12, P3730, DOI 10.1158/1078-0432.CCR-06-0054
   Difeo A, 2009, CANCER RES, V69, P4733, DOI 10.1158/0008-5472.CAN-08-4282
   Dionyssiou MG, 2013, SKELET MUSCLE, V3, DOI 10.1186/2044-5040-3-7
   Dumayne C, 2020, MOL METAB, V35, DOI 10.1016/j.molmet.2020.02.001
   Eming SA, 2014, SCI TRANSL MED, V6, DOI 10.1126/scitranslmed.3009337
   Sabatino ME, 2019, FRONT CELL DEV BIOL, V7, DOI 10.3389/fcell.2019.00297
   Fischer EA, 2001, J AM SOC NEPHROL, V12, P726, DOI 10.1681/ASN.V124726
   Gallardo-Vara E, 2016, ANGIOGENESIS, V19, P155, DOI 10.1007/s10456-016-9495-8
   Gao JJ, 2013, SCI SIGNAL, V6, DOI 10.1126/scisignal.2004088
   Gao Y, 2017, CANCER RES, V77, P330, DOI 10.1158/0008-5472.CAN-16-0348
   Garrido-Martín EM, 2013, CIRC RES, V112, P113, DOI 10.1161/CIRCRESAHA.112.275586
   Gasteiger G, 2017, J INNATE IMMUN, V9, P111, DOI 10.1159/000453397
   Gehrau RC, 2010, PLOS ONE, V5, DOI 10.1371/journal.pone.0008929
   Goodman WA, 2016, MUCOSAL IMMUNOL, V9, P1250, DOI 10.1038/mi.2016.1
   Hanahan D, 2011, CELL, V144, P646, DOI 10.1016/j.cell.2011.02.013
   Hanoun N, 2010, J HEPATOL, V53, P880, DOI 10.1016/j.jhep.2010.04.038
   Hatami R, 2013, SCI TRANSL MED, V5, DOI 10.1126/scitranslmed.3004688
   He AD, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-02801-1
   He Y, 2019, FRONT PHARMACOL, V10, DOI 10.3389/fphar.2019.00361
   Holian J, 2008, AM J PHYSIOL-RENAL, V295, pF1388, DOI 10.1152/ajprenal.00055.2008
   Hornbeck PV, 2015, NUCLEIC ACIDS RES, V43, pD512, DOI 10.1093/nar/gku1267
   Horne SJ, 2018, DIABETES, V67, P2420, DOI 10.2337/db17-0958
   Hsu LS, 2017, INT J MED SCI, V14, P530, DOI 10.7150/ijms.19024
   Huang XW, 2008, J BIOL CHEM, V283, P29795, DOI 10.1074/jbc.M802515200
   Inuzuka H, 1999, BIOCHEM BIOPH RES CO, V265, P664, DOI 10.1006/bbrc.1999.1734
   Ito G, 2004, CANCER RES, V64, P3838, DOI 10.1158/0008-5472.CAN-04-0185
   Kaczynski J, 2003, GENOME BIOL, V4, DOI 10.1186/gb-2003-4-2-206
   Kim GD, 2020, FASEB J, V34, P3209, DOI 10.1096/fj.201902221R
   Kim GD, 2019, FASEB J, V33, P10902, DOI 10.1096/fj.201900867RR
   Kim GD, 2016, J BIOL CHEM, V291, P21271, DOI 10.1074/jbc.M116.738617
   Kim W, 2011, MOL CELL, V44, P325, DOI 10.1016/j.molcel.2011.08.025
   Kim Y, 1998, J BIOL CHEM, V273, P33750, DOI 10.1074/jbc.273.50.33750
   Kimmelman AC, 2004, ONCOGENE, V23, P5077, DOI 10.1038/sj.onc.1207662
   KLEVIT RE, 1991, SCIENCE, V253, P1367, DOI 10.1126/science.1896847
   Köhler B, 2004, INT J CANCER, V111, P644, DOI 10.1002/ijc.20302
   Koi C, 2017, ONCOTARGET, V8, P106429, DOI 10.18632/oncotarget.22472
   Koivisto PA, 2004, INT J CANCER, V111, P642, DOI 10.1002/ijc.20301
   Koizume S, 2015, MOL CANCER, V14, DOI 10.1186/s12943-015-0351-z
   Kojima S, 2000, BLOOD, V95, P1309
   Koritschoner NP, 1997, J BIOL CHEM, V272, P9573
   Kotas ME, 2015, CELL, V160, P816, DOI 10.1016/j.cell.2015.02.010
   Krafts KP, 2010, ORGANOGENESIS, V6, P225, DOI 10.4161/org.6.4.12555
   Kremer-Tal S, 2007, J HEPATOL, V46, P645, DOI 10.1016/j.jhep.2006.10.012
   Laitman BM, 2016, PLOS BIOL, V14, DOI 10.1371/journal.pbio.1002467
   Lalazar A, 1997, GENE, V195, P235, DOI 10.1016/S0378-1119(97)00159-5
   Lang UE, 2013, ONCOGENE, V32, P4557, DOI 10.1038/onc.2012.457
   Laub F, 2001, MECH DEVELOP, V106, P167, DOI 10.1016/S0925-4773(01)00419-1
   Lee SJ, 2006, MOL PHARMACOL, V70, P415, DOI 10.1124/mol.106.022954
   Leow CC, 2009, J BIOL CHEM, V284, P21057, DOI 10.1074/jbc.M109.001776
   Li D, 2005, J BIOL CHEM, V280, P26941, DOI 10.1074/jbc.M500463200
   Li D, 2005, CANCER RES, V65, P9216, DOI 10.1158/0008-5472.CAN-05-1040
   Li H, 2018, FRONT IMMUNOL, V9, DOI 10.3389/fimmu.2018.01175
   Lièvre A, 2005, ONCOGENE, V24, P7253, DOI 10.1038/sj.onc.1208867
   Lin Y, 2020, FASEB J, V34, P12691, DOI 10.1096/fj.202000506R
   Ma LY, 2019, BIOCHEM BIOPH RES CO, V509, P845, DOI 10.1016/j.bbrc.2019.01.030
   Mallipattu SK, 2015, J CLIN INVEST, V125, P1347, DOI 10.1172/JCI77084
   Matsumoto N, 2006, BLOOD, V107, P1357, DOI 10.1182/blood-2005-05-1916
   McConnell BB, 2010, PHYSIOL REV, V90, P1337, DOI 10.1152/physrev.00058.2009
   Mertins P, 2013, NAT METHODS, V10, P634, DOI 10.1038/nmeth.2518
   Mgbemena V, 2013, CELL IMMUNOL, V283, P1, DOI 10.1016/j.cellimm.2013.06.002
   Mgbemena V, 2012, J IMMUNOL, V189, P606, DOI 10.4049/jimmunol.1102742
   Miele L, 2008, GASTROENTEROLOGY, V135, P282, DOI 10.1053/j.gastro.2008.04.004
   Montanini L, 2004, INT J CANCER, V111, P640, DOI 10.1002/ijc.20303
   Mühlbauer KR, 2003, BRIT J CANCER, V89, P687, DOI 10.1038/sj.bjc.6601164
   Muñoz U, 2012, MOL CANCER RES, V10, P1216, DOI 10.1158/1541-7786.MCR-12-0213
   Nakamura H, 2004, INVEST OPHTH VIS SCI, V45, P4327, DOI 10.1167/iovs.04-0353
   Narla G, 2007, ONCOGENE, V26, P4428, DOI 10.1038/sj.onc.1210223
   Narla G, 2005, CANCER RES, V65, P5761, DOI 10.1158/0008-5472.CAN-05-0217
   Narla G, 2005, CANCER RES, V65, P1213, DOI 10.1158/0008-5472.CAN-04-4249
   Narla G, 2001, SCIENCE, V294, P2563, DOI 10.1126/science.1066326
   Narla G, 2008, J CLIN INVEST, V118, P2711, DOI 10.1172/JCI34780
   NUSSLEINVOLHARD C, 1980, NATURE, V287, P795, DOI 10.1038/287795a0
   Okano J, 2000, FEBS LETT, V473, P95, DOI 10.1016/S0014-5793(00)01468-X
   Pei JM, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0081109
   Penn JW, 2012, INT J BURNS TRAUMA, V2, P18
   PERKINS AC, 1995, NATURE, V375, P318
   Qi W, 2007, NEPHROL DIAL TRANSPL, V22, P3147, DOI 10.1093/ndt/gfm365
   Qi WE, 2011, INT J BIOCHEM CELL B, V43, P383, DOI 10.1016/j.biocel.2010.11.008
   Racca AC, 2011, PLOS ONE, V6, DOI 10.1371/journal.pone.0022438
   Ratziu V, 1998, P NATL ACAD SCI USA, V95, P9500, DOI 10.1073/pnas.95.16.9500
   Rees HA, 2018, NAT REV GENET, V19, P770, DOI 10.1038/s41576-018-0059-1
   Reeves HL, 2004, GASTROENTEROLOGY, V126, P1090, DOI 10.1053/j.gastro.2004.01.005
   Rubinstein M, 2004, ENDOCRINOLOGY, V145, P3769, DOI 10.1210/en.2004-0173
   Rui LY, 2014, COMPR PHYSIOL, V4, P177, DOI 10.1002/cphy.c130024
   Sangodkar J, 2009, EUR J CANCER, V45, P666, DOI 10.1016/j.ejca.2008.11.009
   Sengupta S, 2017, TRENDS CANCER, V3, P269, DOI 10.1016/j.trecan.2017.03.006
   Seppälä EH, 2007, EUR UROL, V52, P1076, DOI 10.1016/j.eururo.2006.11.019
   Sirach E, 2007, CELL DEATH DIFFER, V14, P1202, DOI 10.1038/sj.cdd.4402114
   Slavin D, 1999, BIOL REPROD, V61, P1586, DOI 10.1095/biolreprod61.6.1586
   Slavin DA, 2004, ONCOGENE, V23, P8196, DOI 10.1038/sj.onc.1208020
   Song J, 2006, J GASTROEN HEPATOL, V21, P1286, DOI 10.1111/j.1440-1746.2006.04445.x
   Spinola M, 2007, CANCER LETT, V251, P311, DOI 10.1016/j.canlet.2006.11.029
   Spitz F, 2012, NAT REV GENET, V13, P613, DOI 10.1038/nrg3207
   Stärkel P, 2003, J HEPATOL, V39, P538, DOI 10.1016/S0168-8278(03)00360-X
   Stelzl U, 2005, CELL, V122, P957, DOI 10.1016/j.cell.2005.08.029
   Sugiyama S, 2019, GENES CELLS, V24, P354, DOI 10.1111/gtc.12680
   Suzuki T, 1998, J BIOCHEM, V124, P389, DOI 10.1093/oxfordjournals.jbchem.a022124
   Syafruddin SE, 2019, NAT COMMUN, V10, DOI 10.1038/s41467-019-09116-x
   Sydor S, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-08680-w
   Tahara E, 2009, CANCER BIOL THER, V8, P801, DOI 10.4161/cbt.8.9.8186
   Tallack MR, 2010, IUBMB LIFE, V62, P886, DOI 10.1002/iub.404
   Tang ZF, 2017, NUCLEIC ACIDS RES, V45, pW98, DOI 10.1093/nar/gkx247
   Tarabishi R, 2005, KIDNEY INT, V68, P1511, DOI 10.1111/j.1523-1755.2005.00563.x
   Turner J, 1999, TRENDS BIOCHEM SCI, V24, P236, DOI 10.1016/S0968-0004(99)01406-1
   Udeshi ND, 2013, MOL CELL PROTEOMICS, V12, P825, DOI 10.1074/mcp.O112.027094
   Wang ZM, 2018, SCI REP-UK, V8, DOI 10.1038/s41598-018-31101-5
   Warke VG, 2003, J BIOL CHEM, V278, P14812, DOI 10.1074/jbc.M300787200
   Wolfe SA, 2000, ANNU REV BIOPH BIOM, V29, P183, DOI 10.1146/annurev.biophys.29.1.183
   Xue YY, 2017, DEV CELL, V42, P349, DOI 10.1016/j.devcel.2017.07.012
   Yamashita K, 2002, CANCER CELL, V2, P485, DOI 10.1016/S1535-6108(02)00215-5
   Yang YH, 2019, BIOL OPEN, V8, DOI 10.1242/bio.040121
   Yea S, 2008, GASTROENTEROLOGY, V134, P1521, DOI 10.1053/j.gastro.2008.02.015
   Yin CY, 2013, J CLIN INVEST, V123, P1902, DOI 10.1172/JCI66369
   Yu TY, 2020, INT J BIOL SCI, V16, P2340, DOI 10.7150/ijbs.46573
   Zhang B, 2018, EUR J CANCER PREV, V27, P20, DOI 10.1097/CEJ.0000000000000410
   Zhang N, 2019, J CANCER, V10, P5324, DOI 10.7150/jca.34212
   Zhang XY, 2012, TUMOR BIOL, V33, P1589, DOI 10.1007/s13277-012-0414-3
   Zhang Y, 2014, J BIOL CHEM, V289, P12876, DOI 10.1074/jbc.M113.535831
   Zhang Y, 2020, FRONT PHYSIOL, V11, DOI 10.3389/fphys.2020.00510
   Zhao XA, 2010, DEV BIOL, V344, P79, DOI 10.1016/j.ydbio.2010.04.018
   Zou XZ, 2017, PULM PHARMACOL THER, V44, P70, DOI 10.1016/j.pupt.2017.03.012
NR 151
TC 50
Z9 55
U1 3
U2 25
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
EI 2218-273X
J9 BIOMOLECULES
JI Biomolecules
PD OCT
PY 2020
VL 10
IS 10
AR 1378
DI 10.3390/biom10101378
PG 22
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA OJ6AP
UT WOS:000584042000001
PM 32998281
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Grifone, R
   Shao, M
   Saquet, A
   Shi, DL
AF Grifone, Raphaelle
   Shao, Ming
   Saquet, Audrey
   Shi, De-Li
TI RNA-Binding Protein Rbm24 as a Multifaceted Post-Transcriptional
   Regulator of Embryonic Lineage Differentiation and Cellular Homeostasis
SO CELLS
LA English
DT Review
DE RNA-binding protein; Rbm24; cell differentiation; alternative splicing;
   cytoplasmic polyadenylation; muscle; head sensory organ; lens; inner ear
ID MESSENGER-RNA; SKELETAL-MUSCLE; P53 FAMILY; CYTOPLASMIC POLYADENYLATION;
   SYSTEMATIC ANALYSIS; P63 EXPRESSION; TARGET; GENE; RECOGNITION; CELLS
AB RNA-binding proteins control the metabolism of RNAs at all stages of their lifetime. They are critically required for the post-transcriptional regulation of gene expression in a wide variety of physiological and pathological processes. Rbm24 is a highly conserved RNA-binding protein that displays strongly regionalized expression patterns and exhibits dynamic changes in subcellular localization during early development. There is increasing evidence that it acts as a multifunctional regulator to switch cell fate determination and to maintain tissue homeostasis. Dysfunction of Rbm24 disrupts cell differentiation in nearly every tissue where it is expressed, such as skeletal and cardiac muscles, and different head sensory organs, but the molecular events that are affected may vary in a tissue-specific, or even a stage-specific manner. Recent works using different animal models have uncovered multiple post-transcriptional regulatory mechanisms by which Rbm24 functions in key developmental processes. In particular, it represents a major splicing factor in muscle cell development, and plays an essential role in cytoplasmic polyadenylation during lens fiber cell terminal differentiation. Here we review the advances in understanding the implication of Rbm24 during development and disease, by focusing on its regulatory roles in physiological and pathological conditions.
C1 [Grifone, Raphaelle; Saquet, Audrey; Shi, De-Li] Sorbonne Univ, IBPS, CNRS UMR7622, Dev Biol Lab, F-75005 Paris, France.
   [Shao, Ming] Shandong Univ, Sch Life Sci, Shandong Prov Key Lab Anim Cell & Dev Biol, Qingdao 266237, Peoples R China.
C3 Centre National de la Recherche Scientifique (CNRS); CNRS - National
   Institute for Biology (INSB); Sorbonne Universite; Shandong University
RP Shi, DL (corresponding author), Sorbonne Univ, IBPS, CNRS UMR7622, Dev Biol Lab, F-75005 Paris, France.
EM raphaelle.grifone@sorbonne-universite.fr; shaoming@sdu.edu.cn;
   audrey.saquet@sorbonne-universite.fr; de-li.shi@upmc.fr
RI Shi, De-Li/AAG-1807-2021; Shao, Ming/AAZ-8099-2021
OI Shi, Deli/0000-0002-6104-9137
FU Institut de Biologie Paris-Seine (IBPS); Centre National de la Recherche
   Scientifique (CNRS); Sorbonne University; National Natural Science
   Foundation of China [31871451]
FX This work was supported by the Institut de Biologie Paris-Seine (IBPS),
   the Centre National de la Recherche Scientifique (CNRS), the Sorbonne
   University, and the National Natural Science Foundation of China (grant
   number 31871451).
CR Afroz T, 2015, METHOD ENZYMOL, V558, P235, DOI 10.1016/bs.mie.2015.01.015
   Amrane S, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms5595
   Anyanful A, 2004, J CELL BIOL, V167, P639, DOI 10.1083/jcb.200407085
   Barnum CE, 2020, HUM MOL GENET, V29, P2076, DOI 10.1093/hmg/ddaa096
   Bentaya S, 2012, DEV BIOL, V363, P362, DOI 10.1016/j.ydbio.2011.12.040
   Blanco-Sánchez B, 2017, METHOD CELL BIOL, V138, P415, DOI 10.1016/bs.mcb.2016.10.006
   Boy S, 2004, DEVELOPMENT, V131, P851, DOI 10.1242/dev.00983
   Brastrom LK, 2019, BIOMEDICINES, V7, DOI 10.3390/biomedicines7020028
   Brauch KM, 2009, J AM COLL CARDIOL, V54, P930, DOI 10.1016/j.jacc.2009.05.038
   Brinegar AE, 2016, BRAIN RES, V1647, P1, DOI 10.1016/j.brainres.2016.02.050
   Buckingham M, 2006, CURR OPIN GENET DEV, V16, P525, DOI 10.1016/j.gde.2006.08.008
   Cai TT, 2015, J NEUROSCI, V35, P5870, DOI 10.1523/JNEUROSCI.5083-14.2015
   Cao H, 2018, PROTEIN CELL, V9, P930, DOI 10.1007/s13238-018-0507-x
   Cao Q, 2017, NAT GENET, V49, P1428, DOI 10.1038/ng.3950
   Cardinali B, 2016, CELL DEATH DIS, V7, DOI 10.1038/cddis.2016.10
   Carron C, 2016, WIRES DEV BIOL, V5, P150, DOI 10.1002/wdev.217
   Castello A, 2013, TRENDS GENET, V29, P318, DOI 10.1016/j.tig.2013.01.004
   Charlesworth A, 2013, WIRES RNA, V4, P437, DOI 10.1002/wrna.1171
   Chatterjee P, 2015, MOL CELL BIOL, V35, P1043, DOI 10.1128/MCB.01439-14
   Cheng XN, 2020, J GENET GENOMICS, V47, P403, DOI 10.1016/j.jgg.2020.07.002
   Ciafrè SA, 2013, RNA BIOL, V10, P935, DOI 10.4161/rna.24641
   Conlon EG, 2017, GENE DEV, V31, P1509, DOI 10.1101/gad.304055.117
   Cvekl A, 2014, DEVELOPMENT, V141, P4432, DOI 10.1242/dev.107953
   Dash S, 2020, HUM MOL GENET, V29, P591, DOI 10.1093/hmg/ddz278
   Dash S, 2016, WIRES RNA, V7, P527, DOI 10.1002/wrna.1355
   de Groot NE, 2020, SCI REP-UK, V10, DOI 10.1038/s41598-020-64667-0
   DeSmidt AA, 2020, ANAT REC, V303, P544, DOI 10.1002/ar.24115
   Despic V, 2018, J CELL SCI, V131, DOI 10.1242/jcs.201996
   Du CX, 2016, BBA-MOL BASIS DIS, V1862, P2127, DOI 10.1016/j.bbadis.2016.08.017
   Eckmann C. R., 2010, REV RNA, V2, P348, DOI DOI 10.1002/WRNA.56
   Ehler E, 2012, CARDIOVASC RES, V94, P393, DOI 10.1093/cvr/cvs151
   Fetka I, 2000, MECH DEVELOP, V94, P283, DOI 10.1016/S0925-4773(00)00284-7
   Fochi S, 2020, GENES-BASEL, V11, DOI 10.3390/genes11040402
   Gaertner A, 2019, PROTEIN CELL, V10, P393, DOI 10.1007/s13238-018-0590-z
   Glisovic T, 2008, FEBS LETT, V582, P1977, DOI 10.1016/j.febslet.2008.03.004
   Goss DJ, 2013, WIRES RNA, V4, P167, DOI 10.1002/wrna.1151
   Green YS, 2011, DEV BIOL, V358, P240, DOI 10.1016/j.ydbio.2011.07.034
   Greiling TMS, 2010, INVEST OPHTH VIS SCI, V51, P1540, DOI 10.1167/iovs.09-4388
   Grifone R, 2018, DEV DYNAM, V247, P1160, DOI 10.1002/dvdy.24666
   Grifone R, 2014, MECH DEVELOP, V134, P1, DOI 10.1016/j.mod.2014.08.003
   Guo W, 2012, NAT MED, V18, P766, DOI 10.1038/nm.2693
   Hey TM, 2019, CIRC-HEART FAIL, V12, DOI 10.1161/CIRCHEARTFAILURE.118.005700
   Hong S, 2017, J CANCER PREV, V22, P203, DOI 10.15430/JCP.2017.22.4.203
   Hua WF, 2016, CELL DEATH DIS, V7, DOI 10.1038/cddis.2016.252
   Ito J, 2016, FEBS LETT, V590, P2262, DOI 10.1002/1873-3468.12251
   Jiang YR, 2013, 2013 ACM/IEEE INTERNATIONAL CONFERENCE ON INFORMATION PROCESSING IN SENSOR NETWORKS (IPSN), P289, DOI 10.1109/IPSN.2013.6917570
   Jin DH, 2010, GENES CELLS, V15, P1158, DOI 10.1111/j.1365-2443.2010.01446.x
   Kent M.C, 2020, CELLS, V9, P662, DOI [10.3390/cells9030662 32182827, DOI 10.3390/CELLS9030662]
   Kuroyanagi H, 2007, MOL CELL BIOL, V27, P8612, DOI 10.1128/MCB.01508-07
   Kuwasako K, 2014, NAT STRUCT MOL BIOL, V21, P778, DOI 10.1038/nsmb.2870
   Lachke SA, 2011, SCIENCE, V331, P1571, DOI 10.1126/science.1195970
   Li HY, 2010, MECH DEVELOP, V127, P281, DOI 10.1016/j.mod.2010.03.002
   Lin XY, 2006, HUM MOL GENET, V15, P2087, DOI 10.1093/hmg/ddl132
   Lin Y, 2018, INT J BIOCHEM CELL B, V94, P10, DOI 10.1016/j.biocel.2017.11.002
   Liu J, 2019, PROTEIN CELL, V10, P405, DOI 10.1007/s13238-018-0578-8
   Liu J, 2017, SCI REP-UK, V7, DOI 10.1038/srep44870
   Liu YS, 2016, CELL, V165, P535, DOI 10.1016/j.cell.2016.03.014
   Llorian M, 2011, CURR OPIN GENET DEV, V21, P380, DOI 10.1016/j.gde.2011.03.006
   Lucchesi C, 2016, TRANSL CANCER RES, V5, P676, DOI 10.21037/tcr.2016.08.30
   Lucchesi CA, 2019, CANCER RES, V79, P807, DOI 10.1158/0008-5472.CAN-18-2209
   Lukong KE, 2008, TRENDS GENET, V24, P416, DOI 10.1016/j.tig.2008.05.004
   Lush ME, 2019, ELIFE, V8, DOI 10.7554/eLife.44431
   Maragh S, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0105460
   Maragh S, 2011, BMC DEV BIOL, V11, DOI 10.1186/1471-213X-11-62
   Mendez R, 2001, NAT REV MOL CELL BIO, V2, P521, DOI 10.1038/35080081
   Miller RA, 2008, PLOS ONE, V3, DOI 10.1371/journal.pone.0002176
   Mishima Y, 2012, P NATL ACAD SCI USA, V109, P1104, DOI 10.1073/pnas.1113350109
   Miyamoto S, 2009, GENES CELLS, V14, P1241, DOI 10.1111/j.1365-2443.2009.01347.x
   Morita H, 2018, INT HEART J, V59, P6, DOI 10.1536/ihj.17-519
   Morris AR, 2010, WIRES SYST BIOL MED, V2, P162, DOI 10.1002/wsbm.54
   Müller-McNicoll M, 2019, J MOL CELL BIOL, V11, P930, DOI 10.1093/jmcb/mjz043
   Nicholson AL, 2019, TRENDS CELL BIOL, V29, P191, DOI 10.1016/j.tcb.2018.11.002
   Nicolson T, 2017, J NEUROGENET, V31, P102, DOI 10.1080/01677063.2017.1342246
   Nikonova E, 2019, INT J BIOCHEM CELL B, V110, P29, DOI 10.1016/j.biocel.2019.02.008
   Ohe K, 2017, RNA, V23, P1393, DOI 10.1261/rna.059428.116
   Ohno G, 2012, PLOS GENET, V8, DOI 10.1371/journal.pgen.1002991
   Pereira B, 2017, TRENDS CANCER, V3, P506, DOI 10.1016/j.trecan.2017.05.003
   Poon KL, 2012, CARDIOVASC RES, V94, P418, DOI 10.1093/cvr/cvs095
   Qian KY, 2020, BIOCHEM J, V477, P161, DOI 10.1042/BCJ20190652
   Ray D, 2009, NAT BIOTECHNOL, V27, P667, DOI 10.1038/nbt.1550
   Relaix F, 2005, NATURE, V435, P948, DOI 10.1038/nature03594
   Reyes JM, 2016, WIRES RNA, V7, P71, DOI 10.1002/wrna.1316
   Schultz CW, 2020, WIRES RNA, V11, DOI 10.1002/wrna.1581
   Shao M, 2020, P NATL ACAD SCI USA, V117, P7245, DOI 10.1073/pnas.1917922117
   Shotwell CR, 2020, WIRES RNA, V11, DOI 10.1002/wrna.1573
   Shu LM, 2006, GENE DEV, V20, P2961, DOI 10.1101/gad.1463306
   Shum EY, 2015, NUCLEIC ACIDS RES, V43, P9314, DOI 10.1093/nar/gkv324
   Slaugenhaupt SA, 2002, CURR OPIN GENET DEV, V12, P307, DOI 10.1016/S0959-437X(02)00303-9
   Sokpor G, 2018, MOL NEUROBIOL, V55, P8306, DOI 10.1007/s12035-018-0987-y
   Souopgui J, 2008, GENE DEV, V22, P2347, DOI 10.1101/gad.479808
   Sun WQ, 2016, COMP BIOCHEM PHYS B, V198, P27, DOI 10.1016/j.cbpb.2016.03.008
   Upadhyay SK, 2016, BIOMOL NMR ASSIGN, V10, P237, DOI 10.1007/s12104-016-9674-y
   Vacchi-Suzzi C, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0052442
   van den Hoogenhof MMG, 2018, SCI REP-UK, V8, DOI 10.1038/s41598-018-29552-x
   Villalba A, 2011, CURR OPIN GENET DEV, V21, P452, DOI 10.1016/j.gde.2011.04.006
   Vogel C, 2012, NAT REV GENET, V13, P227, DOI 10.1038/nrg3185
   Ware JS, 2018, NAT REV CARDIOL, V15, P241, DOI 10.1038/nrcardio.2017.190
   Weeland CJ, 2015, J MOL CELL CARDIOL, V81, P107, DOI 10.1016/j.yjmcc.2015.02.008
   Wei PT, 2020, ONCOTARGETS THER, V13, P4523, DOI 10.2147/OTT.S246274
   Winata CL, 2018, DEVELOPMENT, V145, DOI 10.1242/dev.159566
   Xu ES, 2014, MOL CANCER RES, V12, P359, DOI 10.1158/1541-7786.MCR-13-0526
   Xu XQ, 2009, STEM CELLS, V27, P2163, DOI 10.1002/stem.166
   Yang JW, 2014, DEV CELL, V31, P87, DOI 10.1016/j.devcel.2014.08.025
   Yao YX, 2019, J VIROL, V93, DOI 10.1128/JVI.02161-18
   Yao YX, 2018, EMERG MICROBES INFEC, V7, DOI 10.1038/s41426-018-0091-4
   Zammit PS, 2017, SEMIN CELL DEV BIOL, V72, P19, DOI 10.1016/j.semcdb.2017.11.011
   Zhang J, 2011, GENE DEV, V25, P1528, DOI 10.1101/gad.2069311
   Zhang J, 2010, P NATL ACAD SCI USA, V107, P9614, DOI 10.1073/pnas.0912594107
   Zhang M, 2018, CELL DEATH DIFFER, V25, P1118, DOI 10.1038/s41418-017-0029-8
   Zhang M, 2013, GENE DEV, V27, P2246, DOI 10.1101/gad.221739.113
   Zhang T, 2016, STEM CELLS, V34, P1776, DOI 10.1002/stem.2366
   Zhang YH, 2019, J BIOL CHEM, V294, P2449, DOI 10.1074/jbc.RA118.005779
NR 112
TC 27
Z9 30
U1 0
U2 13
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
EI 2073-4409
J9 CELLS-BASEL
JI Cells
PD AUG
PY 2020
VL 9
IS 8
AR 1891
DI 10.3390/cells9081891
PG 18
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA NH6XZ
UT WOS:000564812400001
PM 32806768
OA gold, Green Submitted, Green Published
DA 2025-04-10
ER

PT J
AU Alhamoudi, KM
   Alswailem, M
   Alghamdi, B
   Alashwal, A
   Alzahrani, AS
AF Alhamoudi, Kheloud M.
   Alswailem, Meshael
   Alghamdi, Balgees
   Alashwal, Abdullah
   Alzahrani, Ali S.
TI A CYP11A1 homozygous exonic variant inducing an alternative
   splicing, frameshift and truncation in a family with congenital adrenal
   hyperplasia
SO HELIYON
LA English
DT Article
DE Congenital adrenal hyperplasia; Missense variant; Whole exome
   sequencing; Disorders of sex; development
ID CHAIN CLEAVAGE ENZYME; ACUTE REGULATORY PROTEIN; 46,XY SEX REVERSAL;
   MOLECULAR-BIOLOGY; CYP11A1; GENE; INSUFFICIENCY; MUTATIONS; DEFICIENCY;
   PATIENT
AB Background: Congenital adrenal hyperplasia (CAH) is a heterogeneous group of adrenal steroidogenesis disorders with variable degrees of glucocorticoid, mineralocorticoid and sex steroid deficiencies. CYP11A1 gene encodes the mitochondrial cholesterol side-chain cleavage enzyme (P450scc), which initiates the first reaction in steroidogenesis by converting cholesterol to pregnenolone. Variants in this gene are extremely rare but associated with severe forms of CAH due to its early and critical function in various steroid biosynthesis pathways. Here, we report a CYP11A1 exonic homozygous variant that, although exonic in location, affects splicing by creating an additional aberrant splicing site with frameshift and truncation of the gene. Patients and methods: The proband is a 23-year old 46,XY patient raised as a girl. She was a product of normal pregnancy for first-degree relative parents. Soon after birth, she had vomiting, dehydration, hypotension, hyponatremia and hyperkalemia. She was started on glucocorticoids and mineralocorticoids with prompt recovery. Apart from a chronic need for these medications, her neonatal and childhood history was unremarkable. She sought medical advice at age 19 years for delayed puberty with primary amenorrhea and lack of breast development. On evaluation, she had normal external female genitalia, no breast development, undescended testes and absent uterus and ovaries. Her hormonal evaluation revealed very low estrogen, testosterone, cortisol, aldosterone, 17-hydroxyprogesterone, and androstenedione levels. ACTH, LH, FSH and renin were very high consistent with primary gonadal and adrenal failure. Her parents are healthy first- degree cousins. She has three sisters, all with 46,XX karyotype. One of them is clinically and biochemically normal while the other two sisters have normal female phenotype, normal uterus and ovaries, similar hormonal profile to the proband but different karyotype (46,XX) and absence of undescended testes. gDNA was used for whole exome sequencing (WES). Sanger sequencing was performed to confirm the detected variant and its segregation with the disease. Results: WES identified a homozygous missense variant in CYP11A1 changing the second nucleotide (GCG > GTG) at position 189 in exon 3 and resulting in a change of Alanine to Valine (p. Ala189Val). This variant was confirmed by PCR and Sanger sequencing. It was found in a homozygous form in the proband and her two affected sisters and in a heterozygous form in the unaffected sister. In-silico analysis predicted this variant to create a new splicing site with frameshift and truncation of the gene transcript. This was confirmed by isolation of RNA, cDNA synthesis, gel electrophoresis and sequencing. Conclusion: We describe a family with a very rare form of CAH due to a CYP11A1 variant leading to creation of a new splice site, frameshift and premature truncation of the protein.
C1 [Alhamoudi, Kheloud M.; Alswailem, Meshael; Alghamdi, Balgees; Alzahrani, Ali S.] King Faisal Specialist Hosp & Res Ctr, Dept Mol Oncol, POB 3354, Riyadh 11211, Saudi Arabia.
   [Alhamoudi, Kheloud M.; Alzahrani, Ali S.] Alfaisal Univ, Coll Med, Riyadh, Saudi Arabia.
   [Alashwal, Abdullah] King Faisal Specialist Hosp & Res Ctr, Dept Paediat, Riyadh, Saudi Arabia.
   [Alzahrani, Ali S.] King Faisal Specialist Hosp & Res Ctr, Dept Med, Riyadh, Saudi Arabia.
C3 King Faisal Specialist Hospital & Research Center; Alfaisal University;
   King Faisal Specialist Hospital & Research Center; King Faisal
   Specialist Hospital & Research Center
RP Alzahrani, AS (corresponding author), King Faisal Specialist Hosp & Res Ctr, Dept Mol Oncol, POB 3354, Riyadh 11211, Saudi Arabia.
EM aliz@kfshrc.edu.sa
RI Alhamoudi, Kheloud/IWU-8410-2023; Alzahrani, Ali/L-3664-2017
OI Alzahrani, Ali/0000-0003-4294-3624; Alhamoudi,
   kheloud/0000-0002-2738-9154
CR Adzhubei Ivan, 2013, Curr Protoc Hum Genet, VChapter 7, DOI 10.1002/0471142905.hg0720s76
   al Kandari Hessa, 2006, J Clin Endocrinol Metab, V91, P2821, DOI 10.1210/jc.2005-2230
   Alhamoudi KM, 2022, FRONT GENET, V13, DOI 10.3389/fgene.2022.885589
   Alswailem M, 2021, J STEROID BIOCHEM, V208, DOI 10.1016/j.jsbmb.2020.105736
   Chan LF, 2016, FRONT ENDOCRINOL, V6, DOI 10.3389/fendo.2015.00113
   Choi Y, 2015, BIOINFORMATICS, V31, P2745, DOI 10.1093/bioinformatics/btv195
   CHUNG B, 1986, P NATL ACAD SCI USA, V83, P8962, DOI 10.1073/pnas.83.23.8962
   Goursaud C, 2018, FRONT ENDOCRINOL, V9, DOI 10.3389/fendo.2018.00491
   Guran T, 2016, J CLIN ENDOCR METAB, V101, P283, DOI 10.1210/jc.2015-3250
   Hiort O, 2005, J CLIN ENDOCR METAB, V90, P538, DOI 10.1210/jc.2004-1059
   Kallali W, 2020, EUR J ENDOCRINOL, V182, pK15, DOI 10.1530/EJE-19-0696
   Kara O, 2021, FETAL PEDIATR PATHOL, V40, P518, DOI 10.1080/15513815.2020.1716901
   Katsumata N, 2002, J CLIN ENDOCR METAB, V87, P3808, DOI 10.1210/jc.87.8.3808
   Kaur J, 2016, ENDOCRINOL DIAB META, DOI 10.1530/EDM-16-0059
   Kim A, 2018, HORM RES PAEDIAT, V89, P205, DOI 10.1159/000487638
   Kim CJ, 2008, J CLIN ENDOCR METAB, V93, P696, DOI 10.1210/jc.2007-2330
   Klli V, 2019, J CLIN ENDOCR METAB, V104, P269, DOI 10.1210/jc.2018-01661
   Kopanos C, 2019, BIOINFORMATICS, V35, P1978, DOI 10.1093/bioinformatics/bty897
   Lara-Velazquez M, 2017, MOL GENET GENOM MED, V5, P781, DOI 10.1002/mgg3.322
   Le BT, 2022, BMJ CASE REP, V15, DOI 10.1136/bcr-2022-250238
   LIN D, 1995, SCIENCE, V267, P1828, DOI 10.1126/science.7892608
   Maharaj A, 2019, J ENDOCR SOC, V3, P201, DOI 10.1210/js.2018-00130
   Matusik P, 2021, INT J ENV RES PUB HE, V18, DOI 10.3390/ijerph18137186
   Miller WL, 2011, ENDOCR REV, V32, P81, DOI 10.1210/er.2010-0013
   MILLER WL, 1988, ENDOCR REV, V9, P295, DOI 10.1210/edrv-9-3-295
   MOROHASHI K, 1987, J BIOCHEM, V101, P879, DOI 10.1093/oxfordjournals.jbchem.a121955
   Parajes S, 2012, EUR J ENDOCRINOL, V167, P881, DOI 10.1530/EJE-12-0450
   Parajes S, 2011, J CLIN ENDOCR METAB, V96, pE1798, DOI 10.1210/jc.2011-1277
   Rogers MF, 2018, BIOINFORMATICS, V34, P511, DOI 10.1093/bioinformatics/btx536
   Rubtsov P, 2009, J CLIN ENDOCR METAB, V94, P936, DOI 10.1210/jc.2008-1118
   Sahakitrungruang T, 2011, J CLIN ENDOCR METAB, V96, P792, DOI 10.1210/jc.2010-1828
   Schwarz JM, 2010, NAT METHODS, V7, P575, DOI 10.1038/nmeth0810-575
   Sim NL, 2012, NUCLEIC ACIDS RES, V40, pW452, DOI 10.1093/nar/gks539
   Simard J, 2000, ENDOCR RES, V26, P761, DOI 10.3109/07435800009048597
   Stocco DM, 1996, BIOCHEM PHARMACOL, V51, P197, DOI 10.1016/0006-2952(95)02093-4
   Stocco DM, 1996, ENDOCR REV, V17, P221, DOI 10.1210/er.17.3.221
   Strushkevich N, 2011, P NATL ACAD SCI USA, V108, P10139, DOI 10.1073/pnas.1019441108
   Tajima T, 2001, J CLIN ENDOCR METAB, V86, P3820, DOI 10.1210/jc.86.8.3820
   Tee MK, 2013, J CLIN ENDOCR METAB, V98, P713, DOI 10.1210/jc.2012-2828
   White PC, 2000, ENDOCR REV, V21, P245, DOI 10.1210/er.21.3.245
   WHITE PC, 1994, ENDOCR REV, V15, P421, DOI 10.1210/er.15.4.421
   YANASE T, 1991, ENDOCR REV, V12, P91, DOI 10.1210/edrv-12-1-91
NR 42
TC 1
Z9 1
U1 3
U2 4
PU CELL PRESS
PI CAMBRIDGE
PA 50 HAMPSHIRE ST, FLOOR 5, CAMBRIDGE, MA 02139 USA
EI 2405-8440
J9 HELIYON
JI Heliyon
PD AUG 15
PY 2024
VL 10
IS 15
AR e35058
DI 10.1016/j.heliyon.2024.e35058
EA JUL 2024
PG 9
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA A8J5E
UT WOS:001284945900001
PM 39157388
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Ackermann, MA
   Kontrogianni-Konstantopoulo, A
AF Ackermann, Maegen A.
   Kontrogianni-Konstantopoulo, Aikaterini
TI Myosin binding protein-C slow: a multifaceted family of proteins with a
   complex expression profile in fast and slow twitch skeletal muscles
SO FRONTIERS IN PHYSIOLOGY
LA English
DT Article
DE MYBPC1; skeletal muscle; single fiber expression
ID MYBP-C; THICK FILAMENT; A-BAND; IDENTIFICATION; SEQUENCE; ISOFORM;
   FIBERS; SOLEUS; DOMAIN
AB Myosin Binding Protein-C slow (sMyBP-C) comprises a complex family of proteins expressed in slow and fast type skeletal muscles. Similar to its fast and cardiac counterparts, sMyBP-C functions to modulate the formation of actomyosin cross-bridges, and to organize and stabilize sarcomeric A- and M-bands. The slow form of MyBP-C was originally classified as a single protein, however several variants encoded by the single MYBPC1 gene have been recently identified. Alternative splicing of the 5' and 3' ends of the MYBPC1 transcript has led to the differential expression of small unique segments interspersed between common domains. In addition, the NH2-terminus of sMyBP-C undergoes complex phosphorylation. Thus, alternative splicing and phosphorylation appear to regulate the functional activities of sMyBP-C. sMyBP-C proteins are not restricted to slow twitch muscles, but they are abundantly expressed in fast twitch muscles, too. Using bioinformatic tools, we herein perform a systematic comparison of the known human and mouse sMyBP-C variants. In addition, using single fiber westerns and antibodies to a common region of all known sMyBP-C variants, we present a detailed and comprehensive characterization of the expression profile of sMyBP-C proteins in the slow twitch soleus and the fast twitch flexor digitorum brevis (FDB) mouse muscles. Our studies demonstrate for the first time that distinct sMyBP-C variants are co-expressed in the same fiber, and that their expression profile differs among fibers. Given the differential expression of sMyBP-C variants in single fibers, it becomes apparent that each variant or combination thereof may play unique roles in the regulation of actomyosin cross-bridges formation and the stabilization of thick filaments.
C1 [Ackermann, Maegen A.; Kontrogianni-Konstantopoulo, Aikaterini] Univ Maryland, Sch Med, Dept Biochem & Mol Biol, Baltimore, MD 21201 USA.
C3 University System of Maryland; University of Maryland Baltimore
RP Kontrogianni-Konstantopoulo, A (corresponding author), Univ Maryland, Sch Med, Dept Biochem & Mol Biol, 108 N Greene St, Baltimore, MD 21201 USA.
EM akons001@umaryland.edu
OI Sadayappan, Sakthivel/0000-0003-2006-7678
FU Aikaterini Kontrogianni-Konstantopoulos from the National Institutes of
   Health [R01 AR52768]; National Institutes of Health [K99 KHL116778A]
FX Our research has been supported by grants to Aikaterini
   Kontrogianni-Konstantopoulos from the National Institutes of Health (R01
   AR52768) and to Maegen A. Ackermann from the National Institutes of
   Health (K99 KHL116778A).
CR Ackermann MA, 2013, FASEB J, V27, P3217, DOI 10.1096/fj.13-228882
   Ackermann MA, 2011, J PROTEOME RES, V10, P4547, DOI 10.1021/pr200355w
   Ackermann MA, 2010, J BIOMED BIOTECHNOL, DOI 10.1155/2010/652065
   Ackermann MA, 2009, MOL BIOL CELL, V20, P2963, DOI 10.1091/mbc.E08-12-1251
   ANDERSON JM, 1974, BIOCHEMISTRY-US, V13, P1195, DOI 10.1021/bi00703a602
   BENNETT P, 1986, J MUSCLE RES CELL M, V7, P550, DOI 10.1007/BF01753571
   Calderón JC, 2010, J PHYSIOL-LONDON, V588, P267, DOI 10.1113/jphysiol.2009.180893
   Calderón JC, 2009, J MUSCLE RES CELL M, V30, P125, DOI 10.1007/s10974-009-9181-1
   Carrier L, 1997, CIRC RES, V80, P427, DOI 10.1161/01.res.0000435859.24609.b3
   de Tombe PP, 2006, CIRC RES, V98, P1234, DOI 10.1161/01.RES.0000225873.63162.c4
   Drzymala-Celichowska H, 2012, J PHYSIOL PHARMACOL, V63, P187
   EINHEBER S, 1990, P NATL ACAD SCI USA, V87, P2157, DOI 10.1073/pnas.87.6.2157
   Gilbert R, 1996, J CELL SCI, V109, P101
   Gilbert R, 1999, J CELL SCI, V112, P69
   James J, 2011, J BIOL CHEM, V286, P9913, DOI 10.1074/jbc.R110.171801
   Liu YW, 1997, AM J PHYSIOL-CELL PH, V272, pC1919, DOI 10.1152/ajpcell.1997.272.6.C1919
   Martyn DA, 2004, J MOL CELL CARDIOL, V37, P813, DOI 10.1016/j.yjmcc.2004.07.005
   McClellan G, 2004, J MOL CELL CARDIOL, V37, P823, DOI 10.1016/j.yjmcc.2004.05.023
   Oakley CE, 2007, INT J BIOCHEM CELL B, V39, P2161, DOI 10.1016/j.biocel.2006.12.008
   OFFER G, 1973, J MOL BIOL, V74, P653, DOI 10.1016/0022-2836(73)90055-7
   Shaffer JF, 2009, J MUSCLE RES CELL M, V30, P303, DOI 10.1007/s10974-010-9207-8
   WEBER FE, 1993, EUR J BIOCHEM, V216, P661, DOI 10.1111/j.1432-1033.1993.tb18186.x
   YAMAMOTO K, 1983, J BIOL CHEM, V258, P8395
   YASUDA M, 1995, J MOL CELL CARDIOL, V27, P2275, DOI 10.1016/S0022-2828(95)91731-4
NR 24
TC 29
Z9 34
U1 0
U2 4
PU FRONTIERS RESEARCH FOUNDATION
PI LAUSANNE
PA PO BOX 110, LAUSANNE, 1015, SWITZERLAND
SN 1664-042X
J9 FRONT PHYSIOL
JI Front. Physiol.
PY 2013
VL 4
AR 391
DI 10.3389/fphys.2013.00391
PG 10
WC Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Physiology
GA AX2LA
UT WOS:000346774000380
PM 24399972
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Russo, R
   Cavaliere, F
   Varano, GP
   Milanese, M
   Adornetto, A
   Nucci, C
   Bonanno, G
   Morrone, LA
   Corasaniti, MT
   Bagetta, G
AF Russo, Rossella
   Cavaliere, Federica
   Varano, Giuseppe Pasquale
   Milanese, Marco
   Adornetto, Annagrazia
   Nucci, Carlo
   Bonanno, Giambattista
   Morrone, Luigi Antonio
   Corasaniti, Maria Tiziana
   Bagetta, Giacinto
TI Impairment of Neuronal Glutamate Uptake and Modulation of the Glutamate
   Transporter GLT-1 Induced by Retinal Ischemia
SO PLOS ONE
LA English
DT Article
ID AMYOTROPHIC-LATERAL-SCLEROSIS; GANGLION-CELL DEATH; AMINO-ACIDS;
   DIFFERENTIAL EXPRESSION; EXPERIMENTAL GLAUCOMA; INTRAOCULAR-PRESSURE;
   ELEVATED GLUTAMATE; MAMMALIAN RETINA; SPLICE VARIANT; NMDA RECEPTOR
AB Excitotoxicity has been implicated in the retinal neuronal loss in several ocular pathologies including glaucoma. Dysfunction of Excitatory Amino Acid Transporters is often a key component of the cascade leading to excitotoxic cell death. In the retina, glutamate transport is mainly operated by the glial glutamate transporter GLAST and the neuronal transporter GLT-1. In this study we evaluated the expression of GLAST and GLT-1 in a rat model of acute glaucoma based on the transient increase of intraocular pressure (IOP) and characterized by high glutamate levels during the reperfusion that follows the ischemic event associated with raised IOP. No changes were reported in GLAST expression while, at neuronal level, a reduction of glutamate uptake and of transporter reversal-mediated glutamate release was observed in isolated retinal synaptosomes. This was accompanied by modulation of GLT-1 expression leading to the reduction of the canonical 65 kDa form and upregulation of a GLT-1-related 38 kDa protein. These results support a role for neuronal transporters in glutamate accumulation observed in the retina following an ischemic event and suggest the presence of a GLT-1 neuronal new alternative splice variant, induced in response to the detrimental stimulus.
C1 [Russo, Rossella; Cavaliere, Federica; Varano, Giuseppe Pasquale; Adornetto, Annagrazia; Morrone, Luigi Antonio; Bagetta, Giacinto] Univ Calabria, Dept Pharm Hlth & Nutr Sci, Arcavacata Di Rende, Italy.
   [Morrone, Luigi Antonio; Bagetta, Giacinto] Univ Calabria, Sect Neuropharmacol Normal & Pathol Neuronal Plas, Univ Consortium Adapt Disorders & Head Pain UCHAD, Arcavacata Di Rende, Italy.
   [Milanese, Marco; Bonanno, Giambattista] Univ Genoa, Dept Pharm, Unit Pharmacol & Toxicol, Genoa, Italy.
   [Milanese, Marco; Bonanno, Giambattista] Univ Genoa, Ctr Excellence Biomed Res, Genoa, Italy.
   [Nucci, Carlo] Univ Roma Tor Vergata, Dept Expt Med & Surg, Ophthalmol Unit, Rome, Italy.
   [Corasaniti, Maria Tiziana] Magna Graecia Univ Catanzaro, Dept Hlth Sci, Catanzaro, Italy.
C3 University of Calabria; University of Calabria; University of Genoa;
   University of Genoa; University of Rome Tor Vergata; Magna Graecia
   University of Catanzaro
RP Russo, R (corresponding author), Univ Calabria, Dept Pharm Hlth & Nutr Sci, Arcavacata Di Rende, Italy.
EM rossella.russo@unical.it
RI Bagetta, Giacinto/N-9716-2018; Bonanno, Giambattista/C-5856-2008;
   Adornetto, Annagrazia/AAG-5467-2020; MILANESE, MARCO/C-4444-2013;
   CORASANITI, Maria Tiziana/N-1332-2015; Bagetta, Giacinto/E-8402-2012
OI Bonanno, Giambattista/0000-0003-3744-5786; MILANESE,
   MARCO/0000-0003-3384-0666; CORASANITI, Maria
   Tiziana/0000-0001-6472-0697; Bagetta, Giacinto/0000-0001-8540-6218;
   Adornetto, Annagrazia/0000-0003-1869-2642; Russo,
   Rossella/0000-0001-8758-6523
FU University of Calabria
FX This research was funded by the University of Calabria
   (http://www.unical.it/portale/ricerca/finanziamenti/), ex quota 60%. The
   funders had no role in study design, data collection and analysis,
   decision to publish, or preparation of the manuscript.
CR Adachi K, 1998, GRAEF ARCH CLIN EXP, V236, P766, DOI 10.1007/s004170050156
   Barnett NL, 2000, INVEST OPHTH VIS SCI, V41, P585
   Barnett NL, 2001, NEUROCHEM INT, V39, P291, DOI 10.1016/S0197-0186(01)00033-X
   Beart PM, 2007, BRIT J PHARMACOL, V150, P5, DOI 10.1038/sj.bjp.0706949
   Bringmann A, 2009, NEUROCHEM INT, V54, P143, DOI 10.1016/j.neuint.2008.10.014
   Chen WZ, 2002, J NEUROSCI, V22, P2142, DOI 10.1523/JNEUROSCI.22-06-02142.2002
   Chidlow G, 2003, BRAIN RES, V963, P298, DOI 10.1016/S0006-8993(02)04052-0
   Danbolt NC, 2001, PROG NEUROBIOL, V65, P1, DOI 10.1016/S0301-0082(00)00067-8
   Dreyer EB, 1996, ARCH OPHTHALMOL-CHIC, V114, P299, DOI 10.1001/archopht.1996.01100130295012
   DUNKLEY PR, 1988, BRAIN RES, V441, P59, DOI 10.1016/0006-8993(88)91383-2
   Fernandez DC, 2009, INVEST OPHTH VIS SCI, V50, P3922, DOI 10.1167/iovs.08-3344
   Furuya T, 2012, CURR EYE RES, V37, P170, DOI 10.3109/02713683.2011.645105
   Gillessen T, 2002, ADV EXP MED BIOL, V513, P3
   Harada T, 1998, P NATL ACAD SCI USA, V95, P4663, DOI 10.1073/pnas.95.8.4663
   Hare WA, 2004, INVEST OPHTH VIS SCI, V45, P2640, DOI 10.1167/iovs.03-0567
   Honig LS, 2000, NEUROLOGY, V55, P1082, DOI 10.1212/WNL.55.8.1082
   Iuvone PM, 2002, INVEST OPHTH VIS SCI, V43, P564
   Kowluru RA, 2011, INVEST OPHTH VIS SCI, V52, P8665, DOI 10.1167/iovs.10-6768
   Lam DMK, 1997, INVEST OPHTH VIS SCI, V38, P553
   Lee A, 2011, NEUROSCI LETT, V504, P228, DOI 10.1016/j.neulet.2011.09.029
   Li SY, 2012, OXID MED CELL LONGEV, V2012, DOI 10.1155/2012/426769
   Liu CH, 2013, BASIC CLIN PHARMACOL, V112, P19, DOI 10.1111/bcpt.12011
   LOUZADAJUNIOR P, 1992, J NEUROCHEM, V59, P358, DOI 10.1111/j.1471-4159.1992.tb08912.x
   Maragakis NJ, 2004, ANN NEUROL, V55, P469, DOI 10.1002/ana.20003
   Martin KRG, 2002, INVEST OPHTH VIS SCI, V43, P2236
   Meyer T, 1998, NEUROSCI LETT, V241, P68, DOI 10.1016/S0304-3940(97)00973-7
   Milanese M, 2011, J NEUROCHEM, V116, P1028, DOI 10.1111/j.1471-4159.2010.07155.x
   Münch C, 2002, J NEUROCHEM, V82, P594, DOI 10.1046/j.1471-4159.2002.01012.x
   Napper GA, 1999, VISUAL NEUROSCI, V16, P149, DOI 10.1017/S0952523899161108
   Naskar R, 2000, INVEST OPHTH VIS SCI, V41, P1940
   NICHOLLS D, 1990, TRENDS PHARMACOL SCI, V11, P462, DOI 10.1016/0165-6147(90)90129-V
   Nucci C, 2005, NEUROTOXICOLOGY, V26, P935, DOI 10.1016/j.neuro.2005.06.002
   Osborne NN, 2004, PROG RETIN EYE RES, V23, P91, DOI 10.1016/j.preteyeres.2003.12.001
   Park CK, 2009, EXP BRAIN RES, V197, P101, DOI 10.1007/s00221-009-1896-0
   Pow DV, 2004, DEV BRAIN RES, V153, P1, DOI 10.1016/j.devbrainres.2004.06.019
   Pow DV, 1999, CELL TISSUE RES, V297, P57, DOI 10.1007/s004410051333
   Pow DV, 2001, NEUROCHEM INT, V38, P463, DOI 10.1016/S0197-0186(00)00114-5
   Qu J, 2010, EXP EYE RES, V91, P48, DOI 10.1016/j.exer.2010.04.002
   Quigley HA, 1999, PROG RETIN EYE RES, V18, P39, DOI 10.1016/S1350-9462(98)00014-7
   RAITERI M, 1984, J PHARMACOL EXP THER, V231, P671
   Rao VLR, 2001, NEUROCHEM RES, V26, P497
   Rauen T, 2004, NEUROCHEM INT, V45, P1095, DOI 10.1016/j.neuint.2004.04.006
   RAUEN T, 1994, NEUROSCI LETT, V169, P137, DOI 10.1016/0304-3940(94)90375-1
   Rauen T, 2000, NEUROCHEM INT, V37, P179, DOI 10.1016/S0197-0186(00)00021-8
   Rauen T, 2000, AMINO ACIDS, V19, P53, DOI 10.1007/s007260070033
   Rauen T, 1996, CELL TISSUE RES, V286, P325, DOI 10.1007/s004410050702
   Rothstein JD, 1996, NEURON, V16, P675, DOI 10.1016/S0896-6273(00)80086-0
   Russo R, 2011, CELL DEATH DIS, V2, DOI 10.1038/cddis.2011.29
   Russo R, 2008, J NEUROCHEM, V107, P1347, DOI 10.1111/j.1471-4159.2008.05694.x
   Russo R, 2008, PROG BRAIN RES, V173, P583, DOI 10.1016/S0079-6123(08)01144-8
   Russo R, 2009, INT REV NEUROBIOL, V85, P407, DOI 10.1016/S0074-7742(09)85028-9
   Schmitt A, 2002, NEUROSCIENCE, V109, P45, DOI 10.1016/S0306-4522(01)00451-1
   Schuettauf F, 2007, GRAEF ARCH CLIN EXP, V245, P1157, DOI 10.1007/s00417-006-0531-z
   Scott HA, 2011, NEUROBIOL AGING, V32, DOI 10.1016/j.neurobiolaging.2010.03.008
   SILIPRANDI R, 1992, VISUAL NEUROSCI, V8, P567, DOI 10.1017/S0952523800005666
   Sucher NJ, 1997, VISION RES, V37, P3483, DOI 10.1016/S0042-6989(97)00047-3
   Sullivan RKP, 2006, INVEST OPHTH VIS SCI, V47, P3853, DOI 10.1167/iovs.06-0231
   UtsunomiyaTate N, 1997, FEBS LETT, V416, P312, DOI 10.1016/S0014-5793(97)01232-5
   Vorwerk CK, 2000, INVEST OPHTH VIS SCI, V41, P3615
   Walton HS, 2005, J NEUROCHEM, P371
   WoldeMussie E, 2002, J GLAUCOMA, V11, P474, DOI 10.1097/00061198-200212000-00003
   Yeh TH, 2005, NEUROBIOL DIS, V18, P476, DOI 10.1016/j.nbd.2004.12.011
NR 62
TC 24
Z9 27
U1 2
U2 13
PU PUBLIC LIBRARY SCIENCE
PI SAN FRANCISCO
PA 1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA
SN 1932-6203
J9 PLOS ONE
JI PLoS One
PD AUG 6
PY 2013
VL 8
IS 8
AR e69250
DI 10.1371/journal.pone.0069250
PG 10
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA 217ZG
UT WOS:000324401500008
PM 23936321
OA gold, Green Published, Green Submitted
DA 2025-04-10
ER

PT J
AU Katsumata, N
   Ohtake, M
   Hojo, T
   Ogawa, E
   Hara, T
   Sato, N
   Tanaka, T
AF Katsumata, N
   Ohtake, M
   Hojo, T
   Ogawa, E
   Hara, T
   Sato, N
   Tanaka, T
TI Compound heterozygous mutations in the cholesterol side-chain cleavage
   enzyme gene (CYP11A) cause congenital adrenal insufficiency in
   humans
SO JOURNAL OF CLINICAL ENDOCRINOLOGY & METABOLISM
LA English
DT Article
ID ACUTE REGULATORY PROTEIN; MESSENGER-RNA; HYPOPLASIA CONGENITA;
   MOLECULAR-CLONING; SEX REVERSAL; CDNA CLONING; HYPERPLASIA; DEFICIENCY;
   P450SCC; SEQUENCE
AB Cholesterol side-chain cleavage enzyme (P450sec) catalyzes the conversion of cholesterol to pregnenolone in mitochondria, which is the first step in the biosynthesis of all steroid hormones. Until now, no homozygous or compound heterozygous mutations in CYP11A have been described in humans. Here we describe novel compound heterozygous mutations in CYP11A in a patient with congenital adrenal insufficiency born to healthy parents. One mutation, a maternally inherited R353W mutation, resulted in markedly reduced P450scc activity by the single amino acid substitution, indicating that Arg(353) is a crucial amino acid residue for P450scc activity. The other mutation, a de novo A189V mutation in the paternal allele, did not affect the P450scc activity by the single amino acid substitution and turned out to be a splicing mutation, which created a novel alternative splice-donor site. It resulted in a deletion of 61 nucleotides in the open reading frame and thus partially inactivated CYP11A. These experimental data are consistent with the clinical findings indicating that the patient had partially preserved ability to synthesize adrenal steroid hormones. This is the first report of the compound heterozygote for the CYP11A mutations with congenital adrenal insufficiency and the phenotypically normal heterozygote in humans.
C1 Natl Res Inst Child Hlth & Dev, Dept Endocrinol & Metab, Setagaya Ku, Tokyo 1548567, Japan.
   Sendai City Hosp, Dept Pediat, Sendai, Miyagi 9848501, Japan.
   Watari Hosp, Dept Pediat, Fukushima 9608141, Japan.
   Tohoku Univ, Sch Med, Dept Pediat, Sendai, Miyagi 9808574, Japan.
   Nakamura Gakuen Univ, Dept Food & Nutr, Fukuoka 8140198, Japan.
C3 National Center for Child Health & Development - Japan; Tohoku
   University
RP Katsumata, N (corresponding author), Natl Res Inst Child Hlth & Dev, Dept Endocrinol & Metab, Setagaya Ku, 3-35-31 Taishido, Tokyo 1548567, Japan.
EM nkatsumata@nch.go.jp
CR Achermann JC, 1999, NAT GENET, V22, P125, DOI 10.1038/9629
   BECKMANN JS, 1993, HUM MOL GENET, V2, P2019, DOI 10.1093/hmg/2.12.2019
   Bose HS, 1996, NEW ENGL J MED, V335, P1870, DOI 10.1056/NEJM199612193352503
   CHUNG B, 1986, P NATL ACAD SCI USA, V83, P8962, DOI 10.1073/pnas.83.23.8962
   DEGENHART HJ, 1972, ACTA ENDOCRINOL-COP, V71, P512, DOI 10.1530/acta.0.0710512
   Guo WW, 1996, J CLIN ENDOCR METAB, V81, P2481, DOI 10.1210/jc.81.7.2481
   HIGUCHI R, 1988, NUCLEIC ACIDS RES, V16, P7351, DOI 10.1093/nar/16.15.7351
   Katsumata N, 1999, J CLIN ENDOCR METAB, V84, P3983, DOI 10.1210/jc.84.11.3983
   Kitanaka S, 1998, NEW ENGL J MED, V338, P653, DOI 10.1056/NEJM199803053381004
   KOIZUMI S, 1977, CLIN CHIM ACTA, V77, P512
   LIN D, 1991, J CLIN INVEST, V88, P1955, DOI 10.1172/JCI115520
   LIN D, 1995, SCIENCE, V267, P1828, DOI 10.1126/science.7892608
   Miller WL, 1998, J CLIN ENDOCR METAB, V83, P1399, DOI 10.1210/jc.83.4.1399
   MOROHASHI K, 1987, J BIOCHEM, V101, P879, DOI 10.1093/oxfordjournals.jbchem.a121955
   MOROHASHI K, 1984, P NATL ACAD SCI-BIOL, V81, P4647, DOI 10.1073/pnas.81.15.4647
   Nakae J, 1997, HUM MOL GENET, V6, P571, DOI 10.1093/hmg/6.4.571
   Nunez S, 1997, GENE, V187, P123, DOI 10.1016/S0378-1119(96)00734-2
   Okuyama E, 1996, J STEROID BIOCHEM, V57, P179, DOI 10.1016/0960-0760(95)00263-4
   OONK RB, 1989, J BIOL CHEM, V264, P21934
   PADGETT RA, 1986, ANNU REV BIOCHEM, V55, P1119, DOI 10.1146/annurev.biochem.55.1.1119
   SAKAI Y, 1994, J CLIN ENDOCR METAB, V79, P1198, DOI 10.1210/jc.79.4.1198
   Simard J, 2000, ENDOCR RES, V26, P761, DOI 10.3109/07435800009048597
   Stocco DM, 1996, ENDOCR REV, V17, P221, DOI 10.1210/er.17.3.221
   Tajima T, 2001, J CLIN ENDOCR METAB, V86, P3820, DOI 10.1210/jc.86.8.3820
   TAKAHASHI M, 1993, FEBS LETT, V319, P45, DOI 10.1016/0014-5793(93)80034-R
   White PC, 2000, ENDOCR REV, V21, P245, DOI 10.1210/er.21.3.245
   WHITE PC, 1994, ENDOCR REV, V15, P421, DOI 10.1210/er.15.4.421
   YANASE T, 1991, ENDOCR REV, V12, P91, DOI 10.1210/edrv-12-1-91
   YANG XM, 1993, ENDOCRINOLOGY, V132, P1977, DOI 10.1210/en.132.5.1977
   ZANARIA E, 1994, NATURE, V372, P635, DOI 10.1038/372635a0
NR 30
TC 77
Z9 89
U1 1
U2 1
PU ENDOCRINE SOC
PI CHEVY CHASE
PA 8401 CONNECTICUT AVE, SUITE 900, CHEVY CHASE, MD 20815-5817 USA
SN 0021-972X
J9 J CLIN ENDOCR METAB
JI J. Clin. Endocrinol. Metab.
PD AUG
PY 2002
VL 87
IS 8
BP 3808
EP 3813
DI 10.1210/jc.87.8.3808
PG 6
WC Endocrinology & Metabolism
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism
GA 581HG
UT WOS:000177285400045
PM 12161514
OA Bronze
DA 2025-04-10
ER

PT J
AU Moya-Molina, M
   Dorgau, B
   Flood, E
   Letteboer, SJF
   Lorentzen, E
   Coxhead, J
   Smith, G
   Roepman, R
   Grellscheid, SN
   Armstrong, L
   Lako, M
AF Moya-Molina, Marina
   Dorgau, Birthe
   Flood, Emily
   Letteboer, Stef J. F.
   Lorentzen, Esben
   Coxhead, Jonathan
   Smith, Graham
   Roepman, Ronald
   Nagaraja Grellscheid, Sushma
   Armstrong, Lyle
   Lako, Majlinda
TI Deciphering the impact of PROM1 alternative splicing on human
   photoreceptor development and maturation
SO CELL DEATH & DISEASE
LA English
DT Article
ID CONE-ROD DYSTROPHY; RETINITIS-PIGMENTOSA; FRAMESHIFT MUTATION; NEURAL
   PROGENITORS; MEMBRANE-PROTEIN; PROMININ-1 CD133; PLASMA-MEMBRANE;
   STEM-CELLS; CHOLESTEROL; DEGENERATION
AB Alternative splicing (AS) is a crucial mechanism contributing to proteomic diversity, which is highly regulated in tissue- and development-specific patterns. Retinal tissue exhibits one of the highest levels of AS. In particular, photoreceptors have a distinctive AS pattern involving the inclusion of microexons not found in other cell types. PROM1 whose encoded protein Prominin-1 is located in photoreceptor outer segments (OSs), undergoes exon 4 inclusion from the 12(th) post-conception week of human development through adulthood. Exon 4 skipping in PROM1 is associated with late-onset mild maculopathy, however its role in photoreceptor maturation and function is unknown. In this study retinal organoids, a valuable model system, were employed in combination with phosphorodiamidate morpholino oligos (PMOs) to assess the role of exon 4 AS in the development of human retina. Retinal organoids were treated with the PMOs for four weeks after which RT-PCR, western blotting and immunofluorescence analysis were performed to assess exon 4 exclusion and its impact on photoreceptors. The transcriptome of treated ROs was studied by bulk RNA-Seq. Our data demonstrate that 55% skipping of PROM1 exon 4 resulted in decreased Prominin-1 expression by 40%, abnormal accumulation of cones in the basal side of the retinal organoids as well as detectable cone photoreceptor cilium defects. Transcriptomic and western blot analyses revealed decreased expression of cone, inner segment and connecting cilium basal body markers, increased expression of genes associated with stress response and the ubiquitin-proteasome system, and downregulation of autophagy. Importantly, the use of retinal organoids provides a valuable platform to study AS and unravel disease mechanisms in a more physiologically relevant context, opening avenues for further research and potential therapeutic interventions. Together our data indicate that cones may be more sensitive to PROM1 exon 4 skipping and/or reduced Prominin-1 expression, corroborating the pathogenesis of late-onset mild maculopathy.
C1 [Moya-Molina, Marina; Dorgau, Birthe; Flood, Emily; Coxhead, Jonathan; Smith, Graham; Armstrong, Lyle; Lako, Majlinda] Newcastle Univ, Biosci Inst, Newcastle Upon Tyne, England.
   [Moya-Molina, Marina] Newcells Biotech, Newcastle Upon Tyne, England.
   [Letteboer, Stef J. F.; Roepman, Ronald] Radboud Univ Nijmegen, Res Inst Med Innovat, Med Ctr, Dept Human Genet, Nijmegen, Netherlands.
   [Lorentzen, Esben] Aarhus Univ, Dept Mol Biol & Genet, Aarhus, Denmark.
   [Nagaraja Grellscheid, Sushma] Univ Durham, Dept Biosci, Durham, England.
   [Nagaraja Grellscheid, Sushma] Univ Bergen, Dept Informat, Bergen, Norway.
C3 Newcastle University - UK; Radboud University Nijmegen; Aarhus
   University; Durham University; University of Bergen
RP Lako, M (corresponding author), Newcastle Univ, Biosci Inst, Newcastle Upon Tyne, England.
EM majlinda.lako@ncl.ac.uk
RI Moya Molina, MARINA/LFT-9062-2024; Armstrong, Lyle/B-7812-2013; Lako,
   Majlinda/B-6297-2013; Letteboer, Stef/P-8272-2015; Lorentzen,
   Esben/AAX-8077-2020
OI Dorgau, Birthe/0000-0003-4031-4402; Moya Molina,
   Marina/0000-0002-4787-3015; Lorentzen, Esben/0000-0001-6493-7220; Flood,
   Emily/0009-0005-3052-8089
FU Novo Nordisk UK Research Foundation; Electron Microscopy Research
   Services (Newcastle University) [861329]; European Union [BB/T004460/1,
   Y031016/1]; BBSRC UK [601, MR/R006237/1, MR/X008304/1, 226202/Z/22/Z];
   Retina UK; Wellcome Trust [226202/Z/22/Z] Funding Source: Wellcome Trust
FX The authors would like to acknowledge the Bioimaging Unit (Newcastle
   University) and the Electron Microscopy Research Services (Newcastle
   University) for their support and assistance in this work, and European
   Union's Horizon 2020 research and innovation programme Marie
   Sklodowska-Curie Innovative Training Networks (ITN) SCilS (# 861329),
   BBSRC UK (# BB/T004460/1), ERC/EPSRC (# Y031016/1) and Retina UK (# 601)
   for funding this work. The human embryonic and fetal material was
   provided by the Joint MRC / Wellcome (MR/R006237/1, MR/X008304/1, and
   226202/Z/22/Z) Human Developmental Biology Resource
   (https://www.hdbr.org/).
CR Barrio R, 2020, Proteostasis and Disease From Basic Mechanisms to Clinics, V1233
   Bhattacharya S, 2023, J CELL PHYSIOL, V238, P2373, DOI 10.1002/jcp.31094
   Bhattacharya S, 2017, INVEST OPHTH VIS SCI, V58, P2366, DOI 10.1167/iovs.16-21162
   Carr BJ, 2021, J CELL SCI, V134, DOI 10.1242/jcs.253906
   Cehajic-Kapetanovic J, 2019, JAMA NETW OPEN, V2, DOI 10.1001/jamanetworkopen.2019.5752
   Ciampi L, 2022, P NATL ACAD SCI USA, V119, DOI 10.1073/pnas.2117090119
   Collin J, 2016, STEM CELLS, V34, P311, DOI 10.1002/stem.2240
   Corbeil D, 2013, ADV EXP MED BIOL, V777, P1, DOI 10.1007/978-1-4614-5894-4
   Corbeil D, 2001, TRAFFIC, V2, P82, DOI 10.1034/j.1600-0854.2001.020202.x
   Corbeil D, 2010, SUBCELL BIOCHEM, V51, P399, DOI 10.1007/978-90-481-8622-8_14
   Corral-Serrano JC, 2023, CELLS-BASEL, V12, DOI 10.3390/cells12121575
   Del Pozo-Valero M, 2019, AM J OPHTHALMOL, V207, P204, DOI 10.1016/j.ajo.2019.05.014
   Dellett M, 2015, INVEST OPHTH VIS SCI, V56, P164, DOI 10.1167/iovs.14-15479
   Dorgau B, 2024, ISCIENCE, V27, DOI 10.1016/j.isci.2024.109397
   Dorgau B, 2019, BIOMATERIALS, V199, P63, DOI 10.1016/j.biomaterials.2019.01.028
   Dubreuil V, 2007, J CELL BIOL, V176, P483, DOI 10.1083/jcb.200608137
   Eidinger O, 2015, MOL VIS, V21, P1295
   Evans R., 2021, bioRxiv, DOI [DOI 10.1101/2021.10.04.463034, 10.1101/2021.10.04.463034]
   Fargeas CA, 2007, TISSUE ANTIGENS, V69, P602, DOI 10.1111/j.1399-0039.2007.00825.x
   Fujinami K, 2020, AM J MED GENET C, V184, P656, DOI 10.1002/ajmg.c.31826
   Gisina A, 2023, INT J MOL SCI, V24, DOI 10.3390/ijms242417398
   Goldberg AFX, 2016, PROG RETIN EYE RES, V55, P52, DOI 10.1016/j.preteyeres.2016.05.003
   Imani S, 2018, ONCOTARGET, V9, P122, DOI 10.18632/oncotarget.22343
   Jószai J, 2020, J BIOL CHEM, V295, P6007, DOI 10.1074/jbc.RA119.011253
   Jumper J, 2021, NATURE, V596, P583, DOI 10.1038/s41586-021-03819-2
   Khan AO, 2015, OPHTHALMIC GENET, V36, P349, DOI 10.3109/13816810.2014.886266
   Lemaigre C, 2023, TRAFFIC, V24, P190, DOI 10.1111/tra.12883
   Letteboer SJF, 2008, METHODS MOL BIOL, V484, P145, DOI 10.1007/978-1-59745-398-1_10
   Liang J, 2019, GRAEF ARCH CLIN EXP, V257, P619, DOI 10.1007/s00417-018-04206-w
   Love MI, 2014, GENOME BIOL, V15, DOI 10.1186/s13059-014-0550-8
   Lu ZJ, 2019, J BIOL CHEM, V294, P13953, DOI 10.1074/jbc.RA119.008618
   Margaritescu C, 2014, J GASTROINTEST LIVER, V23, P161
   Marzesco AM, 2005, J CELL SCI, V118, P2849, DOI 10.1242/jcs.02439
   Maw MA, 2000, HUM MOL GENET, V9, P27, DOI 10.1093/hmg/9.1.27
   Mayer AK, 2016, EUR J HUM GENET, V24, P459, DOI 10.1038/ejhg.2015.144
   Melguizo-Sanchis D, 2018, CELL DEATH DIS, V9, DOI 10.1038/s41419-017-0141-1
   Mellough CB, 2019, DEVELOPMENT, V146, DOI 10.1242/dev.169474
   Michaelides M, 2010, INVEST OPHTH VIS SCI, V51, P4771, DOI 10.1167/iovs.09-4561
   Miraglia S, 1997, BLOOD, V90, P5013, DOI 10.1182/blood.V90.12.5013.5013_5013_5021
   Murphy D, 2016, PLOS GENET, V12, DOI 10.1371/journal.pgen.1006256
   Patro R, 2017, NAT METHODS, V14, P417, DOI 10.1038/nmeth.4197
   Permanyer J, 2010, INVEST OPHTH VIS SCI, V51, P2656, DOI 10.1167/iovs.09-4857
   Pras E, 2009, MOL VIS, V15, P1709
   Renard HF, 2020, NAT COMMUN, V11, DOI 10.1038/s41467-020-15303-y
   Shmelkov SV, 2005, INT J BIOCHEM CELL B, V37, P715, DOI 10.1016/j.biocel.2004.08.010
   Thamm K, 2019, TRAFFIC, V20, P39, DOI 10.1111/tra.12618
   Toulis V., 2020, Proteostasis and Disease From Basic Mechanisms to Clinics
   Weigmann A, 1997, P NATL ACAD SCI USA, V94, P12425, DOI 10.1073/pnas.94.23.12425
   Weisschuh N, 2021, PROG RETIN EYE RES, V80, DOI 10.1016/j.preteyeres.2020.100874
   Yang ZL, 2008, J CLIN INVEST, V118, P2908, DOI 10.1172/JCI35891
   Zacchigna S, 2009, J NEUROSCI, V29, P2297, DOI 10.1523/JNEUROSCI.2034-08.2009
   Zhang QJ, 2007, HUM GENET, V122, P293, DOI 10.1007/s00439-007-0395-2
   Zhou Yi-fei, 2019, Nature Communications, V10, DOI [10.1038/s41467-019-13698-x, 10.1038/s41467-019-12821-2]
NR 53
TC 1
Z9 1
U1 3
U2 3
PU SPRINGERNATURE
PI LONDON
PA CAMPUS, 4 CRINAN ST, LONDON, N1 9XW, ENGLAND
SN 2041-4889
J9 CELL DEATH DIS
JI Cell Death Dis.
PD OCT 1
PY 2024
VL 15
IS 10
AR 721
DI 10.1038/s41419-024-07105-7
PG 17
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA H9S8P
UT WOS:001326767100003
PM 39353897
OA gold
DA 2025-04-10
ER

PT J
AU Christie, AE
   Rivera, CD
   Call, CM
   Dickinson, PS
   Stemmler, EA
   Hull, JJ
AF Christie, Andrew E.
   Rivera, Cindy D.
   Call, Catherine M.
   Dickinson, Patsy S.
   Stemmler, Elizabeth A.
   Hull, J. Joe
TI Multiple transcriptome mining coupled with tissue specific molecular
   cloning and mass spectrometry provide insights into agatoxin-like
   peptide conservation in decapod crustaceans
SO GENERAL AND COMPARATIVE ENDOCRINOLOGY
LA English
DT Article
DE In silico transcriptome mining; RT-PCR; Mass spectrometry; Nervous
   system; Testis; Hepatopancreas
AB Over the past decade, in silico genome and transcriptome mining has led to the identification of many new crustacean peptide families, including the agatoxin-like peptides (ALPs), a group named for their structural similarity to agatoxin, a spider venom component. Here, analysis of publicly accessible transcriptomes was used to expand our understanding of crustacean ALPs. Specifically, transcriptome mining was used to investigate the phylogenetic/structural conservation, tissue localization, and putative functions of ALPs in decapod species. Transcripts encoding putative ALP precursors were identified from one or more members of the Penaeoidea (penaeid shrimp), Sergestoidea (sergestid shrimps), Caridea (caridean shrimp), Astacidea (clawed lobsters and freshwater crayfish), Achelata (spiny/slipper lobsters), and Brachyura (true crabs), suggesting a broad, and perhaps ubiquitous, conservation of ALPs in decapods. Comparison of the predicted mature structures of decapod ALPs revealed high levels of amino acid conservation, including eight identically conserved cysteine residues that presumably allow for the formation of four identically positioned disulfide bridges. All decapod ALPs are predicted to have amidated carboxyl-terminals. Two isoforms of ALP appear to be present in most decapod species, one 44 amino acids long and the other 42 amino acids in length, both likely generated by alternative splicing of a single gene. In carideans, a gene or terminal exon duplication appears to have occurred, with alternative splicing producing four ALPs, two 44 and two 42 amino acid isoforms. The identification of ALP precursor-encoding transcripts in nervous system-specific transcriptomes (e.g., Homarus americanus brain, eyestalk ganglia, and cardiac ganglion assemblies, finding confirmed using RT-PCR) suggests that members of this peptide family may serve as locally-released and/or hormonally-delivered neuromodulators in decapods. Their detection in testis- and hepatopancreas-specific transcriptomes suggests that members of the ALP family may also play roles in male reproduction and innate immunity/detoxification.
C1 [Christie, Andrew E.] Univ Hawaii Manoa, Pacific Biosci Res Ctr, Sch Ocean & Earth Sci & Technol, Bekesy Lab Neurobiol, 1993 East West Rd, Honolulu, HI 96822 USA.
   [Rivera, Cindy D.; Call, Catherine M.; Stemmler, Elizabeth A.] Bowdoin Coll, Dept Chem, 6600 Coll Stn, Brunswick, ME 04011 USA.
   [Dickinson, Patsy S.] Bowdoin Coll, Dept Biol, 6500 Coll Stn, Brunswick, ME 04011 USA.
   [Hull, J. Joe] USDA ARS, Pest Management & Biocontrol Res Unit, US Arid Land Agr Res Ctr, 21881 North Cardon Lane, Maricopa, AZ 85138 USA.
C3 University of Hawaii System; University of Hawaii Manoa; Bowdoin
   College; Bowdoin College; United States Department of Agriculture (USDA)
RP Hull, JJ (corresponding author), USDA ARS, Pest Management & Biocontrol Res Unit, US Arid Land Agr Res Ctr, 21881 North Cardon Lane, Maricopa, AZ 85138 USA.
EM joe.hull@ars.usda.gov
FU National Science Foundation [IOS-1353023, IOS-1856307, IOS-1354567,
   IOS-1856433, CHE-1126657]; National Institutes of Health (INBRE)
   [8P20GM103423-12]; Cades Foundation; US Department of Agriculture
   [2020-22620-022-00D]
FX This work was supported by funds from the National Science Foundation
   (IOS-1353023 [to AEC]; IOS-1856307 [to AEC]; IOS-1354567 [to PSD];
   IOS-1856433 [to PSD and EAS]; CHE-1126657 [to EAS]), the National
   Institutes of Health (INBRE grant 8P20GM103423-12), the Cades Foundation
   (to AEC), and base CRIS funding from the US Department of Agriculture
   (Project #2020-22620-022-00D; to JJH).
CR Abascal F, 2015, PLOS COMPUT BIOL, V11, DOI 10.1371/journal.pcbi.1004325
   ADAMS ME, 1990, J BIOL CHEM, V265, P861
   Adams ME, 2004, TOXICON, V43, P509, DOI 10.1016/j.toxicon.2004.02.004
   Armstrong EK, 2019, MAR GENOM, V47, DOI 10.1016/j.margen.2019.04.002
   Bao CC, 2020, FRONT ENDOCRINOL, V11, DOI 10.3389/fendo.2020.00226
   Bao CC, 2018, GEN COMP ENDOCR, V269, P122, DOI 10.1016/j.ygcen.2018.09.002
   Bao CC, 2015, SCI REP-UK, V5, DOI 10.1038/srep17055
   Bendtsen JD, 2004, J MOL BIOL, V340, P783, DOI 10.1016/j.jmb.2004.05.028
   BINDOKAS VP, 1989, J NEUROBIOL, V20, P171, DOI 10.1002/neu.480200402
   Bouzid W, 2014, BMC GENOMICS, V15, DOI 10.1186/1471-2164-15-987
   Buckley SJ, 2016, GEN COMP ENDOCR, V228, P111, DOI 10.1016/j.ygcen.2016.02.001
   Ceroni A, 2006, NUCLEIC ACIDS RES, V34, pW177, DOI 10.1093/nar/gkl266
   Christie AE, 2020, INVERTEBR NEUROSCI, V20, DOI 10.1007/s10158-020-0235-9
   Christie AE, 2019, GEN COMP ENDOCR, V282, DOI 10.1016/j.ygcen.2019.113217
   Christie AE, 2018, INVERTEBR NEUROSCI, V18, DOI 10.1007/s10158-018-0216-4
   Christie AE, 2018, MAR GENOM, V41, P19, DOI 10.1016/j.margen.2018.07.001
   Christie AE, 2018, MAR GENOM, V40, P25, DOI 10.1016/j.margen.2018.03.002
   Christie AE, 2017, GEN COMP ENDOCR, V243, P96, DOI 10.1016/j.ygcen.2016.11.001
   Christie AE, 2016, GEN COMP ENDOCR, V230, P1, DOI 10.1016/j.ygcen.2016.03.008
   Christie AE, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0145964
   Christie AE, 2011, CELL TISSUE RES, V345, P41, DOI 10.1007/s00441-011-1183-9
   Christie AE, 2010, CELL MOL LIFE SCI, V67, P4135, DOI 10.1007/s00018-010-0482-8
   Compton PD, 2011, ANAL CHEM, V83, P6868, DOI 10.1021/ac2010795
   Dickinson PS, 2019, COMP BIOCHEM PHYS D, V30, P262, DOI 10.1016/j.cbd.2019.03.002
   Edgar RC, 2004, NUCLEIC ACIDS RES, V32, P1792, DOI 10.1093/nar/gkh340
   Ezkurdia I, 2012, MOL BIOL EVOL, V29, P2265, DOI 10.1093/molbev/mss100
   Ferrè F, 2005, NUCLEIC ACIDS RES, V33, pW230, DOI 10.1093/nar/gki412
   Havird JC, 2016, INTEGR COMP BIOL, V56, P1170, DOI 10.1093/icb/icw003
   He L, 2012, PLOS ONE, V7, DOI [10.1371/journal.pone.0033735, 10.1371/journal.pone.0045607]
   Huerlimann R, 2018, SCI REP-UK, V8, DOI 10.1038/s41598-018-31148-4
   JONES DT, 1992, COMPUT APPL BIOSCI, V8, P275, DOI 10.1093/bioinformatics/8.3.275
   Katoh K, 2013, MOL BIOL EVOL, V30, P772, DOI 10.1093/molbev/mst010
   Kearse M, 2012, BIOINFORMATICS, V28, P1647, DOI 10.1093/bioinformatics/bts199
   Kumar S, 2016, MOL BIOL EVOL, V33, P1870, DOI [10.1093/molbev/msw054, 10.1093/molbev/msv279]
   Li YD, 2015, COMP BIOCHEM PHYS D, V13, P1, DOI 10.1016/j.cbd.2014.10.002
   Liessem S, 2018, J PROTEOME RES, V17, P2192, DOI 10.1021/acs.jproteome.8b00155
   Liu ZR, 2015, SCI REP-UK, V5, DOI 10.1038/srep09454
   Lv JJ, 2017, PLOS ONE, V12, DOI 10.1371/journal.pone.0175315
   Manfrin C, 2015, GENE, V557, P28, DOI 10.1016/j.gene.2014.12.001
   Monigatti F, 2002, BIOINFORMATICS, V18, P769, DOI 10.1093/bioinformatics/18.5.769
   Northcutt AJ, 2016, BMC GENOMICS, V17, DOI 10.1186/s12864-016-3215-z
   Oliphant A, 2020, GEN COMP ENDOCR, V292, DOI 10.1016/j.ygcen.2020.113443
   Oliphant A, 2018, BMC GENOMICS, V19, DOI 10.1186/s12864-018-5057-3
   Rahi ML, 2019, GENOME BIOL EVOL, V11, P1002, DOI 10.1093/gbe/evz045
   RZHETSKY A, 1992, MOL BIOL EVOL, V9, P945
   SAITOU N, 1987, MOL BIOL EVOL, V4, P406, DOI 10.1093/oxfordjournals.molbev.a040454
   Santos CA, 2018, FRONT GENET, V9, DOI 10.3389/fgene.2018.00120
   SKINNER WS, 1989, J BIOL CHEM, V264, P2150
   Souza CA, 2018, MAR GENOM, V42, P58, DOI 10.1016/j.margen.2018.05.005
   Stemmler EA, 2013, PEPTIDES, V46, P108, DOI 10.1016/j.peptides.2013.05.008
   Sturm S, 2016, J PROTEOMICS, V132, P77, DOI 10.1016/j.jprot.2015.11.021
   Sun Y, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0095827
   Tom M, 2014, J EXP BIOL, V217, P4337, DOI 10.1242/jeb.109140
   Torres AFC, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0087556
   Tran NM, 2019, BMC GENOMICS, V20, DOI 10.1186/s12864-018-5363-9
   Nguyen TV, 2016, SCI REP-UK, V6, DOI 10.1038/srep38658
   Veenstra JA, 2000, ARCH INSECT BIOCHEM, V43, P49, DOI 10.1002/(SICI)1520-6327(200002)43:2<49::AID-ARCH1>3.0.CO;2-M
   Veenstra JA, 2016, PEERJ, V4, DOI 10.7717/peerj.2043
   Veenstra JA, 2015, GEN COMP ENDOCR, V224, P84, DOI 10.1016/j.ygcen.2015.06.013
   Ventura T, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0097323
   Verbruggen B, 2015, BMC GENOMICS, V16, DOI 10.1186/s12864-015-1667-1
   von Reumont BM, 2014, MOL BIOL EVOL, V31, P48, DOI 10.1093/molbev/mst199
   Wang ZK, 2019, GEN COMP ENDOCR, V274, P60, DOI 10.1016/j.ygcen.2019.01.002
   Xu ZQ, 2015, GENE, V569, P280, DOI 10.1016/j.gene.2015.05.075
NR 64
TC 3
Z9 3
U1 1
U2 14
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0016-6480
EI 1095-6840
J9 GEN COMP ENDOCR
JI Gen. Comp. Endocrinol.
PD DEC 1
PY 2020
VL 299
AR 113609
DI 10.1016/j.ygcen.2020.113609
PG 12
WC Endocrinology & Metabolism; Zoology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism; Zoology
GA PC2PG
UT WOS:000596848500023
PM 32916171
OA Green Accepted, Bronze
DA 2025-04-10
ER

PT J
AU Ishigaki, C
   Patria, SY
   Nishio, H
   Yoshioka, A
   Matsuo, M
AF Ishigaki, C
   Patria, SY
   Nishio, H
   Yoshioka, A
   Matsuo, M
TI Early cardiac failure in a child with Becker muscular dystrophy is due
   to an abnormally low amount of dystrophin transcript lacking exon 13
SO ACTA PAEDIATRICA JAPONICA
LA English
DT Article
DE Becker muscular-dystrophy; cardiac failure; dystrophin transcript
ID LINKED DILATED CARDIOMYOPATHY; MESSENGER-RNA; GENE DELETIONS; DUCHENNE;
   MUSCLE; PROMOTER; TISSUES; LOCUS
AB Two Japanese brothers with Becker muscular dystrophy were shown by polymerase chain reaction (PCR) and cDNA sequence analysis to produce a dystrophin gene transcript lacking a single exon; that is, number 13. Despite having the same deletion mutation, the brothers showed clearly different clinical phenotypes: the younger-brother-developed cardiac failure at the age of nine, while the elder brother was asymptomatic. As alternative splicing was not responsible for this clinical difference, the amount of dystrophin transcript was examined by using reverse transcription semi-nested and parallel PCR. The results showed that the amount of the dystrophin transcript in the younger brother was 20% of that of the elder brother. This finding suggested that lesser amount of dystrophin transcript in the younger brother was responsible for the early onset of cardiac failure. This would represent a novel molecular mechanism for dystrophinopathy.
C1 Kobe Univ, Sch Med, Int Ctr Med Res, Div Genet, Kobe, Hyogo 650, Japan.
   Kobe Univ, Sch Med, Dept Publ Hlth, Kobe, Hyogo 650, Japan.
   Nara Med Univ, Dept Pediat, Nara, Japan.
C3 Kobe University; Kobe University; Nara Medical University
RP Matsuo, M (corresponding author), Kobe Univ, Sch Med, Int Ctr Med Res, Div Genet, 7-5-1 Kusunokicho, Kobe, Hyogo 650, Japan.
CR ANAN R, 1992, AM HEART J, V123, P1088, DOI 10.1016/0002-8703(92)90732-B
   BEGGS AH, 1990, HUM GENET, V86, P45
   BOYCE FM, 1991, P NATL ACAD SCI USA, V88, P1276, DOI 10.1073/pnas.88.4.1276
   Chamberlain J., 1990, Multiplex PCR for the Diagnosis of duchenne muscular dystrophy, P272
   CHELLY J, 1990, CELL, V63, P1239, DOI 10.1016/0092-8674(90)90419-F
   CHELLY J, 1988, NATURE, V333, P858, DOI 10.1038/333858a0
   GILBERTS ECAM, 1994, P NATL ACAD SCI USA, V91, P12721, DOI 10.1073/pnas.91.26.12721
   HAGIWAR Y, 1994, AM J HUM GENET, V54, P53
   HOFFMAN EP, 1987, CELL, V51, P919, DOI 10.1016/0092-8674(87)90579-4
   Ishigaki C, 1996, NEUROLOGY, V46, P1347, DOI 10.1212/WNL.46.5.1347
   KOENIG M, 1989, AM J HUM GENET, V45, P498
   KOENIG M, 1987, CELL, V50, P509, DOI 10.1016/0092-8674(87)90504-6
   MATSUO M, 1991, J CLIN INVEST, V87, P2127, DOI 10.1172/JCI115244
   Milasin J, 1996, HUM MOL GENET, V5, P73, DOI 10.1093/hmg/5.1.73
   MUNTONI F, 1995, AM J HUM GENET, V56, P151
   MUNTONI F, 1993, NEW ENGL J MED, V329, P921, DOI 10.1056/NEJM199309233291304
   NARITA N, 1993, J CLIN INVEST, V91, P1862, DOI 10.1172/JCI116402
   ROBERTS RG, 1991, AM J HUM GENET, V49, P298
   TOWBIN JA, 1993, CIRCULATION, V87, P1854, DOI 10.1161/01.CIR.87.6.1854
   YOSHIDA K, 1993, MUSCLE NERVE, V16, P1161, DOI 10.1002/mus.880161104
NR 20
TC 6
Z9 7
U1 0
U2 0
PU BLACKWELL SCIENCE
PI CARLTON
PA 54 UNIVERSITY ST, P O BOX 378, CARLTON, VICTORIA 3053, AUSTRALIA
SN 0374-5600
J9 ACTA PAEDIATR JAPON
JI Acta Pediatr. Jpn.
PD DEC
PY 1997
VL 39
IS 6
BP 685
EP 689
PG 5
WC Pediatrics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Pediatrics
GA YQ546
UT WOS:000071398600009
PM 9447758
DA 2025-04-10
ER

PT J
AU Creemers, EE
   Sutherland, LB
   Oh, J
   Barbosa, AC
   Olson, EN
AF Creemers, Esther E.
   Sutherland, Lillian B.
   Oh, Jiyeon
   Barbosa, Ana C.
   Olson, Eric N.
TI Coactivation of MEF2 by the SAP domain proteins myocardin and MASTR
SO MOLECULAR CELL
LA English
DT Article
ID SERUM RESPONSE FACTOR; MUSCLE GENE-EXPRESSION; TRANSCRIPTION FACTOR
   MEF2C; CELL DIFFERENTIATION; REGULATORY SEQUENCES; ACTIN DYNAMICS; MICE
   LACKING; DNA-BINDING; STEM-CELLS; FAMILY
AB Myocardin is a cardiac- and smooth muscle-specific SAP domain transcription factor that functions as acoactivator for serum response factor (SRF), which controls genes involved in muscle differentiation and cell proliferation. The DNA binding domain of SRF, which interacts with myocardin, shares homology with the MEF2 transcription factor, which also controls muscle and growth-associated genes. Here we show that alternative splicing produces a cardiac-enriched isoform of myocardin containing a unique peptide sequence that confers the ability to interact with and stimulate the transcriptional activity of MEF2. This MEF2 binding motif is also contained in a previously unknown SAP domain transcription factor, referred to as MASTR, which functions as a MEF2 coactivator. This unique protein-protein interaction motif expands the regulatory potential of myocardin, and its presence in MASTR reveals a new mechanism for the control of MEF2 activity.
C1 Univ Texas, SW Med Ctr, Dept Mol Biol, Dallas, TX 75390 USA.
C3 University of Texas System; University of Texas Southwestern Medical
   Center Dallas; University of Texas Dallas
RP Olson, EN (corresponding author), Univ Texas, SW Med Ctr, Dept Mol Biol, 6000 Harry Hines Blvd, Dallas, TX 75390 USA.
EM eric.olson@utsouthwestern.edu
RI Olson, Eric/B-4391-2013
OI Olson, Eric N./0000-0003-1151-8262; Creemers, Esther/0000-0002-9001-3854
CR Aravind L, 2000, TRENDS BIOCHEM SCI, V25, P112, DOI 10.1016/S0968-0004(99)01537-6
   Black BL, 1998, ANNU REV CELL DEV BI, V14, P167, DOI 10.1146/annurev.cellbio.14.1.167
   Chen JY, 2002, J MOL CELL CARDIOL, V34, P1345, DOI 10.1006/jmcc.2002.2086
   Du KL, 2004, J BIOL CHEM, V279, P17578, DOI 10.1074/jbc.M400961200
   Du KL, 2003, MOL CELL BIOL, V23, P2425, DOI 10.1128/MCB.23.7.2425-2437.2003
   Firulli AB, 1996, CIRC RES, V78, P196, DOI 10.1161/01.RES.78.2.196
   KELLY R, 1995, J CELL BIOL, V129, P383, DOI 10.1083/jcb.129.2.383
   Kuwahara K, 2005, MOL CELL BIOL, V25, P3173, DOI 10.1128/MCB.25.8.3173-3181.2005
   Li SJ, 2003, P NATL ACAD SCI USA, V100, P9366, DOI 10.1073/pnas.1233635100
   Lin Q, 1998, DEVELOPMENT, V125, P4565
   Lin Q, 1997, SCIENCE, V276, P1404, DOI 10.1126/science.276.5317.1404
   McGrew MJ, 1996, MOL CELL BIOL, V16, P4524
   McKinsey TA, 2002, TRENDS BIOCHEM SCI, V27, P40, DOI 10.1016/S0968-0004(01)02031-X
   Messenguy F, 2003, GENE, V316, P1, DOI 10.1016/S0378-1119(03)00747-9
   Miralles F, 2003, CELL, V113, P329, DOI 10.1016/S0092-8674(03)00278-2
   Molkentin JD, 1995, CELL, V83, P1125, DOI 10.1016/0092-8674(95)90139-6
   Nakagawa O, 2005, GENE DEV, V19, P2066, DOI 10.1101/gad.1338705
   Naya FJ, 2002, NAT MED, V8, P1303, DOI 10.1038/nm789
   PHAN D, 1908, DEVELOPMENT, V132, P2669
   Pipes GCT, 2006, GENE DEV, V20, P1545, DOI 10.1101/gad.1428006
   Pipes GCT, 2005, DEV BIOL, V288, P502, DOI 10.1016/j.ydbio.2005.10.014
   Santelli E, 2000, J MOL BIOL, V297, P437, DOI 10.1006/jmbi.2000.3568
   SHORE P, 1995, EUR J BIOCHEM, V229, P1, DOI 10.1111/j.1432-1033.1995.tb20430.x
   Small EM, 2005, DEVELOPMENT, V132, P987, DOI 10.1242/dev.01684
   TAPSCOTT SJ, 1988, SCIENCE, V242, P405, DOI 10.1126/science.3175662
   TREISMAN R, 1986, CELL, V46, P567, DOI 10.1016/0092-8674(86)90882-2
   Wang DZ, 2002, P NATL ACAD SCI USA, V99, P14855, DOI 10.1073/pnas.222561499
   Wang DZ, 2001, CELL, V105, P851, DOI 10.1016/S0092-8674(01)00404-4
   Wang ZG, 2003, P NATL ACAD SCI USA, V100, P7129, DOI 10.1073/pnas.1232341100
   Wang ZG, 2004, NATURE, V428, P185, DOI 10.1038/nature02382
   Weinhold B, 2000, EMBO J, V19, P5835, DOI 10.1093/emboj/19.21.5835
   West AG, 1997, MOL CELL BIOL, V17, P2876, DOI 10.1128/MCB.17.5.2876
   Yoshida T, 2003, CIRC RES, V92, P856, DOI 10.1161/01.RES.0000068405.49081.09
NR 33
TC 93
Z9 120
U1 0
U2 9
PU CELL PRESS
PI CAMBRIDGE
PA 1100 MASSACHUSETTS AVE, CAMBRIDGE, MA 02138 USA
SN 1097-2765
J9 MOL CELL
JI Mol. Cell
PD JUL 7
PY 2006
VL 23
IS 1
BP 83
EP 96
DI 10.1016/j.molcel.2006.05.026
PG 14
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA 066FS
UT WOS:000239215700008
PM 16818234
OA Bronze
DA 2025-04-10
ER

PT J
AU Kang, SM
   Yoon, MH
   Park, BJ
AF Kang, So-mi
   Yoon, Min-Ho
   Park, Bum-Joon
TI Laminopathies; Mutations on single gene and various human genetic
   diseases
SO BMB REPORTS
LA English
DT Review
DE EDMD; HGPS; Lamin A; Laminopathy; Nuclear membrane
ID GILFORD-PROGERIA-SYNDROME; DREIFUSS MUSCULAR-DYSTROPHY; A-TYPE LAMINS;
   INTERMEDIATE-FILAMENT PROTEINS; CORONARY-ARTERY-DISEASE; MOUSE MODEL;
   DILATED CARDIOMYOPATHY; NUCLEAR LAMINA; FARNESYLTRANSFERASE INHIBITOR;
   RESTRICTIVE DERMOPATHY
AB Lamin A and its alternative splicing product Lamin C are the key intermediate filaments (IFs) of the inner nuclear membrane intermediate filament. Lamin A/C forms the inner nuclear mesh with Lamin B and works as a frame with a nuclear shape. In addition to supporting the function of nucleus, nuclear lamins perform important roles such as holding the nuclear pore complex and chromatin. However, mutations on the Lamin A or Lamin B related proteins induce various types of human genetic disorders and diseases including premature aging syndromes, muscular dystrophy, lipodystrophy and neuropathy. In this review, we briefly overview the relevance of genetic mutations of Lamin A, human disorders and laminopathies. We also discuss a mouse model for genetic diseases. Finally, we describe the current treatment for laminopathies.
C1 [Kang, So-mi; Yoon, Min-Ho; Park, Bum-Joon] Pusan Natl Univ, Coll Nat Sci, Dept Mol Biol, Busan 46241, South Korea.
C3 Pusan National University
RP Park, BJ (corresponding author), Pusan Natl Univ, Coll Nat Sci, Dept Mol Biol, Busan 46241, South Korea.
EM bjpark1219@pusan.ac.kr
RI park, bum-joon/LCD-8534-2024; Min, Hyung-Ki/AAW-5665-2021
FU Pusan National University
FX This work was supported by a 2-Year Research Grant from Pusan National
   University (2017-2019).
CR AEBI U, 1986, NATURE, V323, P560, DOI 10.1038/323560a0
   Ambrosi P, 2009, INT J CARDIOL, V137, pE75, DOI 10.1016/j.ijcard.2009.04.036
   Arimura T, 2005, HUM MOL GENET, V14, P155, DOI 10.1093/hmg/ddi017
   Barrowman J, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0032120
   Barrowman J, 2008, MOL BIOL CELL, V19, P5398, DOI 10.1091/mbc.E08-07-0704
   Ben Yaou Rabah, 2005, V264, P81
   Bonne G, 2000, ANN NEUROL, V48, P170, DOI 10.1002/1531-8249(200008)48:2<170::AID-ANA6>3.0.CO;2-J
   Briand N, 2018, NUCLEUS-PHILA, V9, P216, DOI 10.1080/19491034.2018.1449498
   Broers JLV, 2006, PHYSIOL REV, V86, P967, DOI 10.1152/physrev.00047.2005
   Canki-Klain N, 2000, CROAT MED J, V41, P389
   Capell BC, 2005, P NATL ACAD SCI USA, V102, P12879, DOI 10.1073/pnas.0506001102
   Chang W, 2013, MOL BIOL CELL, V24, P3869, DOI 10.1091/mbc.E13-06-0307
   Chen LS, 2003, LANCET, V362, P440, DOI 10.1016/S0140-6736(03)14069-X
   Choi JC, 2012, SCI TRANSL MED, V4, DOI 10.1126/scitranslmed.3003875
   Chojnowski A, 2015, CELL TISSUE RES, V360, P621, DOI 10.1007/s00441-014-2069-4
   Clements L, 2000, BIOCHEM BIOPH RES CO, V267, P709, DOI 10.1006/bbrc.1999.2023
   Coffinier C, 2010, J BIOL CHEM, V285, P20818, DOI 10.1074/jbc.M110.128835
   Constantinescu D, 2006, STEM CELLS, V24, P474, DOI 10.1634/stemcells.2006-erratum.2
   Cronshaw JA, 2002, J CELL BIOL, V158, P915, DOI 10.1083/jcb.200206106
   Dechat T, 2007, P NATL ACAD SCI USA, V104, P4955, DOI 10.1073/pnas.0700854104
   DYCK JD, 1987, J PEDIATR-US, V111, P407, DOI 10.1016/S0022-3476(87)80466-3
   EMERY AEH, 1966, J NEUROL NEUROSUR PS, V29, P338, DOI 10.1136/jnnp.29.4.338
   Eriksson M, 2003, NATURE, V423, P293, DOI 10.1038/nature01629
   Fatkin D, 1999, NEW ENGL J MED, V341, P1715, DOI 10.1056/NEJM199912023412302
   FISHER DZ, 1986, P NATL ACAD SCI USA, V83, P6450, DOI 10.1073/pnas.83.17.6450
   Fong LG, 2006, SCIENCE, V311, P1621, DOI 10.1126/science.1124875
   Fong LG, 2006, J CLIN INVEST, V116, P743, DOI 10.1172/JCI27125
   Garg A, 2009, J CLIN ENDOCR METAB, V94, P4971, DOI 10.1210/jc.2009-0472
   GILLAR PJ, 1991, PEDIATR DERMATOL, V8, P199, DOI 10.1111/j.1525-1470.1991.tb00859.x
   Gordon LB, 2016, CIRCULATION, V134, P114, DOI 10.1161/CIRCULATIONAHA.116.022188
   Gordon LB, 2012, P NATL ACAD SCI USA, V109, P16666, DOI 10.1073/pnas.1202529109
   GOTO M, 1978, J AM GERIATR SOC, V26, P341, DOI 10.1111/j.1532-5415.1978.tb03681.x
   Gruenbaum Y, 2015, ANNU REV BIOCHEM, V84, P131, DOI 10.1146/annurev-biochem-060614-034115
   Helbling-Leclerc A, 2002, EUR J HUM GENET, V10, P157, DOI 10.1038/sj.ejhg.5200744
   Heng MY, 2013, J CLIN INVEST, V123, P2719, DOI 10.1172/JCI66737
   Hisama FM, 2012, EUR J HUM GENET, V20, DOI 10.1038/ejhg.2011.265
   Hisama FM, 2011, AM J MED GENET A, V155A, P3002, DOI 10.1002/ajmg.a.34336
   HOLLSTEIN M, 1991, SCIENCE, V253, P49, DOI 10.1126/science.1905840
   Kieran MW, 2007, PEDIATRICS, V120, P834, DOI 10.1542/peds.2007-1356
   KITTEN GT, 1991, J CELL BIOL, V113, P13, DOI 10.1083/jcb.113.1.13
   Kubben N, 2011, NUCLEUS-PHILA, V2, P195, DOI 10.4161/nucl.2.3.15731
   Landires I, 2007, CLIN GENET, V71, P592, DOI 10.1111/j.1399-0004.2007.00772.x
   Lee SJ, 2016, J CLIN INVEST, V126, P3879, DOI 10.1172/JCI84164
   LIN F, 1993, J BIOL CHEM, V268, P16321
   McKenna T, 2013, GENETIC DISORDERS, P28
   McPherson E, 2009, AM J MED GENET A, V149A, P567, DOI 10.1002/ajmg.a.32627
   Melcon G, 2006, HUM MOL GENET, V15, P637, DOI 10.1093/hmg/ddi479
   Merideth MA, 2008, NEW ENGL J MED, V358, P592, DOI 10.1056/NEJMoa0706898
   MOK Q, 1990, J MED GENET, V27, P315, DOI 10.1136/jmg.27.5.315
   Mounkes LC, 2005, HUM MOL GENET, V14, P2167, DOI 10.1093/hmg/ddi221
   Mounkes LC, 2003, NATURE, V423, P298, DOI 10.1038/nature01631
   Muchir A, 2000, HUM MOL GENET, V9, P1453, DOI 10.1093/hmg/9.9.1453
   Muchir A, 2007, CURR NEUROL NEUROSCI, V7, P78, DOI 10.1007/s11910-007-0025-3
   Odgren PR, 2010, PLOS ONE, V5, DOI 10.1371/journal.pone.0009959
   Osorio FG, 2011, SCI TRANSL MED, V3, DOI 10.1126/scitranslmed.3002847
   Ozawa R, 2006, AM J PATHOL, V168, P907, DOI 10.2353/ajpath.2006.050564
   Padiath QS, 2006, NAT GENET, V38, P1114, DOI 10.1038/ng1872
   Pendás AM, 2002, NAT GENET, V31, P94, DOI 10.1038/ng871
   Pilat U, 2013, J CELL SCI, V126, P1753, DOI 10.1242/jcs.115246
   Ramos FJ, 2012, SCI TRANSL MED, V4, DOI 10.1126/scitranslmed.3003802
   ROBER RA, 1989, DEVELOPMENT, V105, P365
   Rodríguez JI, 1999, AM J MED GENET, V82, P242, DOI 10.1002/(SICI)1096-8628(19990129)82:3<242::AID-AJMG9>3.3.CO;2-5
   Salamat M, 2010, PEDIATR CARDIOL, V31, P925, DOI 10.1007/s00246-010-9711-z
   Salpingidou G, 2007, J CELL BIOL, V178, P897, DOI 10.1083/jcb.200702026
   Scaffidi P, 2006, SCIENCE, V312, P1059, DOI 10.1126/science.1127168
   Schuster J, 2011, NEUROGENETICS, V12, P65, DOI 10.1007/s10048-010-0269-y
   Shackleton S, 2000, NAT GENET, V24, P153, DOI 10.1038/72807
   Smigiel R, 2010, AM J MED GENET A, V152A, P447, DOI 10.1002/ajmg.a.33221
   Stewart CL, 2007, EXP CELL RES, V313, P2144, DOI 10.1016/j.yexcr.2007.03.026
   Sullivan T, 1999, J CELL BIOL, V147, P913, DOI 10.1083/jcb.147.5.913
   Varga R, 2006, P NATL ACAD SCI USA, V103, P3250, DOI 10.1073/pnas.0600012103
   Vergnes L, 2004, P NATL ACAD SCI USA, V101, P10428, DOI 10.1073/pnas.0401424101
   Verstraeten VLRM, 2011, P NATL ACAD SCI USA, V108, P4997, DOI 10.1073/pnas.1019532108
   Wang YX, 2006, HUM MOL GENET, V15, P2479, DOI 10.1093/hmg/ddl170
   Wojtanik KM, 2009, J LIPID RES, V50, P1068, DOI 10.1194/jlr.M800491-JLR200
   Worman HJ, 2012, J PATHOL, V226, P316, DOI 10.1002/path.2999
   Yu CE, 1996, SCIENCE, V272, P258, DOI 10.1126/science.272.5259.258
   Yuan WL, 2009, CHINESE MED J-PEKING, V122, P2840, DOI 10.3760/cma.j.issn.0366-6999.2009.23.007
   Zastrow MS, 2004, J CELL SCI, V117, P979, DOI 10.1242/jcs.01102
NR 79
TC 52
Z9 60
U1 0
U2 8
PU KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
PI SEOUL
PA KOREA SCIENCE & TECHNOLOGY CENTER, # 801,  635-4 , YEOKSAM-DONG,
   KANGNAM-KU, SEOUL, 135-703, SOUTH KOREA
SN 1976-6696
EI 1976-670X
J9 BMB REP
JI BMB Rep.
PY 2018
VL 51
IS 7
BP 327
EP 337
DI 10.5483/BMBRep.2018.51.7.113
PG 11
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA GP9AO
UT WOS:000441209400004
PM 29764566
OA Green Published, Green Submitted, gold
DA 2025-04-10
ER

PT J
AU Jam, FA
   Kadota, Y
   Mendsaikhan, A
   Tooyama, I
   Mori, M
AF Jam, Faidruz Azura
   Kadota, Yosuke
   Mendsaikhan, Anarmaa
   Tooyama, Ikuo
   Mori, Masaki
TI Identification of juvenility-associated genes in the mouse hepatocytes
   and cardiomyocytes
SO SCIENTIFIC REPORTS
LA English
DT Article
ID LEFT-VENTRICULAR MASS; SIZE-CONTROL; POSTNATAL-DEVELOPMENT;
   LIVER-REGENERATION; BRAIN MATURATION; DNA METHYLATION; DRUG CLEARANCE;
   BODY-SIZE; CHILDREN; ADULTS
AB Young individuals possess distinct properties that adults do not. The juvenile animals show higher activities for growth, healing, learning and plasticity than adults. The machinery for establishing these juvenile properties is not fully understood. To better understand the molecular constituents for the above properties, we performed a comprehensive transcriptome analysis of differently aged cells of mice by high-throughput sequencing and identified the genes selectively highly expressed in the young cells. These genes, collectively called as juvenility-associated genes (JAGs), show significant enrichments in the functions such as alternative splicing, phosphorylation and extracellular matrix (ECM). This implies the juvenescence might be achieved by these functions at the cell level. The JAG mutations are associated with progeria syndromes and growth disorders. Thus, the JAGs might organize the juvenile property of young animals and analysis of JAGs may provide scientific and therapeutic approaches toward treating the genetic diseases.
C1 [Jam, Faidruz Azura; Kadota, Yosuke; Mendsaikhan, Anarmaa; Tooyama, Ikuo; Mori, Masaki] Shiga Univ Med Sci, MNRC, Tsukinowa Cho, Otsu, Shiga 5202192, Japan.
   [Mori, Masaki] Tokyo Med & Dent Univ, Dept Syst BioMed, Bunkyo Ku, 1-5-45 Yushima, Tokyo 1138510, Japan.
C3 Shiga University of Medical Science; Institute of Science Tokyo; Tokyo
   Medical & Dental University (TMDU)
RP Mori, M (corresponding author), Shiga Univ Med Sci, MNRC, Tsukinowa Cho, Otsu, Shiga 5202192, Japan.; Mori, M (corresponding author), Tokyo Med & Dent Univ, Dept Syst BioMed, Bunkyo Ku, 1-5-45 Yushima, Tokyo 1138510, Japan.
EM morim@belle.shiga-med.ac.jp
RI Jam, faidruz/AAQ-8304-2020; MORI, MASAKI/AFU-9866-2022
OI Tooyama, Ikuo/0000-0001-8054-9666; Kadota, Yosuke/0000-0001-7335-561X;
   azura, faidruz/0000-0003-0870-8444; Mori, Masaki/0000-0001-7632-3875
FU Kanae Foundation; Miyata foundation bounty for pediatric cardiovascular
   research from Miyata Cardiac Research Promotion Foundation; Kato
   Memorial Bioscience Foundation; Meiji Yasuda Life Foundation of Health
   and Welfare; Japan Intractable Diseases (Nanbyo) Research Foundation;
   MEXT KAKENHI [15K15387]; JSPS KAKENHI [15H01486]; Leading Initiative for
   Excellent Young Researchers (LEADER) [5013323]; Central Research
   Laboratory at Shiga university of medical science (SUMS); Grants-in-Aid
   for Scientific Research [15K15387, 15H01486] Funding Source: KAKEN
FX We would like to thank all the lab members of the Molecular Neuroscience
   Research Center (MNRC) for the helpful discussion and sincere
   cooperation. M.M. is supported by the Research grant from Kanae
   Foundation and the Miyata foundation bounty for pediatric cardiovascular
   research from Miyata Cardiac Research Promotion Foundation, Kato
   Memorial Bioscience Foundation and Meiji Yasuda Life Foundation of
   Health and Welfare. This study was supported by Grants-in-Aid for
   Scientific Research for Young Scientists from the Japan Intractable
   Diseases (Nanbyo) Research Foundation. This work was supported by MEXT
   KAKENHI Grant Number 15K15387 and JSPS KAKENHI Grant Number 15H01486 and
   Leading Initiative for Excellent Young Researchers (LEADER) 5013323.
   This research was supported by the Central Research Laboratory at Shiga
   university of medical science (SUMS).
CR Ackers-Johnson M, 2016, CIRC RES, V119, P909, DOI 10.1161/CIRCRESAHA.116.309202
   Alison M, 1997, J HEPATOL, V26, P343, DOI 10.1016/S0168-8278(97)80051-7
   Apte U, 2007, AM J PHYSIOL-GASTR L, V292, pG1578, DOI 10.1152/ajpgi.00359.2006
   Attig L, 2011, ORGANOGENESIS, V7, P88, DOI 10.4161/org.7.2.14871
   BAYER SA, 1982, EXP BRAIN RES, V46, P315
   BAYER SA, 1982, SCIENCE, V216, P890, DOI 10.1126/science.7079742
   Behrens A, 2002, EMBO J, V21, P1782, DOI 10.1093/emboj/21.7.1782
   Bersell K, 2009, CELL, V138, P257, DOI 10.1016/j.cell.2009.04.060
   Bostick M, 2007, SCIENCE, V317, P1760, DOI 10.1126/science.1147939
   Cano-Gauci DF, 1999, J CELL BIOL, V146, P255
   Chiu ST, 2002, AQUACULTURE, V205, P141, DOI 10.1016/S0044-8486(01)00669-X
   Colombani J, 2003, CELL, V114, P739, DOI 10.1016/S0092-8674(03)00713-X
   Conlon I, 1999, CELL, V96, P235, DOI 10.1016/S0092-8674(00)80563-2
   CROM WR, 1991, CLIN PHARMACOL THER, V50, P132, DOI 10.1038/clpt.1991.117
   DANIELS SR, 1995, AM J CARDIOL, V76, P699, DOI 10.1016/S0002-9149(99)80200-8
   DESIMONE G, 1995, J AM COLL CARDIOL, V25, P1056, DOI 10.1016/0735-1097(94)00540-7
   DESIMONE G, 1992, J AM COLL CARDIOL, V20, P1251, DOI 10.1016/0735-1097(92)90385-Z
   DILORENZO C, 1995, J PEDIATR-US, V127, P593, DOI 10.1016/S0022-3476(95)70120-6
   Doetsch F, 1999, CELL, V97, P703, DOI 10.1016/S0092-8674(00)80783-7
   Dong JX, 2007, CELL, V130, P1120, DOI 10.1016/j.cell.2007.07.019
   Ellis MD, 2007, EXP BRAIN RES, V176, P594, DOI 10.1007/s00221-006-0637-x
   Fair DA, 2008, P NATL ACAD SCI USA, V105, P4028, DOI 10.1073/pnas.0800376105
   Fluhr JW, 2000, PEDIATR DERMATOL, V17, P436, DOI 10.1046/j.1525-1470.2000.01815.x
   Hawke TJ, 2001, J APPL PHYSIOL, V91, P534, DOI 10.1152/jappl.2001.91.2.534
   HEIMANN G, 1980, EUR J CLIN PHARMACOL, V18, P43, DOI 10.1007/BF00561477
   HENNING SJ, 1981, AM J PHYSIOL, V241, pG199, DOI 10.1152/ajpgi.1981.241.3.G199
   Huang S, 1999, NAT CELL BIOL, V1, pE131, DOI 10.1038/13043
   Huang WD, 2006, SCIENCE, V312, P233, DOI 10.1126/science.1121435
   Jia DS, 2014, HEPATOLOGY, V60, P1686, DOI 10.1002/hep.27243
   Johnson TN, 2003, TOXICOLOGY, V192, P37, DOI 10.1016/S0300-483X(03)00249-X
   Kearns GL, 2003, NEW ENGL J MED, V349, P1157, DOI 10.1056/NEJMra035092
   Klassen TP, 2008, PLOS MED, V5, P1180, DOI 10.1371/journal.pmed.0050172
   KLOTZ U, 1975, J CLIN INVEST, V55, P347, DOI 10.1172/JCI107938
   Kushnerenko E, 2002, NEUROREPORT, V13, P1843, DOI 10.1097/00001756-200210280-00002
   Lacroix D, 1997, EUR J BIOCHEM, V247, P625, DOI 10.1111/j.1432-1033.1997.00625.x
   LI E, 1992, CELL, V69, P915, DOI 10.1016/0092-8674(92)90611-F
   Licht DJ, 2009, J THORAC CARDIOV SUR, V137, P529, DOI 10.1016/j.jtcvs.2008.10.025
   Lobo MK, 2006, NAT NEUROSCI, V9, P443, DOI 10.1038/nn1654
   Lopaschuk GD, 2010, J CARDIOVASC PHARM, V56, P130, DOI 10.1097/FJC.0b013e3181e74a14
   Meier JJ, 2008, DIABETES, V57, P1584, DOI 10.2337/db07-1369
   Michalopoulos GK, 1997, SCIENCE, V276, P60, DOI 10.1126/science.276.5309.60
   Mollova M, 2013, P NATL ACAD SCI USA, V110, P1446, DOI 10.1073/pnas.1214608110
   Mootha VK, 2003, NAT GENET, V34, P267, DOI 10.1038/ng1180
   MURRY DJ, 1995, DRUG METAB DISPOS, V23, P1110
   Nishiyama A, 2013, NATURE, V502, P249, DOI 10.1038/nature12488
   Ooi SKT, 2010, EPIGENET CHROMATIN, V3, DOI 10.1186/1756-8935-3-17
   Penzo-Méndez AI, 2015, CSH PERSPECT BIOL, V7, DOI 10.1101/cshperspect.a019240
   Pilia G, 1996, NAT GENET, V12, P241, DOI 10.1038/ng0396-241
   Raz N, 2005, CEREB CORTEX, V15, P1676, DOI 10.1093/cercor/bhi044
   Rebhan M, 1998, BIOINFORMATICS, V14, P656, DOI 10.1093/bioinformatics/14.8.656
   Rothbart SB, 2012, NAT STRUCT MOL BIOL, V19, P1155, DOI 10.1038/nsmb.2391
   ROWLAND TW, 1988, MED SCI SPORT EXER, V20, P474
   Safran M, 2003, NUCLEIC ACIDS RES, V31, P142, DOI 10.1093/nar/gkg050
   SCHILLERSCOTLAND CF, 1994, TOXICOL LETT, V72, P137, DOI 10.1016/0378-4274(94)90020-5
   Sharif J, 2007, NATURE, V450, P908, DOI 10.1038/nature06397
   Shioi T, 2002, MOL CELL BIOL, V22, P2799, DOI 10.1128/MCB.22.8.2799-2809.2002
   Snel B, 2000, NUCLEIC ACIDS RES, V28, P3442, DOI 10.1093/nar/28.18.3442
   Sowell ER, 1999, NAT NEUROSCI, V2, P859, DOI 10.1038/13154
   SPANGRUDE GJ, 1988, SCIENCE, V241, P58, DOI 10.1126/science.2898810
   Strassburg CP, 2002, GUT, V50, P259, DOI 10.1136/gut.50.2.259
   Su TT, 1998, CURR BIOL, V8, pR687, DOI 10.1016/S0960-9822(98)70436-1
   Subramanian A, 2005, P NATL ACAD SCI USA, V102, P15545, DOI 10.1073/pnas.0506580102
   TANNER JM, 1981, NUTR REV, V39, P43, DOI 10.1111/j.1753-4887.1981.tb06734.x
   Taub R, 2004, NAT REV MOL CELL BIO, V5, P836, DOI 10.1038/nrm1489
   TRELUYER JM, 1991, EUR J BIOCHEM, V202, P583, DOI 10.1111/j.1432-1033.1991.tb16411.x
   Treluyer JM, 1997, PHARMACOGENETICS, V7, P441, DOI 10.1097/00008571-199712000-00002
   VALCARCE C, 1988, J BIOL CHEM, V263, P7767
   Wang ET, 2008, NATURE, V456, P470, DOI 10.1038/nature07509
   Yanowitz TD, 1999, J APPL PHYSIOL, V87, P370, DOI 10.1152/jappl.1999.87.1.370
   Zhou XM, 2011, J NEUROSCI, V31, P5625, DOI 10.1523/JNEUROSCI.6470-10.2011
NR 70
TC 7
Z9 7
U1 0
U2 4
PU NATURE PORTFOLIO
PI BERLIN
PA HEIDELBERGER PLATZ 3, BERLIN, 14197, GERMANY
SN 2045-2322
J9 SCI REP-UK
JI Sci Rep
PD FEB 15
PY 2018
VL 8
AR 3132
DI 10.1038/s41598-018-21445-3
PG 12
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA FW3EX
UT WOS:000425190500036
PM 29449671
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Dube, DK
   Mclean, MD
   Dube, S
   Poiesz, BJ
AF Dube, Dipak K.
   Mclean, Matthew D.
   Dube, Syamalima
   Poiesz, Bernard J.
TI Translational Control of Tropomyosin Expression in Vertebrate Hearts
SO ANATOMICAL RECORD-ADVANCES IN INTEGRATIVE ANATOMY AND EVOLUTIONARY
   BIOLOGY
LA English
DT Article
DE tropomyosin; regulation; translation; Mexican axolotl; mouse
ID AXOLOTL AMBYSTOMA-MEXICANUM; ALPHA-TROPOMYOSIN; HYPERTROPHIC
   CARDIOMYOPATHY; CARDIAC MYOFIBRILLOGENESIS; DIFFERENTIAL EXPRESSION;
   ISOFORM DIVERSITY; EMBRYONIC HEARTS; GENE-EXPRESSION; XENOPUS EMBRYOS;
   MESSENGER-RNAS
AB The tropomyosin (TM) gene family produces a set of related TM proteins with important functions in striated and smooth muscle, and nonmuscle cells. In vertebrate striated muscle, the thin filament consists largely of actin, TM, the troponin (Tn) complex (Tn-I, Tn-C and Tn-T), and tropomodulin (Tmod) and is responsible for mediating Ca2+ control of muscle contraction and relaxation. There are four known genes (designated as TPM1, TPM2, TPM3, and TPM4) for TM in vertebrates. The four TM genes generate a multitude of tissue-and developmental-specific isoforms through the use of different promoters, alternative mRNA splicing, different 3'-end mRNA processing and tissue-specific translational control. In this review, we have focused mainly on the regulation of TM expression in striated muscles, primarily in vertebrate hearts with special emphasis on translational control using mouse and Mexican axolotl animal models. (C) 2014 Wiley Periodicals, Inc.
C1 [Dube, Dipak K.; Dube, Syamalima; Poiesz, Bernard J.] SUNY Upstate Med Univ, Dept Med, Syracuse, NY 13210 USA.
   [Dube, Dipak K.; Mclean, Matthew D.] SUNY Upstate Med Univ, Dept Cell & Dev Biol, Syracuse, NY 13210 USA.
C3 State University of New York (SUNY) System; State University of New York
   (SUNY) Upstate Medical Center; State University of New York (SUNY)
   System; State University of New York (SUNY) Upstate Medical Center
RP Dube, DK (corresponding author), SUNY Upstate Med Univ, Dept Med, Syracuse, NY 13210 USA.
EM dubed@upstate.edu
FU American Heart Association; CNY Children's Miracle Network; Golisano
   Children's Hospital; College of Health Professionals, Upstate Medical
   University; Barbara Kopp Cancer Research Fund
FX Grant sponsors: American Heart Association (both National and New York
   State affiliate), CNY Children's Miracle Network; Golisano Children's
   Hospital; College of Health Professionals, Upstate Medical University
   (DKD); Barbara Kopp Cancer Research Fund (BJP).
CR Bharadwaj S, 2002, CANCER LETT, V183, P205, DOI 10.1016/S0304-3835(02)00119-2
   Blanchard EM, 1997, CIRC RES, V81, P1005
   Bottinelli R, 1998, CIRC RES, V82, P106
   BRIERLEY I, 1993, BIOCHEM SOC T, V21, P822, DOI 10.1042/bst0210822
   BUGLER B, 1991, MOL CELL BIOL, V11, P573, DOI 10.1128/MCB.11.1.573
   Denz CR, 2011, CARDIOVASC TOXICOL, V11, P235, DOI 10.1007/s12012-011-9117-z
   Denz CR, 2004, BIOCHEM BIOPH RES CO, V320, P1291, DOI 10.1016/j.bbrc.2004.06.084
   FLEENOR DE, 1992, J MUSCLE RES CELL M, V13, P55, DOI 10.1007/BF01738428
   FORRYSCHAUDIES S, 1990, CELL GROWTH DIFFER, V1, P473
   Gaillard C, 1998, DEV GENES EVOL, V207, P435, DOI 10.1007/s004270050134
   Gebauer F, 2004, NAT REV MOL CELL BIO, V5, P827, DOI 10.1038/nrm1488
   Gunning P, 2008, PHYSIOL REV, V88, P1, DOI 10.1152/physrev.00001.2007
   Gunning P, 2008, ADV EXP MED BIOL, V644, P1
   HANN SR, 1992, GENE DEV, V6, P1229, DOI 10.1101/gad.6.7.1229
   HARDY S, 1995, GENE, V156, P265, DOI 10.1016/0378-1119(94)00929-M
   HERRERA VLM, 1990, J BIOL CHEM, V265, P9555
   Jagatheesan G, 2007, AM J PHYSIOL-HEART C, V293, pH949, DOI 10.1152/ajpheart.01341.2006
   JANSEN M, 1995, PEDIATR RES, V37, P681, DOI 10.1203/00006450-199506000-00001
   Karam CN, 2011, J MUSCLE RES CELL M, V31, P315, DOI 10.1007/s10974-010-9237-2
   KOZAK M, 1987, NUCLEIC ACIDS RES, V15, P8125, DOI 10.1093/nar/15.20.8125
   LEESMILLER JP, 1991, BIOESSAYS, V13, P429, DOI 10.1002/bies.950130902
   LEMANSKI LF, 1973, DEV BIOL, V33, P312, DOI 10.1016/0012-1606(73)90140-1
   Lemanski LF, 1996, BIOCHEM BIOPH RES CO, V229, P974, DOI 10.1006/bbrc.1996.1910
   Luque EA, 1997, GENE, V185, P175, DOI 10.1016/S0378-1119(96)00606-3
   Mathews MB, 2000, COLD SPRING HARBOR M, V39, P1
   MOHUN TJ, 1989, EMBO J, V8, P1153, DOI 10.1002/j.1460-2075.1989.tb03486.x
   Muthuchamy M, 1999, CIRC RES, V85, P47
   Muthuchamy M, 1995, J BIOL CHEM, V270, P30593, DOI 10.1074/jbc.270.51.30593
   NADALGINARD B, 1990, CURR OPIN CELL BIOL, V6, P96
   Narshi A, 2005, CARDIOVASC TOXICOL, V5, P1, DOI 10.1385/CT:5:1:001
   Palermo J, 1996, CIRC RES, V78, P504, DOI 10.1161/01.RES.78.3.504
   Perry SV, 2001, J MUSCLE RES CELL M, V22, P5, DOI 10.1023/A:1010303732441
   Pieples K, 2000, BIOCHEMISTRY-US, V39, P8291, DOI 10.1021/bi000047x
   Pieples K, 2002, AM J PHYSIOL-HEART C, V283, pH1344, DOI 10.1152/ajpheart.00351.2002
   Pinnamaneni S, 2013, AM BASED RES J, V2, P24
   Rethinasamy P, 1998, CIRC RES, V82, P116
   Robbins J, 1998, CIRC RES, V82, P134
   ROM E, 1994, P NATL ACAD SCI USA, V91, P3959, DOI 10.1073/pnas.91.9.3959
   ROY RK, 1982, FEBS LETT, V149, P22, DOI 10.1016/0014-5793(82)81063-6
   RUIZOPAZO N, 1987, J BIOL CHEM, V262, P4755
   Sadek H, 2008, P NATL ACAD SCI USA, V105, P6063, DOI 10.1073/pnas.0711507105
   Schevzov Galina, 2011, Bioarchitecture, V1, P135
   Spinner BJ, 2002, J CELL BIOCHEM, V85, P747, DOI 10.1002/jcb.10178
   TAYLOR MV, 1991, NUCLEIC ACIDS RES, V19, P2669, DOI 10.1093/nar/19.10.2669
   Ueyama T, 2003, MOL CELL BIOL, V23, P9222, DOI 10.1128/MCB.23.24.9222-9232.2003
   Varga AE, 2005, ONCOGENE, V24, P5043, DOI 10.1038/sj.onc.1208688
   VOSS JW, 1991, J BIOL CHEM, V266, P12832
   Welle S, 1999, J APPL PHYSIOL, V86, P1220, DOI 10.1152/jappl.1999.86.4.1220
   WIECZOREK DF, 1988, MOL CELL BIOL, V8, P679, DOI 10.1128/MCB.8.2.679
   Yoshida T, 2003, CIRC RES, V92, P856, DOI 10.1161/01.RES.0000068405.49081.09
   Zajdel RW, 2006, J CELL BIOCHEM, V99, P952, DOI 10.1002/jcb.20954
   Zajdel RT, 1998, DEV DYNAM, V213, P412, DOI 10.1002/(SICI)1097-0177(199812)213:4<412::AID-AJA6>3.0.CO;2-C
   Zajdel RW, 2005, CARDIOVASC TOXICOL, V5, P75, DOI 10.1385/CT:5:1:075
   Zajdel RW, 2005, J CELL BIOCHEM, V95, P840, DOI 10.1002/jcb.20456
   Zajdel RW, 2000, ANAT EMBRYOL, V201, P217, DOI 10.1007/s004290050312
   Zajdel RW, 1999, EXP CELL RES, V248, P557, DOI 10.1006/excr.1999.4419
   Zajdel RW, 2003, J CELL BIOCHEM, V89, P427, DOI 10.1002/jcb.10504
   Zajdel RW, 2002, FEBS LETT, V520, P35, DOI 10.1016/S0014-5793(02)02756-4
   Zhang C, 2009, J BIOMED SCI, V16, DOI 10.1186/1423-0127-16-81
   Zhu SM, 2007, J BIOL CHEM, V282, P14328, DOI 10.1074/jbc.M611393200
NR 60
TC 13
Z9 14
U1 2
U2 13
PU WILEY-BLACKWELL
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 1932-8486
EI 1932-8494
J9 ANAT REC
JI Anat. Rec.
PD SEP
PY 2014
VL 297
IS 9
BP 1585
EP 1595
DI 10.1002/ar.22978
PG 11
WC Anatomy & Morphology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Anatomy & Morphology
GA AN6BJ
UT WOS:000340678300007
PM 25125172
OA Bronze
DA 2025-04-10
ER

PT J
AU Favot, L
   Gillingwater, M
   Scott, C
   Kemp, PR
AF Favot, L
   Gillingwater, M
   Scott, C
   Kemp, PR
TI Overexpression of a family of RPEL proteins modifies cell shape
SO FEBS LETTERS
LA English
DT Article
DE actin; cytoskeleton; cell shape; RPEL; subcellular localization
ID SERUM RESPONSE FACTOR; ACTIN DYNAMICS; MYOCARDIN
AB Proteins containing RPEL motifs (e.g., MAL) are important in the regulation of gene expression by the actin cytoskeleton. Screening the ENSEMBL database for RPEL proteins identified four additional proteins that contain RPEL motifs and nuclear localisation sequences, three of which (RPEL-A, RPEL-B and RPEL-C) are expressed in adult mouse tissues with different expression profiles. The mRNAs encoding RPEL-B and RPEL-C were subject to alternative splicing. Expression of these genes in cells indicated that they had a marked effect on cell shape. Furthermore, when expressed with a nuclear localised actin all of the different forms became restricted to the nucleus. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
C1 Univ Cambridge, Dept Biochem, Cambridge CB2 1QW, England.
C3 University of Cambridge
RP Univ Cambridge, Dept Biochem, Bldg O Downing Site,Tennis Court Rd, Cambridge CB2 1QW, England.
EM pk@mole.bio.cam.ac.uk
RI Laforge, Laure/AGW-2729-2022
OI Kemp, Paul/0000-0001-8975-7293; Scott, Caroline/0000-0002-1708-7427
CR Chen JY, 2002, J MOL CELL CARDIOL, V34, P1345, DOI 10.1006/jmcc.2002.2086
   Ellis PD, 2002, BIOCHEM J, V364, P547, DOI 10.1042/BJ20020269
   KEMP PR, 1995, BIOCHEM J, V310, P1037, DOI 10.1042/bj3101037
   Kemp PR, 2000, BIOCHEM J, V345, P445, DOI 10.1042/0264-6021:3450445
   Martin KM, 2000, BIOCHEM J, V345, P529, DOI 10.1042/0264-6021:3450529
   Miralles F, 2003, CELL, V113, P329, DOI 10.1016/S0092-8674(03)00278-2
   Sagara J, 2003, J BIOL CHEM, V278, P45611, DOI 10.1074/jbc.M305227200
   Sotiropoulos A, 1999, CELL, V98, P159, DOI 10.1016/S0092-8674(00)81011-9
   Wang DZ, 2002, P NATL ACAD SCI USA, V99, P14855, DOI 10.1073/pnas.222561499
NR 9
TC 17
Z9 21
U1 0
U2 4
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 1873-3468
J9 FEBS LETT
JI FEBS Lett.
PD JAN 3
PY 2005
VL 579
IS 1
BP 100
EP 104
DI 10.1016/j.febslet.2004.11.054
PG 5
WC Biochemistry & Molecular Biology; Biophysics; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics; Cell Biology
GA 885PT
UT WOS:000226170100016
PM 15620697
OA Bronze
DA 2025-04-10
ER

PT J
AU Mehaffey, JH
   Hawkins, RB
   Fashandi, A
   Cherry, KJ
   Kern, JA
   Kron, IL
   Upchurch, GR
   Robinson, WP
AF Mehaffey, J. Hunter
   Hawkins, Robert B.
   Fashandi, Anna
   Cherry, Kenneth J.
   Kern, John A.
   Kron, Irving L.
   Upchurch, Gilbert R., Jr.
   Robinson, William P.
TI Lower extremity bypass for critical limb ischemia decreases major
   adverse limb events with equivalent cardiac risk compared with
   endovascular intervention
SO JOURNAL OF VASCULAR SURGERY
LA English
DT Article
ID QUALITY IMPROVEMENT PROGRAM; OBJECTIVE PERFORMANCE GOALS; INFRAINGUINAL
   BYPASS; SURGERY; OUTCOMES; SALVAGE; THERAPY; SOCIETY; DISEASE
AB Objective: Lower extremity bypass (LEB) has traditionally been the "gold standard" in the treatment of critical limb ischemia (CLI). Infrainguinal endovascular intervention (IEI) has become more commonly performed than LEB, but comparative outcomes are limited. We sought to compare rates of major adverse limb events (MALEs) and major adverse cardiovascular events (MACEs) after LEB and IEI in a propensity score-matched, national cohort of patients with CLI.
   Methods: The National Surgical Quality Improvement Program (NSQIP) vascular targeted files (2011-2014) for LEB and IEI were merged. CLI patients were identified by ischemic rest pain or tissue loss. Patients were matched on a 1:1 basis for propensity to undergo LEB or IEI. Primary outcomes were 30-day MALEs and MACEs. Within the propensity-matched cohort, multivariate logistic regression was used to identify independent predictors of MALEs and MACEs.
   Results: A total of 13,294 LEBs and IEIs were identified, with 8066 cases performed for CLI. Propensity matching identified 3848 cases (1924 per group). There were no differences in preoperative variables between the propensity-matched LEB and IEI groups (all P > .05). At 30 days, rates of MALEs were significantly lower in the LEB group (9.2% LEB vs IEI 12.2%; P = .003). On multivariate logistic regression, bypass with single-segment saphenous vein vs IEI (odds ratio [OR], 0.7; 95% confidence interval [CI], 0.54-0.92; P = .01), bypass with alternative conduit (prosthetic, spliced vein, or composite) vs IEI (OR, 0.7; 95% CI, 0.56-0.98; P = .04), antiplatelet therapy (OR, 0.8; 95% CI, 0.58-1.00; P = .049), and statin therapy (OR, 0.8; 95% CI, 0.62-0.99; P = .04) were protective against MALEs, whereas infrageniculate intervention (OR, 1.4; 95% CI, 1.09-1.72; P = .01) and a history of prior bypass of the same arterial segment (OR, 1.8; 95% CI, 1.41-2.41; P < . 0001) were predictive. Rates of 30-day MACEs were not significantly different (4.9% LEB vs 3.7% IEI; P = .07) between the groups. Independent predictors of MACEs included age (OR, 1.02; 95% CI, 1.01-1.04; P = .01), steroid use (OR, 1.8; 95% CI, 1.08-2.99; P = .03), congestive heart failure (OR, 1.7; 95% CI, 1.00-1.96; P = .02), beta blocker use (OR, 1.6; 95% CI, 1.09-1.43; P = .01), dialysis (OR, 2.3; 95% CI, 1.55-3.45; P < .0001), totally dependent functional status (OR, 3.1; 95% CI, 1.25-7.58; P = .02), and suboptimal conduit for LEB compared with IEI (OR, 1.6; 95% CI, 1.08-2.36; P = .02).
   Conclusions: Within this large, propensity-matched, national cohort, LEB predicted lower risk-adjusted 30-day MALE rate compared with IEI. Furthermore, there was no difference in 30-day MACE rate between the groups despite higher inherent risk with open surgical procedures. Therefore, this study supports the effectiveness and primacy of LEB for revascularization in CLI.
C1 Univ Virginia, Dept Surg, Div Vasc & Endovasc Surg, Charlottesville, VA 22903 USA.
   Univ Virginia, Dept Surg, Div Thorac & Cardiovasc Surg, Charlottesville, VA 22903 USA.
C3 University of Virginia; University of Virginia
RP Robinson, WP (corresponding author), Univ Virginia, Div Vasc & Endovasc Surg, Box 800679, Charlottesville, VA 22908 USA.
EM wr4w@virginia.edu
RI Hawkins, Robert/J-3890-2019; Mehaffey, James/L-5385-2019
OI Hawkins, Robert/0000-0002-3959-8201
FU National Institutes of Health [T32 HL07849]
FX This work was supported by the National Institutes of Health (T32
   HL07849). The content is solely the responsibility of the authors and
   does not necessarily represent the official views of the National
   Institutes of Health.
CR Aiello FA, 2012, J VASC SURG, V55, P371, DOI 10.1016/j.jvs.2011.08.044
   Bradbury AW, 2010, J VASC SURG, V51, p18S, DOI 10.1016/j.jvs.2010.01.074
   Cohen ME, 2009, J AM COLL SURGEONS, V208, P1009, DOI 10.1016/j.jamcollsurg.2009.01.043
   Conte MS, 2009, J VASC SURG, V50, P1462, DOI 10.1016/j.jvs.2009.09.044
   Conte MS, 2005, J VASC SURG, V42, P456, DOI 10.1016/j.jvs.2005.05.001
   Crawford RS, 2010, J VASC SURG, V51, P351, DOI 10.1016/j.jvs.2009.08.065
   Goodney PP, 2011, J VASC SURG, V54, P100, DOI 10.1016/j.jvs.2010.11.107
   Hughes K, 2014, VASC ENDOVASC SURG, V48, P402, DOI 10.1177/1538574414543276
   Jafarian Ali, 2015, Med J Islam Repub Iran, V29, P278
   Kim Hyo-Sin, 2014, Vasc Specialist Int, V30, P26, DOI 10.5758/vsi.2014.30.1.26
   Lucas LC, 2011, PLAST RECONSTR SURG, V127, p163S, DOI 10.1097/PRS.0b013e3182028eab
   Masaki Hisao, 2014, Ann Vasc Dis, V7, P227, DOI 10.3400/avd.oa.14-00070
   McMurry TL, 2015, J THORAC CARDIOV SUR, V150, P14, DOI 10.1016/j.jtcvs.2015.03.057
   Menard MT, 2014, SEMIN VASC SURG, V27, P82, DOI 10.1053/j.semvascsurg.2015.01.003
   Parsons LD, 2004, 29 SUGI
   Raval MV, 2010, J AM COLL SURGEONS, V211, P715, DOI 10.1016/j.jamcollsurg.2010.07.021
   Santo VJ, 2014, J VASC SURG, V60, P129, DOI 10.1016/j.jvs.2014.01.013
   Saraidaridis JT, 2016, ANN VASC SURG, V30, P59, DOI 10.1016/j.avsg.2015.09.001
   Selvarajah S, 2014, J SURG RES, V190, P335, DOI 10.1016/j.jss.2014.04.029
   Simons JP, 2012, J VASC SURG, V55, P1629, DOI 10.1016/j.jvs.2011.12.043
   Siracuse JJ, 2016, J VASC SURG, V63, DOI [10.1016/j.jvs.2015.09.063, DOI 10.1016/J.JVS.2015.09.063]
   Soga Y, 2013, CIRC J, V77, P2102, DOI 10.1253/circj.CJ-13-0020
   Verzini F, 2012, J CARDIOVASC SURG, V53, P179
   Zhang JQ, 2014, J VASC SURG, V59, P1331, DOI 10.1016/j.jvs.2013.12.032
NR 24
TC 34
Z9 34
U1 0
U2 1
PU MOSBY-ELSEVIER
PI NEW YORK
PA 360 PARK AVENUE SOUTH, NEW YORK, NY 10010-1710 USA
SN 0741-5214
J9 J VASC SURG
JI J. Vasc. Surg.
PD OCT
PY 2017
VL 66
IS 4
BP 1109
EP +
DI 10.1016/j.jvs.2017.04.036
PG 9
WC Surgery; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Surgery; Cardiovascular System & Cardiology
GA FJ2QM
UT WOS:000412574300040
PM 28655549
OA Green Accepted, Bronze
DA 2025-04-10
ER

PT J
AU Park, S
   Mathis, KW
   Lee, IK
AF Park, S.
   Mathis, K. W.
   Lee, I. K.
TI The physiological roles of apolipoprotein J/clusterin in metabolic and
   cardiovascular diseases
SO REVIEWS IN ENDOCRINE & METABOLIC DISORDERS
LA English
DT Article
DE Atherosclerosis; Clusterin-deficientmice; Diabetes; High density
   cholesterol; Oxidative stress
ID HIGH-DENSITY-LIPOPROTEIN; GENOME-WIDE ASSOCIATION; HISTONE DEACETYLASE
   INHIBITORS; CORONARY-ARTERY-DISEASE; SMOOTH-MUSCLE-CELLS;
   ALZHEIMERS-DISEASE; CLUSTERIN OVEREXPRESSION; NUCLEAR CLUSTERIN;
   CLUSTERIN/APOLIPOPROTEIN-J; ENDOTHELIAL FUNCTION
AB Several isoforms of apolipoprotein J/clusterin (CLU) are encoded from a single gene located on chromosome 8 in humans. These isoforms are ubiquitously expressed in the tissues, and have been implicated in aging, neurodegenerative disorders, cancer progression, and metabolic/cardiovascular diseases including dyslipidemia, diabetes, atherosclerosis and myocardial infarction. The conventional secreted form of CLU (sCLU) is thought to be a component of high density lipoprotein-cholesterol. sCLU functions as a chaperone for misfolded proteins and it is thought to promote survival by reducing oxidative stress. Nuclear CLU, a truncated CLU formed by alternative splicing, is responsible for promoting apoptosis via a Bax-dependent pathway. There are putative regulatory sites in the promoter regions of CLU, which are occupied by transcription factors such as transforming growth factor (TGF)-beta inhibitory element, activator protein-1, CLU-specific elements, and carbohydrate response element. However, the molecular mechanisms underlying the distinct roles of CLU in a variety of conditions remain unclear. Although the function of CLU in cancer or neurological disease has been studied intensively for three decades, physiological roles of CLU seem unexplored in the cardiovascular system and metabolic diseases. In this review, we will discuss general characteristics and regulations of CLU based on previous literature and assess the recent findings associated with its physiological roles in different tissues including the vasculature, heart, liver, kidney, adipose tissue, and brain.
C1 [Park, S.] Kyungpook Natl Univ, Leading Edge Res Ctr Drug Discovery & Dev Diabet, Taegu 700721, South Korea.
   [Mathis, K. W.] Univ Mississippi, Med Ctr, Dept Physiol & Biophys, Jackson, MS 39216 USA.
   [Lee, I. K.] Kyungpook Natl Univ, Sch Med, Dept Internal Med, Taegu 700721, South Korea.
C3 Kyungpook National University (KNU); University of Mississippi;
   University of Mississippi Medical Center; Kyungpook National University
   (KNU)
RP Lee, IK (corresponding author), Kyungpook Natl Univ, Sch Med, Dept Internal Med, 50 Samduk 2Ga, Taegu 700721, South Korea.
EM leei@knu.ac.kr
FU National Research Foundation of Korea (NRF); Korean Ministry of
   Education (MOE) [2012R1A2A1A03670452]; Korea Health Technology R&D
   Project, Ministry of Health and Welfare, Republic of Korea [A111345];
   Kyungpook National University
FX This work was supported by the National Research Foundation of Korea
   (NRF) grant funded by the Korean Ministry of Education
   (MOE)(2012R1A2A1A03670452), a grant of the Korea Health Technology R&D
   Project, Ministry of Health and Welfare, Republic of Korea (A111345),
   and supported by Kyungpook National University Research Fund, 2013.
CR Ammar H, 2008, J BIOL CHEM, V283, P12851, DOI 10.1074/jbc.M800403200
   Antonelou MH, 2011, PLOS ONE, V6, DOI 10.1371/journal.pone.0026032
   Bajari TM, 2003, FASEB J, V17, P1505, DOI 10.1096/fj.02-1106fje
   Bertram L, 2009, HUM MOL GENET, V18, pR137, DOI 10.1093/hmg/ddp406
   Besler C, 2011, J CLIN INVEST, V121, P2693, DOI 10.1172/JCI42946
   BLASCHUK O, 1983, J BIOL CHEM, V258, P7714
   Caro JF, 1996, LANCET, V348, P159, DOI 10.1016/S0140-6736(96)03173-X
   Chang YJ, 2011, ANN SURG ONCOL, V18, P2395, DOI 10.1245/s10434-011-1597-3
   Chen YR, 2007, J BIOL CHEM, V282, P32640, DOI 10.1074/jbc.M702294200
   Daimon M, 2011, METABOLISM, V60, P815, DOI 10.1016/j.metabol.2010.07.033
   Deng X, 2007, J BIOL CHEM, V282, P17517, DOI 10.1074/jbc.M702228200
   DESILVA HV, 1990, BIOCHEMISTRY-US, V29, P5380, DOI 10.1021/bi00474a025
   Di Angelantonio E, 2009, JAMA-J AM MED ASSOC, V302, P1993, DOI 10.1001/jama.2009.1619
   DONNELLY TJ, 1992, CIRCULATION, V85, P769, DOI 10.1161/01.CIR.85.2.769
   Du YF, 2013, BIOCHEM BIOPH RES CO, V436, P462, DOI 10.1016/j.bbrc.2013.05.127
   Forte TM, 2002, J LIPID RES, V43, P477
   Franco DA, 2012, ATHEROSCLEROSIS, V225, P220, DOI 10.1016/j.atherosclerosis.2012.08.028
   Friedman JM, 1998, NATURE, V395, P763, DOI 10.1038/27376
   Fryirs MA, 2010, ARTERIOSCL THROM VAS, V30, P1642, DOI 10.1161/ATVBAHA.110.207373
   Getz GS, 2010, CURR PHARM DESIGN, V16, P3173
   Gil SY, 2013, NAT COMMUN, V4, DOI 10.1038/ncomms2896
   Hamada N, 2011, J ATHEROSCLER THROMB, V18, P209, DOI 10.5551/jat.5819
   Han BH, 2001, NAT MED, V7, P338, DOI 10.1038/85487
   Harlan SM, 2011, CIRC RES, V108, P808, DOI 10.1161/CIRCRESAHA.111.240226
   Harold D, 2009, NAT GENET, V41, P1088, DOI 10.1038/ng.440
   Hedrick CC, 2000, DIABETOLOGIA, V43, P312, DOI 10.1007/s001250050049
   Henderson B, 2012, CELL STRESS CHAPERON, V17, P303, DOI 10.1007/s12192-011-0318-y
   Horton JD, 1998, P NATL ACAD SCI USA, V95, P5987, DOI 10.1073/pnas.95.11.5987
   Humphreys D, 1997, BIOCHEMISTRY-US, V36, P15233, DOI 10.1021/bi9703507
   JENNE DE, 1989, P NATL ACAD SCI USA, V86, P7123, DOI 10.1073/pnas.86.18.7123
   Johnstone RW, 2003, CANCER CELL, V4, P13, DOI 10.1016/S1535-6108(03)00165-X
   July LV, 2002, PROSTATE, V50, P179, DOI 10.1002/pros.10047
   Jung GS, 2012, J AM SOC NEPHROL, V23, P73, DOI 10.1681/ASN.2011010048
   Khan QES, 2013, EUR J ORAL SCI, V121, P303, DOI 10.1111/eos.12056
   Kim G, 2011, BIOCHEM BIOPH RES CO, V408, P720, DOI 10.1016/j.bbrc.2011.04.111
   Kim HJ, 2009, ARTERIOSCL THROM VAS, V29, P1558, DOI 10.1161/ATVBAHA.109.190058
   Kim N, 2012, J CELL PHYSIOL, V227, P1157, DOI 10.1002/jcp.22836
   Kususda Y, 2012, BRIT J CANCER, V106, P1945, DOI 10.1038/bjc.2012.209
   Lambert JC, 2009, NAT GENET, V41, P1094, DOI 10.1038/ng.439
   LAPING NJ, 1994, NEUROSCIENCE, V58, P563, DOI 10.1016/0306-4522(94)90081-7
   Laskin JJ, 2012, J THORAC ONCOL, V7, P579, DOI 10.1097/JTO.0b013e31823f459c
   Lee DH, 2011, BIOCHEM BIOPH RES CO, V408, P541, DOI 10.1016/j.bbrc.2011.04.054
   Lee KB, 2008, BIOCHEM BIOPH RES CO, V366, P905, DOI 10.1016/j.bbrc.2007.12.033
   Leskov KS, 2011, J BIOL CHEM, V286, P40083, DOI 10.1074/jbc.M111.252957
   Leskov KS, 2003, J BIOL CHEM, V278, P11590, DOI 10.1074/jbc.M209233200
   Levitan I, 2010, ANTIOXID REDOX SIGN, V13, P39, DOI 10.1089/ars.2009.2733
   Lin ZF, 2013, CELL METAB, V17, P779, DOI 10.1016/j.cmet.2013.04.005
   Liu T, 2009, EUR J CANCER, V45, P1846, DOI 10.1016/j.ejca.2009.03.002
   Madamanchi NR, 2005, ARTERIOSCL THROM VAS, V25, P950, DOI 10.1161/01.ATV.0000161050.77646.68
   MARBER MS, 1995, J CLIN INVEST, V95, P1446, DOI 10.1172/JCI117815
   McMurray JJV, 2005, LANCET, V365, P1877, DOI 10.1016/S0140-6736(05)66621-4
   MICHEL D, 1995, EUR J BIOCHEM, V229, P215, DOI 10.1111/j.1432-1033.1995.0215l.x
   Miyata M, 2001, CIRCULATION, V104, P1407, DOI 10.1161/hc3701.095583
   Morales CR, 1996, BIOL REPROD, V55, P676, DOI 10.1095/biolreprod55.3.676
   Morgantini C, 2011, DIABETES, V60, P2617, DOI 10.2337/db11-0378
   Morgantini C, 2010, DIABETES, V59, P3223, DOI 10.2337/db10-0844
   Moxon JV, 2011, ATHEROSCLEROSIS, V219, P432, DOI 10.1016/j.atherosclerosis.2011.08.013
   Navab M, 2005, CIRC RES, V97, P524, DOI 10.1161/01.RES.0000181229.69508.2f
   Navab M, 2004, CIRCULATION, V109, P3215, DOI 10.1161/01.CIR.0000134275.90823.87
   Navab M, 2001, CIRCULATION, V104, P2386, DOI 10.1161/circ.104.20.2386
   Navab M, 2001, ARTERIOSCL THROM VAS, V21, P481, DOI 10.1161/01.ATV.21.4.481
   Navab M, 2009, DIABETES, V58, P2711, DOI 10.2337/db09-0538
   Nizard P, 2007, TRAFFIC, V8, P554, DOI 10.1111/j.1600-0854.2007.00549.x
   Park S, 2013, HYPERTENSION, V62, P41, DOI 10.1161/HYPERTENSIONAHA.113.01330
   Poon S, 2000, BIOCHEMISTRY-US, V39, P15953, DOI 10.1021/bi002189x
   Postic C, 2008, J CLIN INVEST, V118, P829, DOI 10.1172/JCI34275
   Rahman ST, 2012, J CARDIOVASC PHARM T, V17, P139, DOI 10.1177/1074248411413282
   Rahmouni K, 2005, DIABETES, V54, P2012, DOI 10.2337/diabetes.54.7.2012
   Ranney MK, 2007, BBA-MOL BASIS DIS, V1772, P1103, DOI 10.1016/j.bbadis.2007.06.004
   Riwanto M, 2013, CIRCULATION, V127, P891, DOI 10.1161/CIRCULATIONAHA.112.108753
   Rosenberg ME, 2002, MOL CELL BIOL, V22, P1893, DOI 10.1128/MCB.22.6.1893-1902.2002
   Saad F, 2011, CLIN CANCER RES, V17, P5765, DOI 10.1158/1078-0432.CCR-11-0859
   Schrijvers EMC, 2011, JAMA-J AM MED ASSOC, V305, P1322, DOI 10.1001/jama.2011.381
   Seo HY, 2013, ENDOCRINOLOGY, V154, P1722, DOI 10.1210/en.2012-2009
   Tanzi RE, 2004, NEURON, V43, P605, DOI 10.1016/j.neuron.2004.08.024
   THOMASSALGAR S, 1994, J BIOL CHEM, V269, P17879
   Trougakos IP, 2006, FREE RADICAL RES, V40, P1324, DOI 10.1080/10715760600902310
   Trougakos IP, 2009, CLIN CANCER RES, V15, P48, DOI 10.1158/1078-0432.CCR-08-1805
   Trougakos IP, 2002, INT J BIOCHEM CELL B, V34, P1430, DOI 10.1016/S1357-2725(02)00041-9
   Troutt JS, 2008, J LIPID RES, V49, P581, DOI 10.1194/jlr.M700385-JLR200
   Tunçdemir M, 2008, J MOL HISTOL, V39, P605, DOI 10.1007/s10735-008-9201-2
   Tycko B, 1996, HUM GENET, V98, P430, DOI 10.1007/s004390050234
   Urbich C, 2000, CIRCULATION, V101, P352, DOI 10.1161/01.CIR.101.4.352
   Valko M, 2007, INT J BIOCHEM CELL B, V39, P44, DOI 10.1016/j.biocel.2006.07.001
   van Dijk A, 2010, EUR J CLIN INVEST, V40, P893, DOI 10.1111/j.1365-2362.2010.02345.x
   Wang C, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0055981
   Wei L, 2009, INT J CANCER, V125, P791, DOI 10.1002/ijc.24316
   Wilson MR, 2000, TRENDS BIOCHEM SCI, V25, P95, DOI 10.1016/S0968-0004(99)01534-0
   WONG P, 1994, EUR J BIOCHEM, V221, P917, DOI 10.1111/j.1432-1033.1994.tb18807.x
   WONG P, 1993, J BIOL CHEM, V268, P5021
   Xie D, 2005, WORLD J GASTROENTERO, V11, P3285, DOI 10.3748/wjg.v11.i21.3285
   Yom CK, 2009, ANTICANCER RES, V29, P3909
   Zlokovic BV, 1996, P NATL ACAD SCI USA, V93, P4229, DOI 10.1073/pnas.93.9.4229
   Zong WX, 2001, GENE DEV, V15, P1481, DOI 10.1101/gad.897601
NR 94
TC 100
Z9 103
U1 0
U2 11
PU SPRINGER
PI NEW YORK
PA 233 SPRING ST, NEW YORK, NY 10013 USA
SN 1389-9155
EI 1573-2606
J9 REV ENDOCR METAB DIS
JI Rev. Endocr. Metab. Disord.
PD MAR
PY 2014
VL 15
IS 1
BP 45
EP 53
DI 10.1007/s11154-013-9275-3
PG 9
WC Endocrinology & Metabolism
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism
GA AB7NW
UT WOS:000331978400005
PM 24097125
DA 2025-04-10
ER

PT J
AU Ueyama, T
   Kasahara, H
   Ishiwata, T
   Nie, Q
   Izumo, S
AF Ueyama, T
   Kasahara, H
   Ishiwata, T
   Nie, Q
   Izumo, S
TI Myocardin expression is regulated by Nkx2.5, and its function is
   required for cardiomyogenesis
SO MOLECULAR AND CELLULAR BIOLOGY
LA English
DT Article
ID SERUM RESPONSE FACTOR; BONE MORPHOGENETIC PROTEINS; HEART DEVELOPMENT;
   MOUSE EMBRYOGENESIS; CARDIOMYOCYTE DIFFERENTIATION; TRANSCRIPTION
   FACTORS; SIGNAL-TRANSDUCTION; CARDIAC MYOGENESIS; GENE-EXPRESSION;
   EMBRYOS LACKING
AB Nkx2.5 (also known as Csx) is an evolutionarily conserved cardiac transcription factor of the homeobox gene family. Nkx2.5 is required for early heart development, since Nkx2.5-null mice die before completion of cardiac looping. To identify genes regulated by Nkx2.5 in the developing heart, we performed subtractive hybridization by using RNA isolated from wild-type and Nkx2.5-null hearts at embryonic day 8.5. We isolated a mouse cDNA encoding myocardin A, which is an alternative spliced isoform of myocardin and the most abundant isoform in the heart from embryo to adult. The expression of myocardin A and myocardin was markedly downregulated in Nkx2.5-null mouse hearts. Transient-cotransfection analysis showed that Nkx2.5 transactivates the myocardin promoter. Inhibition of myocardin function in the teratocarcinoma cell line P19CL6 prevented differentiation into cardiac myocytes after dimethyl sulfoxide treatment. Myocardin A transactivated the promoter of the atrial natriuretic factor gene through the serum response element, which was augmented by bone morphogenetic protein 2 and transforming growth factor beta-activated kinase 1. These results suggest that myocardin expression is regulated by Nkx2.5 and that its function is required for cardiomyogenesis.
C1 Harvard Univ, Sch Med, Beth Israel Deaconess Med Ctr, Div Cardiovasc,Dept Med, Boston, MA 02215 USA.
C3 Harvard University; Harvard University Medical Affiliates; Beth Israel
   Deaconess Medical Center; Harvard Medical School
RP Izumo, S (corresponding author), Harvard Univ, Sch Med, Beth Israel Deaconess Med Ctr, Div Cardiovasc,Dept Med, Boston, MA 02215 USA.
FU NHLBI NIH HHS [P50 HL 61036] Funding Source: Medline
CR Arsenian S, 1998, EMBO J, V17, P6289, DOI 10.1093/emboj/17.21.6289
   Beppu H, 2000, DEV BIOL, V221, P249, DOI 10.1006/dbio.2000.9670
   Biben C, 1997, COLD SPRING HARB SYM, V62, P395, DOI 10.1101/SQB.1997.062.01.047
   Biben C, 1997, GENE DEV, V11, P1357, DOI 10.1101/gad.11.11.1357
   BODMER R, 1993, DEVELOPMENT, V118, P719
   Bruneau BG, 2000, DEV BIOL, V217, P266, DOI 10.1006/dbio.1999.9548
   Chen JY, 2002, J MOL CELL CARDIOL, V34, P1345, DOI 10.1006/jmcc.2002.2086
   CHEN WS, 1995, ONCOL REP, V2, P5
   Christoffels VM, 2000, DEV BIOL, V223, P266, DOI 10.1006/dbio.2000.9753
   FRASCH M, 1995, NATURE, V374, P464, DOI 10.1038/374464a0
   Gu ZY, 1999, DEVELOPMENT, V126, P2551
   HabaraOhkubo A, 1996, CELL STRUCT FUNCT, V21, P101, DOI 10.1247/csf.21.101
   Harvey RP, 1996, DEV BIOL, V178, P203, DOI 10.1006/dbio.1996.0212
   Hines WA, 1999, MOL CELL BIOL, V19, P1841
   Jamali M, 2001, FEBS LETT, V509, P126, DOI 10.1016/S0014-5793(01)03151-9
   Jamali M, 2001, J BIOL CHEM, V276, P42252, DOI 10.1074/jbc.M107814200
   Kasahara H, 1998, CIRC RES, V82, P936, DOI 10.1161/01.RES.82.9.936
   Kasahara H, 2001, J BIOL CHEM, V276, P4570, DOI 10.1074/jbc.M004995200
   Kawabata M, 1998, CYTOKINE GROWTH F R, V9, P49, DOI 10.1016/S1359-6101(97)00036-1
   KOMURO I, 1993, P NATL ACAD SCI USA, V90, P8145, DOI 10.1073/pnas.90.17.8145
   Ladd AN, 1998, DEV BIOL, V204, P407, DOI 10.1006/dbio.1998.9094
   LINTS TJ, 1993, DEVELOPMENT, V119, P419
   LYONS I, 1995, GENE DEV, V9, P1654, DOI 10.1101/gad.9.13.1654
   MACLELLAN WR, 1994, J BIOL CHEM, V269, P16754
   Mishina Y, 1999, DEV BIOL, V213, P314, DOI 10.1006/dbio.1999.9378
   Mishina Y, 1995, GENE DEV, V9, P3027, DOI 10.1101/gad.9.24.3027
   Monzen K, 1999, MOL CELL BIOL, V19, P7096
   Monzen K, 2001, J CELL BIOL, V153, P687, DOI 10.1083/jcb.153.4.687
   Palmer S, 2001, J CELL BIOL, V153, P985, DOI 10.1083/jcb.153.5.985
   Radice GL, 1997, DEV BIOL, V181, P64, DOI 10.1006/dbio.1996.8443
   REECY L, 1999, HEART DEV, P273
   SADOSHIMA J, 1992, J BIOL CHEM, V267, P10551
   Schultheiss TM, 1997, GENE DEV, V11, P451, DOI 10.1101/gad.11.4.451
   Sepulveda JL, 2002, J BIOL CHEM, V277, P25775, DOI 10.1074/jbc.M203122200
   Shi YQ, 2000, DEV BIOL, V224, P226, DOI 10.1006/dbio.2000.9802
   Tanaka M, 1999, DEVELOPMENT, V126, P1269
   Thuerauf DJ, 1998, J BIOL CHEM, V273, P20636, DOI 10.1074/jbc.273.32.20636
   Toko H, 2002, J BIOL CHEM, V277, P24735, DOI 10.1074/jbc.M107669200
   Ueyama T, 1998, J MOL CELL CARDIOL, V30, P551, DOI 10.1006/jmcc.1997.0619
   von Bubnoff A, 2001, DEV BIOL, V239, P1, DOI 10.1006/dbio.2001.0388
   Walters MJ, 2001, MECH DEVELOP, V100, P263, DOI 10.1016/S0925-4773(00)00535-9
   Wang DZ, 2001, CELL, V105, P851, DOI 10.1016/S0092-8674(01)00404-4
   YAMAGUCHI K, 1995, SCIENCE, V270, P2008, DOI 10.1126/science.270.5244.2008
   Zhang D, 2000, NAT MED, V6, P556, DOI 10.1038/75037
   Zhang HB, 1996, DEVELOPMENT, V122, P2977
   Zhu C, 1997, MOL CELL BIOL, V17, P4957, DOI 10.1128/MCB.17.9.4957
   Zou YM, 1997, DEVELOPMENT, V124, P793
NR 47
TC 100
Z9 132
U1 0
U2 6
PU AMER SOC MICROBIOLOGY
PI WASHINGTON
PA 1752 N ST NW, WASHINGTON, DC 20036-2904 USA
SN 0270-7306
J9 MOL CELL BIOL
JI Mol. Cell. Biol.
PD DEC
PY 2003
VL 23
IS 24
BP 9222
EP 9232
DI 10.1128/MCB.23.24.9222-9232.2003
PG 11
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA 751ET
UT WOS:000187040400027
PM 14645532
OA Green Published
DA 2025-04-10
ER

PT J
AU Suay-Corredera, C
   Pricolo, MR
   Velázquez-Carreras, D
   Pathak, D
   Nandwani, N
   Pimenta-Lopes, C
   Sánchez-Ortiz, D
   Urrutia-Irazabal, I
   Vilches, S
   Dominguez, F
   Frisso, G
   Monserrat, L
   García-Pavía, P
   de Sancho, D
   Spudich, JA
   Ruppel, KM
   Herrero-Galán, E
   Alegre-Cebollada, J
AF Suay-Corredera, Carmen
   Pricolo, Maria Rosaria
   Velazquez-Carreras, Diana
   Pathak, Divya
   Nandwani, Neha
   Pimenta-Lopes, Carolina
   Sanchez-Ortiz, David
   Urrutia-Irazabal, Inigo
   Vilches, Silvia
   Dominguez, Fernando
   Frisso, Giulia
   Monserrat, Lorenzo
   Garcia-Pavia, Pablo
   de Sancho, David
   Spudich, James A.
   Ruppel, Kathleen M.
   Herrero-Galan, Elias
   Alegre-Cebollada, Jorge
TI Nanomechanical Phenotypes in Cardiac Myosin-Binding Protein C Mutants
   That Cause Hypertrophic Cardiomyopathy
SO ACS NANO
LA English
DT Article
DE hypertrophic cardiomyopathy; protein mechanics; cMyBP-C;
   single-molecule; AFM; contraction
ID CMYBP-C; CIRCULAR-DICHROISM; TALIN ROD; FORCE; MUTATIONS; MYBPC3;
   DOMAIN; HCM; ACTIN; PHOSPHORYLATION
AB Hypertrophic cardiomyopathy (HCM) is a disease of the myocardium caused by mutations in sarcomeric proteins with mechanical roles, such as the molecular motor myosin. Around half of the HCM-causing genetic variants target contraction modulator cardiac myosin-binding protein C (cMyBP-C), although the underlying pathogenic mechanisms remain unclear since many of these mutations cause no alterations in protein structure and stability. As an alternative pathomechanism, here we have examined whether pathogenic mutations perturb the nanomechanics of cMyBP-C, which would compromise its modulatory mechanical tethers across sliding actomyosin filaments. Using single-molecule atomic force spectroscopy, we have quantified mechanical folding and unfolding transitions in cMyBP-C domains targeted by HCM mutations that do not induce RNA splicing alterations or protein thermodynamic destabilization. Our results show that domains containing mutation R495W are mechanically weaker than wild -type at forces below 40 pN and that R502Q mutant domains fold faster than wild-type. None of these alterations are found in control, nonpathogenic variants, suggesting that nanomechanical phenotypes induced by pathogenic cMyBP-C mutations contribute to HCM development. We propose that mutation-induced nanomechanical alterations may be common in mechanical proteins involved in human pathologies.
C1 [Suay-Corredera, Carmen; Pricolo, Maria Rosaria; Velazquez-Carreras, Diana; Pimenta-Lopes, Carolina; Sanchez-Ortiz, David; Urrutia-Irazabal, Inigo; Dominguez, Fernando; Herrero-Galan, Elias; Alegre-Cebollada, Jorge] Ctr Nacl Invest Cardiovasc CNIC, Madrid 28029, Spain.
   [Pricolo, Maria Rosaria; Frisso, Giulia] Univ Napoli Federico II, Dipartimento Med Mol & Biotecnol Med, I-80131 Naples, Italy.
   [Pathak, Divya; Nandwani, Neha; Spudich, James A.; Ruppel, Kathleen M.] Stanford Univ, Sch Med, Dept Biochem, Stanford, CA 94305 USA.
   [Pathak, Divya; Nandwani, Neha; Spudich, James A.; Ruppel, Kathleen M.] Stanford Univ, Stanford Cardiovasc Inst, Sch Med, Stanford, CA 94305 USA.
   [Vilches, Silvia; Dominguez, Fernando; Garcia-Pavia, Pablo] Hosp Univ Puerta Hierro, Dept Cardiol, Heart Failure & Inherited Cardiac Dis Unit, Madrid 28222, Spain.
   [Vilches, Silvia; Dominguez, Fernando; Garcia-Pavia, Pablo] European Reference Network Rare & Low Prevalence, Madrid 28222, Spain.
   [Dominguez, Fernando; Garcia-Pavia, Pablo] Ctr Invest Biomed Red Enfermedades Cardiovasc CIB, Madrid 28029, Spain.
   [Frisso, Giulia] Scarl, CEINGE Biotecnol Avanzate, I-80145 Naples, Italy.
   [Monserrat, Lorenzo] Hlth Code, La Coruna 15006, Spain.
   [Garcia-Pavia, Pablo] Univ Francisco Vitoria UFV, Madrid 28223, Spain.
   [de Sancho, David] Euskal Herriko Unibertsitatea UPV EHU, Kimika Fak, Polimero & Mat Aurreratuak Fis, Kimika & Teknol, Donostia San Sebastian 20018, Spain.
   [de Sancho, David] Donostia Int Phys Ctr DIPC, Donostia San Sebastian 20018, Spain.
C3 Centro Nacional de Investigaciones Cardiovasculares (CNIC); University
   of Naples Federico II; Stanford University; Stanford University;
   Hospital Puerta de Hierro-Majadahonda; CIBER - Centro de Investigacion
   Biomedica en Red; CIBERCV; CEINGE Biotecnologie Avanzate; Universidad
   Francisco de Vitoria; University of Basque Country
RP Alegre-Cebollada, J (corresponding author), Ctr Nacl Invest Cardiovasc CNIC, Madrid 28029, Spain.
EM jalegre@cnic.es
RI Garcia-Pavia, Pablo/T-9100-2019; Sánchez-Ortiz, David/AAF-5020-2019;
   Frisso, Giulia/A-5675-2014; Herrero-Galán, Elías/L-1207-2014; Nandwani,
   Neha/AAC-6975-2022; Pathak, Divya/HJH-3987-2023; Dominguez,
   Fernando/HOF-9354-2023; Pricolo, Maria Rosaria/T-9200-2019;
   Alegre-Cebollada, Jorge/I-4301-2014; De Sancho, David/C-4995-2009;
   Urrutia-Irazabal, Inigo/C-9331-2019
OI Garcia-Pavia, Pablo/0000-0002-5470-2257; Dominguez,
   Fernando/0000-0001-8408-363X; , Divya/0000-0001-9944-2308; Monserrat,
   Lorenzo/0000-0001-5776-0623; Pricolo, Maria Rosaria/0000-0002-6362-780X;
   Alegre-Cebollada, Jorge/0000-0003-0542-0170; Piments Costa da Silva
   Lopes, Carolina Isabel/0000-0002-9101-9051; De Sancho,
   David/0000-0002-8985-2685; Nandwani, Neha/0000-0002-6958-3756; Velazquez
   Carreras, Diana/0000-0002-0671-2549; Urrutia-Irazabal,
   Inigo/0000-0003-3653-1308; Suay-Corredera, Carmen/0000-0003-2100-4847;
   Teorikoa, Kimika/0009-0006-5627-3798; Sanchez-Ortiz,
   David/0000-0002-3551-6416
FU Ministerio de Ciencia e Innovacion (MCIN) [BIO2014-54768-P,
   BIO2017-83640-P, EIN2019-102966, RYC-2014-16604, BFU2017-90692-REDT];
   European Research Area Network on Cardiovascular Diseases [AC16/00045];
   Comunidad de Madrid [S2018/NMT-4443]; NIH [RM1 GM33289, HL117138];
   Stanford Maternal and Child Health Research Institute (MCHRI)
   Postdoctoral Fellowship [1220552-140-DHPEU]; Eusko Jaurlaritza (Basque
   Government) [IT1254-19]; Instituto de Salud Carlos III (ISCIII), MCIN;
   Pro CNIC Foundation; Severo Ochoa Center of Excellence [SEV-2015-0505];
   ISCIII to the Centro de Investigacion Biomedica en Red (CIBERCV)
   [CB16/11/00425]; FPI-SO predoctoral fellowship [BES-2016-076638];
   Italian Ministry of Education, Universities and Research (MIUR); CNIC
   Master Fellowship; Consejeria de Educacion, Juventud y Deporte de la
   Comunidad de Madrid [PEJ16/MED/TL-1593]; European Social Fund; MCIN
   (FEDER) [RYC-2016-19590, PGC2018-099321-B-I00]; National Heart Lung and
   Blood Institute [R01HL117138] Funding Source: NIH RePORTER
FX J.A.C. acknowledges funding from the Ministerio de Ciencia e Innovacion
   (MCIN) through grants BIO2014-54768-P, BIO2017-83640-P (AEI/FEDER, UE),
   EIN2019-102966, RYC-2014-16604, and BFU2017-90692-REDT, the European
   Research Area Network on Cardiovascular Diseases (ERACVD/ISCIII,
   MINOTAUR, AC16/00045), and the Comunidad de Madrid (consortium
   Tec4Bio-CM, S2018/NMT-4443, FEDER). This work was supported by NIH
   grants RM1 GM33289 and HL117138 to J.A.S.; a Stanford Dean's
   Postdoctoral Fellowship to D.P. and N.N.; and a Stanford Maternal and
   Child Health Research Institute (MCHRI) Postdoctoral Fellowship
   (1220552-140-DHPEU) to N.N. Financial support to D.D.S. comes from Eusko
   Jaurlaritza (Basque Government) through the project IT1254-19, and
   grants RYC-2016-19590 and PGC2018-099321-B-I00 from the MCIN (FEDER).
   The CNIC is supported by the Instituto de Salud Carlos III (ISCIII),
   MCIN, and the Pro CNIC Foundation and was a Severo Ochoa Center of
   Excellence (SEV-2015-0505). We acknowledge funding from ISCIII to the
   Centro de Investigacion Biomedica en Red (CIBERCV), CB16/11/00425.
   C.S.C. is the recipient of an FPI-SO predoctoral fellowship,
   BES-2016-076638. M.R.P. was the recipient of a Ph.D. fellowship from the
   Italian Ministry of Education, Universities and Research (MIUR). C.P.L.
   was a recipient of a CNIC Master Fellowship. We thank N. Vicente for
   excellent technical support (through grant PEJ16/MED/TL-1593 from
   Consejeria de Educacion, Juventud y Deporte de la Comunidad de Madrid
   and the European Social Fund). We thank the Spectroscopy and Nuclear
   Magnetic Resonance Core Unit at CNIO for access to CD instrumentation
   and discussion about protein binding assays. We thank A. Thompson and S.
   Day for their insights. We thank all members of the Molecular Mechanics
   of the Cardiovascular System team for helpful discussions and the
   contribution of five anonymous reviewers.
CR Ababou A, 2007, J BIOL CHEM, V282, P9204, DOI 10.1074/jbc.M610899200
   Ababou A, 2008, J MOL BIOL, V384, P615, DOI 10.1016/j.jmb.2008.09.065
   Abraham Mark James, 2015, SoftwareX, V1-2, P19, DOI 10.1016/j.softx.2015.06.001
   Ackermann MA, 2011, J BIOMED BIOTECHNOL, DOI 10.1155/2011/636403
   Adhikari AS, 2019, NAT COMMUN, V10, DOI 10.1038/s41467-019-10555-9
   Adhikari AS, 2016, CELL REP, V17, P2857, DOI 10.1016/j.celrep.2016.11.040
   Akhtar Mohammed, 2018, Glob Cardiol Sci Pract, V2018, P36, DOI 10.21542/gcsp.2018.36
   Alcalai R, 2008, J CARDIOVASC ELECTR, V19, P104, DOI 10.1111/j.1540-8167.2007.00965.x
   Alegre-Cebollada J, 2014, CELL, V156, P1235, DOI 10.1016/j.cell.2014.01.056
   Alegre-Cebollada J, 2010, J BIOL CHEM, V285, P11235, DOI 10.1074/jbc.M110.102962
   Anderson BR, 2013, J BIOL CHEM, V288, P5303, DOI 10.1074/jbc.M112.401372
   Barefield D, 2015, J MOL CELL CARDIOL, V79, P234, DOI 10.1016/j.yjmcc.2014.11.018
   BELL GI, 1978, SCIENCE, V200, P618, DOI 10.1126/science.347575
   Best RB, 2003, J MOL BIOL, V330, P867, DOI 10.1016/S0022-2836(03)00618-1
   Best RB, 2012, CURR OPIN STRUC BIOL, V22, P52, DOI 10.1016/j.sbi.2011.12.001
   Braunwald E., 2015, Hypertrophic Cardiomyopathy, P1
   Carrier L, 1997, CIRC RES, V80, P427, DOI 10.1161/01.res.0000435859.24609.b3
   Carrier L, 2015, GENE, V573, P188, DOI 10.1016/j.gene.2015.09.008
   Carrion-Vazquez M, 1999, P NATL ACAD SCI USA, V96, P3694, DOI 10.1073/pnas.96.7.3694
   Chen B, 2011, CSH PERSPECT BIOL, V3, DOI 10.1101/cshperspect.a004374
   DARDEN T, 1993, J CHEM PHYS, V98, P10089, DOI 10.1063/1.464397
   Davis J, 2016, CELL, V165, P1147, DOI 10.1016/j.cell.2016.04.002
   De Lange WJ, 2013, J GEN PHYSIOL, V142, P241, DOI 10.1085/jgp.201311018
   del Rio A, 2009, SCIENCE, V323, P638, DOI 10.1126/science.1162912
   Flashman E, 2004, CIRC RES, V94, P1279, DOI 10.1161/01.RES.0000127175.21818.C2
   Gasteiger E., 2005, PROTEOMICS PROTOCOLS, P571, DOI [DOI 10.1385/1-59259-890-0:571, 10.1385/1-59259-890-0:571]
   Gautel M, 2016, J EXP BIOL, V219, P135, DOI 10.1242/jeb.124941
   Glazier AA, 2018, JCI INSIGHT, V3, DOI 10.1172/jci.insight.99319
   GOLDSTEIN H, 1995, J ROY STAT SOC A STA, V158, P175, DOI 10.2307/2983411
   Green EM, 2016, SCIENCE, V351, P617, DOI 10.1126/science.aad3456
   Greenfield NJ, 2006, NAT PROTOC, V1, P2876, DOI 10.1038/nprot.2006.202
   Gruen M, 1999, J MOL BIOL, V286, P933, DOI 10.1006/jmbi.1998.2522
   Haining AWM, 2016, ACS NANO, V10, P6648, DOI 10.1021/acsnano.6b01658
   Harris SP, 2011, CIRC RES, V108, P751, DOI 10.1161/CIRCRESAHA.110.231670
   Heling LWHJ, 2020, J MUSCLE RES CELL M, V41, P91, DOI 10.1007/s10974-019-09567-1
   Helms AS, 2020, CIRC-GENOM PRECIS ME, V13, P396, DOI 10.1161/CIRCGEN.120.002929
   Helms AS, 2014, CIRC-CARDIOVASC GENE, V7, P434, DOI 10.1161/CIRCGENETICS.113.000448
   Huang J, 2017, NAT METHODS, V14, P71, DOI [10.1038/nmeth.4067, 10.1038/NMETH.4067]
   Hummer G, 2003, BIOPHYS J, V85, P5, DOI 10.1016/S0006-3495(03)74449-X
   HUTTER JL, 1993, REV SCI INSTRUM, V64, P1868, DOI 10.1063/1.1143970
   Irving TC, 2000, AM J PHYSIOL-HEART C, V279, pH2568, DOI 10.1152/ajpheart.2000.279.5.H2568
   Ito K, 2017, P NATL ACAD SCI USA, V114, P7689, DOI 10.1073/pnas.1707741114
   JORGENSEN WL, 1983, J CHEM PHYS, V79, P926, DOI 10.1063/1.445869
   Kampourakis T, 2014, P NATL ACAD SCI USA, V111, P18763, DOI 10.1073/pnas.1413922112
   Karsai A, 2013, BIOPHYS J, V104, P2465, DOI 10.1016/j.bpj.2013.04.027
   Karsai A, 2011, BIOPHYS J, V101, P1968, DOI 10.1016/j.bpj.2011.08.030
   Kelly SM, 2000, CURR PROTEIN PEPT SC, V1, P349, DOI 10.2174/1389203003381315
   Kosuri P, 2012, CELL, V151, P794, DOI 10.1016/j.cell.2012.09.036
   Krans LJ., 2010, Nature Education, V3, P66
   Leckband DE, 2014, ANNU REV CELL DEV BI, V30, P291, DOI 10.1146/annurev-cellbio-100913-013212
   Lee K, 2015, J MOL BIOL, V427, P274, DOI 10.1016/j.jmb.2014.10.023
   Lei H, 2017, J AM CHEM SOC, V139, P1538, DOI 10.1021/jacs.6b11371
   Li HB, 2002, NATURE, V418, P998, DOI 10.1038/nature00938
   Luther PK, 2011, P NATL ACAD SCI USA, V108, P11423, DOI 10.1073/pnas.1103216108
   MacKerell AD, 1998, J PHYS CHEM B, V102, P3586, DOI 10.1021/jp973084f
   Marston S, 2012, J MUSCLE RES CELL M, V33, P75, DOI 10.1007/s10974-011-9268-3
   Marston S, 2009, CIRC RES, V105, P219, DOI 10.1161/CIRCRESAHA.109.202440
   Marston SB, 2011, J CARDIOVASC TRANSL, V4, P245, DOI 10.1007/s12265-011-9266-2
   Marszalek PE, 1999, NATURE, V402, P100, DOI 10.1038/47083
   McGibbon RT, 2015, BIOPHYS J, V109, P1528, DOI 10.1016/j.bpj.2015.08.015
   McNamara JW, 2019, P NATL ACAD SCI USA, V116, P11731, DOI 10.1073/pnas.1821660116
   McNamara JW, 2017, PLOS ONE, V12, DOI 10.1371/journal.pone.0180064
   Michalek AJ, 2013, BIOPHYS J, V104, P442, DOI [10.1016/j.bpj.2012.10.021, 10.1016/j.bpj.2012.12.021]
   Moss RL, 2015, CIRC RES, V116, P183, DOI 10.1161/CIRCRESAHA.116.300561
   Mun JY, 2016, J MOL CELL CARDIOL, V91, P141, DOI 10.1016/j.yjmcc.2015.12.014
   Nag S, 2017, NAT STRUCT MOL BIOL, V24, P525, DOI 10.1038/nsmb.3408
   Nakamura F, 2011, CELL ADHES MIGR, V5, P160, DOI 10.4161/cam.5.2.14401
   Nunes JM, 2015, NAT COMMUN, V6, DOI 10.1038/ncomms7307
   O'Leary TS, 2019, J MOL CELL CARDIOL, V127, P165, DOI 10.1016/j.yjmcc.2018.12.003
   Olivotto I, 2020, LANCET, V396, P759, DOI 10.1016/S0140-6736(20)31792-X
   Parbhudayal RY, 2018, J MOL CELL CARDIOL, V123, P59, DOI 10.1016/j.yjmcc.2018.08.023
   Payton ME, 2003, J INSECT SCI, V3, DOI 10.1093/jis/3.1.34
   Pettersen EF, 2004, J COMPUT CHEM, V25, P1605, DOI 10.1002/jcc.20084
   Pfuhl M, 2012, J MUSCLE RES CELL M, V33, P83, DOI 10.1007/s10974-012-9291-z
   Pimenta-Lopes C, 2019, COMMUN PHYS-UK, V2, DOI 10.1038/s42005-019-0192-y
   Popa I, 2016, J AM CHEM SOC, V138, P10546, DOI 10.1021/jacs.6b05429
   Popa I, 2013, NAT PROTOC, V8, P1261, DOI 10.1038/nprot.2013.056
   Previs MJ, 2012, SCIENCE, V337, P1215, DOI 10.1126/science.1223602
   Previs MJ, 2014, PFLUG ARCH EUR J PHY, V466, P439, DOI 10.1007/s00424-013-1433-7
   Pricolo MR, 2020, J CARDIOVASC TRANSL, V13, P867, DOI 10.1007/s12265-020-09959-6
   Rivas-Pardo JA, 2016, CELL REP, V14, P1339, DOI 10.1016/j.celrep.2016.01.025
   Roma-Rodrigues C, 2014, APPL CLIN GENET, V7, P195, DOI 10.2147/TACG.S49126
   Sadayappan Sakthivel, 2012, Biophys Rev, V4, P93, DOI 10.1007/s12551-012-0067-x
   SANTORO MM, 1988, BIOCHEMISTRY-US, V27, P8063, DOI 10.1021/bi00421a014
   Sarkar SS, 2020, SCI ADV, V6, DOI 10.1126/sciadv.aax0069
   Schlierf M, 2004, P NATL ACAD SCI USA, V101, P7299, DOI 10.1073/pnas.0400033101
   Schlossarek S, 2011, CURR OPIN CARDIOL, V26, P190, DOI 10.1097/HCO.0b013e32834598fe
   Schreiber KH, 2013, CELL, V152, P1365, DOI 10.1016/j.cell.2013.02.015
   Schuldt M, 2021, CIRC-HEART FAIL, V14, P39, DOI 10.1161/CIRCHEARTFAILURE.120.007022
   Semsarian C, 2015, J AM COLL CARDIOL, V65, P1249, DOI 10.1016/j.jacc.2015.01.019
   Smelter DF, 2018, AM J PHYSIOL-HEART C, V314, pH1179, DOI 10.1152/ajpheart.00686.2017
   SMITH SB, 1992, SCIENCE, V258, P1122, DOI 10.1126/science.1439819
   Sommese RF, 2013, P NATL ACAD SCI USA, V110, P12607, DOI 10.1073/pnas.1309493110
   Spudich JA, 2001, NAT REV MOL CELL BIO, V2, P387, DOI 10.1038/35073086
   Squire J. M, 2016, GLOB CARDIOL SCI PRA, V2016, P11
   Suay-Corredera C., 2020, PROTEIN HAPLOINSUFFI, DOI [10.1101/2020.05.04.20087726v1, DOI 10.1101/2020.05.04.20087726V1]
   Suay-Corredera C., 2020, NANOMECHANICAL PHENO, DOI [10. 1101/2020.09.19.304618v1, DOI 10.1101/2020.09.19.304618V1]
   Teekakirikul P, 2019, BIOMOLECULES, V9, DOI 10.3390/biom9120878
   Toepfer CN, 2019, SCI TRANSL MED, V11, DOI 10.1126/scitranslmed.aat1199
   van Dijk SJ, 2016, ARCH BIOCHEM BIOPHYS, V601, P133, DOI 10.1016/j.abb.2016.01.006
   van Dijk SJ, 2009, CIRCULATION, V119, P1473, DOI 10.1161/CIRCULATIONAHA.108.838672
   Walcott S, 2015, BIOPHYS J, V108, P10, DOI 10.1016/j.bpj.2014.11.1852
   Walsh R, 2017, GENET MED, V19, P192, DOI 10.1038/gim.2016.90
   Walters J, 2009, METHOD ENZYMOL, V455, P1, DOI 10.1016/S0076-6879(08)04201-8
   Wang LT, 2017, EXP CELL RES, V355, P18, DOI 10.1016/j.yexcr.2017.03.025
   Watkins H, 2011, NEW ENGL J MED, V364, P1643, DOI 10.1056/NEJMra0902923
   Weith A, 2012, J MOL CELL CARDIOL, V52, P219, DOI 10.1016/j.yjmcc.2011.09.019
   Wijnker PJM, 2016, J MOL CELL CARDIOL, V97, P82, DOI 10.1016/j.yjmcc.2016.03.003
   Woody MS, 2019, ELIFE, V8, DOI 10.7554/eLife.49266
   Zhang XL, 2014, BIOCHEMISTRY-US, V53, P5332, DOI 10.1021/bi500784g
   Zheng P, 2011, J AM CHEM SOC, V133, P6791, DOI 10.1021/ja200715h
NR 111
TC 17
Z9 17
U1 1
U2 22
PU AMER CHEMICAL SOC
PI WASHINGTON
PA 1155 16TH ST, NW, WASHINGTON, DC 20036 USA
SN 1936-0851
EI 1936-086X
J9 ACS NANO
JI ACS Nano
PD JUN 22
PY 2021
VL 15
IS 6
BP 10203
EP 10216
DI 10.1021/acsnano.1c02242
EA JUN 2021
PG 14
WC Chemistry, Multidisciplinary; Chemistry, Physical; Nanoscience &
   Nanotechnology; Materials Science, Multidisciplinary
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Chemistry; Science & Technology - Other Topics; Materials Science
GA SY2UZ
UT WOS:000665748900087
PM 34060810
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Rossi, V
   Beffagna, G
   Rampazzo, A
   Bauce, B
   Danieli, GA
AF Rossi, V
   Beffagna, G
   Rampazzo, A
   Bauce, B
   Danieli, GA
TI TAIL1:: an isthmin-like gene, containing type 1
   thrombospondin-repeat and AMOP domain, mapped to ARVD1 critical region
SO GENE
LA English
DT Article
DE TSR; TATA-less; CpG island; glycoprotein; heart
ID SEQUENCE; PROTEINS; IDENTIFICATION; GLYCOPROTEIN; EXPRESSION;
   PREDICTION; HOMOLOGIES; PEPTIDES; ADHESION; MUTATION
AB Isthmins represent a novel family of vertebrate secreted proteins containing one copy of the thrombospondin type I repeat (TSR), which in mammals is shared by several proteins with diverse biological functions, including cell adhesion, angiogenesis, and patterning of developing nervous system. We have determined the genomic organization of human TAIL1 (thrombospondin and AMOP containing isthmin-like 1). a novel isthmin-like gene encoding a protein that contains a TSR and a C-terminal AMOP domain (adhesion-associated domain in NTUC4 and other proteins), characteristic of extracellular proteins involved in adhesion processes. TAIL1 gene encompasses more than 24.4 kb. Analysis of the DNA sequence surrounding the putative transcriptional start region revealed a TATA-less promoter located in a CpG island. Several consensus binding sites for the transcription factors Sp1 and MZF-1 were identified in this promoter region. In humans, TAIL1 gene is located on chromosome 14q24.3 within ARVD1 (arrhythmogenic right ventricular dysplasia/cardiomyopathy,. type 1) critical region; preliminary evidence suggests that it is expressed in several tissues, showing multiple alternative splicing. (C) 2004 Elsevier B.V. All rights reserved.
C1 Univ Padua, Dept Biol, I-35131 Padua, Italy.
   Univ Padua, Dept Cardiol, I-35131 Padua, Italy.
C3 University of Padua; University of Padua
RP Univ Padua, Dept Biol, Via U Bassi 58-B, I-35131 Padua, Italy.
EM vrossi@mail.bio.unipd.it
CR Adams JC, 2000, DEV DYNAM, V218, P280
   Adams JC, 2001, ANNU REV CELL DEV BI, V17, P25, DOI 10.1146/annurev.cellbio.17.1.25
   AKIYAMA Y, 1998, NUCLEIC ACIDS RES, V26, P364
   Aono S, 2000, J BIOL CHEM, V275, P337, DOI 10.1074/jbc.275.1.337
   Bateman A, 2004, NUCLEIC ACIDS RES, V32, pD138, DOI [10.1093/nar/gkr1065, 10.1093/nar/gkp985, 10.1093/nar/gkh121]
   Cheek Dennis J, 2003, J Cardiovasc Nurs, V18, P50
   Ciccarelli FD, 2002, TRENDS BIOCHEM SCI, V27, P113, DOI 10.1016/S0968-0004(01)02049-7
   Danieli GA, 2002, CURR OPIN CARDIOL, V17, P218, DOI 10.1097/00001573-200205000-00002
   Dawson DW, 1997, J CELL BIOL, V138, P707, DOI 10.1083/jcb.138.3.707
   DYNAN WS, 1986, NATURE, V319, P246, DOI 10.1038/319246a0
   Friedl P, 2002, CELL MOL LIFE SCI, V59, P1347, DOI 10.1007/s00018-002-8512-9
   Guo NH, 2000, CANCER RES, V60, P457
   Guo NH, 1997, CANCER RES, V57, P1735
   Hansen JE, 1998, GLYCOCONJUGATE J, V15, P115, DOI 10.1023/A:1006960004440
   Hromas R, 1996, CURR TOP MICROBIOL, V211, P159
   Hutter H, 2000, SCIENCE, V287, P989, DOI 10.1126/science.287.5455.989
   Ince TA, 1995, J BIOL CHEM, V270, P30249, DOI 10.1074/jbc.270.51.30249
   LAWLER J, 1986, J CELL BIOL, V103, P1635, DOI 10.1083/jcb.103.5.1635
   Letunic I, 2002, NUCLEIC ACIDS RES, V30, P242, DOI 10.1093/nar/30.1.242
   Nielsen H, 1997, PROTEIN ENG, V10, P1, DOI 10.1093/protein/10.1.1
   NOTHIAS JY, 1995, J BIOL CHEM, V270, P22077, DOI 10.1074/jbc.270.38.22077
   PATTHY L, 1988, J MOL BIOL, V202, P689, DOI 10.1016/0022-2836(88)90550-5
   Pera EM, 2002, MECH DEVELOP, V116, P169, DOI 10.1016/S0925-4773(02)00123-5
   PUGH BF, 1990, CELL, V61, P1187, DOI 10.1016/0092-8674(90)90683-6
   Rampazzo A, 2003, EUR J HUM GENET, V11, P69, DOI 10.1038/sj.ejhg.5200914
   Rampazzo A, 2002, AM J HUM GENET, V71, P1200, DOI 10.1086/344208
   RAMPAZZO A, 1994, HUM MOL GENET, V3, P959, DOI 10.1093/hmg/3.6.959
   ROGERS S, 1986, SCIENCE, V234, P364, DOI 10.1126/science.2876518
   RUBERTI F, 1994, J IMMUNOL METHODS, V173, P33, DOI 10.1016/0022-1759(94)90280-1
   Schultz J, 1998, P NATL ACAD SCI USA, V95, P5857, DOI 10.1073/pnas.95.11.5857
   SCHULTZCHERRY S, 1994, J BIOL CHEM, V269, P26783
   SHAPIRO MB, 1987, NUCLEIC ACIDS RES, V15, P7155, DOI 10.1093/nar/15.17.7155
   Sussman MA, 2002, CIRC RES, V91, P888, DOI 10.1161/01.RES.0000041680.43270.F8
   THOMPSON JD, 1994, NUCLEIC ACIDS RES, V22, P4673, DOI 10.1093/nar/22.22.4673
   Wengelnik K, 1999, EMBO J, V18, P5195, DOI 10.1093/emboj/18.19.5195
   Williams GW., 1998, NIX NUCLEOTIDE IDENT
NR 36
TC 13
Z9 15
U1 0
U2 2
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
SN 0378-1119
EI 1879-0038
J9 GENE
JI Gene
PD JUN 23
PY 2004
VL 335
BP 101
EP 108
DI 10.1016/j.gene.2004.03.008
PG 8
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA 834TR
UT WOS:000222434300009
PM 15194193
DA 2025-04-10
ER

PT J
AU Ishikawa, T
   Masuda, T
   Hachiya, T
   Dina, C
   Simonet, F
   Nagata, Y
   Tanck, MWT
   Sonehara, K
   Glinge, C
   Tadros, R
   Khongphatthanayothin, A
   Lu, TP
   Higuchi, C
   Nakajima, T
   Hayashi, K
   Aizawa, Y
   Nakano, Y
   Nogami, A
   Morita, H
   Ohno, S
   Aiba, T
   Juárez, CK
   Mauleekoonphairoj, J
   Poovorawan, Y
   Gourraud, JB
   Shimizu, W
   Probst, V
   Horie, M
   Wilde, AAM
   Redon, R
   Juang, JMJ
   Nademanee, K
   Bezzina, CR
   Barc, J
   Tanaka, T
   Okada, Y
   Schott, JJ
   Makita, N
AF Ishikawa, Taisuke
   Masuda, Tatsuo
   Hachiya, Tsuyoshi
   Dina, Christian
   Simonet, Floriane
   Nagata, Yuki
   Tanck, Michael W. T.
   Sonehara, Kyuto
   Glinge, Charlotte
   Tadros, Rafik
   Khongphatthanayothin, Apichai
   Lu, Tzu-Pin
   Higuchi, Chihiro
   Nakajima, Tadashi
   Hayashi, Kenshi
   Aizawa, Yoshiyasu
   Nakano, Yukiko
   Nogami, Akihiko
   Morita, Hiroshi
   Ohno, Seiko
   Aiba, Takeshi
   Juarez, Christian Krijger
   Mauleekoonphairoj, John
   Poovorawan, Yong
   Gourraud, Jean-Baptiste
   Shimizu, Wataru
   Probst, Vincent
   Horie, Minoru
   Wilde, Arthur A. M.
   Redon, Richard
   Juang, Jyh-Ming Jimmy
   Nademanee, Koonlawee
   Bezzina, Connie R.
   Barc, Julien
   Tanaka, Toshihiro
   Okada, Yukinori
   Schott, Jean-Jacques
   Makita, Naomasa
TI Brugada syndrome in Japan and Europe: a genome-wide association study
   reveals shared genetic architecture and new risk loci
SO EUROPEAN HEART JOURNAL
LA English
DT Article
DE Brugada syndrome; Genome-wide association studies; Cross-ancestry
   meta-analysis; SCN5A; Genetic risk score
ID HEART-RHYTHM-SOCIETY; LONG-TERM PROGNOSIS; NATURAL-HISTORY;
   ISCHEMIC-STROKE; VARIANTS; COMMON; MECHANISM; DISEASE
AB Background and Aims Brugada syndrome (BrS) is an inherited arrhythmia with a higher disease prevalence and more lethal arrhythmic events in Asians than in Europeans. Genome-wide association studies (GWAS) have revealed its polygenic architecture mainly in European populations. The aim of this study was to identify novel BrS-associated loci and to compare allelic effects across ancestries.Methods A GWAS was conducted in Japanese participants, involving 940 cases and 1634 controls, followed by a cross-ancestry meta-analysis of Japanese and European GWAS (total of 3760 cases and 11 635 controls). The novel loci were characterized by fine-mapping, gene expression, and splicing quantitative trait associations in the human heart.Results The Japanese-specific GWAS identified one novel locus near ZSCAN20 (P = 1.0 x 10-8), and the cross-ancestry meta-analysis identified 17 association signals, including six novel loci. The effect directions of the 17 lead variants were consistent (94.1%; P for sign test = 2.7 x 10-4), and their allelic effects were highly correlated across ancestries (Pearson's R = .91; P = 2.9 x 10-7). The genetic risk score derived from the BrS GWAS of European ancestry was significantly associated with the risk of BrS in the Japanese population [odds ratio 2.12 (95% confidence interval 1.94-2.31); P = 1.2 x 10-61], suggesting a shared genetic architecture across ancestries. Functional characterization revealed that a lead variant in CAMK2D promotes alternative splicing, resulting in an isoform switch of calmodulin kinase II-delta, favouring a pro-inflammatory/pro-death pathway.Conclusions This study demonstrates novel susceptibility loci implicating potentially novel pathogenesis underlying BrS. Despite differences in clinical expressivity and epidemiology, the polygenic architecture of BrS was substantially shared across ancestries.
   Structured Graphical Abstract Japanese-specific GWAS (940 cases and 1634 controls) followed by a cross-ancestry GWAS meta-analysis using Japanese (JPN) and European (EUR) populations (2820 cases and 10001 controls) have identified six novel BrS risk loci including CAMK2D and shared polygenic architectures across JPN and EUR. BrS, Brugada syndrome; GRS, genetic risk score; GWAS, genome-wide association study; LAE, lethal arrhythmic event; QTL, quantitative trait locus; sQTL, cis-splice quantitative trait locus.
C1 [Ishikawa, Taisuke] Natl Cerebral & Cardiovasc Ctr, Omics Res Ctr, Suita, Japan.
   [Masuda, Tatsuo; Sonehara, Kyuto; Okada, Yukinori] Osaka Univ, Grad Sch Med, Dept Stat Genet, Suita, Japan.
   [Masuda, Tatsuo] Osaka Univ, StemRIM Inst Regenerat Inducing Med, Grad Sch Med, Suita, Japan.
   [Masuda, Tatsuo] Osaka Univ, Grad Sch Med, Dept Obstet & Gynecol, Suita, Japan.
   [Hachiya, Tsuyoshi] Iwate Med Univ, Inst Biomed Sci, Morioka, Iwate, Japan.
   [Dina, Christian; Simonet, Floriane; Gourraud, Jean-Baptiste; Probst, Vincent; Redon, Richard; Barc, Julien; Schott, Jean-Jacques] Nantes Univ, CHU Nantes, Inst Thorax, CNRS,INSERM, Nantes, France.
   [Nagata, Yuki; Higuchi, Chihiro; Tanaka, Toshihiro] Tokyo Med & Dent Univ, Bioresource Res Ctr, Tokyo, Japan.
   [Nagata, Yuki; Tanaka, Toshihiro] Tokyo Med & Dent Univ, Dept Human Genet & Dis Divers, Tokyo, Japan.
   [Tanck, Michael W. T.] Univ Amsterdam, Amsterdam UMC Locat, Epidemiol & Data Sci, Amsterdam, Netherlands.
   [Sonehara, Kyuto; Okada, Yukinori] Univ Tokyo, Grad Sch Med, Dept Genome Informat, Tokyo, Japan.
   [Glinge, Charlotte; Tadros, Rafik; Juarez, Christian Krijger; Bezzina, Connie R.] Univ Amsterdam, Heart Ctr, Dept Expt Cardiol, Amsterdam UMC Locat, Amsterdam, Netherlands.
   [Glinge, Charlotte; Tadros, Rafik; Juarez, Christian Krijger; Wilde, Arthur A. M.; Bezzina, Connie R.] Amsterdam Cardiovasc Sci, Heart Failure & Arrhythmias, Amsterdam, Netherlands.
   [Glinge, Charlotte] Copenhagen Univ Hosp, Rigshosp, Heart Ctr, Dept Cardiol, Copenhagen, Denmark.
   [Glinge, Charlotte; Gourraud, Jean-Baptiste; Probst, Vincent; Bezzina, Connie R.; Barc, Julien; Schott, Jean-Jacques] European Reference Network Rare & Low Prevalence C, Amsterdam, Netherlands.
   [Tadros, Rafik] Univ Montreal, Montreal Heart Inst, Cardiovasc Genet Ctr, Montreal, PQ, Canada.
   [Khongphatthanayothin, Apichai; Nademanee, Koonlawee] Chulalongkorn Univ, Ctr Excellence Arrhythmia Res Fac Med, Dept Med, Bangkok, Thailand.
   [Khongphatthanayothin, Apichai] Chulalongkorn Univ, Div Cardiol Fac Med, Dept Pediat, Div Cardiol, Bangkok, Thailand.
   [Khongphatthanayothin, Apichai] Bangkok Hosp, Dept Cardiol, Bangkok, Thailand.
   [Lu, Tzu-Pin] Natl Taiwan Univ, Inst Hlth Data Analyt & Stat, Dept Publ Hlth, Taipei, Taiwan.
   [Higuchi, Chihiro] Natl Inst Biomed Innovat Hlth & Nutr, Artificial Intelligence Ctr Hlth & Biomed Res, Settsu, Japan.
   [Nakajima, Tadashi] Gunma Univ, Grad Sch Med, Dept Cardiovasc Med, Maebashi, Japan.
   [Hayashi, Kenshi] Kanazawa Univ, Grad Sch Med Sci, Dept Cardiovasc Med, Kanazawa, Japan.
   [Aizawa, Yoshiyasu] Int Univ Hlth & Welf, Dept Cardiovasc Med, Narita, Japan.
   [Nakano, Yukiko] Hiroshima Univ, Grad Sch Biomed & Hlth Sci, Dept Cardiovasc Med, Hiroshima, Japan.
   [Nogami, Akihiko] Univ Tsukuba, Dept Cardiol, Tsukuba, Japan.
   [Morita, Hiroshi] Okayama Univ, Fac Med Dent & Pharmaceut Sci, Dept Cardiovasc Therapeut, Okayama, Japan.
   [Ohno, Seiko] Natl Cerebral & Cardiovasc Ctr, Med Genome Ctr, Suita, Japan.
   [Ohno, Seiko; Horie, Minoru] Shiga Univ Med Sci, Dept Cardiovasc Med, Otsu, Japan.
   [Aiba, Takeshi] Natl Cerebral & Cardiovasc Ctr, Dept Cardiovasc Med, Suita, Japan.
   [Poovorawan, Yong] Chulalongkorn Univ, Fac Med, Ctr Excellence Clin Virol, Bangkok, Thailand.
   [Shimizu, Wataru] Nippon Med Sch, Dept Cardiovasc Med, Tokyo, Japan.
   [Wilde, Arthur A. M.] Univ Amsterdam, Heart Ctr, Amsterdam UMC Locat, Dept Cardiol, Amsterdam, Netherlands.
   [Juang, Jyh-Ming Jimmy] Natl Taiwan Univ Hosp, Cardiovasc Ctr, Heart Failure Ctr, Taipei, Taiwan.
   [Juang, Jyh-Ming Jimmy] Natl Taiwan Univ Hosp, Dept Internal Med, Div Cardiol, Taipei, Taiwan.
   [Juang, Jyh-Ming Jimmy] Natl Taiwan Univ, Coll Med, Dept Med, Taipei, Taiwan.
   [Nademanee, Koonlawee] Bumrungrad Int Hosp, Pacific Rim Electrophysiol Res Inst, Bangkok, Thailand.
   [Okada, Yukinori] RIKEN Ctr Integrat Med Sci, Lab Syst Genet, Yokohama, Kanagawa, Japan.
   [Okada, Yukinori] Osaka Univ, Immunol Frontier Res Ctr, Lab Stat Immunol, Suita, Japan.
   [Makita, Naomasa] Sapporo Teishinkai Hosp, Dept Cardiol, N33,E1, Sapporo 0650033, Japan.
   [Makita, Naomasa] Natl Cerebral & Cardiovasc Ctr Res Inst, Dept Cell Biol, 6-1 Kishibe Shimmachi, Suita 5648565, Japan.
C3 National Cerebral & Cardiovascular Center - Japan; The University of
   Osaka; The University of Osaka; The University of Osaka; Iwate Medical
   University; Institut National de la Sante et de la Recherche Medicale
   (Inserm); Centre National de la Recherche Scientifique (CNRS); Nantes
   Universite; CHU de Nantes; Institute of Science Tokyo; Tokyo Medical &
   Dental University (TMDU); Institute of Science Tokyo; Tokyo Medical &
   Dental University (TMDU); University of Amsterdam; University of Tokyo;
   University of Amsterdam; Rigshospitalet; University of Copenhagen;
   Copenhagen University Hospital; Universite de Montreal; Chulalongkorn
   University; Chulalongkorn University; National Taiwan University; Gunma
   University; Kanazawa University; International University of Health &
   Welfare; Hiroshima University; University of Tsukuba; Okayama
   University; National Cerebral & Cardiovascular Center - Japan; Shiga
   University of Medical Science; National Cerebral & Cardiovascular Center
   - Japan; Chulalongkorn University; Nippon Medical School; University of
   Amsterdam; National Taiwan University; National Taiwan University
   Hospital; National Taiwan University; National Taiwan University
   Hospital; National Taiwan University; RIKEN; The University of Osaka;
   National Cerebral & Cardiovascular Center - Japan
RP Makita, N (corresponding author), Sapporo Teishinkai Hosp, Dept Cardiol, N33,E1, Sapporo 0650033, Japan.; Makita, N (corresponding author), Natl Cerebral & Cardiovasc Ctr Res Inst, Dept Cell Biol, 6-1 Kishibe Shimmachi, Suita 5648565, Japan.
EM makitanaomasa@gmail.com
RI Tanck, Michael/AFY-1138-2022; ภู่วรวรรณ, ศนพ.ยง/GZK-8615-2022; Hachiya,
   Tsuyoshi/AAM-8691-2021; Aizawa, Yoshiyasu/L-8334-2013; Schott,
   jean-Jacques/F-8842-2013; Lu, Tzupin/ABC-2195-2021; probst,
   vincent/D-4996-2015; Redon, Richard/F-3303-2014; Shimizu,
   Wataru/IAM-9119-2023; Horie, Minoru/ABG-7128-2020; Simonet,
   Floriane/D-3538-2015; Gourraud, Jean baptiste/GSI-4249-2022; Ohno,
   Seiko/AEL-3289-2022; Dina, Christian/D-3535-2015; barc,
   julien/K-5495-2014; Glinge, Charlotte/C-4983-2018
OI Tadros, Rafik/0000-0002-1472-0258; Simonet,
   Floriane/0000-0002-6366-7211; Dina, Christian/0000-0002-7722-7348; barc,
   julien/0000-0003-4106-5946; Mauleekoonphairoj, John/0000-0001-7644-0940;
   Glinge, Charlotte/0000-0003-0406-256X
FU Japan Society for the Promotion of Science (JSPS) KAKENHI grant
   [CPD5Y-2022003-HF]; Sakakibara Heart Foundation Cardiovascular Research
   Program 2020; National Research Council of Thailand; Ministry of
   Education in Taiwan [JP22K08184]; Danish Cardiovascular Academy - Novo
   Nordisk Foundation [JP21H02888]; Danish Heart Foundation; JSPS KAKENHI
   grants [CVON 2018-30 292, ANR-GENSUD-14-CE10-0001]; Federation Francaise
   de Cardiologie (PREVENT project); Dutch Heart Foundation
   [RPH081-U1087-REG-PDL]; National Agency for Research [R21006NN];
   Research program Etoiles montantes des Pays de la Loire REGIOCARD
   [RPV21014NNA]; ANR JCJC LEARN [RISTRAD-661617, DEQ20140329545];
   H2020-MSCA-IF-2014 Program of the European Commission [22H00476];
   Foundation pour la Recherche Medicale [JP18KK0245]; IRP- VERACITIES-New
   Mechanisms for Ventricular Arrhythmia And CardIomeTabolic DiseasES, an
   I-SITE NexT health and engineering initiative (Ecole Centrale & Nantes
   University); IRP- GAINES-Genetic Architecture IN cardiovascular disEaSes
   - INSERM; CNRS; JSPS KAKENHI [JP18H02808, JP21H02920, JP21gm4010006,
   JP22km0405211]; AMED [JP22ek0410075, JP22km0405217, JP22ek0109594,
   JP223fa627002, JP223fa627010, JP233fa627011, JP17km0405109,
   JP21kk0305011, JPMJMS2021, JPMJMS2024]; JST Moonshot RD
   [JPJSBP220224403]; Takeda Science Foundation; Bioinformatics Initiative
   of Osaka University Graduate School of Medicine; Institute for Open and
   Transdisciplinary Research Initiatives; Center for Infectious Disease
   Education and Research (CiDER), Osaka University; JSPS Bilateral
   Program;  [JP20K08416];  [NTU-112L9004]; Grants-in-Aid for Scientific
   Research [21H02920] Funding Source: KAKEN
FX This work was supported by the Japan Society for the Promotion of
   Science (JSPS) KAKENHI grant (JP20K08416) and the Sakakibara Heart
   Foundation Cardiovascular Research Program 2020 to T.I. Furthermore,
   A.K., Y.P., and K.N. received a research grant from the National
   Research Council of Thailand. T.P.L. was supported by a grant
   (NTU-112L9004) from the Ministry of Education in Taiwan. C.G. received a
   research grant (CPD5Y-2022003-HF) from the Danish Cardiovascular
   Academy, which is funded by the Novo Nordisk Foundation and The Danish
   Heart Foundation. Y.N. and S.O. were supported by JSPS KAKENHI grants
   (JP22K08184 and JP21H02888, respectively). J.B.G. received a grant from
   the Federation Francaise de Cardiologie (PREVENT project). A.A.W. and
   C.R.B. were supported by the PREDICT2 project (CVON 2018-30 292) of the
   Dutch Heart Foundation. R.R. was supported by the National Agency for
   Research (ANR-GENSUD-14-CE10-0001). J.B. was supported by the research
   program Etoiles montantes des Pays de la Loire REGIOCARD
   RPH081-U1087-REG-PDL, ANR JCJC LEARN (R21006NN, RPV21014NNA), and the
   H2020-MSCA-IF-2014 Program of the European Commission (RISTRAD-661617).
   J.J.S. was supported by the Foundation pour la Recherche Medicale
   (DEQ20140329545), IRP- VERACITIES-New Mechanisms for Ventricular
   Arrhythmia And CardIomeTabolic DiseasES, an I-SITE NexT health and
   engineering initiative (Ecole Centrale & Nantes University), and the
   IRP- GAINES-Genetic Architecture IN cardiovascular disEaSes funded by
   INSERM and CNRS. Y.O. was supported by JSPS KAKENHI (22H00476), AMED
   (JP21gm4010006, JP22km0405211, JP22ek0410075, JP22km0405217,
   JP22ek0109594, JP223fa627002, JP223fa627010, and JP233fa627011), JST
   Moonshot R&D (JPMJMS2021 and JPMJMS2024), Takeda Science Foundation,
   Bioinformatics Initiative of Osaka University Graduate School of
   Medicine, Institute for Open and Transdisciplinary Research Initiatives,
   and the Center for Infectious Disease Education and Research (CiDER),
   Osaka University. N.M. was supported by grants from the AMED
   (JP17km0405109 and JP21kk0305011), JSPS KAKENHI grants (JP18KK0245,
   JP18H02808, and JP21H02920), and JSPS Bilateral Program
   (JPJSBP220224403).
CR Antzelevitch C, 2005, CIRCULATION, V111, P659, DOI 10.1161/01.CIR.0000152479.54298.51
   Barc J, 2022, NAT GENET, V54, P232, DOI 10.1038/s41588-021-01007-6
   Behr ER, 2021, EUR HEART J, V42, DOI 10.1093/eurheartj/ehaa1051
   Bers DM, 2008, ANNU REV PHYSIOL, V70, P23, DOI 10.1146/annurev.physiol.70.113006.100455
   Bezzina CR, 2013, NAT GENET, V45, P1044, DOI 10.1038/ng.2712
   Bezzina CR, 2006, CIRCULATION, V113, P338, DOI 10.1161/CIRCULATIONAHA.105.580811
   Brugada P, 2003, J CARDIOVASC ELECTR, V14, P455, DOI 10.1046/j.1540-8167.2003.02517.x
   Chen QY, 1998, NATURE, V392, P293, DOI 10.1038/32675
   Chong R, 2019, MOL CELL, V73, P183, DOI 10.1016/j.molcel.2018.10.037
   Eckardt L, 2005, CIRCULATION, V111, P257, DOI 10.1161/01.CIR.0000153267.21278.8D
   Evangelou E, 2013, NAT REV GENET, V14, P379, DOI 10.1038/nrg3472
   Hachiya T, 2020, STROKE, V51, P759, DOI 10.1161/STROKEAHA.119.027520
   Hachiya T, 2017, STROKE, V48, P253, DOI 10.1161/STROKEAHA.116.014506
   Hirata J, 2018, J INVEST DERMATOL, V138, P542, DOI 10.1016/j.jid.2017.10.001
   Hosseini SM, 2018, CIRCULATION, V138, P1195, DOI 10.1161/CIRCULATIONAHA.118.035070
   Ishikawa T, 2021, EUR HEART J, V42, P2854, DOI 10.1093/eurheartj/ehab254
   Jaganathan K, 2019, CELL, V176, P535, DOI 10.1016/j.cell.2018.12.015
   Juang JMJ, 2020, CIRC-GENOM PRECIS ME, V13, DOI 10.1161/CIRCGEN.119.002797
   Juang JMJ, 2015, J FORMOS MED ASSOC, V114, P620, DOI 10.1016/j.jfma.2013.02.002
   Little GH, 2009, J BIOL CHEM, V284, P24857, DOI 10.1074/jbc.M109.003186
   Lonsdale J, 2013, NAT GENET, V45, P580, DOI 10.1038/ng.2653
   Makarawate P, 2020, HEART RHYTHM, V17, P2145, DOI 10.1016/j.hrthm.2020.06.027
   Matsuo K, 2003, PACE, V26, P1551, DOI 10.1046/j.1460-9592.2003.t01-1-00227.x
   Milman A, 2019, HEART RHYTHM, V16, P1468, DOI 10.1016/j.hrthm.2019.07.003
   Milman A, 2018, HEART RHYTHM, V15, P1457, DOI 10.1016/j.hrthm.2018.06.019
   Mizusawa Y, 2012, CIRC-ARRHYTHMIA ELEC, V5, P606, DOI 10.1161/CIRCEP.111.964577
   Nademanee K, 2015, J AM COLL CARDIOL, V66, P1976, DOI 10.1016/j.jacc.2015.08.862
   Nielsen JB, 2018, NAT GENET, V50, P1234, DOI 10.1038/s41588-018-0171-3
   Ntalla I, 2020, NAT COMMUN, V11, DOI 10.1038/s41467-020-15706-x
   Prins BP, 2018, GENOME BIOL, V19, DOI 10.1186/s13059-018-1457-6
   Priori SG, 2002, CIRCULATION, V105, P1342, DOI 10.1161/hc1102.105288
   Priori SG, 2013, HEART RHYTHM, V10, P1932, DOI 10.1016/j.hrthm.2013.05.014
   Probst V, 2010, CIRCULATION, V121, P635, DOI 10.1161/CIRCULATIONAHA.109.887026
   Richards Sue, 2015, Genet Med, V17, P405, DOI 10.1038/gim.2015.30
   Ruan YF, 2022, NAT GENET, V54, P573, DOI 10.1038/s41588-022-01054-7
   Skene PJ, 2018, NAT PROTOC, V13, P1006, DOI 10.1038/nprot.2018.015
   So HC, 2011, GENET EPIDEMIOL, V35, P310, DOI 10.1002/gepi.20579
   van den Boogaard M, 2014, J CLIN INVEST, V124, P1844, DOI 10.1172/JCI73140
   Vutthikraiyit W, 2018, ACTA CARDIOL SIN, V34, P267, DOI 10.6515/ACS.201805_34(3).20180302B
   Wilde AAM, 2022, HEART RHYTHM, V19, pE1, DOI 10.1016/j.hrthm.2022.03.1225
   Xiong HY, 2015, SCIENCE, V347, DOI 10.1126/science.1254806
   Yamagata K, 2017, CIRCULATION, V135, P2255, DOI 10.1161/CIRCULATIONAHA.117.027983
   Yao Y, 2022, CIRC RES, V130, P887, DOI 10.1161/CIRCRESAHA.121.319478
   Zhang M, 2019, NAT CELL BIOL, V21, P1152, DOI 10.1038/s41556-019-0380-8
NR 44
TC 5
Z9 5
U1 1
U2 4
PU OXFORD UNIV PRESS
PI OXFORD
PA GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND
SN 0195-668X
EI 1522-9645
J9 EUR HEART J
JI Eur. Heart J.
PD MAY 15
PY 2024
VL 45
IS 26
SI SI
BP 2320
EP 2332
DI 10.1093/eurheartj/ehae251
EA MAY 2024
PG 13
WC Cardiac & Cardiovascular Systems
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology
GA YU0D4
UT WOS:001222910700001
PM 38747976
DA 2025-04-10
ER

PT J
AU Larsen, MC
   Lee, JW
   Jorgensen, JS
   Jefcoate, CR
AF Larsen, Michele Campaigne
   Lee, Jinwoo
   Jorgensen, Joan S.
   Jefcoate, Colin R.
TI STARD1 Functions in Mitochondrial Cholesterol Metabolism and Nascent HDL
   Formation. Gene Expression and Molecular mRNA Imaging Show Novel
   Splicing and a 1:1 Mitochondrial Association
SO FRONTIERS IN ENDOCRINOLOGY
LA English
DT Review
DE START proteins; cholesterol trafficking; SIK1; CRTC2; nascent HDL
   formation; sm-FISH
ID ACUTE REGULATORY PROTEIN; HORMONE-SENSITIVE LIPASE; RAT ADRENAL
   MITOCHONDRIA; KNOCKOUT MICE LACKING; LEYDIG TUMOR-CELLS;
   LUTEINIZING-HORMONE; ACUTE STIMULATION; PLASMA-MEMBRANE;
   STEROIDOGENESIS; TRANSPORT
AB STARD1 moves cholesterol (CHOL) from the outer mitochondrial membrane (OMM) to the inner membrane (IMM) in steroidogenic cells. This activity is integrated into CHOL trafficking and synthesis homeostasis, involving uptake through SR-B1 and LDL receptors and distribution through endosomes, ER, and lipid droplets. In adrenal cells, STARD1 is imported into the mitochondrial matrix accompanied by delivery of several hundred CHOL molecules. This transfer limits CYP11A1-mediated generation of pregnenolone. CHOL transfer is coupled to translation of STARD1 mRNA at the OMM. In testis cells, slower CHOL trafficking seems to be limiting. STARD1 also functions in a slower process through ER OMM contacts. The START domain of STARD1 is utilized by a family of genes, which includes additional STARD (forms 3-6) and GRAMD1B proteins that transfer CHOL. STARD forms 2 and 7 deliver phosphatidylcholine. STARD1 and STARD7 target their respective activities to mitochondria, via N-terminal domains (NTD) of over 50 amino acids. The NTD is not essential for steroidogenesis but exerts tissue-selective enhancement (testis>>adrenal). Three conserved sites for cleavage by the mitochondrial processing protease (MPP) generate three forms, each potentially with specific functions, as demonstrated in STARD7. STARD1 is expressed in macrophage and cardiac repair fibroblasts. Additional functions include CHOL metabolism by CYP27A1 that directs activation of LXR and CHOL export processes. STARD1 generates 3.5- and 1.6-kb mRNA from alternative polyadenylation. The 3.5-kb form exclusively binds the PKA-induced regulator, TIS11b, which binds at conserved sites in the extended 3'UTR to control mRNA translation and turnover. STARD1 expression also exhibits a novel, slow splicing that delayed splicing delivery of mRNA to mitochondria. Stimulation of transcription by PKA is directed by suppression of SIK forms that activate a CRTC/CREB/CBP promoter complex. This process is critical to pulsatile hormonal activation in vivo. sm-FISH RNA imaging shows a flow of single STARD1 mRNA particles from asymmetric accumulations of primary transcripts at gene loci to 1:1 complex of 3.5-kb mRNA with peri-nuclear mitochondria. Adrenal cells are similar but distinguished from testis cells by appreciable basal expression prior to hormonal activation. This difference is conserved in culture and in vivo.
C1 [Larsen, Michele Campaigne; Lee, Jinwoo; Jefcoate, Colin R.] Univ Wisconsin, Dept Cell & Regenerat Biol, Sch Med & Publ Hlth, Madison, WI 53706 USA.
   [Lee, Jinwoo; Jorgensen, Joan S.; Jefcoate, Colin R.] Univ Wisconsin, Endocrinol & Reprod Physiol Program, Sch Med & Publ Hlth, Madison, WI 53706 USA.
   [Jorgensen, Joan S.] Univ Wisconsin, Sch Vet Med, Dept Comparat Biosci, Madison, WI 53706 USA.
C3 University of Wisconsin System; University of Wisconsin Madison;
   University of Wisconsin System; University of Wisconsin Madison;
   University of Wisconsin System; University of Wisconsin Madison
RP Jefcoate, CR (corresponding author), Univ Wisconsin, Dept Cell & Regenerat Biol, Sch Med & Publ Hlth, Madison, WI 53706 USA.; Jefcoate, CR (corresponding author), Univ Wisconsin, Endocrinol & Reprod Physiol Program, Sch Med & Publ Hlth, Madison, WI 53706 USA.
EM jefcoate@wisc.edu
OI Larsen, Michele/0000-0001-7497-1510
FU National Institutes of Health [R01 HD090660]
FX This work was supported by the National Institutes of Health [grant
   number: R01 HD090660].
CR Aghazadeh Y, 2012, J BIOL CHEM, V287, P15380, DOI 10.1074/jbc.M112.339580
   Ai D, 2012, J CLIN INVEST, V122, P1262, DOI 10.1172/JCI61919
   Allen JA, 2006, ENDOCRINOLOGY, V147, P3924, DOI 10.1210/en.2005-1204
   Altarejos JY, 2011, NAT REV MOL CELL BIO, V12, P141, DOI 10.1038/nrm3072
   Amelio AL, 2009, EMBO J, V28, P2733, DOI 10.1038/emboj.2009.216
   Anuka E, 2013, MOL ENDOCRINOL, V27, P1502, DOI 10.1210/me.2013-1006
   Arakane F, 1997, J BIOL CHEM, V272, P32656, DOI 10.1074/jbc.272.51.32656
   Ariyoshi N, 1998, J BIOL CHEM, V273, P7610, DOI 10.1074/jbc.273.13.7610
   Artemenko IP, 2001, J BIOL CHEM, V276, P46583, DOI 10.1074/jbc.M107815200
   Baker BY, 2007, J BIOL CHEM, V282, P10223, DOI 10.1074/jbc.M611221200
   Bentley DL, 2014, NAT REV GENET, V15, P163, DOI 10.1038/nrg3662
   Blanc M, 2013, IMMUNITY, V38, P106, DOI 10.1016/j.immuni.2012.11.004
   Bose HS, 2002, NATURE, V417, P87, DOI 10.1038/417087a
   Castellano BM, 2017, SCIENCE, V355, P1306, DOI 10.1126/science.aag1417
   Castillo AF, 2015, MOL CELL ENDOCRINOL, V408, P73, DOI 10.1016/j.mce.2014.12.011
   Chen JJ, 2002, BIOL REPROD, V66, P1336, DOI 10.1095/biolreprod66.5.1336
   Cioni JM, 2019, CELL, V176, P56, DOI 10.1016/j.cell.2018.11.030
   Clark Barbara J., 2015, Biology-Basel, V4, P200, DOI 10.3390/biology4010200
   CLARK BJ, 1994, J BIOL CHEM, V269, P28314
   Clem BF, 2005, ENDOCRINOLOGY, V146, P1348, DOI 10.1210/en.2004-0761
   CRIVELLO JF, 1978, BIOCHIM BIOPHYS ACTA, V542, P315, DOI 10.1016/0304-4165(78)90027-2
   CRIVELLO JF, 1980, J BIOL CHEM, V255, P8144
   Cummins CL, 2006, J CLIN INVEST, V116, P1902, DOI 10.1172/JCI28400
   Daems C, 2015, ENDOCRINOLOGY, V156, P2693, DOI 10.1210/en.2014-1964
   Dai S, 2017, AUTOPHAGY, V13, P1435, DOI 10.1080/15548627.2017.1329081
   de Joussineau C, 2012, MOL CELL ENDOCRINOL, V351, P28, DOI 10.1016/j.mce.2011.10.006
   Desroches-Castan A, 2017, FRONT ENDOCRINOL, V8, DOI 10.3389/fendo.2017.00003
   DIBARTOLOMEIS MJ, 1984, J BIOL CHEM, V259, P159
   Doghman-Bouguerra M, 2016, EMBO REP, V17, P1264, DOI 10.15252/embr.201541504
   Dong JQ, 2019, NAT COMMUN, V10, DOI 10.1038/s41467-019-08791-0
   Du XM, 2011, J CELL BIOL, V192, P121, DOI 10.1083/jcb.201004142
   Duan HC, 2007, J MOL ENDOCRINOL, V38, P159, DOI 10.1677/jme.1.02153
   Duan H, 2009, MOL ENDOCRINOL, V23, P497, DOI 10.1210/me.2008-0296
   Duarte A, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0100387
   Dyson MT, 2008, BIOL REPROD, V78, P267, DOI 10.1095/biolreprod.107.064238
   Eid W, 2017, P NATL ACAD SCI USA, V114, P7999, DOI 10.1073/pnas.1705304114
   ELLIOTT ME, 1993, ENDOCRINOLOGY, V133, P1669, DOI 10.1210/en.133.4.1669
   Elustondo P, 2017, BBA-MOL CELL BIOL L, V1862, P90, DOI 10.1016/j.bbalip.2016.08.012
   Enyeart JJ, 2013, J GEN PHYSIOL, V142, P137, DOI 10.1085/jgp.201310964
   Fan JJ, 2015, P NATL ACAD SCI USA, V112, P7261, DOI 10.1073/pnas.1502670112
   Fielding CJ, 1997, J LIPID RES, V38, P1503
   Flippo KH, 2018, J NEUROSCI, V38, P8233, DOI 10.1523/JNEUROSCI.0649-18.2018
   França LR, 2016, ANDROLOGY-US, V4, P189, DOI 10.1111/andr.12165
   Gao FY, 2018, J CELL BIOL, V217, P2103, DOI 10.1083/jcb.201710078
   Gatliff J, 2012, CURR MOL MED, V12, P356
   Gatta AT, 2015, ELIFE, V4, DOI 10.7554/eLife.07253
   Gold VAM, 2017, EMBO REP, V18, P1786, DOI 10.15252/embr.201744261
   Golkowski M, 2016, CELL SIGNAL, V28, P764, DOI 10.1016/j.cellsig.2015.11.014
   Graham A, 2015, FREE RADICAL BIO MED, V89, P982, DOI 10.1016/j.freeradbiomed.2015.08.010
   Granot Z, 2002, ENDOCR RES, V28, P375, DOI 10.1081/ERC-120016812
   Granot Z, 2007, MOL ENDOCRINOL, V21, P2164, DOI 10.1210/me.2005-0458
   Grozdanov PN, 2012, MOL ENDOCRINOL, V26, P2104, DOI 10.1210/me.2012-1123
   HALL PF, 1979, J BIOL CHEM, V254, P9080
   Halpern KB, 2017, NATURE, V542, P352, DOI 10.1038/nature21065
   Halpern KB, 2015, CELL REP, V13, P2653, DOI 10.1016/j.celrep.2015.11.036
   Hanada K, 2018, J LIPID RES, V59, P2034, DOI 10.1194/jlr.R085324ERR
   HANUKOGLU I, 1981, J BIOL CHEM, V256, P4321, DOI 10.1016/S0021-9258(19)69436-6
   Hazell G, 2019, ENDOCRINOLOGY, V160, P587, DOI 10.1210/en.2018-00840
   Herzel L, 2018, GENOME RES, V28, P1008, DOI 10.1101/gr.232025.117
   Höglinger D, 2019, NAT COMMUN, V10, DOI 10.1038/s41467-019-12152-2
   Hu MC, 2002, MOL ENDOCRINOL, V16, P1943, DOI 10.1210/me.2002-0055
   Iaea DB, 2020, BBA-MOL CELL BIOL L, V1865, DOI 10.1016/j.bbalip.2020.158609
   Ikonen E, 2008, NAT REV MOL CELL BIO, V9, P125, DOI 10.1038/nrm2336
   Infante RE, 2017, ELIFE, V6, DOI 10.7554/eLife.25466
   Ishii T, 2002, MOL ENDOCRINOL, V16, P2297, DOI 10.1210/me.2001-0320
   Ishii T, 2012, ENDOCRINOLOGY, V153, P2714, DOI 10.1210/en.2011-1627
   Issop L, 2015, ENDOCRINOLOGY, V156, P334, DOI 10.1210/en.2014-1503
   Itoh K, 2018, J BIOL CHEM, V293, P11809, DOI 10.1074/jbc.RA117.001253
   Jacquemyn J, 2017, EMBO REP, V18, P1905, DOI 10.15252/embr.201643426
   Javitt NB, 2002, J LIPID RES, V43, P665
   Jefcoate C, 2002, J CLIN INVEST, V110, P881, DOI 10.1172/JCI200216771
   Jefcoate CR, 2006, J CLIN INVEST, V116, P1832, DOI 10.1172/JCI29160
   Jefcoate CR, 2018, J MOL ENDOCRINOL, V60, pR213, DOI 10.1530/JME-17-0281
   Jefcoate CR, 2011, MOL CELL ENDOCRINOL, V336, P53, DOI 10.1016/j.mce.2010.12.006
   JEFCOATE CR, 1975, J BIOL CHEM, V250, P4671
   JEFCOATE CR, 1973, ANN NY ACAD SCI, V212, P243, DOI 10.1111/j.1749-6632.1973.tb47600.x
   Johnson KA, 2019, J BIOL CHEM, V294, P17289, DOI 10.1074/jbc.RA119.010393
   Katahira J, 2015, GENES-BASEL, V6, P163, DOI 10.3390/genes6020163
   Kennedy BE, 2012, J LIPID RES, V53, P2632, DOI 10.1194/jlr.M029942
   King SR, 2012, FRONT BIOSCI-LANDMRK, V17, P824, DOI 10.2741/3959
   Kishida T, 2004, J BIOL CHEM, V279, P19276, DOI 10.1074/jbc.M400717200
   Korytowski W, 2015, ARTERIOSCL THROM VAS, V35, P2104, DOI 10.1161/ATVBAHA.115.306210
   KOWLURU R, 1995, MOL CELL ENDOCRINOL, V107, P181, DOI 10.1016/0303-7207(94)03441-U
   Kraemer FB, 2004, MOL ENDOCRINOL, V18, P549, DOI 10.1210/me.2003-0179
   Kraemer FB, 2017, MOL CELL ENDOCRINOL, V441, P17, DOI 10.1016/j.mce.2016.07.034
   Kraemer FB, 2013, MOL CELL ENDOCRINOL, V371, P15, DOI 10.1016/j.mce.2012.10.012
   Kwak H, 2013, SCIENCE, V339, P950, DOI 10.1126/science.1229386
   Lam M, 2018, MOL PHARMACOL, V93, P101, DOI 10.1124/mol.117.110742
   Lee J, 2017, FRONT ENDOCRINOL, V8, DOI 10.3389/fendo.2017.00289
   Lee J, 2017, MOL CELL ENDOCRINOL, V441, P22, DOI 10.1016/j.mce.2016.08.015
   Lee JW, 2016, FRONT ENDOCRINOL, V7, DOI 10.3389/fendo.2016.00107
   Lee J, 2016, MOL CELL ENDOCRINOL, V429, P93, DOI 10.1016/j.mce.2016.04.001
   Lee J, 2015, MOL CELL ENDOCRINOL, V408, P80, DOI 10.1016/j.mce.2015.01.022
   Létourneau D, 2015, MOL CELL ENDOCRINOL, V408, P53, DOI 10.1016/j.mce.2014.12.016
   Létourneau D, 2012, J LIPID RES, V53, P2677, DOI 10.1194/jlr.M031245
   Li Z, 2017, CIRCULATION, V136, P1315, DOI 10.1161/CIRCULATIONAHA.117.027462
   Lin Y, 2016, MOL ENDOCRINOL, V30, P234, DOI 10.1210/me.2015-1281
   Liu J, 2006, J BIOL CHEM, V281, P38879, DOI 10.1074/jbc.M608820200
   Liu Y, 2013, MOL CELL ENDOCRINOL, V371, P62, DOI 10.1016/j.mce.2012.10.011
   Luo LD, 1998, BIOL REPROD, V59, P263, DOI 10.1095/biolreprod59.2.263
   Ma WR, 2018, CELL, V175, P1492, DOI 10.1016/j.cell.2018.10.007
   Ma XL, 2018, J BIOL CHEM, V293, P14155, DOI 10.1074/jbc.RA118.001854
   Malik S, 2015, J BIOL CHEM, V290, P27972, DOI 10.1074/jbc.M115.668491
   Manna PR, 2015, BIOCHEM BIOPH RES CO, V464, P312, DOI 10.1016/j.bbrc.2015.06.150
   Manna PR, 2013, J BIOL CHEM, V288, P8505, DOI 10.1074/jbc.M112.417873
   Manna PR, 2009, MOL HUM REPROD, V15, P321, DOI 10.1093/molehr/gap025
   Marí M, 2014, REDOX BIOL, V3, P100, DOI 10.1016/j.redox.2014.09.005
   Martinot E, 2017, SCI REP-UK, V7, DOI 10.1038/srep42182
   Maxfield FR, 2002, J CLIN INVEST, V110, P891, DOI 10.1172/JCI200216500
   Maxfield FR, 2016, BIOCHEM CELL BIOL, V94, P499, DOI 10.1139/bcb-2015-0154
   Mayer A, 2017, CURR OPIN CELL BIOL, V46, P72, DOI 10.1016/j.ceb.2017.03.002
   McClelland KS, 2015, BIOL REPROD, V92, DOI 10.1095/biolreprod.115.128918
   Miller WL, 2017, J STEROID BIOCHEM, V165, P18, DOI 10.1016/j.jsbmb.2016.03.009
   Miller WL, 2011, J LIPID RES, V52, P2111, DOI 10.1194/jlr.R016675
   Morohaku K, 2014, ENDOCRINOLOGY, V155, P89, DOI 10.1210/en.2013-1556
   Murley A, 2017, J CELL BIOL, V216, P2679, DOI 10.1083/jcb.201610032
   Mutemberezi V, 2016, PROG LIPID RES, V64, P152, DOI 10.1016/j.plipres.2016.09.002
   Muzumdar MD, 2007, GENESIS, V45, P593, DOI 10.1002/dvg.20335
   Naito T, 2019, ELIFE, V8, DOI 10.7554/eLife.51401
   Nettebrock NT, 2020, BBA-MOL CELL BIOL L, V1865, DOI 10.1016/j.bbalip.2019.04.008
   O'Hara L, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0084541
   Ouimet M, 2019, CIRC RES, V124, P1505, DOI 10.1161/CIRCRESAHA.119.312617
   Owen DR, 2017, BIOCHEM J, V474, P3985, DOI 10.1042/BCJ20170648
   Pal R, 2016, AM J PHYSIOL-HEART C, V311, pH1392, DOI 10.1152/ajpheart.00463.2016
   Pandak William M, 2019, Liver Res, V3, P88, DOI 10.1016/j.livres.2019.05.001
   Papadopoulos V, 2015, MOL CELL ENDOCRINOL, V408, P90, DOI 10.1016/j.mce.2015.03.014
   Patel K, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms5535
   PAYNE AH, 1995, BIOL REPROD, V52, P217, DOI 10.1095/biolreprod52.2.217
   Paz C, 2016, FRONT ENDOCRINOL, V7, DOI 10.3389/fendo.2016.00060
   Pernas L, 2016, ANNU REV PHYSIOL, V78, P505, DOI 10.1146/annurev-physiol-021115-105011
   Pfisterer SG, 2016, CURR OPIN LIPIDOL, V27, P282, DOI 10.1097/MOL.0000000000000292
   PON LA, 1986, J BIOL CHEM, V261, P3309
   Prasad M, 2017, SCI ADV, V3, DOI 10.1126/sciadv.1602038
   Prasad M, 2016, MOL CELL BIOL, V36, P3058, DOI 10.1128/MCB.00411-16
   Prasad M, 2015, J BIOL CHEM, V290, P2604, DOI 10.1074/jbc.M114.605808
   Raniga K, 2018, VIRUSES-BASEL, V10, DOI 10.3390/v10010036
   Rebourcet D, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0105687
   Rodriguez-Agudo D, 2008, J LIPID RES, V49, P1409, DOI 10.1194/jlr.M700537-JLR200
   Rodriguez-Agudo D, 2019, J LIPID RES, V60, P1087, DOI 10.1194/jlr.M091967
   Rogala KB, 2019, SCIENCE, V366, P468, DOI 10.1126/science.aay0166
   Rone MB, 2012, MOL ENDOCRINOL, V26, P1868, DOI 10.1210/me.2012-1159
   Saita S, 2018, EMBO J, V37, DOI 10.15252/embj.201797909
   Sandhu J, 2018, CELL, V175, P514, DOI 10.1016/j.cell.2018.08.033
   Sasaki G, 2008, MOL ENDOCRINOL, V22, P951, DOI 10.1210/me.2007-0493
   Sasaki G, 2014, MOL ENDOCRINOL, V28, P1088, DOI 10.1210/me.2014-1028
   Sato TK, 2019, SCI REP-UK, V9, DOI 10.1038/s41598-019-44152-z
   Schimmer BP, 2007, MOL CELL ENDOCRINOL, V265, P102, DOI 10.1016/j.mce.2006.12.024
   Schrick K, 2014, BMC BIOL, V12, DOI 10.1186/s12915-014-0070-8
   Sèdes L, 2018, FRONT ENDOCRINOL, V9, DOI 10.3389/fendo.2018.00369
   Selvaraj V, 2020, FRONT ENDOCRINOL, V11, DOI 10.3389/fendo.2020.00472
   Sjöström M, 2007, P NATL ACAD SCI USA, V104, P16922, DOI 10.1073/pnas.0706838104
   Song MS, 2001, BIOCHEM J, V356, P151, DOI 10.1042/0264-6021:3560151
   Sonntag T, 2019, ISCIENCE, V11, P134, DOI 10.1016/j.isci.2018.12.012
   Sonntag T, 2018, FEBS J, V285, P467, DOI 10.1111/febs.14351
   Sorci-Thomas MG, 2016, CIRC RES, V118, P679, DOI 10.1161/CIRCRESAHA.115.306246
   Spiga F, 2015, J ENDOCRINOL, V226, pT55, DOI 10.1530/JOE-15-0132
   Stevenson J, 2016, ANNU REV NUTR, V36, P511, DOI 10.1146/annurev-nutr-071715-051030
   STOCCO DM, 1991, J BIOL CHEM, V266, P19731
   Szarek E, 2014, HORM METAB RES, V46, P863, DOI 10.1055/s-0034-1389916
   Szymanski J, 2017, INT J MOL SCI, V18, DOI 10.3390/ijms18071576
   Takemori H, 2008, J STEROID BIOCHEM, V108, P287, DOI 10.1016/j.jsbmb.2007.09.006
   Taub M, 2019, INT J MOL SCI, V20, DOI 10.3390/ijms20133219
   Thelen AM, 2017, TRENDS CELL BIOL, V27, P843, DOI 10.1016/j.tcb.2017.07.006
   Torres S, 2017, FRONT PHYSIOL, V8, DOI 10.3389/fphys.2017.00982
   Tsai LCL, 2011, CURR OPIN PHARMACOL, V11, P670, DOI 10.1016/j.coph.2011.09.003
   Tsujishita Y, 2000, NAT STRUCT BIOL, V7, P408
   Tu LN, 2016, ENDOCRINOLOGY, V157, P1110, DOI 10.1210/en.2015-1795
   Venugopal S, 2016, J BIOL CHEM, V291, P26109, DOI 10.1074/jbc.M116.740928
   Walther TC, 2017, ANNU REV CELL DEV BI, V33, P491, DOI 10.1146/annurev-cellbio-100616-060608
   Wang MQ, 2013, J ALLERGY CLIN IMMUN, V132, P1174, DOI 10.1016/j.jaci.2013.05.027
   Wein MN, 2019, TRENDS ENDOCRIN MET, V30, P407, DOI 10.1016/j.tem.2019.01.009
   Welte MA, 2017, BBA-MOL CELL BIOL L, V1862, P1260, DOI 10.1016/j.bbalip.2017.07.006
   Westerfield JM, 2020, J BIOL CHEM, V295, P1792, DOI 10.1074/jbc.REV119.009457
   Wilhelm LP, 2017, EMBO J, V36, P1412, DOI 10.15252/embj.201695917
   Wolfson RL, 2017, CELL METAB, V26, P301, DOI 10.1016/j.cmet.2017.07.001
   Xu BQ, 2017, ARTERIOSCL THROM VAS, V37, P2260, DOI 10.1161/ATVBAHA.117.310290
   Xu YF, 2018, MOL HUM REPROD, V24, P2, DOI 10.1093/molehr/gax061
   Xu YQ, 2019, J BIOL CHEM, V294, P19306, DOI 10.1074/jbc.RA119.011160
   YAMAZAKI T, 1995, ARCH BIOCHEM BIOPHYS, V318, P131, DOI 10.1006/abbi.1995.1213
   Yamazaki T, 2006, BBA-PROTEINS PROTEOM, V1764, P1561, DOI 10.1016/j.bbapap.2006.08.016
   Yang WH, 2009, MOL CELL BIOL, V29, P613, DOI 10.1128/MCB.00295-08
   Ye LP, 2017, FRONT PHYSIOL, V8, DOI 10.3389/fphys.2017.00430
   Yu SB, 2018, J MOL BIOL, V430, P3922, DOI 10.1016/j.jmb.2018.07.027
   Zhao D, 2005, J STEROID BIOCHEM, V96, P155, DOI 10.1016/j.jsbmb.2005.02.011
NR 184
TC 11
Z9 12
U1 1
U2 12
PU FRONTIERS MEDIA SA
PI LAUSANNE
PA AVENUE DU TRIBUNAL FEDERAL 34, LAUSANNE, CH-1015, SWITZERLAND
SN 1664-2392
J9 FRONT ENDOCRINOL
JI Front. Endocrinol.
PD OCT 20
PY 2020
VL 11
AR 559674
DI 10.3389/fendo.2020.559674
PG 29
WC Endocrinology & Metabolism
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism
GA OJ3BV
UT WOS:000583841100001
PM 33193082
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Miyazaki, T
AF Miyazaki, Takuro
TI Calpain and Cardiometabolic Diseases
SO INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
LA English
DT Review
DE alternative mRNA splicing; amino acids; inflammation; dyslipidemia;
   macrophages; nonalcoholic fatty liver disease (NAFLD); non-alcoholic
   steatohepatitis (NASH); regulatory T cells; vascular endothelial cells
ID FLUID-PHASE PINOCYTOSIS; STIMULATED GLUCOSE-UPTAKE; FOAM CELL-FORMATION;
   PROTEOLYTIC SYSTEMS; GENE POLYMORPHISMS; INSULIN-SECRETION; LYMPHATIC
   VESSELS; ADIPOSE-TISSUE; VE-CADHERIN; ATHEROSCLEROSIS
AB Calpain is defined as a member of the superfamily of cysteine proteases possessing the CysPC motif within the gene. Calpain-1 and -2, which are categorized as conventional isozymes, execute limited proteolysis in a calcium-dependent fashion. Accordingly, the calpain system participates in physiological and pathological phenomena, including cell migration, apoptosis, and synaptic plasticity. Recent investigations have unveiled the contributions of both conventional and unconventional calpains to the pathogenesis of cardiometabolic disorders. In the context of atherosclerosis, overactivation of conventional calpain attenuates the barrier function of vascular endothelial cells and decreases the immunosuppressive effects attributed to lymphatic endothelial cells. In addition, calpain-6 induces aberrant mRNA splicing in macrophages, conferring atheroprone properties. In terms of diabetes, polymorphisms of the calpain-10 gene can modify insulin secretion and glucose disposal. Moreover, conventional calpain reportedly participates in amino acid production from vascular endothelial cells to induce alteration of amino acid composition in the liver microenvironment, thereby facilitating steatohepatitis. Such multifaceted functionality of calpain underscores its potential as a promising candidate for pharmaceutical targets for the treatment of cardiometabolic diseases. Consequently, the present review highlights the pivotal role of calpains in the complications of cardiometabolic diseases and embarks upon a characterization of calpains as molecular targets.
C1 [Miyazaki, Takuro] Showa Univ, Sch Med, Dept Biochem, Tokyo 1428555, Japan.
C3 Showa University
RP Miyazaki, T (corresponding author), Showa Univ, Sch Med, Dept Biochem, Tokyo 1428555, Japan.
EM taku@pharm.showa-u.ac.jp
OI Miyazaki, Takuro/0000-0003-3354-0292
FU Japan Society for the Promotion of Science KAKENHI; Grants-in-Aid for
   Scientific Research [23K24777] Funding Source: KAKEN
FX No Statement Available
CR Akasu R, 2022, J BIOL CHEM, V298, DOI 10.1016/j.jbc.2022.101953
   Almeida SO, 2019, TRENDS CARDIOVAS MED, V29, P451, DOI 10.1016/j.tcm.2019.01.001
   Andrique C, 2018, JCI INSIGHT, V3, DOI 10.1172/jci.insight.121225
   Bäck M, 2019, NAT REV CARDIOL, V16, P389, DOI 10.1038/s41569-019-0169-2
   Baier LJ, 2000, J CLIN INVEST, V106, pR69, DOI 10.1172/JCI10665
   Bandaru S, 2019, CIRCULATION, V140, P67, DOI 10.1161/CIRCULATIONAHA.119.039697
   Barefield DY, 2019, J MOL CELL CARDIOL, V129, P236, DOI 10.1016/j.yjmcc.2019.03.006
   Bayramci NS, 2017, TURK J MED SCI, V47, P1568, DOI 10.3906/sag-1701-174
   Bedogni G, 2020, CURR OPIN LIPIDOL, V31, P27, DOI 10.1097/MOL.0000000000000652
   Björkegren JLM, 2022, CELL, V185, P1630, DOI 10.1016/j.cell.2022.04.004
   Bobryshev YV, 1999, CARDIOVASC RES, V43, P1003, DOI 10.1016/S0008-6363(99)00125-X
   Brown AE, 2007, MOL GENET METAB, V91, P318, DOI 10.1016/j.ymgme.2007.05.001
   Brown E, 2021, LANCET, V398, P262, DOI 10.1016/S0140-6736(21)00536-5
   Brunner KT, 2019, CURR OBES REP, V8, P220, DOI 10.1007/s13679-019-00345-1
   Buono C, 2009, J CLIN INVEST, V119, P1373, DOI 10.1172/JCI35548
   Cassell PG, 2002, DIABETES, V51, P1622, DOI 10.2337/diabetes.51.5.1622
   Chisolm GM, 2000, FREE RADICAL BIO MED, V28, P1815, DOI 10.1016/S0891-5849(00)00344-0
   Dear N, 1997, GENOMICS, V45, P175, DOI 10.1006/geno.1997.4870
   Elbein SC, 2002, J CLIN ENDOCR METAB, V87, P650, DOI 10.1210/jc.87.2.650
   Engelbrecht E, 2021, ARTERIOSCL THROM VAS, V41, P564, DOI 10.1161/ATVBAHA.120.305565
   Evans JC, 2001, AM J HUM GENET, V69, P544, DOI 10.1086/323315
   Fiehn O, 2010, PLOS ONE, V5, DOI 10.1371/journal.pone.0015234
   Flores-Toro J, 2021, CELLS-BASEL, V10, DOI 10.3390/cells10081863
   Foteinos G, 2008, CIRCULATION, V117, P1856, DOI 10.1161/CIRCULATIONAHA.107.746008
   Friedrich EE, 2019, P NATL ACAD SCI USA, V116, P12980, DOI 10.1073/pnas.1902165116
   Garant MJ, 2002, DIABETES, V51, P231, DOI 10.2337/diabetes.51.1.231
   Goll DE, 2003, PHYSIOL REV, V83, P731, DOI 10.1152/physrev.00029.2002
   Guan LC, 2023, J CELL MOL MED, V27, P232, DOI 10.1111/jcmm.17642
   Guo XW, 2021, FRONT MOL BIOSCI, V8, DOI 10.3389/fmolb.2021.725274
   Gustafson B, 2010, J ATHEROSCLER THROMB, V17, P332, DOI 10.5551/jat.3939
   Gutiérrez-Cuevas J, 2021, INT J MOL SCI, V22, DOI 10.3390/ijms222111629
   Hatta T, 2018, SCI REP-UK, V8, DOI 10.1038/s41598-018-35204-x
   Hegele RA, 2001, DIABETES CARE, V24, P1498, DOI 10.2337/diacare.24.8.1498-a
   Higuchi M, 2012, FASEB J, V26, P1204, DOI 10.1096/fj.11-187740
   Hong JM, 2011, J BONE MINER RES, V26, P657, DOI 10.1002/jbmr.241
   Horikawa Y, 2000, NAT GENET, V26, P163, DOI 10.1038/79876
   Jang YN, 2009, J NEUROSCI, V29, P5974, DOI 10.1523/JNEUROSCI.6178-08.2009
   Karambataki M, 2017, BIOMED REP, V6, P146, DOI 10.3892/br.2016.833
   Kruth HS, 2013, CURR PHARM DESIGN, V19, P5865
   Kruth HS, 2011, CURR OPIN LIPIDOL, V22, P386, DOI 10.1097/MOL.0b013e32834adadb
   Kruth HS, 2005, J BIOL CHEM, V280, P2352, DOI 10.1074/jbc.M407167200
   Kutkut I, 2015, EUR J CLIN INVEST, V45, P100, DOI 10.1111/eci.12372
   Le Couteur DG, 2020, AGEING RES REV, V64, DOI 10.1016/j.arr.2020.101198
   Lim HY, 2013, CELL METAB, V17, P671, DOI 10.1016/j.cmet.2013.04.002
   Ling C, 2009, PLOS ONE, V4, DOI 10.1371/journal.pone.0006558
   Lynn S, 2002, DIABETES, V51, P247, DOI 10.2337/diabetes.51.1.247
   MAKI M, 1987, FEBS LETT, V223, P174, DOI 10.1016/0014-5793(87)80531-8
   Martel C, 2013, J CLIN INVEST, V123, P1571, DOI 10.1172/JCI63685
   Marton A, 2021, NAT REV NEPHROL, V17, P65, DOI 10.1038/s41581-020-00350-x
   Matsumoto T, 2007, CURR MED CHEM, V14, P3209, DOI 10.2174/092986707782793899
   Mehta D, 2006, PHYSIOL REV, V86, P279, DOI 10.1152/physrev.00012.2005
   Miyazaki T, 2023, ARTERIOSCL THROM VAS, V43, pE66, DOI 10.1161/ATVBAHA.122.317781
   Miyazaki T, 2021, FRONT CARDIOVASC MED, V8, DOI 10.3389/fcvm.2021.701229
   Miyazaki T, 2021, CURR PHARM DESIGN, V27, P3128, DOI 10.2174/1381612827666210311143053
   Miyazaki T, 2020, INFLAMM REGEN, V40, DOI 10.1186/s41232-020-00114-x
   Miyazaki T, 2019, FASEB J, V33, P2037, DOI 10.1096/fj.201800588RR
   Miyazaki T, 2018, J ATHEROSCLER THROMB, V25, P1, DOI 10.5551/jat.RV17008
   Miyazaki T, 2017, FRONT CARDIOVASC MED, V4, DOI 10.3389/fcvm.2017.00079
   Miyazaki T, 2017, CELL MOL LIFE SCI, V74, P3011, DOI 10.1007/s00018-017-2528-7
   Miyazaki T, 2016, J CLIN INVEST, V126, P3417, DOI 10.1172/JCI85880
   Miyazaki T, 2015, CIRC RES, V116, P1170, DOI 10.1161/CIRCRESAHA.116.305363
   Miyazaki T, 2011, CIRCULATION, V124, P2522, DOI 10.1161/CIRCULATIONAHA.111.021675
   Miyazaki T, 2019, CURR MED CHEM, V26, P1631, DOI 10.2174/0929867325666180326165234
   Moore KJ, 2013, NAT REV IMMUNOL, V13, P709, DOI 10.1038/nri3520
   Morales-Corraliza J, 2012, NEUROBIOL AGING, V33, DOI 10.1016/j.neurobiolaging.2011.11.023
   Mueller P, 2015, EXP CELL RES, V333, P190, DOI 10.1016/j.yexcr.2015.03.016
   Muniappan L, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-14719-9
   Muzurovic E, 2022, HYPERTENSION, V79, P1319, DOI 10.1161/HYPERTENSIONAHA.122.17982
   Nam TG, 2011, TOX RESEARCH, V27, P1, DOI 10.5487/TR.2011.27.1.001
   Newgard CB, 2017, CELL METAB, V25, P43, DOI 10.1016/j.cmet.2016.09.018
   O'Sullivan JW, 2023, EUR HEART J, V44, P89, DOI 10.1093/eurheartj/ehac648
   Obata T, 2007, DIABETES, V56, P2028, DOI 10.2337/db07-0394
   Oesterle A, 2017, CIRC RES, V120, P229, DOI 10.1161/CIRCRESAHA.116.308537
   Ogata H, 2022, EXPERT OPIN DRUG SAF, V21, P947, DOI 10.1080/14740338.2022.2044472
   Ono Y, 2016, NAT REV DRUG DISCOV, V15, P854, DOI 10.1038/nrd.2016.212
   Ono Y, 2012, BBA-PROTEINS PROTEOM, V1824, P224, DOI 10.1016/j.bbapap.2011.08.005
   Onodera J, 2005, J BIOL CHEM, V280, P31582, DOI 10.1074/jbc.M506736200
   Paul DS, 2003, BIOCHEM J, V376, P625, DOI 10.1042/BJ20030681
   Rademakers T, 2017, SCI REP-UK, V7, DOI 10.1038/srep45263
   Ridker PM, 2017, NEW ENGL J MED, V377, P1119, DOI 10.1056/NEJMoa1707914
   Rios-Doria J, 2003, J BIOL CHEM, V278, P1372, DOI 10.1074/jbc.M208772200
   Ross R, 1999, NEW ENGL J MED, V340, P115, DOI 10.1056/NEJM199901143400207
   Sarnak MJ, 2019, J AM COLL CARDIOL, V74, P1823, DOI 10.1016/j.jacc.2019.08.1017
   Sato H, 2016, INFLAMM REGEN, V36, DOI 10.1186/s41232-016-0012-7
   Sato K, 2011, J NEUROCHEM, V117, P504, DOI 10.1111/j.1471-4159.2011.07222.x
   Sato Toshifumi, 2023, Matrix Biol Plus, V17, P100127, DOI 10.1016/j.mbplus.2022.100127
   Sattar N, 2020, NAT MED, V26, P320, DOI 10.1038/s41591-020-0786-7
   Seachrist JL, 2003, LIFE SCI, V74, P225, DOI 10.1016/j.lfs.2003.09.009
   Seike T, 2022, CELL MOL GASTROENTER, V14, P925, DOI 10.1016/j.jcmgh.2022.06.008
   Shinkai-Ouchi F, 2016, MOL CELL PROTEOMICS, V15, P1262, DOI 10.1074/mcp.M115.053413
   Sreenan SK, 2001, DIABETES, V50, P2013, DOI 10.2337/diabetes.50.9.2013
   Steckelberg AL, 2015, NUCLEIC ACIDS RES, V43, P4687, DOI 10.1093/nar/gkv320
   Steckelberg AL, 2012, CELL REP, V2, P454, DOI 10.1016/j.celrep.2012.08.017
   STEINBRECHER UP, 1992, ARTERIOSCLER THROMB, V12, P608, DOI 10.1161/01.ATV.12.5.608
   Stumvoll M, 2001, DIABETES, V50, P2161, DOI 10.2337/diabetes.50.9.2161
   Su WJ, 2017, MOL BIOL CELL, V28, P76, DOI 10.1091/mbc.E16-09-0658
   Sun XD, 2020, BIOMED PHARMACOTHER, V124, DOI 10.1016/j.biopha.2020.109822
   Suraweera A, 2012, MOL CELL, V48, P242, DOI 10.1016/j.molcel.2012.08.003
   TAKANO E, 1982, J BIOCHEM, V92, P2021, DOI 10.1093/oxfordjournals.jbchem.a134134
   Targher G, 2023, LANCET GASTROENTEROL, V8, P179, DOI 10.1016/S2468-1253(22)00338-7
   Teng XM, 2019, DIABETOLOGIA, V62, P860, DOI 10.1007/s00125-019-4828-y
   Tomita T, 2020, NAT COMMUN, V11, DOI 10.1038/s41467-020-16003-3
   Tonami K, 2013, PLOS GENET, V9, DOI 10.1371/journal.pgen.1003668
   Tonami K, 2011, J CELL SCI, V124, P1214, DOI 10.1242/jcs.072561
   Turner MD, 2007, BIOCHEM BIOPH RES CO, V352, P650, DOI 10.1016/j.bbrc.2006.11.077
   Uno K, 2015, NAT COMMUN, V6, DOI 10.1038/ncomms8940
   Weber JJ, 2018, NEUROPHARMACOLOGY, V133, P94, DOI 10.1016/j.neuropharm.2018.01.022
   White PJ, 2019, SCIENCE, V363, P582, DOI 10.1126/science.aav0558
   Woodward LA, 2017, WIRES RNA, V8, DOI 10.1002/wrna.1411
   Xu H, 2021, FOOD SCI NUTR, V9, P367, DOI 10.1002/fsn3.2002
   Yang XY, 2016, CAN J PHYSIOL PHARM, V94, P1336, DOI 10.1139/cjpp-2016-0295
   Yin MH, 2017, J VASC RES, V54, P123, DOI 10.1159/000464288
   Yu L, 2018, CAN J PHYSIOL PHARM, V96, P60, DOI 10.1139/cjpp-2016-0652
   Yu QW, 2021, MOL MED REP, V24, DOI 10.3892/mmr.2021.12314
   Yuasa T, 2021, BMJ OPEN DIAB RES CA, V9, DOI 10.1136/bmjdrc-2021-002467
   Yuasa T, 2016, DIABETOLOGIA, V59, P2711, DOI 10.1007/s00125-016-4102-5
   Zheng D, 2021, ACTA PHARMACOL SIN, V42, P909, DOI 10.1038/s41401-020-00526-y
   Zhou YP, 2003, METABOLISM, V52, P528, DOI 10.1053/meta.2003.50091
NR 118
TC 5
Z9 5
U1 0
U2 2
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
SN 1661-6596
EI 1422-0067
J9 INT J MOL SCI
JI Int. J. Mol. Sci.
PD DEC
PY 2023
VL 24
IS 23
AR 16782
DI 10.3390/ijms242316782
PG 20
WC Biochemistry & Molecular Biology; Chemistry, Multidisciplinary
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Chemistry
GA AE4X2
UT WOS:001116785300001
PM 38069105
OA gold
DA 2025-04-10
ER

PT J
AU Stamova, B
   Ander, BP
   Jickling, G
   Hamade, F
   Durocher, M
   Zhan, XH
   Liu, D
   Cheng, XY
   Hull, H
   Yee, A
   Ng, K
   Shroff, N
   Sharp, FR
AF Stamova, Boryana
   Ander, Bradley P.
   Jickling, Glen
   Hamade, Farah
   Durocher, Marc
   Zhan, Xinhua
   Liu, Da Zhi
   Cheng, Xiyuan
   Hull, Heather
   Yee, Alan
   Ng, Kwan
   Shroff, Natasha
   Sharp, Frank R.
TI The intracerebral hemorrhage blood transcriptome in humans differs from
   the ischemic stroke and vascular risk factor control blood
   transcriptomes
SO JOURNAL OF CEREBRAL BLOOD FLOW AND METABOLISM
LA English
DT Article
DE Alternative splicing; angiogenesis; intracerebral hemorrhage; ischemic
   stroke; T-cell receptors
ID TO-LYMPHOCYTE RATIO; GENE-EXPRESSION; INFLAMMATORY INJURY; MICROGLIA
   ACTIVATION; IMMUNE-SYSTEM; BRAIN-BARRIER; NEUTROPHIL; VIMENTIN; CELLS;
   MECHANISMS
AB Understanding how the blood transcriptome of human intracerebral hemorrhage (ICH) differs from ischemic stroke (IS) and matched controls (CTRL) will improve understanding of immune and coagulation pathways in both disorders. This study examined RNA from 99 human whole-blood samples using GeneChip (R) HTA 2.0 arrays to assess differentially expressed transcripts of alternatively spliced genes between ICH, IS and CTRL. We used a mixed regression model with FDR-corrected p(Dx) < 0.2 and p < 0.005 and |FC| > 1.2 for individual comparisons. For time-dependent analyses, subjects were divided into four time-points: 0(CTRL), <24 h, 24-48 h, >48 h; 489 transcripts were differentially expressed between ICH and CTRL, and 63 between IS and CTRL. ICH had differentially expressed T-cell receptor and CD36 genes, and iNOS, TLR, macrophage, and T-helper pathways. IS had more non-coding RNA. ICH and IS both had angiogenesis, CTLA4 in T lymphocytes, CD28 in T helper cells, NFAT regulation of immune response, and glucocorticoid receptor signaling pathways. Self-organizing maps revealed 4357 transcripts changing expression over time in ICH, and 1136 in IS. Understanding ICH and IS transcriptomes will be useful for biomarker development, treatment and prevention strategies, and for evaluating how well animal models recapitulate human ICH and IS.
C1 [Stamova, Boryana; Ander, Bradley P.; Jickling, Glen; Hamade, Farah; Durocher, Marc; Zhan, Xinhua; Liu, Da Zhi; Cheng, Xiyuan; Hull, Heather; Yee, Alan; Ng, Kwan; Shroff, Natasha; Sharp, Frank R.] Univ Calif Davis, Sch Med, Dept Neurol, 2805 50th St, Sacramento, CA 95817 USA.
   [Jickling, Glen] Univ Alberta, Dept Med, Edmonton, AB, Canada.
C3 University of California System; University of California Davis;
   University of Alberta
RP Stamova, B (corresponding author), Univ Calif Davis, Sch Med, Dept Neurol, 2805 50th St, Sacramento, CA 95817 USA.; Stamova, B (corresponding author), Mind Inst Biosci, 2805 50th St, Sacramento, CA 95817 USA.
EM bsstamova@ucdavis.edu
RI Yee, Alan/AAH-4604-2019; Jickling, Glen/J-8790-2019; Stamova,
   Boryana/ABA-2981-2020
OI Jickling, Glen/0000-0003-3543-0820; Stamova, Boryana/0000-0002-5440-8816
FU American Heart Association; National Institutes of Health/National
   Institute of Neurological Disorders and Stroke [NS079153, NS075035,
   NS097000, NS101718]; American Heart Association Fellow
FX The author(s) disclosed receipt of the following financial support for
   the research, authorship, and/or publication of this article: These
   studies were supported by American Heart Association grants to Stamova
   and Liu, an American Heart Association Fellow to Faculty award to
   Jickling, and National Institutes of Health/National Institute of
   Neurological Disorders and Stroke grants to Sharp, Jickling, Stamova and
   Ander (NS079153, NS075035, NS097000, NS101718).
CR Adeoye O, 2014, J STROKE CEREBROVASC, V23, pE107, DOI 10.1016/j.jstrokecerebrovasdis.2013.09.006
   Agnihotri S, 2011, J NEUROINFLAMM, V8, DOI 10.1186/1742-2094-8-160
   [Anonymous], 2000, Statistics and Data Analysis from Elementary to Intermediate
   Asano S, 2016, CURR OPIN PHARMACOL, V26, P80, DOI 10.1016/j.coph.2015.10.004
   Benjamin EJ, 2017, CIRCULATION, V135, pE146, DOI [10.1161/CIR.0000000000000558, 10.1161/CIR.0000000000000485, 10.1161/CIR.0000000000000530]
   Boilard E, 2003, BLOOD, V102, P2901, DOI 10.1182/blood-2002-12-3702
   Chamorro A, 2012, NAT REV NEUROL, V8, P401, DOI 10.1038/nrneurol.2012.98
   Dykstra-Aiello C, 2016, STROKE, V47, P2896, DOI 10.1161/STROKEAHA.116.013869
   Fujimura M, 2016, FRONT NEUROL NEUROSC, V40, P204, DOI 10.1159/000448314
   Gamazon ER, 2014, HUM GENET, V133, P679, DOI 10.1007/s00439-013-1411-3
   Gu LJ, 2015, NEUROCHEM RES, V40, P1786, DOI 10.1007/s11064-015-1676-0
   Gusdon AM, 2017, STROKE, V48, P2589, DOI 10.1161/STROKEAHA.117.018120
   Hammond MD, 2012, TRANSL STROKE RES, V3, pS125, DOI 10.1007/s12975-012-0174-9
   Hu JZ, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0149537
   Iadecola C, 2011, NAT MED, V17, P796, DOI 10.1038/nm.2399
   Janeway C.A., 2001, Immunology: the immune system in health and disease, V5th
   Jiang SX, 2012, J NEUROCHEM, V122, P764, DOI 10.1111/j.1471-4159.2012.07823.x
   Jickling GC, 2014, J CEREBR BLOOD F MET, V34, P185, DOI 10.1038/jcbfm.2013.203
   Jickling GC, 2013, ANN NEUROL, V74, P232, DOI 10.1002/ana.23883
   Keep RF, 2014, FLUIDS BARRIERS CNS, V11, DOI 10.1186/2045-8118-11-18
   Keep RF, 2012, LANCET NEUROL, V11, P720, DOI 10.1016/S1474-4422(12)70104-7
   KINDY MS, 1992, MOL BRAIN RES, V13, P199, DOI 10.1016/0169-328X(92)90027-9
   Kohonen T, 2000, IEEE IJCNN, P3, DOI 10.1109/IJCNN.2000.857865
   Landskroner-Eiger S, 2013, CSH PERSPECT MED, V3, DOI 10.1101/cshperspect.a006643
   Lattanzi S, 2016, STROKE, V47, P1654, DOI 10.1161/STROKEAHA.116.013627
   Lei C, 2013, NEUROSCIENCE, V229, P12, DOI 10.1016/j.neuroscience.2012.10.054
   Levin EC, 2009, BRAIN RES, V1298, P194, DOI 10.1016/j.brainres.2009.08.072
   Li QJ, 2007, CELL, V129, P147, DOI 10.1016/j.cell.2007.03.008
   Luco RF, 2011, CELL, V144, P16, DOI 10.1016/j.cell.2010.11.056
   Lynch KW, 2004, NAT REV IMMUNOL, V4, P931, DOI 10.1038/nri1497
   Mackenzie J M, 1999, J Stroke Cerebrovasc Dis, V8, P1, DOI 10.1016/S1052-3057(99)80032-9
   Macrez R, 2011, LANCET NEUROL, V10, P471, DOI 10.1016/S1474-4422(11)70066-7
   Mao LL, 2017, CELL MOL NEUROBIOL, V37, P919, DOI 10.1007/s10571-016-0429-1
   Martinez NM, 2013, IMMUNOL REV, V253, P216, DOI 10.1111/imr.12047
   Mehndiratta P, 2012, NEUROSURG FOCUS, V32, DOI 10.3171/2012.1.FOCUS11370
   Mehta A, 2016, NAT REV IMMUNOL, V16, P279, DOI 10.1038/nri.2016.40
   Meller R, 2016, ANN CLIN TRANSL NEUR, V3, P70, DOI 10.1002/acn3.272
   Moisan E, 2006, J LEUKOCYTE BIOL, V79, P489, DOI 10.1189/jlb.0405190
   Moore DF, 2005, CIRCULATION, V111, P212, DOI 10.1161/01.CIR.0000152105.79665.C6
   Mor-Vaknin N, 2003, NAT CELL BIOL, V5, P59, DOI 10.1038/ncb898
   Morotti A, 2016, STROKE, V47, P1473, DOI 10.1161/STROKEAHA.116.013176
   Mouchtouris N, 2015, J CEREBR BLOOD F MET, V35, P167, DOI 10.1038/jcbfm.2014.179
   Moxon-Emre I, 2011, J NEUROPATH EXP NEUR, V70, P218, DOI 10.1097/NEN.0b013e31820d94a5
   Mracsko E, 2014, FRONT CELL NEUROSCI, V8, DOI 10.3389/fncel.2014.00388
   Mracsko E, 2014, STROKE, V45, P2107, DOI 10.1161/STROKEAHA.114.005801
   Murugaiyan G, 2015, ONCOTARGET, V6, P9644, DOI 10.18632/oncotarget.3928
   Newman AM, 2015, NAT METHODS, V12, P453, DOI [10.1038/NMETH.3337, 10.1038/nmeth.3337]
   Ouyang YB, 2012, NEUROBIOL DIS, V45, P555, DOI 10.1016/j.nbd.2011.09.012
   Palacios EH, 2004, ONCOGENE, V23, P7990, DOI 10.1038/sj.onc.1208074
   Pan Q, 2008, NAT GENET, V40, P1413, DOI 10.1038/ng.259
   Park L, 2013, P NATL ACAD SCI USA, V110, P3089, DOI 10.1073/pnas.1300021110
   Pías-Peleteiro J, 2017, NEURAL REGEN RES, V12, P558, DOI 10.4103/1673-5374.205085
   Podor TJ, 2002, J BIOL CHEM, V277, P7529, DOI 10.1074/jbc.M109675200
   Poulos MG, 2011, CSH PERSPECT BIOL, V3, DOI 10.1101/cshperspect.a000778
   Qureshi AI, 2009, LANCET, V373, P1632, DOI 10.1016/S0140-6736(09)60371-8
   Rodríguez-Yáñez M, 2012, J NEUROIMMUNOL, V247, P75, DOI 10.1016/j.jneuroim.2012.03.019
   Sang M, 2017, DNA CELL BIOL, V36, P647, DOI 10.1089/dna.2017.3650
   Sansing LH, 2011, ANN NEUROL, V70, P646, DOI 10.1002/ana.22528
   Sansing LH, 2011, ACTA NEUROCHIR SUPPL, V111, P173, DOI 10.1007/978-3-7091-0693-8_29
   Scotti MM, 2016, NAT REV GENET, V17, P19, DOI 10.1038/nrg.2015.3
   Sharp FR, 2013, STROKE, V44, pS23, DOI 10.1161/STROKEAHA.112.679357
   Sharp FR, 2011, J CEREBR BLOOD F MET, V31, P1513, DOI 10.1038/jcbfm.2011.45
   Stamova B, 2011, NEUROTOX RES, V19, P31, DOI 10.1007/s12640-009-9137-7
   Tao CY, 2017, BIOMARK MED, V11, P33, DOI 10.2217/bmm-2016-0187
   THOMPSON WA, 1962, ANN MATH STAT, V33, P273, DOI 10.1214/aoms/1177704731
   van Asch CJJ, 2010, LANCET NEUROL, V9, P167, DOI 10.1016/S1474-4422(09)70340-0
   Wang F, 2016, J STROKE CEREBROVASC, V25, P182, DOI 10.1016/j.jstrokecerebrovasdis.2015.09.013
   Wang YC, 2014, ANN NEUROL, V75, P876, DOI 10.1002/ana.24159
   Watkins NA, 2009, BLOOD, V113, pE1, DOI 10.1182/blood-2008-06-162958
   Xi GH, 2014, PROG NEUROBIOL, V115, P45, DOI 10.1016/j.pneurobio.2013.09.007
   Xie WD, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0058639
   Xiong HQ, 2009, J NEUROSCI, V29, P5463, DOI 10.1523/JNEUROSCI.5103-08.2009
   Xu B, 2004, MOL CELL BIOL, V24, P9198, DOI 10.1128/MCB.24.20.9198-9206.2004
   Yang J, 2016, SCI REP-UK, V6, DOI 10.1038/srep38372
   Yang Z, 2014, INT IMMUNOPHARMACOL, V22, P522, DOI 10.1016/j.intimp.2014.06.037
   Yew KS, 2009, AM FAM PHYSICIAN, V80, P33
   Zhao XR, 2015, CNS NEUROSCI THER, V21, P357, DOI 10.1111/cns.12350
   Zhao XR, 2007, ANN NEUROL, V61, P352, DOI 10.1002/ana.21097
   Zhao XR, 2017, NAT COMMUN, V8, DOI 10.1038/s41467-017-00770-7
   Zhao XR, 2014, TRANSL STROKE RES, V5, P554, DOI 10.1007/s12975-014-0341-2
   Zhou K, 2017, J CEREBR BLOOD F MET, V37, P967, DOI 10.1177/0271678X16648712
   Zhou Y, 2014, PROG NEUROBIOL, V115, P25, DOI 10.1016/j.pneurobio.2013.11.003
   Ziai WC, 2013, STROKE, V44, pS74, DOI 10.1161/STROKEAHA.111.000662
NR 83
TC 44
Z9 45
U1 3
U2 8
PU SAGE PUBLICATIONS INC
PI THOUSAND OAKS
PA 2455 TELLER RD, THOUSAND OAKS, CA 91320 USA
SN 0271-678X
EI 1559-7016
J9 J CEREBR BLOOD F MET
JI J. Cereb. Blood Flow Metab.
PD SEP
PY 2019
VL 39
IS 9
BP 1818
EP 1835
DI 10.1177/0271678X18769513
PG 18
WC Endocrinology & Metabolism; Hematology; Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism; Hematology; Neurosciences & Neurology
GA IV8NP
UT WOS:000484522500014
PM 29651892
OA Green Submitted, Green Published, Bronze
DA 2025-04-10
ER

PT J
AU Funakoshi, E
   Hamano, A
   Fukui, M
   Nishiyama, N
   Ogita, K
   Shimizu, N
   Ito, F
AF Funakoshi, E
   Hamano, A
   Fukui, M
   Nishiyama, N
   Ogita, K
   Shimizu, N
   Ito, F
TI Molecular cloning of the m-Golsyn gene and its expression in the
   mouse brain
SO GENE EXPRESSION
LA English
DT Article
DE GOLSYN; m-Golsyn; brain; protein trafficking; syntaphilin; neuronal
   cells; genomic structure; choroid plexus; chromosome 15B3.2; cDNA
   cloning
ID OPEN-ANGLE GLAUCOMA; N-MYC GENE; NEURITE OUTGROWTH; IN-VITRO; PROTEIN;
   REGION; LOCUS; IDENTIFICATION; ORGANOGENESIS; LOCALIZATION
AB The mouse ortholog of the human GOLSYN gene, termed the m-Golsyn gene, was isolated and mapped to the region on mouse chromosome 15B3.2 syntenic with human chromosome 8q23. Three mRNA species (type 1a, 1b, and type 2) were produced by use of alternative transcription initiation points and alternative splicing events. The type 1 mRNAs were expressed only in the brain, whereas the type 2 was detected in various tissues. m-Golsyn protein was expressed in various tissues including the brain. Immunohistochemical study of m-Golsyn protein showed its prominent expression in the neuronal cells in various regions of the brain and strong expression in the choroid plexus ependymal cells lining the ventricles. m-Golsyn protein was found to be homologous to syntaphilin, a regulator of synaptic vesicle exocytosis. These results indicate that the m-Golsyn protein may play an important role in intracellular protein transport in neuronal cells of the brain.
C1 Setsunan Univ, Fac Pharmaceut Sci, Dept Biochem, Osaka 5730101, Japan.
   Setsunan Univ, Fac Pharmaceut Sci, Dept Pharmacol, Osaka 5730101, Japan.
   Keio Univ, Sch Med, Dept Mol Biol, Shinjuku Ku, Tokyo 1608582, Japan.
C3 Setsunan University; Setsunan University; Keio University
RP Funakoshi, E (corresponding author), Setsunan Univ, Fac Pharmaceut Sci, Dept Biochem, 45-1 Nagaotoge Cho, Osaka 5730101, Japan.
EM funakos@pharm.setsunan.ac.jp
CR ALTSCHUL SF, 1990, J MOL BIOL, V215, P403, DOI 10.1016/S0022-2836(05)80360-2
   Chakrabortty S, 2000, J NEUROCYTOL, V29, P707, DOI 10.1023/A:1010930819854
   DAVSON H, 1955, J PHYSIOL-LONDON, V129, P111, DOI 10.1113/jphysiol.1955.sp005341
   DEBUS E, 1983, DIFFERENTIATION, V25, P193, DOI 10.1111/j.1432-0436.1984.tb01355.x
   DYNAN WS, 1985, NATURE, V316, P774, DOI 10.1038/316774a0
   Funakoshi E, 2005, GENE, V344, P259, DOI 10.1016/j.gene.2004.10.024
   GLOWINSKI J, 1966, J NEUROCHEM, V13, P655, DOI 10.1111/j.1471-4159.1966.tb09873.x
   HAGEN G, 1994, EMBO J, V13, P3843, DOI 10.1002/j.1460-2075.1994.tb06695.x
   HIRNING U, 1991, MECH DEVELOP, V33, P119, DOI 10.1016/0925-4773(91)90078-K
   HUTTNER WB, 1983, J CELL BIOL, V96, P1374, DOI 10.1083/jcb.96.5.1374
   Ide C, 2001, EXP NEUROL, V167, P242, DOI 10.1006/exnr.2000.7566
   Kimura K, 2004, J NEUROCYTOL, V33, P465, DOI 10.1023/B:NEUR.0000046576.70319.3a
   LAEMMLI UK, 1970, NATURE, V227, P680, DOI 10.1038/227680a0
   Lao GF, 2000, NEURON, V25, P191, DOI 10.1016/S0896-6273(00)80882-X
   MITCHELL PJ, 1986, MOL CELL BIOL, V6, P425, DOI 10.1128/MCB.6.2.425
   MULLEN RJ, 1992, DEVELOPMENT, V116, P201
   Ogita K, 2004, NEUROPHARMACOLOGY, V47, P619, DOI 10.1016/j.neuropharm.2004.06.012
   Okui M, 1999, GENOMICS, V62, P165, DOI 10.1006/geno.1999.5998
   OYLER GA, 1989, J CELL BIOL, V109, P3039, DOI 10.1083/jcb.109.6.3039
   Ray K, 2003, MOL CELL BIOCHEM, V253, P223, DOI 10.1023/A:1026059800470
   REYNOLDS GA, 1984, CELL, V38, P275, DOI 10.1016/0092-8674(84)90549-X
   Rezaie T, 2002, SCIENCE, V295, P1077, DOI 10.1126/science.1066901
   Sarfarazi M, 1998, AM J HUM GENET, V62, P641, DOI 10.1086/301767
   SAWAI S, 1993, DEVELOPMENT, V117, P1445
   SAWAI S, 1990, MOL CELL BIOL, V10, P2017, DOI 10.1128/MCB.10.5.2017
   SHEFFIELD VC, 1993, NAT GENET, V4, P47, DOI 10.1038/ng0593-47
   Stoilova D, 1996, GENOMICS, V36, P142, DOI 10.1006/geno.1996.0434
   Stone EM, 1997, SCIENCE, V275, P668, DOI 10.1126/science.275.5300.668
   Trifan OC, 1998, AM J OPHTHALMOL, V126, P17, DOI 10.1016/S0002-9394(98)00073-7
   Wirtz MK, 1997, AM J HUM GENET, V60, P296
   Wirtz MK, 1999, ARCH OPHTHALMOL-CHIC, V117, P237
NR 31
TC 4
Z9 4
U1 0
U2 1
PU COGNIZANT COMMUNICATION CORP
PI ELMSFORD
PA 3 HARTSDALE ROAD, ELMSFORD, NY 10523-3701 USA
SN 1052-2166
J9 GENE EXPRESSION
JI Gene Expr.
PY 2006
VL 13
IS 1
BP 27
EP 40
DI 10.3727/000000006783991917
PG 14
WC Biotechnology & Applied Microbiology; Gastroenterology & Hepatology;
   Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biotechnology & Applied Microbiology; Gastroenterology & Hepatology;
   Genetics & Heredity
GA 020ZA
UT WOS:000235950800003
PM 16572588
OA Green Published
DA 2025-04-10
ER

PT J
AU Chen, Q
   Takahashi, Y
   Oka, K
   Ma, JX
AF Chen, Qian
   Takahashi, Yusuke
   Oka, Kazuhiro
   Ma, Jian-xing
TI Functional Differences of Very-Low-Density Lipoprotein Receptor Splice
   Variants in Regulating Wnt Signaling
SO MOLECULAR AND CELLULAR BIOLOGY
LA English
DT Article
ID RETINAL ANGIOMATOUS PROLIFERATION; AMYLOID PRECURSOR PROTEIN;
   NECROSIS-FACTOR-ALPHA; GROWTH-FACTOR-ALPHA; RHINOVIRUS INFECTION;
   CARDIAC-HYPERTROPHY; ENDOTHELIAL-CELLS; VLDL RECEPTOR; EXPRESSION; MOUSE
AB The very-low-density lipoprotein receptor (VLDLR) negatively regulates Wnt signaling. VLDLR has two major alternative splice variants, VLDLRI and VLDLRII, but their biological significance and distinction are unknown. Here we found that most tissues expressed both VLDLRI and VLDLRII, while the retina expressed only VLDLRII. The shed soluble VLDLR extracellular domain (sVLDLR-N) was detected in the conditioned medium of retinal pigment epithelial cells, interphotoreceptor matrix, and mouse plasma, indicating that ectodomain shedding of VLDLR occurs endogenously. VLDLRII displayed a higher ectodomain shedding rate and a more potent inhibitory effect on Wnt signaling than VLDLRI in vitro and in vivo. O-glycosylation, which is present in VLDLRI but not VLDLRII, determined the differential ectodomain shedding rates. Moreover, the release of sVLDLR-N was inhibited by a metalloproteinase inhibitor, TAPI-1, while it was promoted by phorbol 12-myristate 13-acetate (PMA). In addition, sVLDLR-N shedding was suppressed under hypoxia. Further, plasma levels of sVLDLR-N were reduced in both type 1 and type 2 diabetic mouse models. We concluded that VLDLRI and VLDLRII had differential roles in regulating Wnt signaling and that decreased plasma levels of sVLDLR-N may contribute to Wnt signaling activation in diabetic complications. Our study reveals a novel mechanism for intercellular regulation of Wnt signaling through VLDLR ectodomain shedding.
C1 [Chen, Qian; Ma, Jian-xing] Univ Oklahoma, Hlth Sci Ctr, Dept Physiol, Oklahoma City, OK USA.
   [Takahashi, Yusuke] Univ Oklahoma, Hlth Sci Ctr, Dept Med, Oklahoma City, OK USA.
   [Chen, Qian; Takahashi, Yusuke; Ma, Jian-xing] Univ Oklahoma, Hlth Sci Ctr, Harold Hamm Diabet Ctr, Oklahoma City, OK USA.
   [Oka, Kazuhiro] Baylor Coll Med, Dept Mol & Cellular Biol, Houston, TX 77030 USA.
C3 University of Oklahoma System; University of Oklahoma Health Sciences
   Center; University of Oklahoma System; University of Oklahoma Health
   Sciences Center; University of Oklahoma System; University of Oklahoma
   Health Sciences Center; Baylor College of Medicine
RP Ma, JX (corresponding author), Univ Oklahoma, Hlth Sci Ctr, Dept Physiol, Oklahoma City, OK USA.; Ma, JX (corresponding author), Univ Oklahoma, Hlth Sci Ctr, Harold Hamm Diabet Ctr, Oklahoma City, OK USA.
EM jian-xing-ma@ouhsc.edu
RI Chen, Ruoqiao/LDE-8215-2024
FU NIH [EY012231, EY018659, EY019309, GM104934]; OCAST [HR13-076,
   HR12-103]; American Heart Association (AHA) [14PRE20460229]; American
   Heart Association (AHA) [14PRE20460229] Funding Source: American Heart
   Association (AHA)
FX This work, including the efforts of Jian-xing Ma, was funded by NIH
   (EY012231, EY018659, EY019309, and GM104934) and OCAST (HR13-076). This
   work, including the efforts of Yusuke Takahashi, was funded by OCAST
   (HR12-103). This work, including the efforts of Qian Chen, was funded by
   American Heart Association (AHA) (14PRE20460229).
CR Arden GB, 2011, CURR DIABETES REV, V7, P291, DOI 10.2174/157339911797415620
   Argraves WS, 2001, FRONT BIOSCI, V6, pD406, DOI 10.2741/Argraves
   Arribas J, 1997, J BIOL CHEM, V272, P17160, DOI 10.1074/jbc.272.27.17160
   ARRIBAS J, 1995, J CELL BIOL, V128, P433, DOI 10.1083/jcb.128.3.433
   Barber AJ, 2005, INVEST OPHTH VIS SCI, V46, P2210, DOI 10.1167/iovs.04-1340
   BECKER JC, 1991, J IMMUNOL, V147, P4398
   Bergmann MW, 2010, CIRC RES, V107, P1198, DOI 10.1161/CIRCRESAHA.110.223768
   Bollin F, 2011, PROTEIN EXPRES PURIF, V78, P61, DOI 10.1016/j.pep.2011.02.008
   Chen J, 2011, CIRCULATION, V124, P1871, DOI 10.1161/CIRCULATIONAHA.111.040337
   Chen T, 2005, WORLD J GASTROENTERO, V11, P2817, DOI 10.3748/wjg.v11.i18.2817
   Chen Y, 2007, J BIOL CHEM, V282, P34420, DOI 10.1074/jbc.M611289200
   Chen Y, 2009, AM J PATHOL, V175, P2676, DOI 10.2353/ajpath.2009.080945
   Chua SC, 1996, SCIENCE, V271, P994, DOI 10.1126/science.271.5251.994
   Clevers H, 2012, CELL, V149, P1192, DOI 10.1016/j.cell.2012.05.012
   Dieckmann M, 2010, BIOL CHEM, V391, P1341, DOI 10.1515/BC.2010.129
   Dorrell MI, 2009, J CLIN INVEST, V119, P611, DOI 10.1172/JCI35977
   FRYKMAN PK, 1995, P NATL ACAD SCI USA, V92, P8453, DOI 10.1073/pnas.92.18.8453
   Garton KJ, 2003, J BIOL CHEM, V278, P37459, DOI 10.1074/jbc.M305877200
   Hu WZ, 2008, INVEST OPHTH VIS SCI, V49, P407, DOI 10.1167/iovs.07-0870
   Hussain MM, 1999, ANNU REV NUTR, V19, P141, DOI 10.1146/annurev.nutr.19.1.141
   Iijima H, 1998, J BIOCHEM-TOKYO, V124, P747, DOI 10.1093/oxfordjournals.jbchem.a022175
   Jiang AH, 2009, INVEST OPHTH VIS SCI, V50, P844, DOI 10.1167/iovs.08-2447
   KINGSLEY DM, 1986, CELL, V44, P749, DOI 10.1016/0092-8674(86)90841-X
   Lee K, 2014, J CELL SCI, V127, P4857, DOI 10.1242/jcs.149302
   Li C, 2007, ARCH OPHTHALMOL-CHIC, V125, P795, DOI 10.1001/archopht.125.6.795
   Liu Q, 2009, MOL NEURODEGENER, V4, DOI 10.1186/1750-1326-4-17
   Lustig B, 2002, MOL CELL BIOL, V22, P1184, DOI 10.1128/MCB.22.4.1184-1193.2002
   MacDonald BT, 2009, DEV CELL, V17, P9, DOI 10.1016/j.devcel.2009.06.016
   Magrané J, 1999, FEBS LETT, V451, P56, DOI 10.1016/S0014-5793(99)00494-9
   Malekar P, 2010, HYPERTENSION, V55, P939, DOI 10.1161/HYPERTENSIONAHA.109.141127
   MARLIN SD, 1990, NATURE, V344, P70, DOI 10.1038/344070a0
   Marlovits TC, 1998, J VIROL, V72, P10246, DOI 10.1128/JVI.72.12.10246-10250.1998
   Masood R, 2001, BLOOD, V98, P1904, DOI 10.1182/blood.V98.6.1904
   Mazumdar J, 2010, NAT CELL BIOL, V12, P1007, DOI 10.1038/ncb2102
   McBride JD, 2014, J INVEST DERMATOL, V134, P1725, DOI 10.1038/jid.2014.40
   MIDENA E, 1989, OPHTHALMIC RES, V21, P106, DOI 10.1159/000266787
   Murray AR, 2013, INVEST OPHTH VIS SCI, V54, P1689, DOI 10.1167/iovs.12-10921
   Nyengaard JR, 2004, DIABETES, V53, P2931, DOI 10.2337/diabetes.53.11.2931
   Sakai K, 2009, BRAIN RES, V1276, P11, DOI 10.1016/j.brainres.2009.04.030
   Shen GM, 2012, BIOCHEM J, V441, P675, DOI 10.1042/BJ20111377
   Tadayoni R, 2003, EXP EYE RES, V77, P497, DOI 10.1016/S0014-4835(03)00155-6
   Takahashi Y, 2015, FEBS LETT, V589, P1143, DOI 10.1016/j.febslet.2015.03.010
   Tissir F, 2003, NAT REV NEUROSCI, V4, P496, DOI 10.1038/nrn1113
   Varela-Nallar L, 2014, FRONT CELL NEUROSCI, V8, DOI 10.3389/fncel.2014.00017
   Wang J, 1999, J CLIN INVEST, V103, P27, DOI 10.1172/JCI4431
   Wang ZX, 2015, ARTERIOSCL THROM VAS, V35, P855, DOI 10.1161/ATVBAHA.114.304627
   WU YQ, 1995, PROTEIN EXPRES PURIF, V6, P447, DOI 10.1006/prep.1995.1060
   Wyne KL, 1996, ARTERIOSCL THROM VAS, V16, P407, DOI 10.1161/01.ATV.16.3.407
   Yang P, 2009, LIFE SCI, V84, P402, DOI 10.1016/j.lfs.2008.12.020
   Yoshioka M, 1997, DIABETES, V46, P887, DOI 10.2337/diabetes.46.5.887
   Zhou T, 2012, DIABETOLOGIA, V55, P255, DOI 10.1007/s00125-011-2314-2
NR 51
TC 14
Z9 17
U1 1
U2 12
PU AMER SOC MICROBIOLOGY
PI WASHINGTON
PA 1752 N ST NW, WASHINGTON, DC 20036-2904 USA
SN 0270-7306
EI 1098-5549
J9 MOL CELL BIOL
JI Mol. Cell. Biol.
PD OCT 15
PY 2016
VL 36
IS 20
BP 2645
EP 2654
DI 10.1128/MCB.00235-16
PG 10
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA DX7CI
UT WOS:000384543300009
PM 27528615
OA Green Published, hybrid
DA 2025-04-10
ER

PT J
AU Maroney, SA
   Ellery, PE
   Mast, AE
AF Maroney, Susan A.
   Ellery, Paul E.
   Mast, Alan E.
TI Alternatively spliced isoforms of tissue factor pathway inhibitor
SO THROMBOSIS RESEARCH
LA English
DT Review
DE Tissue factor pathway inhibitor; Blood coagulation; Alternative
   splicing; Translational regulation
ID COAGULATION INHIBITOR; FACTOR-X; ANTICOAGULANT ACTIVITY; FACTOR-VIIA;
   EXPRESSION; SURFACE; PLASMA; DEFICIENCY; LOCALIZATION; PURIFICATION
AB Tissue factor pathway inhibitor (TFPI) is the major regulator of tissue factor (TF)-induced coagulation. It down regulates coagulation by binding to the TF/fVIIa complex in a fXa dependent manner. It is predominantly produced by microvascular endothelial cells, though it is also found in platelets, monocytes, smooth muscle cells, and plasma. Its physiological importance is demonstrated by the embryonic lethality observed in TFPI knockout mice and by the increase in thrombotic burden that occurs when heterozygous TFPI mice are bred with mice carrying genetic risk factors for thrombotic disease, such as factor V Leiden. Multiple TFPI isoforms, termed TFPI alpha, TFPI beta, and TFPI delta in humans and TFPI alpha, TFPI beta, and TFP gamma in mice, have been described, which differ in their domain structure and method for cell surface attachment. A significant functional difference between these isoforms has yet to be described in vivo. Both human and mouse tissues produce, on average, approximately 10 times more TFPI alpha message when compared to that of TFPI beta. Consistent with this finding, several lines of evidence suggest that TFPI alpha is the predominant protein isoform in humans. In contrast, recent work from our laboratory demonstrates that TFPI beta is the major protein isoform produced in adult mice, suggesting that TFPI isoform production is translationally regulated. (C) 2010 Elsevier Ltd. All rights reserved.
C1 [Mast, Alan E.] Blood Ctr Wisconsin, Blood Res Inst, Milwaukee, WI 53226 USA.
   [Mast, Alan E.] Med Coll Wisconsin, Dept Cell Biol Neurobiol & Anat, Milwaukee, WI 53226 USA.
C3 Versiti Blood Center of Wisconsin; Medical College of Wisconsin
RP Mast, AE (corresponding author), Blood Ctr Wisconsin, Blood Res Inst, 8727 Watertown Plank Rd, Milwaukee, WI 53226 USA.
EM alan.mast@bcw.edu
OI Ellery, Paul/0000-0002-3124-8397
FU NHLBI [R01HL068835, K01HL096419]
FX AEM is an Established Investigator of the American Heart Association.
   Funding was provided by NHLBI (R01HL068835 to AEM and K01HL096419 to
   SAM) and Novo Nordisk. The study sponsors had no involvement in study
   design, the collection, analysis and interpretation of data, in the
   writing of the manuscript or in the decision to submit the manuscript
   for publication.
CR BAUER KA, 1989, BLOOD, V74, P2007
   BROZE GJ, 1994, BLOOD COAGUL FIBRIN, V5, P551
   BROZE GJ, 1987, P NATL ACAD SCI USA, V84, P1886, DOI 10.1073/pnas.84.7.1886
   Caplice NM, 1998, CIRC RES, V83, P1264, DOI 10.1161/01.RES.83.12.1264
   CARSON SD, 1981, FEBS LETT, V132, P37, DOI 10.1016/0014-5793(81)80422-X
   Chang JY, 1999, THROMB HAEMOSTASIS, V81, P45
   CHEN HH, 2005, BLOOD, P2004
   Crawley J, 2000, ARTERIOSCL THROM VAS, V20, P1362, DOI 10.1161/01.ATV.20.5.1362
   DRAKE TA, 1989, J CELL BIOL, V109, P389, DOI 10.1083/jcb.109.1.389
   DRAKE TA, 1989, AM J PATHOL, V134, P1087
   Eitzman DT, 2002, CIRCULATION, V105, P2139, DOI 10.1161/01.CIR.0000017361.39256.82
   Engelmann B, 2006, BLOOD CELL MOL DIS, V36, P188, DOI 10.1016/j.bcmd.2005.12.020
   Giesen PLA, 1999, P NATL ACAD SCI USA, V96, P2311, DOI 10.1073/pnas.96.5.2311
   GIRARD TJ, 1991, J BIOL CHEM, V266, P5036
   GIRARD TJ, 1989, NATURE, V338, P518, DOI 10.1038/338518a0
   Huang ZF, 1997, THROMB HAEMOSTASIS, V78, P699
   LINDAHL AK, 1991, BLOOD COAGUL FIBRIN, V2, P713, DOI 10.1097/00001721-199112000-00004
   Lockett JM, 2002, BIOCHEMISTRY-US, V41, P4989, DOI 10.1021/bi016058n
   Maroney SA, 2008, J THROMB HAEMOST, V6, P1344, DOI 10.1111/j.1538-7836.2008.03033.x
   Maroney SA, 2008, J THROMB HAEMOST, V6, P111
   Maroney SA, 2009, J THROMB HAEMOST, V7, P1106, DOI 10.1111/j.1538-7836.2009.03454.x
   Maroney SA, 2006, J THROMB HAEMOST, V4, P1114, DOI 10.1111/j.1538-7836.2006.01873.x
   Maroney SA, 2007, BLOOD, V109, P1931, DOI 10.1182/blood-2006-07-037283
   Mast AE, 2002, ARTERIOSCL THROM VAS, V22, P2099, DOI 10.1161/01.ATV.0000042456.84190.F0
   NOSSEL HL, 1974, J CLIN INVEST, V54, P43, DOI 10.1172/JCI107749
   NOVOTNY WF, 1991, BLOOD, V78, P394
   NOVOTNY WF, 1988, BLOOD, V72, P2020
   NOVOTNY WF, 1989, J BIOL CHEM, V264, P18832
   Ott I, 2001, BLOOD, V97, P3721, DOI 10.1182/blood.V97.12.3721
   Pedersen B, 2005, BLOOD, V105, P2777, DOI 10.1182/blood-2004-09-3724
   Pendurthi UR, 1999, BLOOD, V94, P579, DOI 10.1182/blood.V94.2.579.414k23_579_586
   Piro O, 2005, J THROMB HAEMOST, V3, P2677, DOI 10.1111/j.1538-7836.2005.01636.x
   SANDERS NL, 1985, BLOOD, V66, P204
   SANDSET PM, 1988, THROMB RES, V50, P803, DOI 10.1016/0049-3848(88)90340-4
   Sevinsky JR, 1996, J CELL BIOL, V133, P293, DOI 10.1083/jcb.133.2.293
   WESSELSCHMIDT R, 1992, BLOOD, V79, P2004
   Westrick RJ, 2001, CIRCULATION, V103, P3044, DOI 10.1161/hc2501.092492
   WUN TC, 1988, J BIOL CHEM, V263, P6001
   Zhang J, 2003, CIRCULATION, V108, P623, DOI 10.1161/01.CIR.0000078642.45127.7B
NR 39
TC 42
Z9 45
U1 0
U2 2
PU PERGAMON-ELSEVIER SCIENCE LTD
PI OXFORD
PA THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND
SN 0049-3848
J9 THROMB RES
JI Thromb. Res.
PD APR
PY 2010
VL 125
SU 1
BP S52
EP S56
DI 10.1016/j.thromres.2010.01.038
PG 5
WC Hematology; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Hematology; Cardiovascular System & Cardiology
GA 571WX
UT WOS:000275787800017
PM 20176395
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Di Feo, MF
   Oghabian, A
   Nippala, E
   Gautel, M
   Jungbluth, H
   Forzano, F
   Malfatti, E
   Castiglioni, C
   Krey, I
   Andres, DG
   Brady, AF
   Iascone, M
   Cereda, A
   Pezzani, L
   De Benito, DN
   Osorio, AN
   Arias, BE
   Kurbatov, SA
   Attie-Bitach, T
   Nampoothiri, S
   Ryan, E
   Morrow, M
   Gorokhova, S
   Chabrol, B
   Sinisalo, J
   Tolppanen, H
   Tolva, J
   Munell, F
   Soriano, JC
   Duran, MAS
   Johari, M
   Tajsharghi, H
   Hackman, P
   Udd, B
   Savarese, M
AF Di Feo, Maria Francesca
   Oghabian, Ali
   Nippala, Ella
   Gautel, Mathias
   Jungbluth, Heinz
   Forzano, Francesca
   Malfatti, Edoardo
   Castiglioni, Claudia
   Krey, Ilona
   Andres, David Gomez
   Brady, Angela F.
   Iascone, Maria
   Cereda, Anna
   Pezzani, Lidia
   De Benito, Daniel Natera
   Osorio, Andres Nascimiento
   Arias, Berta Estevez
   Kurbatov, Sergei A.
   Attie-Bitach, Tania
   Nampoothiri, Sheela
   Ryan, Erin
   Morrow, Michelle
   Gorokhova, Svetlana
   Chabrol, Brigitte
   Sinisalo, Juha
   Tolppanen, Heli
   Tolva, Johanna
   Munell, Francina
   Soriano, Jessica Camacho
   Duran, Maria Angeles Sanchez
   Johari, Mridul
   Tajsharghi, Homa
   Hackman, Peter
   Udd, Bjarne
   Savarese, Marco
TI Inferring disease course from differential exon usage in the wide
   titinopathy spectrum
SO ANNALS OF CLINICAL AND TRANSLATIONAL NEUROLOGY
LA English
DT Article
ID ARTHROGRYPOSIS MULTIPLEX CONGENITA; TTN; TITIN; MUTATIONS; MYOPATHY;
   ISOFORM
AB ObjectiveBiallelic titin truncating variants (TTNtv) have been associated with a wide phenotypic spectrum, ranging from complex prenatal muscle diseases with dysmorphic features to adult-onset limb-girdle muscular dystrophy, with or without cardiac involvement. Given the size and complexity of TTN, reaching an unequivocal molecular diagnosis and precise disease prognosis remains challenging.MethodsIn this case series, 12 unpublished cases and one already published case with biallelic TTNtv were collected from multiple international medical centers between November 2022 and September 2023. TTN mutations were detected through exome or genome sequencing. Information about familial and personal clinical history was collected in a standardized form. RNA-sequencing and analysis of TTN exon usage were performed on an internal sample cohort including postnatal skeletal muscles, fetal skeletal muscles, postnatal heart muscles, and fetal heart muscles. In addition, publicly available RNA-sequencing data was retrieved from ENCODE.ResultsWe generated new RNA-seq data on TTN exons and identified genotype-phenotype correlations with prognostic implications for each titinopathy patient (whether worsening or improving in prenatal and postnatal life) using percentage spliced in (PSI) data for the involved exons. Interestingly, thanks to exon usage, we were also able to rule out a titinopathy diagnosis in one prenatal case.InterpretationThis study demonstrates that exon usage provides valuable insights for a more exhaustive clinical interpretation of TTNtv; additionally, it may serve as a model for implementing personalized medicine in many other genetic diseases, since most genes undergo alternative splicing.
C1 [Di Feo, Maria Francesca] Univ Genoa, Dept Neurosci Rehabil Ophthalmol Genet & Maternal, Genoa, Italy.
   [Di Feo, Maria Francesca; Oghabian, Ali; Nippala, Ella; Johari, Mridul; Hackman, Peter; Udd, Bjarne; Savarese, Marco] Folkhalsan Res Ctr, Helsinki, Uusimaa, Finland.
   [Gautel, Mathias; Jungbluth, Heinz] Kings Coll London, BHF Ctr Res Excellence, Randall Div Cell & Mol Biophys, London, England.
   [Gautel, Mathias; Jungbluth, Heinz] Kings Coll London, BHF Ctr Res Excellence, Cardiovasc Div, London, England.
   [Jungbluth, Heinz] Guys & St Thomas Hosp NHS Trust, Evelinas Children Hosp, Neuromuscular Serv, Paediat Neurol, London, England.
   [Forzano, Francesca] Guys & St Thomas NHS Fdn Trust, Clin Genet Dept, London SE1 9RT, England.
   [Malfatti, Edoardo] Univ Paris Est Creteil, IMRB, INSERM, U955, Creteil, France.
   [Malfatti, Edoardo] Henri Mondor Univ Hosp, APHP, Reference Ctr Neuromuscular Disorders, Creteil, France.
   [Castiglioni, Claudia] Clin MEDS, Santiago, Chile.
   [Krey, Ilona] Univ Leipzig Hosp & Clin, Inst Human Genet, Leipzig, Germany.
   [Andres, David Gomez] Hosp Univ Vall Hebron, Vall Hebron Res Inst VHIR, Child Neurol Unit, Barcelona, Spain.
   [Brady, Angela F.] Northwick Pk & St Marks Hosp, North West Thames Reg Serv, London, England.
   [Iascone, Maria] ASST Papa Giovanni XXIII, Med Genet Lab, Bergamo, Italy.
   [Cereda, Anna; Pezzani, Lidia] ASST Papa Giovanni XXIII, Paediat 1, Clin Genet Serv, Bergamo, Italy.
   [De Benito, Daniel Natera; Osorio, Andres Nascimiento] Hosp St Joan De Deu, Inst Recerca St Joan De Deu, Neuropaediat Dept, Barcelona 08950, Spain.
   [Arias, Berta Estevez] Hosp St Joan De Deu, Dept Neurol, Neuromuscular Unit, Barcelona, Spain.
   [Kurbatov, Sergei A.] Voronezh NN Burdenko State Med Univ, Voronezh 394036, Russia.
   [Kurbatov, Sergei A.] Saratov State Med Univ, Saratov 410012, Russia.
   [Attie-Bitach, Tania] Hop Necker Enfants Malad, Unite Embryofoetopathol, Serv Histologie Embryologie Cytogenet, Paris, France.
   [Nampoothiri, Sheela] Amrita Inst Med Sci & Res Ctr, Dept Pediat Genet, Kochi, Kerala, India.
   [Ryan, Erin; Morrow, Michelle] GeneDx, Gaithersburg, MD USA.
   [Gorokhova, Svetlana] Aix Marseille Univ, Marseille Med Genet, Fac Sci Med & Paramed, Marseille, France.
   [Chabrol, Brigitte] Marseille Univ Hosp, Reference Ctr Inherited Metab Dis, Marseille, France.
   [Sinisalo, Juha; Tolppanen, Heli] Univ Helsinki, Cent Hosp, Helsinki, Finland.
   [Tolva, Johanna] Univ Helsinki, Dept Pathol, Transplantat Lab, Helsinki, Finland.
   [Munell, Francina] Hosp Univ Vall Dhebron, Unitat Malalties Neuromusculars Pediat, Barcelona, Spain.
   [Soriano, Jessica Camacho] Vall Hebron Univ Hosp, Histol Dept, Barcelona, Spain.
   [Duran, Maria Angeles Sanchez] Univ Autonoma Barcelona, Hosp Univ Vall Dhebron, Dept Obstet, Maternal Fetal Med Unit, Barcelona, Spain.
   [Johari, Mridul] Univ Western Australia, Harry Perkins Inst Med Res, Ctr Med Res, Nedlands, WA, Australia.
   [Tajsharghi, Homa] Univ Skovde, Sch Hlth Sci, Div Biomed, Skovde, Sweden.
   [Udd, Bjarne] Tampere Univ Hosp, Dept Musculoskeletal Dis, Tampere, Finland.
C3 University of Genoa; Folkhalsan Research Center; University of London;
   King's College London; University of London; King's College London;
   Guy's & St Thomas' NHS Foundation Trust; Guy's & St Thomas' NHS
   Foundation Trust; Institut National de la Sante et de la Recherche
   Medicale (Inserm); Universite Paris-Est-Creteil-Val-de-Marne (UPEC);
   Assistance Publique Hopitaux Paris (APHP); Universite
   Paris-Est-Creteil-Val-de-Marne (UPEC); Hopital Universitaire
   Henri-Mondor - APHP; Leipzig University; Autonomous University of
   Barcelona; Hospital Universitari Vall d'Hebron; Vall d'Hebron Institut
   de Recerca (VHIR); ASST Papa Giovanni XXIII; ASST Papa Giovanni XXIII;
   University of Barcelona; University of Barcelona; Voronezh State Medical
   University; Razumovsky Saratov State Medical University; Assistance
   Publique Hopitaux Paris (APHP); Universite Paris Cite; Hopital
   Universitaire Necker-Enfants Malades - APHP; Amrita Vishwa Vidyapeetham;
   Amrita Vishwa Vidyapeetham Kochi; Aix-Marseille Universite;
   Aix-Marseille Universite; Assistance Publique-Hopitaux de Marseille;
   University of Helsinki; Helsinki University Central Hospital; University
   of Helsinki; Hospital Universitari Vall d'Hebron; Hospital Universitari
   Vall d'Hebron; Hospital Universitari Vall d'Hebron; Autonomous
   University of Barcelona; University of Western Australia; Harry Perkins
   Institute of Medical Research; University of Skovde; Tampere University;
   Tampere University Hospital
RP Di Feo, MF (corresponding author), Univ Genoa, Dept Neurosci Rehabil Ophthalmol Genet & Maternal, Genoa, Italy.
EM mariafrancescadifeo@gaslini.org
RI Pezzani, Lidia/AAA-5742-2019; Nampoothiri, Sheela/AAQ-4854-2021;
   ATTIE-BITACH, Tania/K-1453-2017; Kurbatov, Sergei/AAE-7910-2022;
   Gorokhova, Svetlana/L-9380-2019; Natera-de Benito, Daniel/AAC-9892-2021;
   Johari, Mridul/AAP-4002-2021; Malfatti, Edoardo/KEI-9379-2024; cereda,
   anna/AAB-5376-2019; Udd, Bjarne/JBE-3483-2023; Savarese,
   Marco/J-8307-2016
OI Sinisalo, Juha/0000-0002-0169-5137; Johari, Mridul/0000-0002-3549-558X;
   Natera-de Benito, Daniel/0000-0001-7764-2085; Malfatti,
   Edoardo/0000-0001-7871-8600; Di Feo, Maria
   Francesca/0000-0002-4090-9521; Savarese, Marco/0000-0002-2591-244X
FU Academy of Finland [339437]; Association Francssaise contre les
   Myopathies [23281]; Magnus Ehrnrooth Foundation; European Joint Program
   on Rare Diseases (project IDOLS-G); Juselius Foundation; Sam fundet
   Folkhalsan i Svenska Finland; European Joint Program onRare Diseases;
   Instituto de SaludCarlos III, Spain [AC19/00048]; Jane and Aatos Erkko
   foundation
FX M.S. received support from the Academy of Finland(grant 339437),
   Association Francssaise contre les Myopathies (grant 23281),
   Sydantutkimussaatio, and SamfundetFolkhalsan i Svenska, Finland. A.O.
   received supported by Magnus Ehrnrooth Foundation. B.U. received support
   from the European Joint Program on Rare Diseases (project IDOLS-G),
   Academy of Finland, Juselius Foundation,and Sam fundet Folkhalsan i
   Svenska Finland. F.M.received support from the European Joint Program
   onRare Diseases (project IDOLS-G) and Instituto de SaludCarlos III,
   Spain (project number AC19/00048). P.H.received support from the Jane
   and Aatos Erkko foundation
CR Averdunk L, 2022, NEUROPEDIATRICS, V53, P309, DOI 10.1055/a-1859-0800
   Balasundaram Palanikumar, 2023, Case Rep Genet, V2023, P5535083, DOI 10.1155/2023/5535083
   Bang ML, 2001, CIRC RES, V89, P1065, DOI 10.1161/hh2301.100981
   Bryen SJ, 2020, HUM MUTAT, V41, P403, DOI 10.1002/humu.23938
   Cardone N., 2023, ACTA NEUROPATHOL COM, V11, P1, DOI [10.1186/S40478023015394/FIGURES/5, DOI 10.1186/S40478023015394/FIGURES/5]
   Chauveau C, 2014, HUM MUTAT, V35, P1046, DOI 10.1002/humu.22611
   Chauveau C, 2014, HUM MOL GENET, V23, P980, DOI 10.1093/hmg/ddt494
   Chervinsky E, 2018, AM J MED GENET A, V176, P1001, DOI 10.1002/ajmg.a.38639
   Di Feo MF, 2023, J MED GENET, V60, P866, DOI 10.1136/jmg-2022-109018
   Dobin A, 2013, BIOINFORMATICS, V29, P15, DOI 10.1093/bioinformatics/bts635
   Fernández-Marmiesse A, 2017, NEUROMUSCULAR DISORD, V27, P188, DOI 10.1016/j.nmd.2016.11.002
   Gerull B, 2002, NAT GENET, V30, P201, DOI 10.1038/ng815
   Guo W, 2010, J BIOMED BIOTECHNOL, DOI 10.1155/2010/753675
   Hackman P, 2002, AM J HUM GENET, V71, P492, DOI 10.1086/342380
   Kasinathan Ananthanarayanan, 2018, J Clin Neuromuscul Dis, V19, P232, DOI 10.1097/CND.0000000000000167
   Laquerriere A, 2022, J MED GENET, V59, P559, DOI 10.1136/jmedgenet-2020-107595
   Lillback V, 2023, EUR J NEUROL, V30, P1080, DOI 10.1111/ene.15688
   Linke WA, 2002, J STRUCT BIOL, V137, P194, DOI 10.1006/jsbi.2002.4468
   Luther PK, 2009, J MUSCLE RES CELL M, V30, P171, DOI 10.1007/s10974-009-9189-6
   Oates EC, 2018, ANN NEUROL, V83, P1105, DOI 10.1002/ana.25241
   Oghabian A, 2018, BMC BIOINFORMATICS, V19, DOI 10.1186/s12859-018-2122-5
   Perrin A, 2020, NEUROMUSCULAR DISORD, V30, P877, DOI 10.1016/j.nmd.2020.09.032
   Prado LG, 2005, J GEN PHYSIOL, V126, P461, DOI 10.1085/jgp.200509364
   Rees M, 2021, ACTA NEUROPATHOL, V141, P431, DOI 10.1007/s00401-020-02257-0
   Reese Fairlie, 2023, bioRxiv, DOI 10.1101/2023.05.15.540865
   Savarese M, 2020, GENET MED, V22, P2029, DOI 10.1038/s41436-020-0914-2
   Savarese M, 2020, J NEUROMUSCULAR DIS, V7, P153, DOI 10.3233/JND-190423
   Savarese M, 2018, JAMA NEUROL, V75, P557, DOI 10.1001/jamaneurol.2017.4899
   Savarese M, 2018, SKELET MUSCLE, V8, DOI 10.1186/s13395-018-0156-z
   Savarese Marco, 2016, J Neuromuscul Dis, V3, P293
   Schafer S, 2017, NAT GENET, V49, P46, DOI 10.1038/ng.3719
   Schoch K, 2020, GENET MED, V22, P1269, DOI 10.1038/s41436-020-0781-x
   Tardaguila M, 2018, GENOME RES, V28, P396, DOI 10.1101/gr.222976.117
   Tasca G, 2018, NEUROMUSCULAR DISORD, V28, P268, DOI 10.1016/j.nmd.2017.12.002
   Töpf A, 2024, NAT GENET, V56, DOI 10.1038/s41588-023-01651-0
   Tskhovrebova L, 2010, J BIOMED BIOTECHNOL, DOI 10.1155/2010/612482
   van den Hoogenhof MMG, 2018, CIRCULATION, V138, P1330, DOI 10.1161/CIRCULATIONAHA.117.031947
   Ware JS, 2018, NAT REV CARDIOL, V15, P241, DOI 10.1038/nrcardio.2017.190
   Ware JS, 2016, NEW ENGL J MED, V374, P233, DOI 10.1056/NEJMoa1505517
   Zou PJ, 2006, NATURE, V439, P229, DOI 10.1038/nature04343
NR 40
TC 1
Z9 1
U1 0
U2 2
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 2328-9503
J9 ANN CLIN TRANSL NEUR
JI Ann. Clin. Transl. Neurol.
PD OCT
PY 2024
VL 11
IS 10
BP 2745
EP 2755
DI 10.1002/acn3.52189
EA AUG 2024
PG 11
WC Clinical Neurology; Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA K6W8Y
UT WOS:001299553100001
PM 39198997
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Dunn, J
   Elias, CL
   Le, HD
   Omelchenko, A
   Hryshko, LV
   Lytton, J
AF Dunn, J
   Elias, CL
   Le, HD
   Omelchenko, A
   Hryshko, LV
   Lytton, J
TI The molecular determinants of ionic regulatory differences between brain
   and kidney Na<SUP>+</SUP>/Ca<SUP>2+</SUP> exchanger (NCX1) isoforms
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID CARDIAC NA+-CA2+ EXCHANGER; SODIUM-CALCIUM EXCHANGE; ALTERNATIVELY
   SPLICED ISOFORMS; NA-CA EXCHANGER; INHIBITORY PEPTIDE; SARCOLEMMAL
   VESICLES; CA2+-BINDING DOMAIN; DYNAMIC PROPERTIES; STEADY-STATE; XIP
AB The Na+/Ca2+ exchanger gene NCX1 undergoes alternative splicing leading to several isoforms that differ in a small portion of the large cytoplasmic loop. This loop is involved in many regulatory processes of NCX1, including ionic regulation by the transported substrates Na+ and Ca2+. High intracellular Ca2+ can alleviate intracellular Na+-dependent inactivation in exon A (NCX1.4)-containing isoforms but not in those containing the mutually exclusive exon B (NCX1.3). Giant excised patches from Xenopus oocytes expressing various NCX1 constructs were used to examine the specific amino acids responsible for these observed regulatory differences. Using a chimeric approach, the region responsible was narrowed down to the small central part of exon A (IDDEEYEKNKTF). Replacing the second aspartic acid of this sequence with arginine (the corresponding amino acid in exon B) in an exon A background completely prevented the effect of Ca2+ on intracellular Na+-dependent inactivation. Mutating the second lysine to cysteine (exon B) had a similar, but only partial, effect. The converse double mutant, but neither single mutation alone, introduced into an exon B background (arginine to aspartic acid and cysteine to lysine) was able to restore the NCX1.4 regulatory phenotype. These data demonstrate that aspartic acid 610 and lysine 617 (using the rat NCX1.4 numbering scheme) are critical molecular determinants.
C1 Univ Calgary, Hlth Sci Ctr, Dept Biochem & Mol Biol, Cardiovasc Res Grp, Calgary, AB T2N 4N1, Canada.
   Univ Manitoba, Fac Med, Dept Physiol, Inst Cardiovasc Sci,St Boniface Gen Hosp,Res Ctr, Winnipeg, MB R2H 2A6, Canada.
C3 University of Calgary; University Calgary Hospital; University of
   Manitoba; Children's Hospital Research Institute of Manitoba
RP Lytton, J (corresponding author), Univ Calgary, Hlth Sci Ctr, Dept Biochem & Mol Biol, Cardiovasc Res Grp, Rm 2518,3330 Hosp Dr NW, Calgary, AB T2N 4N1, Canada.
OI Hryshko, Larry/0000-0003-1079-8549; Lytton, Jonathan/0000-0003-4770-2512
CR BERS DM, 1994, METHOD CELL BIOL, V40, P3
   Dyck C, 1999, J GEN PHYSIOL, V114, P701, DOI 10.1085/jgp.114.5.701
   Gatto C, 1996, ANN NY ACAD SCI, V779, P284, DOI 10.1111/j.1749-6632.1996.tb44796.x
   Hale CC, 1997, BIOCHEM BIOPH RES CO, V236, P113, DOI 10.1006/bbrc.1997.6912
   Hale CC, 1996, ANN NY ACAD SCI, V779, P171, DOI 10.1111/j.1749-6632.1996.tb44785.x
   He SW, 1998, J NEUROSCI, V18, P4833
   He Z, 1997, J MEMBRANE BIOL, V156, P149, DOI 10.1007/s002329900197
   Hering S, 2000, J PHYSIOL-LONDON, V528, P237, DOI 10.1111/j.1469-7793.2000.t01-1-00237.x
   HILGEMANN DW, 1992, J GEN PHYSIOL, V100, P905, DOI 10.1085/jgp.100.6.905
   HILGEMANN DW, 1990, NATURE, V344, P242, DOI 10.1038/344242a0
   HILGEMANN DW, 1992, J GEN PHYSIOL, V100, P933, DOI 10.1085/jgp.100.6.933
   Hryshko LV, 1996, J GEN PHYSIOL, V108, P67, DOI 10.1085/jgp.108.1.67
   KOFUJI P, 1994, J BIOL CHEM, V269, P5145
   KOHMOTO O, 1994, CIRC RES, V74, P550, DOI 10.1161/01.RES.74.3.550
   LEE SL, 1994, J BIOL CHEM, V269, P14849
   LEVITSKY DO, 1994, J BIOL CHEM, V269, P22847
   LEVITSKY DO, 1996, MOL CELL BIOCHEM, V160, P27
   LI ZP, 1991, J BIOL CHEM, V266, P1014
   LI ZP, 1994, J BIOL CHEM, V269, P17434
   MATSUOKA S, 1995, J GEN PHYSIOL, V105, P403, DOI 10.1085/jgp.105.3.403
   Matsuoka S, 1997, J GEN PHYSIOL, V109, P273, DOI 10.1085/jgp.109.2.273
   MATSUOKA S, 1993, P NATL ACAD SCI USA, V90, P3870, DOI 10.1073/pnas.90.9.3870
   Nicoll DA, 1996, J BIOL CHEM, V271, P24914, DOI 10.1074/jbc.271.40.24914
   NICOLL DA, 1991, ANN NY ACAD SCI, V639, P181, DOI 10.1111/j.1749-6632.1991.tb17305.x
   NICOLL DA, 1990, SCIENCE, V250, P562, DOI 10.1126/science.1700476
   Omelchenko A, 1998, J GEN PHYSIOL, V111, P691, DOI 10.1085/jgp.111.5.691
   Ottolia M, 2001, J BIOL CHEM, V276, P19603, DOI 10.1074/jbc.M101489200
   Pan Y, 2000, AM J PHYSIOL-CELL PH, V279, pC393, DOI 10.1152/ajpcell.2000.279.2.C393
   Philipson KD, 1996, ANN NY ACAD SCI, V779, P20, DOI 10.1111/j.1749-6632.1996.tb44766.x
   Quednau BD, 1997, AM J PHYSIOL-CELL PH, V272, pC1250, DOI 10.1152/ajpcell.1997.272.4.C1250
   SHANNON TR, 1994, AM J PHYSIOL, V266, pC1350, DOI 10.1152/ajpcell.1994.266.5.C1350
   Trac M, 1997, J GEN PHYSIOL, V109, P361, DOI 10.1085/jgp.109.3.361
   Xu WY, 1997, ARCH BIOCHEM BIOPHYS, V341, P273, DOI 10.1006/abbi.1997.9954
NR 33
TC 39
Z9 40
U1 0
U2 0
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
SN 0021-9258
J9 J BIOL CHEM
JI J. Biol. Chem.
PD SEP 13
PY 2002
VL 277
IS 37
BP 33957
EP 33962
DI 10.1074/jbc.M206677200
PG 6
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 592WD
UT WOS:000177959100058
PM 12118014
OA hybrid
DA 2025-04-10
ER

PT J
AU Loukianov, E
   Loukianova, T
   Periasamy, M
AF Loukianov, E
   Loukianova, T
   Periasamy, M
TI Myosin heavy chain isoforms in smooth muscle
SO COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR
   BIOLOGY
LA English
DT Article
DE smooth muscle cells; myosin heavy chain; isoform; expression;
   differentiation; development; exon; tissue-specific
ID NONMUSCLE MYOSIN; MESSENGER-RNAS; DIFFERENTIAL EXPRESSION; VASCULAR
   DEVELOPMENT; SHORTENING VELOCITY; MULTIGENE FAMILY; CDNA CLONING; CELLS;
   IDENTIFICATION; CHICKEN
AB In recent years, significant progress has been made toward understanding smooth muscle myosin heavy chain (SMHC) structure. Molecular cloning analysis has identified four different MHC isoforms. They are products of a single gene and result from alternative mRNA splicing. In addition, two non-muscle MHC isoforms are also expressed in smooth muscle cells. Studies show that SMHC expression is highly tissue specific and does not appear in cardiac or skeletal muscle cells. Each smooth muscle tissue is characterized by a specific pattern of MHC isoform expression that changes during development and disease. This review essentially focuses on SMHC isoforms and their expression in mammals. (C) 1997 Elsevier Science Inc.
C1 UNIV CINCINNATI,COLL MED,DIV CARDIOL,SECT MOL CARDIOL,CINCINNATI,OH 45267.
   UNIV CINCINNATI,COLL MED,CARDIOVASC RES CTR,CINCINNATI,OH 45267.
C3 University System of Ohio; University of Cincinnati; University System
   of Ohio; University of Cincinnati
OI Periasamy, Muthu/0000-0001-8834-5975
CR AIKAWA M, 1993, CIRC RES, V73, P1000, DOI 10.1161/01.RES.73.6.1000
   ALPERT NR, CARDIAC ADAPTATION H, P147
   BABIJ P, 1989, J MOL BIOL, V210, P673, DOI 10.1016/0022-2836(89)90142-3
   BABIJ P, 1992, AM J PHYSIOL, V262, pC607, DOI 10.1152/ajpcell.1992.262.3.C607
   BABIJ P, 1993, NUCLEIC ACIDS RES, V21, P1467, DOI 10.1093/nar/21.6.1467
   BABIJ P, 1991, P NATL ACAD SCI USA, V88, P10607
   CAI S, 1995, AM J PHYSIOL-CELL PH, V269, pC1126, DOI 10.1152/ajpcell.1995.269.5.C1126
   CAI S, 1993, BIOPHYS J, V64, pA257
   EDDINGER TJ, 1988, BIOCHEMISTRY-US, V27, P3807, DOI 10.1021/bi00410a043
   FRID MG, 1993, J VASC RES, V30, P279, DOI 10.1159/000159007
   FUGLSANG A, 1993, J MUSCLE RES CELL M, V15, P662
   HAMADA Y, 1990, BIOCHEM BIOPH RES CO, V170, P53, DOI 10.1016/0006-291X(90)91239-O
   HEWETT TE, 1993, J PHYSIOL-LONDON, V460, P351, DOI 10.1113/jphysiol.1993.sp019475
   HOROWITZ A, 1992, J BIOL CHEM, V267, P26091
   HUSZAR G, 1972, NATURE-NEW BIOL, V240, P260, DOI 10.1038/newbio240260a0
   IKEBE M, 1991, J BIOL CHEM, V266, P7030
   IZUMO S, 1986, SCIENCE, V231, P597, DOI 10.1126/science.3945800
   KATOH Y, 1994, J BIOL CHEM, V269, P30538
   KATSURAGAWA Y, 1989, EUR J BIOCHEM, V184, P611, DOI 10.1111/j.1432-1033.1989.tb15057.x
   KAWAMOTO S, 1991, J CELL BIOL, V112, P915, DOI 10.1083/jcb.112.5.915
   KAWAMOTO S, 1987, J BIOL CHEM, V262, P7282
   KAWAMOTO S, 1987, J BIOL CHEM, V263, P1099
   KELLEY CA, 1990, J BIOL CHEM, V265, P17876
   KELLEY CA, 1992, J BIOL CHEM, V267, P2127
   KELLEY CA, 1993, J BIOL CHEM, V268, P12848
   KIM HS, 1993, CIRCULATION, V88, P1804, DOI 10.1161/01.CIR.88.4.1804
   KUROO M, 1991, J BIOL CHEM, V266, P3768
   KUROO M, 1989, J BIOL CHEM, V264, P18272
   LOMPRE AM, 1979, NATURE, V282, P105, DOI 10.1038/282105a0
   LOMPRE AM, 1984, J BIOL CHEM, V259, P6437
   MIANO JM, 1994, CIRC RES, V75, P803, DOI 10.1161/01.RES.75.5.803
   NAGAI R, 1987, CIRC RES, V60, P692, DOI 10.1161/01.RES.60.5.692
   NAGAI R, 1989, J BIOL CHEM, V264, P9734
   NAGAI R, 1988, P NATL ACAD SCI USA, V85, P1047, DOI 10.1073/pnas.85.4.1047
   NGUYEN HT, 1982, P NATL ACAD SCI-BIOL, V79, P5230, DOI 10.1073/pnas.79.17.5230
   OLSON EN, 1990, GENE DEV, V4, P1454, DOI 10.1101/gad.4.9.1454
   PAGANI ED, 1984, CIRC RES, V554, P586
   PERIASAMY M, 1985, J BIOL CHEM, V260, P5856
   PERIASAMY M, 1984, J BIOL CHEM, V259, P3573
   RAYMENT I, 1993, SCIENCE, V261, P50, DOI 10.1126/science.8316857
   ROBBINS J, 1986, J BIOL CHEM, V261, P6606
   ROVNER AS, 1986, J BIOL CHEM, V261, P4740
   ROVNER AS, 1986, AM J PHYSIOL, V250, pC861, DOI 10.1152/ajpcell.1986.250.6.C861
   SAEZ CG, 1990, P NATL ACAD SCI USA, V87, P1164, DOI 10.1073/pnas.87.3.1164
   SARTORE S, 1994, J VASC RES, V31, P61, DOI 10.1159/000159033
   SIEMANKOWSKI RF, 1985, P NATL ACAD SCI USA, V82, P658, DOI 10.1073/pnas.82.3.658
   SIMONS M, 1991, CIRC RES, V69, P530, DOI 10.1161/01.RES.69.2.530
   TAKAHASHI M, 1992, J BIOL CHEM, V267, P17864
   WHITE S, 1993, AM J PHYSIOL, V264, pC1252, DOI 10.1152/ajpcell.1993.264.5.C1252
   YANAGISAWA M, 1987, J MOL BIOL, V198, P143, DOI 10.1016/0022-2836(87)90302-0
   ZANELLATO AMC, 1990, ARTERIOSCLEROSIS, V10, P996, DOI 10.1161/01.ATV.10.6.996
NR 51
TC 16
Z9 21
U1 0
U2 7
PU PERGAMON-ELSEVIER SCIENCE LTD
PI OXFORD
PA THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD, ENGLAND OX5 1GB
SN 0305-0491
J9 COMP BIOCHEM PHYS B
JI Comp. Biochem. Physiol. B-Biochem. Mol. Biol.
PD MAY
PY 1997
VL 117
IS 1
BP 13
EP 18
DI 10.1016/S0305-0491(96)00309-4
PG 6
WC Biochemistry & Molecular Biology; Zoology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Zoology
GA WX438
UT WOS:A1997WX43800003
PM 9180010
DA 2025-04-10
ER

PT J
AU Iyer, NV
   Leung, SW
   Semenza, GL
AF Iyer, NV
   Leung, SW
   Semenza, GL
TI The human hypoxia-inducible factor 1α gene:: HIF1A structure and
   evolutionary conservation
SO GENOMICS
LA English
DT Article
ID TRANSCRIPTION FACTOR; MOLECULAR CHARACTERIZATION; CHROMOSOMAL
   ASSIGNMENT; FACTOR-I; EXPRESSION; FACTOR-1-ALPHA; TRANSACTIVATION;
   ORGANIZATION; PURIFICATION; ACTIVATION
AB The HIF1A gene encodes the HIF-1 alpha subunit of hypoxia-inducible factor 1, a transcription factor that is essential for cardiovascular development and systemic O-2 homeostasis. HIF1A consists of 15 exons that are interrupted by introns at the same locations as in the mouse Hif1a gene, although sequences mediating alternative splicing and alternative translation initiation events in the mouse are not present in the human gene. Placement of introns differs between HIF1A and EPAS1, which encodes the human HIF-2 alpha protein. Transcription of the HIF1A gene was initiated over a 15-nt region downstream of two SP1 sites. A 0.7-kb region of 5' flanking sequences functioned as a strong promoter in transient expression assays. Comparison of 0.8 kb of 5' flanking and 5' untranslated sequences from the HIF1A and Hif1a genes revealed 70% identity. The proximal 300 bp of 5' flanking sequences was 83% identical, including the SP1 sites and transcription initiation sites. These results suggest evolutionary selection for maintenance of HIF1A structure, function, and regulation. (C) 1998 Academic Press.
C1 Johns Hopkins Univ, Sch Med, Inst Med Genet, Dept Pediat, Baltimore, MD 21287 USA.
   Johns Hopkins Univ, Sch Med, Inst Med Genet, Dept Med, Baltimore, MD 21287 USA.
C3 Johns Hopkins University; Johns Hopkins University
RP Johns Hopkins Univ Hosp, CMSC-1004,600 N Wolfe St, Baltimore, MD 21287 USA.
EM gsemenza@gwgate1.jhmi.jhu.edu
RI Semenza, Gregg/ABW-5102-2022
FU NHLBI NIH HHS [R01-HL55338] Funding Source: Medline; NIDDK NIH HHS
   [R01-DK39869] Funding Source: Medline
CR BERGERON M, 1997, J CEREB BLOOD FLO S1, V17, pS505
   BREATHNACH R, 1981, ANNU REV BIOCHEM, V50, P349, DOI 10.1146/annurev.bi.50.070181.002025
   BRIGGS MR, 1986, SCIENCE, V234, P47, DOI 10.1126/science.3529394
   Ema M, 1997, P NATL ACAD SCI USA, V94, P4273, DOI 10.1073/pnas.94.9.4273
   Flamme I, 1997, MECH DEVELOP, V63, P51, DOI 10.1016/S0925-4773(97)00674-6
   Forsythe JA, 1996, MOL CELL BIOL, V16, P4604
   Hogenesch JB, 1997, J BIOL CHEM, V272, P8581, DOI 10.1074/jbc.272.13.8581
   Iyer NV, 1998, GENE DEV, V12, P149, DOI 10.1101/gad.12.2.149
   Jiang BH, 1996, J BIOL CHEM, V271, P17771, DOI 10.1074/jbc.271.30.17771
   Jiang BH, 1997, J BIOL CHEM, V272, P19253, DOI 10.1074/jbc.272.31.19253
   Jiang BH, 1996, AM J PHYSIOL-CELL PH, V271, pC1172, DOI 10.1152/ajpcell.1996.271.4.C1172
   Li H, 1996, J BIOL CHEM, V271, P21262, DOI 10.1074/jbc.271.35.21262
   Luo G, 1997, GENE EXPRESSION, V6, P287
   Palmer LA, 1998, AM J PHYSIOL-LUNG C, V274, pL212, DOI 10.1152/ajplung.1998.274.2.L212
   Pugh CW, 1997, J BIOL CHEM, V272, P11205
   SCHMIDT JV, 1993, J BIOL CHEM, V268, P22203
   Semenza GL, 1996, GENOMICS, V34, P437, DOI 10.1006/geno.1996.0311
   SEMENZA GL, 1994, HUM MUTAT, V3, P180, DOI 10.1002/humu.1380030304
   Semenza GL, 1996, J BIOL CHEM, V271, P32529, DOI 10.1074/jbc.271.51.32529
   Smith RF, 1996, GENOME RES, V6, P454, DOI 10.1101/gr.6.5.454
   Tian H, 1997, GENE DEV, V11, P72, DOI 10.1101/gad.11.1.72
   WANG GL, 1995, J BIOL CHEM, V270, P1230, DOI 10.1074/jbc.270.3.1230
   WANG GL, 1995, P NATL ACAD SCI USA, V92, P5510, DOI 10.1073/pnas.92.12.5510
   Wenger RH, 1996, BIOCHEM BIOPH RES CO, V223, P54, DOI 10.1006/bbrc.1996.0845
   Wenger RH, 1997, BIOL CHEM, V378, P609
   Wiener CM, 1996, BIOCHEM BIOPH RES CO, V225, P485, DOI 10.1006/bbrc.1996.1199
NR 26
TC 147
Z9 173
U1 2
U2 28
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0888-7543
EI 1089-8646
J9 GENOMICS
JI Genomics
PD SEP 1
PY 1998
VL 52
IS 2
BP 159
EP 165
DI 10.1006/geno.1998.5416
PG 7
WC Biotechnology & Applied Microbiology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biotechnology & Applied Microbiology; Genetics & Heredity
GA 128TD
UT WOS:000076421700006
PM 9782081
OA hybrid
DA 2025-04-10
ER

PT J
AU Luquero, A
   Pimentel, N
   Vilahur, G
   Badimon, L
   Borrell-Pages, M
AF Luquero, Aureli
   Pimentel, Noelia
   Vilahur, Gemma
   Badimon, Lina
   Borrell-Pages, Maria
TI Unique Splicing of Lrp5 in the Brain: A New Player in
   Neurodevelopment and Brain Maturation
SO INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
LA English
DT Article
DE LRP5; brain; RNA-seq; liver; transcriptome; synapse; retinoic acid
ID BETA-CATENIN; FUNCTIONAL INTERACTION; NERVOUS-SYSTEM; WNT PATHWAY;
   HOMOLOG; GENE; DIFFERENTIATION; OSTEOSARCOMA; TRANSITION; FAMILY
AB Low-density lipoprotein receptor-related protein 5 (LRP5) is a constitutively expressed receptor with observed roles in bone homeostasis, retinal development, and cardiac metabolism. However, the function of LRP5 in the brain remains unexplored. This study investigates LRP5's role in the central nervous system by conducting an extensive analysis using RNA-seq tools and in silico assessments. Two protein-coding Lrp5 transcripts are expressed in mice: full-length Lrp5-201 and a truncated form encoded by Lrp5-202. Wt mice express Lrp5-201 in the liver and brain and do not express the truncated form. Lrp5(-/-) mice express Lrp5-202 in the liver and brain and do not express Lrp5-201 in the liver. Interestingly, Lrp5(-/-) mouse brains show full-length Lrp5-201 expression, suggesting that LRP5 has a role in preserving brain function during development. Functional gene enrichment analysis on RNA-seq unveils dysregulated expression of genes associated with neuronal differentiation and synapse formation in the brains of Lrp5(-/-) mice compared to Wt mice. Furthermore, Gene Set Enrichment Analysis highlights downregulated expression of genes involved in retinol and linoleic acid metabolism in Lrp5(-/-) mouse brains. Tissue-specific alternative splicing of Lrp5 in Lrp5(-/-) mice supports that the expression of LRP5 in the brain is needed for the correct synthesis of vitamins and fatty acids, and it is indispensable for correct brain development.
C1 [Luquero, Aureli; Pimentel, Noelia; Vilahur, Gemma; Badimon, Lina; Borrell-Pages, Maria] Inst Recerca St Pau, Cardiovasc Program, Barcelona 08025, Spain.
   [Luquero, Aureli; Pimentel, Noelia] Univ Barcelona, Biomed Doctorate Program, Barcelona 08007, Spain.
   [Vilahur, Gemma; Badimon, Lina; Borrell-Pages, Maria] Inst Salud Carlos III, Ctr Invest Biomed Red Cardiovasc CIBER CV, Madrid 28029, Spain.
   [Badimon, Lina] Univ Autonoma Barcelona, Barcelona, Spain.
C3 University of Barcelona; CIBER - Centro de Investigacion Biomedica en
   Red; CIBERCV; Instituto de Salud Carlos III; Autonomous University of
   Barcelona
RP Borrell-Pages, M (corresponding author), Inst Recerca St Pau, Cardiovasc Program, Barcelona 08025, Spain.; Borrell-Pages, M (corresponding author), Inst Salud Carlos III, Ctr Invest Biomed Red Cardiovasc CIBER CV, Madrid 28029, Spain.
EM aluquero@santpau.cat; npimentel@santpau.cat; gvilahur@santpau.cat;
   lbadimon@santpau.cat; mborrellpa@santpau.cat
RI Borrell-Pages, Maria/Q-6307-2019; BADIMON, LINA/S-2950-2019; Badimon,
   Lina/O-4711-2014
OI Badimon, Lina/0000-0002-9162-2459; Borrell, Maria/0000-0002-1759-9756;
   Luquero, Aureli/0000-0002-1104-5963
FU Spanish Ministry of Economy and Competitiveness of Science "Agencia
   Estatal de Investigacion (AEI)" [PID2019-107160RB-I00]; FEDER "Una
   Manera de Hacer Europa" [PMP22/00108]; Institute of Health Carlos III
   (ISCIII) [CIBERCV-CB16/11/00411, ERA-CVD JTC 202-023/AC20/00054,
   PI23-00589]; Red RICORS [TERAV-RD21/0017/0013]; FEC 2022; Marato de TV3
   [202304-10]
FX This work was supported by the Spanish Ministry of Economy and
   Competitiveness of Science Agencia Estatal de Investigacion (AEI) Proj.
   Ref. AEI/10.13039/501100011033-[PID2019- 107160RB-I00]; Project
   PMP22/00108 to LB cofounded by FEDER Una Manera de Hacer Europa; the
   Institute of Health Carlos III (ISCIII) CIBERCV-CB16/11/00411 and
   ERA-CVD JTC 202-023/AC20/00054 to LB and PI23-00589 to MBP; Red RICORS
   TERAV-RD21/0017/0013 to LB; FEC 2022 to MBP and Marato de TV3 202304-10
   to MBP. AL is a predoctoral fellow (PRE2020-096422) associated to LBs
   grant PID2019-107160RB-I00. NP is part of the INVESTIGO-Program of the
   Spanish Ministery of Science.
CR Ahmad-Annuar A, 2006, J CELL BIOL, V174, P127, DOI 10.1083/jcb.200511054
   [Anonymous], ENSEMBL MOUSE LRP5 G
   Badimon L, 2021, CARDIOVASC RES, V117, P2054, DOI 10.1093/cvr/cvaa254
   Badimon L, 2019, PLOS ONE, V14, DOI 10.1371/journal.pone.0218098
   Behrens J, 1998, SCIENCE, V280, P596, DOI 10.1126/science.280.5363.596
   Behrens J, 1996, NATURE, V382, P638, DOI 10.1038/382638a0
   Bhanot P, 1996, NATURE, V382, P225, DOI 10.1038/382225a0
   Billin AN, 2000, MOL CELL BIOL, V20, P6882, DOI 10.1128/MCB.20.18.6882-6890.2000
   Borrell-Pages M, 2016, BASIC RES CARDIOL, V111, DOI 10.1007/s00395-016-0585-y
   Borrell-Pages M, 2024, CARDIOVASC RES, V120, P140, DOI 10.1093/cvr/cvad159
   Borrell-Pages M, 2015, IMMUNOL CELL BIOL, V93, P653, DOI 10.1038/icb.2015.41
   Borrell-Pagès M, 2015, J CELL MOL MED, V19, P770, DOI 10.1111/jcmm.12396
   Borrell-Pagès M, 2011, EUR HEART J, V32, P2841, DOI 10.1093/eurheartj/ehr062
   Carter M, 2005, P NATL ACAD SCI USA, V102, P12843, DOI 10.1073/pnas.0501963102
   Ciani L, 2005, NAT REV NEUROSCI, V6, P351, DOI 10.1038/nrn1665
   Clark CEJ, 2012, NEUROSIGNALS, V20, P202, DOI 10.1159/000332153
   DAVISSON MT, 1994, GENE, V147, P157, DOI 10.1016/0378-1119(94)90060-4
   Dobin A, 2013, BIOINFORMATICS, V29, P15, DOI 10.1093/bioinformatics/bts635
   Glaser T, 2005, TRENDS NEUROSCI, V28, P397, DOI 10.1016/j.tins.2005.05.008
   Grünblatt E, 2019, AM J MED GENET B, V180, P365, DOI 10.1002/ajmg.b.32695
   Guo Y, 2008, CLIN ORTHOP RELAT R, V466, P2039, DOI 10.1007/s11999-008-0344-y
   Guo Y, 2007, J ORTHOP RES, V25, P964, DOI 10.1002/jor.20356
   He TC, 1998, SCIENCE, V281, P1509, DOI 10.1126/science.281.5382.1509
   Holmen SL, 2004, J BONE MINER RES, V19, P2033, DOI 10.1359/JBMR.040907
   Jia L, 2019, MOL BRAIN, V12, DOI 10.1186/s13041-019-0525-5
   Kato M, 2002, J CELL BIOL, V157, P303, DOI 10.1083/jcb.200201089
   Krueger F., TRIMGALORE INTERNET
   Li B, 2011, BMC BIOINFORMATICS, V12, DOI 10.1186/1471-2105-12-323
   Luquero A, 2022, FASEB J, V36, DOI 10.1096/fj.202101660RR
   Maden M, 2002, NAT REV NEUROSCI, V3, P843, DOI 10.1038/nrn963
   McCaffery P, 2000, CYTOKINE GROWTH F R, V11, P233, DOI 10.1016/S1359-6101(00)00002-2
   Okerlund ND, 2011, J NEURODEV DISORD, V3, P162, DOI 10.1007/s11689-011-9083-6
   Olson CR, 2010, MOL NUTR FOOD RES, V54, P489, DOI 10.1002/mnfr.200900246
   Queiroz MP, 2019, FRONT NEUROSCI-SWITZ, V13, DOI 10.3389/fnins.2019.00370
   Raudvere U, 2019, NUCLEIC ACIDS RES, V47, pW191, DOI 10.1093/nar/gkz369
   Ren Q, 2021, FRONT CELL DEV BIOL, V9, DOI 10.3389/fcell.2021.670960
   Ritchie ME, 2015, NUCLEIC ACIDS RES, V43, DOI 10.1093/nar/gkv007
   Shtutman M, 1999, P NATL ACAD SCI USA, V96, P5522, DOI 10.1073/pnas.96.10.5522
   SIEGFRIED E, 1992, CELL, V71, P1167, DOI 10.1016/S0092-8674(05)80065-0
   Taha AY, 2020, NPJ SCI FOOD, V4, DOI 10.1038/s41538-019-0061-9
   Tekath T, 2021, BIOINFORMATICS, V37, P3781, DOI 10.1093/bioinformatics/btab629
   Valvezan AJ, 2012, FRONT MOL NEUROSCI, V5, DOI 10.3389/fnmol.2012.00001
   Varela-Nallar L, 2010, P NATL ACAD SCI USA, V107, P21164, DOI 10.1073/pnas.1010011107
   Veerapathiran S, 2020, ELIFE, V9, DOI 10.7554/eLife.59489
   Wang J, 2013, NUCLEIC ACIDS RES, V41, pW77, DOI 10.1093/nar/gkt439
   Wehrli M, 2000, NATURE, V407, P527, DOI 10.1038/35035110
   Wolffe A.P., 1998, Q REV BIOL, V73, P69, DOI [10.1086/420083, DOI 10.1086/420083]
   YangSnyder J, 1996, CURR BIOL, V6, P1302, DOI 10.1016/S0960-9822(02)70716-1
   Zechner D, 2007, DEV BIOL, V303, P181, DOI 10.1016/j.ydbio.2006.10.045
NR 49
TC 0
Z9 0
U1 0
U2 1
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
SN 1661-6596
EI 1422-0067
J9 INT J MOL SCI
JI Int. J. Mol. Sci.
PD JUN
PY 2024
VL 25
IS 12
AR 6763
DI 10.3390/ijms25126763
PG 18
WC Biochemistry & Molecular Biology; Chemistry, Multidisciplinary
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Chemistry
GA WU6I0
UT WOS:001257422000001
PM 38928468
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Bione, S
   DAdamo, P
   Maestrini, E
   Gedeon, AK
   Bolhuis, PA
   Toniolo, D
AF Bione, S
   DAdamo, P
   Maestrini, E
   Gedeon, AK
   Bolhuis, PA
   Toniolo, D
TI A novel X-linked gene, G4.5. is responsible for Barth syndrome
SO NATURE GENETICS
LA English
DT Article
ID XQ28; MITOCHONDRIA
AB Barth Syndrome is a severe inherited disorder, often fatal in childhood, characterized by cardiac and skeletal myopathy, short stature and neutropenia. The disease has been mapped to a very gene-rich region in distal portion of Xq28. We now report the identification of unique mutations in one of the genes in this region, termed G4.5, expressed at high level in cardiac and skeletal muscle, Different mRNAs can be produced by alternative splicing of the primary G4.5 transcript, encoding novel proteins that differ at the N terminus and in the central region. The mutations introduce stop codons in the open reading frame interrupting translation of most of the putative proteins (which we term 'tafazzins'), Our results suggest that G4.5 is the genetic locus responsible for the Barth syndrome.
C1 CNR,INST GENET BIOCHEM & EVOLUT,I-27100 PAVIA,ITALY.
   WOMENS & CHILDRENS HOSP,DEPT CYTOGENET & MOLEC GENET,ADELAIDE,SA 5006,AUSTRALIA.
   UNIV AMSTERDAM,ACAD MED CTR,LAB NEUROL,1105 AZ AMSTERDAM,NETHERLANDS.
C3 Consiglio Nazionale delle Ricerche (CNR); Women's & Children's Hospital;
   University of Amsterdam; Academic Medical Center Amsterdam
RI Maestrini, Elena/K-7508-2012; Toniolo, Daniela/AAE-2969-2019; D'Adamo,
   Patrizia/AAN-3919-2020; Gedeon, Agi/G-7890-2011
OI D'Adamo, Patrizia/0000-0002-0312-5541; Bione,
   Silvia/0000-0002-3924-4606; MAESTRINI, ELENA/0000-0001-5924-3179
FU Telethon [E.0297] Funding Source: Medline
CR ADES LC, 1993, AM J MED GENET, V45, P327, DOI 10.1002/ajmg.1320450309
   BARTH PG, 1983, J NEUROL SCI, V62, P327, DOI 10.1016/0022-510X(83)90209-5
   BIONE S, 1993, P NATL ACAD SCI USA, V90, P10977, DOI 10.1073/pnas.90.23.10977
   BIONE S, 1995, HUM MOL GENET, V4, P1859
   BIONE S, 1994, NAT GENET, V8, P323, DOI 10.1038/ng1294-323
   BOLHUIS PA, 1991, AM J HUM GENET, V48, P481
   FROHMAN MA, 1993, METHOD ENZYMOL, V218, P340
   GEDEON AK, 1995, J MED GENET, V32, P383, DOI 10.1136/jmg.32.5.383
   HURT EC, 1986, TRENDS BIOCHEM SCI, V11, P204, DOI 10.1016/0968-0004(86)90007-1
   KELLEY DP, NEW ENGL J MED, V330, P913
   KOZAK M, 1991, J CELL BIOL, V115, P887, DOI 10.1083/jcb.115.4.887
   McKusick V., 1990, MENDELIAN INHERITANC, V9th
   NELSON DL, 1995, IN PRESS CYTOGENET C
   Sambrook J, 1989, MOL CLONING LAB MANU
   WICKNER WT, 1985, SCIENCE, V230, P400, DOI 10.1126/science.4048938
NR 15
TC 581
Z9 640
U1 0
U2 22
PU NATURE PUBLISHING CO
PI NEW YORK
PA 345 PARK AVE SOUTH, NEW YORK, NY 10010-1707
SN 1061-4036
J9 NAT GENET
JI Nature Genet.
PD APR
PY 1996
VL 12
IS 4
BP 385
EP 389
DI 10.1038/ng0496-385
PG 5
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA UC553
UT WOS:A1996UC55300016
PM 8630491
DA 2025-04-10
ER

PT J
AU Bolger, GB
AF Bolger, Graeme B.
TI The PDE-Opathies: Diverse Phenotypes Produced by a Functionally Related
   Multigene Family
SO TRENDS IN GENETICS
LA English
DT Review
ID ROD CGMP-PHOSPHODIESTERASE; ALPHA-SUBUNIT; BETA-SUBUNIT; MUTATIONS;
   GENE; HYPERTENSION; EXPRESSION; PRKAR1A; ONSET; ORGANIZATION
AB The phosphodiesterase (PDE)-opathies, an expanding set of disorders caused by germline mutations in cyclic nucleotide PDEs, present an intriguing paradox. The enzymes encoded by the PDE family all hydrolyze cAMP and/or cGMP, but mutations in different family members produce very divergent phenotypes. Three interacting factors have been shown recently to contribute to this phenotypic diversity: (i) the 21 genes encode over 80 different isoforms, using alternative mRNA splicing and related mechanisms; (ii) the various isoforms have different regulatory mechanisms, mediated by their unique amino-terminal regulatory domains; (iii) the isoforms differ widely in their pattern of tissue expression. These mechanisms explain why many PDE-opathies are gain-of-function mutations and how they exemplify uniqueness and redundancy within a multigene family.
C1 [Bolger, Graeme B.] BZI Pharma LLC, Birmingham, AL 35203 USA.
RP Bolger, GB (corresponding author), BZI Pharma LLC, Birmingham, AL 35203 USA.
EM graemebolger@BZIpharma.com
RI Bolger, Graeme/JXM-5478-2024
FU BZI Pharma LLC
FX This work was supported by BZI Pharma LLC.
CR Ahmad F, 2015, J BIOL CHEM, V290, P6763, DOI 10.1074/jbc.M115.638585
   Azevedo MF, 2014, ENDOCR REV, V35, P195, DOI 10.1210/er.2013-1053
   Baillie GS, 2019, NAT REV DRUG DISCOV, V18, P770, DOI 10.1038/s41573-019-0033-4
   Beavo JA, 2002, NAT REV MOL CELL BIO, V3, P710, DOI 10.1038/nrm911
   Boda H, 2016, J HUM GENET, V61, P701, DOI 10.1038/jhg.2016.32
   Boikos SA, 2008, HORM METAB RES, V40, P347, DOI 10.1055/s-2008-1076694
   Bolger GB, 2007, CYCLIC NUCLEOTIDE PH, P19
   Briet C, 2017, HUM MOL GENET, V26, P3883, DOI 10.1093/hmg/ddx271
   Card GL, 2004, STRUCTURE, V12, P2233, DOI 10.1016/j.str.2004.10.004
   Cedervall P, 2015, P NATL ACAD SCI USA, V112, pE1414, DOI 10.1073/pnas.1419906112
   Conti M, 2007, ANNU REV BIOCHEM, V76, P481, DOI 10.1146/annurev.biochem.76.060305.150444
   Cummings BB, 2020, NATURE, V581, P452, DOI 10.1038/s41586-020-2329-2
   D'Andrea MR, 2005, J HISTOCHEM CYTOCHEM, V53, P895, DOI 10.1369/jhc.5A6625.2005
   Davydov EV, 2010, PLOS COMPUT BIOL, V6, DOI 10.1371/journal.pcbi.1001025
   Diggle CP, 2016, AM J HUM GENET, V98, P735, DOI 10.1016/j.ajhg.2016.03.015
   Dryja TP, 1999, INVEST OPHTH VIS SCI, V40, P1859
   DRYJA TP, 1995, P NATL ACAD SCI USA, V92, P10177, DOI 10.1073/pnas.92.22.10177
   Dvir L, 2010, AM J HUM GENET, V87, P258, DOI 10.1016/j.ajhg.2010.06.016
   Elli FM, 2016, J BONE MINER RES, V31, P1215, DOI 10.1002/jbmr.2785
   Ercu M, 2020, CIRCULATION, V142, P133, DOI 10.1161/CIRCULATIONAHA.119.043061
   Fawcett L, 2000, P NATL ACAD SCI USA, V97, P3702, DOI 10.1073/pnas.050585197
   Francis SH, 2011, PHYSIOL REV, V91, P651, DOI 10.1152/physrev.00030.2010
   Fuller ZL, 2019, NAT GENET, V51, P772, DOI 10.1038/s41588-019-0383-1
   GAL A, 1994, NAT GENET, V7, P64, DOI 10.1038/ng0594-64
   Grau T, 2011, HUM MOL GENET, V20, P719, DOI 10.1093/hmg/ddq517
   Hartong DT, 2006, LANCET, V368, P1795, DOI 10.1016/S0140-6736(06)69740-7
   HUANG SH, 1995, NAT GENET, V11, P468, DOI 10.1038/ng1295-468
   Johnson KR, 2010, BMC EVOL BIOL, V10, DOI 10.1186/1471-2148-10-247
   Karczewski KJ, 2020, NATURE, V581, P434, DOI 10.1038/s41586-020-2308-7
   Koch Linda, 2011, Nat Rev Endocrinol, V7, P64, DOI 10.1038/nrendo.2010.225
   Lee H, 2012, AM J HUM GENET, V90, P746, DOI 10.1016/j.ajhg.2012.03.004
   Libe R, 2011, J CLIN ENDOCR METAB, V96, pE208, DOI 10.1210/jc.2010-1704
   Linglart A, 2012, J CLIN ENDOCR METAB, V97, pE2328, DOI 10.1210/jc.2012-2326
   Maass PG, 2015, NAT GENET, V47, P647, DOI 10.1038/ng.3302
   Maryam A, 2019, COMPUT STRUCT BIOTEC, V17, P378, DOI 10.1016/j.csbj.2019.03.004
   Maurice DH, 2014, NAT REV DRUG DISCOV, V13, P290, DOI 10.1038/nrd4228
   MCLAUGHLIN ME, 1995, P NATL ACAD SCI USA, V92, P3249, DOI 10.1073/pnas.92.8.3249
   MCLAUGHLIN ME, 1993, NAT GENET, V4, P130, DOI 10.1038/ng0693-130
   Mencacci NE, 2016, AM J HUM GENET, V98, P763, DOI 10.1016/j.ajhg.2016.02.015
   Michot C, 2018, EUR J HUM GENET, V26, P1611, DOI 10.1038/s41431-018-0135-1
   Michot C, 2012, AM J HUM GENET, V90, P740, DOI 10.1016/j.ajhg.2012.03.003
   Minikel EV, 2020, NATURE, V581, P459, DOI 10.1038/s41586-020-2267-z
   Muhn F, 2013, CLIN GENET, V84, P531, DOI 10.1111/cge.12106
   Muradov KG, 2003, BIOCHEMISTRY-US, V42, P3305, DOI 10.1021/bi027095x
   Niccolini F, 2018, MOVEMENT DISORD, V33, P1961, DOI 10.1002/mds.27523
   Omar F, 2019, P NATL ACAD SCI USA, V116, P13320, DOI 10.1073/pnas.1822113116
   Petrovski S, 2013, PLOS GENET, V9, DOI 10.1371/journal.pgen.1003709
   Tejeda GS, 2020, P NATL ACAD SCI USA, V117, P677, DOI 10.1073/pnas.1916398117
   Toka O, 2015, HYPERTENSION, V66, P800, DOI 10.1161/HYPERTENSIONAHA.115.06000
   Vandeput F, 2013, P NATL ACAD SCI USA, V110, P19778, DOI 10.1073/pnas.1305427110
   Weisschuh N, 2018, HUM MUTAT, V39, P1366, DOI 10.1002/humu.23606
   Yau KW, 2009, CELL, V139, P246, DOI 10.1016/j.cell.2009.09.029
   Yuasa K, 2000, J BIOL CHEM, V275, P31469, DOI 10.1074/jbc.M003041200
   Yuasa K, 2001, EUR J BIOCHEM, V268, P168, DOI 10.1046/j.1432-1327.2001.01866.x
   Zhang KYJ, 2004, MOL CELL, V15, P279, DOI 10.1016/j.molcel.2004.07.005
NR 55
TC 21
Z9 24
U1 0
U2 3
PU CELL PRESS
PI CAMBRIDGE
PA 50 HAMPSHIRE ST, FLOOR 5, CAMBRIDGE, MA 02139 USA
SN 0168-9525
EI 1362-4555
J9 TRENDS GENET
JI Trends Genet.
PD JUL
PY 2021
VL 37
IS 7
BP 669
EP 681
DI 10.1016/j.tig.2021.03.002
EA JUN 2021
PG 13
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA SO4FJ
UT WOS:000658930100010
PM 33832760
OA hybrid
DA 2025-04-10
ER

PT J
AU Tokita, MJ
   Braxton, AA
   Shao, YR
   Lewis, AM
   Vincent, M
   Küry, S
   Besnard, T
   Isidor, B
   Latypova, X
   Bézieau, S
   Liu, P
   Motter, CS
   Melver, CW
   Robin, NH
   Infante, EM
   McGuire, M
   El-Gharbawy, A
   Littlejohn, RO
   McLean, SD
   Bi, WM
   Bacino, CA
   Lalani, SR
   Scott, DA
   Eng, CM
   Yang, YP
   Schaaf, CP
   Walkiewicz, MA
AF Tokita, Mari J.
   Braxton, Alicia A.
   Shao, Yunru
   Lewis, Andrea M.
   Vincent, Marie
   Kury, Sebastien
   Besnard, Thomas
   Isidor, Bertrand
   Latypova, Xenia
   Bezieau, Stephane
   Liu, Pengfei
   Motter, Connie S.
   Melver, Catherine Ward
   Robin, Nathaniel H.
   Infante, Elena M.
   McGuire, Marianne
   El-Gharbawy, Areeg
   Littlejohn, Rebecca O.
   McLean, Scott D.
   Bi, Weimin
   Bacino, Carlos A.
   Lalani, Seema R.
   Scott, Daryl A.
   Eng, Christine M.
   Yang, Yaping
   Schaaf, Christian P.
   Walkiewicz, Magdalena A.
TI De Novo Truncating Variants in SON Cause Intellectual Disability,
   Congenital Malformations, and Failure to Thrive
SO AMERICAN JOURNAL OF HUMAN GENETICS
LA English
DT Article
ID MENTAL-RETARDATION; DELETION; 21Q22.11; PROTEIN; HAPLOINSUFFICIENCY;
   THROMBOCYTOPENIA; TRANSCRIPTION; PHENOTYPE
AB SON is a key component of the spliceosomal complex and a critical mediator of constitutive and alternative splicing. Additionally, SON has been shown to influence cell-cycle progression, genomic integrity, and maintenance of pluripotency in stem cell populations. The clear functional relevance of SON in coordinating essential cellular processes and its presence in diverse human tissues suggests that intact SON might be crucial for normal growth and development. However, the phenotypic effects of deleterious germline variants in SON have not been clearly defined. Herein, we describe seven unrelated individuals with de novo variants in SON and propose that deleterious variants in SON are associated with a severe multisystem disorder characterized by developmental delay, persistent feeding difficulties, and congenital malformations, including brain anomalies.
C1 [Tokita, Mari J.; Braxton, Alicia A.; Shao, Yunru; Lewis, Andrea M.; Liu, Pengfei; Bi, Weimin; Bacino, Carlos A.; Lalani, Seema R.; Scott, Daryl A.; Eng, Christine M.; Yang, Yaping; Schaaf, Christian P.; Walkiewicz, Magdalena A.] Baylor Coll Med, Dept Mol & Human Genet, Houston, TX 77030 USA.
   [Tokita, Mari J.; Braxton, Alicia A.; Liu, Pengfei; McGuire, Marianne; Bi, Weimin; Eng, Christine M.; Yang, Yaping; Walkiewicz, Magdalena A.] Baylor Miraca Genet Labs, Houston, TX 77021 USA.
   [Shao, Yunru; Lewis, Andrea M.; Bacino, Carlos A.; Lalani, Seema R.; Scott, Daryl A.; Eng, Christine M.; Schaaf, Christian P.] Texas Childrens Hosp, Houston, TX 77030 USA.
   [Vincent, Marie; Kury, Sebastien; Besnard, Thomas; Isidor, Bertrand; Latypova, Xenia; Bezieau, Stephane] Ctr Hosp Univ Nantes, Gen Med Serv, F-44093 Nantes 1, France.
   [Isidor, Bertrand] INSERM, UMR S 957, 1 Rue Gaston Veil, F-44035 Nantes, France.
   [Motter, Connie S.; Melver, Catherine Ward] Akron Childrens Hosp, Genet Ctr, Akron, OH 44302 USA.
   [Robin, Nathaniel H.] Univ Alabama Birmingham, Dept Genet, Birmingham, AL 35294 USA.
   [Infante, Elena M.; McGuire, Marianne; El-Gharbawy, Areeg] Univ Pittsburgh, Sch Med, Pittsburgh, PA 15224 USA.
   [Infante, Elena M.; McGuire, Marianne; El-Gharbawy, Areeg] Childrens Hosp Pittsburgh, Pittsburgh, PA 15224 USA.
   [Littlejohn, Rebecca O.; McLean, Scott D.] Childrens Hosp San Antonio, San Antonio, TX 78207 USA.
   [Scott, Daryl A.] Baylor Coll Med, Dept Mol Physiol & Biophys, Houston, TX 77030 USA.
   [Schaaf, Christian P.] Texas Childrens Hosp, Jan & Dan Duncan Neurol Res Inst, Houston, TX 77030 USA.
C3 Baylor College of Medicine; Baylor College of Medicine; Baylor College
   Medical Hospital; Nantes Universite; CHU de Nantes; Institut National de
   la Sante et de la Recherche Medicale (Inserm); Akron Children's
   Hospital; University of Alabama System; University of Alabama
   Birmingham; Pennsylvania Commonwealth System of Higher Education
   (PCSHE); University of Pittsburgh; Pennsylvania Commonwealth System of
   Higher Education (PCSHE); University of Pittsburgh; Baylor College of
   Medicine; Baylor College of Medicine; Baylor College Medical Hospital
RP Schaaf, CP; Walkiewicz, MA (corresponding author), Baylor Coll Med, Dept Mol & Human Genet, Houston, TX 77030 USA.; Schaaf, CP (corresponding author), Texas Childrens Hosp, Houston, TX 77030 USA.; Schaaf, CP (corresponding author), Texas Childrens Hosp, Jan & Dan Duncan Neurol Res Inst, Houston, TX 77030 USA.
EM schaaf@bcm.edu; mwalkiew@bcm.edu
RI Schaaf, Christian/AAJ-7318-2021; Bézieau, stéphane/G-5621-2015; Besnard,
   Thomas/L-2303-2019; Isidor, Bertrand/AAJ-3456-2021; El-gharbawy,
   Areeg/N-5134-2017; Cardona, Carlos/AAS-6241-2020; KURY,
   Sebastien/G-5971-2015; Besnard, Thomas/D-1329-2018; Vincent,
   Marie/K-7342-2018
OI KURY, Sebastien/0000-0001-5497-0465; Besnard,
   Thomas/0000-0003-4804-5147; Vincent, Marie/0000-0003-1010-5618; Schaaf,
   Christian Patrick/0000-0002-2148-7490
CR Ahn EY, 2011, MOL CELL, V42, P185, DOI 10.1016/j.molcel.2011.03.014
   [Anonymous], NUCL ACIDS RES
   [Anonymous], 2015, bioRxiv
   Béri-Dexheimer M, 2008, EUR J HUM GENET, V16, P1014, DOI 10.1038/ejhg.2008.89
   Bernier FP, 2012, AM J HUM GENET, V90, P925, DOI 10.1016/j.ajhg.2012.04.004
   Carrascosa-Romero MC, 2013, AM J MED GENET A, V161, P2281, DOI 10.1002/ajmg.a.35862
   Fukai R, 2014, AM J MED GENET A, V164, P1021, DOI 10.1002/ajmg.a.36377
   Gilissen C, 2014, NATURE, V511, P344, DOI [10.1038/nature13394, 10.3389/fnhum.2013.00444]
   Graveley BR, 2000, RNA, V6, P1197, DOI 10.1017/S1355838200000960
   Hickey CJ, 2014, J CELL BIOCHEM, V115, P224, DOI 10.1002/jcb.24672
   Hoyer J, 2007, J MED GENET, V44, P629, DOI 10.1136/jmg.2007.050914
   Huen MSY, 2010, CELL CYCLE, V9, P2679, DOI 10.4161/cc.9.13.12151
   Izumi K, 2012, AM J MED GENET A, V158A, P1535, DOI 10.1002/ajmg.a.35368
   Katzaki E, 2010, AM J MED GENET A, V152A, P1711, DOI 10.1002/ajmg.a.33478
   KHAN IM, 1994, ANN HUM GENET, V58, P25, DOI 10.1111/j.1469-1809.1994.tb00723.x
   Lee H, 2014, JAMA-J AM MED ASSOC, V312, P1880, DOI 10.1001/jama.2014.14604
   Lehalle D, 2015, CLIN GENET, V88, P405, DOI 10.1111/cge.12596
   Lindstrand A, 2010, CLIN GENET, V77, P145, DOI 10.1111/j.1399-0004.2009.01289.x
   Lu XY, 2014, WIRES RNA, V5, P637, DOI 10.1002/wrna.1235
   Lyle R, 2009, EUR J HUM GENET, V17, P454, DOI 10.1038/ejhg.2008.214
   MATTIONI T, 1992, CHROMOSOMA, V101, P618, DOI 10.1007/BF00360539
   Padgett RA, 2012, TRENDS GENET, V28, P147, DOI 10.1016/j.tig.2012.01.001
   Roberson EDO, 2011, EUR J HUM GENET, V19, P235, DOI 10.1038/ejhg.2010.150
   Sacco-Bubulya P, 2002, J CELL BIOL, V156, P425, DOI 10.1083/jcb.200107017
   Saitoh N, 2004, MOL BIOL CELL, V15, P3876, DOI 10.1091/mbc.E04-03-0253
   Sawyer SL, 2016, CLIN GENET, V89, P275, DOI 10.1111/cge.12654
   Sharma A, 2011, J CELL SCI, V124, P4286, DOI 10.1242/jcs.092239
   Shinawi M, 2008, BLOOD, V112, P1042, DOI 10.1182/blood-2008-01-135970
   Spector DL, 2011, CSH PERSPECT BIOL, V3, DOI 10.1101/cshperspect.a000646
   Thevenon J, 2011, AM J MED GENET A, V155A, P126, DOI 10.1002/ajmg.a.33809
   Wang GS, 2007, NAT REV GENET, V8, P749, DOI 10.1038/nrg2164
   Wynn SL, 2000, GENOMICS, V68, P57, DOI 10.1006/geno.2000.6254
   Yang YP, 2014, JAMA-J AM MED ASSOC, V312, P1870, DOI 10.1001/jama.2014.14601
   Zhong XY, 2009, MOL CELL, V35, P1, DOI 10.1016/j.molcel.2009.06.016
   Zhu XL, 2015, GENET MED, V17, P774, DOI 10.1038/gim.2014.191
NR 35
TC 42
Z9 48
U1 0
U2 6
PU CELL PRESS
PI CAMBRIDGE
PA 50 HAMPSHIRE ST, FLOOR 5, CAMBRIDGE, MA 02139 USA
SN 0002-9297
EI 1537-6605
J9 AM J HUM GENET
JI Am. J. Hum. Genet.
PD SEP 1
PY 2016
VL 99
IS 3
BP 720
EP 727
DI 10.1016/j.ajhg.2016.06.035
PG 8
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA DV7KM
UT WOS:000383114800017
PM 27545676
OA Bronze, Green Published
DA 2025-04-10
ER

PT J
AU Chen, JW
   Ghosh, R
   Finberg, RW
   Bergelson, JM
AF Chen, JW
   Ghosh, R
   Finberg, RW
   Bergelson, JM
TI Structure and chromosomal localization of the murine coxsackievirus and
   adenovirus receptor gene
SO DNA AND CELL BIOLOGY
LA English
DT Article
ID PROMOTER SEQUENCES; B VIRUSES; EXPRESSION; MOUSE; MYOCARDITIS; HOMOLOG;
   PROTEIN; BRAIN; CAR
AB We analyzed BAC genomic clones encoding the murine coxsackievirus and adenovirus receptor ( mCAR). The mCAR gene is situated on the distal portion of murine chromosome 16, and is composed of at least eight exons, with intron-exon boundaries similar to those reported for the human CAR gene. We previously described two cDNAs encoding mCAR isoforms: the extracellular and transmembrane portions of both are encoded by exons 1-6; the cytoplasmic domain of mCAR 1 is encoded by exon 7, whereas mCAR 2 results from an RNA splice linking the proximal portion of exon 7 to an alternative exon 8. RT-PCR analysis of the mCAR RNA 59-terminus suggests that transcription may begin 141-161 nucleotides upstream of the ATG translational start site.
C1 Childrens Hosp Philadelphia, Div Infect Dis & Immunol, Philadelphia, PA 19104 USA.
   Univ Massachusetts, Med Ctr, Dept Med, Worcester, MA USA.
C3 University of Pennsylvania; Pennsylvania Medicine; Childrens Hospital of
   Philadelphia; University of Massachusetts System; University of
   Massachusetts Worcester
RP Bergelson, JM (corresponding author), Childrens Hosp Philadelphia, Div Infect Dis & Immunol, 1202 Abramson Res Ctr,3615 Civic Ctr Blvd, Philadelphia, PA 19104 USA.
FU NHLBI NIH HHS [R01 HL 54734-04] Funding Source: Medline
CR Bergelson JM, 1997, SCIENCE, V275, P1320, DOI 10.1126/science.275.5304.1320
   Bergelson JM, 1998, J VIROL, V72, P415, DOI 10.1128/JVI.72.1.415-419.1998
   Bjorn Andersson R.P. T., 2000, Gene Func. Dis, V1, P82, DOI DOI 10.1002/1438-826X(200009)1:2<82::AID-GNFD82>3.0.CO;2-Y
   Bowles KR, 1999, HUM GENET, V105, P354, DOI 10.1007/s004390051114
   Bowles NE, 1998, CURR OPIN CARDIOL, V13, P179
   Cohen CJ, 2001, P NATL ACAD SCI USA, V98, P15191, DOI 10.1073/pnas.261452898
   Fechner H, 1999, GENE THER, V6, P1520, DOI 10.1038/sj.gt.3301030
   Honda T, 2000, MOL BRAIN RES, V77, P19, DOI 10.1016/S0169-328X(00)00036-X
   Ito M, 2000, CIRC RES, V86, P275, DOI 10.1161/01.RES.86.3.275
   Knudsen S, 1999, BIOINFORMATICS, V15, P356, DOI 10.1093/bioinformatics/15.5.356
   Milanesi L, 1996, COMPUT APPL BIOSCI, V12, P399
   Mural RJ, 2002, SCIENCE, V296, P1661, DOI 10.1126/science.1069193
   Noutsias M, 2001, CIRCULATION, V104, P275
   Ohler U., 2000, PAC S BIOCOMPUT, P377
   Okegawa T, 2001, CANCER RES, V61, P6592
   Petrella J, 2002, J VIROL, V76, P10503, DOI 10.1128/JVI.76.20.10503-10506.2002
   PRESTRIDGE DS, 1995, J MOL BIOL, V249, P923, DOI 10.1006/jmbi.1995.0349
   Thoelen I, 2001, BIOCHEM BIOPH RES CO, V287, P216, DOI 10.1006/bbrc.2001.5535
   Thoelen I, 2001, BIOCHEM BIOPH RES CO, V288, P805, DOI 10.1006/bbrc.2001.5851
   Tomko RP, 1997, P NATL ACAD SCI USA, V94, P3352, DOI 10.1073/pnas.94.7.3352
   Xu RL, 1996, VIRUS RES, V46, P157, DOI 10.1016/S0168-1702(96)01398-6
NR 21
TC 24
Z9 26
U1 0
U2 2
PU MARY ANN LIEBERT INC PUBL
PI LARCHMONT
PA 2 MADISON AVENUE, LARCHMONT, NY 10538 USA
SN 1044-5498
J9 DNA CELL BIOL
JI DNA Cell Biol.
PD APR
PY 2003
VL 22
IS 4
BP 253
EP 259
DI 10.1089/104454903321908647
PG 7
WC Biochemistry & Molecular Biology; Cell Biology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology; Genetics & Heredity
GA 687AZ
UT WOS:000183354800005
PM 12823902
DA 2025-04-10
ER

PT J
AU Bottini, N
   Bottini, E
   Gloria-Bottini, F
   Mustelin, T
AF Bottini, N
   Bottini, E
   Gloria-Bottini, F
   Mustelin, T
TI Low-molecular-weight protein tyrosine phosphatase and human disease: in
   search of biochemical mechanisms
SO ARCHIVUM IMMUNOLOGIAE ET THERAPIAE EXPERIMENTALIS
LA English
DT Review
DE tyrosine phosphatase; genetic polymorphisms; allergy; asthma; obesity
ID CELL ACID-PHOSPHATASE; PHOSPHOTYROSINE-PHOSPHATASE; GROWTH-FACTOR;
   SIGNAL-TRANSDUCTION; HUMAN ADAPTABILITY; CRYSTAL-STRUCTURE; ACP1;
   ASSOCIATION; ISOZYMES; GENE
AB A major challenge in the post-genomic era is to identify the physiological functions of genes and elucidate the molecular basis for human disease. Genetic polymorphisms offer a convenient avenue for these efforts by providing evidence for the involvement of a given gene in human pathophysiology. Here we review the current evidence linking the low-molecular-weight protein tyrosine phosphatase (LMPTP) to several common diseases, including allergy, asthma, obesity, myocardial hypertrophy, and Alzheimer's disease. Based on the known effects of the genetic polymorphisms on the alternative mRNA splicing and enzyme levels of LMPTP, we discuss the possible molecular mechanisms of LMPTP involvement in these diseases.
C1 Burnham Inst, La Jolla Canc Res Ctr, Program Signal Transduct, La Jolla, CA 92037 USA.
   Univ Roma Tor Vergata, Dept Neurosci, Rome, Italy.
   Univ Roma Tor Vergata, Dept Biopathol, Rome, Italy.
C3 Sanford Burnham Prebys Medical Discovery Institute; University of Rome
   Tor Vergata; University of Rome Tor Vergata
RP Burnham Inst, La Jolla Canc Res Ctr, Program Signal Transduct, 10901 N Torrey Pines Rd, La Jolla, CA 92037 USA.
EM tmustelin@burnham-inst.org
RI ; Ingegnoli, Francesca/B-6226-2017
OI Mustelin, Tomas/0000-0001-5912-8840; Ingegnoli,
   Francesca/0000-0002-6727-1273
FU NIAID NIH HHS [AI35603, AI40552, AI48032] Funding Source: Medline
CR AMANTE A, 1990, J PERINAT MED, V18, P275, DOI 10.1515/jpme.1990.18.4.275
   BERTI A, 1994, FEBS LETT, V349, P7, DOI 10.1016/0014-5793(94)00620-2
   BOIVIN P, 1986, BIOCHEM BIOPH RES CO, V134, P557, DOI 10.1016/S0006-291X(86)80456-9
   Bottini E, 1998, DIS MARKERS, V14, P143, DOI 10.1155/1998/861096
   Bottini E, 1999, AM J PHYS ANTHROPOL, V108, P241, DOI 10.1002/(SICI)1096-8644(199902)108:2<241::AID-AJPA9>3.0.CO;2-Z
   BOTTINI E, 1971, SCIENCE, V171, P409, DOI 10.1126/science.171.3969.409
   BOTTINI E, 1995, HUM GENET, V96, P629, DOI 10.1007/BF00210290
   BOTTINI E, 1990, HUM BIOL, V62, P403
   BOTTINI E, 1985, EARLY HUM DEV, V10, P237, DOI 10.1016/0378-3782(85)90054-4
   Bottini E, 1997, BLOOD, V89, P2613, DOI 10.1182/blood.V89.7.2613
   Bottini E, 2001, AM J HUM BIOL, V13, P753, DOI 10.1002/ajhb.1121
   Bottini N, 2000, DIS MARKERS, V16, P163, DOI 10.1155/2000/101739
   BOTTINI N, 2001, UNPUB ASS ACID PHOSP
   BOTTINI N, 2001, UNPUB GENOTYPES CYTO
   BOTTINI N, IN PRESS EUR J ALLER
   BOTTINI N, 2001, UNPUB ACTIVATION ZAP
   BRYSON GLM, 1995, GENOMICS, V30, P133
   CHERNOFF J, 1985, ARCH BIOCHEM BIOPHYS, V240, P135, DOI 10.1016/0003-9861(85)90016-5
   Chiarugi P, 1997, BIOCHEM BIOPH RES CO, V238, P676, DOI 10.1006/bbrc.1997.7355
   Cirri P, 1996, J BIOL CHEM, V271, P2604, DOI 10.1074/jbc.271.5.2604
   CIRRI P, 1993, EUR J BIOCHEM, V214, P647, DOI 10.1111/j.1432-1033.1993.tb17965.x
   COMINGS D, 2001, UNPUB ASS ACID PHOSP
   DISSING J, 1987, BIOCHEM GENET, V25, P901, DOI 10.1007/BF00502609
   DISSING J, 1992, BIOCHIM BIOPHYS ACTA, V1121, P261, DOI 10.1016/0167-4838(92)90155-7
   DISSING J, 1993, BIOCHIM BIOPHYS ACTA, V1162, P275, DOI 10.1016/0167-4838(93)90291-X
   DISSING J, 1990, BIOCHIM BIOPHYS ACTA, V1041, P232, DOI 10.1016/0167-4838(90)90277-M
   DISSING J, 1991, J BIOL CHEM, V266, P20619
   FUCHS KR, 1992, BIOCHEM BIOPH RES CO, V189, P1598, DOI 10.1016/0006-291X(92)90259-N
   GloriaBottini F, 1997, HUM GENET, V101, P158, DOI 10.1007/s004390050606
   GloriaBottini F, 1996, NATURE, V379, P395, DOI 10.1038/379395a0
   GloriaBottini F, 1996, EXPERIENTIA, V52, P340, DOI 10.1007/BF01919537
   GloriaBottini F, 1996, DIS MARKERS, V12, P261, DOI 10.1155/1996/814192
   Grangeasse C, 1998, J MOL BIOL, V278, P339, DOI 10.1006/jmbi.1998.1650
   HARRISON ML, 1991, J BIOL CHEM, V266, P4106
   HEINRIKSON RL, 1969, J BIOL CHEM, V244, P299
   HOPKINSON DA, 1963, NATURE, V199, P969, DOI 10.1038/199969a0
   Huang LW, 1999, J BIOL CHEM, V274, P38183, DOI 10.1074/jbc.274.53.38183
   LAZARUK KDA, 1993, BIOCHEM BIOPH RES CO, V196, P440, DOI 10.1006/bbrc.1993.2269
   LOW PS, 1987, J BIOL CHEM, V262, P4592
   Lucarini N, 1998, DIS MARKERS, V14, P121, DOI 10.1155/1998/145391
   Lucarini N, 1997, DIS MARKERS, V13, P169
   LUCARINI N, 1990, EXPERIENTIA, V46, P90, DOI 10.1007/BF01955426
   Lucarini N, 1997, HUM BIOL, V69, P509
   MACCARI AM, 2001, UNPUB LMPTP MODIFIER
   Marian AJ, 2000, LANCET, V355, P58, DOI 10.1016/S0140-6736(99)06187-5
   Maron BJ, 1997, LANCET, V350, P127, DOI 10.1016/S0140-6736(97)01282-8
   MARRACCINI P, 1994, FEBS LETT, V344, P157, DOI 10.1016/0014-5793(94)00377-7
   Miller DT, 2000, GENE, V243, P1, DOI 10.1016/S0378-1119(99)00553-3
   Modesti A, 1998, FEBS LETT, V431, P111, DOI 10.1016/S0014-5793(98)00732-7
   MOHRENWEISER HW, 1982, AM J HUM GENET, V34, P425
   MONDESERT O, 1994, J BIOL CHEM, V269, P27996
   Mustelin T, 2002, FRONT BIOSCI-LANDMRK, V7, pD85, DOI 10.2741/mustelin
   MUSTELIN T, 2001, IN PRESS EUR J ALLER
   Oh S S, 1997, Curr Opin Hematol, V4, P148
   OSTANIN K, 1995, J BIOL CHEM, V270, P18491, DOI 10.1074/jbc.270.31.18491
   PAGGI A, 1991, DIS MARKERS, V9, P1
   PALMARINO R, 1975, AM J PHYS ANTHROPOL, V43, P177, DOI 10.1002/ajpa.1330430205
   Pei JJ, 1998, J NEURAL TRANSM, V105, P69, DOI 10.1007/s007020050039
   RAMPONI G, 1992, INT J CANCER, V51, P652, DOI 10.1002/ijc.2910510424
   RAMPONI G, 1989, FEBS LETT, V250, P469, DOI 10.1016/0014-5793(89)80778-1
   RAMPONI G, 1994, ADV PROT PHOSPHATASE, V8, P1
   Rigacci S, 1996, J BIOL CHEM, V271, P1278, DOI 10.1074/jbc.271.3.1278
   Rudbeck L, 2000, ANN HUM GENET, V64, P107, DOI 10.1017/S0003480000007995
   RUGGIERO M, 1993, FEBS LETT, V326, P294, DOI 10.1016/0014-5793(93)81811-D
   SENSABAUGH GF, 1993, HUM MOL GENET, V2, P1079, DOI 10.1093/hmg/2.7.1079-a
   SHEKELS LL, 1992, PROTEIN SCI, V1, P710, DOI 10.1002/pro.5560010603
   SHIMOHAMA S, 1995, BRAIN RES, V699, P125, DOI 10.1016/0006-8993(95)00995-3
   SHIMOHAMA S, 1993, ANN NEUROL, V33, P616, DOI 10.1002/ana.410330610
   SHIMOHAMA S, 1994, BRAIN RES, V662, P185, DOI 10.1016/0006-8993(94)90811-7
   STEFANI M, 1993, FEBS LETT, V326, P131, DOI 10.1016/0014-5793(93)81776-V
   Stein E, 1998, GENE DEV, V12, P667, DOI 10.1101/gad.12.5.667
   SU XD, 1994, NATURE, V370, P575, DOI 10.1038/370575a0
   Tailor P, 1997, J BIOL CHEM, V272, P5371, DOI 10.1074/jbc.272.9.5371
   Tailor P, 1999, EUR J BIOCHEM, V262, P277, DOI 10.1046/j.1432-1327.1999.00353.x
   Tanino H, 1999, BIOL PHARM BULL, V22, P794
   WO YYP, 1992, J BIOL CHEM, V267, P10856
   Zhang M, 1998, J BIOL CHEM, V273, P21714, DOI 10.1074/jbc.273.34.21714
   Zhang M., 1995, ADV PROTEIN PHOSPHAT, V9, P1
   ZHANG ZY, 1990, ARCH BIOCHEM BIOPHYS, V282, P39, DOI 10.1016/0003-9861(90)90084-C
NR 79
TC 92
Z9 114
U1 0
U2 4
PU SPRINGER BASEL AG
PI BASEL
PA PICASSOPLATZ 4, BASEL, 4052, SWITZERLAND
SN 0004-069X
EI 1661-4917
J9 ARCH IMMUNOL THER EX
JI Arch. Immunol. Ther. Exp.
PY 2002
VL 50
IS 2
BP 95
EP 104
PG 10
WC Immunology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Immunology
GA 546EE
UT WOS:000175258500002
PM 12022706
DA 2025-04-10
ER

PT J
AU Doblado, M
   Moley, KH
AF Doblado, Manuel
   Moley, Kelle H.
TI Facilitative glucose transporter 9, a unique hexose and urate
   transporter
SO AMERICAN JOURNAL OF PHYSIOLOGY-ENDOCRINOLOGY AND METABOLISM
LA English
DT Review
DE splice variants; uric acid; fructose
ID URIC-ACID; SUBSTRATE SPECIFICITIES; FRUCTOSE TRANSPORTER; EXOFACIAL
   VESTIBULE; ESCHERICHIA-COLI; XENOPUS OOCYTES; BINDING-SITE; GLUT1;
   SLC2A9; EXPRESSION
AB Doblado M, Moley KH. Facilitative glucose transporter 9, a unique hexose and urate transporter. Am J Physiol Endocrinol Metab 297: E831-E835, 2009. First published June 30, 2009; doi:10.1152/ajpendo.00296.2009.-GLUT9 is a novel, facilitative glucose transporter isoform that exists as two alternative splice variants encoding two proteins that differ in their NH2-terminal sequence (GLUT9a and GLUT9b). Both forms of GLUT9 protein and mRNA are expressed in the epithelia of various tissues; however, the two splice variants are expressed differentially within polarized cells, with GLUT9a localized predominantly on the basolateral surfaces and GLUT9b expressed on apical surfaces. Protein expression of GLUT9 drops under conditions of starvation but increases with addition of glucose and under hyperglycemic conditions. The substrate specificity of GLUT9 is unique since, in addition to transporting hexose sugars, it also is a high-capacity uric acid transporter. Several recent large-scale human genetic studies show a correlation between SNPs mapped to GLUT9 and the serum uric acid levels in several different cohorts. The relationship between GLUT9 and uric acid is highly clinically significant. Elevated uric acid levels have been associated with metabolic syndrome, obesity, diabetes, hypertension, and chronic renal failure. Although some believe uric acid is elevated as a result of these diseases, there is now evidence that uric acid may play a role in the pathogenesis of these diseases. It is also known that GLUT9 is expressed in articular cartilage and is a uric acid transporter, and thus it is possible that GLUT9 plays a role in gout, a disease of uric acid deposition in the joints. In addition, some studies have suggested that intake of fructose plays an important role in causing elevated serum uric acid levels, especially in diabetes and obesity. It is possible that GLUT9, which seems to be both a fructose and a uric acid transporter, plays an important role in these conditions associated with hyperuricemia.
C1 [Doblado, Manuel; Moley, Kelle H.] Washington Univ, Sch Med, Dept Obstet & Gynecol, St Louis, MO 63110 USA.
C3 Washington University (WUSTL)
RP Moley, KH (corresponding author), Washington Univ, Sch Med, Dept Obstet & Gynecol, 660 S Euclid Ave, St Louis, MO 63110 USA.
EM moleyk@wustl.edu
FU National Institute of Diabetes and Digestive and Kidney Diseases (
   NIDDK) [T32-DK007130/T32-DK-007120, DK-70351]; American Diabetes
   Association
FX This research was supported by National Institute of Diabetes and
   Digestive and Kidney Diseases ( NIDDK) Training Grant
   T32-DK007130/T32-DK-007120 ( M. Doblado), NIDDK Grant DK-70351 ( K. H.
   Moley), and an American Diabetes Association research grant awarded to
   K. H. Moley.
CR Abramson J, 2003, SCIENCE, V301, P610, DOI 10.1126/science.1088196
   Alisio A, 2004, J BIOL CHEM, V279, P26540, DOI 10.1074/jbc.M402303200
   Anzai N, 2008, J BIOL CHEM, V283, P26834, DOI 10.1074/jbc.C800156200
   Augustin R, 2004, J BIOL CHEM, V279, P16229, DOI 10.1074/jbc.M312226200
   Brandstätter A, 2008, DIABETES CARE, V31, P1662, DOI 10.2337/dc08-0349
   BURANT CF, 1992, BIOCHEMISTRY-US, V31, P10414, DOI 10.1021/bi00157a032
   BURANT CF, 1992, J BIOL CHEM, V267, P14523
   Carayannopoulos MO, 2004, ENDOCRINOLOGY, V145, P1435, DOI 10.1210/en.2003-1264
   Caulfield MJ, 2008, PLOS MED, V5, P1509, DOI 10.1371/journal.pmed.0050197
   COLVILLE CA, 1993, BIOCHEM J, V290, P701, DOI 10.1042/bj2900701
   Dehghan A, 2008, LANCET, V372, P1953, DOI 10.1016/S0140-6736(08)61343-4
   Döring A, 2008, NAT GENET, V40, P430, DOI 10.1038/ng.107
   EVANS SA, 2009, ENDOCRINOLO IN PRESS
   Feig DI, 2008, NEW ENGL J MED, V359, P1811, DOI 10.1056/NEJMra0800885
   GOULD GW, 1991, BIOCHEMISTRY-US, V30, P5139, DOI 10.1021/bi00235a004
   Hruz PW, 2001, MOL MEMBR BIOL, V18, P183
   Huang YF, 2003, SCIENCE, V301, P616, DOI 10.1126/science.1087619
   Joost HG, 2001, MOL MEMBR BIOL, V18, P247, DOI 10.1080/09687680110090456
   Keembiyehetty C, 2006, MOL ENDOCRINOL, V20, P686, DOI 10.1210/me.2005-0010
   Kim ST, 2007, REPROD SCI, V14, P445, DOI 10.1177/1933719107306226
   Li S, 2007, PLOS GENET, V3, P2156, DOI 10.1371/journal.pgen.0030194
   Manolescu AR, 2007, MOL MEMBR BIOL, V24, P455, DOI 10.1080/09687680701298143
   Matsuo H, 2008, AM J HUM GENET, V83, P744, DOI 10.1016/j.ajhg.2008.11.001
   Mene P, 2008, J HYPERTENS, V26, P2085, DOI 10.1097/HJH.0b013e32830e4945
   Mobasheri A, 2005, CELL BIOL INT, V29, P249, DOI 10.1016/j.cellbi.2004.11.024
   Mobasheri A, 2002, CELL BIOL INT, V26, P297, DOI 10.1006/cbir.2001.0850
   Mueckler M, 2004, J BIOL CHEM, V279, P10494, DOI 10.1074/jbc.M310786200
   MUECKLER M, 1994, J BIOL CHEM, V269, P17765
   Mueckler M, 1997, J BIOL CHEM, V272, P30141, DOI 10.1074/jbc.272.48.30141
   Nakagawa T, 2006, AM J PHYSIOL-RENAL, V290, pF625, DOI 10.1152/ajprenal.00140.2005
   Pantaleon M, 2001, BIOL REPROD, V64, P1247, DOI 10.1095/biolreprod64.4.1247
   Phay JE, 2000, GENOMICS, V66, P217, DOI 10.1006/geno.2000.6195
   Seatter MJ, 1998, BIOCHEMISTRY-US, V37, P1322, DOI 10.1021/bi972322u
   Takanaga H, 2008, BBA-BIOMEMBRANES, V1778, P1091, DOI 10.1016/j.bbamem.2007.11.015
   Uldry M, 2004, PFLUG ARCH EUR J PHY, V447, P480, DOI 10.1007/s00424-003-1085-0
   Vitart V, 2008, NAT GENET, V40, P437, DOI 10.1038/ng.106
   Wu XH, 2002, GENOMICS, V80, P553, DOI 10.1006/geno.2002.7010
NR 37
TC 71
Z9 84
U1 0
U2 29
PU AMER PHYSIOLOGICAL SOC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA
SN 0193-1849
EI 1522-1555
J9 AM J PHYSIOL-ENDOC M
JI Am. J. Physiol.-Endocrinol. Metab.
PD OCT
PY 2009
VL 297
IS 4
BP E831
EP E835
DI 10.1152/ajpendo.00296.2009
PG 5
WC Endocrinology & Metabolism; Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism; Physiology
GA 498KR
UT WOS:000270139400001
PM 19797240
OA Green Published
DA 2025-04-10
ER

PT J
AU Ostrowski, D
   Heinrich, R
AF Ostrowski, Daniela
   Heinrich, Ralf
TI Alternative Erythropoietin Receptors in the Nervous System
SO JOURNAL OF CLINICAL MEDICINE
LA English
DT Review
DE erythropoietin; non-hematopoietic functions; neuroprotection;
   regeneration; alternative erythropoietin receptors; common beta chain
   receptor; ephrin B4 receptor; cytokine receptor-like factor 3
ID ISCHEMIA-REPERFUSION INJURY; ENDOTHELIAL PROGENITOR-CELL; IMPROVES
   CARDIAC-FUNCTION; TRAUMATIC BRAIN-INJURY; IN-VITRO; GM-CSF;
   PHOSPHATIDYLINOSITOL 3-KINASE; ERYTHROID-DIFFERENTIATION; HIPPOCAMPAL
   NEUROGENESIS; ENHANCES NEUROGENESIS
AB In addition to its regulatory function in the formation of red blood cells (erythropoiesis) in vertebrates, Erythropoietin (Epo) contributes to beneficial functions in a variety of non-hematopoietic tissues including the nervous system. Epo protects cells from apoptosis, reduces inflammatory responses and supports re-establishment of compromised functions by stimulating proliferation, migration and differentiation to compensate for lost or injured cells. Similar neuroprotective and regenerative functions of Epo have been described in the nervous systems of both vertebrates and invertebrates, indicating that tissue-protective Epo-like signaling has evolved prior to its erythropoietic function in the vertebrate lineage. Epo mediates its erythropoietic function through a homodimeric Epo receptor (EpoR) that is also widely expressed in the nervous system. However, identification of neuroprotective but non-erythropoietic Epo splice variants and Epo derivatives indicated the existence of other types of Epo receptors. In this review, we summarize evidence for potential Epo receptors that might mediate Epo's tissue-protective function in non-hematopoietic tissue, with focus on the nervous system. In particular, besides EpoR, we discuss three other potential neuroprotective Epo receptors: (1) a heteroreceptor consisting of EpoR and common beta receptor (beta cR), (2) the Ephrin (Eph) B4 receptor and (3) the human orphan cytokine receptor-like factor 3 (CRLF3).
C1 [Ostrowski, Daniela] Truman State Univ, Dept Biol, Kirksville, MO 63501 USA.
   [Heinrich, Ralf] Georg August Univ Gottingen, Inst Zool, Dept Cellular Neurobiol, D-37073 Gottingen, Germany.
C3 University of Gottingen
RP Ostrowski, D (corresponding author), Truman State Univ, Dept Biol, Kirksville, MO 63501 USA.; Heinrich, R (corresponding author), Georg August Univ Gottingen, Inst Zool, Dept Cellular Neurobiol, D-37073 Gottingen, Germany.
EM dostrowski@truman.edu; rheinri1@gwdg.de
FU Department of Biology at Truman State University
FX We acknowledge the support of the Department of Biology at Truman State
   University for providing partial funding toward the completion of this
   work.
CR Adamcio B, 2008, BMC BIOL, V6, DOI 10.1186/1741-7007-6-37
   ANAGNOSTOU A, 1994, P NATL ACAD SCI USA, V91, P3974, DOI 10.1073/pnas.91.9.3974
   Arcasoy MO, 2008, BRIT J HAEMATOL, V141, P14, DOI 10.1111/j.1365-2141.2008.07014.x
   Ardalan MR, 2013, MED PRIN PRACT, V22, P70, DOI 10.1159/000340060
   Ashton RS, 2012, NAT NEUROSCI, V15, P1399, DOI 10.1038/nn.3212
   Aydin A, 2003, BRAIN DEV-JPN, V25, P494, DOI 10.1016/S0387-7604(03)00039-1
   Bader A, 2011, REJUV RES, V14, P57, DOI 10.1089/rej.2010.1050
   Bennis Y, 2012, J THROMB HAEMOST, V10, P1914, DOI 10.1111/j.1538-7836.2012.04835.x
   Bernaudin M, 1999, J CEREBR BLOOD F MET, V19, P643, DOI 10.1097/00004647-199906000-00007
   Bianchi R, 2006, CLIN CANCER RES, V12, P2607, DOI 10.1158/1078-0432.CCR-05-2177
   Blits-Huizinga CT, 2004, IUBMB LIFE, V56, P257, DOI 10.1080/15216540412331270076
   Bohr S, 2015, J MOL MED, V93, P199, DOI 10.1007/s00109-014-1218-2
   Bond WS, 2014, FRONT IMMUNOL, V5, DOI 10.3389/fimmu.2014.00523
   Bonnas C. B., 2009, THESIS
   Bonnas C, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-03167-0
   BONSDORFF E, 1948, ACTA PHYSIOL SCAND, V16, P150, DOI 10.1111/j.1748-1716.1948.tb00535.x
   Boulay JL, 2003, IMMUNITY, V19, P159, DOI 10.1016/S1074-7613(03)00211-5
   Brines M, 2006, KIDNEY INT, V70, P246, DOI 10.1038/sj.ki.5001546
   Brines M, 2005, NAT REV NEUROSCI, V6, P484, DOI 10.1038/nrn1687
   Brines M, 2004, P NATL ACAD SCI USA, V101, P14907, DOI 10.1073/pnas.0406491101
   Brines M, 2008, P NATL ACAD SCI USA, V105, P10925, DOI 10.1073/pnas.0805594105
   Brines M, 2012, MOL MED, V18, P486, DOI 10.2119/molmed.2011.00414
   Brines M, 2010, BLOOD PURIFICAT, V29, P86, DOI 10.1159/000245630
   Brines ML, 2000, P NATL ACAD SCI USA, V97, P10526, DOI 10.1073/pnas.97.19.10526
   Brown S, 2001, CURR BIOL, V11, P1700, DOI 10.1016/S0960-9822(01)00524-3
   Brown WM, 2007, STEM CELLS, V25, P718, DOI 10.1634/stemcells.2006-0687
   Burger D, 2006, CARDIOVASC RES, V72, P51, DOI 10.1016/j.cardiores.2006.06.026
   Calapai G, 2000, EUR J PHARMACOL, V401, P349, DOI 10.1016/S0014-2999(00)00466-0
   Calvillo L, 2003, P NATL ACAD SCI USA, V100, P4802, DOI 10.1073/pnas.0630444100
   Campana WM, 2003, EUR J NEUROSCI, V18, P1497, DOI 10.1046/j.1460-9568.2003.02875.x
   Cendrowski J, 2016, CYTOKINE GROWTH F R, V32, P63, DOI 10.1016/j.cytogfr.2016.07.002
   Chateauvieux S, 2011, BIOCHEM PHARMACOL, V82, P1291, DOI 10.1016/j.bcp.2011.06.045
   Chen ZY, 2007, J BIOL CHEM, V282, P25875, DOI 10.1074/jbc.M701988200
   Chou CF, 2004, BLOOD, V104, P1498, DOI 10.1182/blood-2003-10-3404
   Chu CY, 2008, CELL MOL LIFE SCI, V65, P3545, DOI 10.1007/s00018-008-8231-y
   Cokic VP, 2012, J TRANSL MED, V10, DOI 10.1186/1479-5876-10-116
   Collino M, 2015, PHARMACOL THERAPEUT, V151, P32, DOI 10.1016/j.pharmthera.2015.02.005
   D'Andrea RJ, 2000, EXP HEMATOL, V28, P231, DOI 10.1016/S0301-472X(99)00159-9
   Dang C, 2006, ONCOL REP, V16, P513
   DelMastro L, 1997, J CLIN ONCOL, V15, P2715, DOI 10.1200/JCO.1997.15.7.2715
   Depping R, 2005, J THORAC CARDIOV SUR, V130, P877, DOI 10.1016/j.jtcvs.2004.12.041
   Dinarello CA, 2007, EUR J IMMUNOL, V37, pS34, DOI 10.1002/eji.200737772
   Dines M, 2015, NEUROBIOL LEARN MEM, V124, P62, DOI 10.1016/j.nlm.2015.07.003
   Ding J, 2017, MOL NEUROBIOL, V54, P5051, DOI 10.1007/s12035-016-0022-0
   Drescher U, 1997, CURR OPIN NEUROBIOL, V7, P75, DOI 10.1016/S0959-4388(97)80123-7
   Dzierzak E, 2013, CSH PERSPECT MED, V3, DOI 10.1101/cshperspect.a011601
   Echigoya MH, 2005, NEPHRON EXP NEPHROL, V100, pE21, DOI 10.1159/000084109
   Ehrenreich H, 2007, MOL PSYCHIATR, V12, P206, DOI 10.1038/sj.mp.4001907
   Ehrenreich H, 2004, METAB BRAIN DIS, V19, P195, DOI 10.1023/B:MEBR.0000043969.96895.3c
   Ehrenreich H, 2002, MOL MED, V8, P495, DOI 10.1007/BF03402029
   Ehrenreich H, 2009, STROKE, V40, pE647, DOI 10.1161/STROKEAHA.109.564872
   El-Kordi A, 2009, BMC BIOL, V7, DOI 10.1186/1741-7007-7-37
   Elfar JC, 2008, J BONE JOINT SURG AM, V90A, P1644, DOI 10.2106/JBJS.G.00557
   Elliott S, 2006, BLOOD, V107, P1892, DOI 10.1182/blood-2005-10-4066
   ERSLEV A, 1953, BLOOD, V8, P349, DOI 10.1182/blood.V8.4.349.349
   Chamorro ME, 2013, BBA-MOL CELL RES, V1833, P1960, DOI 10.1016/j.bbamcr.2013.04.006
   Fandrey J, 2004, AM J PHYSIOL-REG I, V286, pR977, DOI 10.1152/ajpregu.00577.2003
   Foley LS, 2017, ANN THORAC SURG, V104, P1909, DOI 10.1016/j.athoracsur.2017.07.052
   Foley LS, 2015, ANN THORAC SURG, V100, P41, DOI 10.1016/j.athoracsur.2015.01.027
   Garrido P, 2016, INT J MOL SCI, V17, DOI 10.3390/ijms17010028
   Genc S, 2004, RESTOR NEUROL NEUROS, V22, P105
   Ghezzi P, 2004, CELL DEATH DIFFER, V11, pS37, DOI 10.1038/sj.cdd.4401450
   Ghezzi P., 2013, METHODS MOL BIOL, V982
   Grebien F, 2008, BLOOD, V111, P4511, DOI 10.1182/blood-2007-07-102848
   Hahn N, 2017, FRONT MOL NEUROSCI, V10, DOI 10.3389/fnmol.2017.00223
   Hamada K, 2003, ARTERIOSCL THROM VAS, V23, P190, DOI 10.1161/01.ATV.0000055440.89758.C2
   Hamed S, 2014, WOUND REPAIR REGEN, V22, P23, DOI 10.1111/wrr.12135
   Hamed S, 2010, J INVEST DERMATOL, V130, P287, DOI 10.1038/jid.2009.219
   HANAZONO Y, 1995, BIOCHEM BIOPH RES CO, V208, P1060, DOI 10.1006/bbrc.1995.1442
   Hassouna I, 2016, MOL PSYCHIATR, V21, P1752, DOI 10.1038/mp.2015.212
   Heeschen C, 2003, BLOOD, V102, P1340, DOI 10.1182/blood-2003-01-0223
   Heinrich R, 2017, VITAM HORM, V105, P181, DOI 10.1016/bs.vh.2017.02.004
   Henderson JT, 2001, NEURON, V32, P1041, DOI 10.1016/S0896-6273(01)00553-0
   Hruska M, 2012, MOL CELL NEUROSCI, V50, P35, DOI 10.1016/j.mcn.2012.03.004
   Jegalian AG, 2002, J INTERF CYTOK RES, V22, P853, DOI 10.1089/107999002760274863
   Jelkmann W, 2011, J PHYSIOL-LONDON, V589, P1251, DOI 10.1113/jphysiol.2010.195057
   Jia Y, 2012, FASEB J, V26, P2847, DOI 10.1096/fj.11-196618
   Jubinsky PT, 1997, BLOOD, V90, P1867, DOI 10.1182/blood.V90.5.1867
   Juul S, 2007, SEMIN FETAL NEONAT M, V12, P250, DOI 10.1016/j.siny.2007.01.015
   Juul SE, 1999, PEDIATR DEVEL PATHOL, V2, P148, DOI 10.1007/s100249900103
   Juul SE, 1998, EARLY HUM DEV, V52, P235, DOI 10.1016/S0378-3782(98)00030-9
   Juul SE, 1998, PEDIATR RES, V43, P40, DOI 10.1203/00006450-199801000-00007
   Kästner A, 2012, MOL MED, V18, P1029, DOI 10.2119/molmed.2012.00190
   Kania A, 2016, NAT REV MOL CELL BIO, V17, P240, DOI 10.1038/nrm.2015.16
   Khan AI, 2013, DIS MODEL MECH, V6, P1021, DOI 10.1242/dmm.011908
   Khankin EV, 2010, PLOS ONE, V5, DOI 10.1371/journal.pone.0009246
   Kirkeby A, 2007, J NEUROSCI METH, V164, P50, DOI 10.1016/j.jneumeth.2007.03.026
   Klingmuller U, 1996, P NATL ACAD SCI USA, V93, P8324, DOI 10.1073/pnas.93.16.8324
   Knabe W, 2004, ANAT EMBRYOL, V207, P503, DOI 10.1007/s00429-003-0365-y
   Kretz A, 2005, MOL CELL NEUROSCI, V29, P569, DOI 10.1016/j.mcn.2005.04.009
   Kumral A, 2003, BIOL NEONATE, V83, P224, DOI 10.1159/000068926
   Lamon E, 2014, PHYSIOL REP, V2, DOI 10.1002/phy2.256
   Larpthaveesarp A, 2016, NEUROBIOL DIS, V93, P57, DOI 10.1016/j.nbd.2016.04.006
   Leist M, 2004, SCIENCE, V305, P239, DOI 10.1126/science.1098313
   Lin CS, 1996, GENE DEV, V10, P154, DOI 10.1101/gad.10.2.154
   Liongue C, 2007, BMC EVOL BIOL, V7, DOI 10.1186/1471-2148-7-120
   Lisabeth EM, 2013, CSH PERSPECT BIOL, V5, DOI 10.1101/cshperspect.a009159
   Liu C, 1997, J BIOL CHEM, V272, P32395, DOI 10.1074/jbc.272.51.32395
   Liu TT, 2017, CELL PHYSIOL BIOCHEM, V41, P819, DOI 10.1159/000459693
   Lu DY, 2005, J NEUROTRAUM, V22, P1011, DOI 10.1089/neu.2005.22.1011
   Malik J, 2013, HAEMATOLOGICA, V98, P1778, DOI 10.3324/haematol.2013.087361
   Marcuzzi F, 2016, J NEUROCHEM, V139, P596, DOI 10.1111/jnc.13757
   Matthews DJ, 1996, P NATL ACAD SCI USA, V93, P9471, DOI 10.1073/pnas.93.18.9471
   McGraw K, 2017, VITAM HORM, V105, P79, DOI 10.1016/bs.vh.2017.02.002
   McPherson RJ, 2010, CURR OPIN PEDIATR, V22, P139, DOI 10.1097/MOP.0b013e328336eb57
   Mennini T, 2006, MOL MED, V12, P153, DOI 10.2119/2006-00045.Mennini
   Miljus N, 2014, NEUROSCIENCE, V258, P218, DOI 10.1016/j.neuroscience.2013.11.020
   Miljus N, 2017, J NEUROCHEM, V141, P63, DOI 10.1111/jnc.13967
   Miller JL, 2015, MOL PHARMACOL, V88, P357, DOI 10.1124/mol.115.098400
   Miskowiak K, 2008, EXP BRAIN RES, V184, P313, DOI 10.1007/s00221-007-1102-1
   Miskowiak K, 2007, BIOL PSYCHIAT, V62, P1244, DOI 10.1016/j.biopsych.2007.01.011
   Miskowiak K, 2007, J NEUROSCI, V27, P2788, DOI 10.1523/JNEUROSCI.5013-06.2007
   Miskowiak KW, 2016, J CLIN PSYCHIAT, V77, pE1639, DOI 10.4088/JCP.15m10480
   Mitkovski M, 2015, J CEREBR BLOOD F MET, V35, P1233, DOI 10.1038/jcbfm.2015.100
   MIURA O, 1994, BLOOD, V84, P1501
   Moore E, 2011, ANN INTENSIVE CARE, V1, DOI 10.1186/2110-5820-1-3
   Morishita E, 1997, NEUROSCIENCE, V76, P105, DOI 10.1016/s0306-4522(96)00306-5
   Murphy JM, 2006, VITAM HORM, V74, P1, DOI 10.1016/S0083-6729(06)74001-8
   Myklebust JH, 2002, EXP HEMATOL, V30, P990, DOI 10.1016/S0301-472X(02)00868-8
   Nachbauer W, 2012, J NEUROPATH EXP NEUR, V71, P708, DOI 10.1097/NEN.0b013e31825fed76
   Nadam J, 2007, NEUROBIOL DIS, V25, P412, DOI 10.1016/j.nbd.2006.10.009
   Nagai A, 2001, J NEUROPATH EXP NEUR, V60, P386, DOI 10.1093/jnen/60.4.386
   NAKAMURA Y, 1992, SCIENCE, V257, P1138, DOI 10.1126/science.257.5073.1138
   Narmoneva DA, 2004, CIRCULATION, V110, P962, DOI 10.1161/01.CIR.0000140667.37070.07
   Nichol A, 2015, LANCET, V386, P2499, DOI 10.1016/S0140-6736(15)00386-4
   Ninot G, 2006, J SPORT SCI, V24, P383, DOI 10.1080/02640410500131340
   Nogawa-Kosaka N, 2010, EXP HEMATOL, V38, P363, DOI 10.1016/j.exphem.2010.02.009
   Noguchi Constance Tom, 2008, Expert Reviews in Molecular Medicine, V10, P1, DOI 10.1017/S1462399408000860
   Ogilvie M, 2000, J BIOL CHEM, V275, P39754, DOI 10.1074/jbc.M004999200
   Ogunshola Omolara O, 2013, Methods Mol Biol, V982, P13, DOI 10.1007/978-1-62703-308-4_2
   Osredkar D, 2010, NEUROBIOL DIS, V38, P259, DOI 10.1016/j.nbd.2010.01.015
   Ostrowski D, 2011, NEUROSCIENCE, V188, P95, DOI 10.1016/j.neuroscience.2011.05.018
   Ott C, 2015, MOL MED, V21, P816, DOI 10.2119/molmed.2015.00192.erratum
   Paffett-Lugassy N, 2007, BLOOD, V110, P2718, DOI 10.1182/blood-2006-04-016535
   Palis J, 2014, FRONT PHYSIOL, V5, DOI 10.3389/fphys.2014.00003
   Pankratova S, 2012, J NEUROCHEM, V121, P915, DOI 10.1111/j.1471-4159.2012.07751.x
   Pradeep S, 2015, CANCER CELL, V28, P610, DOI 10.1016/j.ccell.2015.09.008
   Prass K, 2003, STROKE, V34, P1981, DOI 10.1161/01.STR.0000080381.76409.B2
   Pregi N, 2006, BBA-MOL CELL RES, V1763, P238, DOI 10.1016/j.bbamcr.2005.12.011
   Robertson CS, 2014, JAMA-J AM MED ASSOC, V312, P36, DOI 10.1001/jama.2014.6490
   Rogers HM, 2008, EXP HEMATOL, V36, P17, DOI 10.1016/j.exphem.2007.08.014
   Rotter R, 2008, J ORTHOP RES, V26, P1618, DOI 10.1002/jor.20692
   Sadamoto Y, 1998, BIOCHEM BIOPH RES CO, V253, P26, DOI 10.1006/bbrc.1998.9748
   Sanchez PE, 2009, P NATL ACAD SCI USA, V106, P9848, DOI 10.1073/pnas.0901840106
   Sanchis-Gomar F, 2014, INT J CARDIOL, V171, P116, DOI 10.1016/j.ijcard.2013.12.011
   Sargin D, 2011, BMC BIOL, V9, DOI 10.1186/1741-7007-9-27
   Sargin D, 2010, BEST PRACT RES-CLIN, V24, P573, DOI 10.1016/j.bpa.2010.10.005
   Sasaki A, 2000, J BIOL CHEM, V275, P29338, DOI 10.1074/jbc.M003456200
   Schmidt EK, 2004, BMC BIOL, V2, DOI 10.1186/1741-7007-2-7
   Schuler B, 2012, FASEB J, V26, P3884, DOI 10.1096/fj.11-191197
   Shein NA, 2005, J CEREBR BLOOD F MET, V25, P1456, DOI 10.1038/sj.jcbfm.9600142
   Shen Y, 2009, NEUROPATHOLOGY, V29, P528, DOI 10.1111/j.1440-1789.2009.01005.x
   Shimizu R, 1999, EXP HEMATOL, V27, P229, DOI 10.1016/S0301-472X(98)00048-4
   Sirén AL, 2001, P NATL ACAD SCI USA, V98, P4044, DOI 10.1073/pnas.051606598
   Soliz J, 2007, J PHYSIOL-LONDON, V583, P329, DOI 10.1113/jphysiol.2007.133454
   Steinle JJ, 2002, J BIOL CHEM, V277, P43830, DOI 10.1074/jbc.M207221200
   Su KH, 2011, J CELL PHYSIOL, V226, P3330, DOI 10.1002/jcp.22678
   Suenobu S, 2002, BIOCHEM BIOPH RES CO, V293, P1124, DOI 10.1016/S0006-291X(02)00330-3
   Sugawa M, 2002, NEUROSCI RES, V44, P391, DOI 10.1016/S0168-0102(02)00161-X
   Suzuki N, 2002, BLOOD, V100, P2279, DOI 10.1182/blood-2002-01-0124
   Swartjes M, 2011, ANESTHESIOLOGY, V115, P1084, DOI 10.1097/ALN.0b013e31822fcefd
   Syed RS, 1998, NATURE, V395, P511, DOI 10.1038/26773
   Szenajch J, 2010, BBA-REV CANCER, V1806, P82, DOI 10.1016/j.bbcan.2010.04.002
   Tada H, 2006, CARDIOVASC RES, V71, P466, DOI 10.1016/j.cardiores.2006.05.010
   Teng R., 2013, NAT COMMUN, V2, P1, DOI [10.1038/ncomms1526.Disrupted, DOI 10.1038/NCOMMS1526.DISRUPTED]
   Todd KL, 2017, J NEUROSCI, V37, P3331, DOI 10.1523/JNEUROSCI.3738-16.2017
   Trincavelli ML, 2013, INT J MOL SCI, V14, P2258, DOI 10.3390/ijms14022258
   Tsai PT, 2006, J NEUROSCI, V26, P1269, DOI 10.1523/JNEUROSCI.4480-05.2006
   Um M, 2007, CELL SIGNAL, V19, P634, DOI 10.1016/j.cellsig.2006.08.014
   Uversky VN, 2017, MOL BIOSYST, V13, P56, DOI 10.1039/c6mb00657d
   van der Meer P, 2005, J AM COLL CARDIOL, V46, P125, DOI 10.1016/j.jacc.2005.03.044
   Villa P, 2007, J CEREBR BLOOD F MET, V27, P552, DOI 10.1038/sj.jcbfm.9600370
   Wandzioch E, 2004, BLOOD, V104, P51, DOI 10.1182/blood-2003-07-2554
   Wang L, 2004, STROKE, V35, P1732, DOI 10.1161/01.STR.0000132196.49028.a4
   Wang L, 2014, INT J BIOL SCI, V10, P921, DOI 10.7150/ijbs.9518
   Wang M, 2017, SCI REP-UK, V7, DOI [10.1038/s41598-017-03137-6, 10.1038/s41598-017-18302-0]
   Wenker SD, 2010, J CELL BIOCHEM, V110, P151, DOI 10.1002/jcb.22521
   Westenbrink BD, 2007, EUR HEART J, V28, P2018, DOI 10.1093/eurheartj/ehm177
   Westenfelder C, 1999, KIDNEY INT, V55, P808, DOI 10.1046/j.1523-1755.1999.055003808.x
   WITTHUHN BA, 1993, CELL, V74, P227, DOI 10.1016/0092-8674(93)90414-L
   Wu H, 1997, P NATL ACAD SCI USA, V94, P1806, DOI 10.1073/pnas.94.5.1806
   Wu H, 1999, DEVELOPMENT, V126, P3597
   WU H, 1995, CELL, V83, P59, DOI 10.1016/0092-8674(95)90234-1
   Wu YW, 2016, PEDIATRICS, V137, DOI 10.1542/peds.2016-0191
   Yamaji R, 1996, EUR J BIOCHEM, V239, P494, DOI 10.1111/j.1432-1033.1996.0494u.x
   Yang C, 2013, EXP BIOL MED, V238, P111, DOI 10.1258/ebm.2012.012185
   Yang F, 2009, INT J BIOCHEM CELL B, V41, P2240, DOI 10.1016/j.biocel.2009.04.022
   Yasuda Y, 1998, J BIOL CHEM, V273, P25381, DOI 10.1074/jbc.273.39.25381
   Yin ZS, 2010, AM J NEURORADIOL, V31, P509, DOI 10.3174/ajnr.A1820
   Yu XB, 2002, DEVELOPMENT, V129, P505
   Yu XB, 2001, BLOOD, V98, P475, DOI 10.1182/blood.V98.2.475
   Zafiriou MP, 2014, STEM CELLS, V32, P2480, DOI 10.1002/stem.1741
   Zhang J, 2003, BLOOD, V102, P3938, DOI 10.1182/blood-2003-05-1479
   Zhang W, 2009, J CLIN NEUROSCI, V16, P554, DOI 10.1016/j.jocn.2008.06.013
   Zhang YXL, 2009, MOL CELL, V33, P266, DOI 10.1016/j.molcel.2008.11.026
   Zhang YY, 2014, INT J MOL SCI, V15, P10296, DOI 10.3390/ijms150610296
   Zhao C, 2015, J CARDIOVASC PHARM, V65, P593, DOI 10.1097/FJC.0000000000000229
   Zou YR, 2016, TRANSPL P, V48, P217, DOI 10.1016/j.transproceed.2016.01.009
NR 198
TC 66
Z9 70
U1 2
U2 15
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
SN 2077-0383
J9 J CLIN MED
JI J. Clin. Med.
PD FEB
PY 2018
VL 7
IS 2
AR 24
DI 10.3390/jcm7020024
PG 20
WC Medicine, General & Internal
WE Science Citation Index Expanded (SCI-EXPANDED)
SC General & Internal Medicine
GA FZ3WQ
UT WOS:000427522200014
PM 29393890
OA gold, Green Submitted, Green Published
DA 2025-04-10
ER

PT J
AU Sato, M
   Hutchinson, DS
   Bengtsson, T
   Floren, A
   Langel, Ü
   Horinouchi, T
   Evans, BA
   Summers, RJ
AF Sato, M
   Hutchinson, DS
   Bengtsson, T
   Floren, A
   Langel, Ü
   Horinouchi, T
   Evans, BA
   Summers, RJ
TI Functional domains of the mouse β3-Adrenoceptor associated
   with differential G protein coupling
SO JOURNAL OF PHARMACOLOGY AND EXPERIMENTAL THERAPEUTICS
LA English
DT Article
ID RECEPTOR SPLICE VARIANTS; SITE-DIRECTED MUTAGENESIS; PDZ-BINDING MOTIF;
   ADRENERGIC-RECEPTOR; 5-HT4 RECEPTOR; BETA-2-ADRENERGIC RECEPTOR;
   SIGNAL-TRANSDUCTION; MOLECULAR-CLONING; CARDIAC MYOCYTES; LIGAND-BINDING
AB Alternative splicing of mouse beta(3)-adrenoceptor transcripts produces an additional receptor isoform (beta(3b)-adrenoceptor) with a C terminus comprising 17 amino acids distinct from the 13 in the known receptor (beta(3a)-adrenoceptor). We have shown that the beta(3b)-adrenoceptor couples to both G(s) and G(i), whereas the beta(3a)-adrenoceptor couples only to G(s). To define the regions involved in this differential G protein coupling, we have compared wild-type, truncated, and mutant beta(3)-adrenoceptors. In Chinese hamster ovary cells expressing beta(3)-adrenoceptors truncated at the splicing point, cAMP accumulation with CL316243 [( R,R)-5-[2-[[2-(3-chlorophenyl)2-hydroxyethyl]-amino]-propyl]1,3-benzodioxole-2,2-dicarboxylate] increased by 59% following pretreatment with pertussis toxin, suggesting that the C-terminal region of the beta(3a)-adrenoceptor inhibits coupling to G(i). We next utilized the cell-penetrating peptide Transportan 10 (Tp10) to introduce peptides comprising the different C-terminal tail fragments into cells expressing beta(3a)-adrenoceptor, beta(3b)-adrenoceptor, and the truncated beta(3)-adrenoceptor. Treatment with beta(3a)-Tp10 (1 mu M) caused cAMP responses to CL316243 in the beta(3a)-adrenoceptor to become pertussis toxin-sensitive and display a 30% increase over control, whereas the other peptides did not affect any receptor. Mutation at a potential tyrosine phosphorylation site (Tyr392Ala beta(3a)-adrenoceptor) did not alter responses or pertussis toxin sensitivity relative to the parent receptor. Surprisingly, a Ser388Ala/ Ser389Ala mutant beta(3b)-adrenoceptor became unresponsive to CL316243 while retaining an extracellular acidification rate response to SR59230A [3-(2ethylphenoxy)-1-[(1,S)-1,2,3,4-tetrahydronapth-1-ylamino]-2S2-propanoloxalate]. Our findings suggest that the beta(3a)-adrenoceptor cannot couple to G(i) because of conformational changes induced by a protein(s) that interacts with residues in the C-terminal tail or because this protein( s) affects the intracellular localization of the beta(3a)-adrenoceptor.
C1 Monash Univ, Dept Pharmacol, Clayton, Vic 3800, Australia.
   Stockholm Univ, Dept Physiol, Wenner Gren Inst, Arrhenius Labs F3, S-10691 Stockholm, Sweden.
   Stockholm Univ, Arrhenius Labs Nat Sci, Dept Neurochem & Neurotoxicol, S-10691 Stockholm, Sweden.
C3 Monash University; Stockholm University; Stockholm University
RP Monash Univ, Dept Pharmacol, POB 13E, Clayton, Vic 3800, Australia.
EM summers@med.monash.edu.au
RI Langel, Ulo/K-9773-2018; Hutchinson, Dana/K-3795-2012; Horinouchi,
   Takahiro/G-1770-2012; Summers, Roger/F-6351-2011
OI Sato, Masaaki/0000-0003-0564-4318; Hutchinson, Dana/0000-0001-9947-0106;
   Langel, Ulo/0000-0001-6107-0844; Summers, Roger/0000-0002-8367-4056
CR BENSAID M, 1993, FEBS LETT, V318, P223, DOI 10.1016/0014-5793(93)80516-W
   Blom N, 1999, J MOL BIOL, V294, P1351, DOI 10.1006/jmbi.1999.3310
   Cao WH, 2000, J BIOL CHEM, V275, P38131, DOI 10.1074/jbc.C000592200
   CHANDHRY A, 1994, CELL SIGNAL, V6, P457
   Chang DJ, 1998, FEBS LETT, V422, P279, DOI 10.1016/S0014-5793(98)00024-6
   CHEUNG AH, 1989, MOL PHARMACOL, V35, P132
   Claeysen S, 1999, MOL PHARMACOL, V55, P910
   Evans BA, 1999, BRIT J PHARMACOL, V127, P1525, DOI 10.1038/sj.bjp.0702688
   GERALD C, 1995, EMBO J, V14, P2806, DOI 10.1002/j.1460-2075.1995.tb07280.x
   Gerhardt CC, 1999, MOL PHARMACOL, V55, P255, DOI 10.1124/mol.55.2.255
   GRANNEMAN JG, 1995, AM J PHYSIOL-CELL PH, V268, pC1040
   GRANNEMAN JG, 1992, MOL PHARMACOL, V42, P964
   GRANNEMAN JG, 1993, MOL PHARMACOL, V44, P264
   Granneman JG, 1998, MOL PHARMACOL, V53, P856
   Gros J, 1998, EUR J BIOCHEM, V251, P590, DOI 10.1046/j.1432-1327.1998.2510590.x
   GUAN XM, 1995, MOL PHARMACOL, V48, P492
   Hällbrink M, 2001, BBA-BIOMEMBRANES, V1515, P101, DOI 10.1016/S0005-2736(01)00398-4
   HAUSDORFF WP, 1991, P NATL ACAD SCI USA, V88, P2979, DOI 10.1073/pnas.88.8.2979
   HIGASHIJIMA T, 1988, J BIOL CHEM, V263, P6491
   HIRASAWA A, 1995, FEBS LETT, V363, P256, DOI 10.1016/0014-5793(95)00330-C
   Hutchinson D. S., 2005, P 4 BRIT PHARM SOC F, VP071
   Hutchinson DS, 2005, J PHARMACOL EXP THER, V312, P1064, DOI 10.1124/jpet.104.076901
   Hutchinson DS, 2002, BRIT J PHARMACOL, V135, P1903, DOI 10.1038/sj.bjp.0704654
   Krobert KA, 2001, N-S ARCH PHARMACOL, V363, P620, DOI 10.1007/s002100000369
   Lindquist C, 2000, RADIOSURG, V3, P1
   Marin EP, 2000, J BIOL CHEM, V275, P1930, DOI 10.1074/jbc.275.3.1930
   Martin NP, 2004, CELL SIGNAL, V16, P1397, DOI 10.1016/j.cellsig.2004.05.002
   Mizuno K, 2000, EUR J PHARMACOL, V404, P63, DOI 10.1016/S0014-2999(00)00601-4
   NAMBA T, 1993, NATURE, V365, P166, DOI 10.1038/365166a0
   ODOWD BF, 1988, J BIOL CHEM, V263, P15985
   Pindon A, 2002, MOL PHARMACOL, V61, P85, DOI 10.1124/mol.61.1.85
   Pinna LA, 1996, BBA-MOL CELL RES, V1314, P191, DOI 10.1016/S0167-4889(96)00083-3
   Pooga M, 1998, FASEB J, V12, P67, DOI 10.1096/fasebj.12.1.67
   Soeder KJ, 1999, J BIOL CHEM, V274, P12017, DOI 10.1074/jbc.274.17.12017
   Soomets U, 2000, BBA-BIOMEMBRANES, V1467, P165, DOI 10.1016/S0005-2736(00)00216-9
   VAN SA, 1993, EUR J BIOCHEM, V213, P1117
   VANETTI M, 1993, FEBS LETT, V331, P260, DOI 10.1016/0014-5793(93)80349-Y
   Xiang Y, 2003, P NATL ACAD SCI USA, V100, P10776, DOI 10.1073/pnas.1831718100
   Xiang Y, 2002, J BIOL CHEM, V277, P33783, DOI 10.1074/jbc.M204136200
NR 39
TC 24
Z9 28
U1 0
U2 0
PU AMER SOC PHARMACOLOGY EXPERIMENTAL THERAPEUTICS
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3995 USA
SN 0022-3565
EI 1521-0103
J9 J PHARMACOL EXP THER
JI J. Pharmacol. Exp. Ther.
PD DEC
PY 2005
VL 315
IS 3
BP 1354
EP 1361
DI 10.1124/jpet.105.091736
PG 8
WC Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Pharmacology & Pharmacy
GA 984VZ
UT WOS:000233335100046
PM 16144970
DA 2025-04-10
ER

PT J
AU Wang, H
   Sartini, BL
   Millette, CF
   Kilpatrick, DL
AF Wang, Hang
   Sartini, Becky L.
   Millette, Clarke F.
   Kilpatrick, Daniel L.
TI A developmental switch in transcription factor isoforms during
   spermatogenesis controlled by alternative messenger RNA 3'-end formation
SO BIOLOGY OF REPRODUCTION
LA English
DT Article
DE developmental biology; gametogenesis; gene regulation; spermatogenesis;
   testis
ID ELEMENT-BINDING PROTEIN-2; MALE GERM-CELLS; CLEAVAGE STIMULATION FACTOR;
   TISSUE-SPECIFIC EXPRESSION; POLYADENYLATION FACTOR; GENE-EXPRESSION;
   SERTOLI CELLS; IMPORTIN-BETA; POLY(A) SITE; RAT TESTIS
AB Spermatogenic cells elaborate a highly specialized differentiation program that is mediated in part by germ cell-enriched transcription factors. This includes a novel member of the sterol response element-binding factor family, SREBF2_v1/SREBP2gc. Somatic SREBFs are predominantly synthesized as precursor proteins and are critical regulators of cholesterol and fatty acid synthesis. In contrast, SREBF2_v1 bypasses the precursor pathway and has been directly implicated in spermatogenic cell-specific gene expression. During spermatogenesis, SREBF2 precursor transcripts predominate in premeiotic stages, while SREBF2_v1 is highly upregulated specifically in pachytene spermatocytes and round spermatids. In the present study, we demonstrate that Srebf2_v1 mRNAs are present in the testis of several mammalian species, including humans. The basis for the stage-dependent transition in SREBF2 isoforms was also investigated. A 3' rapid amplification of cDNA ends (RACE)-PCR analysis of the rat and human revealed that Srebf2_v1 transcripts are generated by alternative pre-mRNA cleavage/polyadenylation. This involves the use of an intronic, A(A/U)UAAA-independent poly(A) signal within intron 7 of the Srebf2 gene. Developmentally regulated competition between germ cell factors that control RNA splicing and pre-mRNA cleavage/ polyadenylation may underlie this process. These results define an important role for alternative polyadenylation in male germ cell gene expression and development by controlling a stage-dependent switch in transcription factor structure and function during spermatogenesis. The Srebf2 gene thus provides a useful model to explore the role of alternative polyadenylation in regulating stage-dependent functions of important protein regulators in spermatogenic cells.
C1 Univ Massachusetts, Sch Med, Dept Mol & Cellular Physiol, Worcester, MA 01655 USA.
   Univ S Carolina, Dept Cell Biol, Sch Med, Columbia, SC 29208 USA.
C3 University of Massachusetts System; University of Massachusetts
   Worcester; University of South Carolina System; University of South
   Carolina Columbia
RP Kilpatrick, DL (corresponding author), Univ Massachusetts, Sch Med, Dept Mol & Cellular Physiol, Worcester, MA 01655 USA.
EM daniel.kilpatrick@umassmed.edu
FU NICHD NIH HHS [R01 HD045723] Funding Source: Medline
CR ALT FW, 1980, CELL, V20, P293, DOI 10.1016/0092-8674(80)90615-7
   BELLVE AR, 1977, J CELL BIOL, V74, P68, DOI 10.1083/jcb.74.1.68
   BELLVE AR, 1977, J HISTOCHEM CYTOCHEM, V25, P480, DOI 10.1177/25.7.893996
   Dass B, 2001, BIOL REPROD, V64, P1722, DOI 10.1095/biolreprod64.6.1722
   Eddy EM, 1998, SEMIN CELL DEV BIOL, V9, P451, DOI 10.1006/scdb.1998.0201
   Edwalds-Gilbert G, 1995, Nucleic Acids Symp Ser, P229
   EDWALDSGILBERT G, 1995, MOL CELL BIOL, V15, P6420
   Elliott DJ, 2004, INT J ANDROL, V27, P328, DOI 10.1111/j.1365-2605.2004.00496.x
   FOULKES NS, 1993, NATURE, V362, P264, DOI 10.1038/362264a0
   Hecht NB, 1998, BIOESSAYS, V20, P555, DOI 10.1002/(SICI)1521-1878(199807)20:7<555::AID-BIES6>3.0.CO;2-J
   Horton JD, 2002, COLD SPRING HARB SYM, V67, P491, DOI 10.1101/sqb.2002.67.491
   Horton JD, 2002, J CLIN INVEST, V109, P1125, DOI 10.1172/JCI200215593
   Kamma H, 1999, EXP CELL RES, V246, P399, DOI 10.1006/excr.1998.4323
   KAMMA H, 1995, EXP CELL RES, V221, P187, DOI 10.1006/excr.1995.1366
   Kashiwabara S, 2002, SCIENCE, V298, P1999, DOI 10.1126/science.1074632
   KEW D, 1989, MOL ENDOCRINOL, V3, P179, DOI 10.1210/mend-3-1-179
   Kimmins S, 2004, REPRODUCTION, V128, P5, DOI 10.1530/rep.1.00170
   Lee J, 2004, MOL HUM REPROD, V10, P259, DOI 10.1093/molehr/gah037
   Malkov M, 1998, BIOL REPROD, V59, P84, DOI 10.1095/biolreprod59.1.84
   Nagoshi E, 1999, MOL BIOL CELL, V10, P2221, DOI 10.1091/mbc.10.7.2221
   Nagoshi E, 2001, MOL CELL BIOL, V21, P2779, DOI 10.1128/MCB.21.8.2779-2789.2001
   OBRIEN DA, 1994, BIOL REPROD, V50, P429, DOI 10.1095/biolreprod50.2.429
   PETERSON ML, 1986, P NATL ACAD SCI USA, V83, P8883, DOI 10.1073/pnas.83.23.8883
   Phillips C, 2004, MOL CELL BIOL, V24, P6162, DOI 10.1128/MCB.24.14.6162-6171.2004
   Proudfoot NJ, 2002, CELL, V108, P501, DOI 10.1016/S0092-8674(02)00617-7
   SHAPER NL, 1990, P NATL ACAD SCI USA, V87, P791, DOI 10.1073/pnas.87.2.791
   Takagaki Y, 1996, CELL, V87, P941, DOI 10.1016/S0092-8674(00)82000-0
   Veraldi KL, 2001, MOL CELL BIOL, V21, P1228, DOI 10.1128/MCB.21.4.1228-1238.2001
   Walker W H, 1999, Front Horm Res, V25, P34
   Wallace AM, 2004, BIOL REPROD, V70, P1080, DOI 10.1095/biolreprod.103.022947
   Wallace AM, 1999, P NATL ACAD SCI USA, V96, P6763, DOI 10.1073/pnas.96.12.6763
   Wang H, 2004, MOL CELL BIOL, V24, P10681, DOI 10.1128/MCB.24.24.10681-10688.2004
   Wang H, 2002, MOL CELL BIOL, V22, P8478, DOI 10.1128/MCB.22.24.8478-8490.2002
   WINGETT D, 1992, NUCLEIC ACIDS RES, V20, P3183, DOI 10.1093/nar/20.12.3183
   Yang GY, 2003, BIOL REPROD, V68, P1620, DOI 10.1095/biolreprod.102.012013
   YANG JX, 1994, GENE DEV, V8, P1910, DOI 10.1101/gad.8.16.1910
   YANG JX, 1995, J BIOL CHEM, V270, P12152, DOI 10.1074/jbc.270.20.12152
   Yang LV, 2003, DEV DYNAM, V228, P606, DOI 10.1002/dvdy.10399
   ZHENGWEI Y, 1990, BIOL REPROD, V43, P629, DOI 10.1095/biolreprod43.4.629
NR 39
TC 16
Z9 22
U1 0
U2 4
PU OXFORD UNIV PRESS INC
PI CARY
PA JOURNALS DEPT, 2001 EVANS RD, CARY, NC 27513 USA
SN 0006-3363
EI 1529-7268
J9 BIOL REPROD
JI Biol. Reprod.
PD SEP
PY 2006
VL 75
IS 3
BP 318
EP 323
DI 10.1095/biolreprod.106.052209
PG 6
WC Reproductive Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Reproductive Biology
GA 075VE
UT WOS:000239912800002
PM 16723505
DA 2025-04-10
ER

PT J
AU Thullner, S
   Gesellchen, F
   Wiemann, S
   Pyerin, W
   Kinzel, V
   Bossemeyer, D
AF Thullner, S
   Gesellchen, F
   Wiemann, S
   Pyerin, W
   Kinzel, V
   Bossemeyer, D
TI The protein kinase A catalytic subunit Cβ2:: molecular characterization
   and distribution of the splice variant
SO BIOCHEMICAL JOURNAL
LA English
DT Article
DE alternative splicing; cAMP-dependent protein kinase; isoform-selective
   antibody; morphological change; tissue distribution
ID AMINO-ACID-SEQUENCE; C-BETA ISOFORMS; CYCLIC-AMP; MASS-SPECTROMETRY;
   ESCHERICHIA-COLI; CULTURED-CELLS; A-KINASE; IN-VIVO; CAMP;
   PHOSPHORYLATION
AB C beta 2, a 46 kDa splice variant of the C beta isoform, is the largest isoform so far described for catalytic subunits from cAMP-dependent protein kinase in mammals. It differs from C beta in the first 15 N-terminal residues which are replaced with a 62-residue domain with no similarity to other known proteins. The C beta 2 protein was identified in cardiac tissue by MS, microsequencing and C-subunit-isoform-selective antibodies. The C beta 2 protein has a very low abundance of about 2% of total affinity-purified C subunits from bovine cardiac tissue. This, and the similarity of its biochemical properties to C alpha and C beta, are probably some of the reasons why the C beta 2 protein has escaped detection so far. The abundance of the C beta 2 protein differs dramatically between tissues, with most protein detected in heart, liver and spleen, and the lowest level in testis. C beta 2 protein shows kinase activity against synthetic substrates, and is inhibited by the protein kinase inhibitor peptide PKI(5-24). The degree of C beta 2 removal from tissue extracts by binding to PKI(5-24) depends on the cAMP level, i..e. on the dissociation state of the holoenzyme. Two sites in the protein are phosphorylated: Thr-244 in the activation segment and Ser-385 close to the C-terminus. By affinity purification and immunodetection C beta 2 was found in cattle, pig, rat, mouse and turkey tissue and in HeLa cells. In the cAMP-insensitive CHO 10260 cell line, which has normal C beta but is depleted of C alpha, Stable transfection with C beta 2 restored most of the cAMP-induced morphological changes. C beta 2 is a ubiquitously expressed protein with characteristic properties of a cAMP-dependent protein kinase catalytic subunit.
C1 Deutsch Krebsforschungszentrum, German Canc Res Ctr, Dept Pathochem, INF 280, D-69120 Heidelberg, Germany.
   Deutsch Krebsforschungszentrum, German Canc Res Ctr, Dept Mol Genome Anal, INF 280, D-69120 Heidelberg, Germany.
   Deutsch Krebsforschungszentrum, German Canc Res Ctr, Dept Biochem Cell Physiol, INF 280, D-69120 Heidelberg, Germany.
C3 Helmholtz Association; German Cancer Research Center (DKFZ); Helmholtz
   Association; German Cancer Research Center (DKFZ); Helmholtz
   Association; German Cancer Research Center (DKFZ)
RP Deutsch Krebsforschungszentrum, German Canc Res Ctr, Dept Pathochem, INF 280, D-69120 Heidelberg, Germany.
EM d.bossemeyer@dkfz-heidelberg.de
RI Wiemann, Stefan/E-4424-2013
OI Wiemann, Stefan/0000-0003-4683-3174
CR BEEBE SJ, 1990, MOL ENDOCRINOL, V4, P465, DOI 10.1210/mend-4-3-465
   CADD G, 1989, NEURON, V3, P71, DOI 10.1016/0896-6273(89)90116-5
   Cauthron RD, 1998, MOL CELL BIOL, V18, P1416, DOI 10.1128/MCB.18.3.1416
   CHEN CA, 1988, BIOTECHNIQUES, V6, P632
   Cheng XD, 1998, P NATL ACAD SCI USA, V95, P9849, DOI 10.1073/pnas.95.17.9849
   CLEGG CH, 1989, J BIOL CHEM, V264, P20140
   Engh RA, 1996, J BIOL CHEM, V271, P26157, DOI 10.1074/jbc.271.42.26157
   Gamm DM, 1996, J BIOL CHEM, V271, P15736, DOI 10.1074/jbc.271.26.15736
   Gangal M, 1999, P NATL ACAD SCI USA, V96, P12394, DOI 10.1073/pnas.96.22.12394
   GEAHLEN RL, 1986, BIOCHEM BIOPH RES CO, V134, P963, DOI 10.1016/S0006-291X(86)80514-9
   GIBBS CS, 1992, J BIOL CHEM, V267, P4806
   Girod A, 1996, FEBS LETT, V391, P121, DOI 10.1016/0014-5793(96)00717-X
   GLASS DB, 1989, J BIOL CHEM, V264, P8802
   GOTTESMAN MM, 1980, SOMAT CELL GENET, V6, P45, DOI 10.1007/BF01538695
   Guthrie CR, 1997, J BIOL CHEM, V272, P29560, DOI 10.1074/jbc.272.47.29560
   Han JD, 1996, J BIOL CHEM, V271, P29211, DOI 10.1074/jbc.271.46.29211
   HANKS SK, 1991, METHOD ENZYMOL, V200, P38
   HAROOTUNIAN AT, 1993, MOL BIOL CELL, V4, P993, DOI 10.1091/mbc.4.10.993
   HERBERG FW, 1993, BIOCHEMISTRY-US, V32, P14015, DOI 10.1021/bi00213a035
   HOWARD P, 1991, J BIOL CHEM, V266, P10189
   Huang YY, 1995, CELL, V83, P1211, DOI 10.1016/0092-8674(95)90146-9
   Jedrzejewski PT, 1998, PROTEIN SCI, V7, P457
   Jedrzejewski PT, 1997, ANAL CHEM, V69, P294, DOI 10.1021/ac9606618
   KINZEL V, 1976, BIOCHEM BIOPH RES CO, V71, P257, DOI 10.1016/0006-291X(76)90276-X
   KINZEL V, 1987, ARCH BIOCHEM BIOPHYS, V253, P341, DOI 10.1016/0003-9861(87)90187-1
   Montminy M, 1997, ANNU REV BIOCHEM, V66, P807, DOI 10.1146/annurev.biochem.66.1.807
   MURTAUGH MP, 1982, J CELL BIOL, V95, P64, DOI 10.1083/jcb.95.1.64
   NELSON NC, 1981, J BIOL CHEM, V256, P3743
   NIGG EA, 1985, EMBO J, V4, P2801, DOI 10.1002/j.1460-2075.1985.tb04006.x
   OLSEN SR, 1989, J BIOL CHEM, V264, P18662
   Qi M, 1996, P NATL ACAD SCI USA, V93, P1571, DOI 10.1073/pnas.93.4.1571
   Razani B, 1999, J BIOL CHEM, V274, P26353, DOI 10.1074/jbc.274.37.26353
   ROGER PP, 1988, FEBS LETT, V232, P409, DOI 10.1016/0014-5793(88)80781-6
   SHOJI S, 1979, J BIOL CHEM, V254, P6211
   SHOJI S, 1981, P NATL ACAD SCI-BIOL, V78, P848, DOI 10.1073/pnas.78.2.848
   SHOJI S, 1986, J CHROMATOGR, V356, P179, DOI 10.1016/S0021-9673(00)91477-8
   SHOJI S, 1983, BIOCHEMISTRY-US, V22, P3702, DOI 10.1021/bi00284a025
   SHOWERS MO, 1986, J BIOL CHEM, V261, P6288
   SHUNTOH H, 1992, BIOCHIM BIOPHYS ACTA, V1131, P175, DOI 10.1016/0167-4781(92)90073-9
   SILVERMAN L, 1992, J CELL BIOL, V119, P415, DOI 10.1083/jcb.119.2.415
   SINGH TJ, 1981, J BIOL CHEM, V256, P926
   SLICE LW, 1989, J BIOL CHEM, V264, P20940
   STEINBERG RA, 1993, MOL CELL BIOL, V13, P2332, DOI 10.1128/MCB.13.4.2332
   THOMIS DC, 1992, J BIOL CHEM, V267, P10723
   TSUGAWA M, 1990, ANTICANCER RES, V10, P63
   UHLER MD, 1986, J BIOL CHEM, V261, P5360
   Wiemann S, 1996, BBA-GENE STRUCT EXPR, V1309, P211, DOI 10.1016/S0167-4781(96)00175-3
   WIEMANN S, 1991, J BIOL CHEM, V266, P5140
   WIEMANN S, 1992, BIOCHIM BIOPHYS ACTA, V1171, P93, DOI 10.1016/0167-4781(92)90144-O
   Yonemoto W, 1997, PROTEIN ENG, V10, P915, DOI 10.1093/protein/10.8.915
NR 50
TC 14
Z9 18
U1 0
U2 1
PU PORTLAND PRESS LTD
PI LONDON
PA CHARLES DARWIN HOUSE, 12 ROGER STREET, LONDON WC1N 2JU, ENGLAND
SN 0264-6021
EI 1470-8728
J9 BIOCHEM J
JI Biochem. J.
PD OCT 1
PY 2000
VL 351
BP 123
EP 132
DI 10.1042/0264-6021:3510123
PN 1
PG 10
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 364RW
UT WOS:000089907600014
PM 10998354
OA Green Published
DA 2025-04-10
ER

PT J
AU Bills, VL
   Varet, J
   Millar, A
   Harper, SJ
   Soothill, PW
   Bates, DO
AF Bills, Victoria L.
   Varet, Julia
   Millar, Ann
   Harper, Steven J.
   Soothill, Peter W.
   Bates, David O.
TI Failure to up-regulate VEGF165b in maternal plasma is a first
   trimester predictive marker for pre-eclampsia
SO CLINICAL SCIENCE
LA English
DT Article
DE angiogenesis; plasma marker; pre-eclampsia; splice variant; vascular
   endothelial growth factor(165)b (VEGF(165)b); vascular permeability
ID ENDOTHELIAL GROWTH-FACTOR; ANGIOGENIC VEGF ISOFORM; SPLICE VARIANT;
   TYROSINE KINASE-1; SOLUBLE ENDOGLIN; IN-VIVO; EXPRESSION; HYPERTENSION;
   PATHOGENESIS; MICE
AB Pre-eclampsia is a pregnancy-related condition characterized by hypertension, proteinuria and endothelial dysfunction. VEGF(165)b, formed by alternative splicing of VEGF (vascular endothelial growth factor) pre-mRNA, inhibits VEGF(165)-mediated vasodilation and angiogenesis, but has not been quantified in pregnancy. ELISAs were used to measure means +/- S.E.M. plasma VEGF(165)b, sEng (soluble endoglin) and sFIt-I (soluble fms-like tyrosine kinase-1). At 12 weeks of gestation, the plasma VEGF(165)b concentration was significantly up-regulated in plasma from women who maintained normal blood pressure throughout their pregnancy (normotensive group, 4.90 +/- 1.6 ng/ml; P < 0.01, as determined using a Mann-Whitney U test) compared with non-pregnant women (0.40 +/- 0.22 ng/ml). In contrast, in patients who later developed pre-eclampsia, VEGF(165)b levels were lower than in the normotensive group (0.467 +/- 0.209 ng/ml), but were no greater than nonpregnant women. At term, plasma VEGF(165)b concentrations were greater than normal in both preeclamptic (3.75 +/- 2.24 ng/ml) and normotensive (10.58 ng/ml +/- 3.74 ng/ml; P > 0.1 compared with pre-eclampsia) pregnancies. Patients with a lower than median plasma VEGF(165)b at 12 weeks had elevated sFIt-I and sEng pre-delivery. Concentrations of sFIt-I (1.20 +/- 0.07 and 1.27 +/- 0.18 ng/ml) and sEng (4.4 +/- 0.18 and 4.1 +/- 0.5 ng/ml) were similar at 12 weeks of gestation in the normotensive and pre-eclamptic groups respectively. Plasma VEGF(165)b levels were elevated in pregnancy, but this increase is delayed in women that subsequently develop pre-eclampsia. In conclusion, low VEGF(165)b may therefore be a clinically useful first trimester plasma marker for increased risk of pre-eclampsia.
C1 [Bills, Victoria L.; Harper, Steven J.; Bates, David O.] Univ Bristol, Preclin Vet Sch, Dept Physiol, Microvasc Res Labs, Bristol BS2 8BJ, Avon, England.
   [Bills, Victoria L.; Soothill, Peter W.] Univ Bristol, St Michaels Hosp, Dept Obstet & Gynaecol, Bristol BS2 8EG, Avon, England.
   [Varet, Julia; Millar, Ann] Southmead Hosp, Med Sch Unit, Bristol BS10 5NB, Avon, England.
C3 University of Bristol; University of Bristol; Southmead Hospital
RP Bates, DO (corresponding author), Univ Bristol, Preclin Vet Sch, Dept Physiol, Microvasc Res Labs, Bristol BS2 8BJ, Avon, England.
EM victoria.bills@bristol.ac.uk; dave.bates@bris.ac.uk
RI Soothill, Peter/D-2814-2009
OI Bates, David/0000-0003-4850-2360
FU British Heart Foundation [FS/05/100, BS06/005]; Wellcome Trust [74702]
FX This work was supported by the British Heart Foundation [grant numbers
   FS/05/100, BS06/005]; and the Wellcome Trust [grant number 74702].
CR Alberry M, 2007, ARCH DIS CHILD-FETAL, V92, pF62, DOI 10.1136/adc.2005.082297
   Anthony FW, 1997, ANN CLIN BIOCHEM, V34, P276, DOI 10.1177/000456329703400309
   Bates DO, 2006, CLIN SCI, V110, P575, DOI 10.1042/CS20050292
   Bates DO, 2002, CANCER RES, V62, P4123
   Baumwell S, 2007, NEPHRON CLIN PRACT, V106, pC72, DOI 10.1159/000101801
   Brockelsby J, 1999, LAB INVEST, V79, P1101
   Duley L, 2001, BMJ-BRIT MED J, V322, P329, DOI 10.1136/bmj.322.7282.329
   Ferrara N, 2004, ENDOCR REV, V25, P581, DOI 10.1210/er.2003-0027
   Glass CA, 2006, J PHYSIOL-LONDON, V572, P243, DOI 10.1113/jphysiol.2005.103127
   Khan KS, 2006, LANCET, V367, P1066, DOI 10.1016/S0140-6736(06)68397-9
   Konopatskaya O, 2006, MOL VIS, V12, P626
   Lee ES, 2007, J KOREAN MED SCI, V22, P94, DOI 10.3346/jkms.2007.22.1.94
   Levine RJ, 2006, NEW ENGL J MED, V355, P992, DOI 10.1056/NEJMoa055352
   Levine RJ, 2004, NEW ENGL J MED, V350, P672, DOI 10.1056/NEJMoa031884
   Li ZH, 2007, HYPERTENSION, V50, P686, DOI 10.1161/HYPERTENSIONAHA.107.092098
   Livingston JC, 2000, AM J OBSTET GYNECOL, V183, P1554, DOI 10.1067/mob.2000.108022
   Lyall F, 1997, PLACENTA, V18, P269, DOI 10.1016/S0143-4004(97)80061-6
   Maynard SE, 2005, PEDIATR RES, V57, p1R, DOI 10.1203/01.PDR.0000159567.85157.B7
   Maynard SE, 2003, J CLIN INVEST, V111, P649, DOI 10.1172/JCI200317189
   McKeeman GC, 2004, AM J OBSTET GYNECOL, V191, P1240, DOI 10.1016/j.ajog.2004.03.004
   Murakami Y, 2005, SEMIN THROMB HEMOST, V31, P307, DOI 10.1055/s-2005-872437
   Nadar SK, 2005, THROMB HAEMOSTASIS, V94, P1071, DOI 10.1160/TH05-03-0167
   Perrin RM, 2005, DIABETOLOGIA, V48, P2422, DOI 10.1007/s00125-005-1951-8
   Pritchard-Jones RO, 2007, BRIT J CANCER, V97, P223, DOI 10.1038/sj.bjc.6603839
   Qiu Y, 2008, FASEB J, V22, P1104, DOI 10.1096/fj.07-9718com
   Rennel ES, 2008, BRIT J CANCER, V98, P1250, DOI 10.1038/sj.bjc.6604309
   Schumacher VA, 2007, J AM SOC NEPHROL, V18, P719, DOI 10.1681/ASN.2006020124
   Sgambati E, 2004, BJOG-INT J OBSTET GY, V111, P564, DOI 10.1111/j.1471-0528.2004.00143.x
   Varey AHR, 2008, BRIT J CANCER, V98, P1366, DOI 10.1038/sj.bjc.6604308
   Venkatesha S, 2006, NAT MED, V12, P642, DOI 10.1038/nm1429
   Woolard J, 2004, CANCER RES, V64, P7822, DOI 10.1158/0008-5472.CAN-04-0934
   Zhou Y, 1997, J CLIN INVEST, V99, P2152, DOI 10.1172/JCI119388
NR 32
TC 41
Z9 49
U1 0
U2 3
PU PORTLAND PRESS LTD
PI LONDON
PA THIRD FLOOR, EAGLE HOUSE, 16 PROCTER STREET, LONDON WC1V 6 NX, ENGLAND
SN 0143-5221
J9 CLIN SCI
JI Clin. Sci.
PD FEB
PY 2009
VL 116
IS 3-4
BP 265
EP 272
DI 10.1042/CS20080270
PG 8
WC Medicine, Research & Experimental
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Research & Experimental Medicine
GA 402WU
UT WOS:000263044600010
PM 18826376
OA Green Published, hybrid, Green Accepted, Green Submitted
DA 2025-04-10
ER

PT J
AU Fingert, JH
   Alward, WL
   Wang, K
   Yorio, T
   Clark, AF
AF Fingert, John H.
   Alward, Wallace L.
   Wang, Kai
   Yorio, Thomas
   Clark, Abbot F.
TI Assessment of SNPs associated with the human glucocorticoid receptor in
   primary open-angle glaucoma and steroid responders
SO MOLECULAR VISION
LA English
DT Article
ID INTRAOCULAR-PRESSURE RESPONSE; OCULAR HYPERTENSION TREATMENT; BETA;
   DEXAMETHASONE; MECHANISMS; DESIGN
AB Purpose: While chronic glucocorticoid (GC) therapy leads to ocular hypertension in about one third of individuals, almost all primary open-angle glaucoma (POAG) patients show this response and are called "steroid responders." Two differentially spliced isoforms of the glucocorticoid receptor (GR), GR alpha and GR beta, regulate GC responsiveness in trabecular meshwork (TM) cells. GR beta acts as a dominant negative regulator of GC activity and is expressed at lower levels in glaucomatous TM cells, making them more sensitive to GCs. Several arginine/serine-rich splicing factor (SR) proteins have been implicated in alternative splicing of the GR. We have previously demonstrated that immunophilins FKBP5 and FKBP4 are required for GR alpha and GR beta translocation into the nucleus, which is essential for their biologic activity. The purpose of the present study was to use single nucleotide polymorphism (SNP) genotyping to determine whether there are any allele frequency differences in GR, FKBP4/5, or SR genes between normal control, POAG, and steroid responder populations.
   Methods: Clinically characterized individuals (400 normal controls, 197 POAG, and 107 steroid responders) were recruited from the U. Iowa Ophthalmology Clinics after IRB approved consent. Genotyping of DNA samples for 48 SNPs in SFRS3, SFRS5, SFRS9, FKBP4, FKBP5, and NR3C1 was done at GeneSeek using a mass spectroscopy based system.
   Results: All 48 SNPs displayed high call rates (99%). There were no significant differences in allele frequencies or genotypes in SNPs for SFRS5, SFRS9, FKBP4, FKBP5, and NR3C1 between the 3 groups. Up to three SNPs in SFRS3 had p-values <0.05 when comparing controls to POAG or steroid responders, but this statistical significance was lost when the p values were adjusted for multiple measures.
   Conclusions: Although these 6 genes may be involved in the pathogenesis of GC-induced ocular hypertension, it does not appear that major heritable risk alleles in these genes are responsible for the development of GC-induced ocular hypertension or POAG.
C1 [Fingert, John H.; Alward, Wallace L.] Univ Iowa, Dept Ophthalmol & Visual Sci, Iowa City, IA USA.
   [Wang, Kai] Univ Iowa, Dept Biostat, Iowa City, IA USA.
   [Yorio, Thomas] Univ N Texas, Hlth Sci Ctr, Dept Pharmacol & Neurosci, Ft Worth, TX 76107 USA.
   [Clark, Abbot F.] Univ N Texas, Hlth Sci Ctr, Dept Cell Biol & Anat, Ft Worth, TX 76107 USA.
   [Yorio, Thomas; Clark, Abbot F.] Univ N Texas, Hlth Sci Ctr, N Texas Eye Res Inst, Ft Worth, TX 76107 USA.
C3 University of Iowa; University of Iowa; University of North Texas
   System; University of North Texas Health Science Center; University of
   North Texas System; University of North Texas Health Science Center;
   University of North Texas System; University of North Texas Health
   Science Center
RP Clark, AF (corresponding author), Univ N Texas, Hlth Sci Ctr, N Texas Eye Res Inst CBH 453, Dept Cell Biol & Anat, 3500 Camp Bowie Blvd, Ft Worth, TX 76107 USA.
EM abe.clark@unthsc.edu
RI Wang, Kai/IWD-8760-2023; Alward, Wallace/AAY-4149-2020; Fingert,
   John/AAX-4750-2021; Fingert, John/F-8787-2012
OI Alward, Wallace/0000-0001-6368-9018; Fingert, John/0000-0002-0377-0479
FU NIH [EY016242]; Alcon Research, Ltd.
FX This work was supported by NIH grant EY016242 (T.Y.). A.F.C. has
   received financial support from Alcon Research, Ltd.
CR ARMALY MF, 1966, ARCH OPHTHALMOL-CHIC, V75, P32
   BAMBERGER CM, 1995, J CLIN INVEST, V95, P2435, DOI 10.1172/JCI117943
   BARTLETT JD, 1993, J OCUL PHARMACOL, V9, P35, DOI 10.1089/jop.1993.9.35
   BECKER B, 1966, ARCH OPHTHALMOL-CHIC, V76, P484
   Budde W M, 2000, Curr Opin Ophthalmol, V11, P101, DOI 10.1097/00055735-200004000-00006
   Chen M, 2009, NAT REV MOL CELL BIO, V10, P741, DOI 10.1038/nrm2777
   Clark AF, 2003, GLAUCOMA SCI PRACTIC, P197
   Duma D, 2006, J STEROID BIOCHEM, V102, P11, DOI 10.1016/j.jsbmb.2006.09.009
   Gerzenstein SM, 2008, OPHTHALMIC GENET, V29, P166, DOI 10.1080/13816810802320217
   Goecke A, 2006, IMMUNOBIOLOGY, V211, P85, DOI 10.1016/j.imbio.2005.11.002
   Gordon MO, 1999, ARCH OPHTHALMOL-CHIC, V117, P573
   Gordon MO, 2002, ARCH OPHTHALMOL-CHIC, V120, P714
   Han B, 2008, ANN HUM GENET, V72, P834, DOI 10.1111/j.1469-1809.2008.00469.x
   KITAZAWA Y, 1981, ARCH OPHTHALMOL-CHIC, V99, P813
   Klein RJ, 2005, SCIENCE, V308, P385, DOI 10.1126/science.1109557
   Kwon YH, 2009, NEW ENGL J MED, V360, P1113, DOI 10.1056/NEJMra0804630
   LEWIS JM, 1988, AM J OPHTHALMOL, V106, P607, DOI 10.1016/0002-9394(88)90595-8
   Lewis-Tuffin LJ, 2006, ANN NY ACAD SCI, V1069, P1, DOI 10.1196/annals.1351.001
   Manolio TA, 2009, NATURE, V461, P747, DOI 10.1038/nature08494
   MCCARTY GR, 1991, INVEST OPHTH VIS SCI, V32, P1600
   Oakley RH, 1996, J BIOL CHEM, V271, P9550, DOI 10.1074/jbc.271.16.9550
   ROZSIVAL P, 1981, CURR EYE RES, V1, P391, DOI 10.3109/02713688109019976
   Schulzer M, 1998, AM J OPHTHALMOL, V126, P487
   Southren A L, 1985, Trans Assoc Am Physicians, V98, P361
   Stokes J, 2003, INVEST OPHTH VIS SCI, V44, P5163, DOI 10.1167/iovs.02-1318
   Thorleifsson G, 2007, SCIENCE, V317, P1397, DOI 10.1126/science.1146554
   Van Veldhuisen PC, 2000, AM J OPHTHALMOL, V130, P429
   Xu Q, 2003, J BIOL CHEM, V278, P27112, DOI 10.1074/jbc.M300824200
   Yan XB, 2010, MOL BIOL REP, V37, P1427, DOI 10.1007/s11033-009-9529-z
   Zhang XY, 2008, INVEST OPHTH VIS SCI, V49, P1037, DOI 10.1167/iovs.07-1279
   Zhang XY, 2007, EXP EYE RES, V84, P275, DOI 10.1016/j.exer.2006.09.022
   Zhang XY, 2005, INVEST OPHTH VIS SCI, V46, P4607, DOI 10.1167/iovs.05-0571
NR 32
TC 22
Z9 27
U1 0
U2 8
PU MOLECULAR VISION
PI ATLANTA
PA C/O JEFF BOATRIGHT, LAB B, 5500 EMORY EYE CENTER, 1327 CLIFTON RD, N E,
   ATLANTA, GA 30322 USA
SN 1090-0535
J9 MOL VIS
JI Mol. Vis.
PD APR 3
PY 2010
VL 16
IS 66-69
BP 596
EP 601
PG 6
WC Biochemistry & Molecular Biology; Ophthalmology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Ophthalmology
GA 619MB
UT WOS:000279433200003
PM 20376328
DA 2025-04-10
ER

PT J
AU Peter, AK
   Rossi, AC
   Buvoli, M
   Ozeroff, CD
   Crocini, C
   Perry, AR
   Buvoli, AE
   Lee, LA
   Leinwand, LA
AF Peter, Angela K.
   Rossi, Alberto C.
   Buvoli, Massimo
   Ozeroff, Christopher D.
   Crocini, Claudia
   Perry, Amy R.
   Buvoli, Ada E.
   Lee, Lindsey A.
   Leinwand, Leslie A.
TI Expression of Normally Repressed Myosin Heavy Chain 7b in the Mammalian
   Heart Induces Dilated Cardiomyopathy
SO JOURNAL OF THE AMERICAN HEART ASSOCIATION
LA English
DT Article
DE cardiac dysfunction; cardiac myocyte; MYH7b; myosin heavy chain;
   transgenic mice
ID VENTRICULAR NONCOMPACTION CARDIOMYOPATHY; NON-COMPACTION;
   GENE-EXPRESSION; MOUSE MODEL; DYSFUNCTION; ALPHA
AB Background-In mammals, muscle contraction is controlled by a family of 10 sarcomeric myosin motors. The expression of one of its members, MYH7b, is regulated by alternative splicing, and while the protein is restricted to specialized muscles such as extraocular muscles or muscle spindles, RNA that cannot encode protein is expressed in most skeletal muscles and in the heart. Remarkably, birds and snakes express MYH7b protein in both heart and skeletal muscles. This observation suggests that in the mammalian heart, the motor activity of MYH7b may only be needed during development since its expression is prevented in adult tissue, possibly because it could promote disease by unbalancing myocardial contractility.
   Methods and Results-We have analyzed MYH7b null mice to determine the potential role of MYH7b during cardiac development and also generated transgenic mice with cardiac myocyte expression of MYH7b protein to measure its impact on cardiomyocyte function and contractility. We found that MYH7b null mice are born at expected Mendelian ratios and do not have a baseline cardiac phenotype as adults. In contrast, transgenic cardiac MYH7b protein expression induced early cardiac dilation in males with significantly increased left ventricular mass in both sexes. Cardiac dilation is progressive, leading to early cardiac dysfunction in males, but later dysfunction in females.
   Conclusions-The data presented show that the expression of MYH7b protein in the mammalian heart has been inhibited during the evolution of mammals most likely to prevent the development of a severe cardiomyopathy that is sexually dimorphic.
C1 [Peter, Angela K.; Rossi, Alberto C.; Buvoli, Massimo; Ozeroff, Christopher D.; Crocini, Claudia; Perry, Amy R.; Buvoli, Ada E.; Lee, Lindsey A.; Leinwand, Leslie A.] Univ Colorado, Biofrontiers Inst, Dept Mol Cellular & Dev Biol, Boulder, CO 80303 USA.
C3 University of Colorado System; University of Colorado Boulder
RP Leinwand, LA (corresponding author), Univ Colorado, BioFrontiers Inst, 3415 Colorado Ave, Boulder, CO 80303 USA.
EM leslie.leinwand@colorado.edu
RI Crocini, Claudia/AAE-2457-2019; L, A/HZI-4043-2023; Rossi,
   Alberto/AAG-8343-2019; Crocini, Claudia/F-5429-2016
OI Lee, Lindsey/0000-0002-7082-5484; Crocini, Claudia/0000-0001-8231-2726
FU Human Frontiers Science Program Fellowship [LT001449/2017-L]; NIH
   [GM029090]
FX Dr Crocini was supported by the Human Frontiers Science Program
   Fellowship (LT001449/2017-L). L. A. Lee received grant support from NIH
   T32 GM008759. Research Grant support was provided by NIH GM029090 to Dr
   Leinwand.
CR Anderson RH, 2017, CAN J CARDIOL, V33, P747, DOI 10.1016/j.cjca.2017.01.017
   Bell ML, 2010, MOL CELL BIOL, V30, P1937, DOI 10.1128/MCB.01370-09
   Blech-Hermoni Y, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0149061
   Crocini C, 2016, J MOL CELL CARDIOL, V91, P42, DOI 10.1016/j.yjmcc.2015.12.013
   Deacon JC, 2012, CELL MOL LIFE SCI, V69, P2261, DOI 10.1007/s00018-012-0927-3
   Desjardins PR, 2002, MOL BIOL EVOL, V19, P375, DOI 10.1093/oxfordjournals.molbev.a004093
   Esposito T, 2013, ORPHANET J RARE DIS, V8, DOI 10.1186/1750-1172-8-91
   Val-Bernal JF, 2010, HISTOL HISTOPATHOL, V25, P495, DOI 10.14670/HH-25.495
   GULICK J, 1991, J BIOL CHEM, V266, P9180
   Haines CD, 2012, ENDOCRINOLOGY, V153, P4470, DOI 10.1210/en.2012-1391
   Haraksingh RR, 2014, BMC GENOMICS, V15, DOI 10.1186/1471-2164-15-1155
   Krenz M, 2004, J AM COLL CARDIOL, V44, P2390, DOI 10.1016/j.jacc.2004.09.044
   Krenz M, 2003, J BIOL CHEM, V278, P17466, DOI 10.1074/jbc.M210804200
   Landrum MJ, 2018, NUCLEIC ACIDS RES, V46, pD1062, DOI 10.1093/nar/gkx1153
   Lange S, 2005, SCIENCE, V308, P1599, DOI 10.1126/science.1110463
   Lee LA, 2019, SKELET MUSCLE, V9, DOI 10.1186/s13395-019-0192-3
   Lim CC, 2000, J MOL CELL CARDIOL, V32, P2075, DOI 10.1006/jmcc.2000.1239
   Long CZ, 2014, SCIENCE, V345, P1184, DOI 10.1126/science.1254445
   Lucas DT, 2003, AM J PHYSIOL-HEART C, V284, pH575, DOI 10.1152/ajpheart.00619.2002
   Nagase T, 2008, DNA RES, V15, P137, DOI 10.1093/dnares/dsn004
   Naiman RJ, 2012, P NATL ACAD SCI USA, V109, P21201, DOI 10.1073/pnas.1213408109
   Nakao K, 1997, J CLIN INVEST, V100, P2362, DOI 10.1172/JCI119776
   Palermo J, 1996, CIRC RES, V78, P504, DOI 10.1161/01.RES.78.3.504
   Parks RJ, 2014, J MOL CELL CARDIOL, V75, P162, DOI 10.1016/j.yjmcc.2014.07.006
   PESELOW ED, 1989, PSYCHOPHARMACOL BULL, V25, P267
   Pugach EK, 2015, J MOL CELL CARDIOL, V86, P54, DOI 10.1016/j.yjmcc.2015.06.019
   Rakus D, 2016, J PROTEOME RES, V15, P2479, DOI 10.1021/acs.jproteome.5b01149
   Robbins TW, 1998, J INT NEUROPSYCH SOC, V4, P474, DOI 10.1017/s1355617798455073
   Rooms I, 2015, ACTA CARDIOL, V70, P625, DOI [10.1080/AC.70.6.3120173, 10.2143/AC.70.6.3120173]
   Rossi AC, 2010, J PHYSIOL-LONDON, V588, P353, DOI 10.1113/jphysiol.2009.181008
   Rubio MD, 2011, J NEUROSCI, V31, P1448, DOI 10.1523/JNEUROSCI.3294-10.2011
   Rüdebusch J, 2017, PLOS ONE, V12, DOI 10.1371/journal.pone.0185915
   Stauffer BL, 2006, J CLIN INVEST, V116, P209, DOI 10.1172/JCI24676
   Stollberger C, 2018, HERZ
   Tardiff JC, 2000, AM J PHYSIOL-HEART C, V278, pH412, DOI 10.1152/ajpheart.2000.278.2.H412
   Towbin JA, 2015, LANCET, V386, P813, DOI 10.1016/S0140-6736(14)61282-4
   Trépanier-Boulay W, 2001, CIRC RES, V89, P437, DOI 10.1161/hh1701.095644
   van der Velden J, 2018, CARDIOVASC RES, V114, P1273, DOI 10.1093/cvr/cvy147
   van Rooij E, 2009, DEV CELL, V17, P662, DOI 10.1016/j.devcel.2009.10.013
   Wang JX, 2011, NAT MED, V17, P71, DOI 10.1038/nm.2282
   Warkman AS, 2012, CYTOSKELETON, V69, P324, DOI 10.1002/cm.21029
   Warren CM, 2003, ANAL BIOCHEM, V320, P149, DOI 10.1016/S0003-2697(03)00350-6
   Wu MF, 2018, PEDIATR CARDIOL, V39, P1082, DOI 10.1007/s00246-018-1868-x
   Zhang WJ, 2013, AM J MED GENET C, V163, P144, DOI 10.1002/ajmg.c.31369
NR 44
TC 17
Z9 20
U1 0
U2 3
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 2047-9980
J9 J AM HEART ASSOC
JI J. Am. Heart Assoc.
PD AUG 6
PY 2019
VL 8
IS 15
AR e013318
DI 10.1161/JAHA.119.013318
PG 29
WC Cardiac & Cardiovascular Systems
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology
GA IV9KT
UT WOS:000484583500053
PM 31364453
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Duong, NT
   Morris, GE
   Lam, LT
   Zhang, QP
   Sewry, CA
   Shanahan, CM
   Holt, I
AF Nguyen Thuy Duong
   Morris, Glenn E.
   Le Thanh Lam
   Zhang, Qiuping
   Sewry, Caroline A.
   Shanahan, Catherine M.
   Holt, Ian
TI Nesprins: Tissue-Specific Expression of Epsilon and Other Short Isoforms
SO PLOS ONE
LA English
DT Article
ID DREIFUSS MUSCULAR-DYSTROPHY; NUCLEAR-MEMBRANE PROTEIN; REAL-TIME PCR;
   LAMIN; ENVELOPE; ROLES; LINC; DIFFERENTIATION; BINDING; SYNE-1
AB Nesprin-1-giant and nesprin-2-giant regulate nuclear positioning by the interaction of their C-terminal KASH domains with nuclear membrane SUN proteins and their N- terminal calponin-homology domains with cytoskeletal actin. A number of short isoforms lacking the actin-binding domains are produced by internal promotion. We have evaluated the significance of these shorter isoforms using quantitative RT-PCR and western blotting with site-specific monoclonal antibodies. Within a complete map of nesprin isoforms, we describe two novel nesprin-2 epsilon isoforms for the first time. Epsilon isoforms are similar in size and structure to nesprin-1-alpha. Expression of nesprin isoforms was highly tissue-dependent. Nesprin-2-epsilon- 1 was found in early embryonic cells, while nesprin-2-epsilon-2 was present in heart and other adult tissues, but not skeletal muscle. Some cell lines lack shorter isoforms and express only one of the two nesprin genes, suggesting that either of the giant nesprins is sufficient for basic cell functions. For the first time, localisation of endogenous nesprin away from the nuclear membrane was shown in cells where removal of the KASH domain by alternative splicing occurs. By distinguishing between degradation products and true isoforms on western blots, it was found that previously-described beta and gamma isoforms are expressed either at only low levels or with a limited tissue distribution. Two of the shortest alpha isoforms, nesprin-1-alpha-2 and nesprin-2-alpha-1, were found almost exclusively in cardiac and skeletal muscle and a highly conserved and alternatively- spliced exon, available in both nesprin genes, was always included in these tissues. These "muscle-specific'' isoforms are thought to form a complex with emerin and lamin A/C at the inner nuclear membrane and mutations in all three proteins cause Emery-Dreifuss muscular dystrophy and/or inherited dilated cardiomyopathy, disorders in which only skeletal muscle and/or heart are affected.
C1 [Nguyen Thuy Duong; Morris, Glenn E.; Le Thanh Lam; Sewry, Caroline A.; Holt, Ian] RJAH Orthopaed Hosp, Wolfson Ctr Inherited Neuromuscular Dis, Oswestry, Shrops, England.
   [Nguyen Thuy Duong] Vietnam Acad Sci & Technol VAST, Inst Genome Res, Hanoi, Vietnam.
   [Morris, Glenn E.; Holt, Ian] Keele Univ, Inst Sci & Technol Med, Keele, Staffs, England.
   [Zhang, Qiuping; Shanahan, Catherine M.] Kings Coll London, James Black Ctr, Div Cardiovasc, London, England.
   [Sewry, Caroline A.] Inst Child Hlth, Dubowitz Neuromuscular Ctr, London, England.
   [Sewry, Caroline A.] Great Ormond St Hosp Sick Children, London, England.
C3 Keele University; Vietnam Academy of Science & Technology (VAST); Keele
   University; University of London; King's College London; University of
   London; University College London; University of London; University
   College London; Great Ormond Street Hospital for Children NHS Foundation
   Trust
RP Holt, I (corresponding author), RJAH Orthopaed Hosp, Wolfson Ctr Inherited Neuromuscular Dis, Oswestry, Shrops, England.
EM ian.holt@rjah.nhs.uk
RI Dương (Elyanah), Nguyễn/JEO-4973-2023; Zhang, Qiuping/L-3522-2019
OI Shanahan, Catherine/0000-0002-8352-8171; zhang,
   Qiuping/0000-0002-4000-3957; Nguyen, Thuy Duong/0000-0001-8691-9138
FU British Heart Foundation [PG/11/71/29091]; Vietnam National Foundation
   for Science and Technology Development (NAFOSTED) [106.06-2010.62]
FX We thank the British Heart Foundation for grant support (PG/11/71/29091
   to IH and GEM). NTD received funding from the Vietnam National
   Foundation for Science and Technology Development (NAFOSTED)
   (106.06-2010.62). The funders had no role in study design, data
   collection and analysis, decision to publish, or preparation of the
   manuscript.
CR ANDREWS PW, 1984, LAB INVEST, V50, P147
   [Anonymous], 2010, PROTEIN PROTOCOLS HD
   Apel ED, 2000, J BIOL CHEM, V275, P31986, DOI 10.1074/jbc.M004775200
   Bastien P, 2008, J CLIN MICROBIOL, V46, P1897, DOI 10.1128/JCM.02258-07
   BIONE S, 1994, NAT GENET, V8, P323, DOI 10.1038/ng1294-323
   Bonne G, 1999, NAT GENET, V21, P285, DOI 10.1038/6799
   GEY GO, 1952, CANCER RES, V12, P264
   Gueneau L, 2009, AM J HUM GENET, V85, P338, DOI 10.1016/j.ajhg.2009.07.015
   Haque F, 2010, J BIOL CHEM, V285, P3487, DOI 10.1074/jbc.M109.071910
   Holt I, 2006, NEUROMUSCULAR DISORD, V16, P368, DOI 10.1016/j.nmd.2006.03.014
   Lam LT, 2011, BIOCHEM BIOPH RES CO, V412, P291, DOI 10.1016/j.bbrc.2011.07.085
   Lei K, 2009, P NATL ACAD SCI USA, V106, P10207, DOI 10.1073/pnas.0812037106
   Li C, 2011, CATAL TODAY, V175, P1, DOI 10.1016/j.cattod.2011.08.002
   Liang WC, 2011, ANN NEUROL, V69, P1005, DOI 10.1002/ana.22338
   Libotte T, 2005, MOL BIOL CELL, V16, P3411, DOI 10.1091/mbc.E04-11-1009
   Livak KJ, 2001, METHODS, V25, P402, DOI 10.1006/meth.2001.1262
   Lombardi ML, 2011, BIOCHEM SOC T, V39, P1729, DOI 10.1042/BST20110686
   Lüke Y, 2008, J CELL SCI, V121, P1887, DOI 10.1242/jcs.019075
   Manilal S, 1997, NEUROMUSCULAR DISORD, V7, P63, DOI 10.1016/S0960-8966(96)00405-1
   Meinke P, 2011, BIOCHEM SOC T, V39, P1693, DOI 10.1042/BST20110658
   Mislow JMK, 2002, FEBS LETT, V525, P135, DOI 10.1016/S0014-5793(02)03105-8
   Mislow JMK, 2002, J CELL SCI, V115, P61
   Morris GE, 2010, BIOCHEM SOC T, V38, P278, DOI 10.1042/BST0380278
   Morris-Stiff GJ, 2010, EUR J GASTROEN HEPAT, V22, P886, DOI 10.1097/MEG.0b013e3283392a62
   Padmakumar VC, 2004, EXP CELL RES, V295, P330, DOI 10.1016/j.yexcr.2004.01.014
   Pare GC, 2005, EXP CELL RES, V303, P388, DOI 10.1016/j.yexcr.2004.10.009
   Pereboev A, 1996, Methods Mol Biol, V66, P195
   Puckelwartz MJ, 2010, J MOL CELL CARDIOL, V48, P600, DOI 10.1016/j.yjmcc.2009.11.006
   Puckelwartz MJ, 2009, HUM MOL GENET, V18, P607, DOI 10.1093/hmg/ddn386
   Rajgor D, 2013, EXPERT REV MOL MED, V15, DOI 10.1017/erm.2013.6
   Rajgor D, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0040098
   Randles KN, 2010, DEV DYNAM, V239, P998, DOI 10.1002/dvdy.22229
   Rashmi RN, 2012, NUCLEUS-PHILA, V3, P172, DOI 10.4161/nucl.19090
   Roux KJ, 2009, P NATL ACAD SCI USA, V106, P2194, DOI 10.1073/pnas.0808602106
   Schmittgen TD, 2008, NAT PROTOC, V3, P1101, DOI 10.1038/nprot.2008.73
   SHANAHAN CM, 1993, CIRC RES, V73, P193, DOI 10.1161/01.RES.73.1.193
   Simpson JG, 2008, BIOCHEM SOC T, V36, P1359, DOI 10.1042/BST0361359
   Sosa BA, 2012, CELL, V149, P1035, DOI 10.1016/j.cell.2012.03.046
   Thomson JA, 1998, SCIENCE, V282, P1145, DOI 10.1126/science.282.5391.1145
   Warren DT, 2010, J BIOL CHEM, V285, P1311, DOI 10.1074/jbc.M109.032557
   Wilhelmsen K, 2005, J CELL BIOL, V171, P799, DOI 10.1083/jcb.200506083
   Zhang JL, 2010, HUM MOL GENET, V19, P329, DOI 10.1093/hmg/ddp499
   Zhang QP, 2007, HUM MOL GENET, V16, P2816, DOI 10.1093/hmg/ddm238
   Zhang QP, 2005, J CELL SCI, V118, P673, DOI 10.1242/jcs.01642
   Zhang QP, 2001, J CELL SCI, V114, P4485
   Zhang XC, 2007, DEVELOPMENT, V134, P901, DOI 10.1242/dev.02783
   Zhen YY, 2002, J CELL SCI, V115, P3207
   Zhou ZC, 2012, J BIOL CHEM, V287, P5317, DOI 10.1074/jbc.M111.304543
NR 48
TC 63
Z9 70
U1 0
U2 7
PU PUBLIC LIBRARY SCIENCE
PI SAN FRANCISCO
PA 1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA
SN 1932-6203
J9 PLOS ONE
JI PLoS One
PD APR 9
PY 2014
VL 9
IS 4
AR e94380
DI 10.1371/journal.pone.0094380
PG 14
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA AE9PC
UT WOS:000334339000112
PM 24718612
OA gold, Green Published, Green Submitted
DA 2025-04-10
ER

PT J
AU Kee, HJ
   Koh, JT
   Kim, MY
   Ahn, KY
   Kim, JK
   Bae, CS
   Park, SS
   Kim, KK
AF Kee, HJ
   Koh, JT
   Kim, MY
   Ahn, KY
   Kim, JK
   Bae, CS
   Park, SS
   Kim, KK
TI Expression of brain-specific angiogenesis inhibitor 2 (BAI2) in normal
   and ischemic brain: Involvement of BAI2 in the ischemia-induced brain
   angiogenesis
SO JOURNAL OF CEREBRAL BLOOD FLOW AND METABOLISM
LA English
DT Article
DE brain-specific angiogenesis inhibitor 2 (BAI2); focal cerebral ischemia;
   angiogenesis; neuron-specific gene; gene expression
ID COA ALPHA-HYDROXYLASE; CEREBRAL-ISCHEMIA; GENE-EXPRESSION; IN-VITRO;
   THROMBOSPONDIN-1; PROTEIN; GROWTH; NEOVASCULARIZATION; DOMAINS; HYPOXIA
AB Previously, the authors cloned and characterized murine brain-specific angiogenesis inhibitor 1 (mBAI1). In this study, the authors cloned mBAI2 and analyzed its functional characteristics. Northern and Western blot analyses demonstrated a unique developmental expression pattern of mBAI2 in the brain. The expression level of mBAI2 appeared to increase as the development of the brain progressed. Reverse transcription-polymerase chain reaction (RT-PCR) analyses demonstrated the existence of alternative splice variants of mBAI2, Which were defective in parts of type I repeat of thrombospondin or the third cytoplasmic loop of the seven-span transmembrane domain that were considered essential to the functions of mBAI2. The expressions of spliced variants in the brain were differently regulated compared with wild-type mBAI2 during development and ischemic conditions. In situ hybridization analyses of the brain showed the same localization of BAI2 as BAII, such as in most neurons of cerebral cortex. In the in vivo focal cerebral ischemia model and the in vitro hypoxic cell culture model with cobalt, BAI2 expression decreased after hypoxia and preceded the increased expression of vascular endothelial growth factor (VEGF). RT-PCR analysis of antisense BAI2 cDNA-transfected SHSY5Y cells showed an increased VEGF expression as well as a decreased BAI2 expression. Immunohistochemical study of focal ischemic cortex showed that the regional localization of decreased BAI2 was related to the formation of new vessels. These results suggest that the brain-specific developmental expression pattern of angiostatic BAI2 is correlated with the decreased neovascularization in the adult brain, and that angiostatic BAI2 participates in the ischemia-induced brain angiogenesis in concert With angiogenic VEGF.
C1 Chonnam Natl Univ, Sch Med, Res Inst Med Sci, Dept Pharmacol,Dong Ku, Kwangju 501190, South Korea.
   Chonnam Natl Univ, Dent Sci Res Inst, Kwangju 501190, South Korea.
   Natl Inst Hlth, Biomed Brain Res Ctr, Seoul, South Korea.
C3 Chonnam National University; Chonnam National University; Korea Disease
   Control & Prevention Agency (KDCA); Korea National Institute of Health
   (KNIH)
RP Kim, KK (corresponding author), Chonnam Natl Univ, Sch Med, Res Inst Med Sci, Dept Pharmacol,Dong Ku, Hak Dong 5, Kwangju 501190, South Korea.
RI Kee, Hae Jin/ABC-9979-2021; Kim, Yong/L-8653-2019
OI Kee, Hae Jin/0000-0002-9774-4828
CR ASCH AS, 1993, SCIENCE, V262, P1436, DOI 10.1126/science.7504322
   Dawson DW, 1997, J CELL BIOL, V138, P707, DOI 10.1083/jcb.138.3.707
   Detmar M, 2000, J DERMATOL SCI, V24, pS78, DOI 10.1016/S0923-1811(00)00145-6
   FEARON DT, 1975, J EXP MED, V142, P856, DOI 10.1084/jem.142.4.856
   HIGGINS JMG, 1995, J IMMUNOL, V155, P5777
   Jiménez B, 2000, NAT MED, V6, P41, DOI 10.1038/71517
   KIM KK, 1994, J BIOL CHEM, V269, P22607
   KLAR A, 1992, CELL, V69, P95, DOI 10.1016/0092-8674(92)90121-R
   Koh JT, 2001, MOL BRAIN RES, V87, P223, DOI 10.1016/S0169-328X(01)00004-3
   Lee ZH, 2000, MOL BRAIN RES, V75, P237, DOI 10.1016/S0169-328X(99)00304-6
   LEUNGHAGESTEIJN CY, 1992, CELL, V71, P289, DOI 10.1016/0092-8674(92)90357-I
   Lin TN, 2000, J CEREBR BLOOD F MET, V20, P387, DOI 10.1097/00004647-200002000-00021
   Marti HH, 2000, AM J PATHOL, V156, P965, DOI 10.1016/S0002-9440(10)64964-4
   MINCHENKO A, 1994, LAB INVEST, V71, P374
   Nishimori H, 1997, ONCOGENE, V15, P2145, DOI 10.1038/sj.onc.1201542
   Plate KH, 1999, J NEUROPATH EXP NEUR, V58, P313, DOI 10.1097/00005072-199904000-00001
   Qabar AN, 2000, BIOCHEM J, V346, P147, DOI 10.1042/0264-6021:3460147
   Sandner P, 1997, PFLUG ARCH EUR J PHY, V433, P803, DOI 10.1007/s004240050348
   SCHUSTER SJ, 1989, BLOOD, V73, P13
   Shafiee A, 2000, INVEST OPHTH VIS SCI, V41, P2378
   Shiratsuchi T, 1997, CYTOGENET CELL GENET, V79, P103, DOI 10.1159/000134693
   STEFAN CJ, 1994, MOL CELL BIOL, V14, P3339, DOI 10.1128/MCB.14.5.3339
   Suzuma K, 1999, AM J PATHOL, V154, P343, DOI 10.1016/S0002-9440(10)65281-9
   TOKINO T, 1994, HUM MOL GENET, V3, P1537, DOI 10.1093/hmg/3.9.1537
   TOLSMA SS, 1993, J CELL BIOL, V122, P497, DOI 10.1083/jcb.122.2.497
   VOLPERT OV, 1995, BIOCHEM BIOPH RES CO, V217, P326, DOI 10.1006/bbrc.1995.2780
   Zhang ZG, 2001, J CEREBR BLOOD F MET, V21, P541, DOI 10.1097/00004647-200105000-00008
NR 27
TC 35
Z9 43
U1 0
U2 0
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA 530 WALNUT ST, PHILADELPHIA, PA 19106-3621 USA
SN 0271-678X
J9 J CEREBR BLOOD F MET
JI J. Cereb. Blood Flow Metab.
PD SEP
PY 2002
VL 22
IS 9
BP 1054
EP 1067
DI 10.1097/00004647-200209000-00003
PG 14
WC Endocrinology & Metabolism; Hematology; Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism; Hematology; Neurosciences & Neurology
GA 592CP
UT WOS:000177919400003
PM 12218411
OA hybrid
DA 2025-04-10
ER

PT J
AU Hiura, Y
   Tabara, Y
   Kokubo, Y
   Okamura, T
   Goto, Y
   Nonogi, H
   Miki, T
   Tomoike, H
   Iwai, N
AF Hiura, Yumiko
   Tabara, Yasuharu
   Kokubo, Yoshihiro
   Okamura, Tomonori
   Goto, Yoichi
   Nonogi, Hiroshi
   Miki, Tetsuro
   Tomoike, Hitonobu
   Iwai, Naoharu
TI Association of the Functional Variant in the
   3-Hydroxy-3-Methylglutaryl-Coenzyme A Reductase Gene With Low-Density
   Lipoprotein-Cholesterol in Japanese
SO CIRCULATION JOURNAL
LA English
DT Article
DE Genetics; Lipids; Myocardial infarction; Polymorphism
ID GENOME-WIDE ASSOCIATION; MYOCARDIAL-INFARCTION; CARDIOVASCULAR-DISEASE;
   LIPID CONCENTRATIONS; POPULATION; LOCI; POLYMORPHISMS; SUITA; RISK;
   HYPERTENSION
AB Background. The association between single nucleotide polymorphisms (SNPs) at 3-hydroxy-3-methylglutarylcoenzyme A reductase (HMGCR) and low-density lipoprotein-cholesterol (LDL-C) levels has been well replicated in genome-wide association studies (GWAS) of white populations. Recently, the common intronic SNP of HMGCR (rs3846662) has been reported to be a functional variant, influencing the alternative splicing of exon 13. The aim of this study was to examine the association between rs3846662 of HMGCR and the level of LDL-C in Japanese.
   Methods and Results: Significant differences in LDL-C levels were observed among the genotypes of rs3846662 (P=0.0002 (n=2,686) and P=0.004 (n=2,110)) for the Suita and Ehime samples, respectively. The G allele of rs3846662 was associated with higher LDL-C levels (beta, 3.56; P=4.91 x10(-5)). Consistent with this observation, the risk G allele at rs3846662 was more prevalent in subjects with myocardial infarction (MI) (n=701) than in subjects without MI (n=3,118); 0.559 and 0.511 in MI cases and controls, respectively (nominal P=0.0038). The odds ratio adjusted for age, sex, diabetes, hypertension, and drinking and smoking habits was 1.15 (95% confidence interval 1.04-1.28; P=0.0075).
   Conclusions: The previously reported association of rs3846662 with LDL-C levels was replicated in the present Suita and Ehime samples. The LDL-associated SNP, rs3846662, appears to confer susceptibility to MI in Japanese. (Circ J 2010; 74: 518-522)
C1 [Hiura, Yumiko; Iwai, Naoharu] Natl Cardiovasc Ctr, Res Inst, Dept Epidemiol, Suita, Osaka 5658565, Japan.
   [Tabara, Yasuharu] Ehime Univ, Grad Sch Med, Dept Basic Med Res & Educ, Matsuyama, Ehime 790, Japan.
   [Tabara, Yasuharu; Miki, Tetsuro] Ehime Proteomed Res Ctr, Div Antiaging & Genom, Toon, Ehime, Japan.
   [Kokubo, Yoshihiro; Okamura, Tomonori; Tomoike, Hitonobu] Natl Cardiovasc Ctr, Div Prevent Cardiol, Suita, Osaka 5658565, Japan.
   [Miki, Tetsuro] Ehime Univ, Grad Sch Med, Dept Geriatr Med, Toon, Ehime, Japan.
   [Goto, Yoichi; Nonogi, Hiroshi; Iwai, Naoharu] Natl Cardiovasc Ctr, Div Cardiol, Suita, Osaka 5658565, Japan.
C3 National Cerebral & Cardiovascular Center - Japan; Ehime University;
   National Cerebral & Cardiovascular Center - Japan; Ehime University;
   National Cerebral & Cardiovascular Center - Japan
RP Iwai, N (corresponding author), Natl Cardiovasc Ctr, Res Inst, Dept Epidemiol, 5-7-1 Fujishirodai, Suita, Osaka 5658565, Japan.
EM iwai@ri.ncvc.go.jp
RI Hiroshi, Nonogi/D-8345-2011; Knudsen, Ann/AAB-2465-2019; Okamura,
   Tomonori/L-1693-2013
OI Okamura, Tomonori/0000-0003-0488-0351
FU National Institute of Biomedical Innovation, Japan
FX We thank all those who participated in the study. In addition, we
   gratefully acknowledge all the members of Suita City Health Center and
   the Suita Medical Association. The technical assistance of Ms Hiromi
   Sawamura was much appreciated.The present study was supported by a
   research grant from the Program for the Promotion of Fundamental Studies
   in Health Sciences of the National Institute of Biomedical Innovation,
   Japan.
CR Aulchenko YS, 2009, NAT GENET, V41, P47, DOI 10.1038/ng.269
   Barrett JC, 2005, BIOINFORMATICS, V21, P263, DOI 10.1093/bioinformatics/bth457
   Burkhardt R, 2008, ARTERIOSCL THROM VAS, V28, P2078, DOI 10.1161/ATVBAHA.108.172288
   Chasman DI, 2008, CIRC-CARDIOVASC GENE, V1, P21, DOI 10.1161/CIRCGENETICS.108.773168
   Chen YC, 2009, LIPIDS, V44, P733, DOI 10.1007/s11745-009-3314-6
   ENDO A, 1992, J LIPID RES, V33, P1569
   FRIEDEWALD WT, 1972, CLIN CHEM, V18, P499
   Friesen JA, 2004, GENOME BIOL, V5, DOI 10.1186/gb-2004-5-11-248
   Hiura Y, 2009, CIRC J, V73, P1119, DOI 10.1253/circj.CJ-08-1101
   Iwai N, 2006, CIRC J, V70, P805, DOI 10.1253/circj.70.805
   Iwai N, 2002, CIRCULATION, V105, P41, DOI 10.1161/hc0102.101780
   Iwai N, 2007, HYPERTENSION, V49, P825, DOI 10.1161/01.HYP.0000258796.52134.26
   Johnson JM, 2003, SCIENCE, V302, P2141, DOI 10.1126/science.1090100
   Kathiresan S, 2009, NAT GENET, V41, P56, DOI 10.1038/ng.291
   Kathiresan S, 2008, NAT GENET, V40, P189, DOI 10.1038/ng.75
   Kokubo Y, 2005, CIRC J, V69, P138, DOI 10.1253/circj.69.138
   Mannami T, 1997, STROKE, V28, P518, DOI 10.1161/01.STR.28.3.518
   Medina MW, 2008, CIRCULATION, V118, P355, DOI 10.1161/CIRCULATIONAHA.108.773267
   Mora S, 2009, CLIN CHEM, V55, P888, DOI 10.1373/clinchem.2008.117929
   Mukamal KJ, 2009, CIRC J, V73, P1302, DOI 10.1253/circj.CJ-08-0912
   Nakayama K, 2009, J MED GENET, V46, P370, DOI 10.1136/jmg.2008.064063
   Sandhu MS, 2008, LANCET, V371, P483, DOI 10.1016/S0140-6736(08)60208-1
   Saxena R, 2007, SCIENCE, V316, P1331, DOI 10.1126/science.1142358
   Shioji K, 2004, HYPERTENS RES, V27, P31, DOI 10.1291/hypres.27.31
   Tabara Y, 2009, DIABETES, V58, P493, DOI 10.2337/db07-1785
   Tai ES, 2009, J LIPID RES, V50, P514, DOI 10.1194/jlr.M800456-JLR200
   Takashima N, 2007, CIRC J, V71, P495, DOI 10.1253/circj.71.495
   Teramoto T, 2007, J ATHEROSCLER THROMB, V14, P45, DOI 10.5551/jat.14.45
   Wallace C, 2008, AM J HUM GENET, V82, P139, DOI 10.1016/j.ajhg.2007.11.001
   Wang ZX, 2009, CIRC J, V73, P2322, DOI 10.1253/circj.CJ-08-1198
   Willer CJ, 2008, NAT GENET, V40, P161, DOI 10.1038/ng.76
NR 31
TC 15
Z9 16
U1 0
U2 2
PU JAPANESE CIRCULATION SOC
PI TOYKO
PA 18TH FLOOR IMPERIAL HOTEL TOWER, 1-1-1 UCHISAIWAI-CHO CHIYODA-KU, TOYKO,
   100-0011, JAPAN
SN 1346-9843
EI 1347-4820
J9 CIRC J
JI Circ. J.
PD MAR
PY 2010
VL 74
IS 3
BP 518
EP 522
DI 10.1253/circj.CJ-09-0790
PG 5
WC Cardiac & Cardiovascular Systems
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology
GA 566UH
UT WOS:000275398200023
PM 20145341
OA Bronze
DA 2025-04-10
ER

PT J
AU Kronert, WA
   Melkani, GC
   Melkani, A
   Bernstein, SI
AF Kronert, William A.
   Melkani, Girish C.
   Melkani, Anju
   Bernstein, Sanford I.
TI Alternative Relay and Converter Domains Tune Native Muscle Myosin
   Isoform Function in Drosophila
SO JOURNAL OF MOLECULAR BIOLOGY
LA English
DT Article
DE myosin; Drosophila; ATPase; motility; myofibril
ID HEAVY-CHAIN GENE; ACTIN SLIDING VELOCITY; INDIRECT FLIGHT-MUSCLE;
   RECOVERY STROKE; ATP HYDROLYSIS; MYOFIBRIL STRUCTURE; MOLECULAR MOTOR;
   LIGHT-CHAIN; II MOTOR; MUTATIONS
AB Myosin isoforms help define muscle-specific contractile and structural properties. Alternative splicing of myosin heavy chain gene transcripts in Drosophila melanogaster yields muscle-specific isoforms and highlights alternative domains that fine-tune myosin function. To gain insight into how native myosin is tuned, we expressed three embryonic myosin isoforms in indirect flight muscles lacking endogenous myosin. These isoforms differ in their relay and/or converter domains. We analyzed isoform-specific ATPase activities, in vitro actin motility and myofibril structure/stability. We find that dorsal acute body wall muscle myosin (EMB-9c11d) shows a significant increase in MgATPase V-max and actin sliding velocity, as well as abnormal myofibril assembly compared to cardioblast myosin (EMB-11d). These properties differ as a result of alternative exon-9-encoded relay domains that are hypothesized to communicate signals among the ATP-binding pocket, actin-binding site and the converter domain. Further, EMB-11d shows significantly reduced levels of basal Ca- and MgATPase as well as MgATPase Vmax compared to embryonic body wall muscle isoform (EMB) (expressed in a multitude of body wall muscles). EMB-11d also induces increased actin sliding velocity and stabilizes myofibril structure compared to EMB. These differences arise from exon-11-encoded alternative converter domains that are proposed to reposition the lever arm during the power and recovery strokes. We conclude that relay and converter domains of native myosin isoforms fine-tune ATPase activity, actin motility and muscle ultrastructure. This verifies and extends previous studies with chimeric molecules and indicates that interactions of the relay and converter during the contractile cycle are key to myosin-isoform-specific kinetic and mechanical functions. (C) 2011 Elsevier Ltd. All rights reserved.
C1 [Bernstein, Sanford I.] San Diego State Univ, Dept Biol, Inst Mol Biol, San Diego, CA 92182 USA.
   San Diego State Univ, Inst Heart, San Diego, CA 92182 USA.
C3 California State University System; San Diego State University;
   California State University System; San Diego State University
RP Bernstein, SI (corresponding author), San Diego State Univ, Dept Biol, Inst Mol Biol, San Diego, CA 92182 USA.
EM sbernst@sciences.sdsu.edu
RI Melkani, Girish/KZT-8700-2024
OI Melkani, Girish/0000-0003-0353-4633; Bernstein,
   Sanford/0000-0001-7094-5390
FU National Institutes of Health [R01 GM32443]; National Science Foundation
   [0308029]; Div Of Biological Infrastructure; Direct For Biological
   Sciences [0308029] Funding Source: National Science Foundation
FX Funds to support this research were provided by the National Institutes
   of Health grant R01 GM32443 to S.I.B. A National Science Foundation
   equipment grant (0308029) to Dr. Steven Barlow of the San Diego State
   University Electron Microscope Facility supported the purchase of the
   electron microscope. We appreciate the efforts of Jennifer Suggs in
   performing the crosses for the crawling assays. We thank Dr. Douglas
   Swank (Rensselaer Polytechnic Institute) for helpful comments on the
   manuscript.
CR Barton B, 2007, J MUSCLE RES CELL M, V28, P219, DOI 10.1007/s10974-007-9120-y
   Bate M, 1993, DEV DROSOPHILA METAN, V2, P1013
   Batra R, 1999, BIOL CHEM, V380, P1017, DOI 10.1515/BC.1999.126
   BECKER KD, 1992, J CELL BIOL, V116, P669, DOI 10.1083/jcb.116.3.669
   BERNSTEIN SI, 1983, NATURE, V302, P393, DOI 10.1038/302393a0
   Bernstein SI, 1997, J MOL BIOL, V271, P1, DOI 10.1006/jmbi.1997.1160
   Bloemink MJ, 2011, J BIOL CHEM, V286, P28435, DOI 10.1074/jbc.M111.258228
   Bloemink MJ, 2009, J MOL BIOL, V389, P707, DOI 10.1016/j.jmb.2009.04.036
   Cammarato A, 2008, MOL BIOL CELL, V19, P553, DOI 10.1091/mbc.E07-09-0890
   COLLIER VL, 1990, GENE DEV, V4, P885, DOI 10.1101/gad.4.6.885
   Dominguez R, 1998, CELL, V94, P559, DOI 10.1016/S0092-8674(00)81598-6
   DRUMMOND DR, 1991, MOL GEN GENET, V226, P70, DOI 10.1007/BF00273589
   Fischer S, 2005, P NATL ACAD SCI USA, V102, P6873, DOI 10.1073/pnas.0408784102
   GEORGE EL, 1989, MOL CELL BIOL, V9, P2957, DOI 10.1128/MCB.9.7.2957
   Gyimesi M, 2008, J BIOL CHEM, V283, P8153, DOI 10.1074/jbc.M708863200
   HASTINGS GA, 1991, J CELL BIOL, V114, P263, DOI 10.1083/jcb.114.2.263
   Holmes KC, 2000, PHILOS T R SOC B, V355, P419, DOI 10.1098/rstb.2000.0583
   Ito K, 2003, J BIOL CHEM, V278, P31049, DOI 10.1074/jbc.M304138200
   Köhler J, 2002, P NATL ACAD SCI USA, V99, P3557, DOI 10.1073/pnas.062415899
   Koppole S, 2007, STRUCTURE, V15, P825, DOI 10.1016/j.str.2007.06.008
   Koppole S, 2006, J MOL BIOL, V361, P604, DOI 10.1016/j.jmb.2006.06.022
   KRONERT WA, 1995, J MOL BIOL, V249, P111, DOI 10.1006/jmbi.1995.0283
   Kronert WA, 2008, J MOL BIOL, V379, P443, DOI 10.1016/j.jmb.2008.04.010
   Kronert WA, 2010, J MOL BIOL, V398, P625, DOI 10.1016/j.jmb.2010.03.049
   Littlefield KP, 2003, AM J PHYSIOL-CELL PH, V284, pC1031, DOI 10.1152/ajpcell.00474.2002
   Mesentean S, 2007, J MOL BIOL, V367, P591, DOI 10.1016/j.jmb.2006.12.058
   Miller BM, 2005, J MOL BIOL, V353, P14, DOI 10.1016/j.jmb.2005.08.012
   Miller BM, 2003, J BIOL CHEM, V278, P50293, DOI 10.1074/jbc.M308318200
   Montana ES, 2004, J CELL BIOL, V164, P1045, DOI 10.1083/jcb.200308158
   Naimi B, 2001, MOL BIOL CELL, V12, P1529, DOI 10.1091/mbc.12.5.1529
   Nongthomba U, 2003, GENETICS, V164, P209
   ODONNELL PT, 1988, J CELL BIOL, V107, P2601, DOI 10.1083/jcb.107.6.2601
   ODONNELL PT, 1989, GENE DEV, V3, P1233, DOI 10.1101/gad.3.8.1233
   Park S, 2000, BIOCHEMISTRY-US, V39, P11732, DOI 10.1021/bi000945t
   Pirrotta V, 1988, Biotechnology, V10, P437
   Ramanath S, 2011, BIOPHYS J, V101, P1114, DOI 10.1016/j.bpj.2011.07.045
   ROZEK CE, 1983, CELL, V32, P23, DOI 10.1016/0092-8674(83)90493-2
   RUBIN GM, 1982, SCIENCE, V218, P348, DOI 10.1126/science.6289436
   Sasaki N, 2003, BIOCHEMISTRY-US, V42, P90, DOI 10.1021/bi026051l
   Schwarzl SM, 2006, BIOCHEMISTRY-US, V45, P5830, DOI 10.1021/bi052433q
   Seebohm B, 2009, BIOPHYS J, V97, P806, DOI 10.1016/j.bpj.2009.05.023
   Shih WM, 2001, J BIOL CHEM, V276, P19491, DOI 10.1074/jbc.M010887200
   Swank DM, 2003, J BIOL CHEM, V278, P17475, DOI 10.1074/jbc.M212727200
   Swank DM, 2002, NAT CELL BIOL, V4, P312, DOI 10.1038/ncb776
   Swank DM, 2001, J BIOL CHEM, V276, P15117, DOI 10.1074/jbc.M008379200
   Tang S, 2007, J MOL BIOL, V373, P1361, DOI 10.1016/j.jmb.2007.08.059
   TOHTONG R, 1995, NATURE, V374, P650, DOI 10.1038/374650a0
   Tsiavaliaris G, 2002, EMBO REP, V3, P1099, DOI 10.1093/embo-reports/kvf214
   van Duffelen M, 2005, BIOCHEM BIOPH RES CO, V329, P563, DOI 10.1016/j.bbrc.2005.01.152
   Wells L, 1996, EMBO J, V15, P4454, DOI 10.1002/j.1460-2075.1996.tb00822.x
   Yang CX, 2008, BIOPHYS J, V95, P5228, DOI 10.1529/biophysj.108.136192
   Yang C, 2010, BIOPHYS J, V99, P1546, DOI 10.1016/j.bpj.2010.06.047
   Yengo CM, 2000, J BIOL CHEM, V275, P25481, DOI 10.1074/jbc.M002910200
   Zhang SX, 2001, MECH DEVELOP, V101, P35, DOI 10.1016/S0925-4773(00)00549-9
NR 54
TC 15
Z9 21
U1 0
U2 9
PU ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
PI LONDON
PA 24-28 OVAL RD, LONDON NW1 7DX, ENGLAND
SN 0022-2836
J9 J MOL BIOL
JI J. Mol. Biol.
PD MAR 2
PY 2012
VL 416
IS 4
BP 543
EP 557
DI 10.1016/j.jmb.2011.12.044
PG 15
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 909KR
UT WOS:000301563900008
PM 22226837
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Palmer, BM
   Georgakopoulos, D
   Janssen, PM
   Wang, Y
   Alpert, NR
   Belardi, DF
   Harris, SP
   Moss, RL
   Burgon, PG
   Seidman, CE
   Seidman, JG
   Maughan, DW
   Kass, DA
AF Palmer, BM
   Georgakopoulos, D
   Janssen, PM
   Wang, Y
   Alpert, NR
   Belardi, DF
   Harris, SP
   Moss, RL
   Burgon, PG
   Seidman, CE
   Seidman, JG
   Maughan, DW
   Kass, DA
TI Role of cardiac myosin binding protein C in sustaining left ventricular
   systolic stiffening
SO CIRCULATION RESEARCH
LA English
DT Article
DE C-protein; ventricular mechanics; time-varying elastance;
   cardiomyopathy; myocardium
ID FAMILIAL HYPERTROPHIC CARDIOMYOPATHY; SPLICE DONOR SITE; MOUSE MODEL;
   MYBP-C; THICK FILAMENTS; SKELETAL-MUSCLE; PHOSPHORYLATION; MICE; GENE;
   IDENTIFICATION
AB Despite advances in the molecular biology of cardiac myosin binding protein-C (cMyBP-C), little is understood about its precise role in muscle contraction, particularly in the intact heart. We tested the hypothesis that cMyBP-C is central to the time course and magnitude of left ventricular systolic elastance ( chamber stiffening), and assessed mechanisms for this influence in intact hearts, trabeculae, and skinned fibers from wild-type (+/+) and homozygous truncated cMyBP-C (t/t) male mice. cMyBP-C protein was not detected by gel electrophoresis or Western blot in t/t myocardium. cMyBP-C t/t ventricles displayed reduced peak elastance, but more strikingly a marked abbreviation of the systolic elastance time course, which peaked earlier (27.6 +/- 2.1 ms) than in +/+ controls (47.8 +/- 1.6 ms). Control hearts reached only 42 +/- 4% of maximum elastance at the onset of ejection, with substantial further stiffening during ejection. This contrasted to t/t mutants, which reached 77 +/- 3% of peak elastance before ejection of peak. These unusual findings were not observed in alternative models involving severe cardiomyopathy, but were recapitulated in a cMyBP-C null mouse. The abbreviated elastance time course and lower peak were consistent with earlier time-to-peak trabecular tension, increased unloaded shortening velocity in t/t skinned muscle strips, and dramatically reduced myofilament stiffness at diastolic calcium concentrations. These results provide novel insights into the role of cMyBP-C in myocardial systolic mechanics. Abnormal sarcomere shortening velocity and abbreviated muscle stiffening may underlie development of cardiac dysfunction associated with deficient incorporation of cMyBP-C.
C1 Univ Vermont, Dept Mol Physiol & Biophys, Burlington, VT 05405 USA.
   Johns Hopkins Med Inst, Dept Med, Baltimore, MD 21205 USA.
   Johns Hopkins Med Inst, Dept Biomed Engn, Baltimore, MD 21205 USA.
   Johns Hopkins Univ, Sch Med, Inst Mol Cardiobiol, Baltimore, MD USA.
   Univ Wisconsin, Sch Med, Dept Physiol, Madison, WI 53706 USA.
   Howard Hughes Med Inst, Dept Genet, Boston, MA 02115 USA.
   Harvard Univ, Sch Med, Boston, MA USA.
C3 University of Vermont; Johns Hopkins University; Johns Hopkins Medicine;
   Johns Hopkins University; Johns Hopkins Medicine; Johns Hopkins
   University; University of Wisconsin System; University of Wisconsin
   Madison; Howard Hughes Medical Institute; Harvard University; Harvard
   Medical School
RP Palmer, BM (corresponding author), Univ Vermont, Dept Mol Physiol & Biophys, 127 HSRF Beaumont Ave, Burlington, VT 05405 USA.
EM palmer@physiology.med.uvm.edu
RI Burgon, Patrick/ABB-1027-2021; Janssen, Paul/E-3307-2011; Seidman,
   Jon/JXN-4736-2024; Georgakopoulos, Dimitrios/C-5019-2011
OI Janssen, Paul/0000-0002-9682-3014; Burgon, Patrick/0000-0003-4771-023X
FU NHLBI NIH HHS [HL59408-3] Funding Source: Medline
CR BENNETT P, 1986, J MUSCLE RES CELL M, V7, P550, DOI 10.1007/BF01753571
   Blanchard E, 1999, CIRC RES, V84, P475, DOI 10.1161/01.RES.84.4.475
   Carrier L, 1997, CIRC RES, V80, P427, DOI 10.1161/01.res.0000435859.24609.b3
   Champion HC, 2003, CIRCULATION, V108, P2790, DOI 10.1161/01.CIR.0000096487.88897.9B
   CRAIG R, 1976, J MOL BIOL, V102, P325, DOI 10.1016/S0022-2836(76)80057-5
   Gao WD, 1998, J PHYSIOL-LONDON, V507, P175, DOI 10.1111/j.1469-7793.1998.175bu.x
   GAUTEL M, 1995, EMBO J, V14, P1952, DOI 10.1002/j.1460-2075.1995.tb07187.x
   Georgakopoulos D, 2000, AM J PHYSIOL-HEART C, V279, pH443, DOI 10.1152/ajpheart.2000.279.1.H443
   Georgakopoulos D, 1998, AM J PHYSIOL-HEART C, V274, pH1416, DOI 10.1152/ajpheart.1998.274.4.H1416
   Gilbert R, 1996, J CELL SCI, V109, P101
   Harris SP, 2002, CIRC RES, V90, P594, DOI 10.1161/01.RES.0000012222.70819.64
   HOFMANN PA, 1991, J PHYSIOL-LONDON, V439, P701, DOI 10.1113/jphysiol.1991.sp018689
   Janssen PML, 2002, AM J PHYSIOL-HEART C, V282, pH499, DOI 10.1152/ajpheart.00595.2001
   KORETZ JF, 1982, BIOPHYS J, V37, P433, DOI 10.1016/S0006-3495(82)84689-4
   Korte FS, 2003, CIRC RES, V93, P752, DOI 10.1161/01.RES.0000096363.85588.9A
   Kunst G, 2000, CIRC RES, V86, P51, DOI 10.1161/01.RES.86.1.51
   Levine R, 2001, BIOPHYS J, V81, P1070, DOI 10.1016/S0006-3495(01)75764-5
   Liao P, 2001, P NATL ACAD SCI USA, V98, P12283, DOI 10.1073/pnas.211086598
   McConnell BK, 1999, J CLIN INVEST, V104, P1235, DOI 10.1172/JCI7377
   Milner DJ, 1999, J MOL CELL CARDIOL, V31, P2063, DOI 10.1006/jmcc.1999.1037
   Moolman JA, 2000, CIRCULATION, V101, P1396, DOI 10.1161/01.CIR.101.12.1396
   Moolman-Smook J, 2002, CIRC RES, V91, P704, DOI 10.1161/01.RES.0000036750.81083.83
   MOOS C, 1980, BIOCHIM BIOPHYS ACTA, V632, P141, DOI 10.1016/0304-4165(80)90071-9
   Murphy AM, 2000, SCIENCE, V287, P488, DOI 10.1126/science.287.5452.488
   PALMER BM, IN PRESS J MOL CELL
   Richard P, 2003, CIRCULATION, V107, P2227, DOI 10.1161/01.CIR.0000066323.15244.54
   Robbins J, 2002, CIRC RES, V91, P656, DOI 10.1161/01.RES.0000039080.47825.CA
   Rottbauer W, 1997, J CLIN INVEST, V100, P475, DOI 10.1172/JCI119555
   Sato N, 2003, MOL BIOL CELL, V14, P3180, DOI 10.1091/mbc.e02-10-0685
   Senzaki H, 1996, CIRCULATION, V94, P2497, DOI 10.1161/01.CIR.94.10.2497
   Song QJ, 2003, J CLIN INVEST, V111, P859, DOI 10.1172/JCI200316738
   Squire JM, 2003, J MOL BIOL, V331, P713, DOI 10.1016/S0022-2836(03)00781-2
   STARR R, 1978, BIOCHEM J, V171, P813, DOI 10.1042/bj1710813
   Stull LB, 2002, J MOL CELL CARDIOL, V34, P1367, DOI 10.1006/jmcc.2002.2065
   VANBUREN P, 1995, CIRC RES, V77, P439, DOI 10.1161/01.RES.77.2.439
   Wang Y, 1999, AUTOIMMUNITY, V31, P151, DOI 10.3109/08916939908994060
   Weisberg A, 1996, P NATL ACAD SCI USA, V93, P8999, DOI 10.1073/pnas.93.17.8999
   Winegrad S, 1999, CIRC RES, V84, P1117, DOI 10.1161/01.RES.84.10.1117
   Witt CC, 2001, J BIOL CHEM, V276, P5353, DOI 10.1074/jbc.M008691200
   Yang QL, 1999, CIRC RES, V85, P841, DOI 10.1161/01.RES.85.9.841
   Yang QL, 2001, CARDIOVASC RES, V51, P80, DOI 10.1016/S0008-6363(01)00273-5
   Yang QL, 1998, J CLIN INVEST, V102, P1292, DOI 10.1172/JCI3880
NR 42
TC 101
Z9 114
U1 0
U2 3
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA 530 WALNUT ST, PHILADELPHIA, PA 19106-3621 USA
SN 0009-7330
J9 CIRC RES
JI Circ.Res.
PD MAY 14
PY 2004
VL 94
IS 9
BP 1249
EP 1255
DI 10.1161/01.RES.0000126898.95550.31
PG 7
WC Cardiac & Cardiovascular Systems; Hematology; Peripheral Vascular
   Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology; Hematology
GA 821ET
UT WOS:000221443900015
PM 15059932
OA Bronze
DA 2025-04-10
ER

PT J
AU Zhang, ZL
   Biesiadecki, BJ
   Jin, JP
AF Zhang, Zhiling
   Biesiadecki, Brandon J.
   Jin, Jian-Ping
TI Selective deletion of the NH2-terminal variable region of
   cardiac troponin T in ischemia reperfusion by myofibril-associated
   μ-calpain cleavage
SO BIOCHEMISTRY
LA English
DT Article
ID RABBIT SKELETAL-MUSCLE; COMPLETE NUCLEOTIDE-SEQUENCE; N-TERMINAL
   TRUNCATION; STRUCTURAL ORGANIZATION; DILATED CARDIOMYOPATHY; ISOFORMS;
   TROPOMYOSIN; EXPRESSION; CONTRACTION; BINDING
AB The structure of the NH2-terminal region of troponin T (TnT) is hypervariable among the muscle type-specific isoforms and is also regulated by alternative RNA splicing. This region does not contain binding sites for other thin filament proteins, but alteration of its structure affects the Ca2+ regulation of muscle contraction. Here we report a truncated cardiac TnT produced during myocardial ischemia reperfusion. Amino acid sequencing and protein fragment reconstruction determined that it is generated by a posttranslational modification selectively removing the NH2-terminal variable region and preserving the conserved core structure of TnT. Triton X-100 extraction of cardiac muscle fibers promoted production of the NH2-terminal truncated cardiac TnT (cTnT-ND), indicating a myofibril-associated proteolytic activity. mu-Calpain is a myofibril-associated protease and is known to degrade TnT. Supporting a role of mu-calpain in producing cTnT-ND in myocardial ischemia reperfusion, calpain inhibitors decreased the level of cTnT-ND in Triton-extracted myofibrils. mu-Calpain treatment of the cardiac myofibril and troponin complex specifically reproduced cTnT-ND. In contrast, mu-calpain treatment of isolated cardiac TnT resulted in nonspecific degradation, suggesting that this structural modification is relevant to physiological structures of the myofilament. Triton X-100 treatment of transgenic mouse cardiac myofibrils overexpressing fast skeletal muscle TnT produced similar NH2-terminal truncations of the endogenous and exogenous TnT, despite different amino acid sequences at the cleavage site. With the functional consequences of removing the NH2-terminal variable region of TnT, the mu-calpain-mediated proteolytic modification of TnT may act as an acute mechanism to adjust muscle contractility under stress conditions.
C1 Evanston NW Healthcare, Sect Mol Cardiol, Evanston, IL 60201 USA.
   Northwestern Univ, Feinberg Sch Med, Evanston, IL 60201 USA.
C3 NorthShore University Health System; Northwestern University; Feinberg
   School of Medicine
RP Jin, JP (corresponding author), Evanston NW Healthcare, Sect Mol Cardiol, Evanston, IL 60201 USA.
EM jpjin@northwestern.edu
RI Zhang, Zhiling/GPS-8205-2022; Jin, Jian-Ping/AAD-1149-2020
OI Jin, JP/0000-0001-9932-1063
FU NHLBI NIH HHS [HL078773, R01 HL078773, R01 HL078773-03, R01 HL078773-02]
   Funding Source: Medline; NIAMS NIH HHS [AR048816, R01 AR048816-06, R01
   AR048816] Funding Source: Medline; NICHD NIH HHS [R21 HD044824,
   HD044824] Funding Source: Medline
CR ANDERSON PAW, 1995, CIRC RES, V76, P681, DOI 10.1161/01.RES.76.4.681
   Barbato JC, 2005, J BIOL CHEM, V280, P6602, DOI 10.1074/jbc.M408525200
   Biesiadecki B, 2005, BIOPHYS J, V88, p360A
   Biesiadecki BJ, 2002, J BIOL CHEM, V277, P50275, DOI 10.1074/jbc.M206369200
   Biesiadecki BJ, 2002, J BIOL CHEM, V277, P18459, DOI 10.1074/jbc.M200788200
   BREITBART RE, 1986, J MOL BIOL, V188, P313, DOI 10.1016/0022-2836(86)90157-9
   Chandra M, 1999, J MOL CELL CARDIOL, V31, P867, DOI 10.1006/jmcc.1999.0928
   Colantonio DA, 2004, CARDIOVASC RES, V63, P217, DOI 10.1016/j.cardiores.2004.04.006
   Communal C, 2002, P NATL ACAD SCI USA, V99, P6252, DOI 10.1073/pnas.092022999
   CONG JY, 1989, J BIOL CHEM, V264, P10096
   DILISA F, 1995, BIOCHEM J, V308, P57, DOI 10.1042/bj3080057
   Foster DB, 2003, CIRC RES, V93, P917, DOI 10.1161/01.RES.0000099889.35340.6F
   FUJITA S, 1992, J BIOCHEM-TOKYO, V112, P306, DOI 10.1093/oxfordjournals.jbchem.a123896
   Goll DE, 2003, PHYSIOL REV, V83, P731, DOI 10.1152/physrev.00029.2002
   Gomes AV, 2002, J BIOL CHEM, V277, P35341, DOI 10.1074/jbc.M204118200
   Guttmann RP, 1997, J BIOL CHEM, V272, P2005, DOI 10.1074/jbc.272.3.2005
   Hinkle A, 1999, J BIOL CHEM, V274, P7157, DOI 10.1074/jbc.274.11.7157
   Hirano Katsuya, 2004, Journal of Smooth Muscle Research, V40, P219, DOI 10.1540/jsmr.40.219
   Huang QQ, 1999, J PHYSIOL-LONDON, V520, P231, DOI 10.1111/j.1469-7793.1999.00231.x
   Huang QQ, 1999, GENE, V229, P1, DOI 10.1016/S0378-1119(99)00051-7
   Jin JP, 2000, AM J PHYSIOL-CELL PH, V279, pC1067, DOI 10.1152/ajpcell.2000.279.4.C1067
   Jin JP, 2000, BIOCHEMISTRY-US, V39, P11702, DOI 10.1021/bi9927437
   Jin JP, 1998, GENE, V214, P121, DOI 10.1016/S0378-1119(98)00214-5
   JIN JP, 1988, J BIOL CHEM, V263, P7309
   JIN JP, 1992, J MOL BIOL, V227, P1269, DOI 10.1016/0022-2836(92)90540-Z
   JIN JP, 1995, J BIOL CHEM, V270, P6908
   Jin JP, 2003, J BIOL CHEM, V278, P26159, DOI 10.1074/jbc.M303469200
   Jin JP, 2001, J MOL EVOL, V52, P103, DOI 10.1007/s002390010139
   Jin JP, 2001, BIOCHEMISTRY-US, V40, P2623, DOI 10.1021/bi002423j
   Jin JP, 1996, GENE, V168, P217, DOI 10.1016/0378-1119(95)00803-9
   Kitamura SI, 2005, J AGR FOOD CHEM, V53, P4178, DOI 10.1021/jf047974l
   Layland J, 2005, CARDIOVASC RES, V66, P12, DOI 10.1016/j.cardiores.2004.12.022
   LEAVIS PC, 1984, CRC CR REV BIOCH MOL, V16, P235, DOI 10.3109/10409238409108717
   LIN JJC, 1985, HYBRIDOMA, V4, P223, DOI 10.1089/hyb.1985.4.223
   MARTIN AF, 1981, J BIOL CHEM, V256, P964
   Murphy AM, 2000, SCIENCE, V287, P488, DOI 10.1126/science.287.5452.488
   Murphy KG, 2006, NAT MED, V12, P32, DOI 10.1038/nm0106-32
   Ogut O, 1998, J BIOL CHEM, V273, P27858, DOI 10.1074/jbc.273.43.27858
   OHTSUKI I, 1984, J BIOCHEM, V95, P1337, DOI 10.1093/oxfordjournals.jbchem.a134740
   PAN BS, 1991, J BIOL CHEM, V266, P12432
   PEARLSTONE JR, 1982, J BIOL CHEM, V257, P587
   PEARLSTONE JR, 1985, CAN J BIOCHEM CELL B, V63, P212, DOI 10.1139/o85-030
   Perry SV, 1998, J MUSCLE RES CELL M, V19, P575
   Piper HM, 2003, ANN THORAC SURG, V75, pS644, DOI 10.1016/S0003-4975(02)04686-6
   SMILLIE LB, 1982, METHOD ENZYMOL, V85, P234
   SOLARO RJ, 1971, BIOCHIM BIOPHYS ACTA, V245, P259, DOI 10.1016/0005-2728(71)90033-8
   Sumandea MP, 2004, ANN NY ACAD SCI, V1015, P39, DOI 10.1196/annals.1302.004
   Takeda S, 2003, NATURE, V424, P35, DOI 10.1038/nature01780
   Tobacman LS, 1996, ANNU REV PHYSIOL, V58, P447, DOI 10.1146/annurev.ph.58.030196.002311
   Vinogradova MV, 2005, P NATL ACAD SCI USA, V102, P5038, DOI 10.1073/pnas.0408882102
   Wang J, 1998, BIOCHEMISTRY-US, V37, P14519, DOI 10.1021/bi9812322
   Wang J, 1997, GENE, V193, P105, DOI 10.1016/S0378-1119(97)00100-5
   Wang KKW, 1996, P NATL ACAD SCI USA, V93, P6687, DOI 10.1073/pnas.93.13.6687
   Wang Q, 2001, ANAT RECORD, V263, P72, DOI 10.1002/ar.1078
   Yu ZB, 2002, BIOPHYS J, V82, p394A
   Yu ZB, 2001, J BIOL CHEM, V276, P15753, DOI 10.1074/jbc.M011048200
   ZOT AS, 1987, ANNU REV BIOPHYS BIO, V16, P535
NR 57
TC 81
Z9 88
U1 0
U2 6
PU AMER CHEMICAL SOC
PI WASHINGTON
PA 1155 16TH ST, NW, WASHINGTON, DC 20036 USA
SN 0006-2960
J9 BIOCHEMISTRY-US
JI Biochemistry
PD SEP 26
PY 2006
VL 45
IS 38
BP 11681
EP 11694
DI 10.1021/bi060273s
PG 14
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 085AQ
UT WOS:000240575900044
PM 16981728
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Kopylova, GV
   Kochurova, AM
   Yampolskaya, DS
   Nefedova, VV
   Tsaturyan, AK
   Koubassova, NA
   Kleymenov, SY
   Levitsky, DI
   Bershitsky, SY
   Matyushenko, AM
   Shchepkin, DV
AF Kopylova, Galina V. V.
   Kochurova, Anastasia M. M.
   Yampolskaya, Daria S. S.
   Nefedova, Victoria V. V.
   Tsaturyan, Andrey K. K.
   Koubassova, Natalia A. A.
   Kleymenov, Sergey Y. Y.
   Levitsky, Dmitrii I. I.
   Bershitsky, Sergey Y. Y.
   Matyushenko, Alexander M. M.
   Shchepkin, Daniil V. V.
TI Structural and Functional Properties of Kappa Tropomyosin
SO INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
LA English
DT Article
DE cardiac tropomyosin isoforms; thin filament; atrial and ventricular
   myosin; actin-myosin interaction; in vitro motility assay
ID HYPERTROPHIC CARDIOMYOPATHY MUTATIONS; CARDIAC TROPONIN-T;
   ALPHA-TROPOMYOSIN; ACTIN-FILAMENT; ISOFORMS; BINDING; MYOSIN; REGION;
   EXPRESSION; JUNCTION
AB In the myocardium, the TPM1 gene expresses two isoforms of tropomyosin (Tpm), alpha (aTpm; Tpm 1.1) and kappa (?Tpm; Tpm 1.2). ?Tpm is the result of alternative splicing of the TPM1 gene. We studied the structural features of ?Tpm and its regulatory function in the atrial and ventricular myocardium using an in vitro motility assay. We tested the possibility of Tpm heterodimer formation from a- and ?-chains. Our result shows that the formation of a?Tpm heterodimer is thermodynamically favorable, and in the myocardium, ?Tpm most likely exists as a?Tpm heterodimer. Using circular dichroism, we compared the thermal unfolding of aaTpm, a?Tpm, and ??Tpm. ??Tpm had the lowest stability, while the a?Tpm was more stable than aaTpm. The differential scanning calorimetry results indicated that the thermal stability of the N-terminal part of ??Tpm is much lower than that of aaTpm. The affinity of aaTpm and ??Tpm to F-actin did not differ, and a?Tpm interacted with F-actin significantly worse. The troponin T1 fragment enhanced the ??Tpm and a?Tpm affinity to F-actin. ??Tpm differently affected the calcium regulation of the interaction of pig and rat ventricular myosin with the thin filament. With rat myosin, calcium sensitivity of thin filaments containing ??Tpm was significantly lower than that with aaTpm and with pig myosin, and the sensitivity did not differ. Thin filaments containing ??Tpm and a?Tpm were better activated by pig atrial myosin than those containing aaTpm.
C1 [Kopylova, Galina V. V.; Kochurova, Anastasia M. M.; Bershitsky, Sergey Y. Y.; Shchepkin, Daniil V. V.] Russian Acad Sci, Inst Immunol & Physiol, Ekaterinburg 620049, Russia.
   [Yampolskaya, Daria S. S.; Nefedova, Victoria V. V.; Kleymenov, Sergey Y. Y.; Levitsky, Dmitrii I. I.; Matyushenko, Alexander M. M.] Russian Acad Sci, Res Ctr Biotechnol, Moscow 119071, Russia.
   [Tsaturyan, Andrey K. K.; Koubassova, Natalia A. A.] Moscow MV Lomonosov State Univ, Inst Mech, Moscow 119192, Russia.
   [Kleymenov, Sergey Y. Y.] Russian Acad Sci, Koltzov Inst Dev Biol, Moscow 119334, Russia.
C3 Russian Academy of Sciences; Institute of Immunology & Physiology UB
   RAS; Russian Academy of Sciences; Research Center of Biotechnology RAS;
   Lomonosov Moscow State University; Russian Academy of Sciences; Koltzov
   Institute of Developmental Biology of the Russian Academy of Sciences
RP Bershitsky, SY (corresponding author), Russian Acad Sci, Inst Immunol & Physiol, Ekaterinburg 620049, Russia.
EM g_rodionova@mail.ru; kochurova.a.m@mail.ru; daria_logvinova@mail.ru;
   victoria.v.nefedova@mail.ru; andrey.tsaturyan@gmail.com;
   nkoubassova@gmail.com; s.yu.kleymenov@gmail.com; levitsky@inbi.ras.ru;
   serg.bersh@gmail.com; ammatyushenko@mail.ru; cmybp@mail.ru
RI Kopylova, Galina/ABF-2117-2020; Tsaturyan, Andrey/GXF-8722-2022;
   Shchepkin, Daniil/ABF-1160-2020; Bershitsky, Sergey/AAE-6814-2019;
   Koubassova, Natalia/AAI-6490-2021; Kleymenov, Sergey/R-1195-2018
OI Bershitsky, Sergey/0000-0001-5342-1739; Koubassova,
   Natalia/0000-0002-0238-4920; Kleymenov, Sergey/0000-0001-5085-0327;
   Matyushenko, Alexander/0009-0004-2645-4593; Kopylova,
   Galina/0000-0003-2976-2108; Levitsky, Dmitrii/0000-0002-7755-9895;
   Tsaturyan, Andrey/0000-0003-4265-1525; Shchepkin,
   Daniil/0000-0001-6660-4673
FU Russian Science Foundation [22-24-00729]
FX This research was funded by the Russian Science Foundation, grant number
   22-24-00729 (to G.V.K.).
CR Abraham Mark James, 2015, SoftwareX, V1-2, P19, DOI 10.1016/j.softx.2015.06.001
   [Anonymous], 1969, Statistical Mechanics of Chain Molecules
   Brunet NM, 2014, ARCH BIOCHEM BIOPHYS, V552, P11, DOI 10.1016/j.abb.2013.12.021
   Colpan M, 2017, ARCH BIOCHEM BIOPHYS, V630, P18, DOI 10.1016/j.abb.2017.07.006
   Denz CR, 2004, BIOCHEM BIOPH RES CO, V320, P1291, DOI 10.1016/j.bbrc.2004.06.084
   Doran MH, 2022, J GEN PHYSIOL, V155, DOI 10.1085/jgp.202213274
   Doran MH, 2020, BIOPHYS J, V119, P821, DOI 10.1016/j.bpj.2020.07.006
   England J, 2017, J MOL CELL CARDIOL, V106, P1, DOI 10.1016/j.yjmcc.2017.03.006
   FREIRE E, 1978, BIOPOLYMERS, V17, P463, DOI 10.1002/bip.1978.360170212
   Gangadharan B, 2017, P NATL ACAD SCI USA, V114, P11115, DOI 10.1073/pnas.1710354114
   Geeves MA, 2015, J MUSCLE RES CELL M, V36, P147, DOI 10.1007/s10974-014-9389-6
   Greenfield NJ, 2006, J MOL BIOL, V364, P80, DOI 10.1016/j.jmb.2006.08.033
   Jin JP, 2016, INT REV CEL MOL BIO, V321, P1, DOI 10.1016/bs.ircmb.2015.09.002
   Johnson CA, 2021, PLOS BIOL, V19, DOI 10.1371/journal.pbio.3001248
   Kalyva A, 2012, BIOCHEMISTRY-US, V51, P6388, DOI 10.1021/bi300340r
   Karam CN, 2011, J MUSCLE RES CELL M, V31, P315, DOI 10.1007/s10974-010-9237-2
   Katrukha IA, 2013, BIOCHEMISTRY-MOSCOW+, V78, P1447, DOI 10.1134/S0006297913130063
   Kopylova GV, 2022, BIOCHEM BIOPH RES CO, V588, P29, DOI 10.1016/j.bbrc.2021.12.051
   Kremneva E, 2004, BIOPHYS J, V87, P3922, DOI 10.1529/biophysj.104.048793
   Lehman W, 2000, J MOL BIOL, V302, P593, DOI 10.1006/jmbi.2000.4080
   LEHRER SS, 1975, P NATL ACAD SCI USA, V72, P3377, DOI 10.1073/pnas.72.9.3377
   Lindorff-Larsen K, 2010, PROTEINS, V78, P1950, DOI 10.1002/prot.22711
   Madan A, 2020, P NATL ACAD SCI USA, V117, P18822, DOI 10.1073/pnas.2001692117
   Malmqvist UP, 2004, BIOCHEMISTRY-US, V43, P15058, DOI 10.1021/bi0495329
   MARGOSSIAN SS, 1982, METHOD ENZYMOL, V85, P55
   Mashanov GI, 2007, BIOPHYS J, V92, P2199, DOI 10.1529/biophysj.106.081117
   Matyushenko AM, 2019, INT J BIOL MACROMOL, V125, P1266, DOI 10.1016/j.ijbiomac.2018.09.105
   Matyushenko AM, 2018, FEBS J, V285, P871, DOI 10.1111/febs.14369
   Matyushenko AM, 2015, BIOPHYS CHEM, V196, P77, DOI 10.1016/j.bpc.2014.10.001
   McKeown CR, 2014, DEV DYNAM, V243, P800, DOI 10.1002/dvdy.24115
   Minakata S, 2008, BIOPHYS J, V95, P710, DOI 10.1529/biophysj.107.126144
   MONTEIRO PB, 1994, J BIOL CHEM, V269, P10461
   Muthuchamy M, 1998, J MOL CELL CARDIOL, V30, P1545, DOI 10.1006/jmcc.1998.0720
   Nefedova VV, 2022, INT J MOL SCI, V23, DOI 10.3390/ijms232415723
   Ohtsuki I, 2007, ADV EXP MED BIOL, V592, P21
   Palm T, 2001, BIOPHYS J, V81, P2827, DOI 10.1016/S0006-3495(01)75924-3
   PARDEE JD, 1982, METHOD ENZYMOL, V85, P164
   Peng Y, 2013, J MUSCLE RES CELL M, V34, P199, DOI 10.1007/s10974-013-9352-y
   Perry SV, 2001, J MUSCLE RES CELL M, V22, P5, DOI 10.1023/A:1010303732441
   Pettersen EF, 2004, J COMPUT CHEM, V25, P1605, DOI 10.1002/jcc.20084
   POTTER JD, 1982, METHOD ENZYMOL, V85, P241
   Prodanovic M, 2022, INT J MOL SCI, V23, DOI 10.3390/ijms23031135
   Racca AW, 2020, J BIOL CHEM, V295, P17128, DOI 10.1074/jbc.RA120.014713
   Rajan S, 2010, CIRCULATION, V121, P410, DOI 10.1161/CIRCULATIONAHA.109.889725
   Shapovalov MV, 2011, STRUCTURE, V19, P844, DOI 10.1016/j.str.2011.03.019
   Shchepkin DV, 2017, BIOCHEM BIOPH RES CO, V490, P324, DOI 10.1016/j.bbrc.2017.06.043
   Sliwinska M, 2011, CYTOSKELETON, V68, P300, DOI 10.1002/cm.20513
   Sumida JP, 2008, J BIOL CHEM, V283, P6728, DOI 10.1074/jbc.M707485200
   Sundar S, 2020, BIOPHYS J, V118, P303, DOI 10.1016/j.bpj.2019.11.3396
   Walklate J, 2021, CELL MOL LIFE SCI, V78, P7309, DOI 10.1007/s00018-021-03971-y
   Whitby FG, 2000, PROTEINS, V38, P49
   Yamashita H, 2003, CARDIOVASC RES, V60, P580, DOI 10.1016/j.cardiores.2003.09.011
   Zajdel RW, 2013, REGEN MED RES, V1, DOI 10.1186/2050-490X-1-8
NR 53
TC 2
Z9 2
U1 0
U2 2
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
SN 1661-6596
EI 1422-0067
J9 INT J MOL SCI
JI Int. J. Mol. Sci.
PD MAY 6
PY 2023
VL 24
IS 9
AR 8340
DI 10.3390/ijms24098340
PG 20
WC Biochemistry & Molecular Biology; Chemistry, Multidisciplinary
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Chemistry
GA G2HP9
UT WOS:000987434700001
PM 37176047
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Cheng, JD
   Tester, DJ
   Tan, BH
   Valdivia, CR
   Kroboth, S
   Ye, B
   January, CT
   Ackerman, MJ
   Makielski, JC
AF Cheng, Jianding
   Tester, David J.
   Tan, Bi-Hua
   Valdivia, Carmen R.
   Kroboth, Stacie
   Ye, Bin
   January, Craig T.
   Ackerman, Michael J.
   Makielski, Jonathan C.
TI The common African American polymorphism SCN5A-S1103Y interacts with
   mutation SCN5A-R680H to increase late Na current
SO PHYSIOLOGICAL GENOMICS
LA English
DT Article
DE sudden death; ion channels; sodium current; genetics
ID SUDDEN-INFANT-DEATH; SPLICE VARIANT; CARDIAC-ARRHYTHMIA; CHANNEL
   VARIANTS; QT-SYNDROME; SCN5A; EXPRESSION; SUSCEPTIBILITY; PHENOTYPE;
   MECHANISM
AB Cheng J, Tester DJ, Tan BH, Valdivia CR, Kroboth S, Ye B, January CT, Ackerman MJ, Makielski JC. The common African American polymorphism SCN5A-S1103Y interacts with mutation SCN5A-R680H to increase late Na current. Physiol Genomics 43: 461-466, 2011. First published March 8, 2011; doi: 10.1152/physiolgenomics.00198.2010.-The common polymorphism SCN5A-S1103Y (similar to 13% allelic frequency in African Americans) is a risk factor for arrhythmia, sudden unexplained death (SUD), and sudden infant death syndrome. Prompted by a case of autopsy-negative SUD in a 23-year-old African American man who collapsed while playing football, we hypothesized that S1103Y interacted with other SCN5A variants to pathologically modify sodium current (I(Na)). Mutational analysis of arrhythmia-associated genes in the victim revealed the variants SCN5A-R680H and SCN5A-S1103Y. These variants were made both separately and in the same cDNA construct of the alternative splice variant backgrounds (SCN5A-Q1077del and Q1077) and expressed in HEK293 cells. In the most abundant SCN5A-Q1077del, late I(Na) for S1103Y alone was not significantly different from wild type (WT). However, late I(Na) for R680H, R680H+S1103Y (coexpressed), and R680H/S1103Y (on the same cDNA) was increased 2.1-, 3.4-, and 3.6-fold, respectively, compared with WT. Intracellular acidosis (pH 6.7) increased late I(Na) for S1103Y, R680H, R680H + S1103Y, and R680H/S1103Y by 2.2-, 2.4-, 5.0-, and 5.5-fold, respectively, compared with WT at pH 6.7. Expression in the less abundant SCN5A-Q1077 showed no increased late I(Na). This is the initial report of a functional interaction for the common polymorphism S1103Y with another mutation in the major transcript Q1077del of SCN5A. The "double hit" and environmental factor of acidosis may have converged to cause arrhythmic sudden death in this case.
C1 [Cheng, Jianding; Tan, Bi-Hua; Valdivia, Carmen R.; Kroboth, Stacie; Ye, Bin; January, Craig T.; Makielski, Jonathan C.] Univ Wisconsin, Dept Med, Div Cardiovasc Med, Madison, WI 53792 USA.
   [Tester, David J.; Ackerman, Michael J.] Mayo Clin, Dept Med, Rochester, MN USA.
   [Tester, David J.; Ackerman, Michael J.] Mayo Clin, Dept Pediat, Rochester, MN USA.
   [Tester, David J.; Ackerman, Michael J.] Mayo Clin, Dept Mol Pharmacol & Expt Therapeut, Rochester, MN USA.
C3 University of Wisconsin System; University of Wisconsin Madison; Mayo
   Clinic; Mayo Clinic; Mayo Clinic
RP Makielski, JC (corresponding author), Univ Wisconsin, Dept Med, Div Cardiovasc Med, 600 Highland Ave,H6-349, Madison, WI 53792 USA.
EM jcm@medicine.wisc.edu
OI Kroboth, Stacie/0000-0001-8767-4021; /0000-0003-1224-3088
FU University of Wisconsin; Mayo Clinic Windland Smith Rice Comprehensive
   Sudden Cardiac Death Program; American Heart Association; National
   Heart, Lung, and Blood Institute [HL-42569, HL-60723, HL-71092];
   National Natural Science Foundation of China [30973367]; Genaissance
   Pharmaceuticals (now PGxHealth); Mayo Medical Ventures (now Mayo Clinic
   Health Solutions)
FX This work was supported by the University of Wisconsin Cellular and
   Molecular Arrhythmia Research Program (J. C. Makielski), the Mayo Clinic
   Windland Smith Rice Comprehensive Sudden Cardiac Death Program (M. J.
   Ackerman), the established Investigator Award from the American Heart
   Association (to M. J. Ackerman), National Heart, Lung, and Blood
   Institute Grants HL-42569 (to M. J. Ackerman), HL-60723 (to C. T.
   January), and HL-71092 (to J. C. Makielski), and Grant 30973367 (to J.
   Cheng) from the National Natural Science Foundation of China.M. J.
   Ackerman is a consultant for PGxHealth and chairs their FAMILION
   Medical/Scientific Advisory Board (approved by Mayo Clinic's
   Medical-Industry Relations Office and Conflict of Interests Review
   Board). In addition, "cardiac channel gene screen" and "know-how
   relating to long QT genetic testing" license agreements, resulting in
   consideration and royalty payments, were established between Genaissance
   Pharmaceuticals (now PGxHealth) and Mayo Medical Ventures (now Mayo
   Clinic Health Solutions) in 2004. C. T. January is a cofounder of
   Cellular Dynamics International.
CR Ackerman MJ, 2004, HEART RHYTHM, V1, P600, DOI 10.1016/j.hrthm.2004.07.013
   Ackerman MJ, 2003, MAYO CLIN PROC, V78, P1479, DOI 10.4065/78.12.1479
   BENNETT PB, 1995, NATURE, V376, P683, DOI 10.1038/376683a0
   Benson DW, 2009, HEART RHYTHM, V6, P1176, DOI 10.1016/j.hrthm.2009.05.012
   Burke A, 2005, CIRCULATION, V112, P798, DOI 10.1161/CIRCULATIONAHA.104.482760
   Chen S, 2002, J MED GENET, V39, P913, DOI 10.1136/jmg.39.12.913
   Cheng JD, 2009, CIRC-ARRHYTHMIA ELEC, V2, P667, DOI 10.1161/CIRCEP.109.891440
   Chu PJ, 2004, J MOL CELL CARDIOL, V36, P423, DOI 10.1016/j.yjmcc.2003.12.012
   Gavillet B, 2006, CIRC RES, V99, P407, DOI 10.1161/01.RES.0000237466.13252.5e
   George CH, 2007, CIRC RES, V100, P874, DOI 10.1161/01.RES.0000260804.77807.cf
   Liao P, 2007, J BIOL CHEM, V282, P35133, DOI 10.1074/jbc.M705478200
   Makielski JC, 2003, CIRC RES, V93, P821, DOI 10.1161/01.RES.0000096652.14509.96
   Medeiros-Domingo A, 2009, HEART RHYTHM, V6, P1170, DOI 10.1016/j.hrthm.2009.04.034
   Nagatomo T, 2002, CARDIOVASC RES, V54, P624, DOI 10.1016/S0008-6363(02)00265-1
   Niu DM, 2006, J MED GENET, V43, P817, DOI 10.1136/jmg.2006.042192
   Plant LD, 2006, J CLIN INVEST, V116, P430, DOI 10.1172/JCI25618
   Poelzing S, 2006, CIRCULATION, V114, P368, DOI 10.1161/CIRCULATIONAHA.105.601294
   Splawski I, 2002, SCIENCE, V297, P1333, DOI 10.1126/science.1073569
   Tan BH, 2005, HEART RHYTHM, V2, P741, DOI 10.1016/j.hrthm.2005.04.021
   Tan BH, 2006, AM J PHYSIOL-HEART C, V291, pH1822, DOI 10.1152/ajpheart.00101.2006
   Van Norstrand DW, 2008, HEART RHYTHM, V5, P712, DOI 10.1016/j.hrthm.2008.02.012
   Wang DW, 2007, CIRCULATION, V115, P368, DOI 10.1161/CIRCULATIONAHA.106.646513
   Wang X, 2008, DEV DYNAM, V237, P2430, DOI 10.1002/dvdy.21671
   Ye B, 2003, PHYSIOL GENOMICS, V12, P187, DOI 10.1152/physiolgenomics.00117.2002
NR 24
TC 26
Z9 30
U1 0
U2 4
PU AMER PHYSIOLOGICAL SOC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA
SN 1094-8341
J9 PHYSIOL GENOMICS
JI Physiol. Genomics
PD MAY
PY 2011
VL 43
IS 9
BP 461
EP 466
DI 10.1152/physiolgenomics.00198.2010
PG 6
WC Cell Biology; Genetics & Heredity; Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Genetics & Heredity; Physiology
GA 763TC
UT WOS:000290581600001
PM 21385947
OA Green Published
DA 2025-04-10
ER

PT J
AU West, J
   Austin, E
   Fessel, JP
   Loyd, J
   Hamid, R
AF West, James
   Austin, Eric
   Fessel, Joshua P.
   Loyd, James
   Hamid, Rizwan
TI Rescuing the BMPR2 signaling axis in pulmonary arterial hypertension
SO DRUG DISCOVERY TODAY
LA English
DT Review
ID NONSENSE-MEDIATED DECAY; CONNECTIVITY MAP; POTENTIAL ROLE; II RECEPTOR;
   METABOLISM; EXPRESSION; GLUTAMINOLYSIS; PROLIFERATION; ATTENUATION;
   PENETRANCE
AB Pulmonary arterial hypertension (PAH) is a lethal disorder characterized by pulmonary arterial remodeling, increased right ventricular systolic pressure (RVSP), vasoconstriction and inflammation. The heritable form of PAH (HPAH) is usually (>80%) caused by mutations in the bone morphogenic protein receptor 2 (BMPR2) gene. Existing treatments for PAH typically focus on the end-stage sequelae of the disease, but do not address underlying mechanisms of vascular obstruction and blood flow and thus, in the long run, have limited effect because they treat the symptoms rather than the cause. Over the past decade, improved understanding of the molecular mechanisms behind the disease has enabled us to consider several novel therapeutic pathways. These include approaches directed toward BMPR2 gene expression, alternative splicing, downstream BMP signaling, metabolic pathways and the role of estrogens and estrogenic compounds in BMP signaling. It is likely that, ultimately, only one or two of these pathways will generate meaningful treatment options, however the potential benefits to PAH patients are still likely to be significant.
C1 [West, James; Fessel, Joshua P.; Loyd, James] Vanderbilt Univ, Med Ctr, Dept Med, Nashville, TN 37232 USA.
   [Austin, Eric; Hamid, Rizwan] Vanderbilt Univ, Med Ctr, Dept Pediat, Nashville, TN 37232 USA.
C3 Vanderbilt University; Vanderbilt University
RP West, J (corresponding author), Vanderbilt Univ, Med Ctr, Dept Med, Nashville, TN 37232 USA.
EM j.west@vanderbilt.edu; rizwan.hamid@vanderbilt.edu
RI Austin, Eric/A-6070-2013; West, James/E-2960-2010
OI Loyd, James/0000-0002-5042-7390; West, James/0000-0002-6004-0202;
   Fessel, Joshua/0000-0003-0797-7693
FU NIH [1R01HL102020]
FX Dr. Hamid's work was supported by NIH 1R01HL102020.
CR Archer SL, 2010, CIRCULATION, V121, P2661, DOI 10.1161/CIRCULATIONAHA.109.916098
   Austin ED, 2009, EUR RESPIR J, V34, P1093, DOI 10.1183/09031936.00010409
   Austin ED, 2012, CIRC-CARDIOVASC GENE, V5, P336, DOI 10.1161/CIRCGENETICS.111.961888
   Austin ED, 2012, BIOL SEX DIFFER, V3, DOI 10.1186/2042-6410-3-6
   Austin Eric D, 2011, Pulm Circ, V1, P389, DOI 10.4103/2045-8932.87308
   Badesch DB, 2010, CHEST, V137, P376, DOI 10.1378/chest.09-1140
   Burlando B, 2002, AM J PHYSIOL-CELL PH, V283, pC1461, DOI 10.1152/ajpcell.00429.2001
   Burton VJ, 2011, BLOOD, V118, P4750, DOI 10.1182/blood-2011-05-347393
   Burton VJ, 2011, BLOOD, V117, P333, DOI 10.1182/blood-2010-05-285973
   Chin KM, 2008, J AM COLL CARDIOL, V51, P1527, DOI 10.1016/j.jacc.2008.01.024
   Cogan J, 2012, CIRCULATION, V126, P1907, DOI 10.1161/CIRCULATIONAHA.112.106245
   Cogan JD, 2006, AM J RESP CRIT CARE, V174, P590, DOI 10.1164/rccm.200602-165OC
   DRESDALE DT, 1951, AM J MED, V11, P686, DOI 10.1016/0002-9343(51)90020-4
   Durrington HJ, 2010, J BIOL CHEM, V285, P37641, DOI 10.1074/jbc.M110.132415
   Ferreira AJ, 2009, AM J RESP CRIT CARE, V179, P1048, DOI 10.1164/rccm.200811-1678OC
   Fessel JP, 2013, PULM CIRC, V3, P564, DOI 10.1086/674312
   Fessel Joshua P, 2012, Pulm Circ, V2, P201, DOI 10.4103/2045-8932.97606
   Flynn C, 2012, AM J RESP CELL MOL, V47, P20, DOI 10.1165/rcmb.2011-0251OC
   Foletta VC, 2003, J CELL BIOL, V162, P1089, DOI 10.1083/jcb.200212060
   Germain M, 2013, NAT GENET, V45, P518, DOI 10.1038/ng.2581
   Hamid R, 2010, CLIN GENET, V77, P280, DOI 10.1111/j.1399-0004.2009.01311.x
   Hamid R, 2009, HUM MUTAT, V30, P649, DOI 10.1002/humu.20922
   Humbert M, 2006, AM J RESP CRIT CARE, V173, P1023, DOI 10.1164/rccm.200510-1668OC
   Johnson JA, 2012, AM J PHYSIOL-LUNG C, V302, pL474, DOI 10.1152/ajplung.00202.2011
   Lamb J, 2006, SCIENCE, V313, P1929, DOI 10.1126/science.1132939
   Lane Kirk L, 2011, Pulm Circ, V1, P72
   Larkin EK, 2012, AM J RESP CRIT CARE, V186, P892, DOI 10.1164/rccm.201205-0886OC
   Lim M, 2004, AM J RESP CELL MOL, V31, P351, DOI 10.1165/rcmb.2002-0086OC
   Ma L, 2013, NEW ENGL J MED, V369, P351, DOI 10.1056/NEJMoa1211097
   Machado RD, 2003, HUM MOL GENET, V12, P3277, DOI 10.1093/hmg/ddg365
   Machado RD, 2001, AM J HUM GENET, V68, P92, DOI 10.1086/316947
   Perez VADJ, 2009, J CELL BIOL, V184, P83, DOI 10.1083/jcb.200806049
   Piao L, 2013, J MOL MED, V91, P333, DOI 10.1007/s00109-012-0982-0
   Plymate SR, 2003, ONCOGENE, V22, P1024, DOI 10.1038/sj.onc.1206210
   Pugh ME, 2013, DIABETES CARE, V36, pE32, DOI 10.2337/dc12-1650
   Pugh ME, 2011, J HEART LUNG TRANSPL, V30, P904, DOI 10.1016/j.healun.2011.02.016
   Roberts KE, 2009, AM J RESP CRIT CARE, V179, P835, DOI 10.1164/rccm.200809-1472OC
   ROSENZWEIG BL, 1995, P NATL ACAD SCI USA, V92, P7632, DOI 10.1073/pnas.92.17.7632
   Spiekerkoetter E, 2013, J CLIN INVEST, V123, P3600, DOI 10.1172/JCI65592
   Takahashi M, 2008, J ENDOCRINOL, V199, P445, DOI 10.1677/JOE-08-0226
   Tuder RM, 2012, AM J RESP CRIT CARE, V185, P260, DOI 10.1164/rccm.201108-1536PP
   Umar S, 2012, AM J RESP CRIT CARE, V186, P125, DOI 10.1164/rccm.201201-0058PP
   West J, 2008, AM J PHYSIOL-LUNG C, V295, pL744, DOI 10.1152/ajplung.90255.2008
   West J, 2013, EUR RESPIR J, V41, P861, DOI 10.1183/09031936.00030312
   Whittle AJ, 2012, CELL, V149, P871, DOI 10.1016/j.cell.2012.02.066
   Wise DR, 2008, P NATL ACAD SCI USA, V105, P18782, DOI 10.1073/pnas.0810199105
NR 46
TC 21
Z9 25
U1 0
U2 8
PU ELSEVIER SCI LTD
PI OXFORD
PA THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND
SN 1359-6446
EI 1878-5832
J9 DRUG DISCOV TODAY
JI Drug Discov. Today
PD AUG
PY 2014
VL 19
IS 8
BP 1241
EP 1245
DI 10.1016/j.drudis.2014.04.015
PG 5
WC Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Pharmacology & Pharmacy
GA AO4VM
UT WOS:000341339500032
PM 24794464
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Müller, JG
   Isomatsu, Y
   Koushik, SV
   O'Quinn, M
   Xu, L
   Kappler, CS
   Hapke, E
   Zile, MR
   Conway, SJ
   Menick, DR
AF Müller, JG
   Isomatsu, Y
   Koushik, SV
   O'Quinn, M
   Xu, L
   Kappler, CS
   Hapke, E
   Zile, MR
   Conway, SJ
   Menick, DR
TI Cardiac-specific expression and hypertrophic upregulation of the feline
   Na<SUP>+</SUP>-Ca<SUP>2+</SUP> exchanger gene H1-promoter in a
   transgenic mouse model
SO CIRCULATION RESEARCH
LA English
DT Article
DE Na+-Ca2+ exchanger; pressure-overload hypertrophy; transgenic mice
ID SODIUM-CALCIUM EXCHANGER; HUMAN VENTRICULAR MYOCYTES; FAILING HUMAN
   HEART; NA-CA EXCHANGE; SARCOPLASMIC-RETICULUM; NA+/CA2+ EXCHANGER; HUMAN
   MYOCARDIUM; NCX1; CONTRACTION; RELAXATION
AB The NCX1 gene contains three promoters (H1, K1, and Br1), and as a result of alternative promoter usage and alternative splicing, there are multiple tissue-specific variants of the Na+-Ca2+ exchanger. We have proposed that for NCX1, the H1 promoter regulates expression in the heart, the K1 promoter regulates expression in the kidney, and the Br1 promoter regulates expression in the brain as well as low-level ubiquitous expression. Here, using a transgenic mouse model, we test the role of the DNA region including -1831 to 67 by of intron 1, encompassing exon H1 of the feline NCX1 gene (NCX1H1). The NCX1H1 promoter was sufficient for driving the normal spatiotemporal pattern of NCX1 expression in cardiac development. The luciferase reporter gene was expressed in a heart-restricted pattern both in early embryos (embryonic days 8 to 14) and in later embryos (after embryonic day 14), when NCX1 is also expressed in other tissues. In the adult, no luciferase activity was detected in the kidney, liver, spleen, uterus, or skeletal muscle; minimal activity was detected in the brain; and very high levels of luciferase expression were detected in the heart. Transverse aortic constriction-operated mice showed significantly increased left ventricular mass after 7 days. In addition, there was a 2-fold upregulation of NCX1H1 promoter activity in the left ventricle in animals after 7 days of pressure overload compared with both control and sham-operated animals. This work demonstrates that the NCX1H1 promoter directs cardiac-specific expression of the exchanger in both the embryo and adult and is also sufficient for the upregulation of NCX1 in response to pressure overload.
C1 Med Univ S Carolina, Gazes Cardiac Res Inst, Charleston, SC 29425 USA.
   Med Univ S Carolina, Div Cardiol, Charleston, SC 29425 USA.
   Ralph H Johnson Dept Vet Affairs, Charleston, SC USA.
   Med Coll Georgia, Inst Mol Med & Genet, Augusta, GA 30912 USA.
C3 Medical University of South Carolina; Medical University of South
   Carolina; US Department of Veterans Affairs; Veterans Health
   Administration (VHA); Ralph H Johnson VA Medical Center; University
   System of Georgia; Augusta University
RP Menick, DR (corresponding author), Med Univ S Carolina, Gazes Cardiac Res Inst, 114 Doughty St,Room 203,POB 250773, Charleston, SC 29425 USA.
OI Zile, Michael/0000-0001-7076-221X
FU NHLBI NIH HHS [HL-60104, P01 HL048788, R01 HL066223, HL-60714, HL-48788]
   Funding Source: Medline
CR Barnes KV, 1997, J BIOL CHEM, V272, P11510, DOI 10.1074/jbc.272.17.11550
   BERS DM, 1990, AM J PHYSIOL, V258, pC944, DOI 10.1152/ajpcell.1990.258.5.C944
   BERS DM, 1989, CIRC RES, V65, P334, DOI 10.1161/01.RES.65.2.334
   Bersohn MM, 1996, ANN NY ACAD SCI, V779, P534, DOI 10.1111/j.1749-6632.1996.tb44830.x
   Cheng GM, 1999, J BIOL CHEM, V274, P12819, DOI 10.1074/jbc.274.18.12819
   CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
   CONWAY SJ, 1996, METH MOLEC MED, P193
   Dipla K, 1999, CIRC RES, V84, P435, DOI 10.1161/01.RES.84.4.435
   Gaughan JP, 1999, AM J PHYSIOL-HEART C, V277, pH714, DOI 10.1152/ajpheart.1999.277.2.H714
   Hamawaki M, 1998, AM J PHYSIOL-HEART C, V274, pH868, DOI 10.1152/ajpheart.1998.274.3.H868
   HASENFUSS G, 1994, CIRC RES, V75, P434, DOI 10.1161/01.RES.75.3.434
   Hasenfuss G, 1999, CIRCULATION, V99, P641, DOI 10.1161/01.CIR.99.5.641
   Hasenfuss G, 1997, BASIC RES CARDIOL, V92, P87, DOI 10.1007/BF00794072
   Hasenfuss G., 1996, CIRCULATION S1, V94, P1
   Houser SR, 2000, J MOL CELL CARDIOL, V32, P1595, DOI 10.1006/jmcc.2000.1206
   KENT RL, 1993, AM J PHYSIOL, V265, pH1024, DOI 10.1152/ajpheart.1993.265.3.H1024
   KOFUJI P, 1993, AM J PHYSIOL, V265, pF598, DOI 10.1152/ajprenal.1993.265.4.F598
   Koushik SV, 1999, MECH DEVELOP, V88, P119, DOI 10.1016/S0925-4773(99)00177-X
   Koushik SV, 2001, FASEB J, V15, P1209, DOI 10.1096/fj.00-0696fje
   Kraev A, 1996, GENOMICS, V37, P105, DOI 10.1006/geno.1996.0526
   LEBLANC N, 1990, SCIENCE, V248, P372, DOI 10.1126/science.2158146
   LEE SL, 1994, J BIOL CHEM, V269, P14849
   Li XF, 1999, J BIOL CHEM, V274, P8153, DOI 10.1074/jbc.274.12.8153
   Mattiello JA, 1998, CARDIOVASC RES, V37, P424, DOI 10.1016/S0008-6363(97)00271-X
   Menick D R, 1996, J Card Fail, V2, pS69, DOI 10.1016/S1071-9164(96)80061-3
   Menick DR, 1996, ANN NY ACAD SCI, V779, P489, DOI 10.1111/j.1749-6632.1996.tb44823.x
   Nicholas SB, 1999, AM J PHYSIOL-HEART C, V277, pH324, DOI 10.1152/ajpheart.1999.277.1.H324
   Nicholas SB, 1998, AM J PHYSIOL-HEART C, V274, pH217, DOI 10.1152/ajpheart.1998.274.1.H217
   Pogwizd SM, 1999, CIRC RES, V85, P1009
   PORZIG H, 1993, AM J PHYSIOL, V265, pC748, DOI 10.1152/ajpcell.1993.265.3.C748
   Quednau BD, 1997, AM J PHYSIOL-CELL PH, V272, pC1250, DOI 10.1152/ajpcell.1997.272.4.C1250
   ROCKMAN HA, 1991, P NATL ACAD SCI USA, V88, P8277, DOI 10.1073/pnas.88.18.8277
   Scheller T, 1998, J BIOL CHEM, V273, P7643, DOI 10.1074/jbc.273.13.7643
   Schlotthauer K, 2000, CIRC RES, V87, P774, DOI 10.1161/01.RES.87.9.774
   Studer R, 1997, BASIC RES CARDIOL, V92, P53, DOI 10.1007/BF00794068
   STUDER R, 1994, CIRC RES, V75, P443, DOI 10.1161/01.RES.75.3.443
   Wang ZY, 2001, J BIOL CHEM, V276, P17706, DOI 10.1074/jbc.M100544200
NR 37
TC 31
Z9 33
U1 0
U2 1
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA 530 WALNUT ST, PHILADELPHIA, PA 19106-3621 USA
SN 0009-7330
J9 CIRC RES
JI Circ.Res.
PD FEB 8
PY 2002
VL 90
IS 2
BP 158
EP 164
DI 10.1161/hh0202.103231
PG 7
WC Cardiac & Cardiovascular Systems; Hematology; Peripheral Vascular
   Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology; Hematology
GA 521CT
UT WOS:000173821800010
PM 11834708
OA Bronze
DA 2025-04-10
ER

PT J
AU Treves, S
   Feriotto, G
   Moccagatta, L
   Gambari, R
   Zorzato, F
AF Treves, S
   Feriotto, G
   Moccagatta, L
   Gambari, R
   Zorzato, F
TI Molecular cloning, expression, functional characterization, chromosomal
   localization, and gene structure of junctate, a novel integral calcium
   binding protein of sarco(endo)plasmic reticulum membrane
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID JUNCTIONAL SARCOPLASMIC-RETICULUM; RABBIT SKELETAL-MUSCLE; CA-2+ RELEASE
   CHANNEL; RYANODINE RECEPTOR; DIHYDROPYRIDINE RECEPTOR; MALIGNANT
   HYPERTHERMIA; TERMINAL CISTERNAE; CA2+ RELEASE; CALSEQUESTRIN;
   OVEREXPRESSION
AB Screening a cDNA library from human skeletal muscle and cardiac muscle with a cDNA probe derived from junctin led to the isolation of two groups of cDNA clones, The first group displayed a deduced amino acid sequence that is 84% identical to that of dog heart junctin, whereas the second group had a single open reading frame that encoded a polypeptide with a predicted mass of 33 kDa, whose first 78 NH2-terminal residues are identical to junctin whereas its COOH terminus domain is identical to aspartyl beta -hydroxylase, a member of the alpha -ketoglutarate-dependent dioxygenase family. We named the latter amino acid sequence junctate, Northern blot analysis indicates that junctate is expressed in a variety of human tissues including heart, pancreas, brain, lung, liver, kidney, and skeletal muscle, Fluorescence in situ hybridization analysis revealed that the genetic loci of junctin and junctate map to the same cytogenetic band oh human chromosome 8, Analysis of intron/exon boundaries of the genomic BAC clones demonstrate that junctin, junctate, and aspartyl beta -hydroxylase result from alternative splicing of the same gene.
   The predicted lumenal portion of junctate is enriched in negatively charged residues and is able to bind calcium. Scatchard analysis of equilibrium Ca-45(2+) binding in the presence of a physiological concentration of KCl demonstrate that junctate binds 21.0 mol of Ca2+/mol protein with a k(D) of 217 +/- 20 muM (n = 5), Tagging recombinant junctate with green fluorescent protein and expressing the chimeric polypeptide in COS-7-transfected cells indicates that junctate is located in endoplasmic reticulum membranes and that its presence increases the peak amplitude and transient calcium released by activation of surface membrane receptors coupled to InsP(3) receptor activation.
   Our study shows that alternative splicing of the same gene generates the following functionally distinct proteins: an enzyme (aspartyl beta -hydroxylase), a structural protein of SR (junctin), and a membrane-bound calcium binding protein (junctate).
C1 Univ Ferrara, Dept Expt & Diagnost Med, Sect Gen Pathol, I-44100 Ferrara, Italy.
   Kantonsspital, Dept Anaesthesia, CH-4031 Basel, Switzerland.
   Kantonsspital, Dept Res, CH-4031 Basel, Switzerland.
   Univ Ferrara, Ctr Biotechnol, I-44100 Ferrara, Italy.
   Univ Ferrara, Dept Biochem & Mol Biol, I-44100 Ferrara, Italy.
C3 University of Ferrara; University of Basel; Kantonsspital Aarau AG
   (KSA); Kantonsspital Aarau AG (KSA); University of Basel; University of
   Ferrara; University of Ferrara
RP Univ Ferrara, Dept Expt & Diagnost Med, Sect Gen Pathol, Via Borsari 46, I-44100 Ferrara, Italy.
EM zor@dns.unife.it
RI Gambari, Roberto/F-9555-2015
OI Gambari, Roberto/0000-0001-9205-6033; Treves, Susan/0000-0002-0007-9631
FU Telethon [908] Funding Source: Medline
CR ANDERSON K, 1995, J GEN PHYSIOL, V105, P363, DOI 10.1085/jgp.105.3.363
   BLOCK BA, 1988, J CELL BIOL, V107, P2587, DOI 10.1083/jcb.107.6.2587
   CASWELL AH, 1991, BIOCHEMISTRY-US, V30, P7507, DOI 10.1021/bi00244a020
   CASWELL AH, 1985, J BIOL CHEM, V260, P6892
   Celio MR., 1996, GUIDEBOOK CALCIUM BI
   Censier K, 1998, J CLIN INVEST, V101, P1233, DOI 10.1172/JCI993
   CHU A, 1990, MOL PHARMACOL, V37, P735
   COSTELLO B, 1986, J CELL BIOL, V103, P741, DOI 10.1083/jcb.103.3.741
   Damiani E, 1997, CELL CALCIUM, V22, P129, DOI 10.1016/S0143-4160(97)90113-5
   FLEISCHER S, 1989, ANNU REV BIOPHYS BIO, V18, P333, DOI 10.1146/annurev.bb.18.060189.002001
   FRANZINIARMSTRONG C, 1987, J CELL BIOL, V105, P49, DOI 10.1083/jcb.105.1.49
   FRANZINIARMSTRONG C, 1994, ANNU REV PHYSIOL, V56, P509, DOI 10.1146/annurev.ph.56.030194.002453
   GIROTTI M, 1992, BIOCHEM J, V281, P203, DOI 10.1042/bj2810203
   Goetz J, 1996, J BIOL CHEM, V271, P29589, DOI 10.1074/jbc.271.47.29589
   Grässel S, 1999, EUR J BIOCHEM, V263, P471, DOI 10.1046/j.1432-1327.1999.00523.x
   GUO W, 1995, J BIOL CHEM, V270, P9027, DOI 10.1074/jbc.270.16.9027
   GUO W, 1994, J BIOL CHEM, V269, P28359
   IKEMOTO N, 1989, BIOCHEMISTRY-US, V28, P6764, DOI 10.1021/bi00442a033
   IMAGAWA T, 1987, J BIOL CHEM, V262, P16636
   INUI M, 1987, J BIOL CHEM, V262, P1740
   Jones LR, 1998, J CLIN INVEST, V101, P1385, DOI 10.1172/JCI1362
   Jones LR, 1995, J BIOL CHEM, V270, P30787, DOI 10.1074/jbc.270.51.30787
   KAWASAKI T, 1994, BIOCHEM BIOPH RES CO, V199, P1120, DOI 10.1006/bbrc.1994.1347
   KIM DH, 1988, BIOCHIM BIOPHYS ACTA, V945, P246, DOI 10.1016/0005-2736(88)90486-5
   KIM KC, 1990, BIOCHEMISTRY-US, V29, P9281, DOI 10.1021/bi00491a025
   Korenberg JR, 1999, GENOME RES, V9, P994, DOI 10.1101/gr.9.10.994
   KORIOTH F, 1994, GENE, V150, P395, DOI 10.1016/0378-1119(94)90460-X
   LAEMMLI UK, 1970, NATURE, V227, P680, DOI 10.1038/227680a0
   LAI FA, 1988, NATURE, V331, P315, DOI 10.1038/331315a0
   LAMB GD, 1986, J PHYSIOL-LONDON, V376, P85, DOI 10.1113/jphysiol.1986.sp016143
   Lavaissiere L, 1996, J CLIN INVEST, V98, P1313, DOI 10.1172/JCI118918
   LIU GH, 1994, J BIOL CHEM, V269, P33028
   LOWRY OH, 1951, J BIOL CHEM, V193, P265
   MACLENNAN DH, 1992, SCIENCE, V256, P789, DOI 10.1126/science.1589759
   MacLennan DH, 1998, NAT STRUCT BIOL, V5, P409, DOI 10.1038/nsb0698-409
   MACLENNAN DH, 1971, P NATL ACAD SCI USA, V68, P1231, DOI 10.1073/pnas.68.6.1231
   MARTY I, 1994, P NATL ACAD SCI USA, V91, P2270, DOI 10.1073/pnas.91.6.2270
   MARUYAMA K, 1984, J BIOCHEM, V95, P511, DOI 10.1093/oxfordjournals.jbchem.a134633
   MELZER W, 1995, BBA-REV BIOMEMBRANES, V1241, P59, DOI 10.1016/0304-4157(94)00014-5
   MENEGAZZI P, 1994, BIOCHEMISTRY-US, V33, P9078, DOI 10.1021/bi00197a008
   Mery L, 1996, J BIOL CHEM, V271, P9332, DOI 10.1074/jbc.271.16.9332
   Mickelson JR, 1996, PHYSIOL REV, V76, P537, DOI 10.1152/physrev.1996.76.2.537
   MIKOSHIBA K, 1993, TRENDS PHARMACOL SCI, V14, P86, DOI 10.1016/0165-6147(93)90069-V
   Murray BE, 1997, BIOCHEM J, V324, P689, DOI 10.1042/bj3240689
   PESSAH IN, 1986, J BIOL CHEM, V261, P8643
   PESSAH IN, 1990, MOL PHARMACOL, V37, P503
   Pinton P, 1998, BIOFACTORS, V8, P243, DOI 10.1002/biof.5520080312
   RIOS E, 1991, PHYSIOL REV, V71, P849, DOI 10.1152/physrev.1991.71.3.849
   SAITO A, 1984, J CELL BIOL, V99, P875, DOI 10.1083/jcb.99.3.875
   SLUPSKY JR, 1987, BIOCHEMISTRY-US, V26, P6539, DOI 10.1021/bi00394a038
   TANABE T, 1988, NATURE, V336, P134, DOI 10.1038/336134a0
   TREVES S, 1990, BIOCHEM J, V271, P473, DOI 10.1042/bj2710473
   Zhang L, 1997, J BIOL CHEM, V272, P23389, DOI 10.1074/jbc.272.37.23389
   ZORZATO F, 1990, J BIOL CHEM, V265, P2244
NR 54
TC 77
Z9 89
U1 0
U2 5
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
SN 0021-9258
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD DEC 15
PY 2000
VL 275
IS 50
BP 39555
EP 39568
DI 10.1074/jbc.M005473200
PG 14
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 384PB
UT WOS:000165953100082
PM 11007777
OA Green Published, hybrid
DA 2025-04-10
ER

PT J
AU Shiojima, I
   Komuro, I
   Mizuno, T
   Aikawa, R
   Akazawa, H
   Oka, T
   Yamazaki, T
   Yazaki, Y
AF Shiojima, I
   Komuro, I
   Mizuno, T
   Aikawa, R
   Akazawa, H
   Oka, T
   Yamazaki, T
   Yazaki, Y
TI Molecular cloning and characterization of human cardiac homeobox gene
   CSX1
SO CIRCULATION RESEARCH
LA English
DT Article
DE cardiac development; cardiac-specific gene expression; transcription
   factor; alternative splicing; evolution
ID DNA-BINDING SPECIFICITY; TRANSCRIPTION FACTOR; HOMEODOMAIN PROTEIN;
   DROSOPHILA EMBRYOS; MURINE; HEART; EXPRESSION; FAMILY; TINMAN; MESODERM
AB Accumulating evidence has suggested that homeodomain-containing proteins play critical roles in regulating the tissue-specific gene expression essential for tissue differentiation and in determining the temporal and spatial patterns of development. In order to elucidate the mechanisms of human heart development. we have isolated a human homologue of the murine cardiac homeobox gene Csx (also called Nkx-2.5) and denoted it as CSX1. The amino acid sequence of the CSX1 homeodomain is 100% and 67% identical to that of murine Csx/Nkx-2.5 and Drosophila tinman, respectively. CSX1 has at least three isoforms generated by an alternative splicing mechanism. One of these isoforms (CSX1a) encodes a protein of approximate to 35 kD that possesses the homeodomain, whereas the other two (CSX1b and CSX1c) encode a truncated protein of approximate to 12 kD that is identical to the CSX1a protein at the amino-terminal 112 amino acids but lacks the homeodomain. Northern blot analysis showed that CSX1 transcripts are abundantly expressed in both fetal and adult hearts, but no signal was detected in other human tissues examined. Amplification of each isoform by reverse transcriptase-polymerase chain reaction I revealed that all of the three isoforms are expressed in fetal and adult hearts and that the homeobox-containing isoform CSX1a is most abundant. The homeodomain-containing protein encoded by CSX1a binds to Csx/Nkx-2.5 binding sequences and transactivates the sequence-containing luciferase reporter gene. Unexpectedly, the homeodomain-lacking protein encoded by CSX1b also transactivates the reporter gene, although CSX1b does not bind to the Csx/Nkx-2.5 binding sequences. The highly conserved homeodomain sequences in evolution and the restricted expression in the heart suggest that CSX1 plays an important role in the development and differentiation of the human heart and that there may be two different mechanisms in transcriptional regulation by the CSX1 protein, homeodomain-dependent and -independent mechanisms.
C1 UNIV TOKYO,SCH MED,DEPT MED 3,BUNKYO KU,TOKYO 113,JAPAN.
C3 University of Tokyo
RI Komuro, Issei/JXL-2876-2024; Akazawa, Hiroshi/AFN-9677-2022
CR ACAMPORA D, 1989, NUCLEIC ACIDS RES, V17, P10385, DOI 10.1093/nar/17.24.10385
   ANANTHAN J, 1993, MOL CELL BIOL, V13, P1599, DOI 10.1128/MCB.13.3.1599
   AZPIAZU N, 1993, GENE DEV, V7, P1325, DOI 10.1101/gad.7.7b.1325
   BERLETH T, 1988, EMBO J, V7, P1749, DOI 10.1002/j.1460-2075.1988.tb03004.x
   BODMER R, 1990, DEVELOPMENT, V110, P661
   BODMER R, 1993, DEVELOPMENT, V118, P719
   BODMER R, 1995, TRENDS CARDIOVAS MED, V5, P21, DOI 10.1016/1050-1738(94)00032-Q
   CASTRILLO JL, 1991, SCIENCE, V253, P197, DOI 10.1126/science.1677216
   CHAN SK, 1994, CELL, V78, P603, DOI 10.1016/0092-8674(94)90525-8
   CHEN C, 1987, MOL CELL BIOL, V7, P2745, DOI 10.1128/MCB.7.8.2745
   CHEN CY, 1995, J BIOL CHEM, V270, P15628, DOI 10.1074/jbc.270.26.15628
   CHISAKA O, 1991, NATURE, V350, P473, DOI 10.1038/350473a0
   CIVITAREALE D, 1989, EMBO J, V8, P2537, DOI 10.1002/j.1460-2075.1989.tb08391.x
   CONDIE BG, 1990, MOL CELL BIOL, V10, P3376, DOI 10.1128/MCB.10.7.3376
   Copeland JWR, 1996, NATURE, V379, P162, DOI 10.1038/379162a0
   DUBOULE D, 1989, EMBO J, V8, P1497, DOI 10.1002/j.1460-2075.1989.tb03534.x
   EDMONDSON DG, 1994, DEVELOPMENT, V120, P1251
   EVANS SM, 1995, DEVELOPMENT, V121, P3889
   GEHRING WJ, 1994, CELL, V78, P211, DOI 10.1016/0092-8674(94)90292-5
   GRAHAM A, 1989, CELL, V57, P367, DOI 10.1016/0092-8674(89)90912-4
   GUAZZI S, 1990, EMBO J, V9, P3631, DOI 10.1002/j.1460-2075.1990.tb07574.x
   HAYASHI S, 1990, CELL, V63, P883, DOI 10.1016/0092-8674(90)90492-W
   HEIKINHEIMO M, 1994, DEV BIOL, V164, P361, DOI 10.1006/dbio.1994.1206
   INGRAHAM HA, 1988, CELL, V55, P519, DOI 10.1016/0092-8674(88)90038-4
   KIM YS, 1989, P NATL ACAD SCI USA, V86, P7716, DOI 10.1073/pnas.86.20.7716
   KOMURO I, 1993, P NATL ACAD SCI USA, V90, P8145, DOI 10.1073/pnas.90.17.8145
   KOMURO I, 1993, EMBO J, V12, P1387, DOI 10.1002/j.1460-2075.1993.tb05783.x
   KOZAK M, 1987, NUCLEIC ACIDS RES, V15, P8125, DOI 10.1093/nar/15.20.8125
   KRUMLAUF R, 1994, CELL, V78, P191, DOI 10.1016/0092-8674(94)90290-9
   KUMAR D, 1987, J MED GENET, V24, P180, DOI 10.1136/jmg.24.3.180
   KUROO M, 1995, CIRC RES, V76, P148, DOI 10.1161/01.RES.76.1.148
   LAROSA GJ, 1988, MOL CELL BIOL, V8, P3906, DOI 10.1128/MCB.8.9.3906
   LAWRENCE PA, 1994, CELL, V78, P181, DOI 10.1016/0092-8674(94)90289-5
   LAZZARO D, 1991, DEVELOPMENT, V113, P1093
   LINTS TJ, 1993, DEVELOPMENT, V119, P419
   LUFKIN T, 1991, CELL, V66, P1105, DOI 10.1016/0092-8674(91)90034-V
   LYONS I, 1995, GENE DEV, V9, P1654, DOI 10.1101/gad.9.13.1654
   MALICKI J, 1990, CELL, V63, P961, DOI 10.1016/0092-8674(90)90499-5
   MCGINNIS N, 1990, CELL, V63, P969, DOI 10.1016/0092-8674(90)90500-E
   Molkentin JD, 1995, CELL, V83, P1125, DOI 10.1016/0092-8674(95)90139-6
   NORDEEN SK, 1988, BIOTECHNIQUES, V6, P454
   OLSON EN, 1993, CIRC RES, V72, P1, DOI 10.1161/01.RES.72.1.1
   PRICE M, 1992, NEURON, V8, P241, DOI 10.1016/0896-6273(92)90291-K
   PROUDFOOT N, 1991, CELL, V64, P671, DOI 10.1016/0092-8674(91)90495-K
   SCOTT MP, 1989, BIOCHIM BIOPHYS ACTA, V989, P25, DOI 10.1016/0304-419X(89)90033-4
   SHAW G, 1986, CELL, V46, P659, DOI 10.1016/0092-8674(86)90341-7
   SHIOJIMA I, 1995, GENOMICS, V27, P204, DOI 10.1006/geno.1995.1027
   TONISSEN KF, 1994, DEV BIOL, V162, P325, DOI 10.1006/dbio.1994.1089
   VANDIJK MA, 1994, CELL, V78, P617, DOI 10.1016/0092-8674(94)90526-6
   WEINTRAUB H, 1991, SCIENCE, V251, P761, DOI 10.1126/science.1846704
   WRIGHT CVE, 1987, EMBO J, V6, P4083, DOI 10.1002/j.1460-2075.1987.tb02754.x
NR 51
TC 67
Z9 72
U1 1
U2 2
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA 530 WALNUT ST, PHILADELPHIA, PA 19106-3621 USA
SN 0009-7330
J9 CIRC RES
JI Circ.Res.
PD NOV
PY 1996
VL 79
IS 5
BP 920
EP 929
DI 10.1161/01.RES.79.5.920
PG 10
WC Cardiac & Cardiovascular Systems; Hematology; Peripheral Vascular
   Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology; Hematology
GA VP030
UT WOS:A1996VP03000002
PM 8888684
DA 2025-04-10
ER

PT J
AU Caruso, P
   Dunmore, BJ
   Schlosser, K
   Schoors, S
   Dos Santos, C
   Perez-Iratxeta, C
   Lavoie, JR
   Zhang, H
   Long, L
   Flockton, AR
   Frid, MG
   Upton, PD
   D'Alessandro, A
   Hadinnapola, C
   Kiskin, FN
   Taha, M
   Hurst, LA
   Ormiston, ML
   Hata, A
   Stenmark, KR
   Carmeliet, P
   Stewart, DJ
   Morrell, NW
AF Caruso, Paola
   Dunmore, Benjamin J.
   Schlosser, Kenny
   Schoors, Sandra
   Dos Santos, Claudia
   Perez-Iratxeta, Carol
   Lavoie, Jessie R.
   Zhang, Hui
   Long, Lu
   Flockton, Amanda R.
   Frid, Maria G.
   Upton, Paul D.
   D'Alessandro, Angelo
   Hadinnapola, Charaka
   Kiskin, Fedir N.
   Taha, Mohamad
   Hurst, Liam A.
   Ormiston, Mark L.
   Hata, Akiko
   Stenmark, Kurt R.
   Carmeliet, Peter
   Stewart, Duncan J.
   Morrell, Nicholas W.
TI Identification of MicroRNA-124 as a Major Regulator of Enhanced
   Endothelial Cell Glycolysis in Pulmonary Arterial Hypertension via PTBP1
   (Polypyrimidine Tract Binding Protein) and Pyruvate Kinase M2
SO CIRCULATION
LA English
DT Article
DE endothelial cells; endothelial progenitor cells; glycolysis;
   hypertension pulmonary; metabolism; microRNAs
ID TUMOR; EXPRESSION; COACTIVATOR; INHIBITION; METABOLISM; APOPTOSIS;
   MIR-124; GROWTH
AB BACKGROUND: Pulmonary arterial hypertension (PAH) is characterized by abnormal growth and enhanced glycolysis of pulmonary artery endothelial cells. However, the mechanisms underlying alterations in energy production have not been identified.
   METHODS: Here, we examined the miRNA and proteomic profiles of blood outgrowth endothelial cells (BOECs) from patients with heritable PAH caused by mutations in the bone morphogenetic protein receptor type 2 (BMPR2) gene and patients with idiopathic PAH to determine mechanisms underlying abnormal endothelial glycolysis. We hypothesized that in BOECs from patients with PAH, the downregulation of microRNA-124 (miR-124), determined with a tiered systems biology approach, is responsible for increased expression of the splicing factor PTBP1 (polypyrimidine tract binding protein), resulting in alternative splicing of pyruvate kinase muscle isoforms 1 and 2 (PKM1 and 2) and consequently increased PKM2 expression. We questioned whether this alternative regulation plays a critical role in the hyperglycolytic phenotype of PAH endothelial cells.
   RESULTS: Heritable PAH and idiopathic PAH BOECs recapitulated the metabolic abnormalities observed in pulmonary artery endothelial cells from patients with idiopathic PAH, confirming a switch from oxidative phosphorylation to aerobic glycolysis. Overexpression of miR-124 or siRNA silencing of PTPB1 restored normal proliferation and glycolysis in heritable PAH BOECs, corrected the dysregulation of glycolytic genes and lactate production, and partially restored mitochondrial respiration. BMPR2 knockdown in control BOECs reduced the expression of miR-124, increased PTPB1, and enhanced glycolysis. Moreover, we observed reduced miR-124, increased PTPB1 and PKM2 expression, and significant dysregulation of glycolytic genes in the rat SUGEN-hypoxia model of severe PAH, characterized by reduced BMPR2 expression and endothelial hyperproliferation, supporting the relevance of this mechanism in vivo.
   CONCLUSIONS: Pulmonary vascular and circulating progenitor endothelial cells isolated from patients with PAH demonstrate downregulation of miR124, leading to the metabolic and proliferative abnormalities in PAH ECs via PTPB1 and PKM1/PKM2. Therefore, the manipulation of this miRNA or its targets could represent a novel therapeutic approach for the treatment of PAH.
C1 [Caruso, Paola; Dunmore, Benjamin J.; Long, Lu; Upton, Paul D.; Hadinnapola, Charaka; Kiskin, Fedir N.; Hurst, Liam A.; Morrell, Nicholas W.] Univ Cambridge, Div Resp Med, Dept Med, Sch Clin Med,Addenbrookes Hosp, Cambridge, England.
   [Schlosser, Kenny; Perez-Iratxeta, Carol; Lavoie, Jessie R.; Taha, Mohamad; Stewart, Duncan J.] Ottawa Hosp, Res Inst, Ottawa, ON, Canada.
   [Schlosser, Kenny; Perez-Iratxeta, Carol; Lavoie, Jessie R.; Taha, Mohamad; Stewart, Duncan J.] Univ Ottawa, Ottawa, ON, Canada.
   [Schoors, Sandra; Carmeliet, Peter] VIB, Lab Angiogenesis & Neurovasc Link, Vesalius Res Ctr, Leuven, Belgium.
   [Schoors, Sandra; Carmeliet, Peter] Univ Leuven, Lab Angiogenesis & Neurovasc Link, Vesalius Res Ctr, Dept Oncol, Leuven, Belgium.
   [Dos Santos, Claudia; Ormiston, Mark L.] Queens Univ, Dept Biomed & Mol Sci, Kingston, ON, Canada.
   [Zhang, Hui; Flockton, Amanda R.; Frid, Maria G.; Stenmark, Kurt R.] Univ Colorado, Cardiovasc Pulm Res Labs, Dept Pediat, Anschutz Med Campus, Aurora, CO USA.
   [Zhang, Hui; Flockton, Amanda R.; Frid, Maria G.; Stenmark, Kurt R.] Univ Colorado, Cardiovasc Pulm Res Labs, Dept Med, Anschutz Med Campus, Aurora, CO USA.
   [D'Alessandro, Angelo] Univ Colorado, Dept Biochem & Mol Genet, Anschutz Med Campus, Aurora, CO USA.
   [Hata, Akiko] Univ Calif San Francisco, Cardiovasc Res Inst, San Francisco, CA 94143 USA.
C3 Cambridge University Hospitals NHS Foundation Trust; Addenbrooke's
   Hospital; University of Cambridge; University of Ottawa; Ottawa Hospital
   Research Institute; University of Ottawa; Flanders Institute for
   Biotechnology (VIB); KU Leuven; Queens University - Canada; University
   of Colorado System; University of Colorado Anschutz Medical Campus;
   University of Colorado System; University of Colorado Anschutz Medical
   Campus; University of Colorado System; University of Colorado Anschutz
   Medical Campus; University of California System; University of
   California San Francisco
RP Caruso, P; Morrell, NW (corresponding author), Univ Cambridge, Sch Clin Med, Dept Med, Addenbrookes Hosp, Box 157,Hills Rd, Cambridge CB2 0QQ, England.
EM pc468@medschl.cam.ac.uk; nwm23@medschl.cam.ac.uk
RI Hadinnapola, Charaka/AAW-1229-2020; D'Alessandro, Angelo/AAA-4695-2019;
   stenmark, kurt/AFI-6776-2022; Carmeliet, Peter/AAQ-5140-2020
OI Morrell, Nicholas/0000-0001-5700-9792; Ormiston,
   Mark/0000-0003-0907-1940; Kiskin, Fedir/0000-0002-6984-9622;
   D'Alessandro, Angelo/0000-0002-2258-6490; Carmeliet,
   Peter/0000-0001-7961-1821; Hadinnapola, Charaka/0000-0002-7794-3432; dos
   Santos, Claudia/0000-0002-6446-8791
FU British Heart Foundation Immediate Post-Doctoral Fellowship
   [FS/13/19/29931]; British Heart Foundation Personal Chair Award
   [CH/09/001/25945, RG/13/4/30107]; Canadian Institutes of Health Research
   [57726]
FX This work was supported by a British Heart Foundation Immediate
   Post-Doctoral Fellowship (Dr Caruso, FS/13/19/29931). Dr Morrell is
   funded by a British Heart Foundation Personal Chair Award
   (CH/09/001/25945) and Program Grant (RG/13/4/30107). Dr Stewart is
   funded by the Canadian Institutes of Health Research (grant 57726).
CR Aasa KL, 2015, BIOL REPROD, V92, DOI 10.1095/biolreprod.114.124677
   Arunachalam G, 2015, J CARDIOVASC PHARM, V65, P419, DOI 10.1097/FJC.0000000000000178
   Atkinson C, 2002, CIRCULATION, V105, P1672, DOI 10.1161/01.CIR.0000012754.72951.3D
   Austin ED, 2014, CIRC RES, V115, P189, DOI 10.1161/CIRCRESAHA.115.303404
   Bienertova-Vasku J, 2015, J AM SOC HYPERTENS, V9, P221, DOI 10.1016/j.jash.2014.12.011
   Breitwieser FP, 2011, J PROTEOME RES, V10, P2758, DOI 10.1021/pr1012784
   Chen M, 2010, CANCER RES, V70, P8977, DOI 10.1158/0008-5472.CAN-10-2513
   Conaco C, 2006, P NATL ACAD SCI USA, V103, P2422, DOI 10.1073/pnas.0511041103
   Courboulin A, 2011, J EXP MED, V208, P535, DOI 10.1084/jem.20101812
   D'Alessandro A, 2017, TRANSFUSION, V57, P1019, DOI 10.1111/trf.14034
   David CJ, 2010, NATURE, V463, P364, DOI 10.1038/nature08697
   Dewachter L, 2009, EUR RESPIR J, V34, P1100, DOI 10.1183/09031936.00183008
   Eddahibi S, 2002, EUR RESPIR J, V20, P1559, DOI 10.1183/09031936.02.00081302
   Eelen G, 2013, TRENDS ENDOCRIN MET, V24, P589, DOI 10.1016/j.tem.2013.08.006
   Fang YH, 2012, J MOL MED, V90, P31, DOI 10.1007/s00109-011-0804-9
   Fessel Joshua P, 2012, Pulm Circ, V2, P201, DOI 10.4103/2045-8932.97606
   Galiè N, 2013, EUR RESPIR REV, V22, P503, DOI 10.1183/09059180.00006613
   Gao P, 2012, CURR GENE THER, V12, P285, DOI 10.2174/156652312802083620
   Goldberg MS, 2012, J EXP MED, V209, P217, DOI 10.1084/jem.20111487
   Halestrap AP, 2013, COMPR PHYSIOL, V3, P1611, DOI 10.1002/cphy.c130008
   Halestrap AP, 2013, MOL ASPECTS MED, V34, P337, DOI 10.1016/j.mam.2012.05.003
   Humbert M, 2004, J AM COLL CARDIOL, V43, p13S, DOI 10.1016/j.jacc.2004.02.029
   John B, 2004, PLOS BIOL, V2, P1862, DOI 10.1371/journal.pbio.0020363
   Johnson JA, 2012, AM J PHYSIOL-LUNG C, V302, pL474, DOI 10.1152/ajplung.00202.2011
   Kang K, 2013, J BIOL CHEM, V288, P25414, DOI 10.1074/jbc.M113.460287
   Koppenol WH, 2011, NAT REV CANCER, V11, P325, DOI 10.1038/nrc3038
   Krek A, 2005, NAT GENET, V37, P495, DOI 10.1038/ng1536
   Lavoie JR, 2014, CIRCULATION, V129, P2125, DOI 10.1161/CIRCULATIONAHA.114.008777
   Long L, 2015, NAT MED, V21, P777, DOI 10.1038/nm.3877
   Luo WB, 2011, ONCOTARGET, V2, P551
   Luo WB, 2011, CELL, V145, P732, DOI 10.1016/j.cell.2011.03.054
   Majka S, 2011, RESP RES, V12, DOI 10.1186/1465-9921-12-84
   Makeyev EV, 2007, MOL CELL, V27, P435, DOI 10.1016/j.molcel.2007.07.015
   Marsboom G, 2012, AM J RESP CRIT CARE, V185, P670, DOI 10.1164/rccm.201108-1562OC
   Mazurek S, 2005, SEMIN CANCER BIOL, V15, P300, DOI 10.1016/j.semcancer.2005.04.009
   Michelakis ED, 2002, CIRCULATION, V105, P244, DOI 10.1161/hc0202.101974
   Ormiston ML, 2015, JOVE-J VIS EXP, DOI 10.3791/53384
   Papagiannakopoulos T, 2008, BMC MED, V6, DOI 10.1186/1741-7015-6-15
   Phanstiel DH, 2011, NAT METHODS, V8, P821, DOI [10.1038/nmeth.1699, 10.1038/NMETH.1699]
   Plecitá-Hlavatá L, 2016, AM J RESP CELL MOL, V55, P47, DOI 10.1165/rcmb.2015-0142OC
   Pullen TJ, 2011, MOL CELL BIOL, V31, P3182, DOI 10.1128/MCB.01433-10
   Sawicka K, 2008, BIOCHEM SOC T, V36, P641, DOI 10.1042/BST0360641
   Scott RW, 2010, J CELL BIOL, V191, P169, DOI 10.1083/jcb.201002041
   Semenza GL, 2011, COLD SH Q B, V76, P347, DOI 10.1101/sqb.2011.76.010678
   Stensjö K, 2007, J PROTEOME RES, V6, P621, DOI 10.1021/pr060517v
   Sun Y, 2012, ONCOL REP, V28, P1346, DOI 10.3892/or.2012.1958
   Taraseviciene-Stewart L, 2001, FASEB J, V15, P427, DOI 10.1096/fj.00-0343com
   Toshner M, 2010, INT J CLIN PRACT, V64, P7, DOI 10.1111/j.1742-1241.2009.02232.x
   Toshner M, 2009, AM J RESP CRIT CARE, V180, P780, DOI 10.1164/rccm.200810-1662OC
   Verdegem D, 2014, CANCER METAB, V2, DOI 10.1186/2049-3002-2-19
   Wang DR, 2014, CIRC RES, V114, P67, DOI 10.1161/CIRCRESAHA.114.301633
   White K, 2015, EMBO MOL MED, V7, P695, DOI 10.15252/emmm.201404511
   White K, 2014, HYPERTENSION, V64, P185, DOI 10.1161/HYPERTENSIONAHA.113.03037
   Wong N, 2015, NUCLEIC ACIDS RES, V43, pD146, DOI 10.1093/nar/gku1104
   Xia JG, 2015, NUCLEIC ACIDS RES, V43, pW251, DOI 10.1093/nar/gkv380
   Xie M, 2016, NAT COMMUN, V7, DOI 10.1038/ncomms13280
   Xu WL, 2007, P NATL ACAD SCI USA, V104, P1342, DOI 10.1073/pnas.0605080104
   Xu WL, 2011, COMPR PHYSIOL, V1, P357, DOI 10.1002/cphy.c090005
   Zhang H, 2017, CIRCULATION, V136, P2468, DOI 10.1161/CIRCULATIONAHA.117.028069
NR 59
TC 191
Z9 200
U1 1
U2 44
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA TWO COMMERCE SQ, 2001 MARKET ST, PHILADELPHIA, PA 19103 USA
SN 0009-7322
EI 1524-4539
J9 CIRCULATION
JI Circulation
PD DEC 19
PY 2017
VL 136
IS 25
BP 2451
EP +
DI 10.1161/CIRCULATIONAHA.117.028034
PG 74
WC Cardiac & Cardiovascular Systems; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology
GA FR2KW
UT WOS:000418896900011
PM 28971999
OA Green Accepted, Green Submitted, Bronze
DA 2025-04-10
ER

PT J
AU Goodwin, LO
   Leeds, NB
   Hurley, I
   Cooper, GW
   Pergolizzi, RG
   Benoff, S
AF Goodwin, LO
   Leeds, NB
   Hurley, I
   Cooper, GW
   Pergolizzi, RG
   Benoff, S
TI Alternative splicing of exons in the α1 subunit of the rat testis L-type
   voltage-dependent calcium channel generates germ line-specific
   dihydropyridine binding sites
SO MOLECULAR HUMAN REPRODUCTION
LA English
DT Article
DE acrosome reaction; alternative splicing; calcium channel; calcium
   influx; dihydropyridine
ID SPERM ACROSOME REACTION; IN-VITRO FERTILIZATION; RABBIT SKELETAL-MUSCLE;
   SEA-URCHIN SPERM; ZONA-PELLUCIDA; CA2+ CHANNEL; MOUSE SPERM;
   1,4-DIHYDROPYRIDINE RECEPTOR; MONOCLONAL-ANTIBODY; MOLECULAR DIVERSITY
AB Cell-specific isoforms of the alpha 1 subunit of the L-type voltage-dependent calcium channel (VDCC) have unique pharmacological reactivities. Prior sequence analysis of nucleotide bases 3908-6077 of the VDCC alpha 1 subunit expressed in rat testis differed from cardiac sequences only in a 84 base pair region corresponding to exons 31/32 encoding a putative dihydropyridine binding region. We now report that sequence analysis of bases 3048-3936 identifies a second difference between the rat testis and rat cardiac alpha 1 sequence in a 60 base pair region corresponding to exons 21/22 and encoding another putative dihydropyridine binding site. Variable VDCC exons 21/22 and 31/32 and their linking introns were sequenced using genomic DNA from rat lung as template, providing evidence that the rat testis and cardiac alpha 1 isoforms are products of the same gene. Reverse transcription in-situ polymerase chain reaction (PCR) with frozen sections of rat testis was carried out with primers identifying the testis-specific exon 32 of the VDCC alpha 1 subunit, PCR products were confined to seminiferous tubules and were associated with the germ cell lineage from Type A spermatogonia to mature spermatozoa. Close coupling of testis alpha 1 VDCC gene transcription and translation was established by in-situ immunolabelling of serial frozen sections with a monoclonal antibody (IIF7) directed against epitopes on rabbit skeletal muscle L-type VDCC alpha 1. Western blot analysis of rat proteins extracted from heart, skeletal muscle, testis and spermatozoa which were reactive with the IIF7 antibody detected primarily 175-220 kDa proteins in the site range of VDCC, These data unequivocally demonstrate that an L-type VDCC is expressed in rat testis and that VDCC isoforms from rat testis and heart differ in deduced amino acid composition in and around potential binding sites for calcium channel blocking drugs such as the dihydropyridines.
C1 NYU, N Shore Univ Hosp, Sch Med, Res Dept, Manhasset, NY USA.
   NYU, N Shore Univ Hosp, Sch Med, Dept Obstet & Gynecol, Manhasset, NY 11030 USA.
   NYU, Sch Med, Dept Cell Biol, New York, NY 10016 USA.
   NYU, Sch Med, Dept Obstet & Gynecol, New York, NY 10003 USA.
C3 New York University; Northwell Health; North Shore University Hospital;
   Northwell Health; North Shore University Hospital; New York University;
   New York University; New York University
RP Goodwin, LO (corresponding author), 300 Community Dr, Manhasset, NY 11030 USA.
FU NIEHS NIH HHS [ES 06100] Funding Source: Medline
CR AKAIKE N, 1989, J PHYSIOL-LONDON, V412, P181, DOI 10.1113/jphysiol.1989.sp017610
   Arnoult C, 1996, P NATL ACAD SCI USA, V93, P13004, DOI 10.1073/pnas.93.23.13004
   Arnoult C, 1996, J CELL BIOL, V134, P637, DOI 10.1083/jcb.134.3.637
   AULD UJ, 1990, P NATL ACAD SCI USA, V88, P2931
   BEDFORD JM, 1994, HUM REPROD, V9, P842, DOI 10.1093/oxfordjournals.humrep.a138604
   BELTRAN C, 1994, FEBS LETT, V338, P23, DOI 10.1016/0014-5793(94)80109-6
   Benoff S, 1997, MOL HUM REPROD, V3, P839, DOI 10.1093/molehr/3.10.839
   Benoff S, 1996, HUM REPROD, V11, P1905
   BENOFF S, 1994, FERTIL STERIL, V62, P606
   Benoff S., 1995, ASSIST REPROD REV, V5, P2
   BIELFELD P, 1994, FERTIL STERIL, V61, P536
   BLACKMORE PF, 1990, J BIOL CHEM, V265, P1376
   CALVO L, 1994, HUM REPROD, V9, P1875, DOI 10.1093/oxfordjournals.humrep.a138351
   CALVO L, 1994, HUM REPROD, V9, P1880, DOI 10.1093/oxfordjournals.humrep.a138352
   CALVO L, 1989, FERTIL STERIL, V52, P1048
   CATTERALL WA, 1992, TRENDS PHARMACOL SCI, V13, P256, DOI 10.1016/0165-6147(92)90079-L
   CATTERALL WA, 1995, ANNU REV BIOCHEM, V64, P493, DOI 10.1146/annurev.biochem.64.1.493
   CATTERALL WA, 1988, SCIENCE, V242, P50, DOI 10.1126/science.2459775
   CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
   DEJONGH KS, 1989, P NATL ACAD SCI USA, V86, P8585
   DEJONGH KS, 1991, P NATL ACAD SCI USA, V88, P10788
   DIEBOLD RJ, 1992, P NATL ACAD SCI USA, V89, P1497, DOI 10.1073/pnas.89.4.1497
   EM, 1991, ELECTRON MARK, V1, P1
   Enders G, 1997, J Am Board Fam Pract, V10, P131
   FALSETTI C, 1993, J ANDROL, V14, P17
   FERON O, 1994, EUR J BIOCHEM, V222, P195, DOI 10.1111/j.1432-1033.1994.tb18857.x
   FLORMAN HM, 1994, DEV BIOL, V165, P152, DOI 10.1006/dbio.1994.1242
   FLORMAN HM, 1992, DEV BIOL, V152, P304, DOI 10.1016/0012-1606(92)90137-6
   FRASER LR, 1993, MOL REPROD DEV, V36, P368, DOI 10.1002/mrd.1080360313
   FRASER LR, 1989, J REPROD FERTIL, V86, P223, DOI 10.1530/jrf.0.0860223
   FRASER LR, 1995, HUM REPROD, V10, P22, DOI 10.1093/humrep/10.suppl_1.22
   GAMIER J, 1978, J MOL BIOL, V120, P97
   Goodwin LO, 1997, MOL HUM REPROD, V3, P255, DOI 10.1093/molehr/3.3.255
   Hecht N B, 1988, Prog Clin Biol Res, V267, P291
   HEINEMANN SH, 1992, NATURE, V356, P441, DOI 10.1038/356441a0
   HERBETTE LG, 1989, J MOL CELL CARDIOL, V21, P187, DOI 10.1016/0022-2828(89)90861-4
   HERSHLAG A, 1995, HUM REPROD, V10, P599, DOI 10.1093/oxfordjournals.humrep.a135996
   HERSHLAG A, 1996, HUM REPROD, V11, P55
   HOLASH JA, 1993, P NATL ACAD SCI USA, V90, P11069, DOI 10.1073/pnas.90.23.11069
   JACOB A, 1997, ADV CONTRACEPT DELIV, V13, P223
   JACOB A, 1997, FERTIL STERIL S, pS182
   JUNEJA R, 1990, CONTRACEPTION, V41, P179, DOI 10.1016/0010-7824(90)90146-M
   Katsoff D, 1997, HUM REPROD, V12, P1480, DOI 10.1093/humrep/12.7.1480
   KAZAZOGLOU T, 1985, P NATL ACAD SCI USA, V82, P1460, DOI 10.1073/pnas.82.5.1460
   KOCH WJ, 1990, J BIOL CHEM, V265, P17786
   KOCH WJ, 1989, FEBS LETT, V250, P386, DOI 10.1016/0014-5793(89)80761-6
   KRAUSZ C, 1995, HUM REPROD, V10, P120, DOI 10.1093/humrep/10.1.120
   LAEMMLI UK, 1970, NATURE, V227, P680, DOI 10.1038/227680a0
   LAKOSKI KA, 1988, BIOL REPROD, V38, P221, DOI 10.1095/biolreprod38.1.221
   LANGS DA, 1990, J COMPUT AID MOL DES, V4, P215, DOI 10.1007/BF00125011
   LEBLOND CP, 1952, ANN NY ACAD SCI, V55, P548, DOI 10.1111/j.1749-6632.1952.tb26576.x
   LEUNG AT, 1987, J BIOL CHEM, V262, P7943
   LEYTON L, 1989, DEV BIOL, V132, P174, DOI 10.1016/0012-1606(89)90215-7
   Lievano A, 1996, FEBS LETT, V388, P150, DOI 10.1016/0014-5793(96)00515-7
   MACKINNON R, 1995, NEURON, V14, P889, DOI 10.1016/0896-6273(95)90327-5
   MASON RP, 1993, BIOCHEM PHARMACOL, V45, P2173, DOI 10.1016/0006-2952(93)90186-Z
   MASON RP, 1992, MOL PHARMACOL, V41, P315
   MENDOZA C, 1995, BIOCHEM BIOPH RES CO, V210, P518, DOI 10.1006/bbrc.1995.1690
   MIKAMI A, 1989, NATURE, V340, P230, DOI 10.1038/340230a0
   MITCHELL RD, 1983, J CELL BIOL, V96, P1008, DOI 10.1083/jcb.96.4.1008
   MORALES CR, 1991, J CELL SCI, V100, P119
   MOUNT SM, 1982, NUCLEIC ACIDS RES, V10, P49
   MYERS TW, 1991, BIOCHEMISTRY-US, V30, P7661, DOI 10.1021/bi00245a001
   Nuovo GJ, 1995, J HISTOTECHNOL, V18, P295
   NUOVO GJ, 1994, PCR IN SITU HYBRIDIZ
   OEHNINGER S, 1994, FERTIL STERIL, V61, P349
   PEREZREYES E, 1995, KIDNEY INT, V48, P1111, DOI 10.1038/ki.1995.395
   RHODES DG, 1985, MOL PHARMACOL, V27, P612
   ROLDAN ERS, 1994, SCIENCE, V266, P1578, DOI 10.1126/science.7985030
   ROSEMBLATT M, 1981, J BIOL CHEM, V256, P8140
   SALING PM, 1986, DEV BIOL, V117, P511, DOI 10.1016/0012-1606(86)90318-0
   SCHACKMANN RW, 1981, DEV BIOL, V81, P145, DOI 10.1016/0012-1606(81)90357-2
   SHARP AH, 1987, J BIOL CHEM, V262, P12309
   SHARP AH, 1989, J BIOL CHEM, V264, P2816
   SNUTCH TP, 1991, NEURON, V7, P45, DOI 10.1016/0896-6273(91)90073-9
   SOLDATOV NM, 1992, P NATL ACAD SCI USA, V89, P4628, DOI 10.1073/pnas.89.10.4628
   SOLDATOV NM, 1995, J BIOL CHEM, V270, P10540, DOI 10.1074/jbc.270.18.10540
   SOLDATOV NM, 1994, GENOMICS, V22, P77, DOI 10.1006/geno.1994.1347
   STUHMER W, 1989, NATURE, V339, P597, DOI 10.1038/339597a0
   SUMMERS D, 1997, J ASSIST REPROD GE S, V14, P2015
   TAKAHASHI M, 1987, P NATL ACAD SCI USA, V84, P5478, DOI 10.1073/pnas.84.15.5478
   TANABE T, 1987, NATURE, V328, P313, DOI 10.1038/328313a0
   TESARIK J, 1992, FERTIL STERIL, V58, P793
   THOMAS P, 1988, GAMETE RES, V20, P397, DOI 10.1002/mrd.1120200402
   TIWARIWOODRUFF SK, 1995, AM J PHYSIOL-CELL PH, V268, pC1284, DOI 10.1152/ajpcell.1995.268.5.C1284
   TOWBIN H, 1979, P NATL ACAD SCI USA, V76, P4340
   TRIMMER JS, 1985, CELL, V40, P697, DOI 10.1016/0092-8674(85)90218-1
   TSIEN RW, 1991, TRENDS PHARMACOL SCI, V12, P349, DOI 10.1016/0165-6147(91)90595-J
   WELLING A, 1993, CIRC RES, V73, P974, DOI 10.1161/01.RES.73.5.974
   Zhorov BS, 1996, BIOPHYS J, V70, P22, DOI 10.1016/S0006-3495(96)79561-9
NR 90
TC 35
Z9 37
U1 1
U2 2
PU OXFORD UNIV PRESS
PI OXFORD
PA GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND
SN 1360-9947
J9 MOL HUM REPROD
JI Mol. Hum. Reprod.
PD MAR
PY 1998
VL 4
IS 3
BP 215
EP 226
DI 10.1093/molehr/4.3.215
PG 12
WC Developmental Biology; Obstetrics & Gynecology; Reproductive Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Developmental Biology; Obstetrics & Gynecology; Reproductive Biology
GA ZG354
UT WOS:000072993200004
PM 9570267
OA Bronze
DA 2025-04-10
ER

PT J
AU Koi, PT
   Milhoua, PM
   Monrose, V
   Melman, A
   DiSanto, ME
AF Koi, P. T.
   Milhoua, P. M.
   Monrose, V.
   Melman, A.
   DiSanto, M. E.
TI Expression of myosin isoforms in the smooth muscle of human corpus
   cavernosum
SO INTERNATIONAL JOURNAL OF IMPOTENCE RESEARCH
LA English
DT Article
DE SM-A; LC17b; pelvic surgery; PDE5 inhibitors
ID BLADDER OUTLET OBSTRUCTION; HEAVY-CHAIN; LIGHT-CHAIN; SHORTENING
   VELOCITY; ERECTILE DYSFUNCTION; SINGLE GENE; NUCLEOTIDE; NONMUSCLE;
   INSERT; CELLS
AB The molecular interaction between smooth muscle (SM) myosin and actin in the corpus cavernosum (CC) determines the erectile state of the penis. A key mechanism regulating this interaction and subsequent development and maintenance of force is alternative splicing of SM myosin heavy chain (MHC) and 17 kDa essential SM myosin light chain (MLC) pre-mRNAs. Our aim was to examine the relative SM myosin isoform composition in human CC. Tissue samples were obtained from 18 patients with erectile dysfunction (ED), Peyronie's disease, or both. One specimen was obtained during a transgender operation. Patients then were stratified according to presence of diabetes mellitus, hypertension, ED, or Peyronie's disease, as well as failure of phosphodiesterase-5 (PDE5) inhibitors and history of previous pelvic or penile surgeries, radiation, or both. Our results revealed that all human CC samples expressed only the SM-A isoform. There was a predominance of SM2 isoform mRNA relative to SM1 across all samples, with a mean of 63.8%, which correlated with protein analysis by gel electrophoresis. A statistically significant difference was found between patients who had undergone previous pelvic surgery, radiation, or both and those who did not. The ratio of LC17b to LC17a was approximately 1:1 for all patients, with a mean of 48.9% LC17b. Statistical difference was seen in the relative ratio of LC17b to LC17a among the group who failed conservative therapy with PDE5 inhibitors compared with all others. In conclusion, we determined the SM myosin isoform composition of human CC and present for the first time differences in relative myosin isoform expression among patients with several risk factors contributing to their cause of ED. Our data reflect the fact that alternative splicing events in the MHC and 17 kDa MLC pre-mRNA may be a possible molecular mechanism involved in the altered contractility of the CCSM in patients with ED.
C1 Albert Einstein Coll Med, Dept Urol, Bronx, NY 10461 USA.
C3 Yeshiva University; Montefiore Medical Center; Albert Einstein College
   of Medicine
RP DiSanto, ME (corresponding author), Albert Einstein Coll Med, Dept Urol, 1300 Morris Pk Ave,Forchheimer Bldg,Room 744, Bronx, NY 10461 USA.
EM mdisanto@aecom.yu.edu
CR Arner A, 2003, J MUSCLE RES CELL M, V24, P165, DOI 10.1023/A:1026001513928
   Aytac IA, 1999, BJU INT, V84, P50
   BABIJ P, 1989, J MOL BIOL, V210, P673, DOI 10.1016/0022-2836(89)90142-3
   BABIJ P, 1991, P NATL ACAD SCI USA, V88, P10676, DOI 10.1073/pnas.88.23.10676
   BABIJ P, 1993, NUCLEIC ACIDS RES, V21, P1467, DOI 10.1093/nar/21.6.1467
   Babu GJ, 2001, NAT CELL BIOL, V3, P1025, DOI 10.1038/ncb1101-1025
   Chang SH, 2002, J UROLOGY, V167, P2636, DOI 10.1016/S0022-5347(05)65050-1
   Damon DH, 2005, AM J PHYSIOL-HEART C, V288, pH2785, DOI 10.1152/ajpheart.00354.2004
   DiSanto ME, 1998, AM J PHYSIOL-CELL PH, V275, pC976, DOI 10.1152/ajpcell.1998.275.4.C976
   DiSanto ME, 2003, J ANDROL, V24, pS6
   DiSanto ME, 2003, AM J PHYSIOL-CELL PH, V285, pC1397, DOI 10.1152/ajpcell.00513.2002
   DiSanto ME, 1997, AM J PHYSIOL-CELL PH, V272, pC1532, DOI 10.1152/ajpcell.1997.272.5.C1532
   Huang QQ, 1999, J BIOL CHEM, V274, P35095, DOI 10.1074/jbc.274.49.35095
   KELLEY CA, 1992, J BIOL CHEM, V267, P2127
   KELLEY CA, 1993, J BIOL CHEM, V268, P12848
   Lauzon AM, 1998, J MUSCLE RES CELL M, V19, P825, DOI 10.1023/A:1005489501357
   LENZ S, 1989, J BIOL CHEM, V264, P9009
   MALMQVIST U, 1991, PFLUG ARCH EUR J PHY, V418, P523, DOI 10.1007/BF00370566
   Matthew JD, 1998, J BIOL CHEM, V273, P31289, DOI 10.1074/jbc.273.47.31289
   McVary Kevin T, 2004, Curr Urol Rep, V5, P251, DOI 10.1007/s11934-004-0047-1
   Meer DP, 1997, AM J PHYSIOL-CELL PH, V273, pC1259, DOI 10.1152/ajpcell.1997.273.4.C1259
   Mitani Y, 2001, EUR RESPIR J, V17, P316, DOI 10.1183/09031936.01.17203160
   Montorsi P, 2004, CURR OPIN UROL, V14, P361, DOI 10.1097/00042307-200411000-00012
   NABESHIMA Y, 1987, J BIOL CHEM, V262, P10608
   Rovner AS, 2002, J CELL BIOL, V156, P113, DOI 10.1083/jcb.200107131
   SAMUEL M, 1990, BIOCHEMISTRY-US, V29, P7124, DOI 10.1021/bi00482a026
   Siegman MJ, 1997, AM J PHYSIOL-GASTR L, V272, pG1571, DOI 10.1152/ajpgi.1997.272.6.G1571
   Somlyo AV, 1998, ACTA PHYSIOL SCAND, V164, P381, DOI 10.1111/j.1365-201X.1998.tb10695.x
   Szymanski PT, 1998, AM J PHYSIOL-CELL PH, V275, pC684, DOI 10.1152/ajpcell.1998.275.3.C684
   WANG Z, 1995, LAB INVEST, V73, P244
   Wyllie Michael G, 2005, Clin Cornerstone, V7, P19, DOI 10.1016/S1098-3597(05)80045-6
NR 31
TC 9
Z9 11
U1 0
U2 5
PU NATURE PUBLISHING GROUP
PI LONDON
PA MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
SN 0955-9930
J9 INT J IMPOT RES
JI Int. J. Impot. Res.
PD JAN-FEB
PY 2007
VL 19
IS 1
BP 62
EP 68
DI 10.1038/sj.ijir.3901503
PG 7
WC Urology & Nephrology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Urology & Nephrology
GA 128UW
UT WOS:000243685500009
PM 16885993
DA 2025-04-10
ER

PT J
AU Blein, S
   Hawrot, E
   Barlow, P
AF Blein, S
   Hawrot, E
   Barlow, P
TI The metabotropic GABA receptor: molecular insights and their functional
   consequences
SO CELLULAR AND MOLECULAR LIFE SCIENCES
LA English
DT Review
DE GABA(B) receptor; G-protein-coupled receptor; seven-transmembrane-domain
   receptor; short consensus repeats; sushi domains; drug target
ID GAMMA-AMINOBUTYRIC-ACID; CALCIUM-SENSING RECEPTOR; IDIOPATHIC
   GENERALIZED EPILEPSY; PROTEIN-COUPLED RECEPTORS; CELL-SURFACE
   EXPRESSION; RECTIFYING K+ CHANNELS; EXTRACELLULAR DOMAIN; GLUTAMATE
   RECEPTORS; RAT-BRAIN; PRESYNAPTIC INHIBITION
AB Recent years have seen rapid and significant advances in our understanding of the G-protein-coupled gamma-amino butyric acid, B-type (GABA,) receptor, which could be a therapeutic target in conditions as diverse as epilepsy and hypertension. This progress originated with the ground-breaking work of Bernhard Bettler's team at Novartis who cloned the DNA encoding a GABA(B) receptor in 1997. Currently, the receptor is thought to be an unusual, possibly unique, example of a heterodimer composed of homologous, seven-transmembrane-domain (7TMD) subunits (named GABA(B) R1 and GABA(B) R2), neither of which is fully functional when expressed alone. The large N-terminal domain of the GABA(B) R1 subunit projects extracellularly and contains a ligand binding site. The similarity of the amino acid sequence of this region to some bacterial periplasmic amino acid-binding proteins of known structure has enabled structural and functional modelling of the N-terminal domain, and the identification of residues whose substitution modulates agonist/antagonist binding affinities. The intracellular C-terminal domains of the R1 and R2 subunits appear to constitute an important means of contact between the two subunits. Alternative splice variants, a common and functionally important feature of 7TMD proteins, have been demonstrated for the R1 subunit. Notably GABA(B) R1a differs from GABA(B) R1b by the possession of an N-terminal extension containing two complement protein modules (also called SCRs, or sushi domains) of unknown function. The levels at which each of the respective variants is expressed are not equal to one another, with variations occurring over the course of development and throughout the central nervous system. It is not yet clear, however, whether one variant is predominantly presynaptically located and the other postsynaptically located. The existence of as yet unidentified splice variants, additional receptor subtypes and alternative quaternary composition has not been ruled out as a source of receptor heterogeneity.
C1 Brown Univ, Dept Mol Pharmacol Physiol & Biotechol, Providence, RI 02912 USA.
   Univ Edinburgh, Edinburgh Ctr Prot Technol, Edinburgh EH9 3JJ, Midlothian, Scotland.
C3 Brown University; University of Edinburgh
RP Hawrot, E (corresponding author), Brown Univ, Dept Mol Pharmacol Physiol & Biotechol, Providence, RI 02912 USA.
RI Barlow, Paul/G-2853-2011; Blein, Stanislas/AFF-8910-2022
CR ALKADHI KA, 1993, ARCH INT PHARMACOD T, V322, P66
   Bai M, 1998, J BIOL CHEM, V273, P23605, DOI 10.1074/jbc.273.36.23605
   BALDWIN JM, 1993, EMBO J, V12, P1693, DOI 10.1002/j.1460-2075.1993.tb05814.x
   Benke D, 1999, J BIOL CHEM, V274, P27323, DOI 10.1074/jbc.274.38.27323
   Bettler B, 1998, CURR OPIN NEUROBIOL, V8, P345, DOI 10.1016/S0959-4388(98)80059-7
   Billinton A, 1999, BRIT J PHARMACOL, V126, P1387, DOI 10.1038/sj.bjp.0702460
   BONANNO G, 1993, TRENDS PHARMACOL SCI, V14, P259, DOI 10.1016/0165-6147(93)90124-3
   BOWERY N, 1989, TRENDS PHARMACOL SCI, V10, P401, DOI 10.1016/0165-6147(89)90188-0
   BOWERY NG, 1993, ANNU REV PHARMACOL, V33, P109, DOI 10.1146/annurev.pa.33.040193.000545
   Bräuner-Osborne H, 1999, J BIOL CHEM, V274, P18382, DOI 10.1074/jbc.274.26.18382
   Caddick SJ, 1996, MOL NEUROBIOL, V13, P23, DOI 10.1007/BF02740750
   CAPASSO A, 1999, BIOL PSYCHIAT, V23, P289
   Couve A, 1998, J BIOL CHEM, V273, P26361, DOI 10.1074/jbc.273.41.26361
   Cvejic S, 1997, J BIOL CHEM, V272, P26959, DOI 10.1074/jbc.272.43.26959
   DAVIES CH, 1991, NATURE, V349, P609, DOI 10.1038/349609a0
   De Luca Francesco, 1998, Current Opinion in Pediatrics, V10, P435
   Deisz RA, 1997, SYNAPSE, V25, P62, DOI 10.1002/(SICI)1098-2396(199701)25:1<62::AID-SYN8>3.0.CO;2-D
   DUTAR P, 1988, NATURE, V332, P156, DOI 10.1038/332156a0
   Dwyer ND, 1998, CELL, V93, P455, DOI 10.1016/S0092-8674(00)81173-3
   Fan GF, 1998, FEBS LETT, V436, P353, DOI 10.1016/S0014-5793(98)01165-X
   Feldman DS, 1997, J PHARMACOL EXP THER, V281, P274
   Fritschy JM, 1999, EUR J NEUROSCI, V11, P761, DOI 10.1046/j.1460-9568.1999.00481.x
   Galvez T, 1999, J BIOL CHEM, V274, P13362, DOI 10.1074/jbc.274.19.13362
   Getova D, 1997, EUR J PHARMACOL, V320, P9, DOI 10.1016/S0014-2999(96)00877-1
   Grifa A, 1998, BIOCHEM BIOPH RES CO, V250, P240, DOI 10.1006/bbrc.1998.9296
   HAMANN J, 1995, J IMMUNOL, V155, P1942
   Hamann J, 1998, EUR J IMMUNOL, V28, P1701, DOI 10.1002/(SICI)1521-4141(199805)28:05<1701::AID-IMMU1701>3.0.CO;2-2
   Hamann J, 1996, J EXP MED, V184, P1185, DOI 10.1084/jem.184.3.1185
   Hawrot E, 1998, FEBS LETT, V432, P103, DOI 10.1016/S0014-5793(98)00794-7
   Hebert TE, 1996, J BIOL CHEM, V271, P16384, DOI 10.1074/jbc.271.27.16384
   Herbst R, 1997, MOL BRAIN RES, V44, P309, DOI 10.1016/S0169-328X(96)00274-4
   HILL DR, 1981, NATURE, V290, P149, DOI 10.1038/290149a0
   Horn F, 1998, NUCLEIC ACIDS RES, V26, P275, DOI 10.1093/nar/26.1.275
   Hoshino M, 1999, DEV GENES EVOL, V209, P1, DOI 10.1007/s004270050221
   Isomoto S, 1998, BIOCHEM BIOPH RES CO, V253, P10, DOI 10.1006/bbrc.1998.9706
   Jones KA, 1998, NATURE, V396, P674, DOI 10.1038/25348
   Jordan BA, 1999, NATURE, V399, P697, DOI 10.1038/21441
   Kaupmann K, 1998, NATURE, V396, P683, DOI 10.1038/25360
   Kaupmann K, 1997, NATURE, V386, P239, DOI 10.1038/386239a0
   Kaupmann K, 1998, P NATL ACAD SCI USA, V95, P14991, DOI 10.1073/pnas.95.25.14991
   KERR DIB, 1995, PHARMACOL THERAPEUT, V67, P187, DOI 10.1016/0163-7258(95)00016-A
   Kilpartick GJ, 1999, TRENDS PHARMACOL SCI, V20, P294, DOI 10.1016/S0165-6147(99)01355-3
   Koulen P, 1998, EUR J NEUROSCI, V10, P1446, DOI 10.1046/j.1460-9568.1998.00156.x
   Krapivinsky G, 1998, J BIOL CHEM, V273, P16946, DOI 10.1074/jbc.273.27.16946
   Kubo Y, 1998, SCIENCE, V279, P1722, DOI 10.1126/science.279.5357.1722
   Kuner R, 1999, SCIENCE, V283, P74, DOI 10.1126/science.283.5398.74
   Luscher C, 1997, NEURON, V19, P687, DOI 10.1016/S0896-6273(00)80381-5
   Malitschek B, 1999, MOL PHARMACOL, V56, P448, DOI 10.1124/mol.56.2.448
   Malitschek B, 1998, MOL CELL NEUROSCI, V12, P56, DOI 10.1006/mcne.1998.0698
   MARGOLIS RU, 1994, METHOD ENZYMOL, V245, P105
   Martin SC, 1999, MOL CELL NEUROSCI, V13, P180, DOI 10.1006/mcne.1999.0741
   McKnight AJ, 1998, J LEUKOCYTE BIOL, V63, P271, DOI 10.1002/jlb.63.3.271
   McLatchie LM, 1998, NATURE, V393, P333, DOI 10.1038/30666
   MEINDL A, 1995, HUM MOL GENET, V4, P2339, DOI 10.1093/hmg/4.12.2339
   Mohler H, 1999, Trends Pharmacol Sci, V20, P87, DOI 10.1016/S0165-6147(99)01323-1
   MORLEY BJ, 1984, EMBO J, V3, P153, DOI 10.1002/j.1460-2075.1984.tb01776.x
   Morris SJ, 1998, J NEUROCHEM, V71, P1329
   MOTT DD, 1994, INT REV NEUROBIOL, V36, P97, DOI 10.1016/S0074-7742(08)60304-9
   Ng GYK, 1999, GENOMICS, V56, P288, DOI 10.1006/geno.1998.5706
   Ng GYK, 1999, J BIOL CHEM, V274, P7607, DOI 10.1074/jbc.274.12.7607
   Nicholson GA, 1996, NAT GENET, V13, P101, DOI 10.1038/ng0596-101
   OHARA PJ, 1993, NEURON, V11, P41, DOI 10.1016/0896-6273(93)90269-W
   Pace AJ, 1999, J BIOL CHEM, V274, P11629, DOI 10.1074/jbc.274.17.11629
   Peters HC, 1998, NEUROGENETICS, V2, P47, DOI 10.1007/s100480050051
   PIN JP, 1995, CURR OPIN NEUROBIOL, V5, P342, DOI 10.1016/0959-4388(95)80047-6
   Romano C, 1996, J BIOL CHEM, V271, P28612, DOI 10.1074/jbc.271.45.28612
   SACK JS, 1989, J MOL BIOL, V206, P171, DOI 10.1016/0022-2836(89)90531-7
   SACK JS, 1989, J MOL BIOL, V206, P193, DOI 10.1016/0022-2836(89)90532-9
   Sander T, 1999, AM J MED GENET, V88, P305, DOI 10.1002/(SICI)1096-8628(19990820)88:4<305::AID-AJMG5>3.0.CO;2-X
   SCANZIANI M, 1992, NEURON, V9, P919, DOI 10.1016/0896-6273(92)90244-8
   SHIMIZUNISHIKAWA K, 1995, BIOCHEM BIOPH RES CO, V216, P382, DOI 10.1006/bbrc.1995.2635
   Shoaib M, 1998, BEHAV PHARMACOL, V9, P195
   Slesinger PA, 1997, P NATL ACAD SCI USA, V94, P12210, DOI 10.1073/pnas.94.22.12210
   SMITH GB, 1995, TRENDS PHARMACOL SCI, V16, P162, DOI 10.1016/S0165-6147(00)89009-4
   TAKAHASHI K, 1993, J BIOL CHEM, V268, P19341
   Takahashi T, 1998, J NEUROSCI, V18, P3138
   THOMPSON SM, 1993, TRENDS NEUROSCI, V16, P222, DOI 10.1016/0166-2236(93)90160-N
   Ward DT, 1998, J BIOL CHEM, V273, P14476, DOI 10.1074/jbc.273.23.14476
   White JH, 1998, NATURE, V396, P679, DOI 10.1038/25354
   Yamada K, 1999, J NEUROPHYSIOL, V81, P2875, DOI 10.1152/jn.1999.81.6.2875
NR 80
TC 40
Z9 43
U1 0
U2 7
PU BIRKHAUSER VERLAG AG
PI BASEL
PA VIADUKSTRASSE 40-44, PO BOX 133, CH-4010 BASEL, SWITZERLAND
SN 1420-682X
J9 CELL MOL LIFE SCI
JI Cell. Mol. Life Sci.
PD APR
PY 2000
VL 57
IS 4
BP 635
EP 650
DI 10.1007/PL00000725
PG 16
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA 319LL
UT WOS:000087342600013
PM 11130463
OA Green Published
DA 2025-04-10
ER

PT J
AU Fasihi, A
   Heydari-Zarnagh, H
   Zahedi, M
   Goudarzian, M
   Kafashzadeh, M
   Meshkani, SE
   Ramazi, S
AF Fasihi, Ali
   Heydari-Zarnagh, Hafez
   Zahedi, Mohmmadsaeid
   Goudarzian, Maryam
   Kafashzadeh, Mehrnaz
   Meshkani, Seyed Elyas
   Ramazi, Shahin
TI Study and Characterization of Long Non-coding RUNX1-IT1 among Large
   Artery Atherosclerosis Stroke Patients Based on the ceRNA Hypothesis
SO JOURNAL OF MOLECULAR NEUROSCIENCE
LA English
DT Article
DE LAA stroke; lncRNA; RUNX1-IT1; miRNAs; Meta-analysis; Regulatory network
ID ISCHEMIC-STROKE; RNA; APOPTOSIS; BLOOD; EXPRESSION; P53
AB Recent studies have shed light on the involvement of long non-coding RNAs (lncRNAs) in the initiation and development of stroke. However, the regulatory function of many lncRNAs in large artery atherosclerosis (LAA) has not been fully elucidated. Based on the competing endogenous RNA (ceRNA) hypothesis recently proposed by Pandolfi, the present study was conducted using experimental techniques and bioinformatics to investigate the expression and regulatory function of a lncRNA involved in the development of LAA. The lncRNAs differentially expressed in stroke were obtained using meta-analysis, and one lncRNA was selected for experimental studies on patients with LAA (n = 100) and healthy controls (n = 100) using quantitative real-time polymerase chain reaction (qRT-PCR). The patients were also evaluated through meta-analysis to identify the function of the selected lncRNA, miRNAs, and mRNAs with altered expression in stroke. Finally, the experimental results and meta-analysis findings were integrated, and different functional groups were assigned. The results indicated that the level of lncRNA-RUNX1-IT1 was significantly lower in the patients with LAA compared to the healthy control subjects (p > 0.05). Logistic regression analyses revealed that the expression of lncRNA-RUNX1-IT1 was inversely correlated with LAA (P = 009, OR = 0.871, 95% CI: 0.786-0.965). In addition, a network of differentially expressed genes (DE genes) was created for miRNAs and mRNAs based on their association with lncRNA-RUNX1-IT1. Functional analysis showed that the DE genes in the network are involved in the apoptosis and alternative splicing of RNAs. The findings of the present study suggest that the downregulation of lncRNA-RUNX1-IT1 is associated with LAA development by interrupting the regulatory network of cells. The results of network analysis demonstrated that the lncRNA-RUNX1-IT1 could influence the expression of mRNAs and miRNAs involved in the apoptosis and alternative splicing of RNAs.
C1 [Fasihi, Ali] Tarbiat Modares Univ, Fac Biol Sci, Mol Genet Dept, Tehran, Iran.
   [Heydari-Zarnagh, Hafez; Kafashzadeh, Mehrnaz; Meshkani, Seyed Elyas; Ramazi, Shahin] Sabzevar Univ Med Sci, Cellular & Mol Res Ctr, Sabzevar, Iran.
   [Zahedi, Mohmmadsaeid] Shiraz Univ Med Sci, Bioinformat & Computat Biol Res Ctr, Shiraz, Iran.
   [Zahedi, Mohmmadsaeid] Shiraz Univ Med Sci, Sch Pharm, Dept Med Chem, Shiraz, Iran.
   [Goudarzian, Maryam] Iranian Res Ctr Hlth Aging, Sabzevar Med Sci, Sabzevar, Iran.
C3 Tarbiat Modares University; Shiraz University of Medical Science; Shiraz
   University of Medical Science
RP Ramazi, S (corresponding author), Sabzevar Univ Med Sci, Cellular & Mol Res Ctr, Sabzevar, Iran.
EM aliac88@gmail.com; hafez1362@gmail.com; msaeidzahedi@gmail.com;
   mary_ac_ir@yahoo.com; Mehrnazkafashzadeh@gmail.com;
   elyas.meshkani92@gmail.com; Shahimamazi@yahoo.com
OI ramazi, shahin/0000-0001-7848-5077
FU Sabzevar University of Medical Sciences [394212163]
FX The present study was supported by Sabzevar University of Medical
   Sciences (grant number: 394212163).
CR [Anonymous], 2016, BRIEF BIOINFORM
   Bai Y, 2018, J NEUROSCI, V38, P32, DOI 10.1523/JNEUROSCI.1348-17.2017
   Bao MH, 2018, CELL DEATH DIS, V9, DOI 10.1038/s41419-018-0282-x
   Beal CC, 2010, J NEUROSCI NURS, V42, P80, DOI 10.1097/JNN.0b013e3181ce5c70
   Chakraborty D, 2017, CELL REP, V21, P3012, DOI 10.1016/j.celrep.2017.11.045
   Chan JJ, 2018, INT J MOL SCI, V19, DOI 10.3390/ijms19051310
   Chen FH, 2018, BIOCHEM BIOPH RES CO, V496, P184, DOI 10.1016/j.bbrc.2018.01.022
   Chen G, 2017, CANCER CELL INT, V17, DOI 10.1186/s12935-017-0466-y
   Chen SC, 2017, BIOCHEM BIOPH RES CO, V485, P167, DOI 10.1016/j.bbrc.2017.02.043
   Deng QW, 2018, CLIN SCI, V132, P1597, DOI 10.1042/CS20180411
   Donkor ES, 2018, STROKE 21 CENTURY SN, V2018
   Dykstra-Aiello C, 2015, TRANSL STROKE RES, V6, P284, DOI 10.1007/s12975-015-0407-9
   Iyengar BR, 2014, FRONT CELL NEUROSCI, V8, DOI 10.3389/fncel.2014.00047
   Jiang LL, 2011, EXP LUNG RES, V37, P387, DOI 10.3109/01902148.2010.492068
   Karagkouni D, 2018, NUCLEIC ACIDS RES, V46, pD239, DOI 10.1093/nar/gkx1141
   Kinouchi M, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0115936
   Kozomara A, 2019, NUCLEIC ACIDS RES, V47, pD155, DOI 10.1093/nar/gky1141
   Leotta M, 2014, J CELL PHYSIOL, V229, P2106, DOI 10.1002/jcp.24669
   Lin ZW, 2017, SCI REP-UK, V7, DOI 10.1038/srep42498
   Lipscombe D, 2019, CURR OPIN NEUROBIOL, V57, P26, DOI 10.1016/j.conb.2018.12.013
   Liu WS, 2016, AM J TRANSL RES, V8, P3179
   Livak KJ, 2001, METHODS, V25, P402, DOI 10.1006/meth.2001.1262
   Meng FM, 2018, PEERJ, V6, DOI 10.7717/peerj.4246
   Shi JX, 2019, CELL BIOCHEM FUNCT, V37, P11, DOI 10.1002/cbf.3368
   Sun YP, 2019, J CELL BIOCHEM, V120, P3874, DOI 10.1002/jcb.27669
   Wang QW, 2019, CURR PHARM DESIGN, V25, P1115, DOI 10.2174/1381612825666190328112844
   Wang SW, 2018, CELL TRANSPLANT, V27, P1763, DOI 10.1177/0963689718806818
   Wang X, 2018, ONCOL REP, V40, P2659, DOI 10.3892/or.2018.6707
   Wang YR, 2017, J STROKE CEREBROVASC, V26, P1055, DOI 10.1016/j.jstrokecerebrovasdis.2016.12.019
   Wei N, 2016, MOL NEUROBIOL, V53, P6809, DOI 10.1007/s12035-015-9605-4
   Wu ZM, 2017, MOL NEUROBIOL, V54, P7670, DOI 10.1007/s12035-016-0246-z
   Yang K, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-00763-y
   Yang ZG, 2016, ANTI-CANCER AGENT ME, V16, P1101, DOI 10.2174/1871520616666151116122921
   Yuan JY, 2009, APOPTOSIS, V14, P469, DOI 10.1007/s10495-008-0304-8
   Zhang GD, 2018, CELL DEATH DISCOV, V4, DOI 10.1038/s41420-018-0036-7
   Zhang L, 2018, J CELL BIOCHEM, V119, P5460, DOI 10.1002/jcb.26705
   Zhang XJ, 2017, J NEUROSCI, V37, P1797, DOI 10.1523/JNEUROSCI.3389-16.2017
   Zheng YH, 2019, J CELL BIOCHEM, V120, P12832, DOI 10.1002/jcb.28554
   Zhu M, 2018, J STROKE CEREBROVASC, V27, P326, DOI 10.1016/j.jstrokecerebrovasdis.2017.09.009
NR 39
TC 5
Z9 5
U1 0
U2 7
PU SPRINGERNATURE
PI LONDON
PA CAMPUS, 4 CRINAN ST, LONDON, N1 9XW, ENGLAND
SN 0895-8696
EI 1559-1166
J9 J MOL NEUROSCI
JI J. Mol. Neurosci.
PD MAR
PY 2021
VL 71
IS 3
BP 455
EP 465
DI 10.1007/s12031-020-01668-8
EA JUL 2020
PG 11
WC Biochemistry & Molecular Biology; Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Neurosciences & Neurology
GA QA9UW
UT WOS:000552941700001
PM 32720226
DA 2025-04-10
ER

PT J
AU Chen, YM
   Green, SR
   Ho, J
   Li, A
   Almazan, F
   Quehenberger, O
AF Chen, YM
   Green, SR
   Ho, J
   Li, A
   Almazan, F
   Quehenberger, O
TI The mouse CCR2 gene is regulated by two promoters that are responsive to
   plasma cholesterol and peroxisome proliferator-activated receptor γ
   ligands
SO BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
LA English
DT Article
DE CCR2; chemokines; promoter; gene expression; cholesterol; PPAR gamma;
   atherosclerosis
ID MONOCYTE CHEMOATTRACTANT PROTEIN-1; LOW-DENSITY-LIPOPROTEIN;
   ATHEROSCLEROTIC LESIONS; DEFICIENT MICE; FUNCTIONAL-CHARACTERIZATION;
   GENOMIC ORGANIZATION; PPAR-GAMMA; EXPRESSION; TROGLITAZONE; REVEALS
AB We have previously shown that the expression of monocyte CCR2, the receptor for monocyte chemoattractant protein-1, is induced by plasma cholesterol. The present study examines the mechanisms that regulate monocyte CCR2 expression in hypercholesterolemia using a mouse model. Our data demonstrate that in the Mouse, CCR2 expression in circulating monocytes is controlled by two promoters P1 and P2. The two distinct transcripts, which encode the same protein, are produced by alternative splicing in the 5'-untranslated region. Both promoters are constitutively active, but only P2 is stimulated by cholesterol. However, both promoters are repressed by peroxisome proliferator-activated receptor gamma. (c) 2005 Elsevier Inc. All rights reserved.
C1 Univ Calif San Diego, Dept Med, La Jolla, CA 92093 USA.
C3 University of California System; University of California San Diego
RP Univ Calif San Diego, Dept Med, La Jolla, CA 92093 USA.
EM oquehenberger@ucsd.edu
FU NHLBI NIH HHS [HL56989] Funding Source: Medline
CR AHUJA SK, 1994, J BIOL CHEM, V269, P26381
   Boring L, 1998, NATURE, V394, P894, DOI 10.1038/29788
   Bursi CA, 2004, CURR OPIN LIPIDOL, V15, P145, DOI [10.1097/00041433-200404000-00007, 10.1097/01.mol.0000124526.75650.13]
   CHARO IF, 1994, P NATL ACAD SCI USA, V91, P2752, DOI 10.1073/pnas.91.7.2752
   Chen Z, 2001, ARTERIOSCL THROM VAS, V21, P372, DOI 10.1161/01.ATV.21.3.372
   Collins AR, 2001, ARTERIOSCL THROM VAS, V21, P365, DOI 10.1161/01.ATV.21.3.365
   DeVries ME, 2003, J BIOL CHEM, V278, P11985, DOI 10.1074/jbc.M211422200
   Garin A, 2002, BIOCHEM J, V368, P753, DOI 10.1042/BJ20020951
   GERRITY RG, 1981, AM J PATHOL, V103, P191
   Gu L, 1998, MOL CELL, V2, P275, DOI 10.1016/S1097-2765(00)80139-2
   Han KH, 1999, J LIPID RES, V40, P1053
   Han KH, 1998, ARTERIOSCL THROM VAS, V18, P1983, DOI 10.1161/01.ATV.18.12.1983
   Han KH, 2000, TRENDS CARDIOVAS MED, V10, P209, DOI 10.1016/S1050-1738(00)00076-1
   Han KH, 2000, J CLIN INVEST, V106, P793, DOI 10.1172/JCI10052
   Law RE, 2000, CIRCULATION, V101, P1311, DOI 10.1161/01.CIR.101.11.1311
   Li AC, 2000, J CLIN INVEST, V106, P523, DOI 10.1172/JCI10370
   Minamikawa J, 1998, J CLIN ENDOCR METAB, V83, P1818, DOI 10.1210/jc.83.5.1818
   Mummidi S, 1997, J BIOL CHEM, V272, P30662, DOI 10.1074/jbc.272.49.30662
   Ricote M, 1998, P NATL ACAD SCI USA, V95, P7614, DOI 10.1073/pnas.95.13.7614
   ROSENFELD ME, 1987, ARTERIOSCLEROSIS, V7, P24, DOI 10.1161/01.ATV.7.1.24
   Tangirala RK, 1997, J BIOL CHEM, V272, P8050, DOI 10.1074/jbc.272.12.8050
   Yamamoto K, 1999, J BIOL CHEM, V274, P4646, DOI 10.1074/jbc.274.8.4646
   YLAHERTTUALA S, 1991, P NATL ACAD SCI USA, V88, P5252, DOI 10.1073/pnas.88.12.5252
   Zimmermann N, 2000, BLOOD, V96, P2346
NR 24
TC 29
Z9 35
U1 0
U2 5
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0006-291X
EI 1090-2104
J9 BIOCHEM BIOPH RES CO
JI Biochem. Biophys. Res. Commun.
PD JUN 24
PY 2005
VL 332
IS 1
BP 188
EP 193
DI 10.1016/j.bbrc.2005.04.110
PG 6
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA 929OK
UT WOS:000229355200027
PM 15896316
DA 2025-04-10
ER

PT J
AU Rankin, J
   Ellard, S
AF Rankin, J.
   Ellard, S.
TI The laminopathies: a clinical review
SO CLINICAL GENETICS
LA English
DT Review
DE laminopathy; lamin A/C; LMNA; Emery Dreifuss; progeria
ID LAMIN A/C GENE; HUTCHINSON-GILFORD-PROGERIA; FAMILIAL PARTIAL
   LIPODYSTROPHY; DREIFUSS MUSCULAR-DYSTROPHY; CHARCOT-MARIE-TOOTH;
   ATYPICAL WERNERS-SYNDROME; DILATED CARDIOMYOPATHY; MANDIBULOACRAL
   DYSPLASIA; LMNA MUTATIONS; NUCLEAR LAMIN
AB The laminopathies are a diverse group of conditions caused by mutations in the LMNA gene (MIM*150330). LMNA encodes the nuclear envelope proteins lamin A and lamin C by utilization of an alternative splice site in exon 10. The human LMNA gene was identified in 1986 but it was another 13 years before it was found to be the causative gene for a disease, namely Emery Dreifuss muscular dystrophy. Since then, a further eight clearly defined phenotypes have been associated with LMNA mutations. The diversity of these phenotypes is striking with features such as premature ageing, axonal neuropathy, lipodystrophy and myopathy being seen. These phenotypes and the emerging genotype/phenotype correlations are the subject of this review.
C1 Royal Devon & Exeter NHS Fdn Trust, Dept Clin Genet, Exeter EX1 2ED, Devon, England.
   Royal Devon & Exeter NHS Fdn Trust, Dept Mol Genet, Exeter EX1 2ED, Devon, England.
   Peninsula Med Sch, Inst Biomed & Clin Sci, Exeter, Devon, England.
C3 University of Exeter; University of Exeter; University of Exeter
RP Rankin, J (corresponding author), Royal Devon & Exeter NHS Fdn Trust, Dept Clin Genet, Gladstone Rd, Exeter EX1 2ED, Devon, England.
EM julia.rankin@rdehc-tr.swest.nhs.uk
OI Ellard, Sian/0000-0002-7620-5526
CR Agarwal AK, 2003, HUM MOL GENET, V12, P1995, DOI 10.1093/hmg/ddg213
   Arbustini E, 2002, J AM COLL CARDIOL, V39, P981, DOI 10.1016/S0735-1097(02)01724-2
   Benedetti S, 2005, J NEUROL NEUROSUR PS, V76, P1019, DOI 10.1136/jnnp.2004.046110
   Bonne G, 2000, ANN NEUROL, V48, P170, DOI 10.1002/1531-8249(200008)48:2<170::AID-ANA6>3.0.CO;2-J
   Bonne G, 2003, LANCET, V362, P1585, DOI 10.1016/S0140-6736(03)14761-7
   Bonne G, 1999, NAT GENET, V21, P285, DOI 10.1038/6799
   Brodsky GL, 2000, CIRCULATION, V101, P473, DOI 10.1161/01.CIR.101.5.473
   Brown CA, 2001, AM J MED GENET, V102, P359, DOI 10.1002/ajmg.1463
   Bushby KMD, 1999, HUM MOL GENET, V8, P1875, DOI 10.1093/hmg/8.10.1875
   Cao H, 2000, HUM MOL GENET, V9, P109, DOI 10.1093/hmg/9.1.109
   Cao HN, 2003, J HUM GENET, V48, P271, DOI 10.1007/s10038-003-0025-3
   Caux F, 2003, J CLIN ENDOCR METAB, V88, P1006, DOI 10.1210/jc.2002-021506
   Chaouch M, 2003, NEUROMUSCULAR DISORD, V13, P60, DOI 10.1016/S0960-8966(02)00196-7
   Charniot JC, 2003, HUM MUTAT, V21, P473, DOI 10.1002/humu.10170
   Chen LS, 2003, LANCET, V362, P440, DOI 10.1016/S0140-6736(03)14069-X
   Clements L, 2000, BIOCHEM BIOPH RES CO, V267, P709, DOI 10.1006/bbrc.1999.2023
   Colomer J, 2002, NEUROMUSCULAR DISORD, V12, P19, DOI 10.1016/S0960-8966(01)00239-5
   Csoka AB, 2004, J MED GENET, V41, P304, DOI 10.1136/jmg.2003.015651
   D'Amico A, 2005, NEUROMUSCULAR DISORD, V15, P521, DOI 10.1016/j.nmd.2005.03.006
   D'Apice MR, 2004, CLIN GENET, V65, P52, DOI 10.1111/j..2004.00181.x
   De Sandre-Giovannoli A, 2003, SCIENCE, V300, P2055, DOI 10.1126/science.1084125
   De Sandre-Giovannoli A, 2002, AM J HUM GENET, V70, P726, DOI 10.1086/339274
   DEBUSK FL, 1972, J PEDIATR-US, V80, P697, DOI 10.1016/S0022-3476(72)80229-4
   di Barletta MR, 2000, AM J HUM GENET, V66, P1407, DOI 10.1086/302869
   Emery AEH, 2000, NEUROMUSCULAR DISORD, V10, P228, DOI 10.1016/S0960-8966(00)00105-X
   Emery AEH, 2002, LANCET, V359, P687, DOI 10.1016/S0140-6736(02)07815-7
   EMERY AEH, 1989, J MED GENET, V26, P637, DOI 10.1136/jmg.26.10.637
   Eriksson M, 2003, NATURE, V423, P293, DOI 10.1038/nature01629
   Fatkin D, 1999, NEW ENGL J MED, V341, P1715, DOI 10.1056/NEJM199912023412302
   Favreau C, 2004, MOL CELL BIOL, V24, P1481, DOI 10.1128/MCB.24.4.1481-1492.2004
   FISHER DZ, 1986, P NATL ACAD SCI USA, V83, P6450, DOI 10.1073/pnas.83.17.6450
   Fukuchi K, 2004, J MED GENET, V41, DOI 10.1136/jmg.2003.014688
   Garg A, 2005, J CLIN ENDOCR METAB, V90, P5259, DOI 10.1210/jc.2004-2560
   Garg A, 1999, J CLIN ENDOCR METAB, V84, P170, DOI 10.1210/jc.84.1.170
   Garg A, 2001, J CLIN ENDOCR METAB, V86, P59, DOI 10.1210/jc.86.1.59
   Genschel J, 2000, HUM MUTAT, V16, P451, DOI 10.1002/1098-1004(200012)16:6<451::AID-HUMU1>3.3.CO;2-0
   Glynn MW, 2005, HUM MOL GENET, V14, P2959, DOI 10.1093/hmg/ddi326
   Goizet C, 2004, J MED GENET, V41, DOI 10.1136/jmg.2003.013383
   Goldman RD, 2002, GENE DEV, V16, P533, DOI 10.1101/gad.960502
   Goldman RD, 2004, P NATL ACAD SCI USA, V101, P8963, DOI 10.1073/pnas.0402943101
   Hegele RA, 2000, J CLIN ENDOCR METAB, V85, P3431, DOI 10.1210/jc.85.9.3431
   Hegele RA, 2003, LANCET, V362, P416, DOI 10.1016/S0140-6736(03)14097-4
   Hermida-Prieto M, 2004, AM J CARDIOL, V94, P50, DOI 10.1016/j.amjcard.2004.03.029
   Holt I, 2003, J CELL SCI, V116, P3027, DOI 10.1242/jcs.00599
   Kärkkäinen S, 2004, EUR HEART J, V25, P885, DOI 10.1016/j.ehj.2004.01.020
   Kirschner J, 2005, ANN NEUROL, V57, P148, DOI 10.1002/ana.20359
   Lammerding J, 2004, J CLIN INVEST, V113, P370, DOI 10.1172/JCI200419670
   LIN F, 1993, J BIOL CHEM, V268, P16321
   Lüdtke A, 2005, AM J GASTROENTEROL, V100, P2218, DOI 10.1111/j.1572-0241.2005.00234.x
   Masny PS, 2004, HUM MOL GENET, V13, P1857, DOI 10.1093/hmg/ddh205
   Mau U, 1997, AM J MED GENET, V71, P179, DOI 10.1002/(SICI)1096-8628(19970808)71:2<179::AID-AJMG11>3.0.CO;2-B
   Mercuri E, 2005, MUSCLE NERVE, V31, P602, DOI 10.1002/mus.20293
   Mercuri E, 2004, ARCH NEUROL-CHICAGO, V61, P690, DOI 10.1001/archneur.61.5.690
   Mounkes LC, 2004, CURR OPIN CELL BIOL, V16, P322, DOI 10.1016/j.ceb.2004.03.009
   Muchir A, 2000, HUM MOL GENET, V9, P1453, DOI 10.1093/hmg/9.9.1453
   Navarro CL, 2004, HUM MOL GENET, V13, P2493, DOI 10.1093/hmg/ddh265
   Navarro CL, 2005, HUM MOL GENET, V14, P1503, DOI 10.1093/hmg/ddi159
   Nikolova V, 2004, J CLIN INVEST, V113, P357, DOI 10.1172/JCI200419448
   Novelli G, 2003, TRENDS MOL MED, V9, P370, DOI 10.1016/S1471-4914(03)00162-X
   Novelli G, 2002, AM J HUM GENET, V71, P426, DOI 10.1086/341908
   Plasilova M, 2004, J MED GENET, V41, P609, DOI 10.1136/jmg.2004.019661
   Reichart B, 2004, BMC CELL BIOL, V5, DOI 10.1186/1471-2121-5-12
   Sanna T, 2003, EUR HEART J, V24, P2227, DOI 10.1016/j.ehj.2003.09.020
   Sébillon P, 2003, J MED GENET, V40, P560, DOI 10.1136/jmg.40.8.560
   Sevenants L, 2005, EUR J PEDIATR, V164, P283, DOI 10.1007/s00431-005-1635-x
   Sewry CA, 2001, NEUROPATH APPL NEURO, V27, P281, DOI 10.1046/j.0305-1846.2001.00323.x
   Shackleton S, 2000, NAT GENET, V24, P153, DOI 10.1038/72807
   Shackleton S, 2005, J MED GENET, V42, DOI 10.1136/jmg.2004.029751
   Shen JJ, 2003, J MED GENET, V40, P854, DOI 10.1136/jmg.40.11.854
   Simha V, 2003, J CLIN ENDOCR METAB, V88, P2821, DOI 10.1210/jc.2002-021575
   Simha V, 2002, J CLIN ENDOCR METAB, V87, P776, DOI 10.1210/jc.87.2.776
   Spann TP, 2002, J CELL BIOL, V156, P603, DOI 10.1083/jcb.200112047
   Speckman RA, 2000, AM J HUM GENET, V66, P1192, DOI 10.1086/302836
   Sullivan T, 1999, J CELL BIOL, V147, P913, DOI 10.1083/jcb.147.5.913
   Sylvius N, 2005, J MED GENET, V42, P639, DOI 10.1136/jmg.2004.023283
   Tazir M, 2004, BRAIN, V127, P154, DOI 10.1093/brain/awh021
   Toriello H V, 1995, Clin Dysmorphol, V4, P12
   Toth JI, 2005, P NATL ACAD SCI USA, V102, P12873, DOI 10.1073/pnas.0505767102
   van Berlo JH, 2005, J MOL MED, V83, P79, DOI 10.1007/s00109-004-0589-1
   van der Kooi AJ, 2002, NEUROLOGY, V59, P620, DOI 10.1212/WNL.59.4.620
   van Engelen BGM, 2005, NEUROLOGY, V64, P374, DOI 10.1212/01.WNL.0000149763.15180.00
   Van Esch H, 2006, J CLIN ENDOCR METAB, V91, P517, DOI 10.1210/jc.2005-1297
   Vantyghem MC, 2004, J CLIN ENDOCR METAB, V89, P5337, DOI 10.1210/jc.2003-031658
   Vigouroux C, 2000, DIABETES, V49, P1958, DOI 10.2337/diabetes.49.11.1958
   Vigouroux C, 2003, LANCET, V362, P1585, DOI 10.1016/S0140-6736(03)14760-5
   Vigouroux C, 2001, J CELL SCI, V114, P4459
   Vytopil M, 2003, J MED GENET, V40, DOI 10.1136/jmg.40.12.e132
   Vytopil M, 2002, NEUROMUSCULAR DISORD, V12, P958, DOI 10.1016/S0960-8966(02)00178-5
   Walter MC, 2005, NEUROMUSCULAR DISORD, V15, P40, DOI 10.1016/j.nmd.2004.09.007
   Worman HJ, 2004, J CLIN INVEST, V113, P349, DOI 10.1172/JCI200420832
   Wuyts W, 2005, AM J MED GENET A, V135A, P66, DOI 10.1002/ajmg.a.30663
   Young J, 2005, DIABETES, V54, P1873, DOI 10.2337/diabetes.54.6.1873
NR 92
TC 139
Z9 160
U1 0
U2 9
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0009-9163
EI 1399-0004
J9 CLIN GENET
JI Clin. Genet.
PD OCT
PY 2006
VL 70
IS 4
BP 261
EP 274
DI 10.1111/j.1399-0004.2006.00677.x
PG 14
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA 081JB
UT WOS:000240312600001
PM 16965317
DA 2025-04-10
ER

PT J
AU Lynch, M
   Barallobre-Barreiro, J
   Jahangiri, M
   Mayr, M
AF Lynch, M.
   Barallobre-Barreiro, J.
   Jahangiri, M.
   Mayr, M.
TI Vascular proteomics in metabolic and cardiovascular diseases
SO JOURNAL OF INTERNAL MEDICINE
LA English
DT Review
DE apolipoproteins; atherosclerosis; diabetes; proteomics; restenosis;
   vascular biology
ID SMOOTH-MUSCLE-CELLS; ISCHEMIC-HEART-DISEASE; HIGH-RISK PATIENTS;
   EXTRACELLULAR-MATRIX; ATHEROSCLEROTIC PLAQUES; REMNANT CHOLESTEROL;
   GLYCOSYLATION SITES; CHONDROITIN SULFATE; N-GLYCOSYLATION; III
   PROCOLLAGEN
AB The vasculature is essential for proper organ function. Many pathologies are directly and indirectly related to vascular dysfunction, which causes significant morbidity and mortality. A common pathophysiological feature of diseased vessels is extracellular matrix (ECM) remodelling. Analysing the protein composition of the ECM by conventional antibody-based techniques is challenging; alternative splicing or post-translational modifications, such as glycosylation, can mask epitopes required for antibody recognition. By contrast, proteomic analysis by mass spectrometry enables the study of proteins without the constraints of antibodies. Recent advances in proteomic techniques make it feasible to characterize the composition of the vascular ECM and its remodelling in disease. These developments may lead to the discovery of novel prognostic and diagnostic markers. Thus, proteomics holds potential for identifying ECM signatures to monitor vascular disease processes. Furthermore, a better understanding of the ECM remodelling processes in the vasculature might make ECM-associated proteins more attractive targets for drug discovery efforts. In this review, we will summarize the role of the ECM in the vasculature. Then, we will describe the challenges associated with studying the intricate network of ECM proteins and the current proteomic strategies to analyse the vascular ECM in metabolic and cardiovascular diseases.
C1 [Lynch, M.; Barallobre-Barreiro, J.; Mayr, M.] Kings Coll London, Kings British Heart Fdn Ctr, 125 Coldharbour Lane, London SE5 9NU, England.
   [Jahangiri, M.] NHS Trust, St Georges Hosp, London, England.
C3 University of London; King's College London; City St Georges, University
   of London
RP Mayr, M (corresponding author), Kings Coll London, Kings British Heart Fdn Ctr, 125 Coldharbour Lane, London SE5 9NU, England.
EM manuel.mayr@kcl.ac.uk
RI BARALLOBRE-BARREIRO, JAVIER/B-7992-2013
OI Mayr, Manuel/0000-0002-0597-829X; Barallobre-Barreiro,
   Javier/0000-0001-6236-2304
FU British Heart Foundation (BHF); Foundation Leducq (MIRVAD) [13 CVD 02];
   excellence initiative [(Competence Centers for Excellent Technologies
   (COMET)] of the Austrian Research Promotion Agency FFG: 'Research Center
   of Excellence in Vascular Ageing - Tyrol, VASCage' (K-Project) [843536];
   National Institute of Health Research (NIHR) Biomedical Research Centre
   based at Guy's and St Thomas' NHS Foundation Trust and King's College
   London; King's College Hospital; Heart Research UK [RG2630/13/15];
   Diabetes UK [12/0004530]
FX ML has been awarded a British Heart Foundation (BHF) PhD studentship. MM
   is a Senior Fellow of the BHF (FS/13/2/29892) and member of the network
   on 'MicroRNA-based Therapeutic Strategies in Vascular Disease' funded by
   the Foundation Leducq (MIRVAD; 13 CVD 02) and an excellence initiative
   [(Competence Centers for Excellent Technologies (COMET)] of the Austrian
   Research Promotion Agency FFG: 'Research Center of Excellence in
   Vascular Ageing - Tyrol, VASCage' (K-Project number 843536). The
   research was funded/supported by the National Institute of Health
   Research (NIHR) Biomedical Research Centre based at Guy's and St Thomas'
   NHS Foundation Trust and King's College London in partnership with
   King's College Hospital, Diabetes UK (12/0004530) and Heart Research UK
   (RG2630/13/15).
CR Aebersold R, 2003, NATURE, V422, P198, DOI 10.1038/nature01511
   Ameye L, 2002, GLYCOBIOLOGY, V12, p107R, DOI 10.1093/glycob/cwf065
   Barallobre-Barreiro J, 2012, CIRCULATION, V125, P789, DOI 10.1161/CIRCULATIONAHA.111.056952
   Barascuk N, 2013, INT J CLIN EXP MED, V6, P174
   BAUSE E, 1983, BIOCHEM J, V209, P331, DOI 10.1042/bj2090331
   BELZ GG, 1995, CARDIOVASC DRUG THER, V9, P73, DOI 10.1007/BF00877747
   Blankenberg S, 2003, CIRCULATION, V107, P1579, DOI 10.1161/01.CIR.0000058700.41738.12
   Boja ES, 2012, PROTEOMICS, V12, P1093, DOI 10.1002/pmic.201100387
   Bonnans C, 2014, NAT REV MOL CELL BIO, V15, P786, DOI 10.1038/nrm3904
   BONNET J, 1988, EUR J CLIN INVEST, V18, P18, DOI 10.1111/j.1365-2362.1988.tb01159.x
   Brachvogel B, 2013, J BIOL CHEM, V288, P13481, DOI 10.1074/jbc.M112.444810
   Brás LED, 2013, J PROTEOMICS, V86, P43, DOI 10.1016/j.jprot.2013.05.004
   Brodsky B, 2005, ADV PROTEIN CHEM, V70, P301, DOI 10.1016/S0065-3233(05)70009-7
   Brooke BS, 2008, NEW ENGL J MED, V358, P2787, DOI 10.1056/NEJMoa0706585
   Cassidy-Bushrow AE, 2013, ARTERIOSCL THROM VAS, V33, P645, DOI 10.1161/ATVBAHA.112.300491
   Cattaruzza Sabrina, 2004, FASEB J, V18, P779
   Cavusoglu E, 2006, AM HEART J, V151, DOI 10.1016/j.ahj.2006.02.029
   Chen YT, 2015, ANAL CHEM, V87, P545, DOI 10.1021/ac5033066
   Cheng XW, 2013, ATHEROSCLEROSIS, V228, P211, DOI 10.1016/j.atherosclerosis.2013.01.004
   Dalpathado DS, 2008, ANALYST, V133, P731, DOI 10.1039/b713816d
   de Kleijn DPV, 2010, ARTERIOSCL THROM VAS, V30, P612, DOI 10.1161/ATVBAHA.109.194944
   Decaris ML, 2014, MOL CELL PROTEOMICS, V13, P1741, DOI 10.1074/mcp.M113.037267
   Didangelos A, 2012, J BIOL CHEM, V287, P19341, DOI 10.1074/jbc.C112.350785
   Didangelos A, 2012, ATHEROSCLEROSIS, V221, P12, DOI 10.1016/j.atherosclerosis.2011.09.043
   Didangelos A, 2011, MOL CELL PROTEOMICS, V10, DOI 10.1074/mcp.M111.008128
   Didangelos A, 2010, MOL CELL PROTEOMICS, V9, P2048, DOI 10.1074/mcp.M110.001693
   Didangelos A, 2009, CURR ATHEROSCLER REP, V11, P188, DOI 10.1007/s11883-009-0030-x
   DIETZ HC, 1991, NATURE, V352, P337, DOI 10.1038/352337a0
   Dunér P, 2015, ATHEROSCLEROSIS, V240, P26, DOI 10.1016/j.atherosclerosis.2015.02.043
   Furman C, 2002, FEBS LETT, V531, P122, DOI 10.1016/S0014-5793(02)03388-4
   Galis ZS, 2002, CIRC RES, V90, P251, DOI 10.1161/res.90.3.251
   Geary RL, 2002, ARTERIOSCL THROM VAS, V22, P2010, DOI 10.1161/01.ATV.0000038147.93527.35
   Ghaderian SMH, 2012, INT J MOL CELL MED, V1, P50
   GIBBONS GH, 1994, NEW ENGL J MED, V330, P1431
   Goldin A, 2006, CIRCULATION, V114, P597, DOI 10.1161/CIRCULATIONAHA.106.621854
   Goncalves I, 2015, ARTERIOSCL THROM VAS, V35, P1723, DOI 10.1161/ATVBAHA.115.305631
   Goodman SL, 2012, TRENDS PHARMACOL SCI, V33, P405, DOI 10.1016/j.tips.2012.04.002
   Hakuno D, 2010, J CLIN INVEST, V120, P2292, DOI 10.1172/JCI40973
   Hansen ML, 2015, ARTERIOSCL THROM VAS, V35, P1896, DOI 10.1161/ATVBAHA.114.304706
   Hellenthal FAMVI, 2009, NAT REV CARDIOL, V6, P464, DOI 10.1038/nrcardio.2009.80
   HENNEY AM, 1991, P NATL ACAD SCI USA, V88, P8154, DOI 10.1073/pnas.88.18.8154
   HERRING GM, 1968, BIOCHEM J, V107, P41, DOI 10.1042/bj1070041
   Hinterwirth H, 2014, CIRC-CARDIOVASC GENE, V7, P941, DOI 10.1161/CIRCGENETICS.114.000550
   Hocking AM, 1998, MATRIX BIOL, V17, P1
   Hutter R, 2013, CIRCULATION, V128, P2351, DOI 10.1161/CIRCULATIONAHA.113.004634
   Hynes RO, 2012, CSH PERSPECT BIOL, V4, DOI 10.1101/cshperspect.a004903
   Iozzo RV, 2015, MATRIX BIOL, V42, P11, DOI 10.1016/j.matbio.2015.02.003
   Iozzo RV, 1999, J BIOL CHEM, V274, P18843, DOI 10.1074/jbc.274.27.18843
   Iozzo RV, 2005, NAT REV MOL CELL BIO, V6, P646, DOI 10.1038/nrm1702
   Järveläinen H, 2009, PHARMACOL REV, V61, P198, DOI 10.1124/pr.109.001289
   Jeremy JY, 2007, BIOMATERIALS, V28, P895, DOI 10.1016/j.biomaterials.2006.10.023
   Johnson JL, 2005, P NATL ACAD SCI USA, V102, P15575, DOI 10.1073/pnas.0506201102
   Jönnsson-Rylander AC, 2005, ARTERIOSCL THROM VAS, V25, P180, DOI 10.1161/01.ATV.0000150045.27127.37
   Jorgensen AB, 2014, NEW ENGL J MED, V371, P32, DOI 10.1056/NEJMoa1308027
   Kadler KE, 2007, J CELL SCI, V120, P1955, DOI 10.1242/jcs.03453
   Kalluri R, 2003, NAT REV CANCER, V3, P422, DOI 10.1038/nrc1094
   Kam R.K., 2008, Clinical Proteomics, V4, P67, DOI DOI 10.1007/S12014-008-9017-9
   Kirsch D, 2000, VASA-J VASCULAR DIS, V29, P173, DOI 10.1024/0301-1526.29.3.173
   Kivirikko KI, 1998, MATRIX BIOL, V16, P357, DOI 10.1016/S0945-053X(98)90009-9
   KIVIRIKKO KI, 1990, ANN NY ACAD SCI, V580, P132, DOI 10.1111/j.1749-6632.1990.tb17925.x
   Küster B, 1999, ANAL CHEM, V71, P1431, DOI 10.1021/ac981012u
   Lehrke M, 2009, CARDIOVASC DIABETOL, V8, DOI 10.1186/1475-2840-8-50
   Luttun A, 2004, CIRCULATION, V109, P1408, DOI 10.1161/01.CIR.0000121728.14930.DE
   Maiolino G, 2015, ARTERIOSCL THROM VAS, V35, P725, DOI 10.1161/ATVBAHA.114.304964
   Majerus EM, 2003, J BIOL CHEM, V278, P46643, DOI 10.1074/jbc.M309872200
   Malemud CJ, 2006, FRONT BIOSCI-LANDMRK, V11, P1696, DOI 10.2741/1915
   Martinez-Aguilar E, 2015, J VASC SURG, V61, P428, DOI 10.1016/j.jvs.2014.09.002
   Matter CM, 2004, CIRC RES, V95, P1225, DOI 10.1161/01.RES.0000150373.15149.ff
   Merline R, 2009, J CELL COMMUN SIGNAL, V3, P323, DOI 10.1007/s12079-009-0066-2
   Minear MA, 2011, HUM GENET, V129, P641, DOI 10.1007/s00439-011-0959-z
   Moiseeva EP, 2001, CARDIOVASC RES, V52, P372, DOI 10.1016/S0008-6363(01)00399-6
   Mongiat M, 2003, J BIOL CHEM, V278, P4238, DOI 10.1074/jbc.M210445200
   Mouw JK, 2014, NAT REV MOL CELL BIO, V15, P771, DOI 10.1038/nrm3902
   Naba A, 2016, MATRIX BIOL, V49, P10, DOI 10.1016/j.matbio.2015.06.003
   Naba A, 2012, MOL CELL PROTEOMICS, V11, DOI 10.1074/mcp.M111.014647
   Nakashima Y, 2007, ARTERIOSCL THROM VAS, V27, P1159, DOI 10.1161/ATVBAHA.106.134080
   Newby AC, 2006, CARDIOVASC RES, V69, P614, DOI 10.1016/j.cardiores.2005.08.002
   Newby AC, 2012, VASC PHARMACOL, V56, P232, DOI 10.1016/j.vph.2012.01.007
   O'Brien KD, 1998, CIRCULATION, V98, P519, DOI 10.1161/01.CIR.98.6.519
   Palmisano G, 2012, J PROTEOME RES, V11, P1949, DOI 10.1021/pr2011268
   Parker BL, 2011, MOL CELL PROTEOMICS, V10, DOI 10.1074/mcp.M110.006833
   Petersen E, 2002, EUR J VASC ENDOVASC, V24, P440, DOI 10.1053/ejvs.2002.1750
   Peterson JT, 2006, CARDIOVASC RES, V69, P677, DOI 10.1016/j.cardiores.2005.11.032
   Pfisterer L, 2014, VASA, V43, P88, DOI 10.1024/0301-1526/a000335
   Phuc Vinh Nguyen Lam, 2013, Genomics Proteomics & Bioinformatics, V11, P96, DOI 10.1016/j.gpb.2012.11.003
   Picotti P, 2012, NAT METHODS, V9, P555, DOI [10.1038/NMETH.2015, 10.1038/nmeth.2015]
   Pokidysheva E, 2014, P NATL ACAD SCI USA, V111, P161, DOI 10.1073/pnas.1307597111
   Ponticos M, 2014, J BIOMED RES, V28, P25, DOI 10.7555/JBR.27.20130064
   Porter S, 2005, BIOCHEM J, V386, P15, DOI 10.1042/BJ20040424
   Poulsen SH, 2000, CIRCULATION, V101, P1527, DOI 10.1161/01.CIR.101.13.1527
   Preil SAR, 2015, CIRC-CARDIOVASC GENE, V8, P727, DOI 10.1161/CIRCGENETICS.115.001165
   Reinboth B, 2002, J BIOL CHEM, V277, P3950, DOI 10.1074/jbc.M109540200
   Rekhter MD, 1999, CARDIOVASC RES, V41, P376, DOI 10.1016/S0008-6363(98)00321-6
   Roy R, 2009, J CLIN ONCOL, V27, P5287, DOI 10.1200/JCO.2009.23.5556
   Shami A, 2015, ATHEROSCLEROSIS, V241, P701, DOI 10.1016/j.atherosclerosis.2015.06.023
   Shriver Z, 2004, NAT REV DRUG DISCOV, V3, P863, DOI 10.1038/nrd1521
   Siow RCM, 2007, CARDIOVASC RES, V75, P659, DOI 10.1016/j.cardiores.2007.06.007
   Somerville RPT, 2004, J BIOL CHEM, V279, P35159, DOI 10.1074/jbc.M402380200
   Stegemann C, 2014, CIRCULATION, V129, P1821, DOI 10.1161/CIRCULATIONAHA.113.002500
   Stegemann C, 2013, CIRC-CARDIOVASC GENE, V6, P106, DOI 10.1161/CIRCGENETICS.112.964452
   Stegemann C, 2011, CIRC-CARDIOVASC GENE, V4, P232, DOI 10.1161/CIRCGENETICS.110.959098
   Talusan P, 2005, MOL CELL PROTEOMICS, V4, P1350, DOI 10.1074/mcp.M500088-MCP200
   The TG and HDL working group of the Exome Sequencing Project NHLBI., 2014, NEW ENGL J MED, V371, P22, DOI [10.1056/NEJMoa1307095, DOI 10.1056/NEJMOA1307095]
   Varbo A, 2014, PHARMACOL THERAPEUT, V141, P358, DOI 10.1016/j.pharmthera.2013.11.008
   Varbo A, 2013, CIRCULATION, V128, P1298, DOI 10.1161/CIRCULATIONAHA.113.003008
   Varki A., 2009, ESSENTIALS GLYCOBIOL, V2nd, P1
   Wagenseil JE, 2009, PHYSIOL REV, V89, P957, DOI 10.1152/physrev.00041.2008
   Wang J, 2014, BBA-MOL BASIS DIS, V1842, P2174, DOI 10.1016/j.bbadis.2014.07.026
   Wang ML, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0053236
   Wight TN, 2004, CIRC RES, V94, P1158, DOI 10.1161/01.RES.0000126921.29919.51
   Wight TN, 2002, CURR OPIN CELL BIOL, V14, P617, DOI 10.1016/S0955-0674(02)00375-7
   WILLIAMS KJ, 1995, ARTERIOSCL THROM VAS, V15, P551, DOI 10.1161/01.ATV.15.5.551
   Yin XK, 2013, MOL CELL PROTEOMICS, V12, P956, DOI 10.1074/mcp.M112.024018
NR 113
TC 41
Z9 46
U1 0
U2 16
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0954-6820
EI 1365-2796
J9 J INTERN MED
JI J. Intern. Med.
PD OCT
PY 2016
VL 280
IS 4
BP 325
EP 338
DI 10.1111/joim.12486
PG 14
WC Medicine, General & Internal
WE Science Citation Index Expanded (SCI-EXPANDED)
SC General & Internal Medicine
GA EA8VI
UT WOS:000386917000001
PM 26940365
OA Green Accepted, Green Published, hybrid
DA 2025-04-10
ER

PT J
AU Zachary, I
AF Zachary, I
TI Vascular endothelial growth factor
SO INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
LA English
DT Article
DE angiogenesis; signal transduction; receptor tyrosine kinase; Flk-l;
   endothelium
ID GENE-TRANSFER; NITRIC-OXIDE; ANGIOGENESIS; KINASE; ACTIVATION
AB Vascular endothelial growth factor (VEGF) plays a crucial role in angiogenesis in development, in cancer and in other important diseases. VEGF regulates multiple endothelial cell functions including mitogenesis, permeability, vascular tone, and the production of vasoactive molecules. VEGF is related to several polypeptides which may have different and overlapping functions. The synthesis of VEGF is regulated by hypoxia-mediated control of gene transcription, alternative mRNA splicing and proteolytic processing. The diverse biological activities of VEGF are mediated through at least two receptor protein tyrosine kinases, KDR/Flk-1 and Flt-1. Because of VEGF's central importance for pathophysiological angiogenesis, he development of antagonists for VEGF in the treatment of cancer, and the use of VEGF therapeutically in cardiovascular diseases are now the focus of major research efforts. (C)) 1998 Elsevier Science Ltd. All rights reserved.
C1 Univ London Univ Coll, Wolfson Inst Biomed Res, London WC1E 6JJ, England.
   Univ London Univ Coll, Dept Med, London WC1E 6JJ, England.
C3 University of London; University College London; University of London;
   University College London
RP Zachary, I (corresponding author), Univ London Univ Coll, Wolfson Inst Biomed Res, 5 Univ St, London WC1E 6JJ, England.
CR Abedi H, 1997, J BIOL CHEM, V272, P15442, DOI 10.1074/jbc.272.24.15442
   Asahara T, 1996, CIRCULATION, V94, P3291, DOI 10.1161/01.CIR.94.12.3291
   Carmeliet P, 1996, NATURE, V380, P435, DOI 10.1038/380435a0
   Clauss M, 1996, J BIOL CHEM, V271, P17629, DOI 10.1074/jbc.271.30.17629
   Ferrara N, 1996, EUR J CANCER, V32A, P2413, DOI 10.1016/S0959-8049(96)00387-5
   FERRARA N, 1992, ENDOCR REV, V13, P18, DOI 10.1210/er.13.1.18
   FOLKMAN J, 1995, NAT MED, V1, P27, DOI 10.1038/nm0195-27
   Jeltsch M, 1997, SCIENCE, V276, P1423, DOI 10.1126/science.276.5317.1423
   Laitinen M, 1997, HUM GENE THER, V8, P1737, DOI 10.1089/hum.1997.8.15-1737
   MILLAUER B, 1994, NATURE, V367, P576, DOI 10.1038/367576a0
   Muller YA, 1997, P NATL ACAD SCI USA, V94, P7192, DOI 10.1073/pnas.94.14.7192
   PLATE KH, 1992, NATURE, V359, P845, DOI 10.1038/359845a0
   Plouet J, 1997, J BIOL CHEM, V272, P13390, DOI 10.1074/jbc.272.20.13390
   Poltorak Z, 1997, J BIOL CHEM, V272, P7151, DOI 10.1074/jbc.272.11.7151
   Risau W, 1997, NATURE, V386, P671, DOI 10.1038/386671a0
   SHWEIKI D, 1992, NATURE, V359, P843, DOI 10.1038/359843a0
   Soker S, 1998, CELL, V92, P735, DOI 10.1016/S0092-8674(00)81402-6
   STAVRI G, 1995, CIRCULATION, V92, P5
   vanderZee R, 1997, CIRCULATION, V95, P1030
   WALTENBERGER J, 1994, J BIOL CHEM, V269, P26988
   Wheeler-Jones C, 1997, FEBS LETT, V420, P28, DOI 10.1016/S0014-5793(97)01481-6
   Xia P, 1996, J CLIN INVEST, V98, P2018, DOI 10.1172/JCI119006
NR 22
TC 99
Z9 116
U1 1
U2 6
PU PERGAMON-ELSEVIER SCIENCE LTD
PI OXFORD
PA THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND
SN 1357-2725
J9 INT J BIOCHEM CELL B
JI Int J. Biochem. Cell Biol.
PD NOV
PY 1998
VL 30
IS 11
BP 1169
EP 1174
DI 10.1016/S1357-2725(98)00082-X
PG 6
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA 139HA
UT WOS:000077021400004
PM 9839443
DA 2025-04-10
ER

PT J
AU Osborne, RJ
   Lin, XY
   Welle, S
   Sobczak, K
   O'Rourke, JR
   Swanson, MS
   Thornton, CA
AF Osborne, Robert J.
   Lin, Xiaoyan
   Welle, Stephen
   Sobczak, Krzysztof
   O'Rourke, Jason R.
   Swanson, Maurice S.
   Thornton, Charles A.
TI Transcriptional and post-transcriptional impact of toxic RNA in myotonic
   dystrophy
SO HUMAN MOLECULAR GENETICS
LA English
DT Article
ID CARDIAC-SPECIFIC OVEREXPRESSION; RETICULUM CALCIUM-TRANSPORT;
   SKELETAL-MUSCLE; CTG REPEAT; TRINUCLEOTIDE REPEAT; MOLECULAR-BASIS;
   MESSENGER-RNA; MOUSE MODELS; PROTEIN; SARCOLIPIN
AB Myotonic dystrophy type 1 (DM1) is an RNA dominant disease in which mutant transcripts containing an expanded CUG repeat (CUG(exp)) cause muscle dysfunction by interfering with biogenesis of other mRNAs. The toxic effects of mutant RNA are mediated partly through sequestration of splicing regulator Muscleblind-like 1 (Mbnl1), a protein that binds to CUG(exp) RNA. A gene that is prominently affected encodes chloride channel 1 (Clcn1), resulting in hyperexcitability of muscle (myotonia). To identify DM1-affected genes and study mechanisms for dysregulation, we performed global mRNA profiling in transgenic mice that express CUG(exp) RNA, when compared with Mbnl1 knockout and Clcn1 null mice. We found that the majority of changes induced by CUG(exp) RNA in skeletal muscle can be explained by reduced activity of Mbnl1, including many changes that are secondary to myotonia. The pathway most affected comprises genes involved in calcium signaling and homeostasis. Some effects of CUG(exp) RNA on gene expression are caused by abnormal alternative splicing or downregulation of Mbnl1-interacting mRNAs. However, several of the most highly dysregulated genes showed altered transcription, as indicated by parallel changes of the corresponding pre-mRNAs. These results support the idea that trans-dominant effects of CUG(exp) RNA on gene expression in this transgenic model may occur at the level of transcription, RNA processing and mRNA decay, and are mediated mainly but not entirely through sequestration of Mbnl1.
C1 [Osborne, Robert J.; Lin, Xiaoyan; Sobczak, Krzysztof; Thornton, Charles A.] Univ Rochester, Sch Med & Dent, Dept Neurol, Rochester, NY 14642 USA.
   [Welle, Stephen] Univ Rochester, Sch Med & Dent, Dept Med, Rochester, NY 14642 USA.
   [O'Rourke, Jason R.; Swanson, Maurice S.] Univ Florida, Coll Med, Genet Inst, Dept Mol Genet & Microbiol, Gainesville, FL USA.
C3 University of Rochester; University of Rochester; State University
   System of Florida; University of Florida
RP Thornton, CA (corresponding author), Box 673 URMC,601 Elmwood Ave, Rochester, NY 14642 USA.
EM charles_thornton@urmc.rochester.edu
RI sobczak, kamil/D-9543-2011
OI Swanson, Maurice/0000-0001-6245-5367; Sobczak,
   Krzysztof/0000-0001-8352-9812
FU National Institutes of Health [AR046806, U54NS48843, AR48143]; Run
   America Foundation; Saunders Family Neuromuscular Research Fund
FX This work was supported by the National Institutes of Health (AR046806,
   U54NS48843, AR48143), the Run America Foundation and the Saunders Family
   Neuromuscular Research Fund.
CR Adereth Y, 2005, NAT CELL BIOL, V7, P1240, DOI 10.1038/ncb1335
   Asahi M, 2004, P NATL ACAD SCI USA, V101, P9199, DOI 10.1073/pnas.0402596101
   ASHIZAWA T, 1993, NEUROLOGY, V43, P2674, DOI 10.1212/WNL.43.12.2674
   Babu GJ, 2006, J BIOL CHEM, V281, P3972, DOI 10.1074/jbc.M508998200
   Babu GJ, 2007, P NATL ACAD SCI USA, V104, P17867, DOI 10.1073/pnas.0707722104
   BROOK JD, 1992, CELL, V68, P799, DOI 10.1016/0092-8674(92)90154-5
   Calvano SE, 2005, NATURE, V437, P1032, DOI 10.1038/nature03985
   Charlet-B N, 2002, MOL CELL, V10, P45, DOI 10.1016/S1097-2765(02)00572-5
   Davis BM, 1997, P NATL ACAD SCI USA, V94, P7388, DOI 10.1073/pnas.94.14.7388
   Ebralidze A, 2004, SCIENCE, V303, P383, DOI 10.1126/science.1088679
   Fardaei M, 2002, HUM MOL GENET, V11, P805, DOI 10.1093/hmg/11.7.805
   GALLANTI A, 1992, ACTA NEUROPATHOL, V85, P88, DOI 10.1007/BF00304637
   Gramolini AO, 2006, P NATL ACAD SCI USA, V103, P2446, DOI 10.1073/pnas.0510883103
   Hamshere MG, 1997, P NATL ACAD SCI USA, V94, P7394, DOI 10.1073/pnas.94.14.7394
   Haslett JN, 2005, MAMM GENOME, V16, P739, DOI 10.1007/s00335-005-0053-8
   Ho TH, 2004, EMBO J, V23, P3103, DOI 10.1038/sj.emboj.7600300
   Hong CS, 2007, BIOCHEM BIOPH RES CO, V362, P1, DOI 10.1016/j.bbrc.2007.07.166
   Hosack DA, 2003, GENOME BIOL, V4, DOI 10.1186/gb-2003-4-10-r70
   Kanadia RN, 2006, P NATL ACAD SCI USA, V103, P11748, DOI 10.1073/pnas.0604970103
   Kanadia RN, 2003, SCIENCE, V302, P1978, DOI 10.1126/science.1088583
   Kimura T, 2005, HUM MOL GENET, V14, P2189, DOI 10.1093/hmg/ddi223
   Krol J, 2007, MOL CELL, V25, P575, DOI 10.1016/j.molcel.2007.01.031
   Kuyumcu-Martinez NM, 2007, MOL CELL, V28, P68, DOI 10.1016/j.molcel.2007.07.027
   Lin XY, 2006, HUM MOL GENET, V15, P2087, DOI 10.1093/hmg/ddl132
   Lueck JD, 2007, AM J PHYSIOL-CELL PH, V292, pC1291, DOI 10.1152/ajpcell.00336.2006
   Lueck JD, 2007, J GEN PHYSIOL, V129, P79, DOI 10.1085/jgp.200609635
   Mankodi A, 2000, SCIENCE, V289, P1769, DOI 10.1126/science.289.5485.1769
   Mankodi A, 2002, MOL CELL, V10, P35, DOI 10.1016/S1097-2765(02)00563-4
   Miller JW, 2000, EMBO J, V19, P4439, DOI 10.1093/emboj/19.17.4439
   Orengo JP, 2008, P NATL ACAD SCI USA, V105, P2646, DOI 10.1073/pnas.0708519105
   Osborne RJ, 2006, HUM MOL GENET, V15, pR162, DOI 10.1093/hmg/ddl181
   Paul S, 2006, EMBO J, V25, P4271, DOI 10.1038/sj.emboj.7601296
   PETTE D, 1992, REV PHYSIOL BIOCH P, V120, P115, DOI 10.1007/BFb0036123
   Philips AV, 1998, SCIENCE, V280, P737, DOI 10.1126/science.280.5364.737
   REININGHAUS J, 1988, MUSCLE NERVE, V11, P433, DOI 10.1002/mus.880110504
   Risheg H, 2007, NAT GENET, V39, P451, DOI 10.1038/ng1992
   Savkur RS, 2001, NAT GENET, V29, P40, DOI 10.1038/ng704
   SILVERMAN H, 1980, EXP NEUROL, V68, P97, DOI 10.1016/0014-4886(80)90069-2
   SOOTHILL PW, 1981, J NEUROCHEM, V37, P506, DOI 10.1111/j.1471-4159.1981.tb00484.x
   Stamm S, 2006, NUCLEIC ACIDS RES, V34, pD46, DOI 10.1093/nar/gkj031
   Subramanian A, 2005, P NATL ACAD SCI USA, V102, P15545, DOI 10.1073/pnas.0506580102
   TANEJA KL, 1995, J CELL BIOL, V128, P995, DOI 10.1083/jcb.128.6.995
   THORNTON CA, 1994, ANN NEUROL, V35, P104, DOI 10.1002/ana.410350116
   Tian B, 2000, RNA, V6, P79, DOI 10.1017/S1355838200991544
   Timchenko NA, 2001, MOL CELL BIOL, V21, P6927, DOI 10.1128/MCB.21.20.6927-6938.2001
   Tusher VG, 2001, P NATL ACAD SCI USA, V98, P5116, DOI 10.1073/pnas.091062498
   WANG JZ, 1995, HUM MOL GENET, V4, P599, DOI 10.1093/hmg/4.4.599
   Welle S, 1999, J APPL PHYSIOL, V86, P1220, DOI 10.1152/jappl.1999.86.4.1220
   Welle S, 2002, BMC BIOINFORMATICS, V3, DOI 10.1186/1471-2105-3-23
   WHALEN RG, 1990, DEV BIOL, V141, P24, DOI 10.1016/0012-1606(90)90099-5
   Wheeler TM, 2007, NEUROMUSCULAR DISORD, V17, P242, DOI 10.1016/j.nmd.2006.12.015
   Wheeler TM, 2007, J CLIN INVEST, V117, P3952, DOI 10.1172/JCI33355
   Wu H, 2002, J CLIN INVEST, V109, P1327, DOI 10.1172/JCI200215417
   Wu ZJ, 2004, NAT BIOTECHNOL, V22, P656, DOI 10.1038/nbt0604-656b
   Yadava RS, 2008, NAT GENET, V40, P61, DOI 10.1038/ng.2007.28
   Yuan Y, 2007, NUCLEIC ACIDS RES, V35, P5474, DOI 10.1093/nar/gkm601
   ZATZ M, 1995, HUM MOL GENET, V4, P401, DOI 10.1093/hmg/4.3.401
NR 57
TC 133
Z9 149
U1 0
U2 10
PU OXFORD UNIV PRESS
PI OXFORD
PA GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND
SN 0964-6906
EI 1460-2083
J9 HUM MOL GENET
JI Hum. Mol. Genet.
PD APR 15
PY 2009
VL 18
IS 8
BP 1471
EP 1481
DI 10.1093/hmg/ddp058
PG 11
WC Biochemistry & Molecular Biology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Genetics & Heredity
GA 428ZE
UT WOS:000264889800010
PM 19223393
OA Green Published, Bronze
DA 2025-04-10
ER

PT J
AU Wang, Z
   Chan, HW
   Gambarotta, G
   Smith, NJ
   Purdue, BW
   Pennisi, DJ
   Porrello, ER
   O'Brien, SL
   Reichelt, ME
   Thomas, WG
   Paravicini, TM
AF Wang, Zhen
   Chan, Hsiu-Wen
   Gambarotta, Giovanna
   Smith, Nicola J.
   Purdue, Brooke W.
   Pennisi, David J.
   Porrello, Enzo R.
   O'Brien, Shannon L.
   Reichelt, Melissa E.
   Thomas, Walter G.
   Paravicini, Tamara M.
TI Stimulation of the four isoforms of receptor tyrosine kinase ErbB4, but
   not ErbB1, confers cardiomyocyte hypertrophy
SO JOURNAL OF CELLULAR PHYSIOLOGY
LA English
DT Article
DE cardiomyocytes; epidermal growth factor receptors; hypertrophy;
   ventricular remodeling
ID GROWTH-FACTOR RECEPTOR; CARDIAC-HYPERTROPHY; EXPRESSION;
   TRANSACTIVATION; NEUREGULIN; SURVIVAL; HEART; RESPONSES; DEGRADATION;
   CLEAVAGE
AB Epidermal growth factor (EGF) receptors (ErbB1-ErbB4) promote cardiac development and growth, although the specific EGF ligands and receptor isoforms involved in growth/repair versus pathology remain undefined. We challenged ventricular cardiomyocytes with EGF-like ligands and observed that selective activation of ErbB4 (the receptor for neuregulin 1 [NRG1]), but not ErbB1 (the receptor for EGF, EGFR), stimulated hypertrophy. This lack of direct ErbB1-mediated hypertrophy occurred despite robust activation of extracellular-regulated kinase 1/2 (ERK) and protein kinase B. Hypertrophic responses to NRG1 were unaffected by the tyrosine kinase inhibitor (AG1478) at concentrations that are selective for ErbB1 over ErbB4. NRG1-induced cardiomyocyte enlargement was suppressed by small interfering RNA (siRNA) knockdown of ErbB4 and ErbB2, whereas ERK phosphorylation was only suppressed by ErbB4 siRNA. Four ErbB4 isoforms exist (JM-a/JM-b and CYT-1/CYT-2), generated by alternative splicing, and their expression declines postnatally and following cardiac hypertrophy. Silencing of all four isoforms in cardiomyocytes, using an ErbB4 siRNA, abrogated NRG1-induced hypertrophic promoter/reporter activity, which was rescued by coexpression of knockdown-resistant versions of the ErbB4 isoforms. Thus, ErbB4 confers cardiomyocyte hypertrophy to NRG1, and all four ErbB4 isoforms possess the capacity to mediate this effect.
C1 [Wang, Zhen; Purdue, Brooke W.; O'Brien, Shannon L.; Reichelt, Melissa E.; Thomas, Walter G.; Paravicini, Tamara M.] Univ Queensland, Fac Med, Sch Biomed Sci, Brisbane, Qld, Australia.
   [Chan, Hsiu-Wen] Univ Queensland, Sch Publ Hlth, Fac Med, Brisbane, Qld, Australia.
   [Gambarotta, Giovanna] Univ Torino, Dept Clin & Biol Sci, Turin, Italy.
   [Smith, Nicola J.] Univ New South Wales, Sch Med Sci, Fac Med, Sydney, NSW, Australia.
   [Pennisi, David J.] Queensland Univ Technol, Sch Biomed Sci, Inst Hlth & Biomed Innovat, Brisbane, Qld, Australia.
   [Porrello, Enzo R.] Murdoch Childrens Res Inst, Melbourne, Vic, Australia.
   [Porrello, Enzo R.] Univ Melbourne, Dept Physiol, Melbourne, Vic, Australia.
   [Paravicini, Tamara M.] RMIT Univ, Sch Hlth & Biomed Sci, Melbourne, Vic, Australia.
C3 University of Queensland; University of Queensland; University of Turin;
   University of New South Wales Sydney; Queensland University of
   Technology (QUT); Murdoch Children's Research Institute; University of
   Melbourne; Royal Melbourne Institute of Technology (RMIT)
RP Thomas, WG (corresponding author), Univ Queensland, Sch Biomed Sci, Brisbane, Qld 4072, Australia.
EM w.thomas@uq.edu.au
RI Gambarotta, Giovanna/I-8473-2012; Porrello, Enzo/G-9934-2012; O'Brien,
   Shannon/ISS-3083-2023; Chan, Hsiu-Wen/G-2665-2010; Reichelt,
   Melissa/C-9579-2014; Thomas, Walter/I-2208-2015
OI Smith, Nicola J/0000-0002-7247-9562; Reichelt,
   Melissa/0000-0002-5059-2046; Thomas, Walter/0000-0003-0685-2952;
   O'Brien, Shannon/0000-0003-3265-6998; Chan,
   Hsiu-Wen/0000-0003-1545-0488; Porrello, Enzo/0000-0001-6105-7463;
   Purdue, Brooke/0000-0001-7618-7180
FU National Health and Medical Research Council of Australia [1024726,
   1085996]; National Health and Medical Research Council of Australia
   [1085996] Funding Source: NHMRC
FX The authors thank Dr. Mona Nemer (University of Ottawa) for kindly
   providing the hypertrophic gene promoter luciferase reporter plasmids
   (MLC-2V, ANP-328, and cyclin D), Dr. Andrew Dunbar (formerly of GroPep
   Limited) for bovine betacelluin, Professor David Riese II (Auburn
   University) for neuregulin isoforms -2 alpha, -2 beta, -3 and -4, and
   Mr. James Goonan for constructing the short hairpin RNA plasmids for
   ErbB2 and ErbB4. The authors also gratefully acknowledge cardiac tissue
   provided by Professor Karen Moritz (University of Queensland). Contract
   grant sponsor National Health and Medical Research Council of Australia;
   Contract grant numbers 1024726 and 1085996 to Walter G. Thomas funded
   this study.
CR Anastassiadis T, 2011, NAT BIOTECHNOL, V29, P1039, DOI 10.1038/nbt.2017
   Asakura M, 2002, NAT MED, V8, P35, DOI 10.1038/nm0102-35
   Baliga RR, 1999, AM J PHYSIOL-HEART C, V277, pH2026, DOI 10.1152/ajpheart.1999.277.5.H2026
   Brandt MC, 2012, J AM COLL CARDIOL, V59, P901, DOI 10.1016/j.jacc.2011.11.034
   Burgess AW, 2008, GROWTH FACTORS, V26, P263, DOI 10.1080/08977190802312844
   D'Uva G, 2015, NAT CELL BIOL, V17, P627, DOI 10.1038/ncb3149
   Djurovic S, 2004, MOL BIOTECHNOL, V28, P21, DOI 10.1385/MB:28:1:21
   Eghbali M, 2005, CIRC RES, V96, P1208, DOI 10.1161/01.RES.0000170652.71414.16
   Elenius K, 1997, J BIOL CHEM, V272, P26761, DOI 10.1074/jbc.272.42.26761
   Elenius K, 1999, ONCOGENE, V18, P2607, DOI 10.1038/sj.onc.1202612
   Forrester SJ, 2016, ANNU REV PHARMACOL, V56, P627, DOI 10.1146/annurev-pharmtox-070115-095427
   Frey N, 2003, ANNU REV PHYSIOL, V65, P45, DOI 10.1146/annurev.physiol.65.092101.142243
   García-Rivello H, 2005, AM J PHYSIOL-HEART C, V289, pH1153, DOI 10.1152/ajpheart.00048.2005
   GASSMANN M, 1995, NATURE, V378, P390, DOI 10.1038/378390a0
   George AJ, 2013, FEBS J, V280, P5258, DOI 10.1111/febs.12509
   Giraud MN, 2005, J APPL PHYSIOL, V99, P313, DOI 10.1152/japplphysiol.00609.2004
   Junttila TT, 2000, TRENDS CARDIOVAS MED, V10, P304, DOI 10.1016/S1050-1738(01)00065-2
   Kaakinen M, 2017, BASIC RES CARDIOL, V112, DOI 10.1007/s00395-017-0613-6
   Kehat I, 2010, ANN NY ACAD SCI, V1188, P96, DOI 10.1111/j.1749-6632.2009.05088.x
   LEE KF, 1995, NATURE, V378, P394, DOI 10.1038/378394a0
   Liu QH, 2006, MOL CELL BIOL, V26, P3785, DOI 10.1128/MCB.26.10.3785-3797.2006
   Louch WE, 2011, J MOL CELL CARDIOL, V51, P288, DOI 10.1016/j.yjmcc.2011.06.012
   Määttä JA, 2006, MOL BIOL CELL, V17, P67, DOI 10.1091/mbc.E05-05-0402
   Marian AJ, 2017, CIRC RES, V121, P749, DOI 10.1161/CIRCRESAHA.117.311059
   Molkentin JD, 1998, CELL, V93, P215, DOI 10.1016/S0092-8674(00)81573-1
   Muraoka-Cook RS, 2009, MOL CELL BIOL, V29, P4935, DOI 10.1128/MCB.01705-08
   Ni CY, 2001, SCIENCE, V294, P2179, DOI 10.1126/science.1065412
   Omerovic J, 2004, EXP CELL RES, V294, P469, DOI 10.1016/j.yexcr.2003.12.002
   Parodi EM, 2014, CARDIOVASC RES, V102, P194, DOI 10.1093/cvr/cvu021
   PELLICCIA A, 1991, NEW ENGL J MED, V324, P295, DOI 10.1056/NEJM199101313240504
   Polizzotti BD, 2015, SCI TRANSL MED, V7, DOI 10.1126/scitranslmed.aaa5171
   Reichelt ME, 2017, INT J BIOCHEM CELL B, V83, P97, DOI 10.1016/j.biocel.2016.12.014
   Rohrbach S, 1999, CIRCULATION, V100, P407, DOI 10.1161/01.CIR.100.4.407
   Rohrbach S, 2005, BASIC RES CARDIOL, V100, P240, DOI 10.1007/s00395-005-0514-4
   Roskoski R, 2014, PHARMACOL RES, V79, P34, DOI 10.1016/j.phrs.2013.11.002
   SADOSHIMA J, 1993, CIRC RES, V73, P413, DOI 10.1161/01.RES.73.3.413
   Sardi SP, 2006, CELL, V127, P185, DOI 10.1016/j.cell.2006.07.037
   Sundaresan S, 1998, ENDOCRINOLOGY, V139, P4756, DOI 10.1210/en.139.12.4756
   Sundvall M, 2008, P NATL ACAD SCI USA, V105, P4162, DOI 10.1073/pnas.0708333105
   Sundvall M, 2010, MOL BIOL CELL, V21, P4275, DOI 10.1091/mbc.E10-04-0332
   Thomas WG, 2002, CIRC RES, V90, P135, DOI 10.1161/hh0202.104109
   THREADGILL DW, 1995, SCIENCE, V269, P230, DOI 10.1126/science.7618084
   Veikkolainen V, 2011, CELL CYCLE, V10, P2647, DOI 10.4161/cc.10.16.17194
   Vermeulen Z, 2016, BASIC RES CARDIOL, V111, DOI 10.1007/s00395-016-0576-z
   Wadugu B, 2012, AM J PHYSIOL-HEART C, V302, pH2139, DOI 10.1152/ajpheart.00063.2012
   Williams CC, 2004, J CELL BIOL, V167, P469, DOI 10.1083/jcb.200403155
   Wilson KJ, 2009, PHARMACOL THERAPEUT, V122, P1, DOI 10.1016/j.pharmthera.2008.11.008
   Yoshioka J, 2005, P NATL ACAD SCI USA, V102, P10622, DOI 10.1073/pnas.0501198102
   Zhao YY, 1998, J BIOL CHEM, V273, P10261, DOI 10.1074/jbc.273.17.10261
   Zhu Y, 2006, CANCER RES, V66, P7991, DOI 10.1158/0008-5472.CAN-05-4397
NR 50
TC 2
Z9 2
U1 0
U2 6
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0021-9541
EI 1097-4652
J9 J CELL PHYSIOL
JI J. Cell. Physiol.
PD DEC
PY 2021
VL 236
IS 12
BP 8160
EP 8170
DI 10.1002/jcp.30487
EA JUN 2021
PG 11
WC Cell Biology; Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Physiology
GA XN4VH
UT WOS:000665775000001
PM 34170016
OA Green Published
DA 2025-04-10
ER

PT J
AU Pagano, M
   Reboud-Ravaux, M
AF Pagano, Maurice
   Reboud-Ravaux, Michele
TI Cryptic activities of fibronectin fragments, particularly cryptic
   proteases
SO FRONTIERS IN BIOSCIENCE-LANDMARK
LA English
DT Article
DE Mammalian Fibronectins; Cryptic Activities; Fn-Proteinase; Small
   Molecular Mass Inhibitors; Review
ID POTENTIAL PROTEOLYTIC ACTIVITY; BASEMENT-MEMBRANE FIBRONECTIN; PLATELET
   THROMBUS FORMATION; HUMAN-PLASMA FIBRONECTIN; MATRIX METALLOPROTEINASES;
   FIBROBLAST MIGRATION; CYSTEINE PROTEINASES; LIMITED PROTEOLYSIS;
   EXPRESSION; GELATINASE
AB Fibronectin (FN) is a modular glycoprotein encoded by a single gene. A soluble form of this protein is found in the plasma of several animals. Alternative splicing of pre-mRNA at three sites produces cellular and plasma FNs. The plasma form contributes to blood clotting and thrombosis. Many extracellular matrices (ECM) contain an FN network associated with a variety of cell activities through binding to cell surface integrin receptors. Fragments of FN can have cryptic activities that are specific to these fragments rather than to the intact protein. The metalloprotease activity present in the basement membrane and plasma fibronectins has been intensively studied in humans, bovine and rats. Organic inhibitors that are selective for the human cryptic enzyme have been produced.
C1 [Pagano, Maurice; Reboud-Ravaux, Michele] Univ Paris 06, UR4, Enzymol Lab, F-75252 Paris 05, France.
C3 Sorbonne Universite
RP Pagano, M (corresponding author), Univ Paris 06, UR4, Enzymol Lab, Case 256,7 Quai St Bernard, F-75252 Paris 05, France.
EM maurice.pagano@upmc.fr
FU Broussais Hotel-Dieu Medical School, University Pierre et Marie Curie;
   French Agency for Cancer Research (ARC); French Agency for Research
   Promotion (ANVAR); French Agency for Medical Research (FRM); French
   League against Cancer
FX This work is dedicated to Vera-Keil-Doulha, research scientist at the
   Pasteur Institute (Paris), who first described the protease activities
   of fibronectin. I thank Professor S. Tabibzabeh, Editor-in-Chief of
   Frontiers in Bioscience for inviting me to organize this special issue.
   I am indebted to two graduate students, Nathalie Guinec (1988-1993), and
   Laziz Boudjennah (1992 -1998), who both worked on the cryptic basement
   membrane protease from fibronectin. This work was performed in the
   "Biochemistry Laboratory, Medical School Broussais Hotel-Dieu,
   University Pierre et Marie Curie". Financial support was provided by:
   Broussais Hotel-Dieu Medical School, University Pierre et Marie Curie:
   1980-1998. The French Agency for Cancer Research (ARC): 1984-1992. The
   French Agency for Research Promotion (ANVAR), in collaboration with
   Pierre Burtin (died 1993): 1984-1988. The French Agency for Medical
   Research (FRM): 1992-1994. The French League against Cancer, with
   Professor Michele Reboud-Ravaux: 2004-2006, I thank Professor Michele
   Reboud-Ravaux for encouraging me to continue my research in her group
   (Enzymologie Moleculaire et Fonctionnelle).
CR Boudjennah L, 1998, EUR J BIOCHEM, V255, P246, DOI 10.1046/j.1432-1327.1998.2550246.x
   CAPUTI M, 1995, NUCLEIC ACIDS RES, V23, P238, DOI 10.1093/nar/23.2.238
   Cho J, 2006, J THROMB HAEMOST, V4, P1461, DOI 10.1111/j.1538-7836.2006.01943.x
   Ding L, 2008, OSTEOARTHR CARTILAGE, V16, P1253, DOI 10.1016/j.joca.2008.02.015
   Du KY, 1997, MOL CELL BIOL, V17, P4096, DOI 10.1128/MCB.17.7.4096
   FFRENCHCONSTANT C, 1989, J CELL BIOL, V109, P903, DOI 10.1083/jcb.109.2.903
   FUKAI F, 1995, BIOCHEMISTRY-US, V34, P11453, DOI 10.1021/bi00036a018
   GEORGE EL, 1993, DEVELOPMENT, V119, P1079
   Graille M, 2010, STRUCTURE, V18, P710, DOI 10.1016/j.str.2010.03.012
   Grant MB, 1998, DIABETES, V47, P1335, DOI 10.2337/diabetes.47.8.1335
   GUINEC N, 1993, BIOL CHEM H-S, V374, P1135, DOI 10.1515/bchm3.1993.374.7-12.1135
   GUINEC N, 1992, FEBS LETT, V308, P305, DOI 10.1016/0014-5793(92)81299-2
   HOMANDBERG GA, 1992, J BIOL CHEM, V267, P3597
   Houard X, 2005, INT J CANCER, V116, P378, DOI 10.1002/ijc.21053
   Houard X, 2003, J CELL BIOCHEM, V88, P1188, DOI 10.1002/jcb.10460
   Ingham KC, 1997, J BIOL CHEM, V272, P1718, DOI 10.1074/jbc.272.3.1718
   Ingley E, 2008, BBA-PROTEINS PROTEOM, V1784, P56, DOI 10.1016/j.bbapap.2007.08.012
   JARNAGIN WR, 1994, J CELL BIOL, V127, P2037, DOI 10.1083/jcb.127.6.2037
   KEILDLOUHA V, 1986, P NATL ACAD SCI USA, V83, P5377, DOI 10.1073/pnas.83.15.5377
   KNIGHT CG, 1992, FEBS LETT, V296, P263, DOI 10.1016/0014-5793(92)80300-6
   Kornblihtt AR, 1996, FASEB J, V10, P248, DOI 10.1096/fasebj.10.2.8641558
   MAIN AL, 1992, CELL, V71, P671, DOI 10.1016/0092-8674(92)90600-H
   Mao Y, 2005, MATRIX BIOL, V24, P389, DOI 10.1016/j.matbio.2005.06.008
   Millard CJ, 2007, J BIOL CHEM, V282, P35530, DOI 10.1074/jbc.M707532200
   Mosher D.F., 1989, Fibronectin
   Ni HY, 2000, J CLIN INVEST, V106, P385, DOI 10.1172/JCI9896
   Ni HY, 2003, P NATL ACAD SCI USA, V100, P2415, DOI 10.1073/pnas.2628067100
   OKADA Y, 1990, EUR J BIOCHEM, V194, P721, DOI 10.1111/j.1432-1033.1990.tb19462.x
   PAGANO M, UNPUB
   Pagano M, 2008, ARCH BIOCHEM BIOPHYS, V479, P158, DOI 10.1016/j.abb.2008.08.016
   Pankov R, 2002, J CELL SCI, V115, P3861, DOI 10.1242/jcs.00059
   Petersen TE, 1989, FIBRONECTIN
   PLANCHENAULT T, 1990, BIOL CHEM H-S, V371, P117, DOI 10.1515/bchm3.1990.371.1.117
   RICE A, 1995, BIOCHEMISTRY-US, V34, P9249, DOI 10.1021/bi00028a038
   Schnepel J, 2000, J PROTEIN CHEM, V19, P685, DOI 10.1023/A:1007104420017
   Schor SL, 1996, J CELL SCI, V109, P2581
   SCHOR SL, 2003, CANCER RES
   SCHWARZBAUER JE, 1989, J CELL BIOL, V109, P3445, DOI 10.1083/jcb.109.6.3445
   Stanton H, 2002, BIOCHEM J, V364, P181, DOI 10.1042/bj3640181
   Tomasini-Johansson BR, 2006, MATRIX BIOL, V25, P282, DOI 10.1016/j.matbio.2006.02.002
   Unger J, 1999, J PROTEIN CHEM, V18, P403, DOI 10.1023/A:1020684508212
   Vakonakis I, 2007, EMBO J, V26, P2575, DOI 10.1038/sj.emboj.7601694
   VIDMAR SL, 1991, EUR J BIOCHEM, V201, P79, DOI 10.1111/j.1432-1033.1991.tb16258.x
   Watanabe K, 2000, BIOCHEMISTRY-US, V39, P7138, DOI 10.1021/bi992670r
   White ES, 2008, J PATHOL, V216, P1, DOI 10.1002/path.2388
NR 45
TC 5
Z9 6
U1 0
U2 6
PU FRONTIERS IN BIOSCIENCE INC
PI IRVINE
PA 16471 SCIENTIFIC WAY, IRVINE, CA 92618 USA
SN 1093-9946
EI 1093-4715
J9 FRONT BIOSCI-LANDMRK
JI Front. Biosci.
PD JAN 1
PY 2011
VL 16
BP 698
EP 706
DI 10.2741/3713
PG 9
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA 757MZ
UT WOS:000290092700020
PM 21196196
OA Bronze
DA 2025-04-10
ER

PT J
AU Shimomura, I
   Shimano, H
   Horton, JD
   Goldstein, JL
   Brown, MS
AF Shimomura, I
   Shimano, H
   Horton, JD
   Goldstein, JL
   Brown, MS
TI Differential expression of exons 1a and 1c in mRNAs for sterol
   regulatory element binding protein-1 in human and mouse organs and
   cultured cells
SO JOURNAL OF CLINICAL INVESTIGATION
LA English
DT Article
DE SREBP-1; alternative splicing; cholesterol; fatty acids; liver;
   adipocytes
ID DENSITY-LIPOPROTEIN RECEPTOR; LEUCINE ZIPPER PROTEIN; COENZYME-A
   REDUCTASE; FULL-LENGTH CDNA; NUCLEOTIDE-SEQUENCE; GENE; TRANSCRIPTION;
   SREBP-1; RNA; SYNTHASE
AB The 5' end of the mRNA-encoding sterol regulatory element binding protein-1 (SREBP-1) exists in two forms, designated 1a and 1c. The divergence results from the use of two transcription start sites that produce two separate 5' exons, each of which is spliced to a common exon 2. Here we show that the ratio of SREBP-1c to 1a transcripts varies markedly among organs of the adult mouse. At one extreme is the liver, in which the 1c transcript predominates by a 9:1 ratio. High 1c:1a ratios are also found in mouse adrenal gland and adipose tissue and in human liver and adrenal gland. At the other extreme is the spleen, which shows a reversed 1c:1a ratio (1:10). In five different lines of cultured cells, including the HepG2 line derived from human hepatocytes, the 1a transcript predominated (1c:1a ratio < 1:2). In mouse 3T3-L1 preadipocytes, the 1a transcript was present, but the 1c transcript was not detectable. When these cells were differentiated into adipocytes by hormone treatment in culture, the amount of 1a transcript rose markedly (8.2-fold), and the 1c transcript remained virtually undetectable. We conclude that the SREBP-1a and 1c transcripts are controlled independently by regulatory regions that respond differentially to organ-specific and metabolic factors.
C1 UNIV TEXAS,SW MED CTR,DEPT MOL GENET,DALLAS,TX 75235.
C3 University of Texas System; University of Texas Dallas; University of
   Texas Southwestern Medical Center Dallas
RI Shimano, Hitoshi/V-1761-2019
OI Shimano, Hitoshi/0000-0002-5562-5572
FU NHLBI NIH HHS [HL-20948] Funding Source: Medline
CR BENNETT MK, 1995, J BIOL CHEM, V270, P25578, DOI 10.1074/jbc.270.43.25578
   CHIN DJ, 1984, NATURE, V308, P613, DOI 10.1038/308613a0
   CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
   Ericsson J, 1996, P NATL ACAD SCI USA, V93, P945, DOI 10.1073/pnas.93.2.945
   GIL G, 1986, J BIOL CHEM, V261, P3710
   HOFFER MJV, 1993, BIOCHEM BIOPH RES CO, V191, P880, DOI 10.1006/bbrc.1993.1299
   HUA XX, 1995, GENOMICS, V25, P667, DOI 10.1016/0888-7543(95)80009-B
   HUA XX, 1993, P NATL ACAD SCI USA, V90, P11603, DOI 10.1073/pnas.90.24.11603
   Hua XX, 1996, J BIOL CHEM, V271, P10379, DOI 10.1074/jbc.271.17.10379
   HUA XX, 1995, J BIOL CHEM, V270, P29422, DOI 10.1074/jbc.270.49.29422
   Kim JB, 1996, GENE DEV, V10, P1096, DOI 10.1101/gad.10.9.1096
   KIRCHGESSNER TG, 1987, J BIOL CHEM, V262, P8463
   KNOWLES BB, 1980, SCIENCE, V209, P497, DOI 10.1126/science.6248960
   LIN FT, 1992, GENE DEV, V6, P533, DOI 10.1101/gad.6.4.533
   LUSKEY KL, 1985, J BIOL CHEM, V260, P271
   OSONO Y, 1995, J CLIN INVEST, V95, P1124, DOI 10.1172/JCI117760
   PONTE P, 1984, NUCLEIC ACIDS RES, V12, P1687, DOI 10.1093/nar/12.3.1687
   Sakai J, 1996, CELL, V85, P1037, DOI 10.1016/S0092-8674(00)81304-5
   SATO R, 1994, J BIOL CHEM, V269, P17267
   SHENG ZQ, 1995, P NATL ACAD SCI USA, V92, P935, DOI 10.1073/pnas.92.4.935
   Shimano H, 1996, J CLIN INVEST, V98, P1575, DOI 10.1172/JCI118951
   Shimano H, 1997, J CLIN INVEST, V99, P846, DOI 10.1172/JCI119248
   TOKUNAGA K, 1986, NUCLEIC ACIDS RES, V14, P2829
   TONTONOZ P, 1993, MOL CELL BIOL, V13, P4753, DOI 10.1128/MCB.13.8.4753
   WANG XD, 1994, CELL, V77, P53, DOI 10.1016/0092-8674(94)90234-8
   Willnow TE, 1996, EMBO J, V15, P2632, DOI 10.1002/j.1460-2075.1996.tb00623.x
   YANG JX, 1994, GENE DEV, V8, P1910, DOI 10.1101/gad.8.16.1910
   YOKOYAMA C, 1993, CELL, V75, P187, DOI 10.1016/S0092-8674(05)80095-9
NR 28
TC 637
Z9 757
U1 0
U2 26
PU ROCKEFELLER UNIV PRESS
PI NEW YORK
PA 1114 FIRST AVE, 4TH FL, NEW YORK, NY 10021
SN 0021-9738
J9 J CLIN INVEST
JI J. Clin. Invest.
PD MAR 1
PY 1997
VL 99
IS 5
BP 838
EP 845
DI 10.1172/JCI119247
PG 8
WC Medicine, Research & Experimental
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Research & Experimental Medicine
GA WN152
UT WOS:A1997WN15200006
PM 9062340
OA Bronze, Green Published
DA 2025-04-10
ER

PT J
AU Wei, B
   Jin, JP
AF Wei, Bin
   Jin, J. -P.
TI Troponin T isoforms and posttranscriptional modifications: Evolution,
   regulation and function
SO ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
LA English
DT Review
DE Troponin T isoform genes; Molecular evolution; Posttranscriptional
   modification; Striated muscle thin filament; Calcium regulation of
   contraction
ID NH2-TERMINAL VARIABLE REGION; METAL-BINDING CLUSTER;
   AMINO-ACID-SEQUENCE; COMPLETE NUCLEOTIDE-SEQUENCE; GLU(180) NONSENSE
   MUTATION; KINASE-C PHOSPHORYLATION; TWITCH SKELETAL-MUSCLE; MOUSE
   CARDIAC-MUSCLE; CA2+ SENSITIVITY; ADULT ISOFORMS
AB Troponin-mediated Ca2+-regulation governs the actin-activated myosin motor function which powers striated (skeletal and cardiac) muscle contraction. This review focuses on the structure-function relationship of troponin T, one of the three protein subunits of the troponin complex. Molecular evolution, gene regulation, alternative RNA splicing, and posttranslational modifications of troponin T isoforms in skeletal and cardiac muscles are summarized with emphases on recent research progresses. The physiological and pathophysiological significances of the structural diversity and regulation of troponin T are discussed for impacts on striated muscle function and adaptation in health and diseases. (C) 2010 Elsevier Inc. All rights reserved.
C1 [Wei, Bin; Jin, J. -P.] Wayne State Univ, Sch Med, Dept Physiol, Detroit, MI 48201 USA.
C3 Wayne State University
RP Jin, JP (corresponding author), Wayne State Univ, Sch Med, Dept Physiol, 540 E Canfield, Detroit, MI 48201 USA.
EM jjin@med.wayne.edu
RI Jin, Jian-Ping/AAD-1149-2020; Wei, Bin/M-2017-2014
OI Jin, JP/0000-0001-9932-1063
FU National Institutes of Health [AR048816, HL078773, HL098945]
FX This work was supported by grants from the National Institutes of Health
   (AR048816, HL078773 and HL098945) to J.-P.J.
CR AKELLA AB, 1995, CIRC RES, V76, P600, DOI 10.1161/01.RES.76.4.600
   ANDERSON PAW, 1995, CIRC RES, V76, P681, DOI 10.1161/01.RES.76.4.681
   Baudenbacher F, 2008, J CLIN INVEST, V118, P3893, DOI 10.1172/JCI36642
   Benoist P, 1998, J BIOL CHEM, V273, P7538, DOI 10.1074/jbc.273.13.7538
   Biesiadecki BJ, 2002, J BIOL CHEM, V277, P50275, DOI 10.1074/jbc.M206369200
   Biesiadecki BJ, 2002, J BIOL CHEM, V277, P18459, DOI 10.1074/jbc.M200788200
   Biesiadecki BJ, 2007, BIOCHEMISTRY-US, V46, P1368, DOI 10.1021/bi061949m
   BREITBART RE, 1986, J MOL BIOL, V188, P313, DOI 10.1016/0022-2836(86)90157-9
   BREITBART RE, 1987, CELL, V49, P793, DOI 10.1016/0092-8674(87)90617-9
   BRIGGS MM, 1993, DEV BIOL, V158, P503, DOI 10.1006/dbio.1993.1208
   CabralLilly D, 1997, BIOPHYS J, V73, P1763, DOI 10.1016/S0006-3495(97)78206-7
   Chandra M, 1999, J MOL CELL CARDIOL, V31, P867, DOI 10.1006/jmcc.1999.0928
   Chaudhuri T, 2005, J MOL BIOL, V352, P58, DOI 10.1016/j.jmb.2005.06.066
   Chong SM, 2009, J MOL EVOL, V68, P448, DOI 10.1007/s00239-009-9202-0
   COLLINS JH, 1991, J MUSCLE RES CELL M, V12, P3, DOI 10.1007/BF01781170
   Communal C, 2002, P NATL ACAD SCI USA, V99, P6252, DOI 10.1073/pnas.092022999
   COOPER TA, 1985, J BIOL CHEM, V260, P1140
   COOPER TA, 1984, SCIENCE, V226, P979, DOI 10.1126/science.6095446
   Domingo A, 1998, J MUSCLE RES CELL M, V19, P393, DOI 10.1023/A:1005349704790
   Farza H, 1998, J MOL CELL CARDIOL, V30, P1247, DOI 10.1006/jmcc.1998.0698
   Feng HZ, 2008, J PHYSIOL-LONDON, V586, P3537, DOI 10.1113/jphysiol.2008.153577
   Feng HZ, 2010, AM J PHYSIOL-HEART C, V299, pH97, DOI 10.1152/ajpheart.01105.2009
   Feng HZ, 2009, J BIOL CHEM, V284, P31798, DOI 10.1074/jbc.M109.020826
   Feng HZ, 2009, ARCH BIOCHEM BIOPHYS, V487, P36, DOI 10.1016/j.abb.2009.05.001
   FUJITA S, 1992, J BIOCHEM-TOKYO, V112, P306, DOI 10.1093/oxfordjournals.jbchem.a123896
   GAHLMANN R, 1987, J BIOL CHEM, V262, P16122
   GAHLMANN R, 1990, J BIOL CHEM, V265, P12520
   Galinska-Rakoczy A, 2008, J MOL BIOL, V379, P929, DOI 10.1016/j.jmb.2008.04.062
   Goll DE, 2003, PHYSIOL REV, V83, P731, DOI 10.1152/physrev.00029.2002
   Gomes AV, 2004, J BIOL CHEM, V279, P49579, DOI 10.1074/jbc.M407340200
   Gomes AV, 2002, J BIOL CHEM, V277, P35341, DOI 10.1074/jbc.M204118200
   Gordon AM, 2000, PHYSIOL REV, V80, P853, DOI 10.1152/physrev.2000.80.2.853
   Granzier H, 2007, MUSCLE NERVE, V36, P740, DOI 10.1002/mus.20886
   GREASER ML, 1971, J BIOL CHEM, V246, P4226
   GREASER ML, 1973, COLD SPRING HARB SYM, V37, P235, DOI 10.1101/SQB.1973.037.01.033
   Hasenfuss G, 1998, CARDIOVASC RES, V39, P60, DOI 10.1016/S0008-6363(98)00110-2
   He XG, 2003, AM J PATHOL, V163, P243, DOI 10.1016/S0002-9440(10)63647-4
   HEELEY DH, 1987, J BIOL CHEM, V262, P9971
   Herranz R, 2005, MOL BIOL EVOL, V22, P2231, DOI 10.1093/molbev/msi223
   Hirao C, 2004, GENE, V338, P243, DOI 10.1016/j.gene.2004.05.023
   Hsiao CD, 2003, DEV DYNAM, V227, P266, DOI 10.1002/dvdy.10305
   Huang QQ, 2008, AM J PHYSIOL-CELL PH, V294, pC213, DOI 10.1152/ajpcell.00146.2007
   Huang QQ, 1999, J PHYSIOL-LONDON, V520, P231, DOI 10.1111/j.1469-7793.1999.00231.x
   Huang QQ, 1999, GENE, V229, P1, DOI 10.1016/S0378-1119(99)00051-7
   Huang XP, 1999, CIRC RES, V84, P1
   Inoue A, 1996, J BIOCHEM-TOKYO, V120, P834
   Jeong EM, 2009, AM J PHYSIOL-HEART C, V297, pH283, DOI 10.1152/ajpheart.01200.2008
   Jideama NM, 1996, J BIOL CHEM, V271, P23277, DOI 10.1074/jbc.271.38.23277
   Jin JP, 2010, ARCH BIOCHEM BIOPHYS, V500, P144, DOI 10.1016/j.abb.2010.06.001
   Jin JP, 2008, CRIT REV EUKAR GENE, V18, P93, DOI 10.1615/CritRevEukarGeneExpr.v18.i2.10
   Jin JP, 1998, BIOCHEM BIOPH RES CO, V242, P540, DOI 10.1006/bbrc.1997.8006
   JIN JP, 1994, FEBS LETT, V341, P135, DOI 10.1016/0014-5793(94)80256-4
   Jin JP, 2000, BIOCHEMISTRY-US, V39, P11702, DOI 10.1021/bi9927437
   Jin JP, 1998, GENE, V214, P121, DOI 10.1016/S0378-1119(98)00214-5
   JIN JP, 1992, J MOL BIOL, V227, P1269, DOI 10.1016/0022-2836(92)90540-Z
   Jin JP, 2003, J BIOL CHEM, V278, P26159, DOI 10.1074/jbc.M303469200
   JIN JP, 1989, J BIOL CHEM, V264, P14471
   Jin JP, 2001, J MOL EVOL, V52, P103, DOI 10.1007/s002390010139
   Jin JP, 1996, GENE, V168, P217, DOI 10.1016/0378-1119(95)00803-9
   Jin JP, 1996, BIOCHEM BIOPH RES CO, V225, P883, DOI 10.1006/bbrc.1996.1267
   Johnston JJ, 2000, AM J HUM GENET, V67, P814, DOI 10.1086/303089
   Kagawa H, 2007, ADV EXP MED BIOL, V592, P153
   KATOH N, 1983, BIOCHEM J, V209, P189, DOI 10.1042/bj2090189
   Knollmann BC, 2001, J BIOL CHEM, V276, P10039, DOI 10.1074/jbc.M006745200
   Ladd AN, 2002, GENOME BIOL, V3
   Larsson L, 2008, AM J PHYSIOL-CELL PH, V295, pC722, DOI 10.1152/ajpcell.00110.2008
   Lehman W, 2009, J MOL BIOL, V388, P673, DOI 10.1016/j.jmb.2009.03.060
   Lin J J, 1997, Int Rev Cytol, V170, P1, DOI 10.1016/S0074-7696(08)61619-8
   LONG MY, 1995, CURR OPIN GENET DEV, V5, P774, DOI 10.1016/0959-437X(95)80010-3
   Marston SB, 2009, J MUSCLE RES CELL M, V30, P93, DOI 10.1007/s10974-009-9184-y
   MARTIN AF, 1981, J BIOL CHEM, V256, P964
   McConnell BK, 1998, AM J PHYSIOL-HEART C, V274, pH385, DOI 10.1152/ajpheart.1998.274.2.H385
   MesnardRouiller L, 1997, J MOL CELL CARDIOL, V29, P3043, DOI 10.1006/jmcc.1997.0519
   Miller T, 2001, J BIOL CHEM, V276, P3743, DOI 10.1074/jbc.M006746200
   Miyazaki JI, 1999, J MUSCLE RES CELL M, V20, P655, DOI 10.1023/A:1005504018059
   Montgomery DE, 2001, AM J PHYSIOL-HEART C, V280, pH1011, DOI 10.1152/ajpheart.2001.280.3.H1011
   Myers CD, 1996, J CELL BIOL, V132, P1061, DOI 10.1083/jcb.132.6.1061
   Nishii K, 2008, DEV BIOL, V322, P65, DOI 10.1016/j.ydbio.2008.07.007
   NOLAND TA, 1993, J MOL CELL CARDIOL, V25, P53, DOI 10.1006/jmcc.1993.1007
   NOLAND TA, 1991, J BIOL CHEM, V266, P4974
   Nongthomba U, 2007, GENETICS, V177, P295, DOI 10.1534/genetics.106.056812
   Nosek TM, 2004, ARCH BIOCHEM BIOPHYS, V430, P178, DOI 10.1016/j.abb.2004.07.014
   Ogut O, 1999, AM J PHYSIOL-CELL PH, V276, pC1162, DOI 10.1152/ajpcell.1999.276.5.C1162
   Ogut O, 1996, BIOCHEMISTRY-US, V35, P16581, DOI 10.1021/bi961712y
   Ogut O, 1998, J BIOL CHEM, V273, P27858, DOI 10.1074/jbc.273.43.27858
   OHTSUKI I, 1984, J BIOCHEM, V95, P1337, DOI 10.1093/oxfordjournals.jbchem.a134740
   OHTSUKUI I, 1967, J BIOCHEM-TOKYO, V61, P817, DOI 10.1093/oxfordjournals.jbchem.a128619
   OJIMA T, 1986, J BIOL CHEM, V261, P6749
   Oota H, 1999, AM J HUM GENET, V64, P250, DOI 10.1086/302197
   PAN BS, 1991, J BIOL CHEM, V266, P12432
   Parmacek MS, 2004, PROG CARDIOVASC DIS, V47, P159, DOI 10.1016/j.pcad.2004.07.003
   PARMACEK MS, 1989, J BIOL CHEM, V264, P13217
   PEARLSTONE JR, 1976, P NATL ACAD SCI USA, V73, P1902, DOI 10.1073/pnas.73.6.1902
   PEARLSTONE JR, 1982, J BIOL CHEM, V257, P587
   PEARLSTONE JR, 1977, J BIOL CHEM, V252, P983
   PECKHAM M, 1990, J MUSCLE RES CELL M, V11, P203, DOI 10.1007/BF01843574
   Perry SV, 1999, MOL CELL BIOCHEM, V190, P9, DOI 10.1023/A:1006939307715
   Perry SV, 2001, J MUSCLE RES CELL M, V22, P5, DOI 10.1023/A:1010303732441
   Perry SV, 1998, J MUSCLE RES CELL M, V19, P575
   REISER PJ, 1992, J PHYSIOL-LONDON, V449, P573, DOI 10.1113/jphysiol.1992.sp019102
   Reiser PJ, 1996, J PHYSIOL-LONDON, V493, P553, DOI 10.1113/jphysiol.1996.sp021403
   SABRY MA, 1991, J MUSCLE RES CELL M, V12, P262, DOI 10.1007/BF01745116
   SAGGIN L, 1990, DEVELOPMENT, V110, P547
   SAGGIN L, 1989, J BIOL CHEM, V264, P16299
   SCHACHAT F, 1995, DEV BIOL, V171, P233, DOI 10.1006/dbio.1995.1274
   Schaertl S, 1995, BIOCHEMISTRY-US, V34, P15890, DOI 10.1021/bi00049a003
   Sfichi-Duke L, 2010, J MOL CELL CARDIOL, V48, P934, DOI 10.1016/j.yjmcc.2010.01.005
   Shenouda SK, 2008, CARDIOVASC RES, V79, P662, DOI 10.1093/cvr/cvn129
   Shiraishi F, 1999, J BIOCHEM-TOKYO, V126, P1020, DOI 10.1093/oxfordjournals.jbchem.a022545
   Simpson JA, 2000, J APPL PHYSIOL, V88, P753, DOI 10.1152/jappl.2000.88.2.753
   SMILLIE LB, 1988, J BIOL CHEM, V263, P18816
   SOLARO RJ, 1988, CIRC RES, V63, P779, DOI 10.1161/01.RES.63.4.779
   Solaro RJ, 1998, CIRC RES, V83, P471, DOI 10.1161/01.RES.83.5.471
   Solis RS, 2008, J MUSCLE RES CELL M, V29, P203, DOI 10.1007/s10974-009-9168-y
   Sumandea MP, 2009, BIOCHEMISTRY-US, V48, P7722, DOI 10.1021/bi900516n
   Sumandea MP, 2004, ANN NY ACAD SCI, V1015, P39, DOI 10.1196/annals.1302.004
   SWIDERSKI RE, 1990, DEV BIOL, V140, P73, DOI 10.1016/0012-1606(90)90054-M
   Tanaka H, 2008, BBA-PROTEINS PROTEOM, V1784, P1037, DOI 10.1016/j.bbapap.2008.04.001
   Taylor JS, 2001, PHILOS T R SOC B, V356, P1661, DOI 10.1098/rstb.2001.0975
   TILLEY LP, 1977, AM J PATHOL, V86, P493
   Tobacman LS, 1996, ANNU REV PHYSIOL, V58, P447, DOI 10.1146/annurev.ph.58.030196.002311
   TOWNSEND PJ, 1995, J MOL CELL CARDIOL, V27, P2223, DOI 10.1016/S0022-2828(95)91587-7
   TOYOTA N, 1981, J CELL BIOL, V91, P497, DOI 10.1083/jcb.91.2.497
   TOYOTA N, 1983, CELL, V33, P297, DOI 10.1016/0092-8674(83)90358-6
   van Rooij E, 2009, DEV CELL, V17, P662, DOI 10.1016/j.devcel.2009.10.013
   Wang J, 1998, BIOCHEMISTRY-US, V37, P14519, DOI 10.1021/bi9812322
   Wang J, 1997, GENE, V193, P105, DOI 10.1016/S0378-1119(97)00100-5
   Wang Q, 2001, ANAT RECORD, V263, P72, DOI 10.1002/ar.1078
   Wang X, 2005, J BIOL CHEM, V280, P13241, DOI 10.1074/jbc.M413696200
   Wendt T, 1997, J STRUCT BIOL, V118, P1, DOI 10.1006/jsbi.1996.3834
   Williams AH, 2009, CURR OPIN CELL BIOL, V21, P461, DOI 10.1016/j.ceb.2009.01.029
   WU QL, 1995, GENE, V155, P225, DOI 10.1016/0378-1119(94)00846-K
   Yanaga F, 1999, J BIOL CHEM, V274, P8806, DOI 10.1074/jbc.274.13.8806
   Zhang ZL, 2006, BIOCHEMISTRY-US, V45, P11681, DOI 10.1021/bi060273s
   Zhang ZL, 2004, BIOCHEMISTRY-US, V43, P2645, DOI 10.1021/bi035067o
NR 135
TC 114
Z9 144
U1 1
U2 25
PU ELSEVIER SCIENCE INC
PI NEW YORK
PA STE 800, 230 PARK AVE, NEW YORK, NY 10169 USA
SN 0003-9861
EI 1096-0384
J9 ARCH BIOCHEM BIOPHYS
JI Arch. Biochem. Biophys.
PD JAN 15
PY 2011
VL 505
IS 2
BP 144
EP 154
DI 10.1016/j.abb.2010.10.013
PG 11
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA 733TN
UT WOS:000288286000002
PM 20965144
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Rein-Smith, CM
   Anderson, NW
   Farrell, DH
AF Rein-Smith, Chantelle M.
   Anderson, Nathan W.
   Farrell, David H.
TI Differential regulation of fibrinogen γ chain splice isoforms by
   interleukin-6
SO THROMBOSIS RESEARCH
LA English
DT Article
DE Cytokines; Expression; Fibrinogen; Inflammation; Liver
ID PLASMA-PROTEINS; CELL-LINES; EXPRESSION; GENE; ATHEROSCLEROSIS;
   INFLAMMATION; ASSOCIATION; PROMOTER; ELEMENTS; DISEASE
AB Introduction: Fibrinogen is a major structural protein in blood clots, and is also a well-known acute phase reactant. The gamma chain gene of fibrinogen has two alternative splice variants, gamma A and gamma' chains. gamma' fibrinogen constitutes about 7% of total fibrinogen. Total fibrinogen levels and gamma' fibrinogen levels have been associated with cardiovascular disease, but the mechanisms regulating the production of the two isoforms are unknown. Several inflammatory cytokines are known to influence the production of total fibrinogen, but the role of cytokines in the production of gamma' fibrinogen has not been examined. However, epidemiologic studies have shown an association between gamma' fibrinogen levels and inflammatory markers in humans.
   Materials and methods: The expression of gamma fibrinogen and total fibrinogen by HepG2 liver cells was quantitated after treatment with interleukin-1 beta, transforming growth factor-beta, tumor necrosis factor-alpha, and interleukin-6.
   Results: Interleukin-1 beta, transforming growth factor-beta, and tumor necrosis factor-alpha, known down-regulators of total fibrinogen synthesis, also downregulate gamma' fibrinogen synthesis in HepG2 cells. However, interleukin-6 differentially up-regulates the production of total and gamma' fibrinogen, leading to a 3.6-fold increase in gamma A mRNA, but an 8.3-fold increase in gamma' mRNA.
   Conclusions: These findings indicate that gamma' fibrinogen is disproportionately up-regulated by inflammatory responses induced by interleukin-6. (C) 2012 Elsevier Ltd. All rights reserved.
C1 [Farrell, David H.] Oregon Hlth & Sci Univ, Sch Med, Dept Med, Div Cardiovasc Med, Portland, OR 97239 USA.
   [Rein-Smith, Chantelle M.] Oregon Hlth & Sci Univ, Dept Mol & Med Genet, Portland, OR 97239 USA.
C3 Oregon Health & Science University; Oregon Health & Science University
RP Farrell, DH (corresponding author), Oregon Hlth & Sci Univ, Sch Med, Dept Med, Div Cardiovasc Med, Mail Code MQ280,3181 SW Sam Jackson Pk Rd, Portland, OR 97239 USA.
EM farrelld@ohsu.edu
FU NIH [R21 HL097298, R44 HL104885]
FX This work was supported by NIH R21 HL097298 and R44 HL104885 (to
   D.H.F.).
CR Alexander KS, 2011, THROMB HAEMOSTASIS, V105, P605, DOI 10.1160/TH10-09-0626
   Cheung EYL, 2008, STROKE, V39, P1033, DOI 10.1161/STROKEAHA.107.495499
   Cheung EYL, 2009, BLOOD, V114, P4603, DOI 10.1182/blood-2009-08-236240
   CHUNG DW, 1984, BIOCHEMISTRY-US, V23, P4232, DOI 10.1021/bi00313a033
   Collet JP, 2004, ARTERIOSCL THROM VAS, V24, P382, DOI 10.1161/01.ATV.0000109748.77727.3e
   de Willige SU, 2009, BLOOD, V114, P3994, DOI 10.1182/blood-2009-05-217968
   Drouet L, 1999, BLOOD COAGUL FIBRIN, V10, P128
   Duan HO, 2003, J BIOL CHEM, V278, P41270, DOI 10.1074/jbc.M304210200
   FARRELL DH, 1991, BIOCHEMISTRY-US, V30, P9414, DOI 10.1021/bi00103a004
   Farrell DH, CLIN CHEM L IN PRESS
   FORNACE AJ, 1984, J BIOL CHEM, V259, P2826
   Grainger DJ, 2007, CARDIOVASC RES, V74, P213, DOI 10.1016/j.cardiores.2007.02.022
   HASSAN JH, 1992, THROMB HAEMOSTASIS, V67, P478
   Kalivendi SV, 2010, FREE RADICAL BIO MED, V48, P377, DOI 10.1016/j.freeradbiomed.2009.10.045
   Kim H, 1999, MOL CELL BIOL, V19, P5326
   KNOWLES BB, 1980, SCIENCE, V209, P497, DOI 10.1126/science.6248960
   Li CY, 2004, CELL RES, V14, P473, DOI 10.1038/sj.cr.7290250
   Libby P, 2009, J AM COLL CARDIOL, V54, P2129, DOI 10.1016/j.jacc.2009.09.009
   Lovely RS, 2010, CLIN CHEM, V56, P781, DOI 10.1373/clinchem.2009.138347
   Lovely RS, 2002, THROMB HAEMOSTASIS, V88, P26
   MACKIEWICZ A, 1991, J IMMUNOL, V146, P3032
   MACKIEWICZ A, 1990, P NATL ACAD SCI USA, V87, P1491, DOI 10.1073/pnas.87.4.1491
   Mannila MN, 2007, J THROMB HAEMOST, V5, P766, DOI 10.1111/j.1538-7836.2007.02406.x
   Matter N, 2002, NATURE, V420, P691, DOI 10.1038/nature01153
   MIZUGUCHI J, 1995, J BIOL CHEM, V270, P28350
   NACHMAN RL, 1986, J EXP MED, V163, P1595, DOI 10.1084/jem.163.6.1595
   NAWROTH PP, 1986, P NATL ACAD SCI USA, V83, P3460, DOI 10.1073/pnas.83.10.3460
   RIIPI L, 1990, INFECT IMMUN, V58, P2750, DOI 10.1128/IAI.58.9.2750-2754.1990
   Robbins EW, 2008, BMC CANCER, V8, DOI 10.1186/1471-2407-8-260
   Sahni A, 2004, BLOOD, V104, P409, DOI 10.1182/blood-2004-01-0126
   SCHORER AE, 1987, BRIT J HAEMATOL, V67, P193, DOI 10.1111/j.1365-2141.1987.tb02326.x
   Weg-Remers S, 2001, EMBO J, V20, P4194, DOI 10.1093/emboj/20.15.4194
   Zhang ZX, 2000, BLOOD, V96, P3466, DOI 10.1182/blood.V96.10.3466.h8003466_3466_3472
   ZHANG ZX, 1995, J BIOL CHEM, V270, P24287, DOI 10.1074/jbc.270.41.24287
NR 34
TC 28
Z9 32
U1 0
U2 8
PU PERGAMON-ELSEVIER SCIENCE LTD
PI OXFORD
PA THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND
SN 0049-3848
J9 THROMB RES
JI Thromb. Res.
PD JAN
PY 2013
VL 131
IS 1
BP 89
EP 93
DI 10.1016/j.thromres.2012.09.017
PG 5
WC Hematology; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Hematology; Cardiovascular System & Cardiology
GA 061FG
UT WOS:000312833000024
PM 23036532
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Murata, K
   Nunomura, W
   Takakuwa, Y
   Cherr, GN
AF Murata, Kenji
   Nunomura, Wataru
   Takakuwa, Yuichi
   Cherr, Gary N.
TI Two different unique cardiac isoforms of protein 4.1R in zebrafish,
   Danio rerio, and insights into their cardiac functions as related
   to their unique structures
SO DEVELOPMENT GROWTH & DIFFERENTIATION
LA English
DT Article
DE atrium and ventricle; FERM domain; protein 4; 1R; spectrin actin binding
   domain; Zebrafish (Danio Rerio)
ID ACTIN-BINDING DOMAIN; TERNARY COMPLEX; EXPRESSION; SPECTRIN; HEART;
   MECHANOCHEMISTRY; TRANSMEMBRANE; GLYCOPHORIN; SKELETAL; FISH
AB Protein 4.1R (4.1R) has been identified as the major component of the human erythrocyte membrane skeleton. The members of the protein 4.1 gene family are expressed in a tissue-specific alternative splicing manner that increases their functions in each tissue; however, the exact roles of cardiac 4.1R in the developing myocardium are poorly understood. In zebrafish (ZF), we identified two heart-specific 4.1R isoforms, ZF4.1RH2 and ZF4.1RH3, encoding N-terminal 30 kDa (FERM) domain and spectrin-actin binding domain (SABD) and C-terminal domain (CTD), separately. Applying immunohistochemistry using specific antibodies for 30 kDa domain and CTD separately, the gene product of ZF4.1RH2 and ZF4.1RH3 appeared only in the ventricle and in the atrium, respectively, in mature hearts. During embryogenesis, both gene expressions are expressed starting 24 h post-fertilization (hpf). Following whole-mount in situ hybridization, ZF4.1RH3 gene expression was detected in the atrium of 37 hpf embryos. These results indicate that the gene product of ZF4.1RH3 is essential for normal morphological shape of the developing heart and to support the repetitive cycles of its muscle contraction and relaxation.
C1 [Murata, Kenji] Univ Calif Davis, Dept Anim Sci, Davis, CA 95616 USA.
   [Nunomura, Wataru; Takakuwa, Yuichi] Tokyo Womens Med Univ, Dept Biochem, Shinjuku Ku, Tokyo 1628666, Japan.
   [Cherr, Gary N.] Univ Calif Davis, Bodega Marine Lab, Dept Environm Toxicol, Bodega Bay, CA 94923 USA.
   [Cherr, Gary N.] Univ Calif Davis, Bodega Marine Lab, Dept Nutr, Bodega Bay, CA 94923 USA.
C3 University of California System; University of California Davis; Tokyo
   Women's Medical University; University of California System; University
   of California Davis; University of California System; University of
   California Davis
RP Murata, K (corresponding author), Univ Calif Davis, Dept Anim Sci, Davis, CA 95616 USA.
EM kmurata@ucdavis.edu
FU American Health Assistance Foundation [017670, 06-002923]; Ministry of
   Education Culture, Sport, Science and Technology of Japan [12680702,
   15570123]; Seed Life Tech. Inc; Grants-in-Aid for Scientific Research
   [12680702, 15570123] Funding Source: KAKEN
FX We express our thanks to Dr Bruce W. Draper, College of Biological
   Science, University of California, Davis for his kind technical support
   for microinjection into ZF embryos. We also express our thanks to Dr
   Fred S. Conte, Department of Animal Science, University of California,
   Davis for his critical editing. We also express our thanks to Ms Nicole
   M. Pierce, Mr Gabriel Senties-Ramirez, Mr Daniel Chu and Ms Elizabeth A.
   McInnis at University of California Davis for their assistance to this
   project. This project was supported by the American Health Assistance
   Foundation (017670 and 06-002923 to KM) and in part by Grant-in-Aid for
   Scientific Research from the Ministry of Education Culture, Sport,
   Science and Technology of Japan 12680702 and 15570123 to WN. Part of
   this work was also supported by Seed Life Tech. Inc. This publication is
   a contribution from the UC Davis Bodega Marine Laboratory.
CR An XL, 1996, J BIOL CHEM, V271, P33187, DOI 10.1074/jbc.271.52.33187
   ANDERSON RA, 1984, NATURE, V307, P655, DOI 10.1038/307655a0
   CHASIS JA, 1993, J CLIN INVEST, V91, P329, DOI 10.1172/JCI116189
   Christensen AK, 2008, BMC DEV BIOL, V8, DOI 10.1186/1471-213X-8-3
   CONBOY JG, 1988, P NATL ACAD SCI USA, V85, P9062, DOI 10.1073/pnas.85.23.9062
   DISCHER D, 1993, J BIOL CHEM, V268, P7186
   DISCHER DE, 1995, J CELL BIOL, V130, P897, DOI 10.1083/jcb.130.4.897
   Gascard P, 1998, BLOOD, V92, P4404, DOI 10.1182/blood.V92.11.4404.423k50_4404_4414
   Gimm JA, 2002, BIOCHEMISTRY-US, V41, P7275, DOI 10.1021/bi0256330
   Hayes NVL, 2000, J CELL SCI, V113, P2023
   Knowlton MN, 2003, DEV BIOL, V264, P407, DOI 10.1016/j.ydbio.2003.09.001
   Liao EC, 2000, DEVELOPMENT, V127, P5123
   Marone Maria, 2001, Biological Procedures Online, V3, P19, DOI 10.1251/bpo20
   MOHANDAS N, 1993, SEMIN HEMATOL, V30, P171
   Mohler PJ, 2005, CURR OPIN CARDIOL, V20, P189, DOI 10.1097/01.hco.0000160372.95116.3e
   Mohler PJ, 2004, P NATL ACAD SCI USA, V101, P17533, DOI 10.1073/pnas.0403711101
   MURATA K, 1994, GEN COMP ENDOCR, V95, P232, DOI 10.1006/gcen.1994.1120
   MURATA K, 1991, DEV GROWTH DIFFER, V33, P553, DOI 10.1111/j.1440-169X.1991.00553.x
   Murata K, 2009, DEV GROWTH DIFFER, V51, P95, DOI 10.1111/j.1440-169X.2008.01084.x
   Nunomura W, 2000, J BIOL CHEM, V275, P24540, DOI 10.1074/jbc.M002492200
   NUNOMURA W, 2001, RES ADV BIOL CHEM, V1, P25
   NUNOMURA W, 2003, RECENT RES DEV CELL, V1, P67
   Nunomura W, 2007, COMP BIOCHEM PHYS B, V148, P124, DOI 10.1016/j.cbpb.2007.05.001
   Nunomura W, 2009, BIOCHEM J, V417, P141, DOI 10.1042/BJ20081372
   PASTERNACK GR, 1985, J BIOL CHEM, V260, P3676
   Shafizadeh E, 2002, DEVELOPMENT, V129, P4359
   Stennard FA, 2003, DEV BIOL, V262, P206, DOI 10.1016/S0012-1606(03)00385-3
   Takeuchi JK, 2005, DEVELOPMENT, V132, P2463, DOI 10.1242/dev.01827
   TANG TK, 1988, P NATL ACAD SCI USA, V85, P3713, DOI 10.1073/pnas.85.11.3713
   Tang Y, 2003, SCIENCE, V299, P574, DOI 10.1126/science.1075994
   Taylor-Harris PM, 2005, MAMM GENOME, V16, P137, DOI 10.1007/s00335-004-2436-7
   Taylor-Harris PM, 2005, CELL MOL BIOL LETT, V10, P135
NR 32
TC 4
Z9 6
U1 1
U2 2
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0012-1592
EI 1440-169X
J9 DEV GROWTH DIFFER
JI Dev. Growth Diff.
PD SEP
PY 2010
VL 52
IS 7
BP 591
EP 602
DI 10.1111/j.1440-169X.2010.01195.x
PG 12
WC Cell Biology; Developmental Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Developmental Biology
GA 643PR
UT WOS:000281311300003
PM 20887560
DA 2025-04-10
ER

PT J
AU Xu, Y
   Zhang, SL
   Malhotra, A
   Edelman-Novemsky, I
   Ma, JP
   Kruppa, A
   Cernicica, C
   Blais, S
   Neubert, TA
   Ren, MD
   Schlame, M
AF Xu, Yang
   Zhang, Shali
   Malhotra, Ashim
   Edelman-Novemsky, Irit
   Ma, Jinping
   Kruppa, Antonina
   Cernicica, Carolina
   Blais, Steven
   Neubert, Thomas A.
   Ren, Mindong
   Schlame, Michael
TI Characterization of Tafazzin Splice Variants from Humans and Fruit Flies
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID MASS-SPECTROMETRIC ANALYSIS; BARTH-SYNDROME; GENE; CARDIOLIPIN;
   TRANSACYLATION; EXPRESSION; DROSOPHILA; PATTERN; PROTEIN; MUTANT
AB The tafazzin gene encodes a phospholipid-lysophospholipid transacylase involved in cardiolipin metabolism, but it is not known why it forms multiple transcripts as a result of alternative splicing. Here we studied the intracellular localization, enzymatic activity, and metabolic function of four isoforms of human tafazzin and three isoforms of Drosophila tafazzin upon expression in different mammalian and insect systems. When expressed in HeLa cells, all isoforms were localized in mitochondria except for the B-form of Drosophila tafazzin, which was associated with multiple intracellular membranes. Among the human isoforms, only full-length tafazzin (FL) and tafazzin lacking exon 5 (Delta 5) had transacylase activity, and only these two isoforms were able to restore a normal cardiolipin pattern, normal respiratory activity of mitochondria, and male fertility in tafazzin-deficient flies. Both FL and Delta 5 were associated with large protein complexes in 293T cell mitochondria, but treatment with alkali and proteinase K suggested that the Delta 5 isoform was more integrated into the hydrophobic core of the membrane than the FL isoform. Although all Drosophila isoforms showed transacylase activity in vitro, only the A-form supported cardiolipin remodeling in flies. The data suggest that humans express two mitochondrial isoenzymes of tafazzin that have similar transacylase activities but different membrane topologies. Furthermore, the data show that the expression of human tafazzin in flies creates cardiolipin with a Drosophila pattern, suggesting that the characteristic fatty acid profile of cardiolipin is not determined by the substrate specificity of tafazzin.
C1 [Zhang, Shali; Edelman-Novemsky, Irit; Ma, Jinping; Kruppa, Antonina; Ren, Mindong; Schlame, Michael] NYU, Sch Med, Dept Cell Biol, New York, NY 10016 USA.
   [Cernicica, Carolina; Schlame, Michael] NYU, Sch Med, Dept Anesthesiol, New York, NY 10016 USA.
   [Blais, Steven; Neubert, Thomas A.] NYU, Sch Med, Kimmel Ctr Biol & Med, Skirball Inst, New York, NY 10016 USA.
   [Blais, Steven; Neubert, Thomas A.] NYU, Sch Med, Dept Pharmacol, New York, NY 10016 USA.
C3 New York University; New York University; New York University; New York
   University
RP Ren, MD (corresponding author), NYU, Sch Med, Dept Cell Biol, 550 1st Ave, New York, NY 10016 USA.
EM mindong.ren@nyumc.org; michael.schlame@med.nyu.edu
OI Kruppa, Antonina/0000-0001-5960-3904
FU National Institutes of Health [R01 HL078788, S10 RR14662, P30 NS050276];
   Barth Syndrome Foundation; United Mitochondrial Disease Foundation;
   Howard Hughes Medical Institute Summer Research Fellowship
FX This work was supported, in whole or in part, by National Institutes of
   Health Grants R01 HL078788 ( to M. S.) and S10 RR14662 and P30 NS050276
   ( to T. A. N.). This work was also supported by the Barth Syndrome
   Foundation and the United Mitochondrial Disease Foundation ( both to M.
   R.) and a Howard Hughes Medical Institute Summer Research Fellowship (
   to A. K.).
CR BARTH PG, 1983, J NEUROL SCI, V62, P327, DOI 10.1016/0022-510X(83)90209-5
   Beranek A, 2009, J BIOL CHEM, V284, P11572, DOI 10.1074/jbc.M805511200
   Bione S, 1996, NAT GENET, V12, P385, DOI 10.1038/ng0496-385
   BLIGH EG, 1959, CAN J BIOCHEM PHYS, V37, P911
   BRAND AH, 1993, DEVELOPMENT, V118, P401
   Claypool SM, 2008, MOL BIOL CELL, V19, P5143, DOI 10.1091/mbc.E08-09-0896
   Claypool SM, 2006, J CELL BIOL, V174, P379, DOI 10.1083/jcb.200605043
   Gonzalez IL, 2005, AM J MED GENET A, V134A, P409, DOI 10.1002/ajmg.a.30661
   Han XL, 2005, MASS SPECTROM REV, V24, P367, DOI 10.1002/mas.20023
   KELLEY RI, 1991, J PEDIATR-US, V119, P738, DOI 10.1016/S0022-3476(05)80289-6
   LOWRY OH, 1951, J BIOL CHEM, V193, P265
   Lu B, 2004, BIOCHEM CELL BIOL, V82, P569, DOI 10.1139/O04-055
   Ma LN, 2004, J BIOL CHEM, V279, P44394, DOI 10.1074/jbc.M405479200
   Magalhaes PJ, 1998, MOL BIOL CELL, V9, P2375, DOI 10.1091/mbc.9.9.2375
   Malhotra A, 2009, BBA-MOL CELL BIOL L, V1791, P314, DOI 10.1016/j.bbalip.2009.01.004
   Malhotra A, 2009, P NATL ACAD SCI USA, V106, P2337, DOI 10.1073/pnas.0811224106
   Oberstein A, 2005, NAT METHODS, V2, P583, DOI 10.1038/NMETH775
   Schlame M, 2002, ANN NEUROL, V51, P634, DOI 10.1002/ana.10176
   Schlame M, 2009, BBA-MOL CELL BIOL L, V1791, P321, DOI 10.1016/j.bbalip.2009.01.018
   Spencer CT, 2006, PEDIATRICS, V118, pE337, DOI 10.1542/peds.2005-2667
   Sun G, 2008, ANAL CHEM, V80, P7576, DOI 10.1021/ac801200w
   Testet E, 2005, BIOCHEM J, V387, P617, DOI 10.1042/BJ20041491
   Tress ML, 2007, P NATL ACAD SCI USA, V104, P5495, DOI 10.1073/pnas.0700800104
   Vaz FM, 2003, J BIOL CHEM, V278, P43089, DOI 10.1074/jbc.M305956200
   Vreken P, 2000, BIOCHEM BIOPH RES CO, V279, P378, DOI 10.1006/bbrc.2000.3952
   Wittig I, 2006, NAT PROTOC, V1, P418, DOI 10.1038/nprot.2006.62
   Xu Y, 2006, P NATL ACAD SCI USA, V103, P11584, DOI 10.1073/pnas.0603242103
   Xu Y, 2006, J BIOL CHEM, V281, P39217, DOI 10.1074/jbc.M606100200
NR 28
TC 56
Z9 70
U1 0
U2 9
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD OCT 16
PY 2009
VL 284
IS 42
BP 29230
EP 29239
DI 10.1074/jbc.M109.016642
PG 10
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 505GD
UT WOS:000270678900077
PM 19700766
OA hybrid, Green Published
DA 2025-04-10
ER

PT J
AU Shimoda, M
   Morita, S
   Obata, Y
   Sotomaru, Y
   Kono, T
   Hatada, I
AF Shimoda, M
   Morita, S
   Obata, Y
   Sotomaru, Y
   Kono, T
   Hatada, I
TI Imprinting of a small nucleolar RNA gene on mouse chromosome 12
SO GENOMICS
LA English
DT Article
ID XIST GENE; IDENTIFICATION; NUCLEUS; DISOMY; MICE
AB We have identified a novel, maternally expressed imprinted gene encoding a C/D-box small nucleolar RNA (snoRNA) called MBII-343, which may regulate RNA editing or alternative splicing of an as yet unknown target gene. This gene is closely linked to an imprinted gene, Meg3, on mouse distal chromosome 12, which is syntenic to human chromosome 14. The paternal duplication of mouse distal chromosome 12 leads to late embryonal/neonatal lethality, growth promotion, and cardiomyopathy, whereas maternal duplication leads to late embryonal lethality and growth retardation. Human paternal uniparental disomy for chromosome 14 leads to musculoskeletal problems and mental retardation, whereas maternal uniparental disomy leads to intrauterine growth retardation, motor developmental delay, premature puberty, hypotonia, joint laxity, macrocephaly, short statue, neonatal poor sucking, skill with jigsaw puzzles, skin picking, obesity, and maturity onset diabetes of the young.
C1 Gunma Univ, Ctr Gene Res, Maebashi, Gumma 3718511, Japan.
   Tokyo Univ Agr, Dept Biosci, Setagaya Ku, Tokyo 1568502, Japan.
C3 Gunma University; Tokyo University of Agriculture
RP Hatada, I (corresponding author), Gunma Univ, Ctr Gene Res, 3-39-22 Showa Machi, Maebashi, Gumma 3718511, Japan.
EM ihatada@showa.gunma-u.ac.jp
CR Bachellerie JP, 1997, TRENDS BIOCHEM SCI, V22, P257, DOI 10.1016/S0968-0004(97)01057-8
   BROCKDORFF N, 1992, CELL, V71, P515, DOI 10.1016/0092-8674(92)90519-I
   BROWN CJ, 1992, CELL, V71, P527, DOI 10.1016/0092-8674(92)90520-M
   Burns CM, 1997, NATURE, V387, P303, DOI 10.1038/387303a0
   Canton H, 1996, MOL PHARMACOL, V50, P799
   CATTANACH BM, 1985, NATURE, V315, P496, DOI 10.1038/315496a0
   Cavaillé J, 2000, P NATL ACAD SCI USA, V97, P14311, DOI 10.1073/pnas.250426397
   de los Santos T, 2000, AM J HUM GENET, V67, P1067, DOI 10.1086/303106
   Georgiades P, 2000, DEVELOPMENT, V127, P4719
   Hatada I, 2001, J BIOCHEM, V130, P187, DOI 10.1093/oxfordjournals.jbchem.a002971
   HENRY I, 1991, NATURE, V351, P665, DOI 10.1038/351665a0
   Hüttenhofer A, 2001, EMBO J, V20, P2943, DOI 10.1093/emboj/20.11.2943
   Manzoni MF, 2000, CLIN GENET, V57, P406, DOI 10.1034/j.1399-0004.2000.570514.x
   MCGRATH J, 1984, CELL, V37, P179, DOI 10.1016/0092-8674(84)90313-1
   Meguro M, 2001, HUM MOL GENET, V10, P383, DOI 10.1093/hmg/10.4.383
   Miyoshi N, 2000, GENES CELLS, V5, P211, DOI 10.1046/j.1365-2443.2000.00320.x
   NICHOLLS RD, 1989, NATURE, V342, P281, DOI 10.1038/342281a0
   Schuster-Gossler K, 1998, DEV DYNAM, V212, P214, DOI 10.1002/(SICI)1097-0177(199806)212:2<214::AID-AJA6>3.0.CO;2-K
   SEARLE AG, 1978, CYTOGENET CELL GENET, V20, P282, DOI 10.1159/000130859
   Sleutels F, 2000, CURR OPIN GENET DEV, V10, P229, DOI 10.1016/S0959-437X(00)00062-9
   Sotomaru Y, 2001, J BIOL CHEM, V276, P26694, DOI 10.1074/jbc.M101367200
   SURANI MAH, 1984, NATURE, V308, P548, DOI 10.1038/308548a0
   Tilghman SM, 1999, CELL, V96, P185, DOI 10.1016/S0092-8674(00)80559-0
   Villar AJ, 2001, GENESIS, V30, P274, DOI 10.1002/gene.1074
   Weinstein LB, 1999, CURR OPIN CELL BIOL, V11, P378, DOI 10.1016/S0955-0674(99)80053-2
NR 25
TC 12
Z9 12
U1 0
U2 3
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0888-7543
J9 GENOMICS
JI Genomics
PD APR
PY 2002
VL 79
IS 4
BP 483
EP 486
DI 10.1006/geno.2002.6727
PG 4
WC Biotechnology & Applied Microbiology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biotechnology & Applied Microbiology; Genetics & Heredity
GA 537ED
UT WOS:000174744600006
PM 11944978
DA 2025-04-10
ER

PT J
AU Rahimi, N
   Golde, TE
   Meyer, RD
AF Rahimi, Nader
   Golde, Todd E.
   Meyer, Rosana D.
TI Identification of Ligand-Induced Proteolytic Cleavage and Ectodomain
   Shedding of VEGFR-1/FLT1 in Leukemic Cancer Cells
SO CANCER RESEARCH
LA English
DT Article
ID ENDOTHELIAL GROWTH-FACTOR; ACUTE MYELOID-LEUKEMIA; RECEPTOR TYROSINE
   KINASE; MYELODYSPLASTIC SYNDROMES; MOLECULAR-MECHANISMS; FLT-1
   RECEPTORS; DOWN-REGULATION; VEGF; ACTIVATION; AUTOCRINE
AB Vascular endothelial growth factor receptor-1/fms-related tyrosine kinase 1 (VEGFR-1/FLT1) is expressed as a membrane-bound receptor tyrosine kinase and as an alternatively spliced soluble protein (sVEGFR-1) containing the 1-6 IgG-like domain of its ectodomain. sVEGFR-1 is known as a naturally occurring inhibitor of angiogenesis and as a surrogate marker for cancer progression; it is also linked to pregnancy-induced hypertension called preeclampsia and to avascularity of normal cornea. It remains an open question whether alternative mRNA splicing is the only mechanism by which sVEGFR-1 is generated. In this study, we show that in leukemic cancer cells, PIGF and VEGF-A both induce tyrosine phosphorylation of VEGFR-1 and render it susceptible to ectodomain shedding, resulting in the generation of sVEGFR-1 and an intracellular cytoplasmic fragment. Activation of protein kinase C and tumor necrosis factor-alpha-converting enzyme family metalloproteases are critically required for the occurrence of sVEGFR-1. Following the removal of the ectodomain, the remnant of VEGFR-1 remains attached to the membrane, and the activity of gamma-secretase/presenilin is required for its release from the cell membrane. We propose that sVEGFR-1 produced via ectodomain shedding plays a prominent role in the VEGF receptor system by antagonizing VEGF receptor signaling by acting as a dominant-negative form and/or forming a nonsignaling dimerizing complex with VEGF receptors. [Cancer Res 2009;69(6):2607-14]
C1 [Rahimi, Nader; Meyer, Rosana D.] Boston Univ, Sch Med, Dept Pathol, Boston, MA 02118 USA.
   [Rahimi, Nader; Meyer, Rosana D.] Boston Univ, Sch Med, Dept Ophthalmol, Boston, MA 02118 USA.
   [Golde, Todd E.] Mayo Clin, Coll Med, Dept Neurosci, Jacksonville, FL 32224 USA.
C3 Boston University; Boston University; Mayo Clinic
RP Rahimi, N (corresponding author), Boston Univ, Sch Med, Dept Pathol, Med Campus,Room 344,650 Albany St, Boston, MA 02118 USA.
EM nrahimi@bu.edu
OI Rahimi, Nader/0000-0002-6745-1725
FU NIH (National Eye Institute) [EY012997]
FX Grant support: NIH (National Eye Institute) grant EY012997 (N. Rahimi).
CR Aguayo A, 1999, BLOOD, V94, P3717, DOI 10.1182/blood.V94.11.3717.423k09_3717_3721
   Ambati BK, 2006, NATURE, V443, P993, DOI 10.1038/nature05249
   Aref S, 2005, HEMATOLOGY, V10, P131, DOI 10.1080/10245330500065797
   Bellamy WT, 2001, BLOOD, V97, P1427, DOI 10.1182/blood.V97.5.1427
   Cai J, 2006, J BIOL CHEM, V281, P3604, DOI 10.1074/jbc.M507401200
   Carpenter G, 2003, CURR OPIN CELL BIOL, V15, P143, DOI 10.1016/S0955-0674(03)00015-2
   Dello Sbarba P, 2002, BIOL CHEM, V383, P69
   DEVRIES C, 1992, SCIENCE, V255, P989, DOI 10.1126/science.1312256
   Fan HZ, 1999, EMBO J, V18, P6962, DOI 10.1093/emboj/18.24.6962
   Fiedler W, 1997, BLOOD, V89, P1870, DOI 10.1182/blood.V89.6.1870
   Fischer C, 2007, CELL, V131, P463, DOI 10.1016/j.cell.2007.08.038
   FONG GH, 1995, NATURE, V376, P66, DOI 10.1038/376066a0
   Fong GH, 1999, DEVELOPMENT, V126, P3015
   Fragoso R, 2006, BLOOD, V107, P1608, DOI 10.1182/blood-2005-06-2530
   Herold-Mende C, 1999, LAB INVEST, V79, P1573
   Hiratsuka S, 1998, P NATL ACAD SCI USA, V95, P9349, DOI 10.1073/pnas.95.16.9349
   Hu QL, 2004, CANCER-AM CANCER SOC, V100, P1884, DOI 10.1002/cncr.20187
   KENDALL RL, 1993, P NATL ACAD SCI USA, V90, P10705, DOI 10.1073/pnas.90.22.10705
   Keyt BA, 1996, J BIOL CHEM, V271, P5638, DOI 10.1074/jbc.271.10.5638
   Masood R, 2001, BLOOD, V98, P1904, DOI 10.1182/blood.V98.6.1904
   Meyer RD, 2006, J BIOL CHEM, V281, P867, DOI 10.1074/jbc.M506454200
   Mutter WP, 2008, MICROVASC RES, V75, P1, DOI 10.1016/j.mvr.2007.04.009
   Nath D, 2001, J CELL SCI, V114, P1213
   Orecchia A, 2003, J CELL SCI, V116, P3479, DOI 10.1242/jcs.00673
   Pillozzi S, 2007, BLOOD, V110, P1238, DOI 10.1182/blood-2006-02-003772
   Rahimi N, 2000, J BIOL CHEM, V275, P16986, DOI 10.1074/jbc.M000528200
   Rahimi N, 2006, EXP EYE RES, V83, P1005, DOI 10.1016/j.exer.2006.03.019
   Singh AJ, 2005, MOL BIOL CELL, V16, P2106, DOI 10.1091/mbc.E04-08-0749
   Vincent L, 2005, CANCER RES, V65, P3185, DOI 10.1158/0008-5472.CAN-04-3598
   WALTENBERGER J, 1994, J BIOL CHEM, V269, P26988
   Wang ES, 2004, BLOOD, V104, P2893, DOI 10.1182/blood-2004-01-0226
   Weihofen A, 2003, TRENDS CELL BIOL, V13, P71, DOI 10.1016/S0962-8924(02)00041-7
   Wierzbowska A, 2003, EUR CYTOKINE NETW, V14, P149
   Wiley HS, 2001, TRAFFIC, V2, P12, DOI 10.1034/j.1600-0854.2001.020103.x
   Yang SY, 2002, ARTERIOSCL THROM VAS, V22, P1797, DOI 10.1161/01.ATV.0000038995.31179.24
   Zeng HY, 2002, J BIOL CHEM, V277, P4003, DOI 10.1074/jbc.M110842200
NR 36
TC 65
Z9 72
U1 0
U2 2
PU AMER ASSOC CANCER RESEARCH
PI PHILADELPHIA
PA 615 CHESTNUT ST, 17TH FLOOR, PHILADELPHIA, PA 19106-4404 USA
SN 0008-5472
J9 CANCER RES
JI Cancer Res.
PD MAR 15
PY 2009
VL 69
IS 6
BP 2607
EP 2614
DI 10.1158/0008-5472.CAN-08-2905
PG 8
WC Oncology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Oncology
GA 424BU
UT WOS:000264541300056
PM 19276374
OA Green Accepted, Bronze
DA 2025-04-10
ER

PT J
AU Hanashima, A
   Hashimoto, K
   Ujihara, Y
   Honda, T
   Yobimoto, T
   Kodama, A
   Mohri, S
AF Hanashima, Akira
   Hashimoto, Ken
   Ujihara, Yoshihiro
   Honda, Takeshi
   Yobimoto, Tomoko
   Kodama, Aya
   Mohri, Satoshi
TI Complete primary structure of the I-band region of connectin at which
   mechanical property is modulated in zebrafish heart and skeletal muscle
SO GENE
LA English
DT Article
DE Connectin; Titin; Zebrafish; Heart; Muscle; Molecular evolution
ID MUSCULAR-DYSTROPHY; ELASTIC PROTEIN; CDNA SEQUENCE; Z-DISK; TITIN;
   EVOLUTION; EXON; CARDIOMYOPATHY; IMMUNOGLOBULIN; CONTRACTILITY
AB Connectin, also called titin, is the largest protein with a critical function as a molecular spring during contraction and relaxation of striated muscle; its mutation leads to severe myopathy and cardiomyopathy. To uncover the cause of this pathogenesis, zebrafish have recently been used as disease models because they are easier to genetically modify than mice. Although the gene structures and putative primary structures of zebrafish connectin have been determined, the actual primary structures of zebrafish connectin in heart and skeletal muscles remain unclear because of its large size and the PCR amplification-associated difficulties. In this research, using RT-PCR amplification from zebrafish heart and skeletal muscles, we determined the complete primary structures of zebrafish connectin in the I-band region at which mechanical property is modulated by alternative splicing. Our results showed that the domain structures of zebrafish connectins were largely similar to those of human connectins; however, the splicing pathways in the middle-Ig segment and the PEVK segment were highly diverse in every isoform. We also found that a set of 10 Ig domains in the middle-Ig segment of zebrafish connectin had been triplicated in human connectin. Because these triplicate regions are expressed in human leg and diaphragm, our findings may provide insight into the establishment of walking with limbs and lung respiration during tetra pod evolution. (C) 2016 Elsevier B.V. All rights reserved.
C1 [Hanashima, Akira; Hashimoto, Ken; Ujihara, Yoshihiro; Honda, Takeshi; Yobimoto, Tomoko; Kodama, Aya; Mohri, Satoshi] Kawasaki Med Sch, Dept Physiol 1, 577 Matsushima, Kurashiki, Okayama 7010192, Japan.
C3 Kawasaki Medical School
RP Hanashima, A (corresponding author), Kawasaki Med Sch, Dept Physiol 1, 577 Matsushima, Kurashiki, Okayama 7010192, Japan.
EM hanashima@med.kawasaki-m.ac.jp
OI Hashimoto, Ken/0000-0001-6194-9971
FU JSPS KAKENHI [16K01385, 26702014, 26282127]; Kawasaki Foundation for
   Medical Science and Medical Welfare; Grants-in-Aid for Scientific
   Research [16K01385, 26702014, 17H02092, 26282127] Funding Source: KAKEN
FX We thank Dr. S. Kimura of Jikei University for providing connectin
   antibodies. This work was supported by JSPS KAKENHI Grant Numbers
   16K01385 to A.H., 26702014 to Y.U. and 26282127 to S.M. and a Research
   Grant from the Kawasaki Foundation for Medical Science and Medical
   Welfare to A.H.
CR Buck D, 2014, J GEN PHYSIOL, V143, P215, DOI 10.1085/jgp.201311129
   Freiburg A, 2000, CIRC RES, V86, P1114
   Gotthardt M, 2003, J BIOL CHEM, V278, P6059, DOI 10.1074/jbc.M211723200
   Granzier HL, 2014, P NATL ACAD SCI USA, V111, P14589, DOI 10.1073/pnas.1411493111
   Granzier HL, 2009, CIRC RES, V105, P557, DOI 10.1161/CIRCRESAHA.109.200964
   Greaser ML, 2002, J MUSCLE RES CELL M, V23, P473, DOI 10.1023/A:1023410523184
   Hanashima A, 2012, METHODS, V56, P18, DOI 10.1016/j.ymeth.2011.12.010
   Katanosaka Y, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms4932
   Kenny PA, 1999, GENE, V232, P11, DOI 10.1016/S0378-1119(99)00122-5
   LABEIT S, 1995, SCIENCE, V270, P293, DOI 10.1126/science.270.5234.293
   Linke WA, 2014, CIRC RES, V114, P1052, DOI 10.1161/CIRCRESAHA.114.301286
   MARUYAMA K, 1976, J BIOCHEM, V80, P405, DOI 10.1093/oxfordjournals.jbchem.a131291
   MARUYAMA K, 1976, NATURE, V262, P58, DOI 10.1038/262058a0
   Miyake T, 2016, ANAT REC, V299, P1203, DOI 10.1002/ar.23392
   Myhre JL, 2014, DEV BIOL, V387, P93, DOI 10.1016/j.ydbio.2013.12.020
   Ohtsuka H, 1997, BIOCHEM BIOPH RES CO, V235, P1, DOI 10.1006/bbrc.1997.6534
   Ohtsuka S, 2011, J MOL BIOL, V409, P415, DOI 10.1016/j.jmb.2011.04.010
   Radke MH, 2007, P NATL ACAD SCI USA, V104, P3444, DOI 10.1073/pnas.0608543104
   Seeley M, 2007, CIRC RES, V100, P238, DOI 10.1161/01.RES.0000255758.69821.b5
   Soeno Y, 1999, MOL CELL BIOCHEM, V190, P125, DOI 10.1023/A:1006906107966
   Sorimachi H, 1997, J MOL BIOL, V270, P688, DOI 10.1006/jmbi.1997.1145
   Sorimachi H, 1995, J BIOL CHEM, V270, P31158, DOI 10.1074/jbc.270.52.31158
   Steffen LS, 2007, DEV BIOL, V309, P180, DOI 10.1016/j.ydbio.2007.06.015
   Tamura K, 2013, MOL BIOL EVOL, V30, P2725, DOI [10.1093/molbev/msr121, 10.1093/molbev/mst197]
   THOMPSON JD, 1994, NUCLEIC ACIDS RES, V22, P4673, DOI 10.1093/nar/22.22.4673
   Ujihara Y, 2016, CARDIOVASC RES, V111, P348, DOI 10.1093/cvr/cvw113
   WANG K, 1979, P NATL ACAD SCI USA, V76, P3698, DOI 10.1073/pnas.76.8.3698
   Watanabe K, 2002, J BIOL CHEM, V277, P11549, DOI 10.1074/jbc.M200356200
   Witt CC, 1998, J STRUCT BIOL, V122, P206, DOI 10.1006/jsbi.1998.3993
   Witt CC, 2006, EMBO J, V25, P3843, DOI 10.1038/sj.emboj.7601242
   Wright CF, 2005, NATURE, V438, P878, DOI 10.1038/nature04195
   Xu XL, 2002, NAT GENET, V30, P205, DOI 10.1038/ng816
   Yajima H, 1996, BIOCHEM BIOPH RES CO, V223, P160, DOI 10.1006/bbrc.1996.0862
   Young P, 1998, EMBO J, V17, P1614, DOI 10.1093/emboj/17.6.1614
   Zou J, 2015, ELIFE, V4, DOI 10.7554/eLife.09406
NR 35
TC 5
Z9 5
U1 1
U2 18
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
SN 0378-1119
EI 1879-0038
J9 GENE
JI Gene
PD JAN 5
PY 2017
VL 596
BP 19
EP 26
DI 10.1016/j.gene.2016.10.010
PG 8
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA ED8CF
UT WOS:000389098800003
PM 27725266
DA 2025-04-10
ER

PT J
AU De Serres-Bérard, T
   Benichou, SA
   Jauvin, D
   Boutjdir, M
   Puymirat, J
   Chahine, M
AF De Serres-Berard, Thiery
   Ait Benichou, Siham
   Jauvin, Dominic
   Boutjdir, Mohamed
   Puymirat, Jack
   Chahine, Mohamed
TI Recent Progress and Challenges in the Development of Antisense Therapies
   for Myotonic Dystrophy Type 1
SO INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
LA English
DT Review
DE antisense oligonucleotides; myotonic dystrophy type 1; myotonic
   dystrophy protein kinase; alternative splicing
ID RETRIEVER MUSCULAR-DYSTROPHY; HIGHLY NUCLEASE-RESISTANT; RNA-BINDING
   PROTEIN; MOUSE MODEL; INTRACELLULAR-DISTRIBUTION; SKELETAL-MUSCLE;
   CHLORIDE CHANNEL; SATELLITE CELLS; TARGETING DMPK; MICE LACKING
AB Myotonic dystrophy type 1 (DM1) is a dominant genetic disease in which the expansion of long CTG trinucleotides in the 3 ' UTR of the myotonic dystrophy protein kinase (DMPK) gene results in toxic RNA gain-of-function and gene mis-splicing affecting mainly the muscles, the heart, and the brain. The CUG-expanded transcripts are a suitable target for the development of antisense oligonucleotide (ASO) therapies. Various chemical modifications of the sugar-phosphate backbone have been reported to significantly enhance the affinity of ASOs for RNA and their resistance to nucleases, making it possible to reverse DM1-like symptoms following systemic administration in different transgenic mouse models. However, specific tissue delivery remains to be improved to achieve significant clinical outcomes in humans. Several strategies, including ASO conjugation to cell-penetrating peptides, fatty acids, or monoclonal antibodies, have recently been shown to improve potency in muscle and cardiac tissues in mice. Moreover, intrathecal administration of ASOs may be an advantageous complementary administration route to bypass the blood-brain barrier and correct defects of the central nervous system in DM1. This review describes the evolution of the chemical design of antisense oligonucleotides targeting CUG-expanded mRNAs and how recent advances in the field may be game-changing by forwarding laboratory findings into clinical research and treatments for DM1 and other microsatellite diseases.
C1 [De Serres-Berard, Thiery; Jauvin, Dominic; Chahine, Mohamed] Inst Univ Sante Mentale Quebec, CERVO Res Ctr, Quebec City, PQ G1J 2G3, Canada.
   [Ait Benichou, Siham; Puymirat, Jack] Univ Laval, CHU Quebec, LOEX, Res Ctr, Quebec City, PQ G1J 1Z4, Canada.
   [Boutjdir, Mohamed] VA New York Harbor Healthcare Syst, Cardiovasc Res Program, New York, NY 11209 USA.
   [Boutjdir, Mohamed] State Univ New York Downstate Hlth Sci Univ, Dept Med, Cell Biol & Pharmacol, New York, NY 11203 USA.
   [Boutjdir, Mohamed] NYU Sch Med, Dept Med, New York, NY 10016 USA.
   [Puymirat, Jack; Chahine, Mohamed] Univ Laval, Fac Med, Dept Med, Quebec City, PQ G1V 0A6, Canada.
C3 Laval University; Laval University; Laval University Hospital; State
   University of New York (SUNY) System; SUNY Downstate Health Sciences
   University; New York University; Laval University
RP Chahine, M (corresponding author), Inst Univ Sante Mentale Quebec, CERVO Res Ctr, Quebec City, PQ G1J 2G3, Canada.; Chahine, M (corresponding author), Univ Laval, Fac Med, Dept Med, Quebec City, PQ G1V 0A6, Canada.
EM mohamed.chahine@phc.ulaval.ca
RI ; Chahine, Mohamed/F-1199-2014
OI De Serres-Berard, Thiery/0000-0003-0663-009X; Chahine,
   Mohamed/0000-0002-9500-2839
FU Canadian Institutes of Health Research grant [MOP-130373]; Muscular
   Dystrophy Canada [855673-Chahine]; U.S. Department of Defense [USAMRAA
   W81XWH-21-1-0426, W81XWH-21-1-0424]; Biomedical Laboratory Research &
   Development Service of Veterans Affairs Office of Research and
   Development [BX002137]; National Heart, Lung, and Blood Institute
   [1R01HL164415-01]; Quebec Cell, Tissue, and Gene Therapy
   Network--TheCell; Canadian Institutes of Health Research (CIHR); Fonds
   de Recherche du Quebec-Sante (FRQS); Fondation du CHU de Quebec,
   Regenerative Medicine Axis
FX This work was funded by a Canadian Institutes of Health Research grant
   (MOP-130373) to M.C., a Muscular Dystrophy Canada grant
   (#855673-Chahine) to M.C., a U.S. Department of Defense grant (USAMRAA
   W81XWH-21-1-0426) to M.C., a Merit Review grant I01 BX002137 from
   Biomedical Laboratory Research & Development Service of Veterans Affairs
   Office of Research and Development to M.B., a National Heart, Lung, and
   Blood Institute grant 1R01HL164415-01 to M.B., and a U.S. Department of
   Defense award number W81XWH-21-1-0424 to M.B. The work was also
   supported by the Quebec Cell, Tissue, and Gene Therapy Network--TheCell.
   T.D.S.-B. was supported by studentships from the Canadian Institutes of
   Health Research (CIHR), the Fonds de Recherche du Quebec-Sante (FRQS),
   and the Fondation du CHU de Quebec, Regenerative Medicine Axis.
CR Benichou SA, 2022, HUM GENE THER, V33, P810, DOI 10.1089/hum.2022.069
   Algalarrondo V, 2015, NEUROMUSCULAR DISORD, V25, P308, DOI 10.1016/j.nmd.2014.11.018
   Alhamadani F, 2022, DRUG METAB DISPOS, V50, P879, DOI 10.1124/dmd.121.000418
   Amantana A, 2007, BIOCONJUGATE CHEM, V18, P1325, DOI 10.1021/bc070060v
   [Anonymous], SCI PUBLICATIONS PRE
   [Anonymous], 2007, Antisense Drug Technology: Principles, Strategies and Applications, V296, P2291, DOI 10.1201/9780849387951-18
   [Anonymous], 2022 MDA CLIN SCI C
   [Anonymous], SEARCH RESULTS DRUGB
   [Anonymous], INVESTORS AVIDITY BI
   Arandel L, 2017, DIS MODEL MECH, V10, P487, DOI 10.1242/dmm.027367
   Arthex Biotech|Pipeline, US
   Barbash IM, 2013, GENE THER, V20, P274, DOI 10.1038/gt.2012.38
   Bargiela A, 2019, P NATL ACAD SCI USA, V116, P25203, DOI 10.1073/pnas.1820297116
   Batra R, 2021, NAT BIOMED ENG, V5, DOI 10.1038/s41551-020-00607-7
   Benichou SA, 2022, GENE THER, V29, DOI 10.1038/s41434-022-00316-7
   Berul CI, 2000, J INTERV CARD ELECTR, V4, P351, DOI 10.1023/A:1009842114968
   Berul CI, 1999, J CLIN INVEST, V103, pR1, DOI 10.1172/JCI5346
   Betts C, 2012, MOL THER-NUCL ACIDS, V1, DOI 10.1038/mtna.2012.30
   Bish LT, 2012, MOL THER, V20, P580, DOI 10.1038/mt.2011.264
   Bisset DR, 2015, HUM MOL GENET, V24, P4971, DOI 10.1093/hmg/ddv219
   Bo XC, 2005, BIOINFORMATICS, V21, P1401, DOI 10.1093/bioinformatics/bti211
   Brautigam CA, 1998, J MOL BIOL, V277, P363, DOI 10.1006/jmbi.1997.1586
   Burel SA, 2013, NUCLEIC ACID THER, V23, P213, DOI 10.1089/nat.2013.0422
   Caillet-Boudin ML, 2014, FRONT MOL NEUROSCI, V6, DOI [10.3389/fnmo1.2013.00057, 10.3389/fnmol.2013.00057]
   Carrell ST, 2016, HUM MOL GENET, V25, P4328, DOI 10.1093/hmg/ddw266
   Cerro-Herreros E, 2021, MOL THER-NUCL ACIDS, V26, P174, DOI 10.1016/j.omtn.2021.07.017
   Cerro-Herreros E, 2020, MOL THER NUCL ACIDS, V21, P837, DOI 10.1016/j.omtn.2020.07.021
   Cerro-Herreros E, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-04892-4
   Chan JHP, 2006, CLIN EXP PHARMACOL P, V33, P533, DOI 10.1111/j.1440-1681.2006.04403.x
   Chappell AE, 2020, NUCLEIC ACIDS RES, V48, P4382, DOI 10.1093/nar/gkaa164
   Charleston JS, 2018, NEUROLOGY, V90, pE2146, DOI 10.1212/WNL.0000000000005680
   Charlet-B N, 2002, MOL CELL, V10, P45, DOI 10.1016/S1097-2765(02)00572-5
   Christou M, 2020, NUCLEIC ACID THER, V30, P80, DOI 10.1089/nat.2019.0811
   Cirak S, 2011, LANCET, V378, P595, DOI 10.1016/S0140-6736(11)60756-3
   Cox DC, 2020, HUM MOL GENET, V29, P1729, DOI 10.1093/hmg/ddaa095
   Crooke ST, 2020, J AM CHEM SOC, V142, P14754, DOI 10.1021/jacs.0c04928
   Crooke ST, 2017, NAT BIOTECHNOL, V35, P230, DOI 10.1038/nbt.3779
   DECLERCQ E, 1969, SCIENCE, V165, P1137
   Desjardins C.A., 2022, NUCL ACIDS RES, V10, P10
   Di Costanzo A, 2002, NEUROMUSCULAR DISORD, V12, P476, DOI 10.1016/S0960-8966(01)00324-8
   Ding Y, 2004, NUCLEIC ACIDS RES, V32, pW135, DOI 10.1093/nar/gkh449
   Dowdy SF, 2017, NAT BIOTECHNOL, V35, P222, DOI 10.1038/nbt.3802
   Du LT, 2011, HUM MOL GENET, V20, P3151, DOI 10.1093/hmg/ddr217
   EGHOLM M, 1993, NATURE, V365, P566, DOI 10.1038/365566a0
   Faria M, 2001, NAT BIOTECHNOL, V19, P40, DOI 10.1038/83489
   Fernández-Garibay X, 2021, BIOFABRICATION, V13, DOI 10.1088/1758-5090/abf6ae
   Finkel RS, 2017, NEW ENGL J MED, V377, P1723, DOI 10.1056/NEJMoa1702752
   Franc DT, 2012, NEUROMUSCULAR DISORD, V22, P483, DOI 10.1016/j.nmd.2012.01.003
   François V, 2011, NAT STRUCT MOL BIOL, V18, P85, DOI 10.1038/nsmb.1958
   Frank DE, 2020, NEUROLOGY, V94, pE2270, DOI 10.1212/WNL.0000000000009233
   Frazier KS, 2015, TOXICOL PATHOL, V43, P78, DOI 10.1177/0192623314551840
   Furling D, 2001, NEUROMUSCULAR DISORD, V11, P728, DOI 10.1016/S0960-8966(01)00226-7
   Furling D, 2003, GENE THER, V10, P795, DOI 10.1038/sj.gt.3301955
   Furling D, 2001, HUM MOL GENET, V10, P2079, DOI 10.1093/hmg/10.19.2079
   Gadgil A, 2021, J GENE MED, V23, DOI 10.1002/jgm.3321
   Gao YZ, 2016, MOL THER, V24, P1378, DOI 10.1038/mt.2016.97
   Geary RS, 2015, ADV DRUG DELIVER REV, V87, P46, DOI 10.1016/j.addr.2015.01.008
   González-Barriga A, 2017, NUCLEIC ACID THER, V27, P144, DOI 10.1089/nat.2016.0641
   González-Barriga A, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0121556
   González-Barriga A, 2013, MOL THER-NUCL ACIDS, V2, DOI 10.1038/mtna.2013.9
   Goyenvalle A, 2012, HUM MOL GENET, V21, P2559, DOI 10.1093/hmg/dds082
   GRYAZNOV SM, 1995, P NATL ACAD SCI USA, V92, P5798, DOI 10.1073/pnas.92.13.5798
   Gudde AEEG, 2016, HUM MOL GENET, V25, P1648, DOI 10.1093/hmg/ddw042
   Hagedorn PH, 2022, NUCLEIC ACID THER, V32, P151, DOI 10.1089/nat.2021.0071
   Hagedorn PH, 2013, NUCLEIC ACID THER, V23, P302, DOI 10.1089/nat.2013.0436
   HARLEY HG, 1992, LANCET, V339, P1125, DOI 10.1016/0140-6736(92)90729-M
   Henry SP, 2002, INT IMMUNOPHARMACOL, V2, P1657, DOI 10.1016/S1567-5769(02)00142-X
   Heo YA, 2020, DRUGS, V80, P329, DOI 10.1007/s40265-020-01267-2
   Hernández-Hernández O, 2013, BRAIN, V136, P957, DOI 10.1093/brain/aws367
   Ho TH, 2005, HUM MOL GENET, V14, P1539, DOI 10.1093/hmg/ddi162
   Hsieh WC, 2018, BIOCHEMISTRY-US, V57, P907, DOI 10.1021/acs.biochem.7b01239
   Hu NY, 2021, MOL THER-NUCL ACIDS, V23, P393, DOI 10.1016/j.omtn.2020.11.014
   Hu N, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-07517-y
   Huguet A, 2012, PLOS GENET, V8, DOI 10.1371/journal.pgen.1003043
   Ionis Pharmaceuticals-Industry Updates On Drug Development, 2018 MDF ANN C MYOT
   Itoh K, 2019, MOLECULES, V24, DOI 10.3390/molecules24173175
   Jansen G, 1996, NAT GENET, V13, P316, DOI 10.1038/ng0796-316
   Jauvin D, 2017, MOL THER-NUCL ACIDS, V7, P465, DOI 10.1016/j.omtn.2017.05.007
   Kaliman P, 2005, J BIOL CHEM, V280, P8016, DOI 10.1074/jbc.M412845200
   Kanadia RN, 2006, P NATL ACAD SCI USA, V103, P11748, DOI 10.1073/pnas.0604970103
   Kanadia RN, 2003, SCIENCE, V302, P1978, DOI 10.1126/science.1088583
   Kielpinski LJ, 2021, NUCLEIC ACID THER, V31, P383, DOI 10.1089/nat.2021.0055
   Klein AF, 2019, J CLIN INVEST, V129, P4739, DOI 10.1172/JCI128205
   Koebis M, 2013, SCI REP-UK, V3, DOI 10.1038/srep02242
   Koller E, 2011, NUCLEIC ACIDS RES, V39, P4795, DOI 10.1093/nar/gkr089
   Labayru G, 2022, SCI REP-UK, V12, DOI 10.1038/s41598-022-07820-1
   Lam LT, 2000, HUM MOL GENET, V9, P2167, DOI 10.1093/hmg/9.14.2167
   Langbehn KE, 2021, NEUROL-GENET, V7, DOI 10.1212/NXG.0000000000000537
   Langlois MA, 2003, MOL THER, V7, P670, DOI 10.1016/S1525-0016(03)00068-6
   Larsen Jan, 2011, BMC Res Notes, V4, P490, DOI 10.1186/1756-0500-4-490
   Lee HJ, 2002, J NUCL MED, V43, P948
   Lee JE, 2012, P NATL ACAD SCI USA, V109, P4221, DOI 10.1073/pnas.1117019109
   Leger AJ, 2013, NUCLEIC ACID THER, V23, P109, DOI 10.1089/nat.2012.0404
   Lehto T, 2014, NUCLEIC ACIDS RES, V42, P3207, DOI 10.1093/nar/gkt1220
   LEONETTI JP, 1991, P NATL ACAD SCI USA, V88, P2702, DOI 10.1073/pnas.88.7.2702
   Lim KRQ, 2017, DRUG DES DEV THER, V11, P533, DOI 10.2147/DDDT.S97635
   Lin YF, 2010, P NATL ACAD SCI USA, V107, P692, DOI 10.1073/pnas.0909740107
   Llagostera E, 2007, PLOS ONE, V2, DOI 10.1371/journal.pone.0001134
   Llagostera E, 2012, MUSCLE NERVE, V45, P128, DOI 10.1002/mus.22256
   Mahadevan MS, 2021, INT J MOL SCI, V22, DOI 10.3390/ijms222111874
   Mahadevan MS, 2006, NAT GENET, V38, P1066, DOI 10.1038/ng1857
   Mankodi A, 2000, SCIENCE, V289, P1769, DOI 10.1126/science.289.5485.1769
   Mankodi A, 2002, MOL CELL, V10, P35, DOI 10.1016/S1097-2765(02)00563-4
   Mankodi A, 2001, HUM MOL GENET, V10, P2165, DOI 10.1093/hmg/10.19.2165
   Manning KS, 2017, ACS CHEM BIOL, V12, P2503, DOI 10.1021/acschembio.7b00416
   McClorey G, 2018, BIOMEDICINES, V6, DOI 10.3390/biomedicines6020051
   Messina S, 2020, J CLIN MED, V9, DOI 10.3390/jcm9072222
   Miller CM, 2016, NUCLEIC ACIDS RES, V44, P2782, DOI 10.1093/nar/gkw112
   Min HS, 2020, ANGEW CHEM INT EDIT, V59, P8173, DOI 10.1002/anie.201914751
   Miyashita K, 2007, CHEM COMMUN, P3765, DOI 10.1039/b707352f
   Mondragon-Gonzalez R, 2018, DIS MODEL MECH, V11, DOI 10.1242/dmm.034728
   Morita K, 2002, BIOORG MED CHEM LETT, V12, P73, DOI 10.1016/S0960-894X(01)00683-7
   Moulton HM, 2010, BBA-BIOMEMBRANES, V1798, P2296, DOI 10.1016/j.bbamem.2010.02.012
   Mounsey JP, 2000, J BIOL CHEM, V275, P23362, DOI 10.1074/jbc.M000899200
   Mulders SAM, 2009, P NATL ACAD SCI USA, V106, P13915, DOI 10.1073/pnas.0905780106
   Mullard A, 2022, NAT REV DRUG DISCOV, V21, P6, DOI 10.1038/d41573-021-00213-5
   Nakamori M, 2013, ANN NEUROL, V74, P862, DOI 10.1002/ana.23992
   Nakamori M, 2011, MOL THER, V19, P2222, DOI 10.1038/mt.2011.191
   Neil Erin E, 2019, J Pediatr Pharmacol Ther, V24, P194, DOI 10.5863/1551-6776-24.3.194
   NeuBase Therapeutics, PRES NEW PREC DAT MD
   NIELSEN PE, 1991, SCIENCE, V254, P1497, DOI 10.1126/science.1962210
   Nielsen PE, 2004, MOL BIOTECHNOL, V26, P233, DOI 10.1385/MB:26:3:233
   Ohrt T, 2006, NUCLEIC ACIDS RES, V34, P1369, DOI 10.1093/nar/gkl001
   Orengo JP, 2008, P NATL ACAD SCI USA, V105, P2646, DOI 10.1073/pnas.0708519105
   Ostergaard ME, 2019, NUCLEIC ACIDS RES, V47, P6045, DOI 10.1093/nar/gkz360
   Overby SJ, 2022, MOL THER-NUCL ACIDS, V27, P1146, DOI 10.1016/j.omtn.2022.02.003
   Owczarzy R, 2008, NUCLEIC ACIDS RES, V36, pW163, DOI 10.1093/nar/gkn198
   Pallan PS, 2012, CHEM COMMUN, V48, P8195, DOI 10.1039/c2cc32286b
   Pandey SK, 2015, J PHARMACOL EXP THER, V355, P329, DOI 10.1124/jpet.115.226969
   Pantic B, 2016, EXP CELL RES, V342, P39, DOI 10.1016/j.yexcr.2016.02.013
   Partridge W, 2021, NUCLEIC ACID THER, V31, P417, DOI 10.1089/nat.2020.0917
   Paterson Judy, 2016, Drug Discov Today Technol, V20, P49, DOI 10.1016/j.ddtec.2016.07.009
   Pelletier R, 2009, NEUROBIOL DIS, V36, P181, DOI 10.1016/j.nbd.2009.07.009
   Prakash TP, 2019, NUCLEIC ACIDS RES, V47, P6029, DOI 10.1093/nar/gkz354
   Prakash TP, 2016, J MED CHEM, V59, P2718, DOI 10.1021/acs.jmedchem.5b01948
   Presentations: NeuBase Therapeutics Inc. (NBSE), US
   Rahman SMA, 2008, J AM CHEM SOC, V130, P4886, DOI 10.1021/ja710342q
   Reddy S, 1996, NAT GENET, V13, P325, DOI 10.1038/ng0796-325
   Renna LV, 2017, PLOS ONE, V12, DOI 10.1371/journal.pone.0184987
   Roberts R, 1997, P NATL ACAD SCI USA, V94, P13221, DOI 10.1073/pnas.94.24.13221
   Roberts TC, 2020, NAT REV DRUG DISCOV, V19, P673, DOI 10.1038/s41573-020-0075-7
   Romero-Palomo F, 2021, TOXICOL PATHOL, V49, P1174, DOI 10.1177/01926233211011615
   Sahu B, 2011, J ORG CHEM, V76, P5614, DOI 10.1021/jo200482d
   Savkur RS, 2001, NAT GENET, V29, P40, DOI 10.1038/ng704
   Sciabola S, 2021, PLOS ONE, V16, DOI 10.1371/journal.pone.0238753
   Seth Punit P, 2008, Nucleic Acids Symp Ser (Oxf), P553, DOI 10.1093/nass/nrn280
   Seznec H, 2000, HUM MOL GENET, V9, P1185, DOI 10.1093/hmg/9.8.1185
   Shen W, 2019, NAT BIOTECHNOL, V37, P640, DOI 10.1038/s41587-019-0106-2
   Sobczak K, 2013, MOL THER, V21, P380, DOI 10.1038/mt.2012.222
   Son HW, 2018, METHODS MOL BIOL, V1828, P57, DOI 10.1007/978-1-4939-8651-4_3
   SPROAT BS, 1989, NUCLEIC ACIDS RES, V17, P3373, DOI 10.1093/nar/17.9.3373
   STEIN CA, 1988, NUCLEIC ACIDS RES, V16, P3209, DOI 10.1093/nar/16.8.3209
   Sugo T, 2016, J CONTROL RELEASE, V237, P1, DOI 10.1016/j.jconrel.2016.06.036
   Summerton J, 1997, ANTISENSE NUCLEIC A, V7, P187, DOI 10.1089/oli.1.1997.7.187
   Sun HG, 2014, MOL THER-NUCL ACIDS, V3, DOI 10.1038/mtna.2014.32
   Suzuki R, 2007, J CONTROL RELEASE, V117, P130, DOI 10.1016/j.jconrel.2006.09.008
   Swayze EE, 2007, NUCLEIC ACIDS RES, V35, P687, DOI 10.1093/nar/gkl1071
   De Serres-Bérard T, 2021, NEUROBIOL DIS, V160, DOI 10.1016/j.nbd.2021.105532
   Trujillo AJ, 2019, ADV EXP MED BIOL, V1185, P119, DOI 10.1007/978-3-030-27378-1_20
   Tsoumpra MK, 2019, EBIOMEDICINE, V45, P630, DOI 10.1016/j.ebiom.2019.06.036
   van der Bent ML, 2019, FASEB J, V33, P11314, DOI 10.1096/fj.201900263R
   Vester B, 2004, BIOCHEMISTRY-US, V43, P13233, DOI 10.1021/bi0485732
   Vickers TA, 2000, NUCLEIC ACIDS RES, V28, P1340, DOI 10.1093/nar/28.6.1340
   Vulin A, 2012, MOL THER, V20, P2120, DOI 10.1038/mt.2012.181
   WALDER RY, 1988, P NATL ACAD SCI USA, V85, P5011, DOI 10.1073/pnas.85.14.5011
   WALKER I, 1995, PHARMACEUT RES, V12, P1548, DOI 10.1023/A:1016260110049
   Wang GS, 2007, J CLIN INVEST, V117, P2802, DOI 10.1172/JCI32308
   Wang PY, 2017, HUM MOL GENET, V26, P2247, DOI 10.1093/hmg/ddx115
   Wang SY, 2019, NUCLEIC ACID THER, V29, P245, DOI 10.1089/nat.2019.0794
   Wang YL, 2021, ADV SCI, V8, DOI 10.1002/advs.202004929
   Wei C, 2018, FASEB J, V32, P2073, DOI 10.1096/fj.201700700R
   Wein N, 2022, MOL THER METH CLIN D, V26, P279, DOI 10.1016/j.omtm.2022.07.005
   Wheeler TM, 2007, J CLIN INVEST, V117, P3952, DOI 10.1172/JCI33355
   Wheeler TM, 2012, NATURE, V488, P111, DOI 10.1038/nature11362
   Wheeler TM, 2009, SCIENCE, V325, P336, DOI 10.1126/science.1173110
   WHITING EJ, 1995, HUM MOL GENET, V4, P1063, DOI 10.1093/hmg/4.6.1063
   Wojtkowiak-Szlachcic A, 2015, NUCLEIC ACIDS RES, V43, P3318, DOI 10.1093/nar/gkv163
   Xie J, 2020, FRONT PHARMACOL, V11, DOI 10.3389/fphar.2020.00697
   Yadava RS, 2021, HUM MOL GENET, V30, P1111, DOI 10.1093/hmg/ddab108
   Yadava RS, 2020, HUM MOL GENET, V29, P1440, DOI 10.1093/hmg/ddaa060
   YAMAMOTO T, 1994, ANTISENSE RES DEV, V4, P119, DOI 10.1089/ard.1994.4.119
   Yin Q, 2020, CELL RES, V30, P133, DOI 10.1038/s41422-019-0264-2
   Yu RZ, 2016, MOL THER NUCL ACIDS, V5, DOI 10.1038/mtna.2016.26
   Yuan Y, 2007, NUCLEIC ACIDS RES, V35, P5474, DOI 10.1093/nar/gkm601
   Zanotti S, 2021, NEUROMUSCULAR DISORD, V31, pS120, DOI 10.1016/j.nmd.2021.07.257
   Zeniya S, 2018, J CONTROL RELEASE, V283, P126, DOI 10.1016/j.jconrel.2018.05.010
NR 186
TC 13
Z9 13
U1 0
U2 5
PU MDPI
PI BASEL
PA MDPI AG, Grosspeteranlage 5, CH-4052 BASEL, SWITZERLAND
SN 1661-6596
EI 1422-0067
J9 INT J MOL SCI
JI Int. J. Mol. Sci.
PD NOV
PY 2022
VL 23
IS 21
AR 13359
DI 10.3390/ijms232113359
PG 28
WC Biochemistry & Molecular Biology; Chemistry, Multidisciplinary
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Chemistry
GA 6D3KH
UT WOS:000882593300001
PM 36362145
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Lutskiy, MI
   Rosen, FS
   Remold-O'Donnell, E
AF Lutskiy, MI
   Rosen, FS
   Remold-O'Donnell, E
TI Genotype-proteotype linkage in the Wiskott-Aldrich syndrome
SO JOURNAL OF IMMUNOLOGY
LA English
DT Article
ID WASP GENE-MUTATIONS; SYNDROME PROTEIN; N-WASP; LINKED THROMBOCYTOPENIA;
   MISSENSE MUTATIONS; IDENTIFICATION; PHENOTYPE; ACTIVATION; MECHANISM;
   COMPLEX
AB Wiskott-Aldrich syndrome (WAS) is a platelet/immunodeficiency disease arising from mutations of WAS protein (WASP), a hemopoietic cytoskeletal protein. Clinical symptoms vary widely from mild (X-linked thrombocytopenia) to life threatening. In this study, we examined the molecular effects of individual mutations by quantifying WASP in peripheral lymphocytes of 44 patients and identifying the molecular variant (collectively called proteotype). Nonpredicted proteotypes were found for 14 genotypes. These include WASP-negative lymphocytes found for five missense genotypes and WASP-positive lymphocytes for two nonsense, five frameshift, and two splice site genotypes. Missense mutations in the Ena/VASP homology 1 (EVH1) domain lead to decreased/absent WASP but normal mRNA levels, indicating that proteolysis causes the protein deficit. Because several of the EVH1 missense mutations alter WIP binding sites, the findings suggest that abrogation of WIP binding induces proteolysis. Whereas platelets of most patients were previously shown to lack WASP, WASP-positive platelets were found for two atypical patients, both of whom have mutations outside the EVH1 domain. WASP variants with alternative splicing and intact C-terminal domains were characterized for eight nonsense and frameshift genotypes. One of these, a nonsense genotype in a mild patient, supports expression of WASP lacking half of the proline-rich region. With one notable exception, genotype and proteotype were linked, indicating that a genotype-proteotype registry could be assembled to aid in predicting disease course and planning therapy for newly diagnosed infants. Knowledge of the molecular effect of mutations would aid also in identifying disease-modifying genes.
C1 CBR Biomed Res Inst, Boston, MA 02115 USA.
   Harvard Univ, Sch Med, Dept Pediat, Boston, MA 02115 USA.
C3 Harvard University; Harvard University Medical Affiliates; Boston
   Children's Hospital; Program in Cellular & Molecular Medicine (PCMM);
   Harvard University; Harvard Medical School
RP CBR Biomed Res Inst, 800 Huntington Ave, Boston, MA 02115 USA.
EM remold@cbr.med.harvard.edu
FU NHLBI NIH HHS [HL 59561] Funding Source: Medline; NIAID NIH HHS [AI
   39574] Funding Source: Medline
CR DERRY JMJ, 1994, CELL, V78, P635, DOI 10.1016/0092-8674(94)90528-2
   Filipovich AH, 2001, BLOOD, V97, P1598, DOI 10.1182/blood.V97.6.1598
   Greer WL, 1996, HUM GENET, V98, P685, DOI 10.1007/s004390050285
   Haddad E, 1999, BLOOD, V94, P509, DOI 10.1182/blood.V94.2.509.414k09_509_518
   Hagemann TL, 1999, BIOCHEM BIOPH RES CO, V256, P104, DOI 10.1006/bbrc.1999.0292
   Halford WP, 1999, ANAL BIOCHEM, V266, P181, DOI 10.1006/abio.1998.2913
   Imai K, 2004, BLOOD, V103, P456, DOI 10.1182/blood-2003-05-1480
   Jin YZ, 2004, BLOOD, V104, P4010, DOI 10.1182/blood-2003-05-1592
   Jones LN, 2002, BLOOD CELL MOL DIS, V28, P392, DOI 10.1006/bcmd.2002.0523
   KENNEY D M, 1990, Current Opinion in Pediatrics, V2, P931, DOI 10.1097/00008480-199010000-00014
   Kim AS, 2000, NATURE, V404, P151, DOI 10.1038/35004513
   KWAN SP, 1995, P NATL ACAD SCI USA, V92, P4706, DOI 10.1073/pnas.92.10.4706
   KWAN SP, 1995, HUM MOL GENET, V4, P1995, DOI 10.1093/hmg/4.10.1995
   Lemahieu V, 1999, HUM MUTAT, V14, P54, DOI 10.1002/(SICI)1098-1004(1999)14:1<54::AID-HUMU7>3.0.CO;2-E
   Lutskiy MI, 2002, HUM GENET, V110, P515, DOI 10.1007/s00439-002-0716-4
   Lutskiy MI, 2002, BLOOD, V100, P2763, DOI 10.1182/blood-2002-02-0388
   Miki H, 1998, NATURE, V391, P93, DOI 10.1038/34208
   Moreau V, 2000, NAT CELL BIOL, V2, P441, DOI 10.1038/35017080
   MURPHY S, 1969, NEW ENGL J MED, V281, P857, DOI 10.1056/NEJM196910162811601
   Nagy E, 1998, TRENDS BIOCHEM SCI, V23, P198, DOI 10.1016/S0968-0004(98)01208-0
   Notarangelo LD, 2002, BLOOD, V99, P2268, DOI 10.1182/blood.V99.6.2268
   Ochs HD, 1999, PRIMARY IMMUNODEFICIENCY DISEASES, P292
   PADGETT RA, 1986, ANNU REV BIOCHEM, V55, P1119, DOI 10.1146/annurev.biochem.55.1.1119
   Park JY, 2004, CLIN EXP IMMUNOL, V136, P104, DOI 10.1111/j.1365-2249.2004.02409.x
   PERRY GS, 1980, J PEDIATR-US, V97, P72, DOI 10.1016/S0022-3476(80)80133-8
   Prehoda KE, 1999, CELL, V97, P471, DOI 10.1016/S0092-8674(00)80757-6
   Rees DD, 1999, AM J RESP CELL MOL, V20, P69, DOI 10.1165/ajrcmb.20.1.3306
   RemoldODonnell E, 1997, J IMMUNOL, V158, P4021
   Rohatgi R, 2000, J CELL BIOL, V150, P1299, DOI 10.1083/jcb.150.6.1299
   Rong SB, 2000, J MOL MED, V78, P530, DOI 10.1007/s001090000136
   Sasahara Y, 2002, MOL CELL, V10, P1269, DOI 10.1016/S1097-2765(02)00728-1
   Scherbina A, 1999, J IMMUNOL, V163, P6314
   Schindelhauer D, 1996, HUM GENET, V98, P68, DOI 10.1007/s004390050162
   Shcherbina A, 2003, BRIT J HAEMATOL, V121, P529, DOI 10.1046/j.1365-2141.2003.04310.x
   Silverman GA, 2001, J BIOL CHEM, V276, P33293, DOI 10.1074/jbc.R100016200
   Stewart DM, 1999, J IMMUNOL, V162, P5019
   SULLIVAN KE, 1994, J PEDIATR-US, V125, P876, DOI 10.1016/S0022-3476(05)82002-5
   Thrasher AJ, 2002, NAT REV IMMUNOL, V2, P635, DOI 10.1038/nri884
   Volkman BF, 2002, CELL, V111, P565, DOI 10.1016/S0092-8674(02)01076-0
   WENGLER GS, 1995, BLOOD, V86, P3648, DOI 10.1182/blood.V86.10.3648.bloodjournal86103648
   Wiskott A., 1937, MONATSSCHR KINDERHEI, V68, P212
   WOLFF JA, 1967, J PEDIATR-US, V70, P221, DOI 10.1016/S0022-3476(67)80417-7
   Zhu QL, 1997, BLOOD, V90, P2680, DOI 10.1182/blood.V90.7.2680.2680_2680_2689
NR 43
TC 46
Z9 53
U1 0
U2 2
PU AMER ASSOC IMMUNOLOGISTS
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA
SN 0022-1767
EI 1550-6606
J9 J IMMUNOL
JI J. Immunol.
PD JUL 15
PY 2005
VL 175
IS 2
BP 1329
EP 1336
DI 10.4049/jimmunol.175.2.1329
PG 8
WC Immunology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Immunology
GA 989BJ
UT WOS:000233647600082
PM 16002738
OA Bronze
DA 2025-04-10
ER

PT J
AU Britanova, O
   Lukyanov, S
   Gruss, P
   Tarabykin, V
AF Britanova, O
   Lukyanov, S
   Gruss, P
   Tarabykin, V
TI The mouse Laf4 gene:: Exon/intron organization, cDNA sequence,
   alternative splicing, and expression during central nervous system
   development
SO GENOMICS
LA English
DT Article
DE cortex; transcription factor; subtraction; Sey; reeler; mutant
ID FMR2; PROTEIN; LEUKEMIA; IDENTITY; ROLES; BRAIN; PAX6; MLL
AB The cerebral cortex is a tissue with a high degree of neuronal diversity. It consists of six cell layers with a unique set of neuronal subtypes. A crucial step in the process of cortical differentiation is the transition from a mitotically active neuroblast to a postmitotic young neuron. To identify genes involved in the control of this transition, we applied a novel method of cDNA subtraction based on mirror-orientation selection. One of the genes we have identified in our screening proved to be a mouse homolog of the human putative transcription factor LAF4. We identified alternatively spliced forms of mouse Laf4 that encode several forms of putative protein with potentially different transactivation functions. Two forms are expressed mainly during embryogenesis, whereas the other forms are expressed mainly in adults. We have found that Laf4 transcription becomes very quickly upregulated as soon as young cortical neurons leave the ventricular zone (VZ), the cortical-proliferative compartment. This coincides with the initial steps of cortical differentiation. Laf4 becomes downregulated in postnatal cortex, indicating its involvement in the transcriptional regulation of the early steps of cortical differentiation. We have also examined Laf4 expression in the brains of Sey and reeler mutants. Laf4 was downregulated in the lateroventral part of the cerebral cortex and completely lost in the piriform cortex of the Sey mutant embryos. We also compared its expression during central nervous system development with that of its closest homolog, Fmr2, a gene implicated in mental retardation in humans.
C1 Max Planck Inst Biophys Chem, Dept Mol Cell Biol, D-37077 Gottingen, Germany.
   MM Shemyakin Inst Bioorgan Chem, Moscow 117631, Russia.
C3 Max Planck Society; Russian Academy of Sciences; Pushchino Scientific
   Center for Biological Research (PSCBI) of the Russian Academy of
   Sciences; Institute of Bioorganic Chemistry of the Russian Academy of
   Sciences
RP Max Planck Inst Expt Med, Dept Mol Biol Neuronal Signals, Hermann Rein Str 3, D-37075 Gottingen, Germany.
EM vtaraby@gwdg.de
RI Britanova, Olga/L-8788-2016; Lukyanov, Sergey/F-9140-2014
OI Britanova, Olga/0000-0002-6295-1392
CR Bayer S.A., 1991, NEOCORTICAL DEV
   Bernier PJ, 1998, J NEUROSCI, V18, P2486
   Chakrabarti L, 1998, HUM MOL GENET, V7, P441, DOI 10.1093/hmg/7.3.441
   DOMER PH, 1993, P NATL ACAD SCI USA, V90, P7884, DOI 10.1073/pnas.90.16.7884
   Gecz J, 1999, EUR J HUM GENET, V7, P157, DOI 10.1038/sj.ejhg.5200279
   Gecz J, 1997, GENOMICS, V44, P201, DOI 10.1006/geno.1997.4867
   Gecz J, 1996, NAT GENET, V13, P105, DOI 10.1038/ng0596-105
   Hillman MA, 2001, J HUM GENET, V46, P251, DOI 10.1007/s100380170074
   Lee JK, 1999, MOL BRAIN RES, V66, P133, DOI 10.1016/S0169-328X(99)00035-2
   Ma C, 1996, BLOOD, V87, P734, DOI 10.1182/blood.V87.2.734.bloodjournal872734
   Matz M, 1999, NUCLEIC ACIDS RES, V27, P1558, DOI 10.1093/nar/27.6.1558
   Prasad R, 1995, P NATL ACAD SCI USA, V92, P12160, DOI 10.1073/pnas.92.26.12160
   RAKIC P, 1995, NEURON, V14, P1101, DOI 10.1016/0896-6273(95)90258-9
   Rebrikov DV, 2000, NUCLEIC ACIDS RES, V28, DOI 10.1093/nar/28.20.e90
   Stoykova A, 2000, J NEUROSCI, V20, P8042
   Taki T, 1999, P NATL ACAD SCI USA, V96, P14535, DOI 10.1073/pnas.96.25.14535
   Tang AH, 2001, DEVELOPMENT, V128, P801
   Tarabykin V, 2001, DEVELOPMENT, V128, P1983
   Toresson H, 2000, DEVELOPMENT, V127, P4361
   URBANEK P, 1994, CELL, V79, P901, DOI 10.1016/0092-8674(94)90079-5
   Wittwer F, 2001, DEVELOPMENT, V128, P791
NR 21
TC 17
Z9 19
U1 0
U2 7
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0888-7543
EI 1089-8646
J9 GENOMICS
JI Genomics
PD JUL
PY 2002
VL 80
IS 1
BP 31
EP 37
DI 10.1006/geno.2002.6796
PG 7
WC Biotechnology & Applied Microbiology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biotechnology & Applied Microbiology; Genetics & Heredity
GA 567QH
UT WOS:000176495300007
PM 12079280
DA 2025-04-10
ER

PT J
AU Werfel, S
   Nothjunge, S
   Schwarzmayr, T
   Strom, TM
   Meitinger, T
   Engelhardt, S
AF Werfel, Stanislas
   Nothjunge, Stephan
   Schwarzmayr, Thomas
   Strom, Tim-Matthias
   Meitinger, Thomas
   Engelhardt, Stefan
TI Characterization of circular RNAs in human, mouse and rat hearts
SO JOURNAL OF MOLECULAR AND CELLULAR CARDIOLOGY
LA English
DT Article
DE Circular RNA; circRNA; Heart; Titin
ID GENE
AB Deep sequencing techniques and advanced data analysis methods recently enabled the characterization of thousands of circular RNA isoforms (circRNAs) from a number of tissues and organisms. There is emerging evidence that some circRNAs may have important biological functions or serve as diagnostic biomarkers in disease conditions.
   In order to analyze circRNA expression in the heart and its changes in different conditions we performed RNA-Seq analysis of ribosome-depleted libraries from rats (neonatal and adult), mice (sham or after transverse aortic constriction, TAC) and humans (failing, non-failing). All samples were sequenced after treatment with exonuclease RNase R or a mock treatment and >9000 candidate circRNAs were detected for each species. Additionally, we performed separate isolation of nuclear and cytoplasmic RNA and co-immunoprecipitated RNA interacting with endogenous argonaute 2 (Ago2) in primary cardiac myocytes. We found circRNAs to be significantly enriched in the cytoplasm compared to linear transcripts and to have a similar level of association with Ago2.
   Notably in all three species we observed dozens of circRNAs arising from the titin (Ttn) gene, which is known to undergo highly complex alternative splicing during heart maturation. Correspondingly we observed extensive differential regulation of Ttn circRNAs between neonatal and adult rat hearts, suggesting that circRNA formation could be involved in the regulation of titin splicing.
   We expect that our inventory of cardiac circRNAs, as well as the information on their conservation and differential expression will provide an important basis for further studies addressing their function and suitability as biomarkers. (C) 2016 The Authors. Published by Elsevier Ltd.
C1 [Werfel, Stanislas; Nothjunge, Stephan; Engelhardt, Stefan] Tech Univ Munich, Inst Pharmakol & Toxikol, Munich, Germany.
   [Werfel, Stanislas; Meitinger, Thomas; Engelhardt, Stefan] DZHK German Ctr Cardiovasc Res, Partner Site Munich Heart Alliance, Munich, Germany.
   [Schwarzmayr, Thomas; Strom, Tim-Matthias; Meitinger, Thomas] German Res Ctr Environm Hlth GmbH, Inst Human Genet, Helmholtz Zentrum Munchen, Neuherberg, Germany.
   [Strom, Tim-Matthias; Meitinger, Thomas] Tech Univ Munich, Inst Human Genet, Munich, Germany.
C3 Technical University of Munich; German Centre for Cardiovascular
   Research; Munich Heart Alliance; Helmholtz Association; Helmholtz-Center
   Munich - German Research Center for Environmental Health; Technical
   University of Munich
RP Engelhardt, S (corresponding author), Tech Univ Munich, Inst Pharmakol & Toxikol, Munich, Germany.
EM stefan.engelhardt@tum.de
RI Engelhardt, Stefan/HJH-5744-2023; Meitinger, Thomas/O-1318-2015
OI Engelhardt, Stefan/0000-0001-5378-8661; Werfel,
   Stanislas/0000-0001-9130-0057; Meitinger, Thomas/0000-0002-8838-8403;
   Nothjunge, Stephan/0000-0003-4845-3765
FU Bavarian Ministry of Sciences, Research and the Arts in the framework of
   the Bavarian Molecular Biosystems Research Network
FX This work was supported by the Bavarian Ministry of Sciences, Research
   and the Arts in the framework of the Bavarian Molecular Biosystems
   Research Network.
CR Ashwal-Fluss R, 2014, MOL CELL, V56, P55, DOI 10.1016/j.molcel.2014.08.019
   Guo W, 2012, NAT MED, V18, P766, DOI 10.1038/nm.2693
   Hansen TB, 2013, NATURE, V495, P384, DOI 10.1038/nature11993
   Jakobi T, 2016, GENOM PROTEOM BIOINF, V14, P216, DOI 10.1016/j.gpb.2016.02.003
   Jeck WR, 2014, NAT BIOTECHNOL, V32, P453, DOI 10.1038/nbt.2890
   Koh W, 2014, P NATL ACAD SCI USA, V111, P7361, DOI 10.1073/pnas.1405528111
   Krüger M, 2011, J BIOL CHEM, V286, P9905, DOI 10.1074/jbc.R110.173260
   Li XF, 1999, J BIOL CHEM, V274, P8153, DOI 10.1074/jbc.274.12.8153
   Memczak S, 2013, NATURE, V495, P333, DOI 10.1038/nature11928
   Michalik KM, 2014, CIRC RES, V114, P1389, DOI 10.1161/CIRCRESAHA.114.303265
   Salzman J, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0030733
NR 11
TC 248
Z9 279
U1 0
U2 48
PU ELSEVIER SCI LTD
PI OXFORD
PA THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND
SN 0022-2828
EI 1095-8584
J9 J MOL CELL CARDIOL
JI J. Mol. Cell. Cardiol.
PD SEP
PY 2016
VL 98
BP 103
EP 107
DI 10.1016/j.yjmcc.2016.07.007
PG 5
WC Cardiac & Cardiovascular Systems; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology; Cell Biology
GA DY0KQ
UT WOS:000384786100012
PM 27476877
OA Green Published, hybrid
DA 2025-04-10
ER

PT J
AU Scavello, F
   Zeni, F
   Tedesco, CC
   Mensà, E
   Veglia, F
   Procopio, AD
   Bonfigli, AR
   Olivieri, F
   Raucci, A
AF Scavello, Francesco
   Zeni, Filippo
   Tedesco, Calogero C.
   Mensa, Emanuela
   Veglia, Fabrizio
   Procopio, Antonio Domenico
   Bonfigli, Anna Rita
   Olivieri, Fabiola
   Raucci, Angela
TI Modulation of soluble receptor for advanced glycation end-products
   (RAGE) isoforms and their ligands in healthy aging
SO AGING-US
LA English
DT Article
DE RAGE isoforms; aging; inflammaging; biomarker; cardiovascular risk;
   obesity
ID PLASMINOGEN-ACTIVATOR INHIBITOR-1; ENDOGENOUS SECRETORY RECEPTOR;
   PULMONARY-FIBROSIS; METABOLIC SYNDROME; SPLICE VARIANTS; AGE; RISK;
   INFLAMMATION; PLASMA; MARKER
AB The receptor for advanced glycation end-products (RAGE) recognizes several ligands involved in inflammatory diseases. Two circulating soluble isoforms exist: esRAGE derived from alternative splicing and cRAGE generated by the membrane-bound RAGE (FL-RAGE) proteolysis. Together, esRAGE and cRAGE constitute sRAGE and function as decoy receptors preventing FL-RAGE/ligands binding.
   We determined serum concentration of both, esRAGE and cRAGE, and their ligands AGEs, HMGB1 and S100A8/A9 in a healthy population of 169 subjects aged 20-90 years. cRAGE showed a negative (r=-0.375, P<0.0001) while AGEs (r=0.160, P=0.0384) and S100A8/A9 (r=0.207, P=0.0091) a positive correlation with age. esRAGE did not change during aging and inversely correlated with Hemoglobin, ALT, insulin, HOMA index, Waist-Hip ratio (W/H), Waist Circumference (WC) and positively with AGEs. cRAGE exhibited also an inverse correlation with WC, W/H, PAI-1, HMGB1, AGEs and S100A8/A9. Age, W/H, HMGB1, S100A8/A9 and AGEs are independent predictors of cRAGE, whereas W/H and AGEs associate with esRAGE. Treatment of cells with glycated albumin reduced cRAGE production and upregulated FL-RAGE.
   These results indicate that in a healthy population cRAGE is a biomarker of aging while esRAGE represents a more reliable marker of obesity and insulin resistance. Hence, sRAGE isoforms levels could be differentially associated with age-related diseases risk factors.
C1 [Scavello, Francesco; Zeni, Filippo; Raucci, Angela] Ctr Cardiol Monzino IRCCS, Unit Expt Cardiooncol & Cardiovasc Aging, Milan, Italy.
   [Tedesco, Calogero C.; Veglia, Fabrizio] Ctr Cardiol Monzino IRCCS, Unit Biostat, Milan, Italy.
   [Mensa, Emanuela; Procopio, Antonio Domenico; Olivieri, Fabiola] Univ Politecn Marche, DISCLIMO, Dept Clin & Mol Sci, Ancona, Italy.
   [Procopio, Antonio Domenico; Olivieri, Fabiola] IRCCS INRCA, Ctr Clin Pathol & Innovat Therapy, Ancona, Italy.
   [Bonfigli, Anna Rita] IRCCS INRCA, Sci Direct, Ancona, Italy.
C3 IRCCS Centro Cardiologico Monzino; IRCCS Centro Cardiologico Monzino;
   Marche Polytechnic University; IRCCS INRCA; IRCCS INRCA
RP Raucci, A (corresponding author), Ctr Cardiol Monzino IRCCS, Unit Expt Cardiooncol & Cardiovasc Aging, Milan, Italy.
EM araucci@ccfm.it
RI Bonfigli, Anna/J-7248-2016; Procopio, Antonio/AAB-2451-2021; Raucci,
   Angela/K-3722-2018; Tedesco, Calogero/ABI-1690-2020; Olivieri,
   Fabiola/K-6465-2016; Scavello, Francesco/AHE-5653-2022; Veglia,
   Fabrizio/K-1958-2016; Mensa, Emanuela/K-2459-2018
OI Procopio, Antonio/0000-0001-6897-8724; Olivieri,
   Fabiola/0000-0002-9606-1144; Raucci, Angela/0000-0003-1333-9671;
   Scavello, Francesco/0000-0002-0297-0946; tedesco, calogero
   claudio/0009-0002-6237-078X; Veglia, Fabrizio/0000-0002-9378-8874;
   Mensa, Emanuela/0000-0002-3284-6161
FU Fondazione Cariplo (Research on Ageing diseases 2015); Centro
   Cardiologico Monzino-IRCCS (Ricerca Corrente 2016-2019); Fellowship of
   Fondazione IEO-Monzino 2017-2018
FX This work was supported by funding from Fondazione Cariplo (Research on
   Ageing diseases 2015) and Centro Cardiologico Monzino-IRCCS (Ricerca
   Corrente 2016-2019) to Angela Raucci. Francesco Scavello was supported
   by a Fellowship of Fondazione IEO-Monzino 2017-2018.
CR [Anonymous], 2016, DEF OLD ELD PERS
   Antonelli A, 2017, BBA-GEN SUBJECTS, V1861, P354, DOI 10.1016/j.bbagen.2016.11.040
   Barnard SA, 2016, BLOOD REV, V30, P421, DOI 10.1016/j.blre.2016.05.002
   Catalán V, 2011, MOL MED, V17, P1157, DOI 10.2119/molmed.2011.00144
   Colhoun HM, 2011, DIABETES, V60, P2379, DOI 10.2337/db11-0291
   Demling N, 2006, CELL TISSUE RES, V323, P475, DOI 10.1007/s00441-005-0069-0
   Di Maggio S, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0153832
   Di Pino A, 2017, J CLIN ENDOCR METAB, V102, P3756, DOI 10.1210/jc.2017-00954
   Dimmeler S, 2013, EMBO MOL MED, V5, P180, DOI 10.1002/emmm.201201986
   Dozio E, 2017, EUR J NUTR, V56, P2557, DOI 10.1007/s00394-016-1291-0
   Eren M, 2014, SEMIN THROMB HEMOST, V40, P645, DOI 10.1055/s-0034-1387883
   Falcone C, 2005, ARTERIOSCL THROM VAS, V25, P1032, DOI 10.1161/01.ATV.0000160342.20342.00
   Franceschi C, 2014, J GERONTOL A-BIOL, V69, pS4, DOI 10.1093/gerona/glu057
   Fritz G, 2011, TRENDS BIOCHEM SCI, V36, P625, DOI 10.1016/j.tibs.2011.08.008
   Frommhold D, 2010, BLOOD, V116, P841, DOI 10.1182/blood-2009-09-244293
   Fujisawa K, 2013, ATHEROSCLEROSIS, V227, P425, DOI 10.1016/j.atherosclerosis.2013.01.016
   Gaens KHJ, 2009, J CLIN ENDOCR METAB, V94, P5174, DOI 10.1210/jc.2009-1067
   Galichet A, 2008, BIOCHEM BIOPH RES CO, V370, P1, DOI 10.1016/j.bbrc.2008.02.163
   Geroldi D, 2006, J AM GERIATR SOC, V54, P1149, DOI 10.1111/j.1532-5415.2006.00776.x
   Herold K, 2007, J LEUKOCYTE BIOL, V82, P204, DOI 10.1189/jlb.1206751
   Hudson BI, 2008, FASEB J, V22, P1572, DOI 10.1096/fj.07-9909com
   Hudson BI, 2008, J BIOL CHEM, V283, P34457, DOI 10.1074/jbc.M801465200
   Kalea AZ, 2011, FRONT BIOSCI-LANDMRK, V16, P2756, DOI 10.2741/3884
   Kalea AZ, 2009, FASEB J, V23, P1766, DOI 10.1096/fj.08-117739
   Kislinger T, 1999, J BIOL CHEM, V274, P31740, DOI 10.1074/jbc.274.44.31740
   Liu Q, 2016, GENET MOL RES, V15, DOI 10.4238/gmr.15028414
   López-Díez R, 2013, GENOME BIOL EVOL, V5, P2420, DOI 10.1093/gbe/evt188
   Mahajan N, 2013, INT J CARDIOL, V168, P1788, DOI 10.1016/j.ijcard.2013.05.013
   Miller S, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0164041
   Miranda ER, 2018, NUTR METAB CARDIOVAS, V28, P1155, DOI 10.1016/j.numecd.2018.07.009
   Miranda ER, 2017, AM J PHYSIOL-ENDOC M, V313, pE631, DOI 10.1152/ajpendo.00146.2017
   Mistry R, 2004, J GERONTOL A-BIOL, V59, P1068
   Momma H, 2014, J CLIN ENDOCR METAB, V99, P587, DOI 10.1210/jc.2013-2936
   Mukherjee TK, 2005, BBA-MOL CELL RES, V1745, P300, DOI 10.1016/j.bbamcr.2005.03.012
   Mukhopadhyay S, 2005, BBA-MOL CELL RES, V1745, P145, DOI 10.1016/j.bbamcr.2005.03.010
   Norata GD, 2009, NUTR METAB CARDIOVAS, V19, P129, DOI 10.1016/j.numecd.2008.03.004
   Ohlmeier S, 2010, PROTEOM CLIN APPL, V4, P97, DOI 10.1002/prca.200900128
   Olivieri F, 2014, AGING-US, V6, P771, DOI 10.18632/aging.100693
   Orlova VV, 2007, EMBO J, V26, P1129, DOI 10.1038/sj.emboj.7601552
   Park' L, 1998, NAT MED, V4, P1025, DOI 10.1038/2012
   Penzo M, 2010, J IMMUNOL, V184, P4497, DOI 10.4049/jimmunol.0903131
   Prakash J, 2015, MECH AGEING DEV, V145, P18, DOI 10.1016/j.mad.2015.01.001
   Queisser MA, 2008, AM J RESP CELL MOL, V39, P337, DOI 10.1165/rcmb.2007-0244OC
   Raucci A, 2008, FASEB J, V22, P3716, DOI 10.1096/fj.08-109033
   Reichert S, 2017, ATHEROSCLEROSIS, V266, P234, DOI 10.1016/j.atherosclerosis.2017.08.015
   Reynaert NL, 2016, INT J BIOCHEM CELL B, V81, P403, DOI 10.1016/j.biocel.2016.06.016
   Sessa L, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0086903
   Shirasawa M, 2004, GENES CELLS, V9, P165, DOI 10.1111/j.1356-9597.2004.00712.x
   Song F, 2014, DIABETES, V63, P1948, DOI 10.2337/db13-1636
   Soro-Paavonen A, 2008, DIABETES, V57, P2461, DOI 10.2337/db07-1808
   Sourris KC, 2010, DIABETOLOGIA, V53, P2442, DOI 10.1007/s00125-010-1837-2
   St-Onge MP, 2010, NUTRITION, V26, P152, DOI 10.1016/j.nut.2009.07.004
   Vazzana N, 2012, J CLIN ENDOCR METAB, V97, pE1726, DOI 10.1210/jc.2012-1473
   Volz HC, 2012, BASIC RES CARDIOL, V107, DOI 10.1007/s00395-012-0250-z
   Volz HC, 2010, BASIC RES CARDIOL, V105, P805, DOI 10.1007/s00395-010-0114-3
   Yamakawa N, 2011, AM J PHYSIOL-LUNG C, V300, pL516, DOI 10.1152/ajplung.00118.2010
   Yamamoto K, 2014, SEMIN THROMB HEMOST, V40, P652, DOI 10.1055/s-0034-1384635
   Yonekura H, 2003, BIOCHEM J, V370, P1097, DOI 10.1042/BJ20021371
   Zaki M, 2017, EXCLI J, V16, P973, DOI 10.17179/excli2017-275
   Zhang L, 2008, J BIOL CHEM, V283, P35507, DOI 10.1074/jbc.M806948200
NR 60
TC 36
Z9 37
U1 0
U2 4
PU IMPACT JOURNALS LLC
PI ORCHARD PARK
PA 6666 E QUAKER ST, STE 1, ORCHARD PARK, NY 14127 USA
SN 1945-4589
J9 AGING-US
JI Aging-US
PD MAR 31
PY 2019
VL 11
IS 6
BP 1648
EP 1663
DI 10.18632/aging.101860
PG 16
WC Cell Biology; Geriatrics & Gerontology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Geriatrics & Gerontology
GA HR8LI
UT WOS:000463408300011
PM 30903794
OA Green Published, Green Submitted, gold
DA 2025-04-10
ER

PT J
AU Ketley, A
   Chen, CZ
   Li, X
   Arya, S
   Robinson, TE
   Granados-Riveron, J
   Udosen, I
   Morris, GE
   Holt, I
   Furling, D
   Chaouch, S
   Haworth, B
   Southall, N
   Shinn, P
   Zheng, W
   Austin, CP
   Hayes, CJ
   Brook, JD
AF Ketley, Ami
   Chen, Catherine Z.
   Li, Xin
   Arya, Sukrat
   Robinson, Thelma E.
   Granados-Riveron, Javier
   Udosen, Inyang
   Morris, Glenn E.
   Holt, Ian
   Furling, Denis
   Chaouch, Soraya
   Haworth, Ben
   Southall, Noel
   Shinn, Paul
   Zheng, Wei
   Austin, Christopher P.
   Hayes, Christopher J.
   Brook, J. David
TI High-content screening identifies small molecules that remove nuclear
   foci, affect MBNL distribution and CELF1 protein levels via a
   PKC-independent pathway in myotonic dystrophy cell lines
SO HUMAN MOLECULAR GENETICS
LA English
DT Article
ID EXPANDED-REPEAT TRANSCRIPTS; 3 UNTRANSLATED REGION; MUSCULAR-DYSTROPHY;
   TRIPLET-REPEAT; MESSENGER-RNA; IN-VIVO; TRINUCLEOTIDE REPEAT; RATIONAL
   DESIGN; SKELETAL-MUSCLE; CTG REPEAT
AB Myotonic dystrophy (DM) is a multi-system neuromuscular disorder for which there is no treatment. We have developed a medium throughput phenotypic assay, based on the identification of nuclear foci in DM patient cell lines using in situ hybridization and high-content imaging to screen for potentially useful therapeutic compounds. A series of further assays based on molecular features of DM have also been employed. Two compounds that reduce and/or remove nuclear foci have been identified, Ro 31-8220 and chromomycin A3. Ro 31-8220 is a PKC inhibitor, previously shown to affect the hyperphosphorylation of CELF1 and ameliorate the cardiac phenotype in a DM1 mouse model. We show that the same compound eliminates nuclear foci, reduces MBNL1 protein in the nucleus, affects ATP2A1 alternative splicing and reduces steady-state levels of CELF1 protein. We demonstrate that this effect is independent of PKC activity and conclude that this compound may be acting on alternative kinase targets within DM pathophysiology. Understanding the activity profile for this compound is key for the development of targeted therapeutics in the treatment of DM.
C1 [Ketley, Ami; Li, Xin; Arya, Sukrat; Robinson, Thelma E.; Granados-Riveron, Javier; Udosen, Inyang; Brook, J. David] Univ Nottingham, Queens Med Ctr, Sch Life Sci, Nottingham NG7 2UH, England.
   [Chen, Catherine Z.; Southall, Noel; Shinn, Paul; Zheng, Wei; Austin, Christopher P.; Hayes, Christopher J.] NIH, Natl Ctr Adv Translat Sci, Bethesda, MD 20892 USA.
   [Morris, Glenn E.; Holt, Ian] RJAH Orthopaed Hosp, Wolfson Ctr Inherited Neuromuscular Dis, Oswestry SY10 7AG, Shrops, England.
   [Morris, Glenn E.; Holt, Ian] Keele Univ, Inst Sci & Technol Med, Keele, Staffs, England.
   [Furling, Denis; Chaouch, Soraya] Univ Paris 06, UM 76, Inst Myol, F-75013 Paris, France.
   [Furling, Denis; Chaouch, Soraya] INSERM, U974, F-75013 Paris, France.
   [Furling, Denis; Chaouch, Soraya] CNRS, UMR7215, F-75013 Paris, France.
   [Haworth, Ben] Mol Devices, Wokingham RG41 5TS, Berks, England.
   [Hayes, Christopher J.] Univ Nottingham, Sch Chem, Nottingham NG7 2RD, England.
C3 University of Nottingham; National Institutes of Health (NIH) - USA; NIH
   National Center for Advancing Translational Sciences (NCATS); Keele
   University; Keele University; Sorbonne Universite; Institut National de
   la Sante et de la Recherche Medicale (Inserm); Centre National de la
   Recherche Scientifique (CNRS); University of Nottingham
RP Brook, JD (corresponding author), Univ Nottingham, Queens Med Ctr, Sch Life Sci, Nottingham NG7 2UH, England.
EM david.brook@nottingham.ac.uk
RI Granados-Riverón, Javier/F-9768-2010; Hayes, Christopher J./B-6022-2016;
   Zheng, Wei/J-8889-2014; Furling, Denis/M-2346-2017; Southall,
   Noel/H-8991-2012
OI Hayes, Christopher J./0000-0003-1692-3646; Zheng,
   Wei/0000-0003-1034-0757; Brook, John David/0000-0002-5946-6740;
   Granados-Riveron, Javier T./0000-0002-0368-225X; Furling,
   Denis/0000-0001-7912-4409; Southall, Noel/0000-0003-4500-880X;
   Granados-Riveron, Javier Tadeo/0000-0001-5485-654X
FU MRC DPFS; Muscular Dystrophy Campaign; Leverhulme Trust; Myotonic
   Dystrophy Support Group; Association Francaise contre les Myopathies;
   Marigold Foundation Research fellowship for CZC; Medical Research
   Council; intramural research of the National Centre for Advancing
   Translational Sciences, NIH; MRC [MC_G0900866, G0802629] Funding Source:
   UKRI
FX This research was funded by an MRC DPFS award, the Muscular Dystrophy
   Campaign, the Leverhulme Trust, the Myotonic Dystrophy Support Group,
   the Association Francaise contre les Myopathies, intramural research of
   the National Centre for Advancing Translational Sciences, NIH, and a
   Marigold Foundation Research fellowship for CZC. Funding to pay the Open
   Access publication charges for this article was provided by the Medical
   Research Council.
CR Arambula JF, 2009, P NATL ACAD SCI USA, V106, P16068, DOI 10.1073/pnas.0901824106
   BERMAN E, 1985, BIOCHEMISTRY-US, V24, P6887, DOI 10.1021/bi00345a022
   BROOK JD, 1992, CELL, V68, P799, DOI 10.1016/0092-8674(92)90154-5
   Chakrabarti S, 2001, BIOPOLYMERS, V56, P85, DOI 10.1002/1097-0282(2000)56:2<85::AID-BIP1054>3.0.CO;2-7
   Chaouch S, 2009, HUM GENE THER, V20, P784, DOI 10.1089/hum.2008.163
   Chen CM, 2012, J ELECTRON MATER, V41, P1, DOI 10.1007/s11664-011-1777-8
   Dansithong W, 2005, J BIOL CHEM, V280, P5773, DOI 10.1074/jbc.M410781200
   Davis BM, 1997, P NATL ACAD SCI USA, V94, P7388, DOI 10.1073/pnas.94.14.7388
   Disney MD, 2010, CHEMBIOCHEM, V11, P375, DOI 10.1002/cbic.200900716
   Fardaei M, 2002, HUM MOL GENET, V11, P805, DOI 10.1093/hmg/11.7.805
   Fardaei M, 2001, NUCLEIC ACIDS RES, V29, P2766, DOI 10.1093/nar/29.13.2766
   FU YH, 1992, SCIENCE, V255, P1256, DOI 10.1126/science.1546326
   García-López A, 2011, P NATL ACAD SCI USA, V108, P11866, DOI 10.1073/pnas.1018213108
   Gareiss PC, 2008, J AM CHEM SOC, V130, P16254, DOI 10.1021/ja804398y
   Hamshere MG, 1997, P NATL ACAD SCI USA, V94, P7394, DOI 10.1073/pnas.94.14.7394
   Harper P.S. Monckton., 2001, MYOTONIC DYSTROPHY, V3e
   Hernández-Hernández O, 2006, J NEUROSCI RES, V84, P841, DOI 10.1002/jnr.20989
   Hino S, 2007, HUM MOL GENET, V16, P2834, DOI 10.1093/hmg/ddm239
   Holt I, 2007, GENES CELLS, V12, P1035, DOI 10.1111/j.1365-2443.2007.01112.x
   Huang RL, 2011, SCI TRANSL MED, V3, DOI 10.1126/scitranslmed.3001862
   Huichalaf C, 2010, FASEB J, V24, P3706, DOI 10.1096/fj.09-151159
   Huichalaf C, 2009, J NEUROSCI, V29, P9042, DOI 10.1523/JNEUROSCI.1983-09.2009
   Jin JL, 2009, CELL CYCLE, V8, P2356, DOI 10.4161/cc.8.15.9248
   KAZIRO Y, 1965, BIOCHEM BIOPH RES CO, V19, P433, DOI 10.1016/0006-291X(65)90142-7
   Kimura T, 2005, HUM MOL GENET, V14, P2189, DOI 10.1093/hmg/ddi223
   Kuyumcu-Martinez NM, 2007, MOL CELL, V28, P68, DOI 10.1016/j.molcel.2007.07.027
   Lin XY, 2006, HUM MOL GENET, V15, P2087, DOI 10.1093/hmg/ddl132
   Liquori CL, 2001, SCIENCE, V293, P864, DOI 10.1126/science.1062125
   Machuca-Tzili L, 2005, MUSCLE NERVE, V32, P1, DOI 10.1002/mus.20301
   MAHADEVAN M, 1992, SCIENCE, V255, P1253, DOI 10.1126/science.1546325
   Mankodi A, 2002, MOL CELL, V10, P35, DOI 10.1016/S1097-2765(02)00563-4
   Mankodi A, 2001, HUM MOL GENET, V10, P2165, DOI 10.1093/hmg/10.19.2165
   Mulders SAM, 2009, P NATL ACAD SCI USA, V106, P13915, DOI 10.1073/pnas.0905780106
   O'Leary Debra A, 2010, Curr Chem Genomics, V4, P9, DOI 10.2174/1875397301004010009
   O'Leary DA, 2009, PLOS ONE, V4, DOI 10.1371/journal.pone.0008348
   Orengo JP, 2006, NUCLEIC ACIDS RES, V34, DOI 10.1093/nar/gkl967
   Philips AV, 1998, SCIENCE, V280, P737, DOI 10.1126/science.280.5364.737
   Pushechnikov A, 2009, J AM CHEM SOC, V131, P9767, DOI 10.1021/ja9020149
   Savkur RS, 2004, AM J HUM GENET, V74, P1309, DOI 10.1086/421528
   Savkur RS, 2001, NAT GENET, V29, P40, DOI 10.1038/ng704
   Sicot G, 2011, HUM MOL GENET, V20, pR116, DOI 10.1093/hmg/ddr343
   Stein CA, 2010, NUCLEIC ACIDS RES, V38, DOI 10.1093/nar/gkp841
   TANEJA KL, 1995, J CELL BIOL, V128, P995, DOI 10.1083/jcb.128.6.995
   Timchenko NA, 2001, MOL CELL BIOL, V21, P6927, DOI 10.1128/MCB.21.20.6927-6938.2001
   Todd P.K., 2013, DIS MODEL MECH
   Wang GS, 2007, NAT REV GENET, V8, P749, DOI 10.1038/nrg2164
   Wang GS, 2009, J CLIN INVEST, V119, P3797, DOI 10.1172/JCI37976
   Warf MB, 2009, P NATL ACAD SCI USA, V106, P18551, DOI 10.1073/pnas.0903234106
   Wheeler TM, 2009, SCIENCE, V325, P336, DOI 10.1126/science.1173110
   Yu ZM, 2011, PLOS GENET, V7, DOI 10.1371/journal.pgen.1001340
NR 50
TC 59
Z9 65
U1 0
U2 22
PU OXFORD UNIV PRESS
PI OXFORD
PA GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND
SN 0964-6906
EI 1460-2083
J9 HUM MOL GENET
JI Hum. Mol. Genet.
PD MAR 15
PY 2014
VL 23
IS 6
BP 1551
EP 1562
DI 10.1093/hmg/ddt542
PG 12
WC Biochemistry & Molecular Biology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Genetics & Heredity
GA AB8MK
UT WOS:000332044300013
PM 24179176
OA Green Published, Green Submitted
DA 2025-04-10
ER

PT J
AU Kogo, H
   Fujimoto, T
AF Kogo, H
   Fujimoto, T
TI Caveolin-1 isoforms are encoded by distinct mRNAs - Identification of
   mouse caveolin-1 mRNA variants caused by alternative transcription
   initiation and splicing
SO FEBS LETTERS
LA English
DT Article
DE caveolin-1 isoform; mRNA variant; alternative transcription initiation
ID ONCOGENICALLY TRANSFORMED-CELLS; ENDOPLASMIC-RETICULUM;
   FREE-CHOLESTEROL; PLASMA-MEMBRANE; EXPRESSION; TRANSPORT; SEQUENCE;
   PROTEIN; COMPONENT; VESICLES
AB By searching the EST database with the known cDNA sequence encoding alpha-caveolin-1 (full-length: FL), we found a variant having a hitherto unknown sequence in place of the first exon (5'-end variant: 5'V), The expression level of 5'V mRNA was equivalent to that of FL mRNA, The entire sequences of FL and 5'V mRNA were determined by 3'- and 5'-RACE analysis; their sizes were 2484 bp and 2533 bp, respectively, and the sequences were identical except for the region of the first exon, By Northern blotting, FL and 5'V mRNAs showed the same tissue distribution, and were intensely expressed in the lung, heart, and skeletal muscle. Analyzing the protein production from these mRNAs using green fluorescent protein as a tag, we found FL mRNA to produce the alpha-isoform predominantly, but to form little beta-isoform, The production of the beta-isoform from 5'V mRNA was also demonstrated. By sequence analysis of the first intron of the caveolin-1 gene, a TATA box was found at 28 bp upstream of the transcription initiation site for 5'V mRNA. This is the first demonstration of caveolin-1 mRNA variants generated by alternative transcription initiation, and it indicates that the two isoforms of caveolin-1 are produced from two distinct mRNAs. (C) 2000 Federation of European Biochemical Societies.
C1 Nagoya Univ, Sch Med, Dept Anat & Mol Cell Biol, Showa Ku, Nagoya, Aichi 4668550, Japan.
C3 Nagoya University
RP Kogo, H (corresponding author), Nagoya Univ, Sch Med, Dept Anat & Mol Cell Biol, Showa Ku, Nagoya, Aichi 4668550, Japan.
RI Kogo, Hiroshi/AAB-8467-2019; Fujimoto, Toyoshi/ABH-9058-2020
OI Kogo, Hiroshi/0000-0003-0584-7158
CR Anderson RGW, 1998, ANNU REV BIOCHEM, V67, P199, DOI 10.1146/annurev.biochem.67.1.199
   Bist A, 1997, P NATL ACAD SCI USA, V94, P10693, DOI 10.1073/pnas.94.20.10693
   DECKER CJ, 1995, CURR OPIN CELL BIOL, V7, P386, DOI 10.1016/0955-0674(95)80094-8
   Engelman JA, 1999, FEBS LETT, V448, P221, DOI 10.1016/S0014-5793(99)00365-8
   Engelman JA, 1998, FEBS LETT, V429, P330, DOI 10.1016/S0014-5793(98)00619-X
   Engelman JA, 1997, J BIOL CHEM, V272, P16374, DOI 10.1074/jbc.272.26.16374
   Fielding CJ, 1997, P NATL ACAD SCI USA, V94, P3753, DOI 10.1073/pnas.94.8.3753
   Fielding CJ, 1997, J LIPID RES, V38, P1503
   FRA AM, 1995, P NATL ACAD SCI USA, V92, P8655, DOI 10.1073/pnas.92.19.8655
   Fujimoto T, 1998, J ELECTRON MICROSC, V47, P451, DOI 10.1093/oxfordjournals.jmicro.a023616
   GLENNEY JR, 1992, FEBS LETT, V314, P45, DOI 10.1016/0014-5793(92)81458-X
   Hailstones D, 1998, J LIPID RES, V39, P369
   Heinemeyer T, 1998, NUCLEIC ACIDS RES, V26, P362, DOI 10.1093/nar/26.1.362
   KIMURA G, 1975, INT J CANCER, V15, P694, DOI 10.1002/ijc.2910150419
   Kogo H, 1997, ACTA HISTOCHEM CYTOC, V30, P593, DOI 10.1267/ahc.30.593
   KOLESKE AJ, 1995, P NATL ACAD SCI USA, V92, P1381, DOI 10.1073/pnas.92.5.1381
   KOO YB, 1994, ENDOCRINOLOGY, V134, P19, DOI 10.1210/en.134.1.19
   Lee SW, 1998, ONCOGENE, V16, P1391, DOI 10.1038/sj.onc.1201661
   Li SW, 1996, J BIOL CHEM, V271, P3863
   MURATA M, 1995, P NATL ACAD SCI USA, V92, P10339, DOI 10.1073/pnas.92.22.10339
   Nomura R, 1999, MOL BIOL CELL, V10, P975, DOI 10.1091/mbc.10.4.975
   Okamoto T, 1998, J BIOL CHEM, V273, P5419, DOI 10.1074/jbc.273.10.5419
   PALADE GE, 1960, ANAT REC, V136, P254
   REESE MG, 1995, 7 INT GEN SEQ AN C H
   ROTHBERG KG, 1992, CELL, V68, P673, DOI 10.1016/0092-8674(92)90143-Z
   SCHERER PE, 1994, J CELL BIOL, V127, P1233, DOI 10.1083/jcb.127.5.1233
   SCHERER PE, 1995, J BIOL CHEM, V270, P16395, DOI 10.1074/jbc.270.27.16395
   Schlegel A, 1998, CELL SIGNAL, V10, P457, DOI 10.1016/S0898-6568(98)00007-2
   Smart EJ, 1996, J BIOL CHEM, V271, P29427, DOI 10.1074/jbc.271.46.29427
   THOMPSON JD, 1994, NUCLEIC ACIDS RES, V22, P4673, DOI 10.1093/nar/22.22.4673
   Yamamoto M, 1999, LIFE SCI, V64, P1349, DOI 10.1016/S0024-3205(99)00070-3
   YUSPA SH, 1980, CANCER RES, V40, P4694
NR 32
TC 66
Z9 80
U1 0
U2 4
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 0014-5793
J9 FEBS LETT
JI FEBS Lett.
PD JAN 14
PY 2000
VL 465
IS 2-3
BP 119
EP 123
DI 10.1016/S0014-5793(99)01730-5
PG 5
WC Biochemistry & Molecular Biology; Biophysics; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics; Cell Biology
GA 284BG
UT WOS:000085310400007
PM 10631317
OA Bronze
DA 2025-04-10
ER

PT J
AU Fischer, D
   Tucker, RP
   ChiquetEhrismann, R
   Adams, JC
AF Fischer, D
   Tucker, RP
   ChiquetEhrismann, R
   Adams, JC
TI Cell-adhesive responses to tenascin-c splice variants involve formation
   of fascin microspikes
SO MOLECULAR BIOLOGY OF THE CELL
LA English
DT Article
ID ACTIN-BUNDLING PROTEIN; EXTRACELLULAR-MATRIX; MESSENGER-RNA;
   INTERFERENCE-REFLECTION; FOCAL ADHESIONS; AVIAN EMBRYO; ANNEXIN-II;
   THROMBOSPONDIN; ATTACHMENT; RECEPTOR
AB Tenascin-C is an adhesion-modulating matrix glycoprotein that has multiple effects on cell behavior. Tenascin-C transcripts are expressed in motile cells and at sites of tissue modeling during development, and alternative splicing generates variants that encode different numbers of fibronectin type III repeats. We have examined the in vivo expression and cell adhesive properties of two full-length recombinant tenascin-C proteins: TN-190, which contains the eight constant fibronectin type III repeats, and TN-ADC, which contains the additional AD2, AD1, and C repeats. In situ hybridization with probes specific for the AD2, AD1, and C repeats shows that these splice variants are expressed at sites of active tissue modeling and fibronectin expression in the developing avian feather bud and sternum. Transcripts incorporating the AD2, AD1, and C repeats are present in embryonic day 10 wing bud but not in embryonic day 10 lung. By using a panel of nine cell lines in attachment assays, we have found that C2C12, G8, and S27 myoblastic cells undergo concentration-dependent adhesion to both variants, organize actin microspikes that contain the actin-bundling protein fascin, and do not assemble focal contacts. On a molar basis, TN-ADC is more active than TN-190 in promoting cell attachment and irregular cell spreading. The addition of either TN-190 or TN-ADC in solution to C2C12, COS-7, or MG-63 cells adherent on fibronectin decreases cell attachment and results in decreased organization of actin microfilament bundles, with formation of cortical membrane ruffles and retention of residual points of substratum contact that contain filamentous actin and fascin. These data establish a biochemical similarity in the processes of cell adhesion to tenascin-C and thrombospondin-1, also an ''antiadhesive'' matrix component, and also demonstrate that both the adhesive and adhesion-modulating properties of tenascin-C involve similar biochemical events in the cortical cytoskeleton. In addition to these generic properties, TN-ADC is less active in adhesion modulation than TN-190. The coordinated expression of different tenascin-C transcripts during development may, therefore, provide appropriate microenvironments for regulated changes in cell shape, adhesion, and movement.
C1 UCL, MRC 1, MOL CELL BIOL LAB, LONDON WC1E 6BT, ENGLAND.
   UCL, MRC 1, DEPT BIOCHEM & MOL BIOL, LONDON WC1E 6BT, ENGLAND.
   FRIEDRICH MIESCHER INST, CH-4002 BASEL, SWITZERLAND.
   UNIV CALIF DAVIS, SCH MED, DEPT CELL BIOL & HUMAN ANAT, DAVIS, CA 95616 USA.
C3 University of London; University College London; University of London;
   University College London; Friedrich Miescher Institute for Biomedical
   Research; University of California System; University of California
   Davis
RI Adams, Josephine C./B-1121-2009
OI Adams, Josephine C./0000-0002-2225-4947
FU Wellcome Trust Funding Source: Medline
CR Adams J.C., 1995, THROMBOSPONDIN GENE
   ADAMS JC, 1994, MOL BIOL CELL, V5, P423, DOI 10.1091/mbc.5.4.423
   ADAMS JC, 1993, J CELL SCI, V104, P1061
   ADAMS JC, 1995, J CELL SCI, V108, P1977
   ASCH AS, 1991, J BIOL CHEM, V266, P1740
   AUKHIL I, 1993, J BIOL CHEM, V268, P2542
   BARNEA G, 1994, J BIOL CHEM, V269, P14349
   BLAU HM, 1985, SCIENCE, V230, P758, DOI 10.1126/science.2414846
   BORNSTEIN P, 1995, J CELL BIOL, V130, P503, DOI 10.1083/jcb.130.3.503
   BOURDON MA, 1989, J CELL BIOL, V108, P1149, DOI 10.1083/jcb.108.3.1149
   BURRIDGE K, 1988, ANNU REV CELL BIOL, V4, P487, DOI 10.1146/annurev.cellbio.4.1.487
   Burridge K, 1996, ANNU REV CELL DEV BI, V12, P463, DOI 10.1146/annurev.cellbio.12.1.463
   CHIQUET M, 1984, J CELL BIOL, V98, P1926, DOI 10.1083/jcb.98.6.1926
   Chiquet-Ehrismann R, 1991, CURR OPIN CELL BIOL, V3, P800, DOI 10.1016/0955-0674(91)90053-2
   CHIQUETEHRISMANN R, 1991, CELL REGUL, V2, P927, DOI 10.1091/mbc.2.11.927
   CHIQUETEHRISMANN R, 1995, EXPERIENTIA, V51, P853, DOI 10.1007/BF01921736
   CHIQUETEHRISMANN R, 1995, CURR OPIN CELL BIOL, V7, P715, DOI 10.1016/0955-0674(95)80114-6
   CHIQUETEHRISMANN R, 1993, SEMIN CANCER BIOL, V4, P301
   CHIQUETEHRISMANN R, 1986, CELL, V47, P131, DOI 10.1016/0092-8674(86)90374-0
   CHIQUETEHRISMANN R, 1988, CELL, V53, P383, DOI 10.1016/0092-8674(88)90158-4
   CHRISTIAN CN, 1977, SCIENCE, V196, P995, DOI 10.1126/science.193191
   Chung CY, 1996, MOL BIOL CELL, V7, P883, DOI 10.1091/mbc.7.6.883
   CHUNG CY, 1994, J CELL BIOL, V126, P539, DOI 10.1083/jcb.126.2.539
   EDWARDS RA, 1995, CELL MOTIL CYTOSKEL, V32, P1, DOI 10.1002/cm.970320102
   EHRISMANN R, 1981, J BIOL CHEM, V256, P4056
   Erickson HP, 1993, CURR OPIN CELL BIOL, V5, P869, DOI 10.1016/0955-0674(93)90037-Q
   ERICKSON HP, 1987, J CELL BIOL, V105, P1387, DOI 10.1083/jcb.105.3.1387
   ERICKSON HP, 1989, ANNU REV CELL BIOL, V5, P71, DOI 10.1146/annurev.cb.05.110189.000443
   Fell HB, 1939, PHILOS T R SOC B, V229, P407, DOI 10.1098/rstb.1939.0002
   FERNS MJ, 1993, NEURON, V11, P491, DOI 10.1016/0896-6273(93)90153-I
   FISCHER D, 1995, J BIOL CHEM, V270, P3378, DOI 10.1074/jbc.270.7.3378
   Frazier WA, 1991, CURR OPIN CELL BIOL, V3, P792, DOI 10.1016/0955-0674(91)90052-Z
   FRIEDLANDER DR, 1988, J CELL BIOL, V107, P2329, DOI 10.1083/jcb.107.6.2329
   GEIGER B, 1979, CELL, V18, P193, DOI 10.1016/0092-8674(79)90368-4
   GLUZMAN Y, 1981, CELL, V23, P175, DOI 10.1016/0092-8674(81)90282-8
   GORDON H, 1989, DEV BIOL, V135, P1, DOI 10.1016/0012-1606(89)90152-8
   Gotz B, 1996, J CELL BIOL, V132, P681, DOI 10.1083/jcb.132.4.681
   GRUMET M, 1994, J BIOL CHEM, V269, P12142
   HEATH JP, 1978, J CELL SCI, V29, P197
   HORTON RM, 1989, GENE, V77, P61, DOI 10.1016/0378-1119(89)90359-4
   HYNES RO, 1992, CELL, V69, P11, DOI 10.1016/0092-8674(92)90115-S
   IZZARD CS, 1976, J CELL SCI, V21, P129
   JIANG TX, 1992, DEV BIOL, V150, P82, DOI 10.1016/0012-1606(92)90009-6
   JONES FS, 1989, P NATL ACAD SCI USA, V86, P1905, DOI 10.1073/pnas.86.6.1905
   JOSHI P, 1993, J CELL SCI, V106, P389
   KIMES BW, 1976, EXP CELL RES, V98, P349, DOI 10.1016/0014-4827(76)90446-8
   LAEMMLI UK, 1970, NATURE, V227, P680, DOI 10.1038/227680a0
   Lahav J, 1993, THROMBOSPONDIN
   LANE TF, 1994, FASEB J, V8, P163, DOI 10.1096/fasebj.8.2.8119487
   LAWLER J, 1988, J CELL BIOL, V107, P2351, DOI 10.1083/jcb.107.6.2351
   LOTZ MM, 1989, J CELL BIOL, V109, P1795, DOI 10.1083/jcb.109.4.1795
   LUPA MT, 1990, DEV BIOL, V142, P31, DOI 10.1016/0012-1606(90)90148-C
   MACKIE EJ, 1992, J CELL SCI, V103, P765
   MACKIE EJ, 1994, PERSPECT DEV NEUROBI, V2, P125
   MurphyUllrich JE, 1996, J CELL SCI, V109, P2499
   MURPHYULLRICH JE, 1991, J CELL BIOL, V115, P1127, DOI 10.1083/jcb.115.4.1127
   MURPHYULLRICH JE, 1992, J CELL BIOL, V116, P833
   ORLANDO RA, 1991, J BIOL CHEM, V266, P19543
   PRIETO AL, 1992, J CELL BIOL, V119, P663, DOI 10.1083/jcb.119.3.663
   PRIETO AL, 1993, P NATL ACAD SCI USA, V90, P10154, DOI 10.1073/pnas.90.21.10154
   RASHEED S, 1974, CANCER, V33, P1027, DOI 10.1002/1097-0142(197404)33:4<1027::AID-CNCR2820330419>3.0.CO;2-Z
   SAGE EH, 1991, J BIOL CHEM, V266, P14831
   SALMIVIRTA M, 1991, J BIOL CHEM, V266, P7733
   Sambrook J, 1989, MOL CLONING LAB MANU
   SCHNAPP LM, 1995, J BIOL CHEM, V270, P23196, DOI 10.1074/jbc.270.39.23196
   Schwartz MA, 1995, ANNU REV CELL DEV BI, V11, P549, DOI 10.1146/annurev.cellbio.11.1.549
   SIRI A, 1991, NUCLEIC ACIDS RES, V19, P525, DOI 10.1093/nar/19.3.525
   SPRING J, 1989, CELL, V59, P325, DOI 10.1016/0092-8674(89)90294-8
   SRIRAMARAO P, 1993, NUCLEIC ACIDS RES, V21, P163, DOI 10.1093/nar/21.1.163
   SRIRAMARAO P, 1993, J CELL SCI, V105, P1001
   STOMSKI FC, 1992, EXP CELL RES, V198, P85, DOI 10.1016/0014-4827(92)90152-X
   TUCKER RP, 1991, ROUX ARCH DEV BIOL, V200, P108, DOI 10.1007/BF00637191
   TUCKER RP, 1993, DEVELOPMENT, V117, P347
   TUCKER RP, 1995, DEV DYNAM, V203, P477, DOI 10.1002/aja.1002030410
   TUCKER RP, 1994, DEVELOPMENT, V120, P637
   Turner CE, 1991, CURR OPIN CELL BIOL, V3, P849, DOI 10.1016/0955-0674(91)90059-8
   TUSZYNSKI GP, 1987, SCIENCE, V236, P1570, DOI 10.1126/science.2438772
   VARANI J, 1988, J CLIN INVEST, V81, P1537, DOI 10.1172/JCI113486
   VARNUMFINNEY B, 1995, NEURON, V14, P1213, DOI 10.1016/0896-6273(95)90268-6
   WESSELLS NK, 1965, DEV BIOL, V12, P131, DOI 10.1016/0012-1606(65)90025-4
   YAMADA KM, 1995, CURR OPIN CELL BIOL, V7, P681, DOI 10.1016/0955-0674(95)80110-3
   YAMASHIROMATSUMURA S, 1986, J CELL BIOL, V103, P631, DOI 10.1083/jcb.103.2.631
   YOKOSAKI Y, 1994, J BIOL CHEM, V269, P26691
   Yokosaki Y, 1996, J BIOL CHEM, V271, P24144, DOI 10.1074/jbc.271.39.24144
   ZISCH AH, 1992, J CELL BIOL, V119, P203, DOI 10.1083/jcb.119.1.203
NR 85
TC 61
Z9 64
U1 0
U2 3
PU AMER SOC CELL BIOLOGY
PI BETHESDA
PA 8120 WOODMONT AVE, STE 750, BETHESDA, MD 20814-2755 USA
SN 1059-1524
J9 MOL BIOL CELL
JI Mol. Biol. Cell
PD OCT
PY 1997
VL 8
IS 10
BP 2055
EP 2075
DI 10.1091/mbc.8.10.2055
PG 21
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA YB663
UT WOS:A1997YB66300016
PM 9348542
OA Green Published
DA 2025-04-10
ER

PT J
AU Labeit, S
   Lahmers, S
   Burkart, C
   Fong, C
   McNabb, M
   Witt, S
   Witt, C
   Labeit, D
   Granzier, H
AF Labeit, Siegfried
   Lahmers, Sunshine
   Burkart, Christoph
   Fong, Chi
   McNabb, Mark
   Witt, Stephanie
   Witt, Christian
   Labeit, Dietmar
   Granzier, Henk
TI Expression of distinct classes of titin isoforms in striated and smooth
   muscles by alternative splicing, and their conserved interaction with
   filamins
SO JOURNAL OF MOLECULAR BIOLOGY
LA English
DT Article
DE smooth and striated muscle; titin; filamins; Z-disks and dense bodies;
   differential splicing
ID TISSUE-SPECIFIC EXPRESSION; C-TERMINAL REGION; ALPHA-ACTININ; IN-VITRO;
   LINKING SYSTEM; CARDIAC-MUSCLE; GIANT PROTEIN; Z-DISK; OBSCURIN; BINDING
AB While the role of titin as a sarcomeric protein is well established, its potential functional role(s) in smooth muscles and non-muscle tissues are controversial. We used a titin exon array to search for which part(s) of the human titin transcriptional unit encompassing 363 exons is(are) expressed in non-striated muscle tissues. Expression profiling of adult smooth muscle tissues (aorta, bladder, carotid, stomach) identified alternatively spliced titin isoforms, encompassing 80 to about 100 exons. These exons code for parts of the titin Z-disk, I-band and A-band regions, allowing the truncated smooth muscle titin isoform to link Z-disks/dense bodies together with thick filaments. Consistent with the array data, Western blot studies detected the expression of similar to 1 MDa smooth muscle titin in adult smooth muscles, reacting with selected Z-disc, I-band, and A-band titin antibodies. immunofluorescence with these antibodies located smooth muscle titin in the cytoplasm of cultured human aortic smooth muscle cells and in the tunica media of intact adult bovine aorta. Real time PCR studies suggested that smooth muscle titins are expressed from a promoter located 35 kb or more upstream of the transcription initiation site used for striated muscle titin, driving expression of a bi-cistronic mRNA, coding 5 ' for the anonymous gene FL39502, followed 3 ' by titin, respectively. Our work showed that smooth muscle and striated muscle titins share in their conserved amino-terminal regions binding sites for at-actinin and filamins: Yeast two-hybrid screens using Z2-Zis1 titin baits identified prey clones coding for alpha-actinin-1 and filamin-A from smooth muscle, and alpha-actinin-2/3, filamin-C, and nebulin from skeletal muscle cDNA libraries, respectively. This suggests that the titin Z2-Zis1 domain can link filamins and alpha-actinin together in the periphery of the Z-line/dense bodies in a fashion that is conserved in smooth and striated muscles. (c) 2006 Elsevier Ltd. All rights reserved.
C1 Univ Hosp Mannheim, Inst Anaesthesiol & Intens Care, Mannheim, Germany.
   Washington State Univ, Dept Vet & Comparat Anat & Pharmacol, Pullman, WA 99164 USA.
C3 Ruprecht Karls University Heidelberg; Washington State University
RP Labeit, S (corresponding author), Univ Hosp Mannheim, Inst Anaesthesiol & Intens Care, Mannheim, Germany.
EM labeit@embl.de
FU NHLBI NIH HHS [HL61487/HL62881] Funding Source: Medline
CR Ayoob JC, 2000, CELL MOTIL CYTOSKEL, V45, P67, DOI 10.1002/(SICI)1097-0169(200001)45:1<67::AID-CM7>3.0.CO;2-T
   Bagnato P, 2003, J CELL BIOL, V160, P245, DOI 10.1083/jcb.200208109
   Bang ML, 2001, CIRC RES, V89, P1065, DOI 10.1161/hh2301.100981
   Bodine SC, 2001, SCIENCE, V294, P1704, DOI 10.1126/science.1065874
   Borisov AB, 2004, J HISTOCHEM CYTOCHEM, V52, P1117, DOI 10.1369/jhc.3A6183.2004
   Centner T, 2001, J MOL BIOL, V306, P717, DOI 10.1006/jmbi.2001.4448
   Centner T, 2000, ADV EXP MED BIOL, V481, P35
   Chi RJ, 2005, INT J BIOCHEM CELL B, V37, P1470, DOI 10.1016/j.biocel.2005.02.014
   Chiang W, 2000, DEV DYNAM, V217, P99, DOI 10.1002/(SICI)1097-0177(200001)217:1<99::AID-DVDY9>3.0.CO;2-5
   Chiang W, 2000, J MUSCLE RES CELL M, V21, P321, DOI 10.1023/A:1005650706464
   Clark KA, 2002, ANNU REV CELL DEV BI, V18, P637, DOI 10.1146/annurev.cellbio.18.012502.105840
   EILERTSEN KJ, 1992, J CELL BIOL, V119, P549, DOI 10.1083/jcb.119.3.549
   EILERTSEN KJ, 1994, J CELL BIOL, V126, P1201, DOI 10.1083/jcb.126.5.1201
   Furukawa T, 2001, J MOL BIOL, V313, P775, DOI 10.1006/jmbi.2001.5053
   GAUTEL M, 1993, EMBO J, V12, P3827, DOI 10.1002/j.1460-2075.1993.tb06061.x
   Gautel M, 1996, J CELL SCI, V109, P2747
   Gontier Y, 2005, J CELL SCI, V118, P3739, DOI 10.1242/jcs.02484
   GRANZIER HL, 1995, BIOPHYS J, V68, P1027, DOI 10.1016/S0006-3495(95)80278-X
   Granzier HL, 2004, CIRC RES, V94, P284, DOI 10.1161/01.RES.0000117769.88862.F8
   Greaser ML, 2000, ADV EXP MED BIOL, V481, P53
   HASHIMOTO K, 1984, TOHOKU J EXP MED, V143, P59, DOI 10.1620/tjem.143.59
   Keller TCS, 2000, ADV EXP MED BIOL, V481, P265
   Kim K, 2002, J CELL BIOL, V156, P101, DOI 10.1083/jcb.200107037
   Knöll R, 2002, CELL, V111, P943, DOI 10.1016/s0092-8674(02)01226-6
   Kolmerer B, 1996, J MOL BIOL, V256, P556, DOI 10.1006/jmbi.1996.0108
   Kontrogianni-Konstantopoulos A, 2003, J BIOL CHEM, V278, P3985, DOI 10.1074/jbc.M209012200
   LABEIT S, 1992, EMBO J, V11, P1711, DOI 10.1002/j.1460-2075.1992.tb05222.x
   Lahmers S, 2004, CIRC RES, V94, P505, DOI 10.1161/01.RES.0000115522.52554.86
   Machado C, 2000, J CELL BIOL, V151, P639, DOI 10.1083/jcb.151.3.639
   Machado C, 1998, J CELL BIOL, V141, P321, DOI 10.1083/jcb.141.2.321
   MAHER PA, 1985, J CELL BIOL, V101, P1871, DOI 10.1083/jcb.101.5.1871
   NAVE R, 1989, J CELL BIOL, V109, P2177, DOI 10.1083/jcb.109.5.2177
   Obermann WMJ, 1996, J CELL BIOL, V134, P1441, DOI 10.1083/jcb.134.6.1441
   Ohtsuka H, 1997, BIOCHEM BIOPH RES CO, V235, P1, DOI 10.1006/bbrc.1997.6534
   Sorimachi H, 1997, J MOL BIOL, V270, P688, DOI 10.1006/jmbi.1997.1145
   Tskhovrebova L, 2003, NAT REV MOL CELL BIO, V4, P679, DOI 10.1038/nrm1198
   Turnacioglu KK, 1997, CELL STRUCT FUNCT, V22, P73, DOI 10.1247/csf.22.73
   van der Flier A, 2002, J CELL BIOL, V156, P361, DOI 10.1083/jcb.200103037
   Warren CM, 2003, ELECTROPHORESIS, V24, P1695, DOI 10.1002/elps.200305392
   Wernyj RP, 2001, CELL MOTIL CYTOSKEL, V50, P101, DOI 10.1002/cm.1044
   WITT CC, 2006, IN PRESS EMBO J
   Witt SH, 2005, J MOL BIOL, V350, P713, DOI 10.1016/j.jmb.2005.05.021
   Wu YM, 2002, CIRCULATION, V106, P1384, DOI 10.1161/01.CIR.0000029804.61510.02
   Young P, 1998, EMBO J, V17, P1614, DOI 10.1093/emboj/17.6.1614
   Young P, 2001, J CELL BIOL, V154, P123, DOI 10.1083/jcb.200102110
   Zastrow MS, 2006, J CELL SCI, V119, P239, DOI 10.1242/jcs.02728
NR 46
TC 73
Z9 87
U1 1
U2 12
PU ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
PI LONDON
PA 24-28 OVAL RD, LONDON NW1 7DX, ENGLAND
SN 0022-2836
EI 1089-8638
J9 J MOL BIOL
JI J. Mol. Biol.
PD SEP 29
PY 2006
VL 362
IS 4
BP 664
EP 681
DI 10.1016/j.jmb.2006.07.077
PG 18
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 095RE
UT WOS:000241324700004
PM 16949617
DA 2025-04-10
ER

PT J
AU Zhang, H
   Brown, RD
   Stenmark, KR
   Hu, CJ
AF Zhang, Hui
   Brown, R. Dale
   Stenmark, Kurt R.
   Hu, Cheng-Jun
TI RNA-Binding Proteins in Pulmonary Hypertension
SO INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
LA English
DT Review
DE pulmonary hypertension; RNA-binding proteins; alternative splicing; RNA
   metabolism; RNA therapeutics
ID GUANYLYL CYCLASE EXPRESSION; TOLL-LIKE RECEPTOR-3; MESSENGER-RNA;
   PYRUVATE-KINASE; INFLAMMATORY PHENOTYPE; ARTERIAL-HYPERTENSION;
   DOWN-REGULATION; CIRCULAR RNA; GENE; BIOGENESIS
AB Pulmonary hypertension (PH) is a life-threatening disease characterized by significant vascular remodeling and aberrant expression of genes involved in inflammation, apoptosis resistance, proliferation, and metabolism. Effective therapeutic strategies are limited, as mechanisms underlying PH pathophysiology, especially abnormal expression of genes, remain unclear. Most PH studies on gene expression have focused on gene transcription. However, post-transcriptional alterations have been shown to play a critical role in inflammation and metabolic changes in diseases such as cancer and systemic cardiovascular diseases. In these diseases, RNA-binding proteins (RBPs) have been recognized as important regulators of aberrant gene expression via post-transcriptional regulation; however, their role in PH is less clear. Identifying RBPs in PH is of great importance to better understand PH pathophysiology and to identify new targets for PH treatment. In this manuscript, we review the current knowledge on the role of dysregulated RBPs in abnormal mRNA gene expression as well as aberrant non-coding RNA processing and expression (e.g., miRNAs) in PH.
C1 [Zhang, Hui; Brown, R. Dale; Stenmark, Kurt R.; Hu, Cheng-Jun] Univ Colorado, Dept Pediat & Med, Sch Med, Cardiovasc Pulm Res Labs, Anschutz Med Campus, Aurora, CO 80045 USA.
   [Hu, Cheng-Jun] Univ Colorado, Dept Craniofacial Biol, Sch Dent Med, Anschutz Med Campus, Aurora, CO 80045 USA.
C3 University of Colorado System; University of Colorado Anschutz Medical
   Campus; University of Colorado System; University of Colorado Anschutz
   Medical Campus
RP Hu, CJ (corresponding author), Univ Colorado, Dept Pediat & Med, Sch Med, Cardiovasc Pulm Res Labs, Anschutz Med Campus, Aurora, CO 80045 USA.; Hu, CJ (corresponding author), Univ Colorado, Dept Craniofacial Biol, Sch Dent Med, Anschutz Med Campus, Aurora, CO 80045 USA.
EM Hui.Zhang@cuanschutz.edu; dale.brown@cuanschutz.edu;
   kurt.stenmark@cuanschutz.edu; Cheng-jun.Hu@cuanschutz.edu
RI stenmark, kurt/AFI-6776-2022
OI Hu, Cheng-Jun/0000-0003-0985-1285
FU National Institutes of Health (PPG) [HL014985]; U.S. Department of
   Defense [W81XWH1910259]; U.S. Department of Defense (DOD)
   [W81XWH1910259] Funding Source: U.S. Department of Defense (DOD)
FX National Institutes of Health (PPG): HL014985; U.S. Department of
   Defense: W81XWH1910259.
CR Aartsma-Rus A, 2016, MOL THER, V24, P193, DOI 10.1038/mt.2016.14
   Abdelmohsen K, 2008, P NATL ACAD SCI USA, V105, P20297, DOI 10.1073/pnas.0809376106
   Alaqeel AM, 2015, BALK J MED GENET, V18, P5, DOI 10.1515/bjmg-2015-0080
   Ames EG, 2013, J MOL CELL CARDIOL, V62, P99, DOI 10.1016/j.yjmcc.2013.05.004
   Banerjee D, 2020, CHEST, V158, P735, DOI 10.1016/j.chest.2019.12.052
   Bartel DP, 2004, CELL, V116, P281, DOI 10.1016/S0092-8674(04)00045-5
   Blech-Hermoni Y, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0149061
   Bouallegue A, 2007, AM J PHYSIOL-HEART C, V293, pH2072, DOI 10.1152/ajpheart.01097.2006
   Brennan CM, 2001, CELL MOL LIFE SCI, V58, P266, DOI 10.1007/PL00000854
   Busch A, 2012, WIRES RNA, V3, P1, DOI 10.1002/wrna.100
   Caruso P, 2017, CIRCULATION, V136, P2451, DOI 10.1161/CIRCULATIONAHA.117.028034
   Cavassani KA, 2008, J EXP MED, V205, P2609, DOI 10.1084/jem.20081370
   Chan SY, 2017, EUR RESPIR REV, V26, DOI 10.1183/16000617.0094-2017
   Chang KT, 2017, CIRC RES, V121, P1140, DOI 10.1161/CIRCRESAHA.117.311281
   Chen M, 2012, NAT STRUCT MOL BIOL, V19, P346, DOI 10.1038/nsmb.2219
   Chen M, 2010, CANCER RES, V70, P8977, DOI 10.1158/0008-5472.CAN-10-2513
   Chester Adrian H, 2017, Glob Cardiol Sci Pract, V2017, P14, DOI 10.21542/gcsp.2017.14
   Chlebowski A, 2013, BBA-GENE REGUL MECH, V1829, P552, DOI 10.1016/j.bbagrm.2013.01.006
   Christofk HR, 2008, NATURE, V452, P230, DOI 10.1038/nature06734
   Ciafrè SA, 2013, RNA BIOL, V10, P935, DOI 10.4161/rna.24641
   Clower CV, 2010, P NATL ACAD SCI USA, V107, P1894, DOI 10.1073/pnas.0914845107
   Cogan J, 2012, CIRCULATION, V126, P1907, DOI 10.1161/CIRCULATIONAHA.112.106245
   Cole JE, 2011, P NATL ACAD SCI USA, V108, P2372, DOI 10.1073/pnas.1018515108
   Conlon EG, 2017, GENE DEV, V31, P1509, DOI 10.1101/gad.304055.117
   Conn SJ, 2015, CELL, V160, P1125, DOI 10.1016/j.cell.2015.02.014
   Connerty P, 2016, BBA-GENE REGUL MECH, V1859, P1299, DOI 10.1016/j.bbagrm.2016.07.013
   D'Alessandro A, 2018, ANTIOXID REDOX SIGN, V28, P230, DOI 10.1089/ars.2017.7217
   Dahariya S, 2019, MOL IMMUNOL, V112, P82, DOI 10.1016/j.molimm.2019.04.011
   Darnell JE, 2013, RNA, V19, P443, DOI 10.1261/rna.038596.113
   Datta S, 2008, J IMMUNOL, V180, P2545, DOI 10.4049/jimmunol.180.4.2545
   David CJ, 2010, NATURE, V463, P364, DOI 10.1038/nature08697
   de Bruin RG, 2017, EUR HEART J, V38, P1380, DOI 10.1093/eurheartj/ehw567
   de Frutos S, 2009, AM J PHYSIOL-LUNG C, V297, pL475, DOI 10.1152/ajplung.00060.2009
   Dhanoa JK, 2018, J ANIM SCI TECHNOL, V60, DOI 10.1186/s40781-018-0183-7
   Díaz-Muñoz MD, 2018, FRONT IMMUNOL, V9, DOI 10.3389/fimmu.2018.01094
   Evans JDW, 2016, LANCET RESP MED, V4, P129, DOI 10.1016/S2213-2600(15)00544-5
   Farkas D, 2019, AM J RESP CRIT CARE, V199, P199, DOI 10.1164/rccm.201707-1370OC
   Friedman RC, 2009, GENOME RES, V19, P92, DOI 10.1101/gr.082701.108
   Galgano A, 2008, PLOS ONE, V3, DOI 10.1371/journal.pone.0003164
   Gao C, 2020, PHYSIOL REV, V100, P673, DOI 10.1152/physrev.00007.2019
   Gao G, 2013, CIRC-ARRHYTHMIA ELEC, V6, P1018, DOI 10.1161/CIRCEP.113.000274
   Gao G, 2011, CIRCULATION, V124, P1124, DOI 10.1161/CIRCULATIONAHA.111.044495
   GARG UC, 1989, J CLIN INVEST, V83, P1774, DOI 10.1172/JCI114081
   Geuens T, 2016, HUM GENET, V135, P851, DOI 10.1007/s00439-016-1683-5
   Giudice J, 2016, SCI REP-UK, V6, DOI 10.1038/srep35550
   Gonzalez I, 2015, NAT STRUCT MOL BIOL, V22, P370, DOI 10.1038/nsmb.3005
   Gosu V, 2019, SCI REP-UK, V9, DOI 10.1038/s41598-019-39984-8
   Grunig G, 2019, AM J RESP CRIT CARE, V199, P138, DOI 10.1164/rccm.201807-1363ED
   Hamilton T, 2010, CYTOKINE, V52, P116, DOI 10.1016/j.cyto.2010.04.003
   Han B, 2018, PHARMACOL THERAPEUT, V187, P31, DOI 10.1016/j.pharmthera.2018.01.010
   Hansen TB, 2013, NATURE, V495, P384, DOI 10.1038/nature11993
   Hasan A, 2014, PLOS GENET, V10, DOI 10.1371/journal.pgen.1004684
   Ho JJD, 2012, J BIOL CHEM, V287, P29003, DOI 10.1074/jbc.M112.373365
   Hocine S, 2010, CSH PERSPECT BIOL, V2, DOI 10.1101/cshperspect.a000752
   Hon CC, 2017, NATURE, V543, P199, DOI 10.1038/nature21374
   Hong S, 2017, J CANCER PREV, V22, P203, DOI 10.15430/JCP.2017.22.4.203
   Hu CJ, 2019, J PHYSIOL-LONDON, V597, P1103, DOI 10.1113/JP275857
   Humbert M, 2019, EUR RESPIR J, V53, DOI 10.1183/13993003.01887-2018
   Ivanov A, 2015, CELL REP, V10, P170, DOI 10.1016/j.celrep.2014.12.019
   Ivy D, 2016, CARDIOL CLIN, V34, P451, DOI 10.1016/j.ccl.2016.04.005
   Kafasla P, 2014, NAT IMMUNOL, V15, P492, DOI 10.1038/ni.2884
   Kanasty R, 2013, NAT MATER, V12, P967, DOI [10.1038/nmat3765, 10.1038/NMAT3765]
   Karikó K, 2004, J BIOL CHEM, V279, P12542, DOI 10.1074/jbc.M310175200
   Kedde M, 2007, CELL, V131, P1273, DOI 10.1016/j.cell.2007.11.034
   Kedde M, 2010, NAT CELL BIOL, V12, P1014, DOI 10.1038/ncb2105
   Keren H, 2010, NAT REV GENET, V11, P345, DOI 10.1038/nrg2776
   Kim Sunshin, 2012, Immune Netw, V12, P113, DOI 10.4110/in.2012.12.3.113
   Klöss S, 2004, MOL PHARMACOL, V65, P1440, DOI 10.1124/mol.65.6.1440
   Klöss S, 2003, J BIOL CHEM, V278, P2377, DOI 10.1074/jbc.M206453200
   Könner AC, 2011, TRENDS ENDOCRIN MET, V22, P16, DOI 10.1016/j.tem.2010.08.007
   Kong J, 2012, NAT REV GENET, V13, P383, DOI 10.1038/nrg3184
   Kurosawa R, 2019, CIRC RES, V125, P309, DOI 10.1161/CIRCRESAHA.119.315229
   Lane KB, 2000, NAT GENET, V26, P81, DOI 10.1038/79226
   Legnini I, 2017, MOL CELL, V66, P22, DOI 10.1016/j.molcel.2017.02.017
   Léveillé N, 2011, NAT COMMUN, V2, DOI 10.1038/ncomms1519
   Li HR, 2019, LIPIDS HEALTH DIS, V18, DOI 10.1186/s12944-019-1006-7
   Li M, 2016, CIRCULATION, V134, P1105, DOI 10.1161/CIRCULATIONAHA.116.023171
   Li M, 2011, J IMMUNOL, V187, P2711, DOI 10.4049/jimmunol.1100479
   Liu L, 2008, SCIENCE, V320, P379, DOI 10.1126/science.1155406
   Liu LM, 2017, RNA BIOL, V14, P1715, DOI 10.1080/15476286.2017.1367886
   Losko Magdalena, 2016, Mediators Inflamm, V2016, P5365209
   Lukong KE, 2008, TRENDS GENET, V24, P416, DOI 10.1016/j.tig.2008.05.004
   Martinez-Contreras R, 2007, ADV EXP MED BIOL, V623, P123, DOI 10.1007/978-0-387-77374-2_8
   Maxwell BG, 2015, PEDIATRICS, V136, P241, DOI 10.1542/peds.2014-3834
   Mendell JT, 2012, CELL, V148, P1172, DOI 10.1016/j.cell.2012.02.005
   Meola N, 2016, MOL CELL, V64, P520, DOI 10.1016/j.molcel.2016.09.025
   Michlewski G, 2019, RNA, V25, P1, DOI 10.1261/rna.068692.118
   Moore KS, 2018, FRONT PHYSIOL, V9, DOI 10.3389/fphys.2018.00910
   Morrell Nicholas W, 2006, Proc Am Thorac Soc, V3, P680, DOI 10.1513/pats.200605-118SF
   Müller-McNicoll M, 2013, NAT REV GENET, V14, P275, DOI 10.1038/nrg3434
   Neelamraju Y, 2015, J PROTEOMICS, V127, P61, DOI 10.1016/j.jprot.2015.04.031
   Negi V, 2017, JCI INSIGHT, V2, DOI 10.1172/jci.insight.91327
   Neumann P, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-017-02431-1
   Newman JH, 2001, NEW ENGL J MED, V345, P319, DOI 10.1056/NEJM200108023450502
   O'Brien J, 2018, FRONT ENDOCRINOL, V9, DOI 10.3389/fendo.2018.00402
   Olson KA, 2016, TRENDS BIOCHEM SCI, V41, P219, DOI 10.1016/j.tibs.2016.01.002
   Orengo JP, 2007, ADV EXP MED BIOL, V623, P212, DOI 10.1007/978-0-387-77374-2_13
   Pamudurti NR, 2017, MOL CELL, V66, P9, DOI 10.1016/j.molcel.2017.02.021
   Pan YY, 2020, CELL BIOL INT, V44, P166, DOI 10.1002/cbin.11216
   Peng R, 2002, RNA, V8, P1334, DOI 10.1017/S1355838202022070
   Plecitá-Hlavatá L, 2016, AM J RESP CELL MOL, V55, P47, DOI 10.1165/rcmb.2015-0142OC
   Reece J.B., 2011, CAMPBELL BIOL, P342
   Rosonina E, 2005, MOL CELL BIOL, V25, P6734, DOI 10.1128/MCB.25.15.6734-6746.2005
   Salem ESB, 2019, FRONT CARDIOVASC MED, V6, DOI 10.3389/fcvm.2019.00106
   Shang LJL, 2007, CIRC RES, V101, P1146, DOI 10.1161/CIRCRESAHA.107.152918
   Shav-Tal Y, 2002, FEBS LETT, V531, P109, DOI 10.1016/S0014-5793(02)03447-6
   Shen HH, 2004, MOL CELL, V13, P367, DOI 10.1016/S1097-2765(04)00025-5
   Shen HH, 2004, MOL CELL, V16, P363, DOI 10.1016/j.molcel.2004.10.021
   Sheng JJ, 2014, FRONT PHYSIOL, V5, DOI 10.3389/fphys.2014.00165
   Silla T, 2018, CELL REP, V23, P2199, DOI 10.1016/j.celrep.2018.04.061
   Simonneau G, 2019, EUR RESPIR J, V53, DOI 10.1183/13993003.01913-2018
   St Laurent G, 2015, TRENDS GENET, V31, P239, DOI 10.1016/j.tig.2015.03.007
   Stenmark Kurt R, 2012, Pulm Circ, V2, P3, DOI 10.4103/2045-8932.94817
   Su H, 2018, RESP RES, V19, DOI 10.1186/s12931-018-0956-z
   SZABO A, 1991, CELL, V67, P325, DOI 10.1016/0092-8674(91)90184-Z
   Tazi J, 2009, BBA-MOL BASIS DIS, V1792, P14, DOI 10.1016/j.bbadis.2008.09.017
   Tokumaru S, 2008, CARCINOGENESIS, V29, P2073, DOI 10.1093/carcin/bgn187
   Tsai Halley, 2016, F1000Res, V5, P2755, DOI 10.12688/f1000research.9739.1
   Tuder RM, 2017, CELL TISSUE RES, V367, P643, DOI 10.1007/s00441-016-2539-y
   Turner M, 2018, NAT IMMUNOL, V19, P120, DOI 10.1038/s41590-017-0028-4
   van Kouwenhove M, 2011, NAT REV CANCER, V11, P644, DOI 10.1038/nrc3107
   Wang DR, 2014, CIRC RES, V114, P67, DOI 10.1161/CIRCRESAHA.114.301633
   Wang J, 2018, INT J MOL MED, V42, P1353, DOI 10.3892/ijmm.2018.3740
   White RJ, 2012, CIRCULATION, V126, P1818, DOI 10.1161/CIRCULATIONAHA.112.135004
   Wijeratne DT, 2018, CIRC-CARDIOVASC QUAL, V11, DOI 10.1161/CIRCOUTCOMES.117.003973
   Will CL, 2011, CSH PERSPECT BIOL, V3, DOI 10.1101/cshperspect.a003707
   Xiang Y, 2017, CELL PHYSIOL BIOCHEM, V42, P357, DOI 10.1159/000477479
   Xiao R, 2019, CELL, V178, P107, DOI 10.1016/j.cell.2019.06.001
   Xing Y, 2019, MOL THER, V27, P2166, DOI 10.1016/j.ymthe.2019.07.022
   Yan KS, 2003, NATURE, V426, P469, DOI 10.1038/nature02129
   Yin H, 2014, NAT REV GENET, V15, P541, DOI 10.1038/nrg3763
   Zahid KR, 2020, CARDIOVASC RES, V116, P1937, DOI 10.1093/cvr/cvaa050
   Zhang H, 2017, CIRCULATION, V136, P2468, DOI 10.1161/CIRCULATIONAHA.117.028069
   Zhao BXS, 2017, NAT REV MOL CELL BIO, V18, P31, DOI 10.1038/nrm.2016.132
   Zhou GF, 2015, AM J RESP CELL MOL, V52, P139, DOI 10.1165/rcmb.2014-0166TR
   Zhou HL, 2014, SCI CHINA LIFE SCI, V57, P432, DOI 10.1007/s11427-014-4647-9
   Zhu TT, 2019, PFLUG ARCH EUR J PHY, V471, P347, DOI 10.1007/s00424-018-2219-8
NR 137
TC 7
Z9 7
U1 0
U2 8
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
EI 1422-0067
J9 INT J MOL SCI
JI Int. J. Mol. Sci.
PD JUN
PY 2020
VL 21
IS 11
AR 3757
DI 10.3390/ijms21113757
PG 17
WC Biochemistry & Molecular Biology; Chemistry, Multidisciplinary
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Chemistry
GA MC6ND
UT WOS:000543400300019
PM 32466553
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Paisdzior, S
   Knierim, E
   Kleinau, G
   Biebermann, H
   Krude, H
   Straussberg, R
   Schuelke, M
AF Paisdzior, Sarah
   Knierim, Ellen
   Kleinau, Gunnar
   Biebermann, Heike
   Krude, Heiko
   Straussberg, Rachel
   Schuelke, Markus
TI A New Mechanism in THRA Resistance: The First Disease-Associated Variant
   Leading to an Increased Inhibitory Function of THRA2
SO INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
LA English
DT Article
DE thyroid hormone receptor alpha; resistance to thyroid hormones;
   gain-of-function; gain-of-antagonistic function
ID THYROID-HORMONE-RECEPTOR; CLINICAL PHENOTYPE; BINDING DOMAIN;
   DNA-BINDING; ALPHA; MUTATION; IDENTIFICATION; GENETICS; GENOMICS;
   PROTEIN
AB The nuclear thyroid hormone receptors (THRs) are key mediators of thyroid hormone function on the cellular level via modulation of gene expression. Two different genes encode THRs (THRA and THRB), and are pleiotropically involved in development, metabolism, and growth. The THRA1 and THRA2 isoforms, which result from alternative splicing of THRA, differ in their C-terminal ligand-binding domain (LBD). Most published disease-associated THRA variants are located in the LBD of THRA1 and impede triiodothyronine (T3) binding. This keeps the nuclear receptor in an inactive state and inhibits target gene expression. Here, we investigated a new dominant THRA variant (chr17:g.38,241,010A > G, GRCh37.13 | c.518A > G, NM_199334 | p.(E173G), NP_955366), which is located between the DNA- and ligand-binding domains and affects both splicing isoforms. Patients presented partially with hypothyroid (intellectual disability, motor developmental delay, brain atrophy, and constipation) and partially with hyperthyroid symptoms (tachycardia and behavioral abnormalities) to varying degrees. Functional characterization of THRA1p.(E173G) by reporter gene assays revealed increased transcriptional activity in contrast to THRA1(WT), unexpectedly revealing the first gain-of-function mutation found in THRA1. The THRA2 isoform does not bind T3 and antagonizes THRA1 action. Introduction of p.(E173G) into THRA2 increased its inhibitory effect on THRA1, which helps to explain the hypothyroid symptoms seen in our patients. We used protein structure models to investigate possible underlying pathomechanisms of this variant with a gain-of-antagonistic function and suggest that the p.(E173G) variant may have an influence on the dimerization domain of the nuclear receptor.
C1 [Paisdzior, Sarah; Biebermann, Heike; Krude, Heiko] Charite Univ Med Berlin, Inst Expt Pediat Endocrinol, D-13353 Berlin, Germany.
   [Paisdzior, Sarah; Knierim, Ellen; Biebermann, Heike; Krude, Heiko; Schuelke, Markus] Free Univ Berlin, D-13353 Berlin, Germany.
   [Paisdzior, Sarah; Knierim, Ellen; Biebermann, Heike; Krude, Heiko; Schuelke, Markus] Humboldt Univ, D-13353 Berlin, Germany.
   [Knierim, Ellen; Schuelke, Markus] NeuroCure Cluster Excellence, D-10117 Berlin, Germany.
   [Knierim, Ellen; Schuelke, Markus] Charite Univ Med Berlin, D-10117 Berlin, Germany.
   [Knierim, Ellen; Schuelke, Markus] Free Univ Berlin, D-10117 Berlin, Germany.
   [Knierim, Ellen; Schuelke, Markus] Humboldt Univ, D-10117 Berlin, Germany.
   [Knierim, Ellen; Schuelke, Markus] Charite Univ Med Berlin, Dept Neuropediat, D-13353 Berlin, Germany.
   [Kleinau, Gunnar] Inst Med Phys & Biophys, Grp Prot Xray Crystallog & Signal Transduct, D-10117 Berlin, Germany.
   [Straussberg, Rachel] Schneider Childrens Med Ctr, Petah Tiqwa, Israel.
   [Straussberg, Rachel] Tel Aviv Univ, Sackler Sch Med, Dept Child Neurol, Neurogenet Serv, IL-69978 Ramat Aviv, Israel.
C3 Berlin Institute of Health; Free University of Berlin; Humboldt
   University of Berlin; Charite Universitatsmedizin Berlin; Free
   University of Berlin; Humboldt University of Berlin; Berlin Institute of
   Health; Free University of Berlin; Humboldt University of Berlin;
   Charite Universitatsmedizin Berlin; Free University of Berlin; Humboldt
   University of Berlin; Berlin Institute of Health; Free University of
   Berlin; Humboldt University of Berlin; Charite Universitatsmedizin
   Berlin; Tel Aviv University; Sackler Faculty of Medicine
RP Schuelke, M (corresponding author), Free Univ Berlin, D-13353 Berlin, Germany.; Schuelke, M (corresponding author), Humboldt Univ, D-13353 Berlin, Germany.; Schuelke, M (corresponding author), NeuroCure Cluster Excellence, D-10117 Berlin, Germany.; Schuelke, M (corresponding author), Charite Univ Med Berlin, D-10117 Berlin, Germany.; Schuelke, M (corresponding author), Free Univ Berlin, D-10117 Berlin, Germany.; Schuelke, M (corresponding author), Humboldt Univ, D-10117 Berlin, Germany.; Schuelke, M (corresponding author), Charite Univ Med Berlin, Dept Neuropediat, D-13353 Berlin, Germany.; Straussberg, R (corresponding author), Schneider Childrens Med Ctr, Petah Tiqwa, Israel.; Straussberg, R (corresponding author), Tel Aviv Univ, Sackler Sch Med, Dept Child Neurol, Neurogenet Serv, IL-69978 Ramat Aviv, Israel.
EM sarah.paisdzior@charite.de; ellen.knierim@charite.de;
   gunnar.kleinau@charite.de; heike.biebermann@charite.de;
   heiko.krude@charite.de; rachels2@clalit.org.il;
   markus.schuelke@charite.de
RI Kleinau, Gunnar/GPX-6330-2022; Paisdzior, Sarah/JXY-3208-2024
OI Knierim, Ellen/0000-0002-4769-7322; Schuelke,
   Markus/0000-0003-2824-3891; Paisdzior, Sarah/0000-0001-6734-4084; Krude,
   Heiko/0000-0002-1169-0348; Biebermann, Heike/0000-0002-2024-7778
FU Deutsche Forschungsgemeinschaft (DFG; German Research Foundation) under
   Germany's Excellence Strategy [EXC-2049-390688087]; Transregio
   Collaborative Research Center "LocoTact" [TRR 296 TP06]
FX This research was funded by grants of the Deutsche
   Forschungsgemeinschaft (DFG; German Research Foundation) under Germany's
   Excellence Strategy-EXC-2049-390688087 to M.S., and by the Transregio
   Collaborative Research Center "LocoTact" (TRR 296 TP06) to H.K. and M.S.
CR Berman HM, 2002, ACTA CRYSTALLOGR D, V58, P899, DOI 10.1107/S0907444902003451
   Bochukova E, 2012, NEW ENGL J MED, V366, P243, DOI 10.1056/NEJMoa1110296
   BRADLEY DJ, 1992, J NEUROSCI, V12, P2288
   Chen Y, 2010, MOL ENDOCRINOL, V24, P1650, DOI 10.1210/me.2010-0129
   Darimont BD, 1998, GENE DEV, V12, P3343, DOI 10.1101/gad.12.21.3343
   Demir K, 2016, J CLIN ENDOCR METAB, V101, P2945, DOI 10.1210/jc.2016-1404
   Dow RL, 2003, BIOORG MED CHEM LETT, V13, P379, DOI 10.1016/S0960-894X(02)00947-2
   Hall TA., 1999, NUCL ACIDS S SER, V41, P95, DOI [DOI 10.1021/BK-1999-0734.CH008, DOI 10.14344/IOC.ML.11.1]
   Harvey CB, 2002, THYROID, V12, P441, DOI 10.1089/105072502760143791
   Hofmann PJ, 2009, TOXICOL SCI, V110, P125, DOI 10.1093/toxsci/kfp086
   Hombach D, 2019, NUCLEIC ACIDS RES, V47, pW114, DOI 10.1093/nar/gkz330
   IZUMO S, 1988, NATURE, V334, P539, DOI 10.1038/334539a0
   Jiménez-Panizo A, 2019, ENDOCR-RELAT CANCER, V26, pR479, DOI 10.1530/ERC-19-0132
   Jouravel N, 2009, PROTEINS, V75, P111, DOI 10.1002/prot.22225
   KATZ D, 1993, J BIOL CHEM, V268, P20904
   Kojetin DJ, 2015, NAT COMMUN, V6, DOI 10.1038/ncomms9013
   KOPP P, 1995, NEW ENGL J MED, V332, P150, DOI 10.1056/NEJM199501193320304
   LAZAR MA, 1988, MOL ENDOCRINOL, V2, P893, DOI 10.1210/mend-2-10-893
   LAZAR MA, 1991, MOL CELL BIOL, V11, P5005, DOI 10.1128/MCB.11.10.5005
   le Maire A, 2020, THYROID, V30, P1217, DOI 10.1089/thy.2019.0602
   Li DS, 2004, J BIOL CHEM, V279, P7427, DOI 10.1074/jbc.M311596200
   Minakhina S, 2020, THYROID, V30, P1193, DOI 10.1089/thy.2019.0763
   Moran C, 2017, THYROID, V27, P973, DOI 10.1089/thy.2017.0157
   Moran C, 2014, LANCET DIABETES ENDO, V2, P619, DOI 10.1016/S2213-8587(14)70111-1
   NAGAYA T, 1993, J BIOL CHEM, V268, P15766
   Pappa T, 2018, METHODS MOL BIOL, V1801, P225, DOI 10.1007/978-1-4939-7902-8_18
   Quignodon L, 2004, J MOL ENDOCRINOL, V33, P467, DOI 10.1677/jme.1.01570
   Richards S, 2015, GENET MED, V17, P405, DOI 10.1038/gim.2015.30
   Robinson JT, 2011, NAT BIOTECHNOL, V29, P24, DOI 10.1038/nbt.1754
   SAKURAI A, 1989, P NATL ACAD SCI USA, V86, P8977, DOI 10.1073/pnas.86.22.8977
   Seiler CY, 2014, NUCLEIC ACIDS RES, V42, pD1253, DOI 10.1093/nar/gkt1060
   Souza PCT, 2014, MOL ENDOCRINOL, V28, P534, DOI 10.1210/me.2013-1359
   Tylki-Szymanska A, 2015, J MED GENET, V52, P312, DOI 10.1136/jmedgenet-2014-102936
   van Gucht ALM, 2017, CURR TOP DEV BIOL, V125, P337, DOI 10.1016/bs.ctdb.2017.02.001
   van Gucht ALM, 2016, THYROID, V26, P338, DOI 10.1089/thy.2015.0463
   van Mullem A, 2012, NEW ENGL J MED, V366, P1451, DOI 10.1056/NEJMc1113940
   van Mullem AA, 2013, J CLIN ENDOCR METAB, V98, P3029, DOI 10.1210/jc.2013-1050
   Visser WE, 2010, HUM MOL GENET, V19, P4189, DOI 10.1093/hmg/ddq337
   WEINBERGER C, 1986, NATURE, V324, P641, DOI 10.1038/324641a0
   Weiss R E, 2000, Rev Endocr Metab Disord, V1, P97, DOI 10.1023/A:1010072605757
NR 40
TC 14
Z9 14
U1 0
U2 1
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
EI 1422-0067
J9 INT J MOL SCI
JI Int. J. Mol. Sci.
PD MAY
PY 2021
VL 22
IS 10
AR 5338
DI 10.3390/ijms22105338
PG 19
WC Biochemistry & Molecular Biology; Chemistry, Multidisciplinary
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Chemistry
GA SS8FT
UT WOS:000661989200001
PM 34069457
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Makino, Y
   Uenishi, R
   Okamoto, K
   Isoe, T
   Hosono, O
   Tanaka, H
   Kanopka, A
   Poellinger, L
   Haneda, M
   Morimoto, C
AF Makino, Yuichi
   Uenishi, Rie
   Okamoto, Kensaku
   Isoe, Tsubasa
   Hosono, Osamu
   Tanaka, Hirotoshi
   Kanopka, Arvydas
   Poellinger, Lorenz
   Haneda, Masakazu
   Morimoto, Chikao
TI Transcriptional up-regulation of inhibitory PAS domain protein gene
   expression by hypoxia-inducible factor 1 (HIF-1) -: A negative
   feedback regulatory circuit in HIF-1-mediated signaling in hypoxic
   cells
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID TUMOR-SUPPRESSOR PROTEIN; NF-KAPPA-B; FACTOR-I; T-CELLS; ALPHA;
   HYDROXYLATION; IDENTIFICATION; HIF-1-ALPHA; MECHANISMS; RESPONSES
AB The inhibitory PAS (Per/Arnt/Sim) domain protein (IPAS), a dominant negative regulator of hypoxia-inducible transcription factors (HIFs), is potentially implicated in negative regulation of angiogenesis in such tissues as the avascular cornea of the eye. We have previously shown IPAS mRNA expression is up-regulated in hypoxic tissues, which at least in part involves hypoxia-dependent alternative splicing of the transcripts from the IPAS/HIF-3 alpha locus. In the present study, we demonstrate that a hypoxia-driven transcriptional mechanism also plays a role in augmentation of IPAS gene expression. Isolation and analyses of the promoter region flanking to the first exon of IPAS gene revealed a functional hypoxia response element at position -834 to -799, whereas the sequence upstream of the HIF-3 alpha first exon scarcely responded to hypoxic stimuli. A transient transfection experiment demonstrated that HIF-1 alpha mediates IPAS promoter activation via the functional hypoxia response element under hypoxic conditions and that a constitutively active form of HIF-1 alpha is sufficient for induction of the promoter in normoxic cells. Moreover, chromatin immunoprecipitation and electrophoretic mobility shift assays showed binding of the HIF-1 complex to the element in a hypoxia-dependent manner. Taken together, HIF-1 directly up-regulates IPAS gene expression through a mechanism distinct from RNA splicing, providing a further level of negative feedback gene regulation in adaptive responses to hypoxic/ischemic conditions.
C1 Asahikawa Med Coll, Dept Internal Med, Sect Metab & Biosyst Sci, Asahikawa, Hokkaido 0788510, Japan.
   Univ Tokyo, Inst Med Sci, Adv Clin Res Ctr, Div Clin Immunol,Minato Ku, Tokyo 1088639, Japan.
   Japan Sci & Technol Agcy, PRESTO, Kawaguchi, Saitama 3320012, Japan.
   Inst Biotechnol, LT-2028 Vilnius, Lithuania.
   Karolinska Inst, Med Nobel Inst, Dept Cell & Mol Biol, S-17177 Stockholm, Sweden.
C3 Asahikawa Medical College; University of Tokyo; Japan Science &
   Technology Agency (JST); Vilnius University; Karolinska Institutet
RP Makino, Y (corresponding author), Asahikawa Med Coll, Dept Internal Med, Sect Metab & Biosyst Sci, 2-1 Midorigaoka Higashi, Asahikawa, Hokkaido 0788510, Japan.
EM makino@asahikawa-med.ac.jp
CR Aprelikova O, 2004, J CELL BIOCHEM, V92, P491, DOI 10.1002/jcb.20067
   Carrero P, 2000, MOL CELL BIOL, V20, P402, DOI 10.1128/MCB.20.1.402-415.2000
   Cormier-Regard S, 1998, J BIOL CHEM, V273, P17787, DOI 10.1074/jbc.273.28.17787
   Demidenko ZN, 2005, ONCOGENE, V24, P4829, DOI 10.1038/sj.onc.1208636
   Ema M, 1997, P NATL ACAD SCI USA, V94, P4273, DOI 10.1073/pnas.94.9.4273
   Ghosh S, 1998, ANNU REV IMMUNOL, V16, P225, DOI 10.1146/annurev.immunol.16.1.225
   Gu YZ, 1998, GENE EXPRESSION, V7, P205
   Hoffmann A, 2006, IMMUNOL REV, V210, P171, DOI 10.1111/j.0105-2896.2006.00375.x
   Hu CJ, 2003, MOL CELL BIOL, V23, P9361, DOI 10.1128/MCB.23.24.9361-9374.2003
   Jelkmann W, 2003, J ENDOCRINOL INVEST, V26, P832, DOI 10.1007/BF03345232
   Kaelin WG, 2005, ANNU REV BIOCHEM, V74, P115, DOI 10.1146/annurev.biochem.74.082803.133142
   Kornblihtt AR, 2005, CURR OPIN CELL BIOL, V17, P262, DOI 10.1016/j.ceb.2005.04.014
   Kornblihtt AR, 2004, RNA, V10, P1489, DOI 10.1261/rna.7100104
   Kung AL, 2000, NAT MED, V6, P1335, DOI 10.1038/82146
   Lando D, 2002, SCIENCE, V295, P858, DOI 10.1126/science.1068592
   Leonard MO, 2003, J BIOL CHEM, V278, P40296, DOI 10.1074/jbc.M302560200
   Lowrey PL, 2000, ANNU REV GENET, V34, P533, DOI 10.1146/annurev.genet.34.1.533
   Makino Y, 2002, J BIOL CHEM, V277, P32405, DOI 10.1074/jbc.C200328200
   Makino Y, 2001, NATURE, V414, P550, DOI 10.1038/35107085
   Makino Y, 2003, J IMMUNOL, V171, P6534, DOI 10.4049/jimmunol.171.12.6534
   Manalo DJ, 2005, BLOOD, V105, P659, DOI 10.1182/blood-2004-07-2958
   Masson N, 2001, EMBO J, V20, P5197, DOI 10.1093/emboj/20.18.5197
   Maxwell PH, 1999, NATURE, V399, P271, DOI 10.1038/20459
   Maynard MA, 2003, J BIOL CHEM, V278, P11032, DOI 10.1074/jbc.M208681200
   Mimura J, 1999, GENE DEV, V13, P20, DOI 10.1101/gad.13.1.20
   Monsalve M, 2000, MOL CELL, V6, P307, DOI 10.1016/S1097-2765(00)00031-9
   Nakamura H, 2005, J IMMUNOL, V174, P7592, DOI 10.4049/jimmunol.174.12.7592
   Olenyuk BZ, 2004, P NATL ACAD SCI USA, V101, P16768, DOI 10.1073/pnas.0407617101
   Pescador N, 2005, BIOCHEM J, V390, P189, DOI 10.1042/BJ20042121
   Poellinger L, 2004, CURR OPIN GENET DEV, V14, P81, DOI 10.1016/j.gde.2003.12.006
   Reppert SM, 2002, NATURE, V418, P935, DOI 10.1038/nature00965
   Safran M, 2003, J CLIN INVEST, V111, P779, DOI 10.1172/JCI200318181
   Schofield CJ, 2004, NAT REV MOL CELL BIO, V5, P343, DOI 10.1038/nrm1366
   SCOTT ML, 1993, GENE DEV, V7, P1266, DOI 10.1101/gad.7.7a.1266
   Semenza GL, 1996, J BIOL CHEM, V271, P32529, DOI 10.1074/jbc.271.51.32529
   SEMENZA GL, 1994, J BIOL CHEM, V269, P23757
   SHWEIKI D, 1992, NATURE, V359, P845
   Tanimoto K, 2000, EMBO J, V19, P4298, DOI 10.1093/emboj/19.16.4298
   Tian H, 1998, GENE DEV, V12, P3320, DOI 10.1101/gad.12.21.3320
   WANG GL, 1993, J BIOL CHEM, V268, P21513
   WANG GL, 1995, J BIOL CHEM, V270, P1230, DOI 10.1074/jbc.270.3.1230
   Wang RS, 2006, FASEB J, V20, P1275, DOI 10.1096/fj.06-5839fje
NR 42
TC 91
Z9 111
U1 0
U2 14
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD MAY 11
PY 2007
VL 282
IS 19
BP 14073
EP 14082
DI 10.1074/jbc.M700732200
PG 10
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 164PJ
UT WOS:000246245800017
PM 17355974
OA hybrid
DA 2025-04-10
ER

PT J
AU Bevitt, DJ
   Li, Z
   Lindrop, JL
   Barker, MD
   Clarke, MP
   McKie, N
AF Bevitt, DJ
   Li, Z
   Lindrop, JL
   Barker, MD
   Clarke, MP
   McKie, N
TI Analysis of full length ADAMTS6 transcript reveals alternative splicing
   and a role for the 5′ untranslated region in translational control
SO GENE
LA English
DT Article
DE metalloprotemase; extracellular matrix; IRES; uAUG
ID CELL-LINE; IN-VIVO; METALLOPROTEINASES; EXPRESSION; MUTATIONS; CLEAVAGE;
   BINDING; FAMILY; AGGRECANASE; DISINTEGRIN
AB The ADAMTS (A Disintegrin and metalloproteinase with thrombospondin-1 type repeats) family of enzymes have been implicated in turnover of extracellular matrix. We previously showed that levels of ADAMTS6 mRNA in ARPE-19 cells were markedly increased following treatment with tumour necrosis factor alpha (TNF alpha). This study shows that the ADAMTS6 transcript contains unusually large untranslated regions (UTRs) at both the 5' and 3'end. The 5'UTR contains I I AUG codons upstream of the predicted ADAMTS6 start codon and potently inhibits translation of a downstream reporter gene. However some translation can be restored by truncating the 5'UTR from the 3'end. The 5'UTR was tested for internal ribosome entry site activity using a bicistronic luciferase reporter plasmid, but none was detected. Using the 5' and 3'UTR sequences to screen the GenBank database we identified a full length ADAMTS6 cDNA of 7262 bp. This transcript is alternatively spliced at the 3'end of the open reading frame (ORF), resulting in an extended ORF containing 3 additional tsp-1 type repeats. Quantitative RT-PCR showed that the long and short form of the ADAMTS6 ORF are co-expressed in ARPE-19 cells, but the relative levels of the two forms is modulated by TNFa. The region of the transcript encoding the catalytic domain also contains several notable differences compared to the previously published ADAMTS6 cDNA sequence, including a redefinition of the predicted active site motif. (c) 2005 Elsevier B.V. All rights reserved.
C1 Newcastle Gen Hosp, Henry Wellcome Lab Biogerontol Res, Sch Clin Med Sci, Newcastle Upon Tyne NE4 6BE, Tyne & Wear, England.
   Newcastle Univ, Sch Neurol Neurobiol & Psychiat, Newcastle Upon Tyne, Tyne & Wear, England.
   Univ Sheffield, Genom Med Acad Unit Pathol, Sheffield, S Yorkshire, England.
C3 Newcastle General Hospital; Newcastle University - UK; University of
   Sheffield
RP Newcastle Gen Hosp, Henry Wellcome Lab Biogerontol Res, Sch Clin Med Sci, Newcastle Upon Tyne NE4 6BE, Tyne & Wear, England.
EM norman.mckie@ncl.ac.uk
OI Li, Zheng/0000-0002-7060-2213
CR Abbaszade I, 1999, J BIOL CHEM, V274, P23443, DOI 10.1074/jbc.274.33.23443
   ALTSCHUL SF, 1990, J MOL BIOL, V215, P403, DOI 10.1016/S0022-2836(05)80360-2
   Apte SS, 2004, INT J BIOCHEM CELL B, V36, P981, DOI 10.1016/j.biocel.2004.01.014
   Barshishat M, 2002, CLIN EXP METASTAS, V19, P327, DOI 10.1023/A:1015528314970
   Bevitt DJ, 2003, BBA-GENE STRUCT EXPR, V1626, P83, DOI 10.1016/S0167-4781(03)00047-2
   Colige A, 2004, J INVEST DERMATOL, V123, P656, DOI 10.1111/j.0022-202X.2004.23406.x
   Colige A, 1997, P NATL ACAD SCI USA, V94, P2374, DOI 10.1073/pnas.94.6.2374
   Colige A, 1999, AM J HUM GENET, V65, P308, DOI 10.1086/302504
   Collins-Racie LA, 2004, MATRIX BIOL, V23, P219, DOI 10.1016/j.matbio.2004.05.004
   Dagoneau N, 2004, AM J HUM GENET, V75, P801, DOI 10.1086/425231
   Dickinson SC, 2003, MATRIX BIOL, V22, P267, DOI 10.1016/S0945-053X(03)00034-9
   Fernandes RJ, 2001, J BIOL CHEM, V276, P31502, DOI 10.1074/jbc.M103466200
   Geballe AP, 2000, COLD SPRING HARBOR M, V39, P595
   Glasson SS, 2005, NATURE, V434, P644, DOI 10.1038/nature03369
   Hurskainen TL, 1999, J BIOL CHEM, V274, P25555, DOI 10.1074/jbc.274.36.25555
   Kashiwagi M, 2004, J BIOL CHEM, V279, P10109, DOI 10.1074/jbc.M312123200
   Kevorkian L, 2004, ARTHRITIS RHEUM-US, V50, P131, DOI 10.1002/art.11433
   Kim YK, 2000, J MOL BIOL, V304, P119, DOI 10.1006/jmbi.2000.4179
   KOZAK M, 1987, NUCLEIC ACIDS RES, V15, P8125, DOI 10.1093/nar/15.20.8125
   KOZAK M, 1978, CELL, V15, P1109, DOI 10.1016/0092-8674(78)90039-9
   Kozak M, 2002, MAMM GENOME, V13, P401, DOI 10.1007/s00335-002-4002-5
   KOZAK M, 1986, CELL, V44, P283, DOI 10.1016/0092-8674(86)90762-2
   Levy GG, 2001, NATURE, V413, P488, DOI 10.1038/35097008
   Llamazares M, 2003, J BIOL CHEM, V278, P13382, DOI 10.1074/jbc.M211900200
   Luque A, 2003, J BIOL CHEM, V278, P23656, DOI 10.1074/jbc.M212964200
   Majerus EM, 2003, J BIOL CHEM, V278, P46643, DOI 10.1074/jbc.M309872200
   Matthews RT, 2000, J BIOL CHEM, V275, P22695, DOI 10.1074/jbc.M909764199
   Meijer HA, 2002, BIOCHEM J, V367, P1, DOI 10.1042/BJ20011706
   Porter S, 2004, CLIN CANCER RES, V10, P2429, DOI 10.1158/1078-0432.CCR-0398-3
   Pratta MA, 2003, J BIOL CHEM, V278, P45539, DOI 10.1074/jbc.M303737200
   Rodríguez-Manzaneque JC, 2000, J BIOL CHEM, V275, P33471, DOI 10.1074/jbc.M002599200
   Rodríguez-Manzaneque JC, 2002, BIOCHEM BIOPH RES CO, V293, P501
   Russell DL, 2003, J BIOL CHEM, V278, P42330, DOI 10.1074/jbc.M300519200
   Sandy JD, 2001, J BIOL CHEM, V276, P13372, DOI 10.1074/jbc.M009737200
   Somerville RPT, 2004, J BIOL CHEM, V279, P51208, DOI 10.1074/jbc.M409036200
   Somerville RPT, 2003, J BIOL CHEM, V278, P9503, DOI 10.1074/jbc.M211009200
   Stanton H, 2005, NATURE, V434, P648, DOI 10.1038/nature03417
   Stoneley M, 2000, NUCLEIC ACIDS RES, V28, P687, DOI 10.1093/nar/28.3.687
   Suzuki Y, 2000, GENOMICS, V64, P286, DOI 10.1006/geno.2000.6076
   Tortorella MD, 1999, SCIENCE, V284, P1664, DOI 10.1126/science.284.5420.1664
   Vagner S, 2001, EMBO REP, V2, P893, DOI 10.1093/embo-reports/kve208
   Wang WM, 2003, J BIOL CHEM, V278, P19549, DOI 10.1074/jbc.M300767200
   Wilkie GS, 2003, TRENDS BIOCHEM SCI, V28, P182, DOI 10.1016/S0968-0004(03)00051-3
   Zheng XL, 2001, J BIOL CHEM, V276, P41059, DOI 10.1074/jbc.C100515200
NR 44
TC 15
Z9 19
U1 0
U2 3
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
SN 0378-1119
EI 1879-0038
J9 GENE
JI Gene
PD OCT 10
PY 2005
VL 359
BP 99
EP 110
DI 10.1016/j.gene.2005.06.011
PG 12
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA 974JG
UT WOS:000232587000011
PM 16129570
DA 2025-04-10
ER

PT J
AU Sun, AJ
   Ge, JB
   Siffert, W
   Frey, UH
AF Sun, AJ
   Ge, JB
   Siffert, W
   Frey, UH
TI Quantification of allele-specific G-protein β3 subunit mRNA transcripts
   in different human cells and tissues by pyrosequencing
SO EUROPEAN JOURNAL OF HUMAN GENETICS
LA English
DT Article
DE G-protein; genetic polymorphism; allele quantification; Pyrosequencing;
   imprinting
ID BETA-3 SUBUNIT GENE; C825T POLYMORPHISM; SPLICE VARIANT; BLOOD-PRESSURE;
   DNA POOLS; ASSOCIATION; GNB3; HYPERTENSION; IDENTIFICATION; MARKER
AB The G-protein 825T allele is associated with altered drug responses while the underlying mechanism is not fully understood. Differential expression of transcripts from the C and T alleles could contribute to this process. The C825T polymorphism located in exon 10 is in close linkage disequilibrium with the A(-350) G promoter single nucleotide polymorphism (SNP) and the C1429T SNP and could therefore serve as a marker for allele-specific expression resulting from the promoter SNP. However, alternative splicing of exon 10 in 825T allele carriers may result in under-represented mRNA transcripts. We, therefore, established a novel method based on the Pyrosequencing technology to quantify allele-specific transcript expression and quantified the allelic variance of the C1429T polymorphism located in the 3'-untranslated region of GNB3. Validation of the method was performed using linear regression analysis of measured versus expected ratios of DNA mixed at different known concentrations as well as determining allele-specific mRNA expression of the partially imprinted IGF-2 gene. We genotyped the C1429T polymorphism of 83 samples derived from six different human tissues and cell lines and quantified mRNA transcripts from different alleles using heterozygous samples. No significantly different transcript amounts from the two alleles were found. There were also no significantly different transcript amounts associated with different G(-350) A genotypes (P > 40.05). As a result, we could show that Pyrosequencing provides a sensitive tool to quantify allele-specific transcript expression. Our data do not support the hypothesis that differential G-protein activity associated with the C825T SNP results from different transcript amounts associated with specific GNB3 genotypes.
C1 Fudan Univ, Zhongshan Hosp, Inst Cardiovasc Dis, Shanghai, Peoples R China.
   Univ Essen Gesamthsch, Fac Med, Inst Pharmacol, D-4300 Essen 1, Germany.
C3 Fudan University; University of Duisburg Essen
RP Univ Hosp, Inst Pharmacol, Hufelandstr 55, D-45122 Essen, Germany.
EM ulrich.frey@uni-essen.de
RI Frey, Ulrich/C-2752-2019; Sun, Jihong/AGN-2573-2022
OI Frey, Ulrich/0000-0003-2961-6629
CR Ahmadian A, 2000, ANAL BIOCHEM, V280, P103, DOI 10.1006/abio.2000.4493
   Beige J, 1999, J AM SOC NEPHROL, V10, P1717
   Benjafield AV, 1998, HYPERTENSION, V32, P1094, DOI 10.1161/01.HYP.32.6.1094
   Brand E, 2003, J HYPERTENS, V21, P729, DOI 10.1097/00004872-200304000-00016
   Brand E, 1999, HYPERTENSION, V33, P1175, DOI 10.1161/01.HYP.33.5.1175
   Cui HM, 2003, SCIENCE, V299, P1753, DOI 10.1126/science.1080902
   EFSTRATIADIS A, 1994, CURR OPIN GENET DEV, V4, P265, DOI 10.1016/S0959-437X(05)80054-1
   Gruber JD, 2002, HUM GENET, V110, P395, DOI 10.1007/s00439-002-0722-6
   Hauner H, 2003, PHARMACOGENETICS, V13, P453, DOI 10.1097/00008571-200308000-00003
   Hengstenberg C, 2001, CARDIOVASC RES, V49, P820, DOI 10.1016/S0008-6363(00)00292-3
   Huang XH, 2003, J MOL MED, V81, P729, DOI 10.1007/s00109-003-0482-3
   Ishikawa K, 2000, AM J HYPERTENS, V13, P140, DOI 10.1016/S0895-7061(99)00118-1
   Knight JC, 2003, NAT GENET, V33, P469, DOI 10.1038/ng1124
   LABARCA C, 1980, ANAL BIOCHEM, V102, P344, DOI 10.1016/0003-2697(80)90165-7
   Lindemann M, 2001, FEBS LETT, V495, P82, DOI 10.1016/S0014-5793(01)02339-0
   Morison IM, 2000, BLOOD, V96, P3023, DOI 10.1182/blood.V96.9.3023.h8003023_3023_3028
   Nürnberger J, 2003, CLIN PHARMACOL THER, V74, P53, DOI 10.1016/S0009-9236(03)00087-0
   Ronaghi M, 1996, ANAL BIOCHEM, V242, P84, DOI 10.1006/abio.1996.0432
   Ronaghi M, 1998, SCIENCE, V281, P363, DOI 10.1126/science.281.5375.363
   Rosskopf D, 2003, CELL SIGNAL, V15, P479, DOI 10.1016/S0898-6568(02)00140-7
   Rosskopf D, 2003, BIOCHEM J, V371, P223, DOI 10.1042/BJ20021208
   Rosskopf D, 2002, PHARMACOGENETICS, V12, P209, DOI 10.1097/00008571-200204000-00005
   Rosskopf D, 2000, HYPERTENSION, V36, P33, DOI 10.1161/01.HYP.36.1.33
   Ruiz-Velasco V, 2003, PHYSIOL GENOMICS, V13, P85, DOI 10.1152/physiolgenomics.00057.2002
   Rydén M, 2002, DIABETES, V51, P1601, DOI 10.2337/diabetes.51.5.1601
   Sakatani T, 2001, BIOCHEM BIOPH RES CO, V283, P1124, DOI 10.1006/bbrc.2001.4916
   Schunkert H, 1998, HYPERTENSION, V32, P510, DOI 10.1161/01.HYP.32.3.510
   Shioji K, 2004, HYPERTENS RES, V27, P31, DOI 10.1291/hypres.27.31
   Siffert W, 1998, NAT GENET, V18, P45, DOI 10.1038/ng0198-45
   Snapir A, 2001, J HYPERTENS, V19, P2149, DOI 10.1097/00004872-200112000-00006
   Sperling H, 2003, J UROLOGY, V169, P1048, DOI 10.1097/01.ju.0000058369.72348.ba
   Suwazono Y, 2004, OBES RES, V12, P4, DOI 10.1038/oby.2004.2
   Turner ST, 2001, HYPERTENSION, V37, P739, DOI 10.1161/01.HYP.37.2.739
   Virchow S, 1998, FEBS LETT, V436, P155, DOI 10.1016/S0014-5793(98)01110-7
   Wasson J, 2002, BIOTECHNIQUES, V32, P1144, DOI 10.2144/02325dd04
   Wu HK, 1997, BIOCHEM BIOPH RES CO, V231, P466, DOI 10.1006/bbrc.1997.6127
   Yan H, 2002, SCIENCE, V297, P1143, DOI 10.1126/science.1072545
   Zill P, 2000, NEUROREPORT, V11, P1893, DOI 10.1097/00001756-200006260-00018
NR 38
TC 27
Z9 35
U1 0
U2 8
PU NATURE PUBLISHING GROUP
PI LONDON
PA MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
SN 1018-4813
EI 1476-5438
J9 EUR J HUM GENET
JI Eur. J. Hum. Genet.
PD MAR
PY 2005
VL 13
IS 3
BP 361
EP 369
DI 10.1038/sj.ejhg.5201334
PG 9
WC Biochemistry & Molecular Biology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Genetics & Heredity
GA 899AK
UT WOS:000227117100017
PM 15536475
OA hybrid
DA 2025-04-10
ER

PT J
AU Sudo, T
   Yagasaki, Y
   Hama, H
   Watanabe, N
   Osada, H
AF Sudo, T
   Yagasaki, Y
   Hama, H
   Watanabe, N
   Osada, H
TI Exip, a new alternative splicing variant of p38α, can induce an earlier
   onset of apoptosis in HeLa cells
SO BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
LA English
DT Article
ID ACTIVATED PROTEIN-KINASE; P38 MAP KINASE; KIDNEY ISCHEMIA; HEAT-SHOCK;
   STRESS; PHOSPHORYLATION; FAMILY; INTERLEUKIN-1; INHIBITOR; ISOFORMS
AB One of the major families of the mitogen-activated kinases (MAPK), p38, has been shown to transduce extracellular stress stimuli into cellular responses. Among them, p38a is the best characterized isoform and many biological phenomena, especially in the inflammatory responses, were attributed to the specific inhibitor-sensitive isoforms, namely p38a and p38beta. However, the roles played by each member are still unclear. Here, we report the identification of a new splice variant of p38alpha, Exip (for exon skip), by RT-PCR using mRNA derived from a renal tumor cell line, OS-RC-2. Exip is predicted to encode a 307-amino-acid protein and the absence of exons 10, 11, and 11' results in the shift of the reading frame at the exon 9-12 junction to produce a unique 53-amino-acid C-terminus. The expression of mRNA was barely observed in cultured cells tested, but substantial amounts of mRNA were detected in mouse tissues. Unlike p38a, Exip lost a common docking domain well conserved in major MAPK families for their specific interactions with upstream kinases or downstream substrates. Even though Exip is not phosphorylated at conserved TGY motif by p38-activating treatments, such as an osmotic shock or coexpression with a constitutive active form of MKK6 in HeLa cells, Exip can induce an earlier onset of apoptosis in HeLa cells. These results indicate that Exip has unique properties as a member of p38a and may play role(s) in the signal transduction pathway(s) different from those of p38alpha. (C) 2002 Elsevier Science (USA)
C1 RIKEN, Antibiot Lab, Wako, Saitama 3510198, Japan.
   RIKEN, Bioarchitect Res Grp, Wako, Saitama 3510198, Japan.
   RIKEN, Brain Sci Inst, Lab Cell Funct & Dynam, Wako, Saitama 3510198, Japan.
   Saitama Univ, Grad Sch Sci & Engn, Urawa, Saitama 3388570, Japan.
   Toho Univ, Fac Sci, Chiba 2748510, Japan.
C3 RIKEN; RIKEN; RIKEN; Saitama University; Toho University
RP Sudo, T (corresponding author), RIKEN, Antibiot Lab, 2-1 Hirosawa, Wako, Saitama 3510198, Japan.
RI Osada, Hiroyuki/AAY-6254-2020; Sudo, Tatsuhiko/KDM-5414-2024
OI xu teng, long yan/0000-0003-2526-3707
CR Adams RH, 2000, MOL CELL, V6, P109, DOI 10.1016/S1097-2765(00)00012-5
   Allen M, 2000, J EXP MED, V191, P859, DOI 10.1084/jem.191.5.859
   Bolduc L, 2001, J BIOL CHEM, V276, P17597, DOI 10.1074/jbc.M011769200
   BOULTON TG, 1991, CELL, V65, P663, DOI 10.1016/0092-8674(91)90098-J
   CUENDA A, 1995, FEBS LETT, V364, P229, DOI 10.1016/0014-5793(95)00357-F
   DERIJARD B, 1995, SCIENCE, V267, P682, DOI 10.1126/science.7839144
   Enslen H, 1998, J BIOL CHEM, V273, P1741, DOI 10.1074/jbc.273.3.1741
   Eyers PA, 1998, CHEM BIOL, V5, P321, DOI 10.1016/S1074-5521(98)90170-3
   Faccio L, 2000, J BIOL CHEM, V275, P2581, DOI 10.1074/jbc.275.4.2581
   Faccio L, 2000, AM J PHYSIOL-CELL PH, V278, pC781, DOI 10.1152/ajpcell.2000.278.4.C781
   FRESHNEY NW, 1994, CELL, V78, P1039, DOI 10.1016/0092-8674(94)90278-X
   Gupta S, 1996, EMBO J, V15, P2760, DOI 10.1002/j.1460-2075.1996.tb00636.x
   HAN J, 1994, SCIENCE, V265, P808, DOI 10.1126/science.7914033
   Han J, 1997, NATURE, V386, P296, DOI 10.1038/386296a0
   Ichida M, 2000, J BIOL CHEM, V275, P15992, DOI 10.1074/jbc.275.21.15992
   Jiang Y, 1997, J BIOL CHEM, V272, P30122, DOI 10.1074/jbc.272.48.30122
   Kawasaki H, 1997, J BIOL CHEM, V272, P18518, DOI 10.1074/jbc.272.30.18518
   LEE JC, 1994, NATURE, V372, P739, DOI 10.1038/372739a0
   MARSHALL CJ, 1995, CELL, V80, P179, DOI 10.1016/0092-8674(95)90401-8
   Mudgett JS, 2000, P NATL ACAD SCI USA, V97, P10454, DOI 10.1073/pnas.180316397
   Mukherjee PK, 1999, J BIOL CHEM, V274, P6493, DOI 10.1074/jbc.274.10.6493
   ROUSE J, 1994, CELL, V78, P1027, DOI 10.1016/0092-8674(94)90277-1
   STOKOE D, 1992, EMBO J, V11, P3985, DOI 10.1002/j.1460-2075.1992.tb05492.x
   Sudo T, 2000, BIOCHEM BIOPH RES CO, V269, P521, DOI 10.1006/bbrc.2000.2333
   Takekawa M, 1998, CELL, V95, P521, DOI 10.1016/S0092-8674(00)81619-0
   Tamura K, 2000, CELL, V102, P221, DOI 10.1016/S0092-8674(00)00027-1
   Tanoue T, 2000, NAT CELL BIOL, V2, P110, DOI 10.1038/35000065
   Tong L, 1997, NAT STRUCT BIOL, V4, P311, DOI 10.1038/nsb0497-311
   Wang XZ, 1996, SCIENCE, V272, P1347, DOI 10.1126/science.272.5266.1347
   XIA ZG, 1995, SCIENCE, V270, P1326, DOI 10.1126/science.270.5240.1326
   ZERVOS AS, 1995, P NATL ACAD SCI USA, V92, P10531, DOI 10.1073/pnas.92.23.10531
NR 31
TC 20
Z9 24
U1 0
U2 1
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0006-291X
J9 BIOCHEM BIOPH RES CO
JI Biochem. Biophys. Res. Commun.
PD MAR 8
PY 2002
VL 291
IS 4
BP 838
EP 843
DI 10.1006/bbrc.2002.6529
PG 6
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA 532EJ
UT WOS:000174458400018
PM 11866441
DA 2025-04-10
ER

PT J
AU Romano, M
   Bacalini, MG
   Verschoor, EJ
   Crovella, S
   Baralle, FE
AF Romano, Maurizio
   Bacalini, Maria Giulia
   Verschoor, Ernst J.
   Crovella, Sergio
   Baralle, Francisco E.
TI Origin and evolution of the c.844_845ins68/c.833T&gt;C mutations within
   the cystathionine β-synthase gene in great apes
SO FEBS LETTERS
LA English
DT Article
DE CBS; 844ins68; T833C; alternative splicing; evolution; apes
ID CORONARY-ARTERY; 844INS68; HOMOCYSTINURIA; VARIANT; POLYMORPHISMS;
   POPULATION; DEFICIENCY; METABOLISM; HISTORY; ENZYMES
AB The c.[833C; 844 845ins68] is a common haplotype of the human cystathionine beta-synthase gene among healthy individuals. This polymorphism (5-40 % allelic frequency in different populations) consists of the c.844_845ins68 insertion that segregates in cis with the pathogenic c.833T>C substitution (p.I278T). Through genotyping of primates, we have found that gorillas, chimpanzees and bonobos are homozygous for the 68 by insertion, c.844_845ins68. In gorillas and bonobos, the c.844_845ins68 lesion segregates in cis with the wild-type c.833T variant, whilst chimpanzees present the human haplotype. These genetic evidences suggest that the origin of the 68 by insertion might be dated back to 6-8 million years ago, and that the c.833T>C substitution occurred within the allele carrying the insertion. The evolutionary conservation of this peculiar haplotype supports the hypothesis of its protective effects against cardiovascular diseases. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
C1 [Romano, Maurizio; Bacalini, Maria Giulia; Baralle, Francisco E.] Int Ctr Genet Engn & Biotechnol, I-34012 Trieste, Italy.
   [Romano, Maurizio] Univ Trieste, Dept Physiol & Pathol, I-34127 Trieste, Italy.
   [Verschoor, Ernst J.] Biomed Primate Res Ctr, Dept Virol, NL-2288 GJ Rijswijk, Netherlands.
   [Crovella, Sergio] Univ Trieste, Dept Reprod & Dev Sci, I-34137 Trieste, Italy.
   [Crovella, Sergio] Genet Serv IRCCS Burlo Garofolo Trieste, I-34137 Trieste, Italy.
C3 International Center for Genetic Engineering & Biotechnology (ICGEB);
   University of Trieste; University of Trieste; IRCCS Burlo Garofolo
RP Baralle, FE (corresponding author), Int Ctr Genet Engn & Biotechnol, Padriciano 99, I-34012 Trieste, Italy.
EM baralle@icgeb.org
RI Crovella, Sergio/K-5050-2016; BACALINI, MARIA GIULIA/K-4931-2016;
   Romano, Maurizio/G-9431-2012
OI BACALINI, MARIA GIULIA/0000-0003-1618-2673; Crovella,
   Sergio/0000-0001-8493-1168; Romano, Maurizio/0000-0002-4820-2897
FU Telethon [GGP06147] Funding Source: Medline
CR Dupont LM, 2001, GEOLOGY, V29, P195, DOI 10.1130/0091-7613(2001)029<0195:MPECIT>2.0.CO;2
   Franco RF, 1998, HUM HERED, V48, P338, DOI 10.1159/000022826
   Fredriksen Å, 2007, HUM MUTAT, V28, P856, DOI 10.1002/humu.20522
   Ge Y, 2002, LEUKEMIA, V16, P2339, DOI 10.1038/sj.leu.2402705
   Glazko GV, 2003, MOL BIOL EVOL, V20, P424, DOI 10.1093/molbev/msg050
   Hofreiter M, 2004, P NATL ACAD SCI USA, V101, P12963, DOI 10.1073/pnas.0403618101
   Janosíková B, 2003, MOL GENET METAB, V79, P167, DOI 10.1016/S1096-7192(03)00079-9
   Kluijtmans LAJ, 1997, BIOCHEM MOL MED, V62, P23, DOI 10.1006/bmme.1997.2623
   Kraus JP, 1999, HUM MUTAT, V13, P362
   Linnebank Michael, 2006, Hum Mutat, V27, P1063, DOI 10.1002/humu.9459
   MAYR E, 1986, EVOLUTION, V40, P55, DOI 10.1111/j.1558-5646.1986.tb05717.x
   Mikkelsen TS, 2005, NATURE, V437, P69, DOI 10.1038/nature04072
   MUDD SH, 1985, AM J HUM GENET, V37, P1
   Pepe G, 1999, HUM GENET, V104, P126, DOI 10.1007/s004390050924
   Richter B, 2001, J HUM GENET, V46, P105, DOI 10.1007/s100380170096
   Romano M, 2002, J BIOL CHEM, V277, P43821, DOI 10.1074/jbc.M208107200
   SEBASTIO G, 1995, AM J HUM GENET, V56, P1324
   Song KS, 2001, THROMB HAEMOSTASIS, V86, P1130
   Sperandeo MP, 1996, AM J HUM GENET, V59, P1391
   Thalmann OH, 2007, MOL BIOL EVOL, V24, P146, DOI 10.1093/molbev/msl160
   Tsai MY, 1996, AM J HUM GENET, V59, P1262
   Vyletal P, 2007, HUM MUTAT, V28, P255, DOI 10.1002/humu.20430
   Zhang GS, 2001, THROMB RES, V104, P187, DOI 10.1016/S0049-3848(01)00352-8
NR 23
TC 5
Z9 5
U1 0
U2 0
PU WILEY-BLACKWELL
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0014-5793
EI 1873-3468
J9 FEBS LETT
JI FEBS Lett.
PD FEB 6
PY 2008
VL 582
IS 3
BP 423
EP 426
DI 10.1016/j.febslet.2007.12.038
PG 4
WC Biochemistry & Molecular Biology; Biophysics; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics; Cell Biology
GA 318EE
UT WOS:000257073600005
PM 18201569
OA Bronze
DA 2025-04-10
ER

PT J
AU Nicolas, HA
   Akimenko, MA
   Tesson, F
AF Nicolas, Hannah A.
   Akimenko, Marie-Andree
   Tesson, Frederique
TI Cellular and Animal Models of Striated Muscle Laminopathies
SO CELLS
LA English
DT Review
DE lamin A; C; striated muscle laminopathies; DCM; EDMD; L-CMD; LGMD;
   cellular models; animal models
ID LAMIN A/C GENE; CHARCOT-MARIE-TOOTH; A-TYPE LAMINS; FAMILIAL PARTIAL
   LIPODYSTROPHY; NUCLEAR-ENVELOPE ALTERATIONS; CAUSE AUTOSOMAL-DOMINANT;
   LMNA-MUTATIONS CAUSE; DILATED CARDIOMYOPATHY; MUSCULAR-DYSTROPHY;
   FARNESYLTRANSFERASE INHIBITOR
AB The lamin A/C (LMNA) gene codes for nuclear intermediate filaments constitutive of the nuclear lamina. LMNA has 12 exons and alternative splicing of exon 10 results in two major isoformslamins A and C. Mutations found throughout the LMNA gene cause a group of diseases collectively known as laminopathies, of which the type, diversity, penetrance and severity of phenotypes can vary from one individual to the other, even between individuals carrying the same mutation. The majority of the laminopathies affect cardiac and/or skeletal muscles. The underlying molecular mechanisms contributing to such tissue-specific phenotypes caused by mutations in a ubiquitously expressed gene are not yet well elucidated. This review will explore the different phenotypes observed in established models of striated muscle laminopathies and their respective contributions to advancing our understanding of cardiac and skeletal muscle-related laminopathies. Potential future directions for developing effective treatments for patients with lamin A/C mutation-associated cardiac and/or skeletal muscle conditions will be discussed.
C1 [Nicolas, Hannah A.; Akimenko, Marie-Andree] Univ Ottawa, Dept Biol, Fac Sci, Ottawa, ON K1N 6N5, Canada.
   [Tesson, Frederique] Univ Ottawa, Interdisciplinary Sch Hlth Sci, Ottawa, ON K1N 6N5, Canada.
C3 University of Ottawa; University of Ottawa
RP Tesson, F (corresponding author), Univ Ottawa, Interdisciplinary Sch Hlth Sci, Ottawa, ON K1N 6N5, Canada.
EM hnico019@uottawa.ca; makimen@uottawa.ca; ftesson@uottawa.ca
OI Nicolas, Hannah/0000-0002-6379-2135
CR Agarwal AK, 2003, HUM MOL GENET, V12, P1995, DOI 10.1093/hmg/ddg213
   Alsheimer M, 1996, EXP CELL RES, V228, P181, DOI 10.1006/excr.1996.0315
   Alsheimer M, 2004, J CELL SCI, V117, P1173, DOI 10.1242/jcs.00975
   Arimura T, 2005, HUM MOL GENET, V14, P155, DOI 10.1093/hmg/ddi017
   Arimura T, 2013, CARDIOVASC RES, V99, P382, DOI 10.1093/cvr/cvt106
   Bank EM, 2011, MOL BIOL CELL, V22, P2716, DOI 10.1091/mbc.E11-01-0064
   Ben Yaou R, 2007, NEUROLOGY, V68, P1883
   Benedetti S, 2007, NEUROLOGY, V69, P1285, DOI 10.1212/01.wnl.0000261254.87181.80
   Bertrand AT, 2014, J CELL SCI, V127, P2873, DOI 10.1242/jcs.144907
   Bertrand AT, 2012, HUM MOL GENET, V21, P1037, DOI 10.1093/hmg/ddr534
   Boguslavsky RL, 2006, HUM MOL GENET, V15, P653, DOI 10.1093/hmg/ddi480
   Bonne G, 2000, ANN NEUROL, V48, P170, DOI 10.1002/1531-8249(200008)48:2<170::AID-ANA6>3.0.CO;2-J
   Bonne G, 1999, NAT GENET, V21, P285, DOI 10.1038/6799
   Boudreau É, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0045918
   Bouhouche A, 2007, BRAIN, V130, P1062, DOI 10.1093/brain/awm014
   Broers JLV, 2006, PHYSIOL REV, V86, P967, DOI 10.1152/physrev.00047.2005
   Buendia B., 2015, ORPHANET J RARE DIS, V10, pO13, DOI [10.1186/1750-1172-10-S2-O13, DOI 10.1186/1750-1172-10-S2-O13]
   Cargnello M, 2011, MICROBIOL MOL BIOL R, V75, P50, DOI 10.1128/MMBR.00031-10
   Cartegni L, 1997, HUM MOL GENET, V6, P2257, DOI 10.1093/hmg/6.13.2257
   Cattin ME, 2013, HUM MOL GENET, V22, P3152, DOI 10.1093/hmg/ddt172
   Cenni V, 2005, J MED GENET, V42, P214, DOI 10.1136/jmg.2004.026112
   Chaouch M, 2003, NEUROMUSCULAR DISORD, V13, P60, DOI 10.1016/S0960-8966(02)00196-7
   Choi JC, 2012, SCI TRANSL MED, V4, DOI 10.1126/scitranslmed.3003875
   Chojnacki S, 2017, NUCLEIC ACIDS RES, V45, pW550, DOI 10.1093/nar/gkx273
   Clements L, 2000, BIOCHEM BIOPH RES CO, V267, P709, DOI 10.1006/bbrc.1999.2023
   Cobb AM, 2016, AGING CELL, V15, P1039, DOI 10.1111/acel.12506
   Coffinier C, 2010, J BIOL CHEM, V285, P20818, DOI 10.1074/jbc.M110.128835
   Cutler DA, 2002, BIOCHEM BIOPH RES CO, V291, P522, DOI 10.1006/bbrc.2002.6466
   D'Amico A, 2005, NEUROMUSCULAR DISORD, V15, P521, DOI 10.1016/j.nmd.2005.03.006
   Davidson PM, 2014, TRENDS CELL BIOL, V24, P247, DOI 10.1016/j.tcb.2013.11.004
   Davies BSJ, 2010, HUM MOL GENET, V19, P2682, DOI 10.1093/hmg/ddq158
   Davis J, 2012, CIRC RES, V111, P761, DOI 10.1161/CIRCRESAHA.111.262717
   De Sandre-Giovannoli A, 2002, AM J HUM GENET, V70, P726, DOI 10.1086/339274
   di Barletta MR, 2000, AM J HUM GENET, V66, P1407, DOI 10.1086/302869
   Dialynas G, 2015, PLOS GENET, V11, DOI 10.1371/journal.pgen.1005231
   Dialynas G, 2012, HUM MOL GENET, V21, P1544, DOI 10.1093/hmg/ddr592
   Dialynas G, 2010, DEVELOPMENT, V137, P3067, DOI 10.1242/dev.048231
   Diraison F, 2008, J LIPID RES, V49, P814, DOI 10.1194/jlr.M700533-JLR200
   Eriksson M, 2003, NATURE, V423, P293, DOI 10.1038/nature01629
   Fatkin D, 1999, NEW ENGL J MED, V341, P1715, DOI 10.1056/NEJM199912023412302
   Fong LG, 2006, J CLIN INVEST, V116, P743, DOI 10.1172/JCI27125
   Forleo C, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0121723
   FRANCISCO A, 2001, CARDIOL, V36, p699.e, DOI DOI 10.1016/j.repc.2016.07.018
   FURUKAWA K, 1994, EXP CELL RES, V212, P426, DOI 10.1006/excr.1994.1164
   Gilchrist S, 2004, BMC CELL BIOL, V5, DOI 10.1186/1471-2121-5-46
   Gordon LB, 2012, P NATL ACAD SCI USA, V109, P16666, DOI 10.1073/pnas.1202529109
   Gupta P, 2010, BASIC RES CARDIOL, V105, P365, DOI 10.1007/s00395-010-0085-4
   Harborth J, 2001, J CELL SCI, V114, P4557
   Hasselberg NE, 2018, EUR HEART J, V39, P853, DOI 10.1093/eurheartj/ehx596
   Hasty AH, 2000, J BIOL CHEM, V275, P31069, DOI 10.1074/jbc.M003335200
   Ho JCY, 2011, AGING-US, V3, P380, DOI 10.18632/aging.100277
   Holt I, 2003, J CELL SCI, V116, P3027, DOI 10.1242/jcs.00599
   Hutchison CJ, 2014, SEMIN CELL DEV BIOL, V29, P158, DOI 10.1016/j.semcdb.2013.12.012
   Jahn D, 2012, NUCLEUS-AUSTIN, V3, P463, DOI 10.4161/nucl.21676
   Kato K, 2016, J CARDIOL, V68, P346, DOI 10.1016/j.jjcc.2015.10.013
   Kim JB, 1996, GENE DEV, V10, P1096, DOI 10.1101/gad.10.9.1096
   Kim Y, 2013, BIOCHEM BIOPH RES CO, V440, P8, DOI 10.1016/j.bbrc.2013.08.082
   Kochin V, 2014, J CELL SCI, V127, P2683, DOI 10.1242/jcs.141820
   Koshimizu E, 2011, PLOS ONE, V6, DOI 10.1371/journal.pone.0017688
   Krimm I, 2002, STRUCTURE, V10, P811, DOI 10.1016/S0969-2126(02)00777-3
   Kubben N, 2011, NUCLEUS-PHILA, V2, P195, DOI 10.4161/nucl.2.3.15731
   Lammerding J, 2004, J CLIN INVEST, V113, P370, DOI 10.1172/JCI200419670
   Lammerding J, 2006, J BIOL CHEM, V281, P25768, DOI 10.1074/jbc.M513511200
   Lanzicher T, 2015, SCI REP-UK, V5, DOI 10.1038/srep13388
   Larrieu D, 2014, SCIENCE, V344, P527, DOI 10.1126/science.1252651
   Laurini E, 2018, CARDIOVASC RES, V114, P846, DOI 10.1093/cvr/cvy040
   Le Dour C, 2017, HUM MOL GENET, V26, P333, DOI 10.1093/hmg/ddw389
   Lee JSH, 2007, BIOPHYS J, V93, P2542, DOI 10.1529/biophysj.106.102426
   LIN F, 1993, J BIOL CHEM, V268, P16321
   Liu J, 2000, MOL BIOL CELL, V11, P3937, DOI 10.1091/mbc.11.11.3937
   Lloyd DJ, 2002, HUM MOL GENET, V11, P769, DOI 10.1093/hmg/11.7.769
   Lu D, 2010, PLOS ONE, V5, DOI 10.1371/journal.pone.0015167
   Machiels BM, 1996, J BIOL CHEM, V271, P9249, DOI 10.1074/jbc.271.16.9249
   MacRae C., 2016, P EUR SOC CARD C ROM
   Markandeya YS, 2016, HEART RHYTHM, V13, P2228, DOI 10.1016/j.hrthm.2016.08.007
   Mattout A, 2011, CURR BIOL, V21, P1603, DOI 10.1016/j.cub.2011.08.030
   MCKEON FD, 1986, NATURE, V319, P463, DOI 10.1038/319463a0
   Mercuri E, 2005, MUSCLE NERVE, V31, P602, DOI 10.1002/mus.20293
   Mitsuhashi H, 2010, J CELL SCI, V123, P3893, DOI 10.1242/jcs.072157
   Motsch I, 2005, EUR J CELL BIOL, V84, P765, DOI 10.1016/j.ejcb.2005.04.004
   Mounkes LC, 2005, HUM MOL GENET, V14, P2167, DOI 10.1093/hmg/ddi221
   Mounkes LC, 2003, NATURE, V423, P298, DOI 10.1038/nature01631
   Muchir A, 2000, HUM MOL GENET, V9, P1453, DOI 10.1093/hmg/9.9.1453
   Muchir A, 2003, EXP CELL RES, V291, P352, DOI 10.1016/j.yexcr.2003.07.002
   Muchir A, 2004, MUSCLE NERVE, V30, P444, DOI 10.1002/mus.20122
   Muchir A, 2007, J CLIN INVEST, V117, P1282, DOI 10.1172/JCI29042
   Muchir A, 2014, BIOCHEM BIOPH RES CO, V452, P958, DOI 10.1016/j.bbrc.2014.09.020
   Muchir A, 2013, SKELET MUSCLE, V3, DOI 10.1186/2044-5040-3-17
   Muchir A, 2012, HUM MOL GENET, V21, P4325, DOI 10.1093/hmg/dds265
   Muchir A, 2012, CARDIOVASC RES, V93, P311, DOI 10.1093/cvr/cvr301
   Muchir A, 2009, HUM MOL GENET, V18, P241, DOI 10.1093/hmg/ddn343
   Nguyeñ-Tran VTB, 2000, CELL, V102, P671, DOI 10.1016/S0092-8674(00)00089-1
   Nikolova V, 2004, J CLIN INVEST, V113, P357, DOI 10.1172/JCI200419448
   Östlund C, 2001, J CELL SCI, V114, P4435
   Quarta G, 2012, EUR HEART J, V33, P1128, DOI 10.1093/eurheartj/ehr451
   Quijano-Roy S, 2008, ANN NEUROL, V64, P177, DOI 10.1002/ana.21417
   Raharjo WH, 2001, J CELL SCI, V114, P4447
   Renaux A, 2018, NUCLEIC ACIDS RES, V46, P2699, DOI 10.1093/nar/gky092
   RIEMER D, 1993, EUR J CELL BIOL, V62, P214
   RIEMER D, 1995, J CELL SCI, V108, P3189
   Ruan J, 2014, ASIAN AUSTRAL J ANIM, V27, P123, DOI 10.5713/ajas.2013.13246
   Sakaki M, 2001, J BIOCHEM-TOKYO, V129, P321, DOI 10.1093/oxfordjournals.jbchem.a002860
   Schulze SR, 2009, PLOS ONE, V4, DOI 10.1371/journal.pone.0007564
   Schulze SR, 2005, GENETICS, V171, P185, DOI 10.1534/genetics.105.043208
   Schwartz C, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-01324-z
   Sébillon P, 2003, J MED GENET, V40, P560, DOI 10.1136/jmg.40.8.560
   Shen J, 2014, REPRODUCTION, V148, P479, DOI 10.1530/REP-14-0012
   Shi XJ, 2018, AMINO ACIDS, V50, P787, DOI 10.1007/s00726-018-2578-7
   Simon DN, 2010, NUCLEUS-PHILA, V1, P264, DOI 10.4161/nucl.1.3.11799
   Siu CW, 2012, AGING-US, V4, P803, DOI 10.18632/aging.100503
   Steele-Stallard HB, 2018, FRONT PHYSIOL, V9, DOI 10.3389/fphys.2018.01332
   STEWART C, 1987, CELL, V51, P383, DOI 10.1016/0092-8674(87)90634-9
   Stuurman N, 1999, EXP CELL RES, V248, P350, DOI 10.1006/excr.1999.4396
   Stuurman N, 1998, J STRUCT BIOL, V122, P42, DOI 10.1006/jsbi.1998.3987
   Sullivan T, 1999, J CELL BIOL, V147, P913, DOI 10.1083/jcb.147.5.913
   Swift J, 2013, SCIENCE, V341, DOI 10.1126/science.1240104
   Sylvius N, 2005, J MED GENET, V42, P639, DOI 10.1136/jmg.2004.023283
   Sylvius N, 2008, EXP CELL RES, V314, P2362, DOI 10.1016/j.yexcr.2008.04.017
   Taylor MRG, 2003, J AM COLL CARDIOL, V41, P771, DOI 10.1016/S0735-1097(02)02954-6
   Tazir M, 2004, BRAIN, V127, P154, DOI 10.1093/brain/awh021
   Tesson F, 2014, CARDIOL J, V21, P331, DOI 10.5603/CJ.a2014.0037
   TONTONOZ P, 1993, MOL CELL BIOL, V13, P4753, DOI 10.1128/MCB.13.8.4753
   Vadrot N, 2015, HUM MOL GENET, V24, P2096, DOI 10.1093/hmg/ddu728
   van Engelen BGM, 2005, NEUROLOGY, V64, P374, DOI 10.1212/01.WNL.0000149763.15180.00
   van Rijsingen IAW, 2013, EUR J HEART FAIL, V15, P376, DOI 10.1093/eurjhf/hfs191
   Verma AD, 2017, CELL BIOL INT, V41, P809, DOI 10.1002/cbin.10784
   Vigouroux C, 2000, DIABETES, V49, P1958, DOI 10.2337/diabetes.49.11.1958
   Vogel B, 2009, BIOCHEM BIOPH RES CO, V390, P516, DOI 10.1016/j.bbrc.2009.09.129
   Vytopil M, 2002, NEUROMUSCULAR DISORD, V12, P958, DOI 10.1016/S0960-8966(02)00178-5
   Wang Hu, 2005, Zhonghua Xinxueguanbing Zazhi, V33, P875
   Wang YX, 2006, HUM MOL GENET, V15, P2479, DOI 10.1093/hmg/ddl170
   Wiesel N, 2008, P NATL ACAD SCI USA, V105, P180, DOI 10.1073/pnas.0708974105
   Wojtanik KM, 2009, J LIPID RES, V50, P1068, DOI 10.1194/jlr.M800491-JLR200
   Wolf CM, 2008, J MOL CELL CARDIOL, V44, P293, DOI 10.1016/j.yjmcc.2007.11.008
   Wu W, 2011, CIRCULATION, V123, P53, DOI 10.1161/CIRCULATIONAHA.110.970673
   Wu W, 2010, BBA-MOL BASIS DIS, V1802, P632, DOI 10.1016/j.bbadis.2010.04.001
   Wu XY, 2010, J HUAZHONG U SCI-MED, V30, P103, DOI 10.1007/s11596-010-0119-z
   Yamanaka S, 2012, CELL STEM CELL, V10, P678, DOI 10.1016/j.stem.2012.05.005
   Yang SH, 2006, J CLIN INVEST, V116, P2115, DOI 10.1172/JCI28968
   YOKOYAMA C, 1993, CELL, V75, P187, DOI 10.1016/S0092-8674(05)80095-9
   Yoshihara M, 2017, STEM CELL REV REP, V13, P7, DOI 10.1007/s12015-016-9680-6
   Zhang YQ, 2008, J CELL BIOL, V182, P35, DOI 10.1083/jcb.200712124
   Zwerger M, 2013, HUM MOL GENET, V22, P2335, DOI 10.1093/hmg/ddt079
NR 143
TC 5
Z9 7
U1 0
U2 5
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
EI 2073-4409
J9 CELLS-BASEL
JI Cells
PD APR
PY 2019
VL 8
IS 4
AR 291
DI 10.3390/cells8040291
PG 27
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA HX3PN
UT WOS:000467304300005
PM 30934932
OA Green Submitted, gold, Green Published
DA 2025-04-10
ER

PT J
AU Broadwell, LJ
   Smallegan, MJ
   Rigby, KM
   Navarro-Arriola, JS
   Montgomery, RL
   Rinn, JL
   Leinwand, LA
AF Broadwell, Lindsey J.
   Smallegan, Michael J.
   Rigby, Kevin M.
   Navarro-Arriola, Jose S.
   Montgomery, Rusty L.
   Rinn, John L.
   Leinwand, Leslie A.
TI Myosin 7b is a regulatory long noncoding RNA (lncMYH7b) in the human
   heart
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID CHAIN GENE-EXPRESSION; VENTRICULAR HYPERTROPHY; MEF2; ADHESION;
   TRANSCRIPTION
AB Myosin heavy chain 7b (MYH7b) is an ancient member of the myosin heavy chain motor protein family that is expressed in striated muscles. In mammalian cardiac muscle, MYH7b RNA is expressed along with two other myosin heavy chains, beta-myosin heavy chain (beta-MyHC) and alpha-myosin heavy chain (alpha-MyHC). However, unlike beta-MyHC and alpha-MyHC, which are maintained in a careful balance at the protein level, the MYH7b locus does not produce a full-length protein in the heart due to a posttranscriptional exon-skipping mechanism that occurs in a tissue-specific manner. Whether this locus has a role in the heart beyond producing its intronic microRNA, miR-499, was unclear. Using cardiomyocytes derived from human induced pluripotent stem cells as a model system, we found that the noncoding exon-skipped RNA (lncMYH7b) affects the transcriptional landscape of human cardiomyocytes, independent of miR-499. Specifically, lncMYH7b regulates the ratio of beta-MyHC to alpha-MyHC, which is crucial for cardiac contractility. We also found that lncMYH7b regulates beat rate and sarcomere formation in cardiomyocytes. This regulation is likely achieved through control of a member of the TEA domain transcription factor family (TEAD3, which is known to regulate beta-MyHC). Therefore, we conclude that this ancient gene has been repurposed by alternative splicing to produce a regulatory long-noncoding RNA in the human heart that affects cardiac myosin composition.
C1 [Broadwell, Lindsey J.; Rinn, John L.] CU Boulder, Dept Biochem, Boulder, CO USA.
   [Broadwell, Lindsey J.; Smallegan, Michael J.; Rinn, John L.; Leinwand, Leslie A.] CU Boulder, BioFrontiers Inst, Boulder, CO 80309 USA.
   [Smallegan, Michael J.; Navarro-Arriola, Jose S.; Leinwand, Leslie A.] CU Boulder, Dept Mol Cellular & Dev Biol, Boulder, CO 80309 USA.
   [Rigby, Kevin M.; Montgomery, Rusty L.] MiRagen Therapeut Inc, Boulder, CO USA.
C3 University of Colorado System; University of Colorado Boulder;
   University of Colorado System; University of Colorado Boulder;
   University of Colorado System; University of Colorado Boulder
RP Leinwand, LA (corresponding author), CU Boulder, BioFrontiers Inst, Boulder, CO 80309 USA.; Leinwand, LA (corresponding author), CU Boulder, Dept Mol Cellular & Dev Biol, Boulder, CO 80309 USA.
EM Leslie.leinwand@colorado.edu
RI Rinn, John/JOZ-3940-2023; L, A/HZI-4043-2023
OI Broadwell, Lindsey/0000-0002-7559-3977; Rinn, John/0000-0002-7231-7539;
   LEINWAND, LESLIE/0000-0003-1470-4810
FU National Heart Lung and Blood Institute [F31HL147487] Funding Source:
   NIH RePORTER
CR Anderson DM, 2015, CELL, V160, P595, DOI 10.1016/j.cell.2015.01.009
   Ballarino M, 2018, EMBO J, V37, DOI 10.15252/embj.201899697
   Bell ML, 2010, MOL CELL BIOL, V30, P1937, DOI 10.1128/MCB.01370-09
   Cardoso AC, 2016, STRUCTURE, V24, P1301, DOI 10.1016/j.str.2016.06.003
   Chang CP, 2016, BBA-MOL CELL RES, V1863, P1767, DOI 10.1016/j.bbamcr.2016.03.005
   Chistiakov DA, 2016, J MOL CELL CARDIOL, V94, P107, DOI 10.1016/j.yjmcc.2016.03.015
   Desjardins PR, 2002, MOL BIOL EVOL, V19, P375, DOI 10.1093/oxfordjournals.molbev.a004093
   Ewels P. A., 2019, bioRxiv, DOI DOI 10.1101/610741
   Fenix AM, 2018, ELIFE, V7, DOI 10.7554/eLife.42144
   Han P, 2015, CELL CYCLE, V14, P787, DOI 10.1080/15384101.2015.1010963
   Haraksingh RR, 2014, BMC GENOMICS, V15, DOI 10.1186/1471-2164-15-1155
   Hasegawa K, 1997, CIRCULATION, V96, P3943
   Huebsch N, 2015, TISSUE ENG PART C-ME, V21, P467, DOI [10.1089/ten.tec.2014.0283, 10.1089/ten.TEC.2014.0283]
   Jin Y, 2011, TRENDS CARDIOVAS MED, V21, P1, DOI 10.1016/j.tcm.2011.12.009
   Karasseva N, 2003, MOL CELL BIOL, V23, P5143, DOI 10.1128/MCB.23.15.5143-5164.2003
   Kim NG, 2015, J CELL BIOL, V210, P503, DOI 10.1083/jcb.201501025
   Krenz M, 2004, J AM COLL CARDIOL, V44, P2390, DOI 10.1016/j.jacc.2004.09.044
   Lee LC, 2019, SCI REP-UK, V9, DOI 10.1038/s41598-018-38276-x
   Lian XJ, 2012, P NATL ACAD SCI USA, V109, pE1848, DOI 10.1073/pnas.1200250109
   Lowes BD, 2002, NEW ENGL J MED, V346, P1357, DOI 10.1056/NEJMoa012630
   Miyata S, 2000, CIRC RES, V86, P386, DOI 10.1161/01.RES.86.4.386
   Nadruz W, 2005, CARDIOVASC RES, V68, P87, DOI 10.1016/j.cardiores.2005.05.011
   Nag S, 2015, SCI ADV, V1, DOI 10.1126/sciadv.1500511
   Nakao K, 1997, J CLIN INVEST, V100, P2362, DOI 10.1172/JCI119776
   Nelson BR, 2016, SCIENCE, V351, P271, DOI 10.1126/science.aad4076
   Park JH, 2018, MOL CELLS, V41, P83, DOI 10.14348/molcells.2018.2242
   Peng X, 2008, P NATL ACAD SCI USA, V105, P6638, DOI 10.1073/pnas.0802319105
   Peter AK, 2019, J AM HEART ASSOC, V8, DOI 10.1161/JAHA.119.013318
   Potthoff MJ, 2007, DEVELOPMENT, V134, P4131, DOI 10.1242/dev.008367
   Rashid F, 2016, GENOM PROTEOM BIOINF, V14, P73, DOI 10.1016/j.gpb.2016.03.005
   Rossi AC, 2010, J PHYSIOL-LONDON, V588, P353, DOI 10.1113/jphysiol.2009.181008
   Rubio MD, 2011, J NEUROSCI, V31, P1448, DOI 10.1523/JNEUROSCI.3294-10.2011
   Rundell VLM, 2005, AM J PHYSIOL-HEART C, V288, pH896, DOI 10.1152/ajpheart.00407.2004
   Sadayappan S., 2010, PHYSIOLOGY, V119, P1253
   Sasaki S, 2014, PLOS ONE, V9
   Taniguchi K, 2009, J BIOL CHEM, V284, P29873, DOI 10.1074/jbc.M109.059303
   Torsoni AS, 2005, AM J PHYSIOL-HEART C, V289, pH1488, DOI 10.1152/ajpheart.00692.2004
   Trcek T, 2013, GENE DEV, V27, P541, DOI 10.1101/gad.209635.112
   Ushijima T, 2018, J BIOL CHEM, V293, P148, DOI 10.1074/jbc.M117.813931
   van Rooij E, 2009, DEV CELL, V17, P662, DOI 10.1016/j.devcel.2009.10.013
   Wales S, 2014, NUCLEIC ACIDS RES, V42, P11349, DOI 10.1093/nar/gku813
   Wang ZH, 2016, NAT MED, V22, P1131, DOI 10.1038/nm.4179
   Warren CM, 2003, ANAL BIOCHEM, V320, P149, DOI 10.1016/S0003-2697(03)00350-6
   Weiss A, 1996, ANNU REV CELL DEV BI, V12, P417, DOI 10.1146/annurev.cellbio.12.1.417
   Zhao HX, 2012, VIROLOGY, V424, P115, DOI 10.1016/j.virol.2011.12.006
NR 45
TC 15
Z9 17
U1 1
U2 2
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD JAN-JUN
PY 2021
VL 296
AR 100694
DI 10.1016/j.jbc.2021.100694
PG 12
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA TI5TQ
UT WOS:000672866400665
PM 33895132
OA Green Published, gold, Green Submitted
DA 2025-04-10
ER

PT J
AU Hochgreb-Hägele, T
   Koo, DES
   Das, NM
   Bronner, ME
AF Hochgreb-Haegele, Tatiana
   Koo, Daniel E. S.
   Das, Neha M.
   Bronner, Marianne E.
TI Zebrafish Stem/Progenitor Factor msi2b Exhibits Two Phases of
   Activity Mediated by Different Splice Variants
SO STEM CELLS
LA English
DT Article
DE Musashi; zebrafish; neuronal progenitor; differentiating
ID RNA-BINDING PROTEIN; STEM-CELL; SPINAL-CORD; MYELOID-LEUKEMIA;
   MESSENGER-RNA; TRANSLATIONAL REPRESSION; SUBVENTRICULAR ZONE;
   GENE-EXPRESSION; NERVOUS-SYSTEM; MAMMALIAN CNS
AB The Musashi (Msi) family of RNA-binding proteins is important in stem and differentiating cells in many species. Here, we present a zebrafish gene/protein trap line gt(msi2b-citrine)(ct57a) that expresses a Citrine fusion protein with endogenous Msi2b. Our results reveal two phases of Msi2b expression: ubiquitous expression in progenitor cells in the early embryo and later, tissue-specific expression in differentiating cells in the olfactory organ, pineal gland, and subpopulations of neurons in the central nervous system (CNS). Interestingly, this division between early and late phases is paralleled by differential expression of msi2b alternative splicing products. Whereas the full-length and long variant v3 Msi2b predominate at early stages, the later expression of variants in differentiating tissues appears to be tissue specific. Using the gt(msi2b-citrine)(ct57a), we characterized tissue-specific expression of Msi2b with cellular resolution in subsets of differentiating cells in the olfactory organ, pineal gland, CNS, and ventral neural tube. By performing transcription activator-like effectors nuclease-mediated biallelic genome editing or morpholino knockdown of Msi2b in zebrafish, our results show that early inactivation of Msi2b results in severe embryonic defects including hypertrophy of the ventricles and shortening of the body, consistent with an important role in cell proliferation and survival. Moreover, specific inactivation of Msi2b full-length indicates that this species is essential for the early role of Msi2b. This line provides a valuable tool both for live imaging of the endogenous Msi2b at subcellular resolution and manipulation of Msi2b-expressing cells. Stem Cells2014;32:558-571
C1 [Hochgreb-Haegele, Tatiana; Koo, Daniel E. S.; Das, Neha M.; Bronner, Marianne E.] CALTECH, Div Biol, Pasadena, CA 91125 USA.
C3 California Institute of Technology
RP Hochgreb-Hägele, T (corresponding author), CALTECH, Div Biol, 1200 E Calif Blvd,MC139-74, Pasadena, CA 91125 USA.
EM hochgreb@caltech.edu; mebronner@caltech.edu
OI Bronner, Marianne/0000-0003-4274-1862; Hochgreb-Hagele,
   Tatiana/0000-0002-7842-8416
FU Pew Latin American Fellowship in the Biomedical Sciences; California
   Institute for Regenerative Medicine [T2-00006]; NIH [HD037105, HG004071]
FX We thank Dr. Tatjana Sauka-Spengler for useful discussions, Drs. Marcos
   Simoes-Costa and Sujata Bhattacharyya for comments on the manuscript,
   and Drs. Le Trinh and Scott Fraser for helpful advice. We also thank
   Leigh Ann Fletcher and Kwok Su for fish care, Alice Plein and Ilana
   Solomon for technical support, Dr. Bruce Appel for sharing the
   Tg(olig2:dsred) line, Dr. Uwe Strahle for the Tg(ngn1:nRFP) line, and
   Dr. Yoshihiro Yoshihara, RIKEN BSI, and National Bioresource Project of
   Japan for the Tg(omp:RFG) and Tg(trpc2:Venus) lines. This work was
   supported by Pew Latin American Fellowship in the Biomedical Sciences
   and by California Institute for Regenerative Medicine Training Grant
   (T2-00006; to T.H.-H.). This work was supported by Grants HD037105 and
   HG004071 from NIH (to M.E.B).
CR Acloque H, 2008, METHOD CELL BIOL, V87, P169, DOI 10.1016/S0091-679X(08)00209-4
   Anderson RM, 2009, DEV BIOL, V334, P213, DOI 10.1016/j.ydbio.2009.07.017
   [Anonymous], 1995, ZEBRAFISH BOOK GUIDE
   Barbouti A, 2003, CANCER RES, V63, P1202
   Battelli C, 2006, MOL CELL NEUROSCI, V31, P85, DOI 10.1016/j.mcn.2005.09.003
   Bedell VM, 2012, NATURE, V491, P114, DOI 10.1038/nature11537
   BERNHARDT RR, 1992, J COMP NEUROL, V326, P263, DOI 10.1002/cne.903260208
   Blader P, 2003, MECH DEVELOP, V120, P211, DOI 10.1016/S0925-4773(02)00413-6
   Calarco JA, 2009, CELL, V138, P898, DOI 10.1016/j.cell.2009.06.012
   Carlson DF, 2012, P NATL ACAD SCI USA, V109, P17382, DOI 10.1073/pnas.1211446109
   Cermak T, 2011, NUCLEIC ACIDS RES, V39, DOI 10.1093/nar/gkr218
   Clarke RB, 2005, DEV BIOL, V277, P443, DOI 10.1016/j.ydbio.2004.07.044
   de Andrés-Aguayo L, 2011, BLOOD, V118, P554, DOI 10.1182/blood-2010-12-322081
   Doyle EL, 2012, NUCLEIC ACIDS RES, V40, pW117, DOI 10.1093/nar/gks608
   Dreyfuss G, 2002, NAT REV MOL CELL BIO, V3, P195, DOI 10.1038/nrm760
   Fukuda T, 2000, NEUROSCI RES, V38, P123, DOI 10.1016/S0168-0102(00)00163-2
   GOOD PJ, 1993, NUCLEIC ACIDS RES, V21, P999, DOI 10.1093/nar/21.4.999
   Gunter KM, 2011, IUBMB LIFE, V63, P678, DOI 10.1002/iub.499
   Hochgreb-Hägele T, 2013, DEV BIOL, V374, P1, DOI 10.1016/j.ydbio.2012.11.035
   Imai T, 2001, MOL CELL BIOL, V21, P3888, DOI 10.1128/MCB.21.12.3888-3900.2001
   Ito T, 2010, NATURE, V466, P765, DOI 10.1038/nature09171
   KAWAGUCHI Y, 1987, BRAIN RES, V416, P369, DOI 10.1016/0006-8993(87)90921-8
   Kawahara H, 2008, J CELL BIOL, V181, P639, DOI 10.1083/jcb.200708004
   Keyoung HM, 2001, NAT BIOTECHNOL, V19, P843, DOI 10.1038/nbt0901-843
   Kharas MG, 2010, NAT MED, V16, P903, DOI 10.1038/nm.2187
   Kim H, 2008, DEV DYNAM, V237, P2081, DOI 10.1002/dvdy.21620
   Lee CJ, 2003, BIOL PSYCHIAT, V54, P771, DOI 10.1016/S0006-3223(03)00375-5
   LEVISON SW, 1993, NEURON, V10, P201, DOI 10.1016/0896-6273(93)90311-E
   Lewis KE, 2004, DEVELOPMENT, V131, P891, DOI 10.1242/dev.00981
   Lewis KE, 2003, PROG NEUROBIOL, V69, P419, DOI 10.1016/S0301-0082(03)00052-2
   Li Q, 2007, NAT REV NEUROSCI, V8, P819, DOI 10.1038/nrn2237
   LOIS C, 1993, P NATL ACAD SCI USA, V90, P2074, DOI 10.1073/pnas.90.5.2074
   Lu JG, 2010, MOL GENET GENOMICS, V283, P531, DOI 10.1007/s00438-010-0538-3
   Lunde BM, 2007, NAT REV MOL CELL BIO, V8, P479, DOI 10.1038/nrm2178
   Moore FE, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0037877
   NAKAMURA M, 1994, NEURON, V13, P67, DOI 10.1016/0896-6273(94)90460-X
   Okabe M, 2001, NATURE, V411, P94, DOI 10.1038/35075094
   Okano H, 2002, J CELL SCI, V115, P1355
   Park HC, 2004, DEVELOPMENT, V131, P5959, DOI 10.1242/dev.01456
   Potten CS, 2003, DIFFERENTIATION, V71, P28, DOI 10.1046/j.1432-0436.2003.700603.x
   Sakakibara S, 2002, P NATL ACAD SCI USA, V99, P15194, DOI 10.1073/pnas.232087499
   Sakakibara S, 2001, J NEUROSCI, V21, P8091, DOI 10.1523/JNEUROSCI.21-20-08091.2001
   Sakakibara S, 1996, DEV BIOL, V176, P230, DOI 10.1006/dbio.1996.0130
   Sakakibara S, 1997, J NEUROSCI, V17, P8300
   Sampath P, 2008, CELL STEM CELL, V2, P448, DOI 10.1016/j.stem.2008.03.013
   Sato Y, 2005, J NEUROSCI, V25, P4889, DOI 10.1523/JNEUROSCI.0679-05.2005
   Sauka-Spengler T, 2007, DEV CELL, V13, P405, DOI 10.1016/j.devcel.2007.08.005
   Schwanhäusser B, 2011, NATURE, V473, P337, DOI 10.1038/nature10098
   Shibata S, 2012, BRAIN RES, V1462, P162, DOI 10.1016/j.brainres.2012.01.068
   Siddall NA, 2006, P NATL ACAD SCI USA, V103, P8402, DOI 10.1073/pnas.0600906103
   Sonenberg N, 2009, CELL, V136, P731, DOI 10.1016/j.cell.2009.01.042
   Summerton JE, 2007, CURR TOP MED CHEM, V7, P651, DOI 10.2174/156802607780487740
   Szabat M, 2011, CELL DEATH DIS, V2, DOI 10.1038/cddis.2011.119
   Trinh LA, 2011, GENE DEV, V25, P2306, DOI 10.1101/gad.174037.111
   Wuebben EL, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0034827
   Wyart C, 2009, NATURE, V461, P407, DOI 10.1038/nature08323
NR 56
TC 6
Z9 7
U1 0
U2 9
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 1066-5099
EI 1549-4918
J9 STEM CELLS
JI Stem Cells
PD FEB
PY 2014
VL 32
IS 2
BP 558
EP 571
DI 10.1002/stem.1583
PG 14
WC Cell & Tissue Engineering; Biotechnology & Applied Microbiology;
   Oncology; Cell Biology; Hematology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Biotechnology & Applied Microbiology; Oncology; Hematology
GA 304JE
UT WOS:000330742100020
PM 24420905
OA Green Accepted, Bronze
DA 2025-04-10
ER

PT J
AU Thomsen, C
   Pekhletski, R
   Haldeman, B
   Gilbert, TA
   OHara, P
   Hampson, DR
AF Thomsen, C
   Pekhletski, R
   Haldeman, B
   Gilbert, TA
   OHara, P
   Hampson, DR
TI Cloning and characterization of a metabotropic glutamate receptor,
   mGluR4b
SO NEUROPHARMACOLOGY
LA English
DT Article
DE metabotropic glutamate receptor; mGluR4a; mGluR4b;
   [H-3]-L-2-amino-4-phosphonobutyrate binding; baculovirus expression
   system
ID ALTERNATIVELY SPLICED FORMS; RAT-BRAIN; SIGNAL TRANSDUCTION;
   GLOBAL-ISCHEMIA; PERFORANT PATH; EXPRESSION; SUBUNIT; ANTIBODIES;
   PATTERNS; FAMILY
AB An alternative spliced variant of metabotropic glutamate receptor subtype mGluR4a, termed mGluR4b was isolated from a rat cDNA library. Subtype mGluR4b was identical to the previously described mGluR4a, except for the last 64 amino acids in the C-terminal region which were replaced by 135 new amino acids in mGluR4b. Recombinant baculoviruses coding for mGluR4a and mGluR4b were expressed in Spodoptera frugiperda, Sf-9, insect cells and characterized pharmacologically by measuring [H-3]-L-2-amino-4-phosphonobutyrate ([H-3]-L-AP4) binding and second messenger formation. [H-3]-L-AP4 binding to membranes prepared from Sf-9 cells expressing mGluR4a and mGluR4b revealed respective affinities (K-d) of 480 and 360 nM and maximal binding densities (B-max) of 4.2 and 0.8 pmol/mg protein. The ligand selectivity of mGluR4a and mGluR4b was similar: L-AP4 > L-serine-O-phosphate > L-glutamate > L-2-amino 2-methyl-4-phosphonobutyrate > (1S,3R)-1-aminocyclopentane-1,3-dicarboxylate greater than or equal to quisqualate. A decrease in the affinity of [H-3]-L-AP4 was observed in the presence of 0.1 mM guanosine-5'-O-(3-thio)trisphosphate-y-S, indicating that mGluR4a and mGluR4b were functionally coupled to G-proteins in Sf-9 cells. Agonists of mGluR4 caused a minor decrease in forskolin-induced cAMP formation in Sf-9 cells expressing either mGluR4a or mGluR4b, suggesting that both receptors are coupled to adenylate cyclase in an inhibitory manner. Thus, mGluR4a and mGluR4b share a common signal transduction pathway and pharmacology when expressed in Sf-9 insect cells. (C) 1997 Elsevier Science Ltd.
C1 UNIV TORONTO,FAC PHARM,TORONTO,ON M5S 1A1,CANADA.
   ZYMOGENET INC,SEATTLE,WA 98105.
C3 University of Toronto; Zymogenet Inc.
RP Thomsen, C (corresponding author), NOVO NORDISK AS,DEPT MOL PHARMACOL,NOVO NORDISK PK,DK-2760 MALOV,DENMARK.
CR ABE T, 1992, J BIOL CHEM, V267, P13361
   BENVENISTE H, 1991, CEREBROVAS BRAIN MET, V3, P213
   BUSHELL TJ, 1995, NEUROPHARMACOLOGY, V34, P239, DOI 10.1016/0028-3908(95)00012-U
   CATANIA MV, 1994, MOL PHARMACOL, V45, P626
   Eriksen L, 1995, BRIT J PHARMACOL, V116, P3279, DOI 10.1111/j.1476-5381.1995.tb15136.x
   Gomeza J, 1996, J BIOL CHEM, V271, P2199, DOI 10.1074/jbc.271.4.2199
   GUDERMANN T, 1995, J MOL MED, V73, P51, DOI 10.1007/BF00270578
   HAMPSON DR, 1994, NEUROSCIENCE, V60, P325, DOI 10.1016/0306-4522(94)90246-1
   HAMPSON DR, 1989, J BIOL CHEM, V264, P13329
   HOUAMED KM, 1991, SCIENCE, V252, P1318, DOI 10.1126/science.1656524
   IVERSEN L, 1994, J NEUROCHEM, V63, P625
   JOLY C, 1995, J NEUROSCI, V15, P3970
   KLUNK WE, 1991, MOL CHEM NEUROPATHOL, V15, P51, DOI 10.1007/BF03161056
   KOERNER JF, 1981, BRAIN RES, V216, P192, DOI 10.1016/0006-8993(81)91288-9
   Laurie DJ, 1996, EUR J PHARMACOL, V296, pR1, DOI 10.1016/0014-2999(95)00868-3
   MINAKAMI R, 1994, BIOCHEM BIOPH RES CO, V199, P1136, DOI 10.1006/bbrc.1994.1349
   NOMURA A, 1994, CELL, V77, P361, DOI 10.1016/0092-8674(94)90151-1
   OHARA PJ, 1993, NEURON, V11, P41, DOI 10.1016/0896-6273(93)90269-W
   Pekhletski R, 1996, J NEUROSCI, V16, P6364
   PELLEGRINIGIAMPIETRO DE, 1992, P NATL ACAD SCI USA, V89, P10499, DOI 10.1073/pnas.89.21.10499
   PICKERING DS, 1993, J NEUROCHEM, V61, P85, DOI 10.1111/j.1471-4159.1993.tb03540.x
   PIN JP, 1995, NEUROPHARMACOLOGY, V34, P1, DOI 10.1016/0028-3908(94)00129-G
   PIN JP, 1994, EMBO J, V13, P342, DOI 10.1002/j.1460-2075.1994.tb06267.x
   PIN JP, 1992, P NATL ACAD SCI USA, V89, P10331, DOI 10.1073/pnas.89.21.10331
   ROSS SM, 1994, NEUROSCI LETT, V173, P139, DOI 10.1016/0304-3940(94)90168-6
   SIMONCINI L, 1993, BIOPHYS J, V64, pA84
   SUZDAK PD, 1994, METABOTROPIC GLUTAMA, P1
   TANABE Y, 1992, NEURON, V8, P169, DOI 10.1016/0896-6273(92)90118-W
   TANABE Y, 1993, J NEUROSCI, V13, P1372
   THOMSEN C, 1992, EUR J PHARM-MOLEC PH, V227, P361, DOI 10.1016/0922-4106(92)90018-Q
   WENTHOLD RJ, 1994, J BIOL CHEM, V269, P1332
NR 31
TC 38
Z9 46
U1 0
U2 0
PU PERGAMON-ELSEVIER SCIENCE LTD
PI OXFORD
PA THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD, ENGLAND OX5 1GB
SN 0028-3908
J9 NEUROPHARMACOLOGY
JI Neuropharmacology
PD JAN
PY 1997
VL 36
IS 1
BP 21
EP 30
DI 10.1016/S0028-3908(96)00153-0
PG 10
WC Neurosciences; Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology; Pharmacology & Pharmacy
GA WN039
UT WOS:A1997WN03900003
PM 9144638
DA 2025-04-10
ER

PT J
AU Urbanek, MO
   Krzyzosiak, WJ
AF Urbanek, Martyna O.
   Krzyzosiak, Wlodzimierz J.
TI Discriminating RNA variants with single-molecule allele-specific FISH
SO MUTATION RESEARCH-REVIEWS IN MUTATION RESEARCH
LA English
DT Review
DE Allele-specific; Point mutation; Splicing; Fused gene; Fluorescence in
   situ hybridization; Single molecule detection
ID IN-SITU HYBRIDIZATION; ROLLING-CIRCLE AMPLIFICATION; GENE-EXPRESSION;
   PADLOCK PROBES; NONCODING RNAS; CAG REPEATS; CELLS; H19; TRANSCRIPTS;
   REVEALS
AB DNA mutations of various types often affect the cellular localization and function of gene products. The role of mutant transcripts in the pathogenesis of human disease is increasingly recognized. Among the pathogenic RNA variants are transcripts with single nucleotide substitutions, small insertions or deletions, aberrantly or alternatively spliced transcripts and RNAs derived from fused genes. To discriminate among transcripts, particularly those of low abundance, showing small or large sequence differences, a highly sensitive and specific RNA imaging method is required. The method that fulfills these criteria is single-molecule fluorescence in situ hybridization (smFISH) combined with probes discriminating among RNA variants. With this method, RNA transcripts produced from individual alleles can be imaged, and differences in their transcription, processing, cellular localization and decay can be revealed. In addition to its applications for studying physiological processes involving RNA variants, smFISH offers several advantages for disease related mutation research. Further development of allele-specific microscopic methods may broaden group of RNA variants analyzed, including RNAs with expanded repeat tract, different variants of 3 ' UTR, RNAs differing in length of polyA tract or transcripts produced from alternative start codons. Moreover, first attempts for allele-specific RNA live imaging were made adding time-lapse analysis. In this review, we discuss important aspects of the variant-specific smFISH methodology and present examples of its applications in deciphering RNA-mediated pathogenic mechanisms in a variety of human diseases, including cancer, neurological, immunological and cardiovascular diseases. (C) 2016 Elsevier B.V. All rights reserved.
C1 [Urbanek, Martyna O.; Krzyzosiak, Wlodzimierz J.] Polish Acad Sci, Inst Bioorgan Chem, Dept Mol Biomed, Ul Noskowskiego 12-14, PL-61704 Poznan, Poland.
C3 Polish Academy of Sciences; Institute of Bioorganic Chemistry of the
   Polish Academy of Sciences
RP Krzyzosiak, WJ (corresponding author), Polish Acad Sci, Inst Bioorgan Chem, Dept Mol Biomed, Ul Noskowskiego 12-14, PL-61704 Poznan, Poland.
EM wlodkrzy@ibch.poznan.pl
RI Urbanek-Trzeciak, Martyna/AAB-7228-2020
OI Urbanek-Trzeciak, Martyna/0000-0002-2397-0603
FU National Science Center [2012/06/A/NZ1/00094, 2015/19/B/NZ2/02453];
   Ministry of Science and Higher Education of the Republic of Poland,
   under the Leading National Research Centre (KNOW)
FX This work was supported by the National Science Center
   (2012/06/A/NZ1/00094 and 2015/19/B/NZ2/02453 to Wlodzimierz J.
   Krzyzosiak); and the Ministry of Science and Higher Education of the
   Republic of Poland, from the quality-promoting subsidy, under the
   Leading National Research Centre (KNOW) program for the years 2014-2019.
CR Adam GIR, 1996, DEVELOPMENT, V122, P839
   Banér J, 2003, NUCLEIC ACIDS RES, V31, DOI 10.1093/nar/gng104
   Blanco AM, 2009, NUCLEIC ACIDS RES, V37, DOI 10.1093/nar/gkp551
   Bonifazi E, 2006, CLIN CHEM, V52, P319, DOI 10.1373/clinchem.2005.056283
   Buckley PT, 2014, WIRES RNA, V5, P223, DOI 10.1002/wrna.1203
   Buxbaum AR, 2014, SCIENCE, V343, P419, DOI 10.1126/science.1242939
   Chen KN, 2015, WORLD J STEM CELLS, V7, P1, DOI 10.4252/wjsc.v7.i1.1
   Choi KD, 2013, NEUROL SCI, V34, P1629, DOI 10.1007/s10072-013-1298-8
   Chou YY, 2013, PLOS PATHOG, V9, DOI 10.1371/journal.ppat.1003358
   Constância M, 2002, NATURE, V417, P945, DOI 10.1038/nature00819
   Dahan L, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0072389
   de Mezer M, 2011, NUCLEIC ACIDS RES, V39, P3852, DOI 10.1093/nar/gkq1323
   Deng RJ, 2014, ANGEW CHEM INT EDIT, V53, P2389, DOI 10.1002/anie.201309388
   Donley N, 2015, PLOS GENET, V11, DOI 10.1371/journal.pgen.1004923
   Du HQ, 2010, NAT STRUCT MOL BIOL, V17, P187, DOI 10.1038/nsmb.1720
   Eckersley-Maslin MA, 2014, DEV CELL, V28, P351, DOI 10.1016/j.devcel.2014.01.017
   Edwards PAW, 2010, J PATHOL, V220, P244, DOI 10.1002/path.2632
   Faustino NA, 2003, GENE DEV, V17, P419, DOI 10.1101/gad.1048803
   Femino A, 1998, SCIENCE, V280, P585, DOI 10.1126/science.280.5363.585
   Galka-Marciniak P, 2012, BIOL CHEM, V393, P1299, DOI 10.1515/hsz-2012-0218
   Garcia SMDA, 2014, NAT STRUCT MOL BIOL, V21, P712, DOI 10.1038/nsmb.2858
   Ginart P, 2016, GENE DEV, V30, P567, DOI 10.1101/gad.275958.115
   Hacisuleyman E, 2014, NAT STRUCT MOL BIOL, V21, P198, DOI 10.1038/nsmb.2764
   Hall RD, 2014, CANCER CONTROL, V21, P221, DOI 10.1177/107327481402100307
   Hansen CH, 2013, NAT METHODS, V10, P869, DOI [10.1038/NMETH.2601, 10.1038/nmeth.2601]
   Hendrix DK, 2005, Q REV BIOPHYS, V38, P221, DOI 10.1017/S0033583506004215
   Herzing LBK, 2002, HUM MOL GENET, V11, P1707, DOI 10.1093/hmg/11.15.1707
   Hocine S, 2013, NAT METHODS, V10, P119, DOI 10.1038/nmeth.2305
   Holt I, 2010, TRANSL NEUROSCI, V1, P195, DOI 10.2478/v10134-010-0029-4
   Jonstrup SP, 2006, RNA, V12, P1747, DOI 10.1261/rna.110706
   Kalo A, 2013, METHODS MOL BIOL, V1042, P87, DOI 10.1007/978-1-62703-526-2_7
   Larsson C, 2004, NAT METHODS, V1, P227, DOI 10.1038/NMETH723
   Larsson C, 2010, NAT METHODS, V7, P395, DOI [10.1038/NMETH.1448, 10.1038/nmeth.1448]
   Levesque MJ, 2013, NAT METHODS, V10, P865, DOI [10.1038/NMETH.2589, 10.1038/nmeth.2589]
   Levsky JM, 2003, J CELL SCI, V116, P2833, DOI 10.1242/jcs.00633
   Li YM, 1998, J BIOL CHEM, V273, P28247, DOI 10.1074/jbc.273.43.28247
   Lin WL, 1999, MECH DEVELOP, V82, P195, DOI 10.1016/S0925-4773(99)00009-X
   Lobashevsky AL, 2002, HUM IMMUNOL, V63, P108, DOI 10.1016/S0198-8859(01)00364-0
   Mankodi A, 2005, CIRC RES, V97, P1152, DOI 10.1161/01.RES.0000193598.89753.e3
   Markey FB, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0093488
   Marx J, 2005, SCIENCE, V310, P603
   Mykowska A, 2011, NUCLEIC ACIDS RES, V39, P8938, DOI 10.1093/nar/gkr608
   Nakamori M, 2013, ANN NEUROL, V74, P862, DOI 10.1002/ana.23992
   Nelles DA, 2016, CELL, V165, P488, DOI 10.1016/j.cell.2016.02.054
   Nilsson M, 2006, HISTOCHEM CELL BIOL, V126, P159, DOI 10.1007/s00418-006-0213-2
   Ochiai H, 2014, SCI REP-UK, V4, DOI 10.1038/srep07125
   Ohlsson R, 1999, CANCER RES, V59, P3889
   Ohlsson R, 1999, DEV GENES EVOL, V209, P113, DOI 10.1007/s004270050233
   Ohlsson R, 2001, METH MOL B, V181, P153
   Ohno M, 2001, GENES CELLS, V6, P249, DOI 10.1046/j.1365-2443.2001.00417.x
   Orjalo AV, 2016, METHODS MOL BIOL, V1402, P119, DOI 10.1007/978-1-4939-3378-5_10
   Perrin BJ, 2010, CYTOSKELETON, V67, P630, DOI 10.1002/cm.20475
   Rogan PK, 1998, HUM MUTAT, V12, P153, DOI 10.1002/(SICI)1098-1004(1998)12:3<153::AID-HUMU3>3.0.CO;2-I
   Sellier C, 2010, EMBO J, V29, P1248, DOI 10.1038/emboj.2010.21
   Semrau S, 2014, CELL REP, V6, P18, DOI 10.1016/j.celrep.2013.12.002
   Shaffer SM, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0075120
   Shav-Tal Y, 2016, METHODS, V98, P1, DOI 10.1016/j.ymeth.2016.02.011
   Shi M, 2015, CELL DISCOV, V1, DOI 10.1038/celldisc.2015.1
   Stavreva DA, 2012, BBA-GENE REGUL MECH, V1819, P657, DOI 10.1016/j.bbagrm.2012.03.004
   Svensson K, 1998, DEVELOPMENT, V125, P61
   Takizawa T, 2008, GENE DEV, V22, P489, DOI 10.1101/gad.1634608
   TANEJA KL, 1995, J CELL BIOL, V128, P995, DOI 10.1083/jcb.128.6.995
   Tassone Flora, 2004, RNA Biol, V1, P103, DOI 10.4161/rna.1.2.1035
   Thomsen R, 2005, RNA, V11, P1745, DOI 10.1261/rna.2139705
   Tomlins SA, 2005, SCIENCE, V310, P644, DOI 10.1126/science.1117679
   Urbanek MO, 2015, INT J MOL SCI, V16, P13259, DOI 10.3390/ijms160613259
   Urbanek MO, 2014, RNA BIOL, V11, P1083, DOI 10.4161/rna.35506
   Vargas DY, 2011, CELL, V147, P1054, DOI 10.1016/j.cell.2011.10.024
   Waks Z, 2011, MOL SYST BIOL, V7, DOI 10.1038/msb.2011.32
   Weibrecht I, 2013, NAT PROTOC, V8, P355, DOI 10.1038/nprot.2013.006
   Xia GB, 2015, STEM CELLS, V33, P1829, DOI 10.1002/stem.1970
   Xia GB, 2015, HISTOCHEM CELL BIOL, V143, P557, DOI 10.1007/s00418-015-1315-5
   Xu Q, 2008, J NEUROSCI, V28, P1452, DOI 10.1523/JNEUROSCI.3253-07.2008
   Yang L, 2015, WIRES RNA, V6, P651, DOI 10.1002/wrna.1307
   Yun K, 1998, J PATHOL, V185, P91, DOI 10.1002/(SICI)1096-9896(199805)185:1<91::AID-PATH44>3.0.CO;2-K
   Zhang B, 2014, MOL CELL BIOL, V34, P2318, DOI 10.1128/MCB.01673-13
   Zhang DY, 2012, NAT CHEM, V4, P208, DOI [10.1038/NCHEM.1246, 10.1038/nchem.1246]
   Zhang K, 2009, NAT METHODS, V6, P613, DOI 10.1038/nmeth.1357
NR 78
TC 8
Z9 8
U1 0
U2 25
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
SN 1383-5742
EI 1388-2139
J9 MUTAT RES-REV MUTAT
JI Mutat. Res.-Rev. Mutat. Res.
PD JUL-SEP
PY 2017
VL 773
BP 230
EP 241
DI 10.1016/j.mrrev.2016.09.003
PG 12
WC Biotechnology & Applied Microbiology; Genetics & Heredity; Toxicology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biotechnology & Applied Microbiology; Genetics & Heredity; Toxicology
GA FJ0DI
UT WOS:000412378300015
PM 28927531
DA 2025-04-10
ER

PT J
AU Maroney, SA
   Ellery, PE
   Wood, JP
   Ferrel, JP
   Martinez, ND
   Mast, AE
AF Maroney, S. A.
   Ellery, P. E.
   Wood, J. P.
   Ferrel, J. P.
   Martinez, N. D.
   Mast, A. E.
TI Comparison of the inhibitory activities of human tissue factor pathway
   inhibitor (TFPI)α and TFPIβ
SO JOURNAL OF THROMBOSIS AND HAEMOSTASIS
LA English
DT Article
DE alternative splicing; hemophilia; migration; TFPI; tissue factor
ID HUMAN ENDOTHELIAL-CELLS; FACTOR VIIA; UP-REGULATION; FACTOR XA;
   COAGULATION; EXPRESSION; HEPARIN; SURFACE; RELEASE; ANTICOAGULANT
AB Background Tissue factor pathway inhibitor (TFPI) is an alternatively spliced protein with two isoforms, TFPI and TFPI, which differ in their C-terminal structure and cellular localization. Detailed characterization of their inhibitory activity is needed to define potentially unique inhibitory roles in tissue factor (TF)-mediated thrombotic and inflammatory disease, and to understand how pharmaceuticals targeted to different structural regions of the TFPI isoforms alter hemostasis in hemophilia patients. Methods The TF inhibitory activity of TFPI localized to the surface of CHO cells was compared with that of soluble TFPI by the use of invitro and invivo assays. Results In TFfactor VIIa-mediated FXa generation assays, TFPI was a slightly better inhibitor than TFPI, which was approximately three-fold better than TFPI-160, a soluble, altered form of TFPI similar to TFPI. In direct FXa inhibitory assays, TFPI had an IC50 2.5-fold lower than that of TFPI and 56-fold lower than that of TFPI-160. TFPI inhibited TF-mediated CHO cell migration though Matrigel, whereas TFPI and TFPI-160 were poor inhibitors, demonstrating that TFPI effectively blocks TF-initiated signaling events during cellular migration through matrices that are not permeable to soluble forms of TFPI. Furthermore, TFPI inhibited TF-dependent CHO cell infiltration into lung tissue following tail vein injection into SCID mice, and blocked the development of consumptive coagulopathy. Conclusions TFPI is a slightly better inhibitor of TF procoagulant activity than TFPI. As a surface-associated protein, TFPI is a much better inhibitor of TF-mediated cellular migration than soluble TFPI, and may specifically act in the inhibition of TF-mediated signaling events on inflamed endothelium and/or monocytes.
C1 [Maroney, S. A.; Ellery, P. E.; Wood, J. P.; Ferrel, J. P.; Martinez, N. D.; Mast, A. E.] Blood Ctr Wisconsin, Blood Res Inst, Milwaukee, WI USA.
   [Mast, A. E.] Med Coll Wisconsin, Dept Cell Biol Neurobiol & Anat, Milwaukee, WI 53226 USA.
C3 Versiti Blood Center of Wisconsin; Medical College of Wisconsin
RP Mast, AE (corresponding author), Blood Ctr Wisconsin, Blood Res Inst, POB 2178, Milwaukee, WI USA.
EM alan.mast@bcw.edu
OI Ellery, Paul/0000-0002-3124-8397
FU NHLBI [HL068835, HL091469, HL007209]; Novo Nordisk
FX This work was supported by NHLBI grants HL068835 to A. E. Mast and
   HL091469 to S. A. Maroney. J. P. Wood gratefully acknowledges training
   grant support from NHLBI grant HL007209. The content is solely the
   responsibility of the authors, and does not necessarily represent the
   official views of the National Institutes of Health. Further support was
   provided through a research grant from Novo Nordisk to A. E. Mast. The
   other authors state that they have no conflict of interest.
CR Abraham E, 2003, JAMA-J AM MED ASSOC, V290, P238, DOI 10.1001/jama.290.2.238
   Ahamed J, 2005, BLOOD, V105, P2384, DOI 10.1182/blood-2004-09-3422
   Baugh RJ, 1998, J BIOL CHEM, V273, P4378, DOI 10.1074/jbc.273.8.4378
   Bromberg ME, 2001, THROMB HAEMOSTASIS, V86, P1210
   BROZE GJ, 1994, BLOOD COAGUL FIBRIN, V5, P551
   Chang JY, 1999, THROMB HAEMOSTASIS, V81, P45
   Chen HH, 2005, BLOOD, V105, P3902, DOI 10.1182/blood-2004-11-4435
   Contrino J, 1996, NAT MED, V2, P209, DOI 10.1038/nm0296-209
   DRAKE TA, 1989, AM J PATHOL, V134, P1087
   Fischer EG, 1999, J CLIN INVEST, V104, P1213, DOI 10.1172/JCI7750
   Girard TJ, 2012, BLOOD, V119, P1256, DOI 10.1182/blood-2011-10-388512
   GIRARD TJ, 1989, NATURE, V338, P518, DOI 10.1038/338518a0
   Hackeng TM, 2006, P NATL ACAD SCI USA, V103, P3106, DOI 10.1073/pnas.0504240103
   Hansen JB, 2000, THROMB HAEMOSTASIS, V83, P937
   Hilden I, 2012, BLOOD, V119, P5871, DOI 10.1182/blood-2012-01-401620
   Hjortoe GM, 2004, BLOOD, V103, P3029, DOI 10.1182/blood-2003-10-3417
   Hu ZW, 2001, P NATL ACAD SCI USA, V98, P12180, DOI 10.1073/pnas.201420298
   Hughes CS, 2010, PROTEOMICS, V10, P1886, DOI 10.1002/pmic.200900758
   Laterre PF, 2008, CRIT CARE, V12, DOI 10.1186/cc7027
   LINDHOUT T, 1994, BIOCHEM J, V297, P131, DOI 10.1042/bj2970131
   Lockett JM, 2002, BIOCHEMISTRY-US, V41, P4989, DOI 10.1021/bi016058n
   Lupu C, 2005, J BIOL CHEM, V280, P22308, DOI 10.1074/jbc.M503333200
   Lupu C, 1999, ARTERIOSCL THROM VAS, V19, P2251, DOI 10.1161/01.ATV.19.9.2251
   LUPU C, 1995, ARTERIOSCL THROM VAS, V15, P2055, DOI 10.1161/01.ATV.15.11.2055
   Maroney SA, 2009, J THROMB HAEMOST, V7, P1106, DOI 10.1111/j.1538-7836.2009.03454.x
   Maroney SA, 2007, BLOOD, V109, P1931, DOI 10.1182/blood-2006-07-037283
   Maroney SA, 2012, BIOCHEM J, V443, P259, DOI 10.1042/BJ20111994
   Maroney SA, 2012, P NATL ACAD SCI USA, V109, P3927, DOI 10.1073/pnas.1119858109
   Maroney SA, 2011, ARTERIOSCL THROM VAS, V31, P821, DOI 10.1161/ATVBAHA.110.220293
   Mast AE, 2002, ARTERIOSCL THROM VAS, V22, P2099, DOI 10.1161/01.ATV.0000042456.84190.F0
   Mueller BM, 1998, J CLIN INVEST, V101, P1372, DOI 10.1172/JCI930
   NOVOTNY WF, 1991, BLOOD, V78, P394
   Pedersen B, 2005, BLOOD, V105, P2777, DOI 10.1182/blood-2004-09-3724
   Pendurthi UR, 1997, P NATL ACAD SCI USA, V94, P12598, DOI 10.1073/pnas.94.23.12598
   Piro O, 2005, J THROMB HAEMOST, V3, P2677, DOI 10.1111/j.1538-7836.2005.01636.x
   Prasad S, 2008, BLOOD, V111, P672, DOI 10.1182/blood-2007-07-098913
   RATNOFF OD, 1962, BIOCHEMISTRY-US, V1, P677, DOI 10.1021/bi00910a022
   SANDSET PM, 1988, THROMB RES, V50, P803, DOI 10.1016/0049-3848(88)90340-4
   Schuepbach RA, 2011, BLOOD, V117, P6338, DOI 10.1182/blood-2010-10-316257
   Sevinsky JR, 1996, J CELL BIOL, V133, P293, DOI 10.1083/jcb.133.2.293
   Stavik B, 2011, BMC CANCER, V11, DOI 10.1186/1471-2407-11-357
   Tang H, 2007, AM J PATHOL, V171, P1066, DOI 10.2353/ajpath.2007.070104
   van den Boogaard FE, 2011, J THROMB HAEMOST, V9, P122, DOI 10.1111/j.1538-7836.2010.04089.x
   Waters EK, 2011, BLOOD, V117, P5514, DOI 10.1182/blood-2010-10-311936
   WESSELSCHMIDT R, 1992, BLOOD, V79, P2004
   Zhang J, 2003, CIRCULATION, V108, P623, DOI 10.1161/01.CIR.0000078642.45127.7B
NR 46
TC 44
Z9 46
U1 0
U2 14
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 1538-7933
EI 1538-7836
J9 J THROMB HAEMOST
JI J. Thromb. Haemost.
PD MAY
PY 2013
VL 11
IS 5
BP 911
EP 918
DI 10.1111/jth.12188
PG 8
WC Hematology; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Hematology; Cardiovascular System & Cardiology
GA 145JQ
UT WOS:000319011900014
PM 23480518
OA Bronze, Green Accepted
DA 2025-04-10
ER

PT J
AU Cano-Corres, R
   Candás-Estébanez, B
   Padró-Miquel, A
   Fanlo-Maresma, M
   Pintó, X
   Alía-Ramos, P
AF Cano-Corres, Ruth
   Candas-Estebanez, Beatriz
   Padro-Miquel, Ariadna
   Fanlo-Maresma, Marta
   Pinto, Xavier
   Alia-Ramos, Pedro
TI Influence of 6 genetic variants on the efficacy of statins in patients
   with dyslipidemia
SO JOURNAL OF CLINICAL LABORATORY ANALYSIS
LA English
DT Article
DE dyslipidemia; genetic variants; non-HDL cholesterol; statins; total
   cholesterol
ID CORONARY-HEART-DISEASE; CARDIOVASCULAR-DISEASE; APOLIPOPROTEIN-E;
   INTERVENTION TRIAL; PRIMARY PREVENTION; CHOLESTEROL LEVELS;
   LDL-CHOLESTEROL; LIPID-LEVELS; RISK-FACTOR; ATORVASTATIN
AB BackgroundMethodsPatients with dyslipidemia are often treated with statins to reduce lipids and hence cardiovascular risk, but treatment response is variable, partly due to genetic factors.
   We studied the influence of 6 gene variants (APOE c.526C>T (APOE2), APOE c.388T>C (APOE4), SLCO1B1 c.521T>C, CYP3A4 c.-392G>A, HMGCR c.1564-106A>G, and LPA c.3947+467T>C) on statin efficacy assessing 2 indicators: the percent reduction in total cholesterol (TC) and non-HDL cholesterol (non-HDL), as well as the achievement of therapeutic goals. The study was performed in a group of patients (n=100) without previous pharmacological treatment. Multiple regression models were used to calculate the percentage of explanation in response variability added by every variant to a basal model constructed with significant nongenetic control variables.
   ResultsConclusionsThe most influential variant was HMGCR c.1564-106A>G (rs3846662), and carriers showed a significantly lower reduction in TC and non-HDL. This variant is related to an alternative splicing involving exon 13, which is also regulated by lipid concentrations in patients without the variant. Concerning therapeutic goals, HMGCR c.1564-106A>G hindered the achievement of TC targets on patients.
   The HMGCR c.1564-106A>G variant was associated with less statin efficacy to decrease cholesterol.
C1 [Cano-Corres, Ruth] Univ Autonoma Barcelona, Parc Tauli Hosp Univ, Inst Invest & Innovacio Parc Tauli I3PT, Clin Lab,Biochem Dept, Sabadell, Spain.
   [Candas-Estebanez, Beatriz; Padro-Miquel, Ariadna; Alia-Ramos, Pedro] Hosp Univ Bellvitge IDIBELL, Clin Lab Biochem & Mol Genet, Barcelona, Spain.
   [Fanlo-Maresma, Marta; Pinto, Xavier] Hosp Univ Bellvitge, Serv Med Interna, Unidad Lipidos & Riesgo Vasc, CiberObn,Idibell, Barcelona, Spain.
C3 Autonomous University of Barcelona; Parc Tauli Hospital Universitari;
   Institut d'Investigacio Biomedica de Bellvitge (IDIBELL); Bellvitge
   University Hospital; CIBER - Centro de Investigacion Biomedica en Red;
   CIBEROBN; Institut d'Investigacio Biomedica de Bellvitge (IDIBELL);
   Bellvitge University Hospital; University of Barcelona
RP Cano-Corres, R (corresponding author), Univ Autonoma Barcelona, Parc Tauli Hosp Univ, Inst Invest & Innovacio Parc Tauli I3PT, Clin Lab,Biochem Dept, Sabadell, Spain.
EM rcano@tauli.cat
RI Pintó, Xavier/AGI-4297-2022
OI Pinto Sala, Xavier/0000-0002-2216-2444; Padro-Miquel,
   Ariadna/0000-0002-6488-447X; Cano-Corres, Ruth/0000-0003-0901-4479
CR Angelini S, 2017, INT J MOL SCI, V19
   Authors/Task Force Members:, 2016, Atherosclerosis, V253, P281, DOI 10.1016/j.atherosclerosis.2016.08.018
   Banerjee A, 2012, INT J CLIN PRACT, V66, P536, DOI 10.1111/j.1742-1241.2012.02908.x
   Bays HE, 2016, J CLIN LIPIDOL, V10, pS1, DOI 10.1016/j.jacl.2015.08.002
   Becker ML, 2010, PHARMACOEPIDEM DR S, V19, P75, DOI 10.1002/pds.1866
   Bennet AM, 2007, JAMA-J AM MED ASSOC, V298, P1300, DOI 10.1001/jama.298.11.1300
   Boekholdt SM, 2012, JAMA-J AM MED ASSOC, V307, P1302, DOI 10.1001/jama.2012.366
   Burkhardt R, 2008, ARTERIOSCL THROM VAS, V28, P2078, DOI 10.1161/ATVBAHA.108.172288
   Chasman DI, 2012, CIRC-CARDIOVASC GENE, V5, P257, DOI 10.1161/CIRCGENETICS.111.961144
   Colhoun HM, 2004, LANCET, V364, P685, DOI 10.1016/S0140-6736(04)16895-5
   Deshmukh HA, 2012, J LIPID RES, V53, P1000, DOI 10.1194/jlr.P021113
   Donnelly LA, 2011, CLIN PHARMACOL THER, V89, P210, DOI 10.1038/clpt.2010.255
   Downs JR, 1998, JAMA-J AM MED ASSOC, V279, P1615, DOI 10.1001/jama.279.20.1615
   Getz GS, 2009, J LIPID RES, V50, pS156, DOI 10.1194/jlr.R800058-JLR200
   GOFMAN JW, 1952, B NEW YORK ACAD MED, V28, P279
   Grundy SM, 2002, CIRCULATION, V106, P3143, DOI 10.1161/circ.106.25.3143
   HIXSON JE, 1990, J LIPID RES, V31, P545
   Kajinami K, 2004, AM J CARDIOL, V93, P104, DOI 10.1016/j.amjcard.2003.08.078
   KANNEL WB, 1979, JAMA-J AM MED ASSOC, V241, P2035, DOI 10.1001/jama.241.19.2035
   Khan TA, 2013, INT J EPIDEMIOL, V42, P475, DOI 10.1093/ije/dyt034
   Leduc V, 2016, PHARMACOGENET GENOM, V26, P1, DOI 10.1097/FPC.0000000000000178
   Li H, 2013, ARTERIOSCL THROM VAS, V33, P687, DOI 10.1161/ATVBAHA.112.301193
   Maeda K, 2008, DRUG METAB PHARMACOK, V23, P223, DOI 10.2133/dmpk.23.223
   Martin NG, 2012, BRIT J CLIN PHARMACO, V73, P303, DOI 10.1111/j.1365-2125.2011.04090.x
   Medina MW, 2010, DISCOV MED, V9, P495
   Medina MW, 2008, CIRCULATION, V118, P355, DOI 10.1161/CIRCULATIONAHA.108.773267
   Medina MW, 2011, PLOS ONE, V6, DOI 10.1371/journal.pone.0019420
   Mega JL, 2009, ARTERIOSCL THROM VAS, V29, P1310, DOI 10.1161/ATVBAHA.109.188474
   Niemi M, 2011, PHARMACOL REV, V63, P157, DOI 10.1124/pr.110.002857
   Postmus I, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms6068
   Ridker PM, 2008, NEW ENGL J MED, V359, P2195, DOI 10.1056/NEJMoa0807646
   RIFKIND BM, 1984, JAMA-J AM MED ASSOC, V251, P365
   RIFKIND BM, 1984, JAMA-J AM MED ASSOC, V251, P351
   Sever PS, 2004, DRUGS, V64, P43, DOI 10.2165/00003495-200464002-00005
   Shepherd J, 2002, LANCET, V360, P1623, DOI 10.1016/S0140-6736(02)11600-X
   SHEPHERD J, 1995, NEW ENGL J MED, V333, P1301, DOI 10.1056/NEJM199511163332001
   Simons J, 2003, FORTUNE, V147, P58
   STAMLER J, 1986, JAMA-J AM MED ASSOC, V256, P2823, DOI 10.1001/jama.256.20.2823
   Wierzbicki AS, 2012, INT J CLIN PRACT, V66, P622, DOI 10.1111/j.1742-1241.2012.02956.x
   Yoshida K, 2013, AAPS J, V15, P618, DOI 10.1208/s12248-013-9471-9
   Zhang W, 2007, BRIT J CLIN PHARMACO, V64, P346, DOI 10.1111/j.1365-2125.2007.02892.x
NR 41
TC 10
Z9 10
U1 0
U2 12
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN, NJ 07030 USA
SN 0887-8013
EI 1098-2825
J9 J CLIN LAB ANAL
JI J. Clin. Lab. Anal.
PD OCT
PY 2018
VL 32
IS 8
AR e22566
DI 10.1002/jcla.22566
PG 8
WC Medical Laboratory Technology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Medical Laboratory Technology
GA GX5GP
UT WOS:000447772900004
PM 29732606
OA Bronze, Green Published
DA 2025-04-10
ER

PT J
AU Tessier, SN
   Storey, KB
AF Tessier, Shannon N.
   Storey, Kenneth B.
TI To be or not to be: the regulation of mRNA fate as a survival strategy
   during mammalian hibernation
SO CELL STRESS & CHAPERONES
LA English
DT Review
DE Mammalian hibernation; Stress tolerance; Transcriptional and
   posttranscriptional regulation; Translation; RNA interacting factors
ID ARCTIC GROUND-SQUIRRELS; METABOLIC-RATE DEPRESSION; DIFFERENTIAL
   GENE-EXPRESSION; MYOCYTE ENHANCER FACTOR-2; STRESS GRANULE FORMATION;
   SPERMOPHILUS-TRIDECEMLINEATUS; NUCLEAR-BODIES; BINDING PROTEINS;
   SKELETAL-MUSCLE; EIF2-ALPHA PHOSPHORYLATION
AB Mammalian hibernators undergo profound behavioral, physiological, and biochemical changes in order to cope with hypothermia, ischemia-reperfusion, and finite fuel reserves over days or weeks of continuous torpor. Against a backdrop of global reductions in energy-expensive processes such as transcription and translation, a subset of genes/proteins are strategically upregulated in order to meet challenges associated with hibernation. Consequently, hibernation involves substantial transcriptional and posttranscriptional regulatory mechanisms and provides a phenomenon with which to understand how a set of common genes/proteins can be differentially regulated in order to enhance stress tolerance beyond that which is possible for nonhibernators. The present review focuses on the involvement of messenger RNA (mRNA) interacting factors that play a role in the regulation of gene/protein expression programs that define the hibernating phenotype. These include proteins involved in mRNA processing (i.e., capping, splicing, and polyadenylation) and the possible role of alternative splicing as a means of enhancing protein diversity. Since the total pool of mRNA remains constant throughout torpor, mechanisms which enhance mRNA stability are discussed in the context of RNA binding proteins and mRNA decay pathways. Furthermore, mechanisms which control the global reduction of cap-dependent translation and the involvement of internal ribosome entry sites in mRNAs encoding stress response proteins are also discussed. Finally, the concept of regulating each of these factors in discrete subcellular compartments for enhanced efficiency is addressed. The analysis draws on recent research from several well-studied mammalian hibernators including ground squirrels, bats, and bears.
C1 [Tessier, Shannon N.; Storey, Kenneth B.] Carleton Univ, Inst Biochem, Ottawa, ON K1S 5B6, Canada.
   [Tessier, Shannon N.; Storey, Kenneth B.] Carleton Univ, Dept Biol, Ottawa, ON K1S 5B6, Canada.
C3 Carleton University; Carleton University
RP Storey, KB (corresponding author), Carleton Univ, Inst Biochem, 1125 Colonel By Dr, Ottawa, ON K1S 5B6, Canada.
EM kenneth_storey@carleton.ca
RI Storey, Kenneth/G-9883-2011
OI Tessier, Shannon/0000-0003-2373-232X
FU Natural Sciences and Engineering Research Council (NSERC) of Canada;
   Canada Research Chairs program; Ontario Graduate Scholarship
FX Thanks to JM Storey for editorial review of the manuscript. Thanks also
   to Dr. TE Audas and Dr. S Lee for their role in our collaborative paper
   aimed at understanding RNA binding proteins during hibernation. This
   work was supported by a discovery grant from the Natural Sciences and
   Engineering Research Council (NSERC) of Canada to KBS and the Canada
   Research Chairs program. SNT held an Ontario Graduate Scholarship.
CR Allan ME, 2012, CELL BIOCHEM FUNCT, V30, P166, DOI 10.1002/cbf.1832
   Anderson P, 2008, TRENDS BIOCHEM SCI, V33, P141, DOI 10.1016/j.tibs.2007.12.003
   Andrews MT, 2007, BIOESSAYS, V29, P431, DOI 10.1002/bies.20560
   Audas TE, 2012, MOL CELL, V45, P147, DOI 10.1016/j.molcel.2011.12.012
   Baird TD, 2012, ADV NUTR, V3, P307, DOI 10.3945/an.112.002113
   Barger JL, 2003, AM J PHYSIOL-REG I, V284, pR1306, DOI 10.1152/ajpregu.00579.2002
   BARNES BM, 1989, SCIENCE, V244, P1593, DOI 10.1126/science.2740905
   Bentley D, 2002, CURR OPIN CELL BIOL, V14, P336, DOI 10.1016/S0955-0674(02)00333-2
   Bentley DL, 2005, CURR OPIN CELL BIOL, V17, P251, DOI 10.1016/j.ceb.2005.04.006
   BERNSTEIN P, 1989, MOL CELL BIOL, V9, P659, DOI 10.1128/MCB.9.2.659
   Biggar KK, 2011, J MOL CELL BIOL, V3, P167, DOI 10.1093/jmcb/mjq045
   Brooks NE, 2011, J EXP BIOL, V214, P2522, DOI 10.1242/jeb.055764
   Busà R, 2010, NUCLEIC ACIDS RES, V38, P3005, DOI 10.1093/nar/gkq004
   Cai DC, 2004, GENE, V343, P203, DOI 10.1016/j.gene.2004.09.003
   CAPONIGRO G, 1995, GENE DEV, V9, P2421, DOI 10.1101/gad.9.19.2421
   Carey HV, 2000, J COMP PHYSIOL B, V170, P551, DOI 10.1007/s003600000135
   Carey HV, 2003, PHYSIOL REV, V83, P1153, DOI 10.1152/physrev.00008.2003
   Chen JP, 2008, COMP BIOCHEM PHYS B, V149, P388, DOI 10.1016/j.cbpb.2007.10.011
   Chen Y, 2001, BIOCHEMISTRY-US, V40, P11565, DOI 10.1021/bi010649w
   Chung D, 2011, J COMP PHYSIOL B, V181, P699, DOI 10.1007/s00360-010-0547-x
   Cowling VH, 2010, BIOCHEM J, V425, P295, DOI 10.1042/BJ20091352
   Dark J, 2005, ANNU REV NUTR, V25, P469, DOI 10.1146/annurev.nutr.25.050304.092514
   DECKER CJ, 1993, GENE DEV, V7, P1632, DOI 10.1101/gad.7.8.1632
   Dutertre M, 2011, RNA BIOL, V8, P740, DOI 10.4161/rna.8.5.16016
   Eddy SF, 2007, CELL BIOCHEM FUNCT, V25, P759, DOI 10.1002/cbf.1416
   Eddy SF, 2005, MOL CELL BIOCHEM, V269, P175, DOI 10.1007/s11010-005-3459-4
   Eddy SF, 2005, ARCH BIOCHEM BIOPHYS, V435, P103, DOI 10.1016/j.abb.2004.11.020
   El Kebbaj Z, 2009, ENDOCRINOLOGY, V150, P1192, DOI 10.1210/en.2008-1394
   Emara MM, 2012, BIOCHEM BIOPH RES CO, V423, P763, DOI 10.1016/j.bbrc.2012.06.033
   Faustino NA, 2003, GENE DEV, V17, P419, DOI 10.1101/gad.1048803
   Fitzgerald KD, 2009, BBA-GENE REGUL MECH, V1789, P518, DOI 10.1016/j.bbagrm.2009.07.004
   Frerichs KU, 1998, P NATL ACAD SCI USA, V95, P14511, DOI 10.1073/pnas.95.24.14511
   Geiser F, 2013, CURR BIOL, V23, pR188, DOI 10.1016/j.cub.2013.01.062
   Gervois P, 1999, MOL ENDOCRINOL, V13, P1535, DOI 10.1210/me.13.9.1535
   Gingras AC, 1999, ANNU REV BIOCHEM, V68, P913, DOI 10.1146/annurev.biochem.68.1.913
   Gottschald OR, 2010, J MOL CELL BIOL, V2, P345, DOI 10.1093/jmcb/mjq032
   GRIGG GC, 1989, COMP BIOCHEM PHYS A, V92, P609, DOI 10.1016/0300-9629(89)90375-7
   Gruber AR, 2014, WIRES RNA, V5, P183, DOI 10.1002/wrna.1206
   HARGROVE JL, 1989, FASEB J, V3, P2360, DOI 10.1096/fasebj.3.12.2676679
   Hittel D, 2001, BBA-GENE STRUCT EXPR, V1522, P238, DOI 10.1016/S0167-4781(01)00338-4
   Hittel D, 2002, ARCH BIOCHEM BIOPHYS, V401, P244, DOI 10.1016/S0003-9861(02)00048-6
   Hizli AA, 2013, MOL CELL BIOL, V33, P596, DOI 10.1128/MCB.01270-12
   Hofmann S, 2012, MOL BIOL CELL, V23, P3786, DOI 10.1091/mbc.E12-04-0296
   Hsu LS, 2001, J BIOL CHEM, V276, P31113, DOI 10.1074/jbc.M011720200
   Iqbal K, 2005, BBA-MOL BASIS DIS, V1739, P198, DOI 10.1016/j.bbadis.2004.09.008
   Johnson JM, 2003, SCIENCE, V302, P2141, DOI 10.1126/science.1090100
   Jones BL, 2013, COMP BIOCHEM PHYS A, V166, P375, DOI 10.1016/j.cbpa.2013.07.009
   Kedersha N, 2007, METHOD ENZYMOL, V431, P61, DOI 10.1016/S0076-6879(07)31005-7
   Kishore S, 2010, BRIEF FUNCT GENOMICS, V9, P391, DOI 10.1093/bfgp/elq028
   Klann E, 2004, NAT REV NEUROSCI, V5, P931, DOI 10.1038/nrn1557
   Knight JE, 2000, MOL CELL BIOL, V20, P6374, DOI 10.1128/MCB.20.17.6374-6379.2000
   Korner CG, 1997, J BIOL CHEM, V272, P10448
   Kornfeld Samantha F., 2012, Genomics Proteomics & Bioinformatics, V10, P295, DOI 10.1016/j.gpb.2012.09.001
   Kramer S, 2008, J CELL SCI, V121, P3002, DOI 10.1242/jcs.031823
   Lander ES, 2001, NATURE, V409, P860, DOI 10.1038/35057062
   Laplante M, 2009, J CELL SCI, V122, P3589, DOI 10.1242/jcs.051011
   Lee CC, 2008, ANNU REV MED, V59, P177, DOI 10.1146/annurev.med.59.061506.110403
   Lee Y, 2007, J CEREBR BLOOD F MET, V27, P950, DOI 10.1038/sj.jcbfm.9600395
   Lindquist ME, 2010, J VIROL, V84, P12274, DOI 10.1128/JVI.00260-10
   Ling C, 2009, DIABETES, V58, P2718, DOI 10.2337/db09-1003
   Liu YT, 2010, PHYSIOL GENOMICS, V42A, P39, DOI 10.1152/physiolgenomics.00054.2010
   Maistrovski Y, 2012, J COMP PHYSIOL B, V182, P849, DOI 10.1007/s00360-012-0662-y
   Malatesta M, 1999, ANAT REC, V254, P389, DOI 10.1002/(SICI)1097-0185(19990301)254:3<389::AID-AR10>3.0.CO;2-E
   MALATESTA M, 1994, EUR J CELL BIOL, V65, P82
   Malatesta M, 1998, CELL TISSUE RES, V292, P531, DOI 10.1007/s004410051082
   MALATESTA M, 1995, CHROMOSOMA, V104, P121, DOI 10.1007/BF00347694
   Malatesta M, 2003, EUR J HISTOCHEM, V47, P233
   Malatesta M, 2001, CHROMOSOMA, V110, P471, DOI 10.1007/s004120100166
   MALATESTA M, 1994, EXP CELL RES, V211, P415, DOI 10.1006/excr.1994.1106
   Malatesta M, 2000, CHROMOSOMA, V109, P506, DOI 10.1007/s004120000102
   Malatesta M, 2008, MICROSC RES TECHNIQ, V71, P564, DOI 10.1002/jemt.20587
   Malatesta M, 2011, MICROSC RES TECHNIQ, V74, P47, DOI 10.1002/jemt.20872
   Mamady H, 2008, ARCH BIOCHEM BIOPHYS, V477, P77, DOI 10.1016/j.abb.2008.05.006
   Mao YTS, 2011, TRENDS GENET, V27, P295, DOI 10.1016/j.tig.2011.05.006
   MILNER RE, 1989, AM J PHYSIOL, V256, pR42, DOI 10.1152/ajpregu.1989.256.1.R42
   MinvielleSebastia L, 1997, P NATL ACAD SCI USA, V94, P7897, DOI 10.1073/pnas.94.15.7897
   Morin PJ, 2008, BBA-GENE REGUL MECH, V1779, P628, DOI 10.1016/j.bbagrm.2008.07.011
   Morin P, 2008, MOL CELL BIOCHEM, V312, P121, DOI 10.1007/s11010-008-9727-3
   Morin PJ, 2006, CRYOBIOLOGY, V53, P310, DOI 10.1016/j.cryobiol.2006.08.002
   Morin P, 2009, INT J DEV BIOL, V53, P433, DOI 10.1387/ijdb.082643pm
   Morin PJ, 2005, BBA-GENE STRUCT EXPR, V1729, P32, DOI 10.1016/j.bbaexp.2005.02.009
   Morris GE, 2008, BBA-MOL CELL RES, V1783, P2108, DOI 10.1016/j.bbamcr.2008.07.016
   Muñoz MJ, 2009, CELL, V137, P708, DOI 10.1016/j.cell.2009.03.010
   O'Hara BF, 1999, J NEUROSCI, V19, P3781
   PALYGA J, 2011, HYPOMETABOLISM STRAT, P183
   Pan PP, 2011, AM J PHYSIOL-REG I, V301, pR370, DOI 10.1152/ajpregu.00748.2010
   Proud CG, 2002, EUR J BIOCHEM, V269, P5337, DOI 10.1046/j.1432-1033.2002.03289.x
   ROSS J, 1995, MICROBIOL REV, V59, P423, DOI 10.1128/MMBR.59.3.423-450.1995
   Rouble AN, 2013, PEERJ, V1, DOI 10.7717/peerj.29
   SACHS AB, 1989, CELL, V58, P857, DOI 10.1016/0092-8674(89)90938-0
   Scott MS, 2010, NUCLEIC ACIDS RES, V38, P7388, DOI 10.1093/nar/gkq653
   Shao CX, 2010, MOL CELL PROTEOMICS, V9, P313, DOI 10.1074/mcp.M900260-MCP200
   Shin C, 2004, NAT REV MOL CELL BIO, V5, P727, DOI 10.1038/nrm1467
   Singh RK, 2012, TRENDS MOL MED, V18, P472, DOI 10.1016/j.molmed.2012.06.006
   Sonenberg N, 2009, CELL, V136, P731, DOI 10.1016/j.cell.2009.01.042
   SRERE HK, 1992, P NATL ACAD SCI USA, V89, P7119, DOI 10.1073/pnas.89.15.7119
   SRERE HK, 1995, AM J PHYSIOL-REG I, V268, pR1507, DOI 10.1152/ajpregu.1995.268.6.R1507
   Stieler JT, 2011, PLOS ONE, V6, DOI 10.1371/journal.pone.0014530
   Storey KB, 2004, BIOL REV, V79, P207, DOI 10.1017/S1464793103006195
   STOREY KB, 2003, HYPOXIA LIFECYCLE, P7
   STOREY KB, 2004, FUNCTIONAL METABOLIS, P442
   Storey KB, 2010, ADV CLIN CHEM, V52, P77, DOI 10.1016/S0065-2423(10)52003-1
   Storey KB, 2010, GERONTOLOGY, V56, P220, DOI 10.1159/000228829
   Suswam EA, 2005, NUCLEIC ACIDS RES, V33, P4507, DOI 10.1093/nar/gki763
   Tamburini M, 1996, HISTOCHEM CELL BIOL, V106, P581
   Tessier SN, 2014, CELL STRESS CHAPERON, V19, P813, DOI 10.1007/s12192-014-0505-8
   Tessier SN, 2012, GENE, V501, P8, DOI 10.1016/j.gene.2012.04.004
   Tessier SN, 2010, MOL CELL BIOCHEM, V344, P151, DOI 10.1007/s11010-010-0538-y
   Thomas MC, 2006, CRIT REV BIOCHEM MOL, V41, P105, DOI 10.1080/10409230600648736
   Thoreen CC, 2012, NATURE, V485, P109, DOI 10.1038/nature11083
   Tian B, 2012, WIRES RNA, V3, P385, DOI 10.1002/wrna.116
   Toien O, 2011, SCIENCE, V331, P906, DOI 10.1126/science.1199435
   van Breukelen F, 2002, J APPL PHYSIOL, V92, P2640, DOI 10.1152/japplphysiol.01007.2001
   van Breukelen F, 2004, AM J PHYSIOL-REG I, V287, pR349, DOI 10.1152/ajpregu.00728.2003
   Van Breukelen F, 2001, AM J PHYSIOL-REG I, V281, pR1374, DOI 10.1152/ajpregu.2001.281.5.R1374
   Wang L.C.H., 1996, HDB PHYSL, P507, DOI DOI 10.1002/CPHY.CP040122
   Wu CW, 2012, J EXP BIOL, V215, P1720, DOI 10.1242/jeb.066225
   Yan J, 2008, PHYSIOL GENOMICS, V32, P170, DOI 10.1152/physiolgenomics.00075.2007
   Yuan LH, 2007, COMP BIOCHEM PHYS B, V146, P438, DOI 10.1016/j.cbpb.2006.12.005
   ZANCANARO C, 1993, BIOL CELL, V79, P55, DOI 10.1016/0248-4900(93)90263-E
   Zhang J., 2011, HYPOMETABOLISM STRAT, P147
   Zhao S, 2010, BMC GENOMICS, V11, DOI 10.1186/1471-2164-11-201
   Zimber A, 2004, CELL SIGNAL, V16, P1085, DOI 10.1016/j.cellsig.2004.03.020
NR 123
TC 18
Z9 23
U1 1
U2 34
PU SPRINGER
PI DORDRECHT
PA VAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDS
SN 1355-8145
EI 1466-1268
J9 CELL STRESS CHAPERON
JI Cell Stress Chaperones
PD NOV
PY 2014
VL 19
IS 6
BP 763
EP 776
DI 10.1007/s12192-014-0512-9
PG 14
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA AT3YX
UT WOS:000344873100003
PM 24789358
OA Green Published
DA 2025-04-10
ER

PT J
AU Wang, YM
   Ni, HY
AF Wang, Yiming
   Ni, Heyu
TI Fibronectin maintains the balance between hemostasis and thrombosis
SO CELLULAR AND MOLECULAR LIFE SCIENCES
LA English
DT Review
DE Fibronectin; Platelet; Fibrinogen and fibrin; Collagen; Integrins;
   Coagulation factors
ID COLD-INSOLUBLE GLOBULIN; VON-WILLEBRAND-FACTOR; COLLAGEN TYPE-I;
   INDEPENDENT PHAGOCYTOSIS IMPLICATIONS; FIBROBLAST SURFACE-ANTIGEN;
   INTRAVENOUS IGG THERAPY; DEEP-VEIN THROMBOSIS; ARG-GLY-ASP;
   PLATELET-AGGREGATION; PLASMA FIBRONECTIN
AB Fibronectin is a dimeric protein widely distributed in solid tissues and blood. This major extracellular matrix protein is indispensable for embryogenesis and plays crucial roles in many physiological and pathological processes. Fibronectin pre-mRNA undergoes alternative splicing to generate over 20 splicing variants, which are categorized as either plasma fibronectin (pFn) or cellular fibronectin (cFn). All fibronectin variants contain integrin binding motifs, as well as N-terminus collagen and fibrin binding motifs. With motifs that can be recognized by platelet integrins and coagulation factors, fibronectin, especially pFn, has long been suspected to be involved in hemostasis and thrombosis, but the exact function of fibronectin in these processes is controversial. The advances made using intravital microscopy models and fibronectin deficient and mutant mice have greatly facilitated the direct investigation of fibronectin function in vivo. Recent studies revealed that pFn is a vital hemostatic factor that is especially crucial for hemostasis in both genetic and anticoagulant-induced deficiencies of fibrin formation. pFn may also be an important self-limiting regulator to prevent hemorrhage as well as excessive thrombus formation and vessel occlusion. In addition to pFn, cFn is found to be prothrombotic and may contribute to thrombotic complications in various diseases. Further investigations of the role of pFn and cFn in thrombotic and hemorrhagic diseases may provide insights into development of novel therapeutic strategies (e. g., pFn transfusion) for the maintenance of the fine balance between hemostasis and thrombosis.
C1 [Wang, Yiming; Ni, Heyu] St Michaels Hosp, LKSKI Keenan Res Ctr Biomed Sci, Dept Lab Med, Room 420,209 Victoria St, Toronto, ON M5B 1W8, Canada.
   [Wang, Yiming; Ni, Heyu] Univ Toronto, Dept Lab Med & Pathobiol, Toronto, ON, Canada.
   [Wang, Yiming; Ni, Heyu] Canadian Blood Serv, Toronto, ON, Canada.
   [Wang, Yiming; Ni, Heyu] Toronto Platelet Immunobiol Grp, Toronto, ON, Canada.
   [Ni, Heyu] Univ Toronto, Dept Physiol, Toronto, ON, Canada.
   [Ni, Heyu] Univ Toronto, Dept Med, Toronto, ON, Canada.
C3 University of Toronto; Saint Michaels Hospital Toronto; University of
   Toronto; Canadian Blood Services; University of Toronto; University of
   Toronto
RP Ni, HY (corresponding author), St Michaels Hosp, LKSKI Keenan Res Ctr Biomed Sci, Dept Lab Med, Room 420,209 Victoria St, Toronto, ON M5B 1W8, Canada.; Ni, HY (corresponding author), Univ Toronto, Dept Lab Med & Pathobiol, Toronto, ON, Canada.; Ni, HY (corresponding author), Canadian Blood Serv, Toronto, ON, Canada.; Ni, HY (corresponding author), Toronto Platelet Immunobiol Grp, Toronto, ON, Canada.; Ni, HY (corresponding author), Univ Toronto, Dept Physiol, Toronto, ON, Canada.; Ni, HY (corresponding author), Univ Toronto, Dept Med, Toronto, ON, Canada.
EM nih@smh.ca
OI Wang, Yiming/0000-0001-8031-6184; Ni, Heyu/0000-0002-7621-2945
CR ALLAIN JP, 1984, SCAND J HAEMATOL, V33, P173
   ANDREW M, 1988, BLOOD, V72, P1651
   Andrews M, 2011, SIGNAL DEPENDENT TRA
   AOTA S, 1994, J BIOL CHEM, V269, P24756
   ARNESON MA, 1980, JAMA-J AM MED ASSOC, V244, P144, DOI 10.1001/jama.244.2.144
   Astrof S, 2007, DEV BIOL, V311, P11, DOI 10.1016/j.ydbio.2007.07.005
   BASTIDA E, 1987, BLOOD, V70, P1437
   BOWDITCH RD, 1994, J BIOL CHEM, V269, P10856
   Brill A, 2012, J THROMB HAEMOST, V10, P136, DOI 10.1111/j.1538-7836.2011.04544.x
   Buratti E, 2004, MOL CELL BIOL, V24, P1387, DOI 10.1128/MCB.24.3.1387-1400.2004
   Callum JL, 2009, TRANSFUS MED REV, V23, P177, DOI 10.1016/j.tmrv.2009.03.001
   CAPUTI M, 1994, NUCLEIC ACIDS RES, V22, P1018, DOI 10.1093/nar/22.6.1018
   Castellanos M, 2004, STROKE, V35, P1671, DOI 10.1161/01.STR.0000131656.47979.39
   Chauhan AK, 2005, BEHAV BRAIN RES, V161, P31, DOI 10.1016/j.bbr.2005.02.020
   Chauhan AK, 2004, GENE, V324, P55, DOI 10.1016/j.gene.2003.09.026
   Chauhan AK, 2008, ARTERIOSCL THROM VAS, V28, P296, DOI 10.1161/ATVBAHA.107.149146
   Cho J, 2006, J THROMB HAEMOST, V4, P1461, DOI 10.1111/j.1538-7836.2006.01943.x
   Cho JH, 2006, BLOOD, V107, P3555, DOI 10.1182/blood-2005-10-4168
   Collet JP, 2005, BLOOD, V106, P3824, DOI 10.1182/blood-2005-05-2150
   Corbett SA, 1997, J BIOL CHEM, V272, P24999, DOI 10.1074/jbc.272.40.24999
   Cramer P, 1999, MOL CELL, V4, P251, DOI 10.1016/S1097-2765(00)80372-X
   Dhanesha N, 2015, CIRCULATION, V132, P2237, DOI 10.1161/CIRCULATIONAHA.115.016540
   DIXIT VM, 1985, P NATL ACAD SCI USA, V82, P3844, DOI 10.1073/pnas.82.11.3844
   Doddapattar P, 2015, ARTERIOSCL THROM VAS, V35, P2391, DOI 10.1161/ATVBAHA.115.306474
   Dunne E, 2012, ARTERIOSCL THROM VAS, V32, P1724, DOI 10.1161/ATVBAHA.112.250464
   Falati S, 2002, NAT MED, V8, P1175, DOI 10.1038/nm782
   Farrell DH, 2008, THROMB HAEMOSTASIS, V100, P173, DOI 10.1160/TH08-07-0441
   Foster C, 2014, BIOMARK MED, V8, P471, DOI 10.2217/bmm.14.28
   Fuchs TA, 2010, P NATL ACAD SCI USA, V107, P15880, DOI 10.1073/pnas.1005743107
   Fukuda T, 2002, CANCER RES, V62, P5603
   GAHMBERG CG, 1973, P NATL ACAD SCI USA, V70, P3329, DOI 10.1073/pnas.70.12.3329
   Geiger B, 2001, NAT REV MOL CELL BIO, V2, P793, DOI 10.1038/35099066
   GEORGE EL, 1993, DEVELOPMENT, V119, P1079
   GINSBERG MH, 1983, J CLIN INVEST, V71, P619, DOI 10.1172/JCI110808
   GINSBERG MH, 1980, P NATL ACAD SCI-BIOL, V77, P1049, DOI 10.1073/pnas.77.2.1049
   GUAN JL, 1990, CELL, V60, P53, DOI 10.1016/0092-8674(90)90715-Q
   Gui T, 2007, THROMB RES, V121, P225, DOI 10.1016/j.thromres.2007.03.026
   Heit JA, 2008, ARTERIOSCL THROM VAS, V28, P370, DOI 10.1161/ATVBAHA.108.162545
   HOGG NM, 1974, P NATL ACAD SCI USA, V71, P489, DOI 10.1073/pnas.71.2.489
   Hou Y, 2015, J BIOMED RES, V29, P437, DOI 10.7555/JBR.29.20150121
   HOUDIJK WPM, 1985, BLOOD, V65, P598
   HOUDIJK WPM, 1985, J CLIN INVEST, V75, P531, DOI 10.1172/JCI111729
   HOUDIJK WPM, 1986, ARTERIOSCLEROSIS, V6, P24, DOI 10.1161/01.ATV.6.1.24
   HUH GS, 1994, GENE DEV, V8, P1561, DOI 10.1101/gad.8.13.1561
   HUH GS, 1993, MOL CELL BIOL, V13, P5301, DOI 10.1128/MCB.13.9.5301
   Hynes R. O, 1990, FIBRONECTINS
   HYNES RO, 1975, VIROLOGY, V64, P492, DOI 10.1016/0042-6822(75)90126-9
   HYNES RO, 1973, P NATL ACAD SCI USA, V70, P3170, DOI 10.1073/pnas.70.11.3170
   Hynes RO, 2002, CELL, V110, P673, DOI 10.1016/S0092-8674(02)00971-6
   Jackson SP, 2007, BLOOD, V109, P5087, DOI 10.1182/blood-2006-12-027698
   KAMYKOWSKI GW, 1981, BIOPHYS CHEM, V13, P25, DOI 10.1016/0301-4622(81)80021-X
   Kanters SDJM, 2001, DIABETES CARE, V24, P323, DOI 10.2337/diacare.24.2.323
   KESKIOJA J, 1976, CELL, V9, P29, DOI 10.1016/0092-8674(76)90049-0
   KORNBLIHTT AR, 1985, EMBO J, V4, P1755, DOI 10.1002/j.1460-2075.1985.tb03847.x
   Kornblihtt AR, 1996, FASEB J, V10, P248, DOI 10.1096/fasebj.10.2.8641558
   KUUSELA P, 1976, IMMUNOCHEMISTRY, V13, P639, DOI 10.1016/0019-2791(76)90203-2
   Lei X, 2014, THROMB HAEMOSTASIS, V111, P279, DOI 10.1160/TH13-06-0490
   Leiss M, 2008, CURR OPIN CELL BIOL, V20, P502, DOI 10.1016/j.ceb.2008.06.001
   Li CL, 2011, J CLIN INVEST, V121, P4537, DOI 10.1172/JCI57850
   Li J, 2015, NAT COMMUN, V6, DOI 10.1038/ncomms8737
   Li June, 2013, Cardiovascular & Hematological Disorders - Drug Targets, V13, P50
   Liao YF, 2002, J BIOL CHEM, V277, P14467, DOI 10.1074/jbc.M201100200
   Mackman N, 2008, NATURE, V451, P914, DOI 10.1038/nature06797
   Matuskova J, 2006, ARTERIOSCL THROM VAS, V26, P1391, DOI 10.1161/01.ATV.0000216282.58291.c6
   Maurer E, 2015, THROMB HAEMOSTASIS, V114, P1175, DOI 10.1160/TH14-11-0958
   Mazzucato M, 2009, BLOOD, V114, P2793, DOI 10.1182/blood-2008-12-193490
   MCKEOWNLONGO PJ, 1985, J CELL BIOL, V100, P364, DOI 10.1083/jcb.100.2.364
   MCMASTER GK, 1982, BIOCHEM BIOPH RES CO, V107, P609, DOI 10.1016/0006-291X(82)91535-2
   McMillan R, 2004, BLOOD, V104, P956, DOI 10.1182/blood-2003-11-3908
   MOON DG, 1986, BLOOD, V67, P450
   Moretti FA, 2007, J BIOL CHEM, V282, P28057, DOI 10.1074/jbc.M611315200
   MORRISON PR, 1948, J AM CHEM SOC, V70, P3103, DOI 10.1021/ja01189a080
   Mosher D.F., 1989, Fibronectin
   MOSHER DF, 1975, J BIOL CHEM, V250, P6614
   MOSHER DF, 1979, J CLIN INVEST, V64, P781, DOI 10.1172/JCI109524
   Muro AF, 2003, J CELL BIOL, V162, P149, DOI 10.1083/jcb.200212079
   Ni H, 2006, J THROMB HAEMOST, V4, P940, DOI 10.1111/j.1538-7836.2006.01899.x
   Ni HY, 2000, J CLIN INVEST, V106, P385, DOI 10.1172/JCI9896
   Ni HY, 2006, BLOOD, V107, P2976, DOI 10.1182/blood-2005-06-2562
   Ni HY, 2003, BLOOD, V102, P3609, DOI 10.1182/blood-2003-03-0850
   Ni HY, 2003, P NATL ACAD SCI USA, V100, P2415, DOI 10.1073/pnas.2628067100
   Nieswandt B, 2001, EMBO J, V20, P2120, DOI 10.1093/emboj/20.9.2120
   NIEVELSTEIN PFEM, 1988, ARTERIOSCLEROSIS, V8, P200, DOI 10.1161/01.ATV.8.2.200
   NIEWIAROWSKA J, 1982, THROMB RES, V27, P611, DOI 10.1016/0049-3848(82)90308-5
   OKADA M, 1985, J BIOL CHEM, V260, P1811
   Palumbo JS, 2004, J THROMB HAEMOST, V2, P1368, DOI 10.1111/j.1538-7836.2004.00788.x
   Pankov R, 2002, J CELL SCI, V115, P3861, DOI 10.1242/jcs.00059
   Pankov R, 2000, J CELL BIOL, V148, P1075, DOI 10.1083/jcb.148.5.1075
   Pecheniuk NM, 2008, THROMB HAEMOSTASIS, V100, P224, DOI 10.1160/TH08-02-0078
   PETERS JH, 1989, J LAB CLIN MED, V113, P586
   PIERSCHBACHER MD, 1984, P NATL ACAD SCI-BIOL, V81, P5985, DOI 10.1073/pnas.81.19.5985
   Polanowska-Grabowska R, 1999, THROMB HAEMOSTASIS, V81, P118
   Prakash P, 2015, BLOOD, V125, P3164, DOI 10.1182/blood-2014-10-608653
   PROCYK R, 1990, BIOPOLYMERS, V29, P559, DOI 10.1002/bip.360290311
   Puetz J, 2013, J THROMB HAEMOST, V11, P1794, DOI 10.1111/jth.12351
   PYTELA R, 1986, SCIENCE, V231, P1559, DOI 10.1126/science.2420006
   Reheman A, 2014, CIRC RES, V114, P1070, DOI 10.1161/CIRCRESAHA.114.303600
   Reheman A, 2010, THROMB RES, V125, pE177, DOI 10.1016/j.thromres.2010.01.009
   Reheman A, 2009, BLOOD, V113, P1809, DOI 10.1182/blood-2008-04-148361
   Rostagno AA, 1999, BIOCHEM J, V338, P375, DOI 10.1042/0264-6021:3380375
   Ruggeri ZM, 1997, THROMB HAEMOSTASIS, V78, P611
   Ruggeri ZM, 2002, NAT MED, V8, P1227, DOI 10.1038/nm1102-1227
   RUOSLAHTI E, 1986, CELL, V44, P517, DOI 10.1016/0092-8674(86)90259-X
   RUOSLAHTI E, 1973, BIOCHIM BIOPHYS ACTA, V322, P352, DOI 10.1016/0005-2795(73)90310-3
   RUOSLAHTI E, 1988, ANNU REV BIOCHEM, V57, P375, DOI 10.1146/annurev.bi.57.070188.002111
   RUOSLAHTI E, 1974, NATURE, V248, P789, DOI 10.1038/248789a0
   Sakai T, 2001, NAT MED, V7, P324, DOI 10.1038/85471
   SANTORO SA, 1983, BIOCHEM BIOPH RES CO, V116, P135, DOI 10.1016/0006-291X(83)90391-1
   Schulz C, 2013, J THROMB HAEMOST, V11, P233, DOI 10.1111/jth.12261
   SCHWARZBAUER JE, 1989, J CELL BIOL, V109, P3445, DOI 10.1083/jcb.109.6.3445
   SCHWARZBAUER JE, 1991, J CELL BIOL, V113, P1463, DOI 10.1083/jcb.113.6.1463
   SCHWARZBAUER JE, 1983, CELL, V35, P421, DOI 10.1016/0092-8674(83)90175-7
   Schwarzbauer JE, 1991, CURR OPIN CELL BIOL, V3, P786, DOI 10.1016/0955-0674(91)90051-Y
   Severinsen MT, 2011, BRIT J HAEMATOL, V152, P360, DOI 10.1111/j.1365-2141.2010.08418.x
   Singh P, 2010, ANNU REV CELL DEV BI, V26, P397, DOI 10.1146/annurev-cellbio-100109-104020
   Stalker TJ, 2013, BLOOD, V121, P1875, DOI 10.1182/blood-2012-09-457739
   STATHAKIS NE, 1977, J CLIN INVEST, V60, P855, DOI 10.1172/JCI108840
   STATHAKIS NE, 1978, BLOOD, V51, P1211
   STONE KR, 1974, VIROLOGY, V58, P86, DOI 10.1016/0042-6822(74)90143-3
   Takahashi S, 2007, J CELL BIOL, V178, P167, DOI 10.1083/jcb.200703021
   Tan MH, 2004, BLOOD, V104, P11, DOI 10.1182/blood-2003-09-3363
   THURLOW PJ, 1990, BRIT J HAEMATOL, V75, P549, DOI 10.1111/j.1365-2141.1990.tb07797.x
   Tomasini-Johansson B, 2009, THROMB HAEMOSTASIS, V102, P1278, DOI 10.1160/TH09-03-0141
   Tomasini-Johansson BR, 2001, J BIOL CHEM, V276, P23430, DOI 10.1074/jbc.M103467200
   Vaheri A, 1978, ANN NY ACAD SCI, V312, P1
   VINCENT PA, 1993, AM J PHYSIOL, V265, pL485, DOI 10.1152/ajplung.1993.265.5.L485
   von Brühl ML, 2012, J EXP MED, V209, P819, DOI 10.1084/jem.20112322
   Wang YC, 2005, J EXP MED, V202, P1587, DOI 10.1084/jem.20051108
   Wang YM, 2016, CURR OPIN HEMATOL, V23, P280, DOI 10.1097/MOH.0000000000000237
   Wang YM, 2015, ONCOTARGET, V6, P19350, DOI 10.18632/oncotarget.5097
   Wang YM, 2015, BLOOD, V125, P3043, DOI 10.1182/blood-2015-03-630855
   Wang YM, 2014, J CLIN INVEST, V124, P4281, DOI 10.1172/JCI74630
   Wang Yiming, 2012, Cardiovascular & Hematological Disorders - Drug Targets, V12, P126
   WAYNER EA, 1989, J CELL BIOL, V109, P1321, DOI 10.1083/jcb.109.3.1321
   Webster Michelle Lee, 2008, Cardiovascular & Hematological Disorders - Drug Targets, V8, P278, DOI 10.2174/187152908786786223
   White ES, 2008, J PATHOL, V216, P1, DOI 10.1002/path.2388
   White ES, 2011, IUBMB LIFE, V63, P538, DOI 10.1002/iub.493
   Wu YP, 1997, ARTERIOSCL THROM VAS, V17, P3202, DOI 10.1161/01.ATV.17.11.3202
   Xu XC, 2006, THROMB HAEMOSTASIS, V95, P931, DOI 10.1160/TH06-01-0020
   YAMADA KM, 1974, P NATL ACAD SCI USA, V71, P3492, DOI 10.1073/pnas.71.9.3492
   Yang H, 2006, J THROMB HAEMOST, V4, P2230, DOI 10.1111/j.1538-7836.2006.02116.x
   Yang H, 2009, BLOOD, V114, P425, DOI 10.1182/blood-2008-03-145821
   Yang JT, 1999, DEV BIOL, V215, P264, DOI 10.1006/dbio.1999.9451
   YANG JT, 1993, DEVELOPMENT, V119, P1093
   Yougbare I, 2015, ONCOTARGET, V6, P15724, DOI 10.18632/oncotarget.4757
   Yougbaré I, 2015, J CLIN INVEST, V125, P1545, DOI 10.1172/JCI77820
   ZARDI L, 1979, CELL, V18, P649, DOI 10.1016/0092-8674(79)90120-X
   Zeng QS, 2012, AM J HEMATOL, V87, P206, DOI 10.1002/ajh.22211
   ZERLAUTH G, 1984, AM J MED, V77, P685, DOI 10.1016/0002-9343(84)90366-8
   Zhai Z, 2007, J THROMB HAEMOST, V5, P1740, DOI 10.1111/j.1538-7836.2007.02625.x
NR 150
TC 43
Z9 50
U1 5
U2 35
PU SPRINGER BASEL AG
PI BASEL
PA PICASSOPLATZ 4, BASEL, 4052, SWITZERLAND
SN 1420-682X
EI 1420-9071
J9 CELL MOL LIFE SCI
JI Cell. Mol. Life Sci.
PD SEP
PY 2016
VL 73
IS 17
BP 3265
EP 3277
DI 10.1007/s00018-016-2225-y
PG 13
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA DU7JM
UT WOS:000382390300003
PM 27098513
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Beazley-Long, N
   Hua, J
   Jehle, T
   Hulse, RP
   Dersch, R
   Lehrling, C
   Bevan, H
   Qiu, Y
   Lagrèze, WA
   Wynick, D
   Churchill, AJ
   Kehoe, P
   Harper, SJ
   Bates, DO
   Donaldson, LF
AF Beazley-Long, Nicholas
   Hua, Jing
   Jehle, Thomas
   Hulse, Richard P.
   Dersch, Rick
   Lehrling, Christina
   Bevan, Heather
   Qiu, Yan
   Lagreze, Wolf A.
   Wynick, David
   Churchill, Amanda J.
   Kehoe, Patrick
   Harper, Steven J.
   Bates, David O.
   Donaldson, Lucy F.
TI VEGF-A165b Is an Endogenous Neuroprotective Splice Isoform of
   Vascular Endothelial Growth Factor A in Vivo and in Vitro
SO AMERICAN JOURNAL OF PATHOLOGY
LA English
DT Article
ID ANGIOGENIC VEGF ISOFORM; GANGLION-CELL DEATH; GENE-TRANSFER;
   TUMOR-GROWTH; VEGF(165)B; SURVIVAL; EXPRESSION; VARIANT; NEURONS; MODEL
AB Vascular endothelial growth factor (VEGF) A is generated as two isoform families by alternative RNA splicing, represented by VEGF-A(165)a and VEGF-A(165)b. These isoforms have opposing actions on vascular permeability, angiogenesis, and vasodilatation. The proangiogenic VEGF-A(165)a isoform is neuroprotective in hippocampal, dorsal root ganglia, and retinal neurons, but its propermeabitity, vaso-dilatatory, and angiogenic properties limit its therapeutic usefulness. In contrast, a neuroprotective effect of endogenous VEGF-A(165)b on neurons would be advantageous for neurodegenerative pathologies. Endogenous expression of human and rat VEGF-A(165)b was detected in hippocampal and cortical neurons. VEGF-A(165)b formed a significant proportion of total VEGF-A in rat brain. Recombinant human VEGF-A(165)b exerted neuroprotective effects in response to multiple insults, including glutamatergic excitotoxicity in hippocampal neurons, chemotherapy-induced cytotoxicity of dorsal root ganglion neurons, and retinal ganglion cells (RGCs) in rat retinal ischemia-reperfusion injury in vivo. Neuroprotection was dependent on VEGFR2 and MEK1/2 activation but not on p38 or phosphatidylinositol 3 kinase activation. Recombinant human VEGF-A(165)b is a neuroprotective agent that effectively. protects both peripheral and central neurons in vivo and in vitro through VEGFR2, MEK1/2, and inhibition of caspase-3 induction. VEGF-A(165)b may be therapeutically useful for pathologies that involve neuronal damage, including hippocampal neurodegeneration, glaucoma diabetic retinopathy, and peripheral neuropathy. The endogenous nature of VEGF-A(165)b expression suggests that non-isoform-specific inhibition of VEGF-A (for antiangiogenic reasons) may be damaging to retinal and sensory neurons.
C1 [Beazley-Long, Nicholas; Hua, Jing; Bevan, Heather; Qiu, Yan; Harper, Steven J.; Bates, David O.] Univ Bristol, Sch Physiol & Pharmacol, Microvasc Res Labs, Bristol, Avon, England.
   [Hulse, Richard P.; Donaldson, Lucy F.] Univ Bristol, Sch Physiol & Pharmacol, Bristol, Avon, England.
   [Kehoe, Patrick] Univ Bristol, Dementia Res Grp, Sch Clin Sci, John James Labs, Bristol, Avon, England.
   [Jehle, Thomas; Lehrling, Christina; Lagreze, Wolf A.] Univ Freiburg, Univ Eye Hosp, D-79106 Freiburg, Germany.
   [Dersch, Rick; Wynick, David] Univ Hosp Freiburg, Dept Neurol, Freiburg, Germany.
   [Churchill, Amanda J.] Bristol Eye Hosp, Bristol BS1 2LX, Avon, England.
C3 University of Bristol; University of Bristol; University of Bristol;
   University of Freiburg; University of Freiburg; Bristol Eye Hospital
RP Bates, DO (corresponding author), Univ Nottingham, Div Preclin Oncol, Queens Med Ctr, D Floor West Block, Nottingham NG7 2UH, England.
EM david.bates@nottingham.ac.uk; lucy.donaldson@bris.ac.uk
RI Hulse, Richard/AAE-2924-2019; Beazley-Long, Nicholas/I-7131-2019; Kehoe,
   Patrick Gavin/P-8760-2018
OI Beazley-long, Nicholas/0000-0001-7342-2771; Donaldson,
   Lucy/0000-0002-4242-5790; Kehoe, Patrick Gavin/0000-0002-7542-1139;
   Hulse, Richard/0000-0002-5193-9822; Bates, David/0000-0003-4850-2360
FU Wellcome Trust [079736, 058083]; Richard Bright VEGF-A Research Trust;
   MRC [G1000863] Funding Source: UKRI
FX Supported by Wellcome Trust grants 079736 and 058083 and the Richard
   Bright VEGF-A Research Trust.
CR AHMED AKMF, 1995, DEV BRAIN RES, V85, P71, DOI 10.1016/0165-3806(94)00191-2
   Almasieh M, 2012, PROG RETIN EYE RES, V31, P152, DOI 10.1016/j.preteyeres.2011.11.002
   Bates DO, 2002, CANCER RES, V62, P4123
   Bevan HS, 2008, NEPHRON PHYSIOL, V110, P57, DOI 10.1159/000177614
   Chen WR, 2007, J PERIPHER NERV SYST, V12, P121, DOI 10.1111/j.1529-8027.2007.00131.x
   Elliott-Hunt CR, 2004, P NATL ACAD SCI USA, V101, P5105, DOI 10.1073/pnas.0304823101
   Foster RR, 2003, AM J PHYSIOL-RENAL, V284, pF1263, DOI 10.1152/ajprenal.00276.2002
   Glass CA, 2006, J PHYSIOL-LONDON, V572, P243, DOI 10.1113/jphysiol.2005.103127
   Gomes E, 2007, MOL CELL BIOCHEM, V305, P179, DOI 10.1007/s11010-007-9542-2
   Harper SJ, 2008, NAT REV CANCER, V8, P880, DOI 10.1038/nrc2505
   Harris S, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0035231
   Hobson MI, 2000, J ANAT, V197, P591, DOI 10.1046/j.1469-7580.2000.19740591.x
   Holmes FE, 2000, P NATL ACAD SCI USA, V97, P11563, DOI 10.1073/pnas.210221897
   Hua J, 2010, INVEST OPHTH VIS SCI, V51, P4282, DOI 10.1167/iovs.09-4360
   Hulse R, 2008, NEUROREPORT, V19, P825, DOI 10.1097/WNR.0b013e328300ee0a
   Hurwitz H, 2004, NEW ENGL J MED, V350, P2335, DOI 10.1056/NEJMoa032691
   Jehle T, 2008, INVEST OPHTH VIS SCI, V49, P1056, DOI 10.1167/iovs.07-1050
   Jin KL, 2000, J MOL NEUROSCI, V14, P197, DOI 10.1385/JMN:14:3:197
   Jin KL, 2000, P NATL ACAD SCI USA, V97, P10242, DOI 10.1073/pnas.97.18.10242
   Kawamura H, 2008, BLOOD, V112, P3638, DOI 10.1182/blood-2007-12-125856
   Kawamura H, 2008, CANCER RES, V68, P4683, DOI 10.1158/0008-5472.CAN-07-6577
   Kovacs Z, 1996, STROKE, V27, P1865, DOI 10.1161/01.STR.27.10.1865
   Lam TT, 1999, INVEST OPHTH VIS SCI, V40, P967
   Lambrechts D, 2003, NAT GENET, V34, P383, DOI 10.1038/ng1211
   Licht T, 2011, P NATL ACAD SCI USA, V108, P5081, DOI 10.1073/pnas.1007640108
   Lin GT, 2010, BJU INT, V105, P114, DOI 10.1111/j.1464-410X.2009.08647.x
   Magnussen AL, 2010, INVEST OPHTH VIS SCI, V51, P4273, DOI 10.1167/iovs.09-4296
   Matsuzaki H, 2001, FASEB J, V15, P1218, DOI 10.1096/fj.00-0495fje
   Nicoletti JN, 2008, NEUROSCIENCE, V151, P232, DOI 10.1016/j.neuroscience.2007.09.083
   Nishijima K, 2007, AM J PATHOL, V171, P53, DOI 10.2353/ajpath.2007.061237
   Oosthuyse B, 2001, NAT GENET, V28, P131, DOI 10.1038/88842
   Pritchard-Jones RO, 2007, BRIT J CANCER, V97, P223, DOI 10.1038/sj.bjc.6603839
   Qiu Y, 2010, J AM SOC NEPHROL, V21, P1498, DOI 10.1681/ASN.2009060617
   Rennel ES, 2008, BRIT J CANCER, V98, P1250, DOI 10.1038/sj.bjc.6604309
   Rennel ES, 2008, EUR J CANCER, V44, P1883, DOI 10.1016/j.ejca.2008.05.027
   Ropper AH, 2009, ANN NEUROL, V65, P386, DOI 10.1002/ana.21675
   Rosenfeld PJ, 2006, NEW ENGL J MED, V355, P1419, DOI 10.1056/NEJMoa054481
   Rosenstein JM, 2003, J NEUROSCI, V23, P11036
   Schratzberger P, 2001, J CLIN INVEST, V107, P1083, DOI 10.1172/JCI12188
   Schratzberger P, 2000, NAT MED, V6, P405, DOI 10.1038/74664
   SellesNavarro I, 1996, INVEST OPHTH VIS SCI, V37, P2002
   Sondell M, 1999, J NEUROSCI, V19, P5731, DOI 10.1523/JNEUROSCI.19-14-05731.1999
   Sondell M, 2001, NEUROREPORT, V12, P105, DOI 10.1097/00001756-200101220-00028
   Storkebaum E, 2004, BIOESSAYS, V26, P943, DOI 10.1002/bies.20092
   Suarez SC, 2006, CELL MOL LIFE SCI, V63, P2067, DOI 10.1007/s00018-006-6254-9
   Varey AHR, 2008, BRIT J CANCER, V98, P1366, DOI 10.1038/sj.bjc.6604308
   Walczak JS, 2005, NEUROSCIENCE, V132, P1093, DOI 10.1016/j.neuroscience.2005.02.010
   Whittles CE, 2002, MICROCIRCULATION, V9, P513, DOI 10.1038/sj.mn.7800164
   Wood JM, 2000, CANCER RES, V60, P2178
   Woolard J, 2004, CANCER RES, V64, P7822, DOI 10.1158/0008-5472.CAN-04-0934
   Yasuhara T, 2005, BRAIN RES, V1053, P10, DOI 10.1016/j.brainres.2005.05.027
   Zachary I, 2005, NEUROSIGNALS, V14, P207, DOI 10.1159/000088637
NR 52
TC 94
Z9 101
U1 0
U2 13
PU ELSEVIER SCIENCE INC
PI NEW YORK
PA STE 800, 230 PARK AVE, NEW YORK, NY 10169 USA
SN 0002-9440
EI 1525-2191
J9 AM J PATHOL
JI Am. J. Pathol.
PD SEP
PY 2013
VL 183
IS 3
BP 918
EP 929
DI 10.1016/j.ajpath.2013.05.031
PG 12
WC Pathology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Pathology
GA 210WP
UT WOS:000323866000025
PM 23838428
OA Green Accepted, Green Published, hybrid
DA 2025-04-10
ER

PT J
AU Jin, JP
   Root, DD
AF Jin, JP
   Root, DD
TI Modulation of troponin T molecular conformation and flexibility by metal
   ion binding to the NH2-terminal variable region
SO BIOCHEMISTRY
LA English
DT Article
ID COMPLETE NUCLEOTIDE-SEQUENCE; SKELETAL-MUSCLE; HYPERTROPHIC
   CARDIOMYOPATHY; CA2+ SENSITIVITY; NONPOLYMERIZABLE TROPOMYOSIN;
   STRUCTURAL ORGANIZATION; ADULT ISOFORMS; F-ACTIN; GENE; CONTRACTION
AB Troponin T (TnT) plays an allosteric signal transduction role in the actin thin-filament-based Ca2+-regulation of striated muscle contraction. Developmentally regulated alternative RNA splicing produces TnT isoforms differing in their NH2-terminal structure. Physical property variations of the NH2-terminal hypervariable region of TnT may have a role in tuning the Ca2+-sensitivity and overall cooperativity of the muscle. We have previously demonstrated that metal ion or monoclonal antibody binding to the NH2-terminal region can modulate the epitopic conformation and troponin I and tropomyosin binding affinity of TnT. To further establish the molecular basis of this conformational and functional modulation, we have characterized the NH2-terminal variable region-originated secondary conformational effect in TnT using fluorescence spectral analysis. The chicken fast skeletal muscle TnT isoform, TnT8e16, containing a cluster of transition-metal ion binding sites (Tx) in the NH2-terminal variable region was used in this study. TnT8e16 was titrated for Cu(II) binding-induced changes in fluorescence intensity and anisotropy of the COOH-domain Trp residues (W234, W236, and W285), which demonstrated considerable environmental sensitivity in TnT denaturation studies, Nonlinear Stern-Volmer plots of Trp quenching indicated a metal ion binding-induced conformational change in TnT, Fluorescence anisotropy changes upon metal ion binding indicated a decrease in the mobility of the Trp residues and an increase in the flexibility of fluorescein-labeled Cys263 in the COOH domain. These data support a model that the alternatively spliced NH2-terminal variable region of TnT modulates conformation and flexibility of other domains of the protein.
C1 Case Western Reserve Univ, Sch Med, Dept Phys & Biophys, Cleveland, OH 44106 USA.
   Univ N Texas, Dept Sci Biol, Div Biochem, Denton, TX 76203 USA.
C3 University System of Ohio; Case Western Reserve University; University
   of North Texas System; University of North Texas Denton
RP Case Western Reserve Univ, Sch Med, Dept Phys & Biophys, 10900 Euclid Ave, Cleveland, OH 44106 USA.
EM jxj12@po.cwru.edu
RI Jin, Jian-Ping/AAD-1149-2020
OI Jin, JP/0000-0001-9932-1063
FU NIAMS NIH HHS [AR44737] Funding Source: Medline
CR AKELLA AB, 1995, CIRC RES, V76, P600, DOI 10.1161/01.RES.76.4.600
   [Anonymous], 1993, PROTEINS STRUCTURES
   ARNOLD FH, 1991, SCIENCE, V252, P1796, DOI 10.1126/science.1648261
   BREITBART RE, 1986, J MOL BIOL, V188, P313, DOI 10.1016/0022-2836(86)90157-9
   BRIGGS MM, 1993, DEV BIOL, V158, P503, DOI 10.1006/dbio.1993.1208
   Bucher EA, 1999, J BIOL CHEM, V274, P17661, DOI 10.1074/jbc.274.25.17661
   Cantor CR., 1980, Biophysical Chemistry II. 10-2. Techniques for the study of biological structure and function
   COOPER TA, 1985, J BIOL CHEM, V260, P1140
   FISHER D, 1995, J BIOL CHEM, V270, P25455, DOI 10.1074/jbc.270.43.25455
   GOLDBERG ME, 1991, TRENDS BIOCHEM SCI, V16, P358, DOI 10.1016/0968-0004(91)90148-O
   HEELEY DH, 1987, J BIOL CHEM, V262, P9971
   Huang QQ, 1999, J PHYSIOL-LONDON, V520, P231, DOI 10.1111/j.1469-7793.1999.00231.x
   Huang QQ, 1999, GENE, V229, P1, DOI 10.1016/S0378-1119(99)00051-7
   Jha PK, 1996, BIOCHEMISTRY-US, V35, P16573, DOI 10.1021/bi9622433
   Jin JP, 2000, AM J PHYSIOL-CELL PH, V279, pC1067, DOI 10.1152/ajpcell.2000.279.4.C1067
   Jin JP, 1998, BIOCHEM BIOPH RES CO, V242, P540, DOI 10.1006/bbrc.1997.8006
   JIN JP, 1994, FEBS LETT, V341, P135, DOI 10.1016/0014-5793(94)80256-4
   JIN JP, 1988, J BIOL CHEM, V263, P7309
   JIN JP, 1992, J MOL BIOL, V227, P1269, DOI 10.1016/0022-2836(92)90540-Z
   LEAVIS PC, 1984, CRC CR REV BIOCH MOL, V16, P235, DOI 10.3109/10409238409108717
   MAK AS, 1983, J BIOL CHEM, V258, P4330
   Mukherjea P, 1999, BIOCHEMISTRY-US, V38, P13296, DOI 10.1021/bi9906120
   NOZAKI Y, 1990, ARCH BIOCHEM BIOPHYS, V277, P324, DOI 10.1016/0003-9861(90)90587-O
   Ogut O, 1999, AM J PHYSIOL-CELL PH, V276, pC1162, DOI 10.1152/ajpcell.1999.276.5.C1162
   Ogut O, 1996, BIOCHEMISTRY-US, V35, P16581, DOI 10.1021/bi961712y
   Ogut O, 1998, J BIOL CHEM, V273, P27858, DOI 10.1074/jbc.273.43.27858
   PAN BS, 1991, J BIOL CHEM, V266, P12432
   PEARLSTONE JR, 1982, J BIOL CHEM, V257, P587
   PEARLSTONE JR, 1985, CAN J BIOCHEM CELL B, V63, P212, DOI 10.1139/o85-030
   Perry SV, 1998, J MUSCLE RES CELL M, V19, P575
   Saba Z, 1996, CIRCULATION, V94, P472, DOI 10.1161/01.CIR.94.3.472
   SCHACHAT F, 1995, DEV BIOL, V171, P233, DOI 10.1006/dbio.1995.1274
   Schaertl S, 1995, BIOCHEMISTRY-US, V34, P15890, DOI 10.1021/bi00049a003
   SMILLIE LB, 1988, J BIOL CHEM, V263, P18816
   TOBACMAN LS, 1988, J BIOL CHEM, V263, P2668
   Tobacman LS, 1999, J BIOL CHEM, V274, P28363, DOI 10.1074/jbc.274.40.28363
   Tobacman LS, 1996, ANNU REV PHYSIOL, V58, P447, DOI 10.1146/annurev.ph.58.030196.002311
   Wang J, 1998, BIOCHEMISTRY-US, V37, P14519, DOI 10.1021/bi9812322
   Wang J, 1997, GENE, V193, P105, DOI 10.1016/S0378-1119(97)00100-5
   Watkins H, 1996, J CLIN INVEST, V98, P2456, DOI 10.1172/JCI119063
   WATKINS H, 1995, NEW ENGL J MED, V332, P1058, DOI 10.1056/NEJM199504203321603
   ZOT AS, 1987, ANNU REV BIOPHYS BIO, V16, P535
NR 42
TC 46
Z9 51
U1 0
U2 3
PU AMER CHEMICAL SOC
PI WASHINGTON
PA 1155 16TH ST, NW, WASHINGTON, DC 20036 USA
SN 0006-2960
J9 BIOCHEMISTRY-US
JI Biochemistry
PD SEP 26
PY 2000
VL 39
IS 38
BP 11702
EP 11713
DI 10.1021/bi9927437
PG 12
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 359DL
UT WOS:000089596200020
PM 10995238
DA 2025-04-10
ER

PT J
AU Tanaka, H
   Abe, K
   Kim, CH
AF Tanaka, H
   Abe, K
   Kim, CH
TI Cloning and expression of the quaking gene in the zebrafish embryo
SO MECHANISMS OF DEVELOPMENT
LA English
DT Article
DE quaking; KH domain; RNA binding; zebrafish; alternative splicing;
   myelination; paraxial mesoderm; homologue; development; nervous system;
   qkI; who/how/struthio; cardiac sac; pectoral finbud; zqk; tailbud;
   snail1; whole mount in situ hybridization; evolution; neural crest;
   somites; embryo; insertion; maternal; hypomyelination; adaxial cells;
   body trunk; gastrulation; neural keel; reverse transcription-polymerase
   chain reaction
ID RNA-BINDING; PROTEIN; PRODUCT; MOUSE
AB The responsible gene for hypomyelinating quaking deficiency, qkI, encoding a KK RNA binding protein, is expressed abundantly in the developing mouse nervous system, whereas who/how/struthio, a homologue of the qkI in Drosophila, is expressed predominantly in the mesoderm. Here we describe the isolation and early developmental expression of a zebrafish homologue of qkI. The zebrafish quaking cDNA, zqk, exhibits striking conservation with qkI across the coding region, accompanied by a unique 123 nucleotide insertion sequence. Maternal and zygotic zqk transcripts are ubiquitously distributed during cleavage and blastula periods, and then accumulate in the dorsal midline of the body trunk during gastrulation. During segmentation and pharyngula periods zqk transcripts are expressed in the neural tissue of the head region, and in the paraxial mesoderm of the body trunk. Subsequently they diminish until the hatching period, when they are expressed only in the cardiac sac and pectoral finbuds. We also found that the zqk transcript is alternatively spliced with the transcript containing a 123 nucleotide additional segment localized in neural tissue in the head region, but not in the paraxial mesoderm in the body trunk. The data suggest that the quaking gene family originated in the mesoderm and evolved to become expressed in the nervous system in lower vertebrates. The insertion of the 123 nucleotide sequence could be related to the acquisition of a neural function for the gene. (C) 1997 Elsevier Science Ireland Ltd.
C1 CUNY Mt Sinai Sch Med, Brookdale Ctr Mol Biol, New York, NY 10029 USA.
   Kumamoto Univ, Sch Med, Inst Mol Embryol & Genet, Kumamoto 860, Japan.
   Osaka Univ, Sch Med, Dept Pharmacol, Osaka, Japan.
C3 City University of New York (CUNY) System; Icahn School of Medicine at
   Mount Sinai; Kumamoto University; The University of Osaka
RP Tanaka, H (corresponding author), CUNY Mt Sinai Sch Med, Brookdale Ctr Mol Biol, Box 1126,Annenberg 25-245,1 Gustave L Levy Pl, New York, NY 10029 USA.
RI Kim, Cheol-Hee/F-6278-2013
OI Kim, Cheol-Hee/0000-0002-3019-0699
FU NINDS NIH HHS [NS 33165] Funding Source: Medline
CR Baehrecke EH, 1997, DEVELOPMENT, V124, P1323
   BENNETT WI, 1971, BIOL REPROD, V5, P30, DOI 10.1093/biolreprod/5.1.30
   CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
   CRUZALVAREZ M, 1987, J BIOL CHEM, V262, P13377
   Ebersole TA, 1996, NAT GENET, V12, P260, DOI 10.1038/ng0396-260
   HAMMERSCHMIDT M, 1993, DEVELOPMENT, V119, P1107
   Hardy RJ, 1996, J NEUROSCI, V16, P7941
   JONES AR, 1995, GENE DEV, V9, P1491, DOI 10.1101/gad.9.12.1491
   KIMMEL CB, 1995, DEV DYNAM, V203, P253, DOI 10.1002/aja.1002030302
   Lo PCH, 1997, DEV BIOL, V190, P241, DOI 10.1006/dbio.1997.8699
   SCHULTEMERKER S, 1992, DEVELOPMENT, V116, P1021
   SIDMAN RL, 1964, SCIENCE, V144, P309, DOI 10.1126/science.144.3616.309
   THISSE C, 1993, DEVELOPMENT, V119, P1203
   WONG G, 1992, CELL, V69, P551, DOI 10.1016/0092-8674(92)90455-L
   Zaffran S, 1997, DEVELOPMENT, V124, P2087
   Zorn AM, 1997, GENE DEV, V11, P2176, DOI 10.1101/gad.11.17.2176
NR 16
TC 21
Z9 25
U1 0
U2 3
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 0925-4773
J9 MECH DEVELOP
JI Mech. Dev.
PD DEC
PY 1997
VL 69
IS 1-2
BP 209
EP 213
DI 10.1016/S0925-4773(97)00164-0
PG 5
WC Developmental Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Developmental Biology
GA YU431
UT WOS:000071716400017
PM 9486543
DA 2025-04-10
ER

PT J
AU Biros, E
   Moran, CS
   Norman, PE
   Hankey, GJ
   Yeap, BB
   Almeida, OP
   Flicker, L
   White, R
   Jones, R
   Golledge, J
AF Biros, Erik
   Moran, Corey S.
   Norman, Paul E.
   Hankey, Graeme J.
   Yeap, Bu B.
   Almeida, Osvaldo P.
   Flicker, Leon
   White, Richard
   Jones, Rhondda
   Golledge, Jonathan
TI Association between the Advanced Glycosylation End Product-Specific
   Receptor Gene and Cardiovascular Death in Older Men
SO PLOS ONE
LA English
DT Article
ID INHIBITS MACROPHAGE ACTIVITY; ABDOMINAL AORTIC-ANEURYSM; SPLICE
   VARIANTS; CAROTID PLAQUE; RAGE GENE; INFLAMMATION; HMGB1; BINDING;
   HEALTH; ALPHA(V)BETA(3)-INTEGRIN
AB Advanced glycosylation end product-specific receptor (AGER) signaling has been implicated in atherosclerosis. The aim of this study was to evaluate whether a common genetic variation in the AGER gene is associated with cardiovascular (CV) death. We included 1304 older men who were genotyped for rs1035798: C>T, which is a single nucleotide polymorphism (SNP) mapped to the third intron of AGER. Cox proportional hazard analysis was used to estimate the association of rs1035798: C>T with CV death. In addition we analyzed total RNA extracted from carotid atherosclerosis biopsies of 18 patients that did or did not have recent symptoms of cerebral embolization by quantitative real-time reverse transcription PCR (qRT-PCR). The minor T-allele of rs1035798: C>T was found to be associated with CV death under dominant (HR = 1.43, 95% CI: 1.01-2.02, P = 0.04) and recessive (HR = 2.05, 95% CI: 1.11-3.81, P = 0.02) models of inheritance even after adjustment for traditional cardiovascular risk factors. No association was found between rs1035798: C>T and non-CV death. qRT-PCR results suggested that median relative expression of AGER isoform 1 and isoform 6 transcripts were approximately 6-(P = 0.01) and 2-fold (P = 0.02) greater, respectively, within carotid biopsies of symptomatic compared to asymptomatic patients. These data suggest that the minor (T) allele of rs1035798: C>T represents an independent susceptibility factor for CV death. The expression of AGER isoforms is different in atheroma from patients with recent symptoms. Further studies are needed to investigate if rs1035798: C>T influences the alternative splicing of AGER.
C1 [Biros, Erik; Moran, Corey S.; Jones, Rhondda; Golledge, Jonathan] James Cook Univ, Coll Med & Dent, Queensland Res Ctr Peripheral Vasc Dis, Townsville, Qld 4811, Australia.
   [Norman, Paul E.] Univ Western Australia, Sch Surg, Perth, WA 6009, Australia.
   [Hankey, Graeme J.; Yeap, Bu B.; Flicker, Leon] Univ Western Australia, Sch Med & Pharmacol, Perth, WA 6009, Australia.
   [Hankey, Graeme J.] Sir Charles Gairdner Hosp, Dept Neurol, Perth, WA, Australia.
   [Yeap, Bu B.] Fremantle Hosp, Dept Endocrinol, Perth, WA, Australia.
   [Yeap, Bu B.] Fiona Stanley Hosp, Dept Endocrinol, Perth, WA, Australia.
   [Almeida, Osvaldo P.] Univ Western Australia, Sch Psychiat & Clin Neurosci, Perth, WA 6009, Australia.
   [Almeida, Osvaldo P.; Flicker, Leon] Med Res Ctr, WA Ctr Hlth & Ageing, Perth, WA, Australia.
   [Almeida, Osvaldo P.] Royal Perth Hosp, Dept Psychiat, Perth, WA 6001, Australia.
   [Flicker, Leon] Royal Perth Hosp, Dept Geriatr Med, Perth, WA 6001, Australia.
   [White, Richard] Townsville Hosp, Dept Neurol, Townsville, Qld, Australia.
   [Golledge, Jonathan] Townsville Hosp, Dept Vasc & Endovasc Surg, Townsville, Qld, Australia.
C3 James Cook University; University of Western Australia; University of
   Western Australia; University of Western Australia; Sir Charles Gairdner
   Hospital; South Metropolitan Health Service; Fiona Stanley Fremantle
   Hospitals Group; Fremantle Hospital; South Metropolitan Health Service;
   Fiona Stanley Fremantle Hospitals Group; Fiona Stanley Hospital;
   University of Western Australia; University of Western Australia; East
   Metropolitan Health Service; Royal Perth Hospital; University of Western
   Australia; East Metropolitan Health Service; Royal Perth Hospital;
   Queensland Health; Townsville Hospital; Queensland Health; Townsville
   Hospital
RP Golledge, J (corresponding author), James Cook Univ, Coll Med & Dent, Queensland Res Ctr Peripheral Vasc Dis, Townsville, Qld 4811, Australia.
EM jonathan.golledge@jcu.edu.au
RI golledge, jonathan/I-2371-2013; Flicker, Leon/AAE-1530-2022; Norman,
   Paul/C-5485-2013; Almeida, Osvaldo/A-4925-2008; Hankey,
   Graeme/H-4968-2014; Jones, Rhondda/E-4853-2013
OI Yeap, Bu/0000-0002-7612-5892; Almeida, Osvaldo/0000-0002-8689-6199;
   Hankey, Graeme/0000-0002-6044-7328; golledge,
   jonathan/0000-0002-5779-8848; Flicker, Leon/0000-0002-3650-0475; Jones,
   Rhondda/0000-0002-1031-2863
FU Townsville Private Practice Trust Fund, Australia [RG04213]; National
   Health and Medical Research Council [1022752, 1021416, 1020955, 1003707,
   1000967]; National Heart Foundation of Australia; Queensland Government;
   National Health and Medical Research Council, Australia [1019921];
   Health and Medical Research Office, Queensland Government
FX The Townsville Private Practice Trust Fund
   (http://www.health.qld.gov.au/; RG04213), Australia, The National Health
   and Medical Research Council (http://www.nhmrc.gov.au/; 1022752,
   1021416, 1020955, 1003707 and 1000967), The National Heart Foundation of
   Australia (http://www.heartfoundation.org.au/), and The Queensland
   Government supported this work. JG holds a Practitioner Fellowship from
   the National Health and Medical Research Council, Australia (1019921),
   and a Senior Clinical Research Fellowship from the Health and Medical
   Research Office, Queensland Government.
CR [Anonymous], Global Status Report on Noncommunicable Diseases 2010
   [Anonymous], ANTHROPOMETRICA
   Barr ELM, 2009, INTERN MED J, V39, P49, DOI 10.1111/j.1445-5994.2008.01864.x
   Bierhaus A, 2005, J MOL MED, V83, P876, DOI 10.1007/s00109-005-0688-7
   Bierhaus A, 2006, CURR OPIN INVEST DR, V7, P985
   Bronte V, 2005, NAT REV IMMUNOL, V5, P641, DOI 10.1038/nri1668
   Caillier SJ, 2008, J IMMUNOL, V181, P5473, DOI 10.4049/jimmunol.181.8.5473
   Cipollone F, 2003, CIRCULATION, V108, P1070, DOI 10.1161/01.CIR.0000086014.80477.0D
   Desmet FO, 2009, NUCLEIC ACIDS RES, V37, DOI 10.1093/nar/gkp215
   Dupont WD, 1998, CONTROL CLIN TRIALS, V19, P589, DOI 10.1016/S0197-2456(98)00037-3
   Frazer KA, 2007, NATURE, V449, P851, DOI 10.1038/nature06258
   Friggeri A, 2010, AM J PHYSIOL-CELL PH, V299, pC1267, DOI 10.1152/ajpcell.00152.2010
   Goiledge J, 2008, EUR J VASC ENDOVASC, V35, P2, DOI 10.1016/j.ejvs.2007.09.004
   Golledge J, 2000, STROKE, V31, P774, DOI 10.1161/01.STR.31.3.774
   Golledge J, 2014, J NUTR HEALTH AGING
   Golledge J, 2007, CIRCULATION, V116, P2275, DOI 10.1161/CIRCULATIONAHA.107.717926
   Harja E, 2008, J CLIN INVEST, V118, P183, DOI 10.1172/JCI32703
   Herisson F, 2011, ATHEROSCLEROSIS, V216, P348, DOI 10.1016/j.atherosclerosis.2011.02.004
   Holman CDJ, 1999, AUST NZ J PUBL HEAL, V23, P453, DOI 10.1111/j.1467-842X.1999.tb01297.x
   HORI O, 1995, J BIOL CHEM, V270, P25752, DOI 10.1074/jbc.270.43.25752
   Hudson BI, 2008, FASEB J, V22, P1572, DOI 10.1096/fj.07-9909com
   Hull J, 2007, PLOS GENET, V3, P1009, DOI 10.1371/journal.pgen.0030099
   Hunter GC, 1999, J VASC SURG, V30, P36, DOI 10.1016/S0741-5214(99)70174-6
   Kierdorf K, 2013, J LEUKOCYTE BIOL, V94, P55, DOI 10.1189/jlb.1012519
   Kigerl KA, 2009, J NEUROSCI, V29, P13435, DOI 10.1523/JNEUROSCI.3257-09.2009
   Kokkola R, 2005, SCAND J IMMUNOL, V61, P1, DOI 10.1111/j.0300-9475.2005.01534.x
   Li SSY, 2003, BIOSTATISTICS, V4, P513, DOI 10.1093/biostatistics/4.4.513
   Mantovani A, 2004, TRENDS IMMUNOL, V25, P677, DOI 10.1016/j.it.2004.09.015
   Matzinger P, 2007, NAT IMMUNOL, V8, P11, DOI 10.1038/ni0107-11
   Mills CD, 2012, CRIT REV IMMUNOL, V32, P463, DOI 10.1615/CritRevImmunol.v32.i6.10
   Moore KJ, 2011, CELL, V145, P341, DOI 10.1016/j.cell.2011.04.005
   Najafi AH, 2013, DIS MODEL MECH, V6, P323, DOI 10.1242/dmm.009977
   Norman PE, 2009, INT J EPIDEMIOL, V38, P48, DOI 10.1093/ije/dyn041
   Norman PE, 2004, BRIT MED J, V329, P1259, DOI 10.1136/bmj.38272.478438.55
   Olsson S, 2013, EUR J NEUROL, V20, P991, DOI 10.1111/ene.12041
   Pisetsky DS, 2010, AM J PHYSIOL-CELL PH, V299, pC1253, DOI 10.1152/ajpcell.00397.2010
   Rossi A, 2006, INT J CARDIOL, V111, P263, DOI 10.1016/j.ijcard.2005.08.030
   Scaffidi P, 2002, NATURE, V418, P191, DOI 10.1038/nature00858
   Schlueter C, 2003, BBA-GENE STRUCT EXPR, V1630, P1, DOI 10.1016/j.bbaexp.2003.08.008
   Shaikh S, 2012, EUR J VASC ENDOVASC, V44, P491, DOI 10.1016/j.ejvs.2012.08.005
   Sheng Y., 2020, Global Atlason Cardiovascular Disease Prevention and Control: Published by theWorld Health Organization in Collaboration with the World Heart Federationand the World Stroke Organization
   Silvestre-Roig C, 2014, CIRC RES, V114, P214, DOI 10.1161/CIRCRESAHA.114.302355
   Tedgui A, 2005, VASC MED, V10, P45, DOI 10.1191/1358863x05vm589ra
   VanderWeele TJ, 2011, BIOMETRICS, V67, P1406, DOI 10.1111/j.1541-0420.2011.01619.x
   Wang J, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0050790
   Yan SF, 2009, ANN MED, V41, P408, DOI 10.1080/07853890902806576
   Yeramian A, 2006, EUR J IMMUNOL, V36, P1516, DOI 10.1002/eji.200535694
   Yonekura H, 2003, BIOCHEM J, V370, P1097, DOI 10.1042/BJ20021371
   Yuan HY, 2006, NUCLEIC ACIDS RES, V34, pW635, DOI 10.1093/nar/gkl236
NR 49
TC 12
Z9 12
U1 0
U2 2
PU PUBLIC LIBRARY SCIENCE
PI SAN FRANCISCO
PA 1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA
SN 1932-6203
J9 PLOS ONE
JI PLoS One
PD JUL 30
PY 2015
VL 10
IS 7
AR e0134475
DI 10.1371/journal.pone.0134475
PG 12
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA CO0JT
UT WOS:000358837700097
PM 26226616
OA Green Published, Green Accepted, Green Submitted, gold
DA 2025-04-10
ER

PT J
AU Payne, MC
   Zhang, HY
   Prosdocimo, T
   Joyce, KM
   Koga, Y
   Ikebe, M
   Fisher, SA
AF Payne, MC
   Zhang, HY
   Prosdocimo, T
   Joyce, KM
   Koga, Y
   Ikebe, M
   Fisher, SA
TI Myosin phosphatase isoform switching in vascular smooth muscle
   development
SO JOURNAL OF MOLECULAR AND CELLULAR CARDIOLOGY
LA English
DT Article
DE smooth muscle phenotype; cGMP signaling; alternative splicing
ID LIGHT-CHAIN PHOSPHATASE; RAT PORTAL-VEIN; PROTEIN PHOSPHATASE; CA2+
   SENSITIVITY; SUBUNIT; PURIFICATION; INNERVATION; EXPRESSION; RESISTANCE;
   BETA
AB We are using the myosin phosphatase targeting Subunit (MYPT1) its a model gene to study smooth muscle phenotypic diversity. Myosin phosphatase (MP) is the primary effector of smooth muscle relaxation, and MYPT1 is a key target of signals that regulate smooth muscle tone. In a model of portal hypertension we previously showed dynamic changes in the expression of MYPTI isoforms in the portal vein and upstream mesenteric artery. We hypothesized that this represents a reversion to the fetal phenotype characteristic of muscle hypertrophy. Here we Studied NIP during vascular smooth muscle phenotypic specification. Between postnatal days 6 and 12 the expression of MYPTI increased approximately twofold in portal vein with a similar increase in MP activity. MYPT1 switched from C-terminal leucine zipper (LZ) positive to LZ negative splice variant isoforms. This was concordant with a switch from sensitive (10(-7) M) to resistant to cGMP-mediated vascular relaxation. This is consistent with the model in which the MYPTI C-terminal LZ is required for cGMP-dependent activation of MP. Concordant changes in the expression of other contractile proteins were consistent with a switch from a slow-tonic to a fast-phasic contractile phenotype. In contrast aortic smooth muscle throughout development expressed the MYPTI LZ positive isoform and relaxed to cGMP. We propose that MP isoform switching during neonatal vascular smooth muscle phenotypic specification may determine changing vascular responses to NO/cGMP signaling in the transition from the fetal to the adult circulation. (c) 2005 Elsevier Ltd. All rights reserved.
C1 Case Western Reserve Sch Med, Dept Med, Cleveland, OH 44106 USA.
   Case Western Reserve Sch Med, Dept Physiol, Cleveland, OH 44106 USA.
   Univ Massachusetts, Dept Physiol, Worcester, MA 01605 USA.
C3 University System of Ohio; Case Western Reserve University; University
   System of Ohio; Case Western Reserve University; University of
   Massachusetts System; University of Massachusetts Worcester
RP Case Western Reserve Sch Med, Dept Med, 422 BRB,2109 Adelbert Rd, Cleveland, OH 44106 USA.
EM saf9@po.cwru.edu
RI Joyce, Kayla/AAP-2265-2020; fisher, steven/G-2630-2010; KOGA,
   YASUHIKO/V-3913-2019
OI KOGA, YASUHIKO/0000-0002-4974-9026
FU NHLBI NIH HHS [HL66171] Funding Source: Medline
CR Bruce L, 1997, EXP PHYSIOL, V82, P985, DOI 10.1113/expphysiol.1997.sp004084
   CHEN YH, 1994, FEBS LETT, V356, P51, DOI 10.1016/0014-5793(94)01231-8
   Chruscinski A, 2001, MOL PHARMACOL, V60, P955, DOI 10.1124/mol.60.5.955
   Damon DH, 2005, AM J PHYSIOL-HEART C, V288, pH2785, DOI 10.1152/ajpheart.00354.2004
   Dirksen WP, 2000, AM J PHYSIOL-CELL PH, V278, pC589, DOI 10.1152/ajpcell.2000.278.3.C589
   FELETOU M, 1989, BLOOD VESSELS, V26, P21
   Fisher SA, 1997, CIRC RES, V80, P885
   Gallagher PJ, 1997, J MUSCLE RES CELL M, V18, P1, DOI 10.1023/A:1018616814417
   Goehler LE, 1996, PEPTIDES, V17, P209, DOI 10.1016/0196-9781(95)02126-4
   GONG MC, 1992, J BIOL CHEM, V267, P14662
   GUNNING P, 1991, FASEB J, V5, P3064, DOI 10.1096/fasebj.5.15.1835946
   Hartshorne DJ, 2004, J BIOL CHEM, V279, P37211, DOI 10.1074/jbc.R400018200
   Huang QQ, 2004, J BIOL CHEM, V279, P597, DOI 10.1074/jbc.M308496200
   Johnson D, 1997, EUR J BIOCHEM, V244, P931, DOI 10.1111/j.1432-1033.1997.00931.x
   Khatri JJ, 2001, J BIOL CHEM, V276, P37250, DOI 10.1074/jbc.M105275200
   LJUNG B, 1979, ACTA PHYSIOL SCAND, V106, P271, DOI 10.1111/j.1748-1716.1979.tb06398.x
   MITSUI T, 1992, J BIOL CHEM, V267, P16727
   Molkentin JD, 2001, ANNU REV PHYSIOL, V63, P391, DOI 10.1146/annurev.physiol.63.1.391
   Nankervis CA, 2001, AM J PHYSIOL-GASTR L, V280, pG678, DOI 10.1152/ajpgi.2001.280.4.G678
   NANKERVIS CA, 1995, AM J PHYSIOL-GASTR L, V268, pG949, DOI 10.1152/ajpgi.1995.268.6.G949
   Nankervis CA, 2001, MICROCIRCULATION, V8, P377
   Nauli SM, 2001, AM J PHYSIOL-HEART C, V280, pH1019, DOI 10.1152/ajpheart.2001.280.3.H1019
   ODY M, 1993, CELL TISSUE RES, V272, P303, DOI 10.1007/BF00302735
   OWENS GK, 1995, PHYSIOL REV, V75, P487
   Payne MC, 2004, AM J PHYSIOL-HEART C, V286, pH1801, DOI 10.1152/ajpheart.00696.2003
   Schiaffino S, 1996, PHYSIOL REV, V76, P371, DOI 10.1152/physrev.1996.76.2.371
   SEKHAR KR, 1992, MOL PHARMACOL, V42, P103
   SHIRAZI A, 1994, J BIOL CHEM, V269, P31598
   SOMLYO AP, 1994, NATURE, V372, P231, DOI 10.1038/372231a0
   STAGE D, 1978, ACTA PHYSIOL SCAND, V102, P218, DOI 10.1111/j.1748-1716.1978.tb06065.x
   Surks HK, 1999, SCIENCE, V286, P1583, DOI 10.1126/science.286.5444.1583
   Tan I, 2001, J BIOL CHEM, V276, P21209, DOI 10.1074/jbc.M102615200
   THIEVENT A, 1995, CELL TISSUE RES, V279, P199, DOI 10.1007/BF00300704
   TSAO C, 1971, ANAT RECORD, V171, P457, DOI 10.1002/ar.1091710403
   Woodsome TP, 2001, J PHYSIOL-LONDON, V535, P553, DOI 10.1111/j.1469-7793.2001.t01-1-00553.x
NR 35
TC 40
Z9 49
U1 0
U2 1
PU ELSEVIER SCI LTD
PI OXFORD
PA THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND
SN 0022-2828
EI 1095-8584
J9 J MOL CELL CARDIOL
JI J. Mol. Cell. Cardiol.
PD FEB
PY 2006
VL 40
IS 2
BP 274
EP 282
DI 10.1016/j.yjmcc.2005.07.009
PG 9
WC Cardiac & Cardiovascular Systems; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology; Cell Biology
GA 014PF
UT WOS:000235491500009
PM 16356512
DA 2025-04-10
ER

PT J
AU Labeit, S
   Kolmerer, B
   Linke, WA
AF Labeit, S
   Kolmerer, B
   Linke, WA
TI The giant protein titin - Emerging roles in physiology and
   pathophysiology
SO CIRCULATION RESEARCH
LA English
DT Review
DE titin(connectin); elasticity; muscle ultrastructure; PEVK region
ID MONOCLONAL-ANTIBODIES; SKELETAL-MUSCLE; IMMUNOELECTRON MICROSCOPY;
   VERTEBRATE SKELETAL; MUSCULAR-DYSTROPHY; STRIATED-MUSCLE; ELASTIC
   PROTEIN; PASSIVE TENSION; CARDIAC-MUSCLE; CONNECTIN
AB Titin is a giant protein of vertebrate striated muscles (M(r), greater than or equal to 3000 kD). Its molecules are of filamentous shape and span from the Z disk to the hi line, thereby forming a third filament system of the sarcomere. This filament system is important for both the structural integrity of the myofibril and the passive tension response of a stretched muscle fiber. The determination of the cDNA sequence of human cardiac titin has shown that the cardiac titin filament is formed by a single, giant, 27 000-residue-long polypeptide chain. The titin strand has a modular structure. and different modular arrangements are expressed in different muscle tissue types by differential splicing. In the A band. the titin modules provide regular arrays of binding sites for other sarcomeric proteins, thereby contributing to a precise assembly of myofibrillar proteins in vivo. In the I band, two specific motif families. tandem-immunoglobulin domains and PEVK-rich sequences, confer extensibility to the titin filament. Expression of muscle tissue-specific length variants of the PEVK region by alternative splicing may explain the differences in the passive tension properties between various striated muscle types. Apart from the titin sequences with apparent functions for muscle structure and elasticity, the titin molecule contains a class of unique sequence insertions. Among these sequences are phosphorylation sites, a serine/threonine kinase domain, and binding sites for muscle-specific calpain pretenses. Thus, it is Likely that the titin filament also plays a role in myofibrillar signal transduction pathways.
C1 UNIV HEIDELBERG,INST PHYSIOL 2,D-6900 HEIDELBERG,GERMANY.
C3 Ruprecht Karls University Heidelberg
RP Labeit, S (corresponding author), EUROPEAN MOL BIOL LAB,MEYERHOFSTR 1,D-69012 HEIDELBERG,GERMANY.
RI Linke, Wolfgang/IXD-9988-2023
OI Linke, Wolfgang/0000-0003-0801-3773
CR AYMESOUTHGATE A, 1995, J CELL BIOL, V128, P393, DOI 10.1083/jcb.128.3.393
   BENIAN GM, 1989, NATURE, V342, P45, DOI 10.1038/342045a0
   Bennett PM, 1996, J MOL BIOL, V259, P896, DOI 10.1006/jmbi.1996.0367
   BRADY AJ, 1968, PHYSIOL REV, V48, P570, DOI 10.1152/physrev.1968.48.3.570
   BRADY AJ, 1991, PHYSIOL REV, V71, P413, DOI 10.1152/physrev.1991.71.2.413
   ERICKSON HP, 1994, P NATL ACAD SCI USA, V91, P10114, DOI 10.1073/pnas.91.21.10114
   FABIATO A, 1976, European Journal of Cardiology, V4, P13
   FULTON AB, 1993, J CELL SCI, V105, P867
   FURST DO, 1988, J CELL BIOL, V106, P1563, DOI 10.1083/jcb.106.5.1563
   GAUTEL M, 1995, EUR J BIOCHEM, V230, P752
   GAUTEL M, 1993, EMBO J, V12, P3827, DOI 10.1002/j.1460-2075.1993.tb06061.x
   Gautel M, 1996, FEBS LETT, V385, P11, DOI 10.1016/0014-5793(96)00338-9
   GRANZIER HL, 1995, BIOPHYS J, V68, P1027, DOI 10.1016/S0006-3495(95)80278-X
   GRANZIER HLM, 1993, BIOPHYS J, V65, P2141, DOI 10.1016/S0006-3495(93)81262-1
   HEIERHORST J, 1994, J BIOL CHEM, V269, P21086
   Heierhorst J, 1996, NATURE, V380, P636, DOI 10.1038/380636a0
   Helmes M, 1996, CIRC RES, V79, P619, DOI 10.1161/01.RES.79.3.619
   HOROWITS R, 1992, BIOPHYS J, V61, P392, DOI 10.1016/S0006-3495(92)81845-3
   ITOH Y, 1988, J BIOCHEM, V104, P504, DOI 10.1093/oxfordjournals.jbchem.a122499
   Kolmerer B, 1996, J MOL BIOL, V256, P556, DOI 10.1006/jmbi.1996.0108
   LABEIT S, 1992, EMBO J, V11, P1711, DOI 10.1002/j.1460-2075.1992.tb05222.x
   LABEIT S, 1995, SCIENCE, V270, P293, DOI 10.1126/science.270.5234.293
   LINKE WA, 1994, BIOPHYS J, V67, P782, DOI 10.1016/S0006-3495(94)80538-7
   Linke WA, 1996, J MOL BIOL, V261, P62, DOI 10.1006/jmbi.1996.0441
   MARUYAMA K, 1977, J BIOCHEM, V82, P317
   MARUYAMA K, 1994, BIOPHYS CHEM, V50, P73, DOI 10.1016/0301-4622(94)85021-6
   MATSUMURA K, 1990, J NEUROL SCI, V98, P155, DOI 10.1016/0022-510X(90)90256-M
   NAVE R, 1989, J CELL BIOL, V109, P2177, DOI 10.1083/jcb.109.5.2177
   Obermann WMJ, 1996, J CELL BIOL, V134, P1441, DOI 10.1083/jcb.134.6.1441
   Politou AS, 1996, J MOL BIOL, V255, P604, DOI 10.1006/jmbi.1996.0050
   RICHARD I, 1995, CELL, V81, P27, DOI 10.1016/0092-8674(95)90368-2
   SEBESTYEN MG, 1995, J CELL SCI, V108, P3029
   SOMMERVILLE LL, 1987, BIOCHEM BIOPH RES CO, V147, P986
   Sorimachi H, 1995, J BIOL CHEM, V270, P31158, DOI 10.1074/jbc.270.52.31158
   TRINICK J, 1994, TRENDS BIOCHEM SCI, V19, P405, DOI 10.1016/0968-0004(94)90088-4
   TROMBITAS K, 1995, CIRC RES, V77, P856, DOI 10.1161/01.RES.77.4.856
   WANG K, 1979, P NATL ACAD SCI USA, V76, P3698, DOI 10.1073/pnas.76.8.3698
   WANG K, 1991, P NATL ACAD SCI USA, V88, P7101, DOI 10.1073/pnas.88.16.7101
   Wang K, 1996, ADV BIOPHYS, V33, P123
   Yajima H, 1996, BIOCHEM BIOPH RES CO, V223, P160, DOI 10.1006/bbrc.1996.0862
NR 40
TC 209
Z9 235
U1 0
U2 16
PU AMER HEART ASSOC
PI DALLAS
PA 7272 GREENVILLE AVENUE, DALLAS, TX 75231-4596
SN 0009-7330
J9 CIRC RES
JI Circ.Res.
PD FEB
PY 1997
VL 80
IS 2
BP 290
EP 294
DI 10.1161/01.RES.80.2.290
PG 5
WC Cardiac & Cardiovascular Systems; Hematology; Peripheral Vascular
   Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology; Hematology
GA WE959
UT WOS:A1997WE95900015
PM 9012751
DA 2025-04-10
ER

PT J
AU Chambers, I
   Cozens, A
   Broadbent, J
   Robertson, M
   Lee, M
   Li, M
   Smith, A
AF Chambers, I
   Cozens, A
   Broadbent, J
   Robertson, M
   Lee, M
   Li, M
   Smith, A
TI Structure of the mouse leukaemia inhibitory factor receptor gene::
   regulated expression of mRNA encoding a soluble receptor isoform from an
   alternative 5′ untranslated region
SO BIOCHEMICAL JOURNAL
LA English
DT Article
ID STIMULATING FACTOR-RECEPTOR; TRUNCATED ERYTHROPOIETIN RECEPTOR;
   EMBRYONIC STEM-CELLS; MESSENGER-RNA; SIGNAL TRANSDUCER; LIF-RECEPTOR;
   BLASTOCYST IMPLANTATION; TARGETED DISRUPTION; ACTIVITY DIA/LIF;
   DIFFERENTIATION
AB The low-affinity leukaemia inhibitory factor receptor (LIF-R) is a component of cell-surface receptor complexes for the multifunctional cytokines leukaemia inhibitory factor, ciliary neurotrophic factor, oncostatin M and cardiotrophin-1. Both soluble and transmembrane forms of the protein have been described and several LIF-R mRNAs have been reported previously. In order to determine the coding potential of LIF-R mRNAs we have isolated and characterized the mouse LIF-R gene, mRNA encoding soluble LIF-R (sLIF-R) is formed by inclusion of an exon in which polyadenylation signals are provided by a B2 repeat, This exon is located centrally within the LIF-R gene but is excluded from the transmembrane LIF-R mRNA by alternative splicing, The transmembrane receptor is encoded by 19 exons distributed over 38 kb. Two distinct 5' non-coding exons have been identified, indicating the existence of alternative promoters. One of these is G/C rich and possesses a consensus initiator sequence as well as potential Spl binding sites. Expression of exon 1 from this promoter occurs in a wide variety of tissues, whereas expression of the alternative 5' untranslated region (exon la) is normally restricted to liver, the principal source of sLIF-R. During pregnancy expression of exon la becomes detectable also in the uterus. Expression of exon la increases dramatically during gestation and is accompanied by a similar quantitative rise in expression of sLIF-R mRNA. These findings establish that expression of LIF-R is under complex transcriptional control and indicate that regulated expression of the soluble cytokine receptor isoform may be due principally to an increase in the activity of a dedicated promoter.
C1 Univ Edinburgh, Ctr Genome Res, Edinburgh EH9 3JQ, Midlothian, Scotland.
   Western Gen Hosp, MRC, Human Genet Unit, Edinburgh EH4 2XU, Midlothian, Scotland.
C3 University of Edinburgh; University of Edinburgh
RP Chambers, I (corresponding author), Univ Edinburgh, Ctr Genome Res, Kings Bldg,W Mains Rd, Edinburgh EH9 3JQ, Midlothian, Scotland.
RI Chambers, Ian/H-5416-2011; Li, Meng/I-6941-2013; Smith,
   Adam/AAI-9966-2020
OI Chambers, Ian/0000-0003-2605-1597; Smith, Austin/0000-0002-3029-4682
CR Azizkhan Jane C., 1993, Critical Reviews in Eukaryotic Gene Expression, V3, P229
   BAZAN JF, 1990, P NATL ACAD SCI USA, V87, P6934, DOI 10.1073/pnas.87.18.6934
   BHATT H, 1991, P NATL ACAD SCI USA, V88, P11408, DOI 10.1073/pnas.88.24.11408
   BRAWERMAN G, 1981, CRC CR REV BIOCH MOL, V10, P1, DOI 10.3109/10409238109114634
   CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
   CHURCH GM, 1984, P NATL ACAD SCI-BIOL, V81, P1991, DOI 10.1073/pnas.81.7.1991
   FEINBERG AP, 1983, ANAL BIOCHEM, V132, P6, DOI 10.1016/0003-2697(83)90418-9
   FERNANDEZBOTRAN R, 1991, J EXP MED, V174, P673, DOI 10.1084/jem.174.3.673
   FROHMAN MA, 1988, P NATL ACAD SCI USA, V85, P8998, DOI 10.1073/pnas.85.23.8998
   FUKUNAGA R, 1990, P NATL ACAD SCI USA, V87, P8702, DOI 10.1073/pnas.87.22.8702
   GEARING DP, 1993, GENOMICS, V18, P148, DOI 10.1006/geno.1993.1441
   GEARING DP, 1991, EMBO J, V10, P2839, DOI 10.1002/j.1460-2075.1991.tb07833.x
   GEBALLE AP, 1994, TRENDS BIOCHEM SCI, V19, P159, DOI 10.1016/0968-0004(94)90277-1
   HILTON DJ, 1992, TRENDS BIOCHEM SCI, V17, P72, DOI 10.1016/0968-0004(92)90505-4
   INAZAWA J, 1991, GENOMICS, V10, P1075, DOI 10.1016/0888-7543(91)90202-P
   KINGSTON RE, 1990, CURRENT PROTOCOLS MO
   KISHIMOTO T, 1994, CELL, V76, P253, DOI 10.1016/0092-8674(94)90333-6
   KREIG PA, 1987, METHOD ENZYMOL, V155, P397
   KRUMLAUF R, 1987, DEVELOPMENT, V99, P603
   LAYTON MJ, 1992, P NATL ACAD SCI USA, V89, P8616, DOI 10.1073/pnas.89.18.8616
   LI M, 1995, NATURE, V378, P724, DOI 10.1038/378724a0
   NAKAGAWA Y, 1994, J BIOL CHEM, V269, P10905
   Nakamura Y, 1996, BIOCHEM BIOPH RES CO, V218, P205, DOI 10.1006/bbrc.1996.0036
   NAKAMURA Y, 1992, SCIENCE, V257, P1138, DOI 10.1126/science.257.5073.1138
   NAKAMURA Y, 1994, SCIENCE, V264, P588, DOI 10.1126/science.8160019
   Nichols J, 1996, MECH DEVELOP, V57, P123, DOI 10.1016/0925-4773(96)00531-X
   NICHOLS J, 1990, DEVELOPMENT, V110, P1341
   Owczarek CM, 1996, J BIOL CHEM, V271, P5495, DOI 10.1074/jbc.271.10.5495
   PADGETT RA, 1986, ANNU REV BIOCHEM, V55, P1119, DOI 10.1146/annurev.biochem.55.1.1119
   PELLETIER J, 1985, CELL, V40, P515, DOI 10.1016/0092-8674(85)90200-4
   PENNICA D, 1995, J BIOL CHEM, V270, P10915, DOI 10.1074/jbc.270.18.10915
   ROBERTSON M, 1993, DEV GENET, V14, P165, DOI 10.1002/dvg.1020140303
   ROSEJOHN S, 1994, BIOCHEM J, V300, P281, DOI 10.1042/bj3000281
   RYSKOV AP, 1983, NUCLEIC ACIDS RES, V11, P6541, DOI 10.1093/nar/11.18.6541
   SAITO M, 1992, J IMMUNOL, V148, P4066
   SETO Y, 1992, J IMMUNOL, V148, P259
   SHARP PA, 1981, CELL, V23, P643, DOI 10.1016/0092-8674(81)90425-6
   SHIELDS DC, 1995, CYTOKINE, V7, P679, DOI 10.1006/cyto.1995.0080
   SMITH AG, 1988, NATURE, V336, P688, DOI 10.1038/336688a0
   SMITH AG, 1992, DEV BIOL, V151, P339, DOI 10.1016/0012-1606(92)90174-F
   STAHL N, 1995, SCIENCE, V267, P1349, DOI 10.1126/science.7871433
   STEWART CL, 1992, NATURE, V359, P76, DOI 10.1038/359076a0
   TOMIDA M, 1993, FEBS LETT, V334, P193, DOI 10.1016/0014-5793(93)81710-H
   TOMIDA M, 1995, J BIOCHEM-TOKYO, V117, P1228, DOI 10.1093/oxfordjournals.jbchem.a124848
   TONMIDA M, 1994, J BIOCHEM-TOKYO, V155, P557
   WARE CB, 1995, DEVELOPMENT, V121, P1283
   WILLIAMS RL, 1988, NATURE, V336, P684, DOI 10.1038/336684a0
   YAMAMORI T, 1994, J PHYSIOLOGY-PARIS, V88, P165, DOI 10.1016/0928-4257(94)90002-7
   YOSHIDA K, 1994, MECH DEVELOP, V45, P163, DOI 10.1016/0925-4773(94)90030-2
   Yoshida K, 1996, P NATL ACAD SCI USA, V93, P407, DOI 10.1073/pnas.93.1.407
NR 50
TC 20
Z9 22
U1 0
U2 0
PU PORTLAND PRESS
PI LONDON
PA 59 PORTLAND PLACE, LONDON, ENGLAND W1N 3AJ
SN 0264-6021
J9 BIOCHEM J
JI Biochem. J.
PD DEC 15
PY 1997
VL 328
BP 879
EP 888
DI 10.1042/bj3280879
PN 3
PG 10
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA YN845
UT WOS:000071213800023
PM 9396734
OA Green Published
DA 2025-04-10
ER

PT J
AU Ottenheijm, CAC
   Heunks, LMA
   Hafmans, T
   van der Ven, PFM
   Benoist, C
   Zhou, HH
   Labeit, S
   Granzier, HL
   Dekhuijzen, PNR
AF Ottenheijm, CAC
   Heunks, LMA
   Hafmans, T
   van der Ven, PFM
   Benoist, C
   Zhou, HH
   Labeit, S
   Granzier, HL
   Dekhuijzen, PNR
TI Titin and diaphragm dysfunction in chronic obstructive pulmonary disease
SO AMERICAN JOURNAL OF RESPIRATORY AND CRITICAL CARE MEDICINE
LA English
DT Article
DE chronic obstructive pulmonary disease; diaphragm; single-fiber
   stiffness; titin; transcript studies
ID VERTEBRATE SKELETAL; ISOFORM EXPRESSION; PASSIVE STIFFNESS;
   GENE-EXPRESSION; CARDIAC TITIN; Z-LINE; PROTEIN; ADAPTATION; FILAMENTS;
   NEBULIN
AB Rationale: Recently, we have shown that Ca2+-activated force generation in diaphragm single fibers is impaired in patients with mild to moderate chronic obstructive pulmonary disease (COPD). For optimal active-force generation, the passive elasticity provided by titin is indispensable.
   Objectives: In the present study, we determined the passive-tension-length relations of single fibers of patients with mild to moderate COPD, hypothesizing that passive-elastic properties of diaphragm fibers are compromised.
   Methods: Passive-tension-length relations were determined in diaphragm fibers from patients with and without COPD (predicted mean FEV1, 76 and 102%, respectively). In diaphragm homogenates titin expression was studied at the protein level by gel electrophoresis and at the transcript level by using a novel titin exon microarray.
   Results: Diaphragm fibers from patients with COPD generate less passive tension on stretch. Titin content in the diaphragm did not differ between patients with and without COPD. However, titin exon transcript studies revealed up-regulation of seven exons, which code for spring elements in the elastic segment rich in proline, glutamate, valine, and lysine. Immunofluorescence analysis indicated elevated protein expression of the up-regulated splice variant in the COPD diaphragm. Simulation studies on titin molecules including the amino acids encoded by the seven up-regulated exons predicted reduced passive-tension generation on molecule stretch.
   Conclusions: Passive-tension generation of diaphragm single fibers is reduced in patients with COPD. Our results suggest that alternative splicing of the titin gene, resulting in increased length of the elastic segment rich in proline, glutamate, valine, and lysine, is involved. Interestingly, these changes occur already in patients with mild to moderate COPD.
C1 Univ Nijmegen St Radboud Hosp, Med Ctr, Dept Pulm Dis Biochem, NCMLS,Inst Fundamental & Clin Human Movement Sci, NL-6500 HB Nijmegen, Netherlands.
   Univ Bonn, Dept Mol Cell Biol, D-5300 Bonn, Germany.
   Univ Klinikum Mannheim, Inst Anasthesiol & Operat Intensivmed, Mannheim, Germany.
   Washington State Univ, Dept Vet & Comparat Anat Pharmacol & Physiol, Pullman, WA 99164 USA.
C3 Radboud University Nijmegen; University of Bonn; Ruprecht Karls
   University Heidelberg; Washington State University
RP Univ Nijmegen St Radboud Hosp, Med Ctr, Dept Pulm Dis Biochem, NCMLS,Inst Fundamental & Clin Human Movement Sci, 454,POB 9101, NL-6500 HB Nijmegen, Netherlands.
EM r.dekhuijzen@long.umcn.nl
RI Dekhuijzen, P/H-8024-2014; Heunks, Leo/L-4370-2015
OI van der Ven, Peter/0000-0002-9750-8913
FU NHLBI NIH HHS [HL61497] Funding Source: Medline
CR Bang ML, 2001, CIRC RES, V89, P1065, DOI 10.1161/hh2301.100981
   BEGIN P, 1991, AM REV RESPIR DIS, V143, P905, DOI 10.1164/ajrccm/143.5_Pt_1.905
   Cazorla O, 2001, CIRC RES, V88, P1028, DOI 10.1161/hh1001.090876
   Celli BR, 2004, EUR RESPIR J, V23, P932, DOI 10.1183/09031936.04.00014304
   Doucet M, 2004, EUR RESPIR J, V24, P971, DOI 10.1183/09031936.04.00020204
   Freiburg A, 2000, CIRC RES, V86, P1114
   FURST DO, 1988, J CELL BIOL, V106, P1563, DOI 10.1083/jcb.106.5.1563
   Granzier H, 2002, J PHYSIOL-LONDON, V541, P335, DOI 10.1113/jphysiol.2001.014381
   Granzier HL, 2004, CIRC RES, V94, P284, DOI 10.1161/01.RES.0000117769.88862.F8
   GRANZIER HLM, 1993, BIOPHYS J, V65, P2141, DOI 10.1016/S0006-3495(93)81262-1
   HOROWITS R, 1987, J CELL BIOL, V105, P2217, DOI 10.1083/jcb.105.5.2217
   HOROWITS R, 1986, NATURE, V323, P160, DOI 10.1038/323160a0
   KRUGER M, 1991, J CELL BIOL, V115, P97, DOI 10.1083/jcb.115.1.97
   Labeit D, 2003, P NATL ACAD SCI USA, V100, P13716, DOI 10.1073/pnas.2235652100
   Laghi F, 2003, AM J RESP CRIT CARE, V168, P10, DOI 10.1164/rccm.2206020
   Lahmers S, 2004, CIRC RES, V94, P505, DOI 10.1161/01.RES.0000115522.52554.86
   Lange S, 2005, SCIENCE, V308, P1599, DOI 10.1126/science.1110463
   Levine S, 1997, NEW ENGL J MED, V337, P1799, DOI 10.1056/NEJM199712183372503
   Levine S, 2003, AM J RESP CRIT CARE, V168, P706, DOI 10.1164/rccm.200209-1070OC
   Levine S, 2002, J APPL PHYSIOL, V92, P1205, DOI 10.1152/japplphysiol.00116.2001
   Makarenko I, 2004, CIRC RES, V95, P708, DOI 10.1161/01.RES.0000143901.37063.2f
   McElhinny AS, 2003, TRENDS CARDIOVAS MED, V13, P195, DOI 10.1016/S1050-1738(03)00076-8
   Mercadier JJ, 1998, AM J PHYSIOL-LUNG C, V274, pL527, DOI 10.1152/ajplung.1998.274.4.L527
   Nagueh SF, 2004, CIRCULATION, V110, P155, DOI 10.1161/01.CIR.0000135591.37759.AF
   Orozco-Levi M, 1999, EUR RESPIR J, V13, P371, DOI 10.1183/09031936.99.13237199
   Orozco-Levi M, 2001, AM J RESP CRIT CARE, V164, P1734, DOI 10.1164/ajrccm.164.9.2011150
   Ottenheijm CAC, 2005, AM J RESP CRIT CARE, V172, P200, DOI 10.1164/rccm.200502-262OC
   OTTENHEIJM CAC, 2005, P AM THORAC SOC, V2, pA530
   Pauwels Romain A., 2001, American Journal of Respiratory and Critical Care Medicine, V163, P1256
   Tskhovrebova L, 2003, NAT REV MOL CELL BIO, V4, P679, DOI 10.1038/nrm1198
   WANG K, 1980, P NATL ACAD SCI-BIOL, V77, P3254, DOI 10.1073/pnas.77.6.3254
   WANG K, 1991, P NATL ACAD SCI USA, V88, P7101, DOI 10.1073/pnas.88.16.7101
   WANG SM, 1985, J MUSCLE RES CELL M, V6, P293, DOI 10.1007/BF00713171
   Watanabe K, 2002, J BIOL CHEM, V277, P11549, DOI 10.1074/jbc.M200356200
   Wu YM, 2002, CIRCULATION, V106, P1384, DOI 10.1161/01.CIR.0000029804.61510.02
   Zielinski J, 1997, Monaldi Arch Chest Dis, V52, P43
NR 36
TC 65
Z9 72
U1 0
U2 4
PU AMER THORACIC SOC
PI NEW YORK
PA 25 BROADWAY, 18 FL, NEW YORK, NY 10004 USA
SN 1073-449X
EI 1535-4970
J9 AM J RESP CRIT CARE
JI Am. J. Respir. Crit. Care Med.
PD MAR 1
PY 2006
VL 173
IS 5
BP 527
EP 534
DI 10.1164/rccm.200507-1056OC
PG 8
WC Critical Care Medicine; Respiratory System
WE Science Citation Index Expanded (SCI-EXPANDED)
SC General & Internal Medicine; Respiratory System
GA 016KK
UT WOS:000235618900009
PM 16339921
OA Green Submitted, Green Accepted, Green Published
DA 2025-04-10
ER

PT J
AU Hegele, RA
   Harris, SB
   Hanley, AJG
   Cao, HN
   Zinman, B
AF Hegele, RA
   Harris, SB
   Hanley, AJG
   Cao, HN
   Zinman, B
TI G protein β3 subunit gene variant and blood pressure variation in
   Canadian Oji-Cree
SO HYPERTENSION
LA English
DT Article
DE ion channels; hypertension, genetic; linkage disequilibrium; genetics
ID IMMORTALIZED LYMPHOBLASTS; ESSENTIAL-HYPERTENSION; PLASMA-LIPOPROTEINS;
   ISOLATE
AB The subunits of the heterotrimeric G proteins are attractive candidate gene products for both susceptibility to essential hypertension and interindividual variation in blood pressure. There is alternative splicing of exon 9 of the gene encoding the beta 3 subunit of heterotrimeric G proteins (GNB3) associated with a C-->T change at nucleotide 825, which activates a cryptic splice site. The 825T allele results in a gene product that is 41 amino acids smaller than the wild-type gene product. G protein heterotrimers containing the shorter variant are more reactive than those containing the wild. type, and the 825T allele appears to be associated with essential hypertension. To evaluate whether this variant is associated with hypertension or blood pressure in other human samples, we genotyped 447 young adult Oji-Cree for the GNB3 C825T variation. We found that the frequency of the GNB3 825T allele was 0.501 in the Oji-Cree, which is considerably higher than the frequency observed in whites. Furthermore, genetic variation of the GNB3 nucleotide 825 was significantly associated with variation in systolic pressure but not diastolic pressure. Specifically, subjects with the 825T/T genotype had significantly lower systolic pressure than subjects with the 825C/T and 825C/C genotypes; the association was independent of sex. Furthermore, the 825T allele frequency tended to be higher in subjects who took antihypertensive medications than in subjects who did not (0.571 versus 0.496; P=NS), although this young sample had relatively few subjects with hypertension. The findings support an association of variation in this gene with Variation in blood pressure.
C1 John P Robarts Res Inst, Blackburn Cardiovasc Genet Lab, London, ON N6A 5K8, Canada.
   Univ Western Ontario, Dept Med, London, ON, Canada.
   Univ Western Ontario, Thames Valley Family Practice Res Unit, London, ON, Canada.
   Univ Toronto, Dept Med, Toronto, ON, Canada.
   Mt Sinai Hosp, Samuel Lunenfeld Res Inst, Toronto, ON M5G 1X5, Canada.
C3 Western University (University of Western Ontario); University Western
   Ontario Hospital; Western University (University of Western Ontario);
   Western University (University of Western Ontario); University of
   Toronto; University of Toronto; Sinai Health System Toronto; Lunenfeld
   Tanenbaum Research Institute
RP Hegele, RA (corresponding author), John P Robarts Res Inst, Blackburn Cardiovasc Genet Lab, 406-100 Perth Dr, London, ON N6A 5K8, Canada.
RI Hegele, Robert/G-3301-2011; Zinman, Bernard/E-7266-2013
FU NIDDK NIH HHS [1-R21-DK44597-01] Funding Source: Medline
CR [Anonymous], 1987, SAS STAT GUID PERS C
   HEGELE RA, 1995, ARTERIOSCL THROM VAS, V15, P861, DOI 10.1161/01.ATV.15.7.861
   Hegele RA, 1997, HYPERTENSION, V29, P1073, DOI 10.1161/01.HYP.29.5.1073
   HEGELE RA, 1994, CIRCULATION, V90, P2207, DOI 10.1161/01.CIR.90.5.2207
   HEGELE RA, 1995, ARTERIOSCL THROM VAS, V15, P89, DOI 10.1161/01.ATV.15.1.89
   HEGELE RA, 1994, ARTERIOSCLER THROMB, V14, P671, DOI 10.1161/01.ATV.14.5.671
   MACLEAN DR, 1992, CAN MED ASSOC J, V146, P1969
   Pietruck F, 1996, CIRC RES, V79, P974, DOI 10.1161/01.RES.79.5.974
   ROSSKOPF D, 1993, J CLIN INVEST, V92, P2553, DOI 10.1172/JCI116865
   SIFFERT W, 1995, J CLIN INVEST, V96, P759, DOI 10.1172/JCI118120
   Siffert W, 1998, NAT GENET, V18, P45, DOI 10.1038/ng0198-45
   WILLIAMS RR, 1994, ATHEROSCLEROSIS, V10, P856
NR 12
TC 70
Z9 80
U1 0
U2 0
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA 227 EAST WASHINGTON SQ, PHILADELPHIA, PA 19106 USA
SN 0194-911X
J9 HYPERTENSION
JI Hypertension
PD OCT
PY 1998
VL 32
IS 4
BP 688
EP 692
DI 10.1161/01.HYP.32.4.688
PG 5
WC Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology
GA 131TZ
UT WOS:000076592500011
PM 9774364
OA Bronze
DA 2025-04-10
ER

PT J
AU Kelaini, S
   Chan, CE
   Cornelius, VA
   Margariti, A
AF Kelaini, Sophia
   Chan, Celine
   Cornelius, Victoria A.
   Margariti, Andriana
TI RNA-Binding Proteins Hold Key Roles in Function, Dysfunction, and
   Disease
SO BIOLOGY-BASEL
LA English
DT Review
DE RNA binding protein; splicing factor; translation regulator; disease;
   stress granules
ID GENOME-WIDE ASSOCIATION; LONG NONCODING RNAS; MESSENGER-RNA;
   POSTTRANSCRIPTIONAL REGULATION; ALTERNATIVE POLYADENYLATION; CANCER;
   MUTATIONS; TRANSLATION; OLIGONUCLEOTIDE; MECHANISMS
AB Simple Summary
   Chronic hyperglycemia manifests in a variety of different micro- and macrovascular disorders such as diabetes mellitus and cardiovascular disease and has been shown to have links to post-transcriptional dysregulation. Equally, the development and progress of other devastating disorders such as tumorigenesis and neurodegenerative disease have also been associated with dysfunction of molecules involved in epigenetics such as RNA-binding proteins. Recent advances, especially on an analytical systemic level, have revealed new roles for these proteins and their contribution in maintaining the balance between normal function and dysfunction/disease.
   RNA-binding proteins (RBPs) are multi-faceted proteins in the regulation of RNA or its RNA splicing, localisation, stability, and translation. Amassing proof from many recent and dedicated studies reinforces the perception of RBPs exerting control through differing expression levels, cellular localization and post-transcriptional alterations. However, since the regulation of RBPs is reliant on the micro-environment and events like stress response and metabolism, their binding affinities and the resulting RNA-RBP networks may be affected. Therefore, any misregulation and disruption in the features of RNA and its related homeostasis can lead to a number of diseases that include diabetes, cardiovascular disease, and other disorders such as cancer and neurodegenerative diseases. As such, correct regulation of RNA and RBPs is crucial to good health as the effect RBPs exert through loss of function can cause pathogenesis. In this review, we will discuss the significance of RBPs and their typical function and how this can be disrupted in disease.
C1 [Kelaini, Sophia; Chan, Celine; Cornelius, Victoria A.; Margariti, Andriana] Queens Univ Belfast, Wellcome Wolfson Inst Expt Med, Sch Med Dent & Biomed Sci, 97 Lisburn Rd, Belfast BT9 7BL, Antrim, North Ireland.
C3 Queens University Belfast
RP Margariti, A (corresponding author), Queens Univ Belfast, Wellcome Wolfson Inst Expt Med, Sch Med Dent & Biomed Sci, 97 Lisburn Rd, Belfast BT9 7BL, Antrim, North Ireland.
EM s.kelaini@qub.ac.uk; cchan10@qub.ac.uk; vcornelius01@qub.ac.uk;
   a.margariti@qub.ac.uk
OI , Sophia/0000-0002-4597-6248; Cornelius, Victoria/0000-0002-1042-6406
FU British Heart Foundation [PG/18/29/33731]
FX This research was funded by British Heart Foundation grant number
   PG/18/29/33731.
CR Abdelmohsen K, 2017, RNA BIOL, V14, P361, DOI 10.1080/15476286.2017.1279788
   Abramzon YA, 2020, FRONT NEUROSCI-SWITZ, V14, DOI 10.3389/fnins.2020.00042
   Aslam N, 2011, J BIOL CHEM, V286, P3767, DOI 10.1074/jbc.M110.168757
   Balzeau J, 2017, FRONT GENET, V8, P1, DOI 10.3389/fgene.2017.00031
   Barmada SJ, 2014, NAT CHEM BIOL, V10, P677, DOI 10.1038/nchembio.1563
   Belzil VV, 2013, MOL CELL NEUROSCI, V56, P406, DOI 10.1016/j.mcn.2012.12.006
   Biamonti G, 2014, SEMIN CELL DEV BIOL, V32, P30, DOI 10.1016/j.semcdb.2014.03.016
   Brosseau JP, 2014, RNA, V20, P189, DOI 10.1261/rna.042168.113
   BUCKANOVICH RJ, 1993, NEURON, V11, P657, DOI 10.1016/0896-6273(93)90077-5
   Chen CYA, 2013, ADV EXP MED BIOL, V768, P183, DOI 10.1007/978-1-4614-5107-5_11
   Chen HJ, 2016, BRAIN, V139, P1417, DOI 10.1093/brain/aww028
   Congrains A, 2013, INT J MOL SCI, V14, P1278, DOI 10.3390/ijms14011278
   Courchaine EM, 2016, EMBO J, V35, P1603, DOI 10.15252/embj.201593517
   Dang H, 2017, CANCER CELL, V32, P101, DOI 10.1016/j.ccell.2017.06.002
   Degrauwe N, 2016, GENE DEV, V30, P2459, DOI 10.1101/gad.287540.116
   Dhatariya K, 2018, THER ADV ENDOCRINOL, V10, DOI 10.1177/2042018818807599
   Duffy AG, 2016, INT J CANCER, V139, P1648, DOI 10.1002/ijc.30199
   Dvinge H, 2016, NAT REV CANCER, V16, P413, DOI 10.1038/nrc.2016.51
   Erson-Bensan AE, 2016, MOL CANCER RES, V14, P507, DOI 10.1158/1541-7786.MCR-15-0489
   Garneau NL, 2007, NAT REV MOL CELL BIO, V8, P113, DOI 10.1038/nrm2104
   Gibbings DJ, 2009, NAT CELL BIOL, V11, P1143, DOI 10.1038/ncb1929
   Gomes CPD, 2020, CIRCULATION, V141, P313, DOI 10.1161/CIRCULATIONAHA.119.042474
   Gorkovskiy A, 2017, P NATL ACAD SCI USA, V114, pE4193, DOI 10.1073/pnas.1704016114
   Govindaraju Suman, 2013, World J Biol Chem, V4, P111, DOI 10.4331/wjbc.v4.i4.111
   He RZ, 2019, GENES DIS, V6, P6, DOI 10.1016/j.gendis.2019.01.003
   Hsieh AC, 2010, CLIN CANCER RES, V16, P4914, DOI 10.1158/1078-0432.CCR-10-0433
   Huang YJ, 2016, RAPID COMMUN MASS SP, V30, P1549, DOI 10.1002/rcm.7586
   Jackrel ME, 2014, CELL, V156, P170, DOI 10.1016/j.cell.2013.11.047
   Jeyabal P, 2016, BIOCHEM BIOPH RES CO, V471, P423, DOI 10.1016/j.bbrc.2016.02.065
   Johnson JO, 2014, NAT NEUROSCI, V17, P664, DOI 10.1038/nn.3688
   Jonas K, 2020, INT J MOL SCI, V21, DOI 10.3390/ijms21082969
   Kang D, 2020, CANCERS, V12, DOI 10.3390/cancers12092699
   Kim HJ, 2013, NATURE, V495, P467, DOI 10.1038/nature11922
   Kristensen LS, 2018, ONCOGENE, V37, P555, DOI 10.1038/onc.2017.361
   Lai WS, 2000, J BIOL CHEM, V275, P17827, DOI 10.1074/jbc.M001696200
   Langa KM, 2017, JAMA INTERN MED, V177, P51, DOI 10.1001/jamainternmed.2016.6807
   Leon BM, 2015, WORLD J DIABETES, V6, P1246, DOI 10.4239/wjd.v6.i13.1246
   Li B, 2017, BLOOD, V130
   Li YR, 2013, J CELL BIOL, V201, P361, DOI 10.1083/jcb.201302044
   Ling SC, 2013, NEURON, V79, P416, DOI 10.1016/j.neuron.2013.07.033
   Liu EY, 2017, DIS MODEL MECH, V10, P508, DOI 10.1242/dmm.028613
   Liu JY, 2014, CELL DEATH DIS, V5, DOI 10.1038/cddis.2014.466
   Liu SM, 2020, CLIN SCI, V134, P1433, DOI 10.1042/CS20200193
   Liu-Yesucevitz L, 2011, J NEUROSCI, V31, P16086, DOI 10.1523/JNEUROSCI.4105-11.2011
   Mackenzie IRA, 2010, LANCET NEUROL, V9, P995, DOI 10.1016/S1474-4422(10)70195-2
   Milne CA, 1999, CURR BIOL, V9, P1243, DOI 10.1016/S0960-9822(99)80504-1
   Mobasseri M, 2020, HEALTH PROMOT PERSPE, V10, P98, DOI 10.34172/hpp.2020.18
   Modic M, 2013, MOL CELL NEUROSCI, V56, P429, DOI 10.1016/j.mcn.2013.04.002
   Mohibi S, 2019, PHARMACOL THERAPEUT, V203, DOI 10.1016/j.pharmthera.2019.07.001
   Mongelard F, 2010, CURR OPIN MOL THER, V12, P107
   Moore KS, 2018, FRONT PHYSIOL, V9, DOI 10.3389/fphys.2018.00910
   Nagaoka K, 2016, ONCOGENE, V35, P2893, DOI 10.1038/onc.2015.350
   Nagaoka K, 2012, NAT COMMUN, V3, DOI 10.1038/ncomms1678
   Nilsen TW, 2010, NATURE, V463, P457, DOI 10.1038/nature08909
   Nussbacher JK, 2019, NEURON, V102, P294, DOI 10.1016/j.neuron.2019.03.014
   Nutter CA, 2016, CELL REP, V15, P2200, DOI 10.1016/j.celrep.2016.05.002
   Palangat M, 2019, GENE DEV, V33, P482, DOI 10.1101/gad.319590.118
   Perron G, 2018, CELL REP, V23, P1639, DOI 10.1016/j.celrep.2018.04.031
   Puthanveetil P, 2015, J CELL MOL MED, V19, P1418, DOI 10.1111/jcmm.12576
   Qin H, 2020, J HEMATOL ONCOL, V13, DOI 10.1186/s13045-020-00927-w
   Qiu GZ, 2016, BIOCHEM BIOPH RES CO, V471, P135, DOI 10.1016/j.bbrc.2016.01.164
   Quattrone A, 2019, ISCIENCE, V21, P706, DOI 10.1016/j.isci.2019.10.058
   Quesada V, 2012, NAT GENET, V44, P47, DOI 10.1038/ng.1032
   Saeedi P, 2019, DIABETES RES CLIN PR, V157, DOI 10.1016/j.diabres.2019.107843
   Scott LJ, 2007, SCIENCE, V316, P1341, DOI 10.1126/science.1142382
   Shang J, 2017, ACTA BIOCH BIOPH SIN, V49, P753, DOI 10.1093/abbs/gmx071
   Shi Q, 2020, MOL METAB, V36, DOI 10.1016/j.molmet.2020.02.011
   Smith J, 2016, ELIFE, V5, DOI 10.7554/eLife.21337
   Stein CA, 2017, MOL THER, V25, P1069, DOI 10.1016/j.ymthe.2017.03.023
   Strawbridge RJ, 2011, DIABETES, V60, P2624, DOI 10.2337/db11-0415
   Tian XL, 2019, NPJ PRECIS ONCOL, V3, DOI 10.1038/s41698-019-0080-7
   Truitt ML, 2017, NAT REV CANCER, V17, P332, DOI 10.1038/nrc.2017.30
   Ule J, 2003, SCIENCE, V302, P1212, DOI 10.1126/science.1090095
   van Kouwenhove M, 2011, NAT REV CANCER, V11, P644, DOI 10.1038/nrc3107
   Van Nostrand EL, 2020, NATURE, V583, P711, DOI 10.1038/s41586-020-2077-3
   Vanderweyde T, 2012, J NEUROSCI, V32, P8270, DOI 10.1523/JNEUROSCI.1592-12.2012
   Venkat S, 2020, GENOME RES, V30, P347, DOI 10.1101/gr.257550.119
   Wang IF, 2012, P NATL ACAD SCI USA, V109, P15024, DOI 10.1073/pnas.1206362109
   Wang JL, 2020, J CELL BIOCHEM, V121, P946, DOI 10.1002/jcb.29366
   Wang J, 2015, BMC GENOMICS, V16, DOI 10.1186/1471-2164-16-S7-S5
   Wang JX, 2018, P NATL ACAD SCI USA, V115, pE4604, DOI 10.1073/pnas.1800260115
   Wang LL, 2011, NEW ENGL J MED, V365, P2497, DOI 10.1056/NEJMoa1109016
   Whelan JT, 2012, J CELL PHYSIOL, V227, P1235, DOI 10.1002/jcp.22899
   Wilcox Gisela, 2005, Clin Biochem Rev, V26, P19
   Wolozin B, 2015, ADV EXP MED BIOL, V822, P11, DOI 10.1007/978-3-319-08927-0_3
   Xiang SH, 2015, CELL, V163, P829, DOI 10.1016/j.cell.2015.10.040
   Xue YC, 2020, FRONT MOL NEUROSCI, V13, DOI 10.3389/fnmol.2020.00078
   Yan BA, 2015, CIRC RES, V116, P1143, DOI 10.1161/CIRCRESAHA.116.305510
   Yang CB, 2020, NAT COMMUN, V11, DOI 10.1038/s41467-020-17468-y
   Yang CB, 2018, FRONT PHYSIOL, V9, DOI 10.3389/fphys.2018.01310
   Yang L, 2014, TRENDS BIOCHEM SCI, V39, P35, DOI 10.1016/j.tibs.2013.10.002
   Yoshida K, 2011, NATURE, V478, P64, DOI 10.1038/nature10496
   Zhang B, 2020, RNA BIOL, V17, P211, DOI 10.1080/15476286.2019.1673657
   Zhang B, 2017, ONCOTARGET, V8, P17347, DOI 10.18632/oncotarget.14468
   Zhang YJ, 2015, BIOCHEM BIOPH RES CO, V464, P679, DOI 10.1016/j.bbrc.2015.06.139
NR 95
TC 49
Z9 53
U1 2
U2 16
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
EI 2079-7737
J9 BIOLOGY-BASEL
JI Biology-Basel
PD MAY
PY 2021
VL 10
IS 5
AR 366
DI 10.3390/biology10050366
PG 13
WC Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Life Sciences & Biomedicine - Other Topics
GA SG4GP
UT WOS:000653399600001
PM 33923168
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Hu, JT
   Zhao, W
   Zhan, SY
   Xiao, P
   Zhou, JX
   Wang, LJ
   Li, L
   Zhang, HP
   Niu, LL
   Zhong, T
AF Hu, Jiangtao
   Zhao, Wei
   Zhan, Siyuan
   Xiao, Ping
   Zhou, Jingxuan
   Wang, Linjie
   Li, Li
   Zhang, Hongping
   Niu, Lili
   Zhong, Tao
TI Delta-like 1 homolog in Capra hircus:
   molecular characteristics, expression pattern and phylogeny
SO MOLECULAR BIOLOGY REPORTS
LA English
DT Article
DE Goat; Dlk1; Alternative splicing; Expression; Muscle
ID INHIBITS ADIPOCYTE DIFFERENTIATION; DELTA-LIKE; SKELETAL-MUSCLE;
   CELL-DIFFERENTIATION; IMPRINTED GENES; DLK1; PREF-1; PROTEIN; GTL2;
   INFERENCE
AB To research the molecular characteristics, expression pattern and phylogeny of the Delta-like 1 homolog gene (Dlk1) in goats. Dlk1 transcripts were identified in the Jianyang Da'er goats by reverse-transcription polymerase chain reaction (RT-PCR). Phylogenetic trees were constructed by Bayesian inference and neighbor-joining methods. Quantitative real-time PCR (qPCR), western blotting and in situ hybridization were performed to analyze the expression pattern of Dlk1. Five alternatively transcripts were identified in different tissues and designated as Dlk1-AS1, 2, 3, 4 and 5. Compared with the normal transcript Dlk1-AS1, Dlk1-AS4 and Dlk1-AS5 retained the identical open reading frame (ORF) and encoded proteins with truncated epidermal-growth-factor like repeats of 121 and 83 amino acids, respectively. Using the Bayesian inference method, the consensus phylogenetic tree indicated that caprine Dlk1 had a closer relationship with bovine Dlk1 than with Dlk1 from pigs, humans and mice. qPCR revealed high expression levels of Dlk1 in the kidney (P < 0.01). However, mRNA and protein levels presented an inconsistent correlation, possibly because of post-transcriptional regulation. RNA in situ hybridization indicated that Dlk1 mRNA was localized in the interlobular bile duct and alongside the hepatocyte nuclei, in the epithelial cells of proximal and distal convoluted tubules and in the connective region between the mesothelium and myocardium in the heart. The Dlk1 gene in goats produces alternatively spliced transcripts, with specific expression and cellular localization patterns. These findings would lay the foundation for further study.
C1 [Hu, Jiangtao; Zhao, Wei; Zhan, Siyuan; Xiao, Ping; Zhou, Jingxuan; Wang, Linjie; Li, Li; Zhang, Hongping; Niu, Lili; Zhong, Tao] Sichuan Agr Univ, Coll Anim Sci & Technol, Farm Anim Genet Resources Explorat & Innovat Key, Chengdu, Sichuan, Peoples R China.
C3 Sichuan Agricultural University
RP Zhong, T (corresponding author), Sichuan Agr Univ, Coll Anim Sci & Technol, Farm Anim Genet Resources Explorat & Innovat Key, Chengdu, Sichuan, Peoples R China.
EM niulili@sicau.deu.cn; zhongtao@sicau.edu.cn
RI Niu, Lili/B-3929-2018; Zhong, Tao/GOV-5060-2022; Li, Li/T-4353-2017;
   ZHAN, SIYUAN/M-6948-2019
OI Hu, Jiangtao/0000-0002-8374-7868; ZHAN, SIYUAN/0000-0003-3449-9682
FU National Natural Science Foundation of China [31301945, 31501936];
   Chinese Domestic Animal Germplasm Resources Infrastructure
FX This study was supported by the grants from National Natural Science
   Foundation of China (31301945 & 31501936), and the Chinese Domestic
   Animal Germplasm Resources Infrastructure.
CR Albrecht E, 2015, MEAT SCI, V100, P237, DOI 10.1016/j.meatsci.2014.10.012
   [Anonymous], 2014, J. Am. Ceram. Soc, DOI DOI 10.1111/JACE.12773
   Cao GL, 2010, MOL BIOL REP, V37, P2259, DOI 10.1007/s11033-009-9714-0
   Carr MS, 2007, GENOMICS, V89, P280, DOI 10.1016/j.ygeno.2006.10.005
   Chacón MR, 2008, INT J OBESITY, V32, P1122, DOI 10.1038/ijo.2008.40
   Charlier C, 2001, NAT GENET, V27, P367, DOI 10.1038/86856
   Chen L, 2011, J BIOL CHEM, V286, P32140, DOI 10.1074/jbc.M111.230110
   da Rocha ST, 2009, PLOS GENET, V5, DOI 10.1371/journal.pgen.1000392
   Davis E, 2004, CURR BIOL, V14, P1858, DOI 10.1016/j.cub.2004.09.079
   Deiuliis JA, 2006, COMP BIOCHEM PHYS B, V145, P50, DOI 10.1016/j.cbpb.2006.06.003
   Espina AG, 2009, MOL BIOL CELL, V20, P3353, DOI 10.1091/mbc.E08-09-0965
   Fahrenkrug SC, 1999, BIOCHEM BIOPH RES CO, V264, P662, DOI 10.1006/bbrc.1999.1558
   Falix FA, 2012, BBA-MOL BASIS DIS, V1822, P988, DOI 10.1016/j.bbadis.2012.02.003
   Floridon C, 2000, DIFFERENTIATION, V66, P49, DOI 10.1046/j.1432-0436.2000.066001049.x
   Frank D, 2002, P NATL ACAD SCI USA, V99, P7490, DOI 10.1073/pnas.122039999
   Gao YQ, 2015, P NATL ACAD SCI USA, V112, P13627, DOI 10.1073/pnas.1511448112
   Garcés C, 1999, DIFFERENTIATION, V64, P103, DOI 10.1046/j.1432-0436.1999.6420103.x
   Huelsenbeck JP, 2001, BIOINFORMATICS, V17, P754, DOI 10.1093/bioinformatics/17.8.754
   Kim KA, 2007, MOL CELL BIOL, V27, P2294, DOI 10.1128/MCB.02207-06
   Kluth SM, 2010, STEM CELLS DEV, V19, P1471, DOI 10.1089/scd.2010.0070
   Lau T, 2004, DIABETOLOGIA, V47, P240, DOI 10.1007/s00125-003-1295-1
   LEE YL, 1995, BBA-GENE STRUCT EXPR, V1261, P223
   Li L, 2005, ONCOGENE, V24, P4472, DOI 10.1038/sj.onc.1208637
   Mei BS, 2002, BIOCHEM J, V364, P137, DOI 10.1042/bj3640137
   Modrek B, 2002, NAT GENET, V30, P13, DOI 10.1038/ng0102-13
   Murphy SK, 2005, MAMM GENOME, V16, P171, DOI 10.1007/s00335-004-2421-1
   Nueda ML, 2008, J MOL BIOL, V379, P428, DOI 10.1016/j.jmb.2008.03.070
   Oczkowicz M, 2010, GENET MOL BIOL, V33, P790, DOI 10.1590/S1415-47572010000400030
   Perkins AC, 2006, ANIM GENET, V37, P535, DOI 10.1111/j.1365-2052.2006.01518.x
   Ronquist F, 2003, BIOINFORMATICS, V19, P1572, DOI 10.1093/bioinformatics/btg180
   Runge S, 2000, J BIOL CHEM, V275, P29562, DOI 10.1074/jbc.M001156200
   Sakajiri S, 2005, LEUKEMIA, V19, P1404, DOI 10.1038/sj.leu.2403832
   Samulewicz SJ, 2002, WOUND REPAIR REGEN, V10, P215, DOI 10.1046/j.1524-475X.2002.10404.x
   Schmidt JV, 2000, GENE DEV, V14, P1997
   Smas CM, 1997, MOL CELL BIOL, V17, P977, DOI 10.1128/MCB.17.2.977
   SMAS CM, 1994, BIOCHEMISTRY-US, V33, P9257, DOI 10.1021/bi00197a029
   Swofford DL., 2002, PAUP*. Phylogenetic analysis using parsimony (*and other methods). version 4.0 b10 (computer program)
   Takada S, 2000, CURR BIOL, V10, P1135, DOI 10.1016/S0960-9822(00)00704-1
   Tamura K, 2007, MOL BIOL EVOL, V24, P1596, DOI 10.1093/molbev/msm092
   Vandesompele J, 2002, GENOME BIOL, V3, DOI 10.1186/gb-2002-3-7-research0034
   Vuocolo T, 2003, COMP BIOCHEM PHYS B, V134, P315, DOI 10.1016/S1096-4959(02)00265-8
   Waddell JN, 2010, PLOS ONE, V5, DOI 10.1371/journal.pone.0015055
   Weidman JR, 2006, MAMM GENOME, V17, P157, DOI 10.1007/s00335-005-0116-x
   White JD, 2008, DIFFERENTIATION, V76, P283, DOI 10.1111/j.1432-0436.2007.00208.x
   Wylie AA, 2000, GENOME RES, V10, P1711, DOI 10.1101/gr.161600
   Xia X, 2001, J HERED, V92, P371, DOI 10.1093/jhered/92.4.371
   Yevtodiyenko A, 2006, DEV DYNAM, V235, P1115, DOI 10.1002/dvdy.20705
NR 47
TC 4
Z9 4
U1 0
U2 8
PU SPRINGER
PI DORDRECHT
PA VAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDS
SN 0301-4851
EI 1573-4978
J9 MOL BIOL REP
JI Mol. Biol. Rep.
PD JUN
PY 2016
VL 43
IS 6
BP 563
EP 571
DI 10.1007/s11033-016-3989-8
PG 9
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA DM8OG
UT WOS:000376623200012
PM 27108112
DA 2025-04-10
ER

PT J
AU Lindenau, S
   von Langsdorff, C
   Saxena, A
   Paul, M
   Orzechowski, HD
AF Lindenau, Steffi
   von Langsdorff, Christian
   Saxena, Amit
   Paul, Martin
   Orzechowski, Hans-Dieter
TI Genomic organisation of the mouse gene encoding endothelin-converting
   enzyme-1 (ECE-1) and mRNA expression of ECE-1 isoforms in murine tissues
SO GENE
LA English
DT Article
DE metalloprotease; exon-intron structure; real-time PCR; splice variant
ID FUNCTIONAL EXPRESSION; CLONING; CELLS; PROMOTER; DISEASE;
   METALLOPROTEASE; IDENTIFICATION; NEPRILYSIN; MECHANISM; CDNA
AB Mouse knockout-models have previously revealed important biological functions of endothelin-converting enzyme-1 (ECE-1) in normal cardiac and craniofacial development. Since human ECE-1 is expressed in various isoforms, termed a, b, c, and d, expression of which is controlled by alternative promoters, we postulated that corresponding isoforms may also be transcribed from the murine Ece1 gene. By comparative sequence analysis using exon-specific sequences of human and rat ECE-1 we have resolved the complete exon-intron structure of the murine Ece1 locus on chromosome 4. The murine Ece1 gene comprises 23 exons distributed over 100 kb of genomic DNA and was found to be structurally highly conserved when compared to the human ECE1 gene. As with the human gene, the exons containing isoform-specific sequences were localised in the 5' terminal region of the murine Ece1 gene. Using specific sense primers, isoform-specific expression of murine ECE-1 mRNA in various mouse tissues was confirmed by RT-PCR. Using real-time PCR we demonstrated that ECE-1c was the most abundantly expressed isoform in most tissues, except for heart and aorta displaying a more even isoform distribution. We detected an additional isoform-specific exon, designated c2, which was apparently constitutively spliced and expressed only as minor fraction of ECE-1c transcripts. Our results provide evidence of structural conservation of mammalian genes encoding ECE-1 and will facilitate a more refined analysis of ECE-1 mRNA expression in the mouse model organism. (c) 2006 Elsevier B.V. All rights reserved.
C1 Charite, Inst Clin Pharmacol & Toxicol, D-12200 Berlin, Germany.
C3 Berlin Institute of Health; Free University of Berlin; Humboldt
   University of Berlin; Charite Universitatsmedizin Berlin
RP Orzechowski, HD (corresponding author), Charite, Inst Clin Pharmacol & Toxicol, Campus Benjamin Franklin,Hindenburgdamm 30, D-12200 Berlin, Germany.
EM hans-dieter.orzechowski@charite.de
RI Paul, Martin/K-5425-2015; Saxena, Amit/KIC-6193-2024
CR Cailler F, 1999, BIOCHEM J, V341, P119, DOI 10.1042/0264-6021:3410119
   Eckman EA, 2003, J BIOL CHEM, V278, P2081, DOI 10.1074/jbc.C200642200
   Emoto N, 1999, J BIOL CHEM, V274, P1509, DOI 10.1074/jbc.274.3.1509
   Funke-Kaiser H, 2003, J HYPERTENS, V21, P2111, DOI 10.1097/00004872-200311000-00021
   Funke-Kaiser H, 2000, FEBS LETT, V466, P310, DOI 10.1016/S0014-5793(00)01086-3
   Hofstra RMW, 1999, AM J HUM GENET, V64, P304, DOI 10.1086/302184
   IKURA T, 1994, BIOCHEM BIOPH RES CO, V203, P1417, DOI 10.1006/bbrc.1994.2343
   Kedzierski RM, 2001, ANNU REV PHARMACOL, V41, P851, DOI 10.1146/annurev.pharmtox.41.1.851
   Korth P, 1999, J HISTOCHEM CYTOCHEM, V47, P447, DOI 10.1177/002215549904700403
   Meidan R, 2005, J BIOL CHEM, V280, P40867, DOI 10.1074/jbc.M505679200
   Muller L, 2003, J BIOL CHEM, V278, P545, DOI 10.1074/jbc.M208949200
   Orzechowski HD, 1997, J MOL MED-JMM, V75, P512, DOI 10.1007/s001090050136
   Orzechowski HD, 2001, MOL PHARMACOL, V60, P1332, DOI 10.1124/mol.60.6.1332
   SCHMIDT M, 1994, FEBS LETT, V356, P238, DOI 10.1016/0014-5793(94)01277-6
   Schweizer A, 1997, BIOCHEM J, V328, P871, DOI 10.1042/bj3280871
   Shimada K, 1996, BIOCHEM J, V315, P863, DOI 10.1042/bj3150863
   SHIMADA K, 1995, BIOCHEM BIOPH RES CO, V207, P807, DOI 10.1006/bbrc.1995.1258
   SHIMADA K, 1994, J BIOL CHEM, V269, P18275
   SHIMADA K, 1995, FEBS LETT, V371, P140, DOI 10.1016/0014-5793(95)00886-E
   Turner AJ, 2001, BIOESSAYS, V23, P261, DOI 10.1002/1521-1878(200103)23:3<261::AID-BIES1036>3.0.CO;2-K
   Valdenaire O, 1999, EUR J BIOCHEM, V264, P341, DOI 10.1046/j.1432-1327.1999.00602.x
   VALDENAIRE O, 1995, J BIOL CHEM, V270, P29794
   XU D, 1994, CELL, V78, P473, DOI 10.1016/0092-8674(94)90425-1
   Yanagisawa H, 1998, DEVELOPMENT, V125, P825
   YORIMITSU K, 1995, BIOCHEM BIOPH RES CO, V208, P721, DOI 10.1006/bbrc.1995.1397
NR 25
TC 14
Z9 15
U1 0
U2 3
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 0378-1119
EI 1879-0038
J9 GENE
JI Gene
PD MAY 24
PY 2006
VL 373
BP 109
EP 115
DI 10.1016/j.gene.2006.01.024
PG 7
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA 049AP
UT WOS:000237988000015
PM 16540265
DA 2025-04-10
ER

PT J
AU Rasmussen, M
   Jin, JP
AF Rasmussen, Monica
   Jin, Jian-Ping
TI Troponin Variants as Markers of Skeletal Muscle Health and Diseases
SO FRONTIERS IN PHYSIOLOGY
LA English
DT Review
DE skeletal muscle; troponin I; troponin T; isoform; splice form;
   development; adaptation; myopathy
ID MYOSIN HEAVY-CHAIN; MYOFILAMENT CALCIUM SENSITIVITY; NH2-TERMINAL
   VARIABLE REGION; ESSENTIAL AMINO-ACIDS; MOUSE CARDIAC-MUSCLE; T ISOFORM
   EXPRESSION; PRE-MESSENGER-RNA; SLOW SKELETAL; FIBER-TYPE; CA2+
   SENSITIVITY
AB Ca2+-regulated contractility is a key determinant of the quality of muscles. The sarcomeric myofilament proteins are essential players in the contraction of striated muscles. The troponin complex in the actin thin filaments plays a central role in the Ca2+-regulation of muscle contraction and relaxation. Among the three subunits of troponin, the Ca2+-binding subunit troponin C (TnC) is a member of the calmodulin super family whereas troponin I (TnI, the inhibitory subunit) and troponin T (TnT, the tropomyosin-binding and thin filament anchoring subunit) are striated muscle-specific regulatory proteins. Muscle type-specific isoforms of troponin subunits are expressed in fast and slow twitch fibers and are regulated during development and aging, and in adaptation to exercise or disuse. TnT also evolved with various alternative splice forms as an added capacity of muscle functional diversity. Mutations of troponin subunits cause myopathies. Owing to their physiological and pathological importance, troponin variants can be used as specific markers to define muscle quality. In this focused review, we will explore the use of troponin variants as markers for the fiber contents, developmental and differentiation states, contractile functions, and physiological or pathophysiological adaptations of skeletal muscle. As protein structure defines function, profile of troponin variants illustrates how changes at the myofilament level confer functional qualities at the fiber level. Moreover, understanding of the role of troponin modifications and mutants in determining muscle contractility in age-related decline of muscle function and in myopathies informs an approach to improve human health.
C1 [Rasmussen, Monica; Jin, Jian-Ping] Wayne State Univ, Sch Med, Dept Physiol, Detroit, MI 48201 USA.
   [Jin, Jian-Ping] Univ Illinois, Dept Physiol & Biophys, Chicago, IL 60680 USA.
C3 Wayne State University; University of Illinois System; University of
   Illinois Chicago; University of Illinois Chicago Hospital
RP Jin, JP (corresponding author), Wayne State Univ, Sch Med, Dept Physiol, Detroit, MI 48201 USA.; Jin, JP (corresponding author), Univ Illinois, Dept Physiol & Biophys, Chicago, IL 60680 USA.
EM jpjin@uic.edu
RI Jin, Jian-Ping/AAD-1149-2020
OI Rasmussen, Monica/0000-0003-2085-8461; Jin, JP/0000-0001-9932-1063
FU National Institutes of Health
FX Funding This work was supported in part by grants from the National
   Institutes of Health HL127691 and HL138007 to J-PJ.
CR Abdul-Hussein S, 2012, BMC MUSCULOSKEL DIS, V13, DOI 10.1186/1471-2474-13-262
   Abdulhaq UN, 2016, MUSCLE NERVE, V53, P564, DOI 10.1002/mus.24885
   Alarcin E, 2021, INT J MOL SCI, V22, DOI 10.3390/ijms22115929
   Amarasinghe C, 2016, BIOCHEMISTRY-US, V55, P4560, DOI 10.1021/acs.biochem.6b00577
   Bastide B, 2002, PFLUG ARCH EUR J PHY, V444, P345, DOI 10.1007/s00424-002-0833-x
   BAUMANN H, 1987, PFLUG ARCH EUR J PHY, V409, P349, DOI 10.1007/BF00583788
   Bicer S, 2011, J EXP BIOL, V214, P1077, DOI 10.1242/jeb.049213
   BRIGGS MM, 1989, J MOL BIOL, V206, P245, DOI 10.1016/0022-2836(89)90538-X
   BRIGGS MM, 1990, DEV BIOL, V140, P253, DOI 10.1016/0012-1606(90)90075-T
   Briggs MM, 1996, AM J PHYSIOL-CELL PH, V270, pC298, DOI 10.1152/ajpcell.1996.270.1.C298
   Brotto MA, 2006, AM J PHYSIOL-CELL PH, V290, pC567, DOI 10.1152/ajpcell.00422.2005
   Calame DG, 2021, NEUROL-GENET, V7, DOI 10.1212/NXG.0000000000000589
   Cao TX, 2020, FRONT PHYSIOL, V11, DOI 10.3389/fphys.2020.01038
   Chal J, 2017, DEVELOPMENT, V144, P2104, DOI 10.1242/dev.151035
   Chaudhuri T, 2005, J MOL BIOL, V352, P58, DOI 10.1016/j.jmb.2005.06.066
   Chong SM, 2009, J MOL EVOL, V68, P448, DOI 10.1007/s00239-009-9202-0
   Ciapaite J, 2015, J NUTR BIOCHEM, V26, P155, DOI 10.1016/j.jnutbio.2014.09.014
   Coble J, 2015, APPL PHYSIOL NUTR ME, V40, P788, DOI 10.1139/apnm-2014-0568
   CONDON K, 1990, DEV BIOL, V138, P256, DOI 10.1016/0012-1606(90)90196-P
   Consitt LA, 2019, NUTRIENTS, V11, DOI 10.3390/nu11112636
   D'Amico A, 2019, NEUROMUSCULAR DISORD, V29, P766, DOI 10.1016/j.nmd.2019.09.005
   Davila AJL, 2020, BIOCHEMISTRY-US, V59, P4189, DOI 10.1021/acs.biochem.0c00499
   de Tombe PP, 2007, AM J PHYSIOL-REG I, V292, pR1129, DOI 10.1152/ajpregu.00630.2006
   Drummond MJ, 2008, J APPL PHYSIOL, V104, P1452, DOI 10.1152/japplphysiol.00021.2008
   Ekmark M, 2007, J PHYSIOL-LONDON, V584, P637, DOI 10.1113/jphysiol.2007.141457
   ELSALEH SC, 1988, J BIOL CHEM, V263, P3274
   Evans EM, 2005, J APPL PHYSIOL, V98, P40, DOI 10.1152/japplphysiol.00928.2004
   Feng HZ, 2016, AM J PHYSIOL-CELL PH, V310, pC27, DOI 10.1152/ajpcell.00173.2015
   Feng HZ, 2011, J APPL PHYSIOL, V111, P834, DOI 10.1152/japplphysiol.00031.2011
   Fox MD, 2018, HUM MOL GENET, V27, P3272, DOI 10.1093/hmg/ddy233
   FURUKAWA T, 1972, ARCH NEUROL-CHICAGO, V26, P385, DOI 10.1001/archneur.1972.00490110019001
   Galler S, 1997, J MUSCLE RES CELL M, V18, P555, DOI 10.1023/A:1018615302548
   Gallon CE, 2006, ARCH BIOCHEM BIOPHYS, V456, P127, DOI 10.1016/j.abb.2006.06.008
   Gannon J, 2009, EUR J CELL BIOL, V88, P685, DOI 10.1016/j.ejcb.2009.06.004
   Géraud J, 2021, J MED GENET, V58, P602, DOI 10.1136/jmedgenet-2019-106714
   Gomes AV, 2004, J BIOL CHEM, V279, P49579, DOI 10.1074/jbc.M407340200
   Gordon AM, 2000, PHYSIOL REV, V80, P853, DOI 10.1152/physrev.2000.80.2.853
   GREASER ML, 1971, J BIOL CHEM, V246, P4226
   GREASER ML, 1988, J PHYSIOL-LONDON, V406, P85, DOI 10.1113/jphysiol.1988.sp017370
   Guerrero L, 2014, GENESIS, V52, P793, DOI 10.1002/dvg.22796
   Hagiwara N, 2005, DEV DYNAM, V234, P301, DOI 10.1002/dvdy.20535
   Hagiwara N, 2007, DEV DYNAM, V236, P2062, DOI 10.1002/dvdy.21223
   Hallauer PL, 2002, DEV DYNAM, V224, P422, DOI 10.1002/dvdy.10122
   Hallauer PL, 2002, AM J PHYSIOL-CELL PH, V282, pC113, DOI 10.1152/ajpcell.00294.2001
   Hastings KEM, 1997, CELL STRUCT FUNCT, V22, P205, DOI 10.1247/csf.22.205
   Hettige P, 2020, BMC GENOMICS, V21, DOI 10.1186/s12864-020-07225-2
   Huang QQ, 1999, J PHYSIOL-LONDON, V520, P231, DOI 10.1111/j.1469-7793.1999.00231.x
   Huang QQ, 1999, GENE, V229, P1, DOI 10.1016/S0378-1119(99)00051-7
   HUNKELER NM, 1991, CIRC RES, V69, P1409, DOI 10.1161/01.RES.69.5.1409
   JANSSON E, 1978, ACTA PHYSIOL SCAND, V104, P235, DOI 10.1111/j.1748-1716.1978.tb06272.x
   Jin JP, 2008, CRIT REV EUKAR GENE, V18, P93, DOI 10.1615/CritRevEukarGeneExpr.v18.i2.10
   Jin JP, 1998, BIOCHEM BIOPH RES CO, V242, P540, DOI 10.1006/bbrc.1997.8006
   Jin JP, 1998, GENE, V214, P121, DOI 10.1016/S0378-1119(98)00214-5
   Jin JP, 2003, J BIOL CHEM, V278, P26159, DOI 10.1074/jbc.M303469200
   JIN JP, 1989, J BIOL CHEM, V264, P14471
   Jin JP, 1996, BIOCHEM BIOPH RES CO, V225, P883, DOI 10.1006/bbrc.1996.1267
   Jozaki M, 2002, J MUSCLE RES CELL M, V23, P235, DOI 10.1023/A:1020956216423
   KAWASHIMA A, 1995, BIOCHEM BIOPH RES CO, V207, P585, DOI 10.1006/bbrc.1995.1228
   Khodabukus A, 2015, J CELL PHYSIOL, V230, P1750, DOI 10.1002/jcp.24848
   Kimber E, 2006, NEUROLOGY, V67, P597, DOI 10.1212/01.wnl.0000230168.05328.f4
   Kischel P, 2005, AM J PHYSIOL-CELL PH, V289, pC437, DOI 10.1152/ajpcell.00365.2004
   Kischel P, 2001, J APPL PHYSIOL, V90, P1095, DOI 10.1152/jappl.2001.90.3.1095
   Klein P, 2016, NUCLEIC ACIDS RES, V44, P10929, DOI 10.1093/nar/gkw703
   Krishan K, 2000, J MUSCLE RES CELL M, V21, P527, DOI 10.1023/A:1026541803317
   Krüger M, 2006, AM J PHYSIOL-HEART C, V291, pH496, DOI 10.1152/ajpheart.00114.2006
   Larsson L, 2008, AM J PHYSIOL-CELL PH, V295, pC722, DOI 10.1152/ajpcell.00110.2008
   Li MX, 2015, GENE, V571, P153, DOI 10.1016/j.gene.2015.07.074
   Lin J, 2002, NATURE, V418, P797, DOI 10.1038/nature00904
   Liu J, 2018, BIOMED RES INT, V2018, DOI 10.1155/2018/1984879
   López-Martínez A, 2020, GENES-BASEL, V11, DOI 10.3390/genes11091109
   Marra JD, 2015, MUSCLE NERVE, V51, P767, DOI 10.1002/mus.24528
   Valenzuela IMPY, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0081311
   MATSUDA R, 1981, DEV BIOL, V82, P11, DOI 10.1016/0012-1606(81)90424-3
   Matsumoto N, 2000, MUSCLE NERVE, V23, P1270, DOI 10.1002/1097-4598(200008)23:8<1270::AID-MUS18>3.0.CO;2-E
   MCDONALD KS, 1995, J PHYSIOL-LONDON, V483, P131, DOI 10.1113/jphysiol.1995.sp020573
   MEDFORD RM, 1984, CELL, V38, P409, DOI 10.1016/0092-8674(84)90496-3
   METZGER JM, 1990, SCIENCE, V247, P1088, DOI 10.1126/science.2309121
   METZGER JM, 1995, J PHYSIOL-LONDON, V485, P447, DOI 10.1113/jphysiol.1995.sp020741
   Metzger JM, 1996, J PHYSIOL-LONDON, V492, P163, DOI 10.1113/jphysiol.1996.sp021298
   Miniou P, 2021, INT J MOL SCI, V22, DOI 10.3390/ijms22136755
   Mitchell WK, 2012, FRONT PHYSIOL, V3, DOI 10.3389/fphys.2012.00260
   Mondal A, 2016, FRONT PHYSIOL, V7, DOI 10.3389/fphys.2016.00449
   Moore AZ, 2014, J AM GERIATR SOC, V62, P230, DOI 10.1111/jgs.12653
   MOSS RL, 1991, J PHYSIOL-LONDON, V440, P273, DOI 10.1113/jphysiol.1991.sp018708
   Mounier Y, 2009, J APPL PHYSIOL, V106, P1086, DOI 10.1152/japplphysiol.90695.2008
   Mullen AJ, 2000, GENE, V242, P313, DOI 10.1016/S0378-1119(99)00519-3
   Muroya S, 2005, DEV GROWTH DIFFER, V47, P483
   Nakada K, 2000, CELL TISSUE RES, V299, P263, DOI 10.1007/s004419900137
   Niro C, 2010, DEV BIOL, V338, P168, DOI 10.1016/j.ydbio.2009.11.031
   Nosek TM, 2004, ARCH BIOCHEM BIOPHYS, V430, P178, DOI 10.1016/j.abb.2004.07.014
   O'Connell B, 2004, BIOCHEM J, V378, P269, DOI 10.1042/BJ20031170
   Ogut O, 1999, AM J PHYSIOL-CELL PH, V276, pC1162, DOI 10.1152/ajpcell.1999.276.5.C1162
   Ogut O, 1996, BIOCHEMISTRY-US, V35, P16581, DOI 10.1021/bi961712y
   Ogut O, 1998, J BIOL CHEM, V273, P27858, DOI 10.1074/jbc.273.43.27858
   Oki K, 2019, J PHYSIOL-LONDON, V597, P3999, DOI 10.1113/JP278119
   Petchey LK, 2014, P NATL ACAD SCI USA, V111, P9515, DOI 10.1073/pnas.1406191111
   Petrucci A, 2021, NEUROMUSCULAR DISORD, V31, P532, DOI 10.1016/j.nmd.2021.03.001
   Pette D, 2000, MICROSC RES TECHNIQ, V50, P500, DOI 10.1002/1097-0029(20000915)50:6<500::AID-JEMT7>3.3.CO;2-Z
   POLGAR J, 1973, J NEUROL SCI, V19, P307, DOI 10.1016/0022-510X(73)90094-4
   Posterino GS, 2011, J APPL PHYSIOL, V111, P236, DOI 10.1152/japplphysiol.00067.2011
   Power GA, 2010, MED SCI SPORT EXER, V42, P1644, DOI 10.1249/MSS.0b013e3181d6f9e9
   Prigozy TI, 1997, DEV DYNAM, V209, P36
   PUTKEY JA, 1991, J BIOL CHEM, V266, P14881
   REISER PJ, 1992, J PHYSIOL-LONDON, V449, P573, DOI 10.1113/jphysiol.1992.sp019102
   Robergs RA, 2004, AM J PHYSIOL-REG I, V287, pR502, DOI 10.1152/ajpregu.00114.2004
   Rowlerson A, 2005, AM J ORTHOD DENTOFAC, V127, P37, DOI 10.1016/j.ajodo.2004.03.025
   SAGGIN L, 1990, DEVELOPMENT, V110, P547
   Salvatori S, 2009, NEUROL SCI, V30, P185, DOI 10.1007/s10072-009-0048-4
   SALVIATI G, 1982, BIOCHEM J, V207, P261, DOI 10.1042/bj2070261
   Sancisi V, 2014, AM J PHYSIOL-REG I, V306, pR124, DOI 10.1152/ajpregu.00379.2013
   Sandaradura SA, 2018, HUM MUTAT, V39, P383, DOI 10.1002/humu.23385
   SCHACHAT F, 1988, J BIOL CHEM, V263, P13975
   SCHACHAT FH, 1987, J MOL BIOL, V198, P551, DOI 10.1016/0022-2836(87)90300-7
   Schiaffino S, 2018, FEBS J, V285, P3688, DOI 10.1111/febs.14502
   Schiaffino S, 2011, PHYSIOL REV, V91, P1447, DOI 10.1152/physrev.00031.2010
   Scott W, 2001, PHYS THER, V81, P1810, DOI 10.1093/ptj/81.11.1810
   Sheng JJ, 2016, GENE, V576, P385, DOI 10.1016/j.gene.2015.10.052
   Sheng JJ, 2014, FRONT PHYSIOL, V5, DOI 10.3389/fphys.2014.00165
   SHIMIZU N, 1985, DEV BIOL, V111, P324, DOI 10.1016/0012-1606(85)90487-7
   Stevens L, 1999, FEBS LETT, V463, P15, DOI 10.1016/S0014-5793(99)01596-3
   SUTHERLAND CJ, 1993, DEV DYNAM, V196, P25, DOI 10.1002/aja.1001960104
   Talbot J, 2016, WIRES DEV BIOL, V5, P518, DOI 10.1002/wdev.230
   Tawil Rabi, 2018, Handb Clin Neurol, V148, P541, DOI 10.1016/B978-0-444-64076-5.00035-1
   Terry EE, 2018, ELIFE, V7, DOI 10.7554/eLife.34613
   Toydemir RM, 2009, ORPHANET J RARE DIS, V4, DOI 10.1186/1750-1172-4-11
   TOYOTA N, 1981, J CELL BIOL, V91, P497, DOI 10.1083/jcb.91.2.497
   Udaka J, 2011, J APPL PHYSIOL, V111, P1080, DOI 10.1152/japplphysiol.00330.2011
   van de Locht M, 2021, J CLIN INVEST, V131, DOI 10.1172/JCI145700
   van der Pol WL, 2014, MOL GENET GENOM MED, V2, P134, DOI 10.1002/mgg3.52
   Van Petegem F, 2012, J BIOL CHEM, V287, P31624, DOI 10.1074/jbc.R112.349068
   VANEERD JP, 1976, BIOCHEMISTRY-US, V15, P1171, DOI 10.1021/bi00650a033
   Vihola A, 2010, ACTA NEUROPATHOL, V119, P465, DOI 10.1007/s00401-010-0637-6
   von Hofsten J, 2008, EMBO REP, V9, P683, DOI 10.1038/embor.2008.73
   Vullhorst D, 2003, J BIOL CHEM, V278, P8370, DOI 10.1074/jbc.M209361200
   Wang J, 1998, BIOCHEMISTRY-US, V37, P14519, DOI 10.1021/bi9812322
   Wang J, 1997, GENE, V193, P105, DOI 10.1016/S0378-1119(97)00100-5
   Wang Q, 2001, ANAT RECORD, V263, P72, DOI 10.1002/ar.1078
   WANG YP, 1994, AM J PHYSIOL, V266, pC1077, DOI 10.1152/ajpcell.1994.266.4.C1077
   Wang ZM, 2005, J PHYSIOL-LONDON, V565, P757, DOI 10.1113/jphysiol.2005.087601
   Wasicky R, 2000, INVEST OPHTH VIS SCI, V41, P980
   WATTANAPERMPOOL J, 1995, AM J PHYSIOL-CELL PH, V268, pC323, DOI 10.1152/ajpcell.1995.268.2.C323
   Wei B, 2016, GENE, V582, P1, DOI 10.1016/j.gene.2016.01.006
   Wei B, 2014, J PHYSIOL-LONDON, V592, P1367, DOI 10.1113/jphysiol.2013.268177
   Wei B, 2011, ARCH BIOCHEM BIOPHYS, V505, P144, DOI 10.1016/j.abb.2010.10.013
   Westfall MV, 1997, P NATL ACAD SCI USA, V94, P5444, DOI 10.1073/pnas.94.10.5444
   Wheelwright M, 2020, STEM CELLS, V38, P1254, DOI 10.1002/stem.3235
   WILKINSON JM, 1978, BIOCHEM J, V169, P229, DOI 10.1042/bj1690229
   WILKINSON JM, 1980, EUR J BIOCHEM, V103, P179, DOI 10.1111/j.1432-1033.1980.tb04302.x
   Xu Z Y, 2010, Animal, V4, P1541, DOI 10.1017/S1751731110000649
   Xu ZR, 2017, J CACHEXIA SARCOPENI, V8, P808, DOI 10.1002/jcsm.12204
   Yonemura I, 2000, J EXP ZOOL, V286, P149, DOI 10.1002/(SICI)1097-010X(20000201)286:2<149::AID-JEZ7>3.0.CO;2-H
   Yu ZB, 2007, AM J PHYSIOL-CELL PH, V292, pC1192, DOI 10.1152/ajpcell.00462.2006
   Yuen M, 2015, HUM MOL GENET, V24, P6278, DOI 10.1093/hmg/ddv334
   Zhang T, 2014, J GERONTOL A-BIOL, V69, P1437, DOI 10.1093/gerona/glt204
   Zhao WF, 2000, J MUSCLE RES CELL M, V21, P463, DOI 10.1023/A:1005617419247
   ZHU L, 1995, DEV BIOL, V169, P487, DOI 10.1006/dbio.1995.1163
NR 156
TC 40
Z9 40
U1 0
U2 9
PU FRONTIERS MEDIA SA
PI LAUSANNE
PA AVENUE DU TRIBUNAL FEDERAL 34, LAUSANNE, CH-1015, SWITZERLAND
EI 1664-042X
J9 FRONT PHYSIOL
JI Front. Physiol.
PD SEP 27
PY 2021
VL 12
AR 747214
DI 10.3389/fphys.2021.747214
PG 14
WC Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Physiology
GA WT2ZB
UT WOS:000715735800001
PM 34733179
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Biros, E
   Staffa, R
   Krejcí, M
   Novotny, T
   Skotáková, M
   Bobák, R
AF Biros, Ernest
   Staffa, Robert
   Krejci, Miroslav
   Novotny, Tomas
   Skotakova, Monika
   Bobak, Robert
TI Autologous Alternative Vein Grafts for Infrainguinal Bypass in the
   Absence of Single-Segment Great Saphenous Vein: A Single-Center Study
SO ANNALS OF VASCULAR SURGERY
LA English
DT Article
ID LOWER-EXTREMITY REVASCULARIZATION; ARM VEIN; AUTOGENOUS CONDUIT; LIMB;
   ISCHEMIA; OUTCOMES
AB Background: Alternative autologous veins can be used as a conduit when adequate great saphenous vein is unavailable. We analyzed the results of our infrainguinal bypasses after adopting upper extremity veins in our practice. Methods: This is a single-center observational study involving all patients whose infrainguinal bypass involved the use of upper extremity veins between April 2019, when we began using arm veins, and February 2023. Results: During the study period, 49 bypasses were done in 48 patients; mean age 68.1 +/- 9.8; men 32 (66.7%); body mass index 28.0 +/- 4.8; indications for surgery: chronic limb threatening ischemia 41 (83.7%); acute limb ischemia 3 (6.1%); complications of previous prosthetic 3 (6.1%), or autologous 2 (4.1%) bypass grafts. Vein splicing was used in 43 (87.8%) bypasses with 3-segment grafts being the most common (26; 53.1%). There were 24 (49.0%) femorotibial, 11 (22.4%) femoropopliteal, 9 (18.4%) femoropedal, and 5 (10.2%) extension jump bypass procedures. Eighteen (36.7%) operations were redo surgeries. Twenty-one (42.9%) bypasses were formed using only arm veins. The median follow-up was 12.9 months (4.5e24.2). Two bypasses occluded during the first 30 postoperative days (2/49; 4.1%). Overall 30-day, 1-year, and 2-year primary patency rates were 93.7% +/- 3.5%, 84.8% +/- 5.9%, and 80.6% +/- 6.9%, and secondary patency (SP) rates were 95.8% +/- 2.9%, 89.2% +/- 5.3%, and 89.2% +/- 5.3%. One-segment grafts had better patencies than 2-, 3-, and 4-segment grafts (1-year SP 100% +/- 0% vs 87.6% +/- 6.0%). Two-year amputation-free survival was 86.8% +/- 6.5%; 2-year overall survival was 88.2% +/- 6.6%. Conclusions: Integration of arm vein grafts in infrainguinal bypass practice can be done safely with low incidences of perioperative graft failure. One-segment grafts had better patencies than spliced vein grafts. The achieved early patency and amputation-free survival rates strongly encourage their use. In the absence of a single -segment great saphenous vein, upper extremity vein grafts should be the preferred conduit choice.
C1 [Biros, Ernest; Staffa, Robert; Krejci, Miroslav; Novotny, Tomas; Bobak, Robert] Masaryk Univ, Fac Med, Ctr Vasc Dis, Dept Surg 2, Pekarska 664-53, Brno 60200, Czech Republic.
   [Biros, Ernest; Staffa, Robert; Krejci, Miroslav; Novotny, Tomas; Bobak, Robert] St Annes Univ Hosp, Pekarska 664-53, Brno 60200, Czech Republic.
   [Skotakova, Monika] St Annes Univ Hosp, Int Clin Res Ctr, Biostat, Brno, Czech Republic.
C3 Masaryk University Brno; St. Anne's University Hospital Brno (FNUSA);
   St. Anne's University Hospital Brno (FNUSA); St. Anne's University
   Hospital Brno (FNUSA-ICRC)
RP Biros, E (corresponding author), Masaryk Univ, Fac Med, Ctr Vasc Dis, Dept Surg 2, Pekarska 664-53, Brno 60200, Czech Republic.
EM ernest.biros@fnusa.cz
RI Novotny, Tomas/LYO-1198-2024; Biroš, Ernest/JCO-9487-2023
OI Biros, Ernest/0000-0001-8416-6814
CR Abdul-Malak OM, 2022, J VASC SURG, V76, P188, DOI 10.1016/j.jvs.2022.03.006
   Guevara-Noriega KA, 2019, ANN VASC SURG, V60, P379, DOI 10.1016/j.avsg.2019.03.018
   Almasri J, 2018, J VASC SURG, V68, P624, DOI 10.1016/j.jvs.2018.01.066
   Neto FB, 2014, EUR J VASC ENDOVASC, V47, P609, DOI 10.1016/j.ejvs.2014.01.019
   Chang H, 2022, EUR J VASC ENDOVASC, V63, P864, DOI 10.1016/j.ejvs.2022.04.002
   Chew DKW, 2001, J VASC SURG, V33, P259, DOI 10.1067/mva.2001.112699
   Conte MS, 2019, J VASC SURG, V69, p3S, DOI 10.1016/j.jvs.2019.02.016
   Conte MS, 2009, SEMIN VASC SURG, V22, P227, DOI 10.1053/j.semvascsurg.2009.10.004
   Daenens K, 2009, J VASC SURG, V49, P1210, DOI 10.1016/j.jvs.2008.12.009
   Evans W, 2022, ANN VASC SURG, V78, P321, DOI 10.1016/j.avsg.2021.06.026
   Farber A, 2003, J VASC SURG, V38, P15, DOI 10.1016/S0741-5214(03)00330-6
   Farber A, 2022, NEW ENGL J MED, V387, P2305, DOI 10.1056/NEJMoa2207899
   Faries PL, 2000, J VASC SURG, V31, P50, DOI 10.1016/S0741-5214(00)70067-X
   Faries PL, 2000, J VASC SURG, V32, P1080, DOI 10.1067/mva.2000.111279
   Gentile AT, 1996, J VASC SURG, V23, P272, DOI 10.1016/S0741-5214(96)70271-9
   Holzenbein TJ, 1996, J VASC SURG, V23, P130, DOI 10.1016/S0741-5214(05)80043-6
   KAKKAR VV, 1969, SURG GYNECOL OBSTETR, V128, P551
   Nierlich P, 2020, EUR J VASC ENDOVASC, V60, P403, DOI 10.1016/j.ejvs.2020.06.016
   Spacek M, 2018, COR VASA, V60, pE317, DOI 10.1016/j.crvasa.2017.03.003
   TAYLOR LM, 1987, AM J SURG, V153, P505, DOI 10.1016/0002-9610(87)90803-8
   Tisi PV, 1996, ANN ROY COLL SURG, V78, P497
   VEITH FJ, 1986, J VASC SURG, V3, P104
   World Med Assoc, 2013, JAMA-J AM MED ASSOC, V310, P2191, DOI 10.1001/jama.2013.281053
NR 23
TC 1
Z9 1
U1 0
U2 1
PU ELSEVIER SCIENCE INC
PI NEW YORK
PA STE 800, 230 PARK AVE, NEW YORK, NY 10169 USA
SN 0890-5096
EI 1615-5947
J9 ANN VASC SURG
JI Ann. Vasc. Surg.
PD JUN
PY 2024
VL 103
BP 133
EP 140
DI 10.1016/j.avsg.2023.12.067
EA MAR 2024
PG 8
WC Surgery; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Surgery; Cardiovascular System & Cardiology
GA PY9K4
UT WOS:001217754800001
PM 38428452
DA 2025-04-10
ER

PT J
AU Homberger, A
   Linnebank, M
   Winter, C
   Willenbring, H
   Marquardt, T
   Harms, E
   Koch, HG
AF Homberger, A
   Linnebank, M
   Winter, C
   Willenbring, H
   Marquardt, T
   Harms, E
   Koch, HG
TI Genomic structure and transcript variants of the human
   methylenetetrahydrofolate reductase gene
SO EUROPEAN JOURNAL OF HUMAN GENETICS
LA English
DT Article
DE methylenetetrahydrofolate reductase; MTHFR; promoter; transcripts;
   genomic structure
ID CYSTATHIONINE BETA-SYNTHASE; COMMON MUTATION; RISK FACTOR; DEFICIENCY;
   IDENTIFICATION; POLYMORPHISMS; MTHFR
AB The human 5,10-methylenetetrahydrofolate reductase (MTHFR) represents a major enzyme in the folate-dependent regulation of methionine and homocysteine concentrations. Different MTHFR mutations lead either to severe homocystinuria as a multisystem disorder or to moderate hyperhomocysteinaemia, which is a common risk factor for disorders ranging from cardiovasculopathy to spina bifida. The N-terminal part of the human MTHFR gene is incompletely characterised. We report the completed genomic structure of this gene including three novel exonic sequences on the basis of a 5'-RACE and a 4.2 kb cloned fragment of human genomic DNA. We demonstrate the existence of four MTHFR transcripts differing in their first exons. The diversity of transcripts is due to alternative transcription initiation and alternative splicing. Three putative polypeptides of 657, 698, and 680 amino acids are encoded. The novel genomic sequence described here includes putative promoter regions as suggested by the presence of regions homologue to binding sites for SP1, AP1, AP2, CAAT or CC boxes. Furthermore, we provide evidence that there are no TATA-box elements to regulate the human MTHFR gene. The results of our study render the full-length characterisation of affected alleles in severe homocystinuria and moderate hyperhomocysteinaemia due to MTHFR deficiency and provide a basis for investigating the regulation of the human MTHFR gene.
C1 Univ Munster, Klin & Poliklin Kinderheilkunde, D-48129 Munster, Germany.
C3 University of Munster
RP Univ Munster, Klin & Poliklin Kinderheilkunde, Albert Schweitzer Str 33, D-48129 Munster, Germany.
EM kochha@uni-muenster.de
CR Bailey LB, 1999, J NUTR, V129, P919, DOI 10.1093/jn/129.5.919
   Chasse JF, 1997, MAMM GENOME, V8, P917, DOI 10.1007/s003359900611
   Chen LH, 1997, J BIOL CHEM, V272, P3628, DOI 10.1074/jbc.272.6.3628
   FROSST P, 1995, NAT GENET, V10, P111, DOI 10.1038/ng0595-111
   GOYETTE P, 1995, AM J HUM GENET, V56, P1052
   Goyette P, 1996, AM J HUM GENET, V59, P1268
   Goyette P, 1998, MAMM GENOME, V9, P652, DOI 10.1007/s003359900838
   GOYETTE P, 1994, NAT GENET, V7, P195, DOI 10.1038/ng0694-195
   Kluijtmans LAJ, 1998, EUR J HUM GENET, V6, P257, DOI 10.1038/sj.ejhg.5200182
   Kraus JP, 1998, GENOMICS, V52, P312, DOI 10.1006/geno.1998.5437
   Leclerc D, 1999, GENE, V240, P75, DOI 10.1016/S0378-1119(99)00431-X
   Rosenblatt DS, 1999, SEMIN HEMATOL, V36, P19
   van der Put NMJ, 1998, AM J HUM GENET, V62, P1044, DOI 10.1086/301825
NR 13
TC 51
Z9 59
U1 0
U2 3
PU NATURE PUBLISHING GROUP
PI LONDON
PA MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
SN 1018-4813
EI 1476-5438
J9 EUR J HUM GENET
JI Eur. J. Hum. Genet.
PD SEP
PY 2000
VL 8
IS 9
BP 725
EP 729
DI 10.1038/sj.ejhg.5200522
PG 5
WC Biochemistry & Molecular Biology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Genetics & Heredity
GA 355YP
UT WOS:000089416400012
PM 10980581
OA Bronze
DA 2025-04-10
ER

PT J
AU Li, H
   Wang, TA
   Xu, CL
   Wang, DD
   Ren, JX
   Li, YM
   Tian, YD
   Wang, YB
   Jiao, YP
   Kang, XT
   Liu, XJ
AF Li, Hong
   Wang, Taian
   Xu, Chunlin
   Wang, Dandan
   Ren, Junxiao
   Li, Yanmin
   Tian, Yadong
   Wang, Yanbin
   Jiao, Yuping
   Kang, Xiangtao
   Liu, Xiaojun
TI Transcriptome profile of liver at different physiological stages reveals
   potential mode for lipid metabolism in laying hens
SO BMC GENOMICS
LA English
DT Article
DE RNA-Seq; Laying hens; Liver; Fat metabolism; Function analysis
ID TRIGLYCERIDE TRANSFER PROTEIN; ACID-BINDING PROTEIN;
   LOW-DENSITY-LIPOPROTEIN; ALTERNATIVE SPLICING EVENTS; NEGATIVE-ENERGY
   BALANCE; APOLIPOPROTEIN-B; MESSENGER-RNA; ER-ALPHA; HORMONAL-REGULATION;
   ESTROGEN INDUCTION
AB Background: Liver is an important metabolic organ that plays a critical role in lipid synthesis, degradation, and transport; however, the molecular regulatory mechanisms of lipid metabolism remain unclear in chicken. In this study, RNA-Seq technology was used to investigate differences in expression profiles of hepatic lipid metabolism-related genes and associated pathways between juvenile and laying hens. The study aimed to broaden the understanding of liver lipid metabolism in chicken, and thereby to help improve laying performance in the poultry industry.
   Results: RNA-Seq analysis was carried out on total RNA harvested from the liver of juvenile (n = 3) and laying (n = 3) hens. Compared with juvenile hens, 2567 differentially expressed genes (1082 up-regulated and 1485 down-regulated) with P <= 0.05 were obtained in laying hens, and 960 of these genes were significantly differentially expressed (SDE) at a false discovery rate (FDR) of <= 0.05 and fold-change >= 2 or <= 0.5. In addition, most of the 198 SDE novel genes (91 up-regulated and 107 down-regulated) were discovered highly expressed, and 332 SDE isoforms were identified. Gene ontology (GO) enrichment and KEGG (Kyoto Encyclopedia of Genes and Genomes) pathway analysis showed that the SDE genes were most enrichment in steroid biosynthesis, PPAR signaling pathway, biosynthesis of unsaturated fatty acids, glycerophospholipid metabolism, three amino acid pathways, and pyruvate metabolism (P <= 0.05). The top significantly enriched GO terms among the SDE genes included lipid biosynthesis, cholesterol and sterol metabolic, and oxidation reduction, indicating that principal lipogenesis occurred in the liver of laying hens.
   Conclusions: This study suggests that the majority of changes at the transcriptome level in laying hen liver were closely related to fat metabolism. Some of the SDE uncharacterized novel genes and alternative splicing isoforms that were detected might also take part in lipid metabolism, although this needs further investigation. This study provides valuable information about the expression profiles of mRNAs from chicken liver, and in-depth functional investigations of these mRNAs could provide new insights into the molecular networks of lipid metabolism in chicken liver.
C1 [Li, Hong; Wang, Taian; Xu, Chunlin; Wang, Dandan; Ren, Junxiao; Li, Yanmin; Tian, Yadong; Wang, Yanbin; Jiao, Yuping; Kang, Xiangtao; Liu, Xiaojun] Henan Agr Univ, Coll Anim Sci & Vet Med, Zhengzhou 450002, Peoples R China.
   [Tian, Yadong; Wang, Yanbin; Kang, Xiangtao; Liu, Xiaojun] Henan Innovat Engn Res Ctr Poultry Germplasm Reso, Zhengzhou 450002, Peoples R China.
   [Kang, Xiangtao; Liu, Xiaojun] Henan Agr Univ, Int Joint Res Lab Poultry Breeding Henan, Zhengzhou 450002, Peoples R China.
   [Jiao, Yuping] Henan Acad Agr Sci, Inst Anim Husb & Vet Med, Zhengzhou 450002, Peoples R China.
C3 Henan Agricultural University; Henan Agricultural University; Henan
   Academy of Agricultural Sciences
RP Kang, XT (corresponding author), Henan Agr Univ, Coll Anim Sci & Vet Med, Zhengzhou 450002, Peoples R China.
EM xtkang2001@263.net; xjliu2008@hotmail.com
RI Li, Yan/JQI-3638-2023; Wang, Dandan/AEC-1897-2022; Yang,
   Guoqing/Q-7238-2017; Xu, Chunlin/AGY-2562-2022; Ren,
   Junxiao/GNP-2142-2022
OI Ren, Junxiao/0000-0003-4203-1289
FU Earmarked Fund for Modern Agro-Industry Technology Research System
   [CARS-41-K04]; Program for Innovation Research Team of Ministry of
   Education [IRT1236]; International Cooperation Project of Henan, China
   [144300510044]
FX This research was supported by the Earmarked Fund for Modern
   Agro-Industry Technology Research System (no. CARS-41-K04), the Program
   for Innovation Research Team of Ministry of Education (IRT1236), and the
   International Cooperation Project of Henan, China (144300510044).
CR Anders S, 2015, BIOINFORMATICS, V31, P166, DOI 10.1093/bioinformatics/btu638
   Atshaves BP, 2004, J BIOL CHEM, V279, P30954, DOI 10.1074/jbc.M313571200
   Bergen WG, 2005, J NUTR, V135, P2499, DOI 10.1093/jn/135.11.2499
   Berriot-Varoqueaux N, 2000, ANNU REV NUTR, V20, P663, DOI 10.1146/annurev.nutr.20.1.663
   BRADY L, 1976, COMP BIOCHEM PHYS B, V54, P403, DOI 10.1016/0305-0491(76)90265-0
   Bujo H, 1997, J NUTR, V127, pS801, DOI 10.1093/jn/127.5.801S
   CAPONY F, 1980, BIOCHEMISTRY-US, V19, P2219, DOI 10.1021/bi00551a035
   Cases S, 1998, J BIOL CHEM, V273, P26755, DOI 10.1074/jbc.273.41.26755
   CHAN L, 1976, J CLIN INVEST, V58, P368, DOI 10.1172/JCI108481
   Chen C, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0031426
   Chen R, 2014, J MOL CELL CARDIOL, V72, P263, DOI 10.1016/j.yjmcc.2014.04.003
   Dakovic N, 2014, MOL BIOL EVOL, V31, P2637, DOI 10.1093/molbev/msu208
   DEELEY RG, 1977, J BIOL CHEM, V252, P8310
   Dennis G, 2003, GENOME BIOL, V4, DOI 10.1186/gb-2003-4-9-r60
   Ding ST, 2000, J ANIM SCI, V78, P2127
   Dong E, 2002, LIFE SCI, V70, P1317, DOI 10.1016/S0024-3205(01)01502-8
   EVANS MI, 1988, GENE DEV, V2, P116, DOI 10.1101/gad.2.1.116
   Fatima A, 2014, BMC GENOMICS, V15, DOI 10.1186/1471-2164-15-28
   Ferré P, 2004, DIABETES, V53, pS43, DOI 10.2337/diabetes.53.2007.S43
   Foissac S, 2007, NUCLEIC ACIDS RES, V35, pW297, DOI 10.1093/nar/gkm311
   Gentleman RR, 2008, LANG ENV STAT COMP
   Gondret F, 2001, J LIPID RES, V42, P106
   Gordon DA, 2000, BBA-MOL CELL BIOL L, V1486, P72, DOI 10.1016/S1388-1981(00)00049-4
   GORDON DA, 1995, TRENDS CELL BIOL, V5, P317, DOI 10.1016/S0962-8924(00)89054-6
   Han W, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0129738
   Hermier D, 1996, COMP BIOCHEM PHYS A, V115, P259, DOI 10.1016/0300-9629(96)00057-6
   HILLGARTNER F, 1995, PHYSIOL REV, V75, P47, DOI 10.1152/physrev.1995.75.1.47
   Hiramine Y, 2010, J LIPID RES, V51, P1424, DOI 10.1194/jlr.M002584
   Huang DW, 2009, NUCLEIC ACIDS RES, V37, P1, DOI 10.1093/nar/gkn923
   Hussain MM, 2008, CURR OPIN LIPIDOL, V19, P277, DOI 10.1097/MOL.0b013e3282feea85
   Hussain MM, 2012, NUTR METAB, V9, DOI 10.1186/1743-7075-9-14
   Hussain MM, 2003, FRONT BIOSCI, V8, pS500, DOI 10.2741/1071
   Ivessa NE, 2013, GENE, V523, P1, DOI 10.1016/j.gene.2013.03.102
   Jacobi SK, 2011, J NUTR, V141, P548, DOI 10.3945/jn.110.127118
   JEFFERSON JR, 1990, J BIOL CHEM, V265, P11062
   Johnson JM, 2003, SCIENCE, V302, P2141, DOI 10.1126/science.1090100
   KAIKAUS RM, 1993, J BIOL CHEM, V268, P26866
   Kang XL, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0071763
   Kim D, 2013, GENOME BIOL, V14, DOI 10.1186/gb-2013-14-4-r36
   KIRCHGESSNER TG, 1987, GENE, V59, P241, DOI 10.1016/0378-1119(87)90332-5
   Klasing KC, 1998, POULTRY SCI, V77, P1119, DOI 10.1093/ps/77.8.1119
   Kong L, 2007, NUCLEIC ACIDS RES, V35, pW345, DOI 10.1093/nar/gkm391
   KUMAR V, 1988, CELL, V55, P145, DOI 10.1016/0092-8674(88)90017-7
   Lander ES, 2001, NATURE, V409, P860, DOI 10.1038/35057062
   Leaños-Castañeda O, 2007, TOXICOL APPL PHARM, V224, P116, DOI 10.1016/j.taap.2007.06.017
   Lefevre P, 1999, ARCH BIOCHEM BIOPHYS, V368, P329, DOI 10.1006/abbi.1999.1315
   LEVEILLE GA, 1968, P SOC EXP BIOL MED, V128, P398
   Li J, 2014, THERIOGENOLOGY, V82, P517, DOI 10.1016/j.theriogenology.2014.05.003
   Martin GG, 2003, J BIOL CHEM, V278, P21429, DOI 10.1074/jbc.M300287200
   Mason TM, 1998, CRIT REV CL LAB SCI, V35, P461, DOI 10.1080/10408369891234246
   McCabe M, 2012, BMC GENOMICS, V13, DOI 10.1186/1471-2164-13-193
   Menuet A, 2001, BIOL REPROD, V65, P1548, DOI 10.1095/biolreprod65.5.1548
   Nikolay B, 2013, BIOCHIMIE, V95, P2445, DOI 10.1016/j.biochi.2013.09.005
   OHEA EK, 1968, COMP BIOCHEM PHYSIOL, V26, P111, DOI 10.1016/0010-406X(68)90317-4
   Pache JC, 2006, ENDOCRINOLOGY, V147, P990, DOI 10.1210/en.2005-0663
   Paech K, 1997, SCIENCE, V277, P1508, DOI 10.1126/science.277.5331.1508
   Rava P, 2007, BIOCHEMISTRY-US, V46, P12263, DOI 10.1021/bi700762z
   Riegler B, 2011, BIOCHEM BIOPH RES CO, V406, P257, DOI 10.1016/j.bbrc.2011.02.029
   Rustaeus S, 1999, J NUTR, V129, p463S, DOI 10.1093/jn/129.2.463S
   Rychlik Wojciech, 2007, V402, P35
   Sammeth M, 2009, J COMPUT BIOL, V16, P1117, DOI 10.1089/cmb.2009.0108
   Schmittgen TD, 2008, NAT PROTOC, V3, P1101, DOI 10.1038/nprot.2008.73
   Schneider WJ, 2007, CYTOGENET GENOME RES, V117, P248, DOI 10.1159/000103186
   Schneider Wolfgang J., 1995, Current Opinion in Lipidology, V6, P92, DOI 10.1097/00041433-199504000-00006
   Schneider WJ, 2009, GEN COMP ENDOCR, V163, P18, DOI 10.1016/j.ygcen.2008.11.032
   Schwerk C, 2005, MOL CELL, V19, P1, DOI 10.1016/j.molcel.2005.05.026
   Soh J, 2013, NAT MED, V19, P892, DOI 10.1038/nm.3200
   Trapnell C, 2012, NAT PROTOC, V7, P562, DOI 10.1038/nprot.2012.016
   Traurig MT, 2013, OBESITY, V21, P193, DOI 10.1002/oby.20243
   VEERKAMP JH, 1993, MOL CELL BIOCHEM, V123, P101, DOI 10.1007/BF01076480
   Walzem RL, 1999, J NUTR, V129, p467S, DOI 10.1093/jn/129.2.467S
   Wang ET, 2008, NATURE, V456, P470, DOI 10.1038/nature07509
   Wang NY, 2006, ANAL BIOCHEM, V359, P189, DOI 10.1016/j.ab.2006.09.014
   Wang XG, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0112896
   Wang Z, 2009, NAT REV GENET, V10, P57, DOI 10.1038/nrg2484
   WISKOCIL R, 1980, P NATL ACAD SCI-BIOL, V77, P4474, DOI 10.1073/pnas.77.8.4474
   WOODFORD JK, 1995, MOL CELL BIOCHEM, V152, P51
   Zheng J, 2015, J DIABETES INVEST, V6, P269, DOI 10.1111/jdi.12303
NR 78
TC 91
Z9 108
U1 0
U2 61
PU BMC
PI LONDON
PA CAMPUS, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
SN 1471-2164
J9 BMC GENOMICS
JI BMC Genomics
PD OCT 9
PY 2015
VL 16
AR 763
DI 10.1186/s12864-015-1943-0
PG 13
WC Biotechnology & Applied Microbiology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biotechnology & Applied Microbiology; Genetics & Heredity
GA CT0KI
UT WOS:000362483700003
PM 26452545
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Jeon, JM
   Kim, BK
   Lee, JH
   Kim, HJ
   Kang, CK
   Mykles, DL
   Kim, HW
AF Jeon, Jeong-Min
   Kim, Bo-Kwang
   Lee, Jun Hyuck
   Kim, Hak Jun
   Kang, Chang-Keun
   Mykles, Donald L.
   Kim, Hyun-Woo
TI Two type I crustacean hyperglycemic hormone (CHH) genes in Morotoge
   shrimp (Pandalopsis japonica): Cloning and expression of eyestalk
   and pericardial organ isoforms produced by alternative splicing and a
   novel type I CHH with predicted structure shared with type II CHH
   peptides
SO COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR
   BIOLOGY
LA English
DT Article
DE Crustacean hyperglycemic hormone (CHH); Pandalopsis japonica;
   Neuropeptide; Crustacean; Gene expression
ID MOLT-INHIBITING HORMONE; CRAYFISH PROCAMBARUS-CLARKII; PRECURSOR-RELATED
   PEPTIDES; AMINO-ACID-SEQUENCES; TROPICAL LAND CRAB; KURUMA PRAWN;
   MOLECULAR CHARACTERIZATION; MACROBRACHIUM-ROSENBERGII;
   GECARCINUS-LATERALIS; DECAPOD CRUSTACEANS
AB Crustacean hyperglycemic hormone (CHH) peptide family members play critical roles in growth and reproduction in decapods. Three cDNAs encoding CHH family members (Pj-CHH1ES, Pj-CHH1PO, and Pj-CHH2) were isolated by a combination of bioinformatic analysis and conventional cloning strategies. Pj-CHH1ES and Pj-CHH1PO were products of the same gene that were generated by alternative mRNA splicing, whereas Pj-CHH2 was the product of a second gene. The Pj-CHH1 and Pj-CHH2 genes had four exons and three introns, suggesting the two genes arose from gene duplication. The three cDNAs were classified in the type I CHH subfamily, as the deduced amino acid sequences had a CHH precursor-related peptide sequence positioned between the N-terminal signal sequence and C-terminal mature peptide sequence. The Pj-CHH1ES isoform was expressed at a higher level in the eyestalk X-organ/sinus gland (XO/SG) complex and at a lower level in the gill. The Pj-CHH1PO isoform was expressed at higher levels in the XO/SG complex, brain, abdominal ganglion, and thoracic ganglion and at a lower level in the epidermis. Pj-CHH2 was expressed at a higher level in the thoracic ganglion and at a lower level in the gill. Real-time polymerase chain reaction was used to quantify the effects of eyestalk ablation on the mRNA levels of the three Pj-CHHs in the brain, thoracic ganglion, and gill. Eyestalk ablation reduced expression of Pj-CHH1ES in the brain and Pj-CHH1PO and Pj-CHH2 in the thoracic ganglion. Sequence alignment of the Pj-CHHs with CHHs from other species indicated that Pj-CHH2 had an additional alanine at position #9 of the mature peptide. Molecular modeling showed that the Pj-CHH2 mature peptide had a short alpha helix (alpha 1) in the N-terminal region, which is characteristic of type II CHHs. This suggests that Pj-CHH2 differs in function from other type 1 CHHs. (C) 2012 Elsevier Inc. All rights reserved.
C1 [Jeon, Jeong-Min; Kim, Bo-Kwang; Kim, Hyun-Woo] Pukyong Natl Univ, Dept Marine Biol, Pusan 608737, South Korea.
   [Lee, Jun Hyuck; Kim, Hak Jun] Korea Polar Res Inst, Div Polar Biol & Ocean Sci, Inchon 406840, South Korea.
   [Kang, Chang-Keun] Pohang Univ Sci & Technol, POSTECH Ocean Sci & Technol Inst, Pohang 790784, South Korea.
   [Mykles, Donald L.] Colorado State Univ, Dept Biol, Ft Collins, CO 80523 USA.
C3 Pukyong National University; Korea Institute of Ocean Science &
   Technology (KIOST); Korea Polar Research Institute (KOPRI); Pohang
   University of Science & Technology (POSTECH); Colorado State University
   System; Colorado State University Fort Collins
RP Kim, HW (corresponding author), Pukyong Natl Univ, Dept Marine Biol, Pusan 608737, South Korea.
EM kimhw@pknu.ac.kr
RI Kim, Hyun-Woo/AFN-9184-2022; Kang, Chang-Keun/GLR-8512-2022; Kim,
   Seok-Hwan/G-9981-2015
OI Mykles, Donald/0000-0003-4030-2575; Kim, Seok-Hwan/0000-0003-0209-0444
FU Ministry of Land, Transport and Maritime Affairs, Korea; Ministry of
   Maritime Affairs and Fisheries
FX This research was a part of the project titled "Long-term change of
   structure and function in marine ecosystems of Korea" funded by the
   Ministry of Land, Transport and Maritime Affairs, Korea; this work is
   supported by the Ministry of Maritime Affairs and Fisheries (EAST-1
   project).
CR Böcking D, 2002, CRUSTACEAN NERVOUS SYSTEM, P84
   BREATHNACH R, 1981, ANNU REV BIOCHEM, V50, P349, DOI 10.1146/annurev.bi.50.070181.002025
   Bulau P, 2003, PEPTIDES, V24, P1871, DOI 10.1016/j.peptides.2003.10.002
   Chan SM, 2003, GEN COMP ENDOCR, V134, P214, DOI 10.1016/S0016-6480(03)00263-6
   Chang CC, 2010, GEN COMP ENDOCR, V167, P68, DOI 10.1016/j.ygcen.2010.02.013
   Chang ES, 2011, GEN COMP ENDOCR, V172, P323, DOI 10.1016/j.ygcen.2011.04.003
   Chang ES, 1999, J COMP NEUROL, V414, P50
   Chang ES, 2005, INTEGR COMP BIOL, V45, P43, DOI 10.1093/icb/45.1.43
   Charmantier G., 1997, Recent Advances in Marine Biotechnology, VI, P109
   Chen HY, 2007, GEN COMP ENDOCR, V151, P72, DOI 10.1016/j.ygcen.2006.11.016
   Chen SH, 2004, MAR BIOTECHNOL, V6, P83, DOI 10.1007/s10126-003-0014-8
   Chen SH, 2005, MAR BIOTECHNOL, V7, P193, DOI 10.1007/s10126-004-0020-5
   Choi CY, 2006, GEN COMP ENDOCR, V148, P383, DOI 10.1016/j.ygcen.2006.03.003
   Chung JS, 2008, FEBS J, V275, P693, DOI 10.1111/j.1742-4658.2007.06231.x
   Chung JS, 2005, ENDOCRINOLOGY, V146, P5545, DOI 10.1210/en.2005-0859
   Chung JS, 2003, EUR J BIOCHEM, V270, P3280, DOI 10.1046/j.1432-1033.2003.03720.x
   Chung JS, 1999, P NATL ACAD SCI USA, V96, P13103, DOI 10.1073/pnas.96.23.13103
   Davis IW, 2007, NUCLEIC ACIDS RES, V35, pW375, DOI 10.1093/nar/gkm216
   De Kleijn DPV, 1998, INVERTEBR REPROD DEV, V33, P263, DOI 10.1080/07924259.1998.9652637
   de Kleijn DPV, 1998, J ENDOCRINOL, V156, P291, DOI 10.1677/joe.0.1560291
   DEKLEIJN DPV, 1994, EUR J BIOCHEM, V224, P623, DOI 10.1111/j.1432-1033.1994.00623.x
   Delano W. L., 2002, The pymol molecular graphics system
   Dircksen H, 2001, BIOCHEM J, V356, P159, DOI 10.1042/0264-6021:3560159
   Dircksen H, 2009, J EXP BIOL, V212, P401, DOI 10.1242/jeb.026112
   Escamllla-Chimal EG, 2001, J EXP BIOL, V204, P1073
   Fanjul-Moles ML, 2006, COMP BIOCHEM PHYS C, V142, P390, DOI 10.1016/j.cbpc.2005.11.021
   Fu Q, 2005, PEPTIDES, V26, P2137, DOI 10.1016/j.peptides.2005.03.040
   Giulianini Piero Giulio, 2006, P225
   Gu PL, 2002, PEPTIDES, V23, P1875, DOI 10.1016/S0196-9781(02)00178-X
   Gu PL, 1998, FEBS LETT, V441, P397, DOI 10.1016/S0014-5793(98)01573-7
   Gu PL, 2000, FEBS LETT, V472, P122, DOI 10.1016/S0014-5793(00)01420-4
   Hopkins PM, 2012, GEN COMP ENDOCR, V175, P357, DOI 10.1016/j.ygcen.2011.12.002
   Hsu YWA, 2008, GEN COMP ENDOCR, V155, P517, DOI 10.1016/j.ygcen.2007.09.001
   Hsu YWA, 2006, J EXP BIOL, V209, P3241, DOI 10.1242/jeb.02372
   Jeon JM, 2010, COMP BIOCHEM PHYS B, V157, P102, DOI 10.1016/j.cbpb.2010.05.006
   Katayama H, 2002, PEPTIDES, V23, P1537, DOI 10.1016/S0196-9781(02)00094-3
   Katayama H, 2004, BIOCHEMISTRY-US, V43, P9629, DOI 10.1021/bi049433v
   Katayama H, 2003, J BIOL CHEM, V278, P9620, DOI 10.1074/jbc.M212962200
   Katayama H, 2004, ZOOL SCI, V21, P1121, DOI 10.2108/zsj.21.1121
   KELLER R, 1985, AM ZOOL, V25, P207
   KELLER R, 1992, EXPERIENTIA, V48, P439, DOI 10.1007/BF01928162
   Kim KS, 2008, COMP BIOCHEM PHYS B, V151, P52, DOI 10.1016/j.cbpb.2008.05.009
   Krungkasem C, 2002, MAR BIOTECHNOL, V4, P132, DOI 10.1007/s10126-001-0079-1
   Lacombe C, 1999, NEUROPEPTIDES, V33, P71, DOI 10.1054/npep.1999.0016
   Lee KJ, 2007, GEN COMP ENDOCR, V154, P174, DOI 10.1016/j.ygcen.2007.05.019
   Lee KJ, 2007, GEN COMP ENDOCR, V150, P505, DOI 10.1016/j.ygcen.2006.09.013
   Lee SO, 2011, COMP BIOCHEM PHYS B, V159, P148, DOI 10.1016/j.cbpb.2011.03.004
   Macins A, 1999, ARCH INSECT BIOCHEM, V40, P107, DOI 10.1002/(SICI)1520-6327(1999)40:2<107::AID-ARCH5>3.0.CO;2-B
   Meredith J, 1996, J EXP BIOL, V199, P1053
   MERKLER DJ, 1994, ENZYME MICROB TECH, V16, P450, DOI 10.1016/0141-0229(94)90014-0
   Mettulio R, 2004, REGUL PEPTIDES, V119, P189, DOI 10.1016/j.regpep.2004.02.002
   Montagné N, 2010, BMC EVOL BIOL, V10, DOI 10.1186/1471-2148-10-62
   Mosco A, 2008, REGUL PEPTIDES, V147, P88, DOI 10.1016/j.regpep.2008.01.005
   Mykles DL, 2011, J STEROID BIOCHEM, V127, P196, DOI 10.1016/j.jsbmb.2010.09.001
   Nagaraju GPC, 2011, J EXP BIOL, V214, P3, DOI 10.1242/jeb.047183
   Nakatsuji T, 2009, COMP BIOCHEM PHYS A, V152, P139, DOI 10.1016/j.cbpa.2008.10.012
   Nakatsuji T, 2006, MOL CELL ENDOCRINOL, V253, P76, DOI 10.1016/j.mce.2006.05.001
   Ohira T, 2006, ZOOL SCI, V23, P383, DOI 10.2108/zsj.23.383
   Peitsch MC, 1996, BIOCHEM SOC T, V24, P274, DOI 10.1042/bst0240274
   Perez Farfante I., 1997, Memoires du Museum National d'Histoire Naturelle, V175, P1
   Qian YQ, 2009, COMP BIOCHEM PHYS B, V154, P37, DOI 10.1016/j.cbpb.2009.04.013
   Serrano L, 2003, J EXP BIOL, V206, P979, DOI 10.1242/jeb.00178
   SOYEZ D, 1994, J BIOL CHEM, V269, P18295
   Tamura K, 2007, MOL BIOL EVOL, V24, P1596, DOI 10.1093/molbev/msm092
   Thompson JD, 1997, NUCLEIC ACIDS RES, V25, P4876, DOI 10.1093/nar/25.24.4876
   Tsutsui N, 2007, MAR BIOTECHNOL, V9, P360, DOI 10.1007/s10126-006-6151-0
   Webster SG, 1996, J EXP BIOL, V199, P1579
   WEBSTER SG, 1986, GEN COMP ENDOCR, V61, P237, DOI 10.1016/0016-6480(86)90201-7
   Webster SG, 2012, GEN COMP ENDOCR, V175, P217, DOI 10.1016/j.ygcen.2011.11.035
   Wilcockson DC, 2002, CELL TISSUE RES, V307, P129, DOI 10.1007/s00441-001-0469-8
   Wiwegweaw A, 2004, J BIOCHEM MOL BIOL, V37, P177
   Yang WJ, 1997, PEPTIDES, V18, P479, DOI 10.1016/S0196-9781(96)00332-4
   Yang WJ, 1996, PEPTIDES, V17, P197, DOI 10.1016/0196-9781(95)02122-1
   Yang WJ, 1995, AQUACULTURE, V135, P205, DOI 10.1016/0044-8486(95)01015-7
   YASUDA A, 1994, GEN COMP ENDOCR, V95, P387, DOI 10.1006/gcen.1994.1138
   Zheng JY, 2010, GEN COMP ENDOCR, V169, P174, DOI 10.1016/j.ygcen.2010.07.013
NR 76
TC 18
Z9 21
U1 1
U2 20
PU ELSEVIER SCIENCE INC
PI NEW YORK
PA STE 800, 230 PARK AVE, NEW YORK, NY 10169 USA
SN 1096-4959
EI 1879-1107
J9 COMP BIOCHEM PHYS B
JI Comp. Biochem. Physiol. B-Biochem. Mol. Biol.
PD AUG
PY 2012
VL 162
IS 4
BP 88
EP 99
DI 10.1016/j.cbpb.2012.04.003
PG 12
WC Biochemistry & Molecular Biology; Zoology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Zoology
GA 964QP
UT WOS:000305712100005
PM 22525298
DA 2025-04-10
ER

PT J
AU Malara, A
   Gruppi, C
   Massa, M
   Tira, ME
   Rosti, V
   Balduini, A
   Barosi, G
AF Malara, Alessandro
   Gruppi, Cristian
   Massa, Margherita
   Tira, Maria Enrica
   Rosti, Vittorio
   Balduini, Alessandra
   Barosi, Giovanni
TI Elevated plasma EDA fibronectin in primary myelofibrosis is determined
   by high allele burden of JAK2V617F mutation and strongly predicts
   splenomegaly progression
SO FRONTIERS IN ONCOLOGY
LA English
DT Article
DE primary myelofibrosis; splenomegaly; neoangiogenesis; extra domain A;
   fibronectin
ID EXTRA-DOMAIN; ENDOTHELIAL-CELLS; SPLEEN; EIIIA; EXPRESSION
AB In primary myelofibrosis, extra-domain A fibronectin (EDA-FN), the result of alternative splicing of FN gene, sustains megakaryocyte proliferation and confers a pro-inflammatory phenotype to bone marrow cell niches. In this work we assessed the levels of circulating EDA-FN in plasma samples of 122 patients with primary myelofibrosis. Patients with a homozygous JAK2V617F genotype displayed the higher level of plasma EDA-FN. Increased EDA-FN levels were associated with anemia, elevated high-sensitivity C-reactive protein, bone marrow fibrosis and splanchnic vein thrombosis at diagnosis. While no correlation was observed with CD34+ hematopoietic stem cell mobilization, elevated blood level of EDA-FN at diagnosis was a predictor of large splenomegaly (over 10 cm from the left costal margin) outcome. Thus, EDA-FN expression in primary myelofibrosis may represent the first marker of disease progression, and a novel target to treat splenomegaly.
C1 [Malara, Alessandro; Gruppi, Cristian; Balduini, Alessandra] Univ Pavia, Dept Mol Med, Pavia, Italy.
   [Massa, Margherita; Rosti, Vittorio; Barosi, Giovanni] IRCCS Policlin S Matteo Fdn, Ctr Study Myelofibrosis, Lab Biochem Biotechnol & Adv Diagnost, Pavia, Italy.
   [Tira, Maria Enrica] Univ Pavia, Dept Biol & Biotechnol Lazzaro Spallanzani, Pavia, Italy.
C3 University of Pavia; IRCCS Fondazione San Matteo; University of Pavia
RP Malara, A; Balduini, A (corresponding author), Univ Pavia, Dept Mol Med, Pavia, Italy.
EM alessandro.malara@unipv.it; alessandra.balduini@unipv.it
RI Barosi, Giovanni/AAI-1714-2019; BALDUINI, ALESSANDRA/AAC-3363-2022;
   Rosti, Vittorio/K-1743-2018; MALARA, ALESSANDRO/K-4027-2016
OI MALARA, ALESSANDRO/0000-0002-3396-3693
FU Associazione Italiana per la Ricerca sul Cancro (AIRC; Milano, Italy)
   [AIRC IG 2016 18700]; Italian Ministry of Health [GR-2016-02363136]
FX This paper was supported by Associazione Italiana per la Ricerca sul
   Cancro (AIRC IG 2016 18700, AIRC; Milano, Italy) to AB; Italian Ministry
   of Health (Ricerca Finalizzata Giovani Ricercatori GR-2016-02363136) to
   AM.
CR Astrof S, 2004, MOL CELL BIOL, V24, P8662, DOI 10.1128/MCB.24.19.8662-8670.2004
   Astrof S, 2009, ANGIOGENESIS, V12, P165, DOI 10.1007/s10456-009-9136-6
   Barosi G, 2004, BRIT J HAEMATOL, V124, P618, DOI 10.1111/j.1365-2141.2004.04829.x
   Bazan-Socha S, 2018, RESP MED, V141, P64, DOI 10.1016/j.rmed.2018.06.023
   Dhanesha N, 2019, STROKE, V50, P1201, DOI 10.1161/STROKEAHA.118.023697
   Doddapattar P, 2015, ARTERIOSCL THROM VAS, V35, P2391, DOI 10.1161/ATVBAHA.115.306474
   Erba BG, 2017, AM J PATHOL, V187, P1879, DOI 10.1016/j.ajpath.2017.04.006
   Fisher DAC, 2017, LEUKEMIA, V31, P1962, DOI 10.1038/leu.2016.377
   Guy A, 2019, HAEMATOLOGICA, V104, P70, DOI 10.3324/haematol.2018.195321
   Halin C, 2002, NAT BIOTECHNOL, V20, P264, DOI 10.1038/nbt0302-264
   Han Z, 2017, J MATER CHEM B, V5, P639, DOI [10.1039/c6tb02008a, 10.1039/C6TB02008A]
   JARNAGIN WR, 1994, J CELL BIOL, V127, P2037, DOI 10.1083/jcb.127.6.2037
   Kelsh-Lasher RM, 2017, J INVEST DERMATOL, V137, P2505, DOI 10.1016/j.jid.2017.08.005
   Lemanska-Perek A, 2016, INFLAMMATION, V39, P1059, DOI 10.1007/s10753-016-0336-0
   Malara A, 2019, J EXP MED, V216, P587, DOI 10.1084/jem.20181074
   Malara A, 2018, HAEMATOLOGICA, V103, pE42, DOI 10.3324/haematol.2017.173070
   Malara A, 2016, STEM CELLS, V34, P2263, DOI 10.1002/stem.2381
   Muro AF, 2003, J CELL BIOL, V162, P149, DOI 10.1083/jcb.200212079
   Muro AF, 2008, AM J RESP CRIT CARE, V177, P638, DOI 10.1164/rccm.200708-1291OC
   Ou JJ, 2010, CANCER BIOL THER, V9, P186, DOI 10.4161/cbt.9.3.10651
   Ou JJ, 2014, CARCINOGENESIS, V35, P1661, DOI 10.1093/carcin/bgu090
   Rossnagl S, 2016, PLOS BIOL, V14, DOI 10.1371/journal.pbio.1002562
   Rosti V, 2013, BLOOD, V121, P360, DOI 10.1182/blood-2012-01-404889
   Rybak JN, 2007, CANCER RES, V67, P10948, DOI 10.1158/0008-5472.CAN-07-1436
   Sozer S, 2009, BLOOD, V113, P5246, DOI 10.1182/blood-2008-11-191544
   Tefferi A, 2021, AM J HEMATOL, V96, P145, DOI 10.1002/ajh.26050
   To WS, 2011, FIBROGENESIS TISSUE, V4, DOI 10.1186/1755-1536-4-21
   White ES, 2008, J PATHOL, V216, P1, DOI 10.1002/path.2388
   Xiang LS, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0035378
NR 29
TC 4
Z9 5
U1 1
U2 6
PU FRONTIERS MEDIA SA
PI LAUSANNE
PA AVENUE DU TRIBUNAL FEDERAL 34, LAUSANNE, CH-1015, SWITZERLAND
SN 2234-943X
J9 FRONT ONCOL
JI Front. Oncol.
PD SEP 21
PY 2022
VL 12
AR 987643
DI 10.3389/fonc.2022.987643
PG 8
WC Oncology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Oncology
GA 5U2DR
UT WOS:000876363300001
PM 36212480
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Huber, RM
   Murphy, K
   Miao, B
   Link, JR
   Cunningham, MR
   Rupar, MJ
   Gunyuzlu, PL
   Haws, TF
   Kassam, A
   Powell, F
   Hollis, GF
   Young, PR
   Mukherjee, R
   Burn, TC
AF Huber, RM
   Murphy, K
   Miao, B
   Link, JR
   Cunningham, MR
   Rupar, MJ
   Gunyuzlu, PL
   Haws, TF
   Kassam, A
   Powell, F
   Hollis, GF
   Young, PR
   Mukherjee, R
   Burn, TC
TI Generation of multiple farnesoid-X-receptor isoforms through the use of
   alternative promoters
SO GENE
LA English
DT Article
DE NR1H4; farnesoid-X-receptor; bile acid; nuclear hormone receptor;
   differential expression
ID THYROID-HORMONE RECEPTOR; ORPHAN NUCLEAR RECEPTOR; BILE-ACID;
   GENE-EXPRESSION; RETINOIC ACID; MESSENGER-RNA; HUMAN-TISSUES; GAMMA
   GENE; IDENTIFICATION; LIGANDS
AB Bile acid biosynthesis is regulated by both feed-forward and feedback mechanisms involving a cascade of nuclear hormone receptors. Feed-forward regulation of the rate limiting enzyme in bile acid biosynthesis is provided by oxysterols through liver-X-receptor alpha (NR1H3), while feedback regulation is provided by bile acids through farnesoid-X-receptor (FXR) (NR1H4). The Syrian golden hamster provides, a useful model for studying lipid metabolism. The hamster metabolizes and transports dietary cholesterol in a similar manner to humans, with the resulting lipid profile being more similar to the human profile than that of other rodent models. Cloning of Fxr from Syrian golden hamster revealed four hamster Fxr splice variants that altered the N-terminal activation domain or the hinge region between the DNA and ligand binding domains. Human genomic sequence and data from hamster Fxr were used to identify and clone a novel human FXR isoform resulting from the use of an alternative promoter. RNA expression analysis indicates that the two human FXR isoforms are differentially expressed in developmental and tissue-specific patterns and are likely to provide a mechanism for cell-specific FXR-dependent transcriptional activity. (C) 2002 Elsevier Science B.V. All rights reserved.
C1 Bristol Myers Squibb Co, Metab Dis, Expt Stn E4003468, Dept Metab Dis, Wilmington, DE 19880 USA.
   Bristol Myers Squibb Co, Expt Stn, Dept Biotechnol, Wilmington, DE 19880 USA.
C3 Bristol-Myers Squibb; Bristol-Myers Squibb; DuPont; DuPont USA
RP Mukherjee, R (corresponding author), Bristol Myers Squibb Co, Metab Dis, Expt Stn E4003468, Dept Metab Dis, POB 80400, Wilmington, DE 19880 USA.
EM ranjan.mukherjee@bms.com
OI Burn, Timothy/0000-0001-6648-4333
CR ARBEENY CM, 1992, J LIPID RES, V33, P843
   BURNSTEIN KL, 1991, STEROIDS, V56, P52, DOI 10.1016/0039-128X(91)90124-E
   Chawla A, 2000, CELL, V103, P1, DOI 10.1016/S0092-8674(00)00097-0
   FORMAN BM, 1995, CELL, V81, P687, DOI 10.1016/0092-8674(95)90530-8
   Gibson UEM, 1996, GENOME RES, V6, P995, DOI 10.1101/gr.6.10.995
   Goodwin B, 2000, MOL CELL, V6, P517, DOI 10.1016/S1097-2765(00)00051-4
   Grad JM, 1999, MOL ENDOCRINOL, V13, P1896, DOI 10.1210/me.13.11.1896
   Grober J, 1999, J BIOL CHEM, V274, P29749, DOI 10.1074/jbc.274.42.29749
   HODIN RA, 1989, SCIENCE, V244, P76, DOI 10.1126/science.2539642
   HORTON JD, 1995, J BIOL CHEM, V270, P5381, DOI 10.1074/jbc.270.10.5381
   KATO S, 1992, BIOCHEM J, V286, P755, DOI 10.1042/bj2860755
   Lander ES, 2001, NATURE, V409, P860, DOI 10.1038/35057062
   LEID M, 1992, TRENDS BIOCHEM SCI, V17, P427, DOI 10.1016/0968-0004(92)90014-Z
   Lu TT, 2000, MOL CELL, V6, P507, DOI 10.1016/S1097-2765(00)00050-2
   Makishima M, 1999, SCIENCE, V284, P1362, DOI 10.1126/science.284.5418.1362
   Maloney PR, 2000, J MED CHEM, V43, P2971, DOI 10.1021/jm0002127
   Oberste-Berghaus C, 2000, J BIOL CHEM, V275, P1787, DOI 10.1074/jbc.275.3.1787
   Parks DJ, 1999, SCIENCE, V284, P1365, DOI 10.1126/science.284.5418.1365
   SAKURAI A, 1989, MOL ENDOCRINOL, V3, P392, DOI 10.1210/mend-3-2-392
   SEOL WG, 1995, MOL ENDOCRINOL, V9, P72, DOI 10.1210/me.9.1.72
   Shih DQ, 2001, NAT GENET, V27, P375, DOI 10.1038/86871
   Sinal CJ, 2000, CELL, V102, P731, DOI 10.1016/S0092-8674(00)00062-3
   SULLIVAN MP, 1993, LAB ANIM SCI, V43, P575
   Valmaseda A, 1999, MOL CELL ENDOCRINOL, V154, P101, DOI 10.1016/S0303-7207(99)00081-7
   VidalPuig AJ, 1997, J CLIN INVEST, V99, P2416, DOI 10.1172/JCI119424
   Wang HB, 1999, MOL CELL, V3, P543, DOI 10.1016/S1097-2765(00)80348-2
   Zavacki AM, 1997, P NATL ACAD SCI USA, V94, P7909, DOI 10.1073/pnas.94.15.7909
   ZHU YJ, 1995, P NATL ACAD SCI USA, V92, P7921, DOI 10.1073/pnas.92.17.7921
NR 28
TC 172
Z9 210
U1 4
U2 17
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 0378-1119
J9 GENE
JI Gene
PD MAY 15
PY 2002
VL 290
IS 1-2
BP 35
EP 43
AR PII S0378-1119(02)00557-7
DI 10.1016/S0378-1119(02)00557-7
PG 9
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA 567HN
UT WOS:000176479500003
PM 12062799
DA 2025-04-10
ER

PT J
AU Xu, S
   Zhou, LY
   Ponnusamy, M
   Zhang, LX
   Dong, YH
   Zhang, YH
   Wang, Q
   Liu, J
   Wang, K
AF Xu, Sheng
   Zhou, LuYu
   Ponnusamy, Murugavel
   Zhang, LiXia
   Dong, YanHan
   Zhang, YanHui
   Wang, Qi
   Liu, Jing
   Wang, Kun
TI A comprehensive review of circRNA: from purification and identification
   to disease marker potential
SO PEERJ
LA English
DT Review
DE CircRNA; Diseases; Marker; Database
ID CIRCULAR RNA EXPRESSION; HUMAN CANCER; BIOMARKER; BIOGENESIS; LANDSCAPE;
   TRANSLATION; REVEALS; PATHWAY; GENES; TRANSCRIPTION
AB Circular RNA (circRNA) is an endogenous noncoding RNA with a covalently closed cyclic structure. Based on their components, circRNAs are divided into exonic circRNAs, intronic circRNAs, and exon-intron circRNAs. CircRNAs have well-conserved sequences and often have high stability due to their resistance to exonucleases. Depending on their sequence, circRNAs are involved in different biological functions, including microRNA sponge activity, modulation of alternative splicing or transcription, interaction with RNA-binding proteins, and rolling translation, and are a derivative of pseudogenes. CircRNAs are involved in the development of a variety of pathological conditions, such as cardiovascular diseases, diabetes, neurological diseases, and cancer. Emerging evidence has shown that circRNAs are likely to be new potential clinical diagnostic markers or treatments for many diseases. Here we describe circRNA research methods and biological functions, and discuss the potential relationship between circRNAs and disease progression.
C1 [Xu, Sheng; Zhou, LuYu; Ponnusamy, Murugavel; Dong, YanHan; Zhang, YanHui; Wang, Qi; Liu, Jing; Wang, Kun] Qingdao Univ, Ctr Dev Cardiol, Inst Translat Med, Qingdao, Shandong, Peoples R China.
   [Xu, Sheng; Zhou, LuYu; Ponnusamy, Murugavel; Dong, YanHan; Zhang, YanHui; Wang, Qi; Liu, Jing; Wang, Kun] Qingdao Univ, Sch Basic Med, Qingdao, Shandong, Peoples R China.
   [Zhang, LiXia] Qingdao Univ, Dept Inspect, Med Fac, Qingdao, Shandong, Peoples R China.
C3 Qingdao University; Qingdao University; Qingdao University
RP Wang, K (corresponding author), Qingdao Univ, Ctr Dev Cardiol, Inst Translat Med, Qingdao, Shandong, Peoples R China.; Wang, K (corresponding author), Qingdao Univ, Sch Basic Med, Qingdao, Shandong, Peoples R China.
EM wangk696@qdu.edu.cn
RI Zhang, Yanhui/L-5680-2017; Zhang, Lixia/E-2898-2014; Wang,
   Qi/JPK-3520-2023; Ponnusamy, Murugavel/X-5699-2018
OI Dong, Yanhan/0000-0001-9940-1303; Ponnusamy,
   Murugavel/0000-0001-5558-8719
FU National Natural Science Foundation of China Youth Fund Project
   [81522005]; National Natural Science Foundation of China [81470522,
   81500222]; Shandong Province Natural Science Outstanding Youth Fund
   [2016JQB01015]; China Postdoctoral Science Foundation [2017M612213]
FX This work was supported by a grant from the National Natural Science
   Foundation of China Youth Fund Project (81522005); National Natural
   Science Foundation of China (81470522); National Natural Science
   Foundation of China (81500222); Shandong Province Natural Science
   Outstanding Youth Fund (2016JQB01015); China Postdoctoral Science
   Foundation (2017M612213). The funders had no role in study design, data
   collection and analysis, decision to publish, or preparation of the
   manuscript.
CR Abe N, 2015, SCI REP-UK, V5, DOI 10.1038/srep16435
   Aktas T, 2017, NATURE, V544, P115, DOI 10.1038/nature21715
   Ashwal-Fluss R, 2014, MOL CELL, V56, P55, DOI 10.1016/j.molcel.2014.08.019
   Bahn JH, 2015, CLIN CHEM, V61, P221, DOI 10.1373/clinchem.2014.230433
   Barrett SP, 2017, PLOS GENET, V13, DOI 10.1371/journal.pgen.1007114
   Burd CE, 2010, PLOS GENET, V6, DOI 10.1371/journal.pgen.1001233
   Chen J, 2017, CANCER LETT, V388, P208, DOI 10.1016/j.canlet.2016.12.006
   Chen L, 2017, ONCOGENE, V36, P4551, DOI 10.1038/onc.2017.89
   Chen LL, 2016, NAT REV MOL CELL BIO, V17, P205, DOI 10.1038/nrm.2015.32
   Chen SJ, 2017, CLIN CHIM ACTA, V466, P167, DOI 10.1016/j.cca.2017.01.025
   Chen XP, 2016, SCI REP-UK, V6, DOI 10.1038/srep34985
   Chen YG, 2017, MOL CELL, V67, P228, DOI 10.1016/j.molcel.2017.05.022
   COCQUERELLE C, 1993, FASEB J, V7, P155, DOI 10.1096/fasebj.7.1.7678559
   Conn SJ, 2015, CELL, V160, P1125, DOI 10.1016/j.cell.2015.02.014
   Couderc C, 2016, NEOPLASIA, V18, P10, DOI 10.1016/j.neo.2015.11.010
   Cui XL, 2016, BIOMARK MED, V10, P943, DOI 10.2217/bmm-2016-0130
   Danan M, 2012, NUCLEIC ACIDS RES, V40, P3131, DOI 10.1093/nar/gkr1009
   Doi A, 2015, GENES CELLS, V20, P310, DOI 10.1111/gtc.12222
   Dong R, 2016, CELL RES, V26, P747, DOI 10.1038/cr.2016.42
   Du WW, 2017, EUR HEART J, V38, P1402, DOI 10.1093/eurheartj/ehw001
   Du WW, 2016, NUCLEIC ACIDS RES, V44, P2846, DOI 10.1093/nar/gkw027
   Dudekulay DB, 2016, RNA BIOL, V13, P34, DOI 10.1080/15476286.2015.1128065
   Ebbesen KK, 2016, BBA-GENE REGUL MECH, V1859, P163, DOI 10.1016/j.bbagrm.2015.07.007
   Errichelli L, 2017, NAT COMMUN, V8, DOI 10.1038/ncomms14741
   Fan XM, 2017, BIOMED RES INT, V2017, DOI 10.1155/2017/5135781
   Fei T, 2017, P NATL ACAD SCI USA, V114, pE5207, DOI 10.1073/pnas.1617467114
   Fu LY, 2017, ONCOTARGET, V8, P58405, DOI 10.18632/oncotarget.16881
   Gao Y., 2017, BRIEF BIOINFORM, DOI [DOI 10.1155/2017/8717369, DOI 10.1093/BIB/BBX014, 10.1093/bib/bbx014]
   Geng HH, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0151753
   Glazar P, 2014, RNA, V20, P1666, DOI 10.1261/rna.043687.113
   Guarnerio J, 2016, CELL, V165, P289, DOI 10.1016/j.cell.2016.03.020
   Guo WZ, 2017, ONCOTARGET, V8, P48169, DOI 10.18632/oncotarget.18327
   Han D, 2017, HEPATOLOGY, V66, P1151, DOI 10.1002/hep.29270
   Hancock JM, 2015, FRONT GENET, V5, DOI 10.3389/fgene.2014.00459
   Hansen TB, 2013, CANCER RES, V73, P5609, DOI 10.1158/0008-5472.CAN-13-1568
   Hansen TB, 2013, NATURE, V495, P384, DOI 10.1038/nature11993
   Hansen TB, 2011, EMBO J, V30, P4414, DOI 10.1038/emboj.2011.359
   Hentze MW, 2013, EMBO J, V32, P923, DOI 10.1038/emboj.2013.53
   Hoffmann S, 2014, GENOME BIOL, V15, DOI 10.1186/gb-2014-15-2-r34
   Holdt LM, 2018, CELL MOL LIFE SCI, V75, P1071, DOI 10.1007/s00018-017-2688-5
   Holdt LM, 2016, NAT COMMUN, V7, DOI 10.1038/ncomms12429
   Hsiao KY, 2017, CANCER RES, V77, P2339, DOI 10.1158/0008-5472.CAN-16-1883
   Huang C, 2018, GENE DEV, V32, P639, DOI 10.1101/gad.314856.118
   Huang C, 2015, TRANSCR-AUSTIN, V6, P61, DOI 10.1080/21541264.2015.1071301
   Huang GL, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0131225
   Huang RR, 2017, AUTOPHAGY, V13, P1722, DOI 10.1080/15548627.2017.1356975
   Ivanov A, 2015, CELL REP, V10, P170, DOI 10.1016/j.celrep.2014.12.019
   Jeck WR, 2014, NAT BIOTECHNOL, V32, P453, DOI 10.1038/nbt.2890
   Jeck WR, 2013, RNA, V19, P141, DOI 10.1261/rna.035667.112
   Kalyana-Sundaram S, 2012, CELL, V149, P1622, DOI 10.1016/j.cell.2012.04.041
   Kramer MC, 2015, GENE DEV, V29, P2168, DOI 10.1101/gad.270421.115
   Kumar L, 2017, MOL NEUROBIOL, V54, P7224, DOI 10.1007/s12035-016-0213-8
   Lee BY, 2015, PHARMACOL THERAPEUT, V146, P132, DOI 10.1016/j.pharmthera.2014.10.001
   Legnini I, 2017, MOL CELL, V66, P22, DOI 10.1016/j.molcel.2017.02.017
   Li B, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0090096
   Li F, 2015, ONCOTARGET, V6, P6001, DOI 10.18632/oncotarget.3469
   Li JQ, 2015, AM J CANCER RES, V5, P472
   Li JH, 2014, NUCLEIC ACIDS RES, V42, pD92, DOI 10.1093/nar/gkt1248
   Li PF, 2015, CLIN CHIM ACTA, V444, P132, DOI 10.1016/j.cca.2015.02.018
   Li SS, 2019, BRIEF BIOINFORM, V20, P1420, DOI 10.1093/bib/bby006
   Li X, 2017, MOL CELL, V67, P214, DOI 10.1016/j.molcel.2017.05.023
   Li ZY, 2017, NAT STRUCT MOL BIOL, V24, P194, DOI 10.1038/nsmb0217-194a
   Liang DM, 2017, MOL CELL, V68, P940, DOI 10.1016/j.molcel.2017.10.034
   Lin F, 2018, Zhonghua Yi Xue Za Zhi, V98, P851, DOI 10.3760/cma.j.issn.0376-2491.2018.11.012
   Lin SP, 2016, BIOCHEM BIOPH RES CO, V471, P52, DOI 10.1016/j.bbrc.2016.01.183
   Lü LS, 2017, ONCOTARGET, V8, P44096, DOI 10.18632/oncotarget.17307
   Lukiw Walter J., 2013, Frontiers in Genetics, V4, P77, DOI [10.3389/fgene.2013.00307, 10.3389/fgene.2013.00077]
   Memczak S, 2013, NATURE, V495, P333, DOI 10.1038/nature11928
   Mendis S, 2015, STROKE, V46, pE121, DOI 10.1161/STROKEAHA.115.008097
   Meng J, 2018, CANCER RES, V78, P4150, DOI 10.1158/0008-5472.CAN-17-3009
   Meng SJ, 2017, MOL CANCER, V16, DOI 10.1186/s12943-017-0663-2
   Metge F, 2017, PEERJ, V5, DOI 10.7717/peerj.2934
   Morris KV, 2014, NAT REV GENET, V15, P423, DOI 10.1038/nrg3722
   Mozaffarian D, 2015, CIRCULATION, V131, pE29, DOI 10.1161/CIR.0000000000000152
   Nan A, 2017, ARCH TOXICOL, V91, P1671, DOI 10.1007/s00204-016-1837-1
   Pamudurti NR, 2017, MOL CELL, V66, P9, DOI 10.1016/j.molcel.2017.02.021
   Panda AC, 2018, BIO-PROTOCOL, V8, DOI 10.21769/BioProtoc.2775
   Peng JJ, 2011, CANCER-AM CANCER SOC, V117, P1415, DOI 10.1002/cncr.25620
   Peng L, 2015, ONCOL REP, V33, P2669, DOI 10.3892/or.2015.3904
   Piwecka M, 2017, SCIENCE, V357, DOI 10.1126/science.aam8526
   Qin ML, 2016, CANCER BIOMARK, V16, P161, DOI 10.3233/CBM-150552
   Qu SB, 2015, CANCER LETT, V365, P141, DOI 10.1016/j.canlet.2015.06.003
   Read DE, 2014, CELL BIOSCI, V4, DOI 10.1186/2045-3701-4-56
   Rodríguez-Trelles F, 2006, ANNU REV GENET, V40, P47, DOI 10.1146/annurev.genet.40.110405.090625
   Rybak-Wolf A, 2015, MOL CELL, V58, P870, DOI 10.1016/j.molcel.2015.03.027
   Salzman J, 2013, PLOS GENET, V9, DOI 10.1371/journal.pgen.1003777
   Salzman J, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0030733
   Shang XC, 2016, MEDICINE, V95, DOI 10.1097/MD.0000000000003811
   Shao YF, 2017, TUMOR BIOL, V39, DOI 10.1177/1010428317699125
   Shi L, 2017, CELL DEATH DIS, V8, DOI 10.1038/cddis.2017.556
   Sui WG, 2017, ONCOL REP, V37, P1804, DOI 10.3892/or.2017.5415
   Suzuki H, 2014, INT J MOL SCI, V15, P9331, DOI 10.3390/ijms15069331
   TABAK HF, 1988, NUCLEIC ACIDS RES, V16, P6597, DOI 10.1093/nar/16.14.6597
   Tay MLI, 2017, CURR BIOL, V27, P1062, DOI 10.1016/j.cub.2017.02.040
   Thompson SR, 2012, WIRES RNA, V3, P697, DOI 10.1002/wrna.1129
   Tian MQ, 2018, J CLIN LAB ANAL, V32, DOI 10.1002/jcla.22281
   Vausort M, 2016, J AM COLL CARDIOL, V68, P1247, DOI 10.1016/j.jacc.2016.06.040
   Wang K, 2017, CELL DEATH DIFFER, V24, P1111, DOI 10.1038/cdd.2017.61
   Wang K, 2016, EUR HEART J, V37, P2602, DOI 10.1093/eurheartj/ehv713
   Wang PL, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0090859
   Wang XN, 2015, INT J CLIN EXP PATHO, V8, P16020
   Wang Y, 2015, RNA, V21, P172, DOI 10.1261/rna.048272.114
   Wang YS, 2015, CELL PHYSIOL BIOCHEM, V35, P1546, DOI 10.1159/000373970
   Wang Y, 2013, DIABETES, V62, P887, DOI 10.2337/db12-0451
   Wang YM, 2017, MOL CANCER, V16, DOI 10.1186/s12943-017-0598-7
   Westholm JO, 2014, CELL REP, V9, P1966, DOI 10.1016/j.celrep.2014.10.062
   Wilusz JE, 2013, SCIENCE, V340, P440, DOI 10.1126/science.1238522
   Wu J, 2018, CANCER LETT, V430, P179, DOI 10.1016/j.canlet.2018.05.033
   Wu SM, 2017, GIGASCIENCE, V7, DOI 10.1093/gigascience/gix118
   Wu Y, 2017, CELL BIOL INT, V41, P1283, DOI 10.1002/cbin.10761
   Xia SY, 2017, BRIEF BIOINFORM, V18, P984, DOI 10.1093/bib/bbw081
   Xia W, 2016, SCI REP-UK, V6, DOI 10.1038/srep27062
   Xie HJ, 2016, ONCOTARGET, V7, P26680, DOI 10.18632/oncotarget.8589
   Xu HY, 2015, SCI REP-UK, V5, DOI 10.1038/srep12453
   Xu LL, 2017, J CANCER RES CLIN, V143, P17, DOI 10.1007/s00432-016-2256-7
   Xu XW, 2017, ONCOTARGET, V8, P91674, DOI 10.18632/oncotarget.21748
   Xu ZQ, 2018, J CELL BIOCHEM, V119, P3317, DOI 10.1002/jcb.26492
   Yang C, 2016, ONCOTARGET, V7, P13479, DOI 10.18632/oncotarget.7266
   Yang L, 2018, AUTOPHAGY, V14, P404, DOI 10.1080/15548627.2017.1414755
   Yang Q, 2017, CELL DEATH DIFFER, V24, P1609, DOI 10.1038/cdd.2017.86
   Yang Yibing, 2018, J Natl Cancer Inst, V110, DOI 10.1093/jnci/djx166
   Yang Y, 2017, CELL RES, V27, P626, DOI 10.1038/cr.2017.31
   Yao ZC, 2017, MOL ONCOL, V11, P422, DOI 10.1002/1878-0261.12045
   You XT, 2016, SCI REP-UK, V6, DOI 10.1038/srep38820
   You XT, 2015, NAT NEUROSCI, V18, P603, DOI 10.1038/nn.3975
   Zhang XO, 2016, GENOME RES, V26, P1277, DOI 10.1101/gr.202895.115
   Zhang XO, 2014, CELL, V159, P134, DOI 10.1016/j.cell.2014.09.001
   Zhang Y, 2017, AGING-US, V9, P1585, DOI 10.18632/aging.101254
   Zhang Y, 2013, MOL CELL, V51, P792, DOI 10.1016/j.molcel.2013.08.017
   Zhao YJ, 2009, CHINESE MED J-PEKING, V122, P1322, DOI 10.3760/cma.j.issn.0366-6999.2009.11.016
   Zhao YH, 2016, GENES-BASEL, V7, DOI 10.3390/genes7120116
   Zhao ZJ, 2017, RNA BIOL, V14, P514, DOI 10.1080/15476286.2015.1122162
   Zhao ZZ, 2017, ACTA DIABETOL, V54, P237, DOI 10.1007/s00592-016-0943-0
   Zheng LL, 2016, NUCLEIC ACIDS RES, V44, pD196, DOI 10.1093/nar/gkv1273
   Zhong ZY, 2016, SCI REP-UK, V6, DOI 10.1038/srep30919
   Zhou ZW, 2018, THERANOSTICS, V8, P575, DOI 10.7150/thno.21648
   Zhu XL, 2017, FEBS J, V284, P2170, DOI 10.1111/febs.14132
   Zhuo C, 2015, CHINA J BIOINFORMA, P77
NR 138
TC 86
Z9 92
U1 3
U2 52
PU PEERJ INC
PI LONDON
PA 341-345 OLD ST, THIRD FLR, LONDON, EC1V 9LL, ENGLAND
SN 2167-8359
J9 PEERJ
JI PeerJ
PD AUG 24
PY 2018
VL 6
AR e5503
DI 10.7717/peerj.5503
PG 28
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA GS1RF
UT WOS:000443307900007
PM 30155370
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Roux, M
   Nizou, A
   Forestier, L
   Ouali, A
   Levéziel, H
   Amarger, V
AF Roux, M
   Nizou, A
   Forestier, L
   Ouali, A
   Levéziel, H
   Amarger, V
TI Characterization of the bovine PRKAG3 gene:: structure,
   polymorphism, and alternative transcripts
SO MAMMALIAN GENOME
LA English
DT Article
ID ACTIVATED PROTEIN-KINASE; SINGLE-NUCLEOTIDE POLYMORPHISMS; PIG
   SKELETAL-MUSCLE; HYPERTROPHIC CARDIOMYOPATHY; GLYCOGEN-CONTENT; ENERGY;
   MUTATIONS; IDENTIFICATION; SUBUNIT; DNA
AB The bovine PRKAG3 gene encodes the AMPK gamma 3 subunit, one isoform of the regulatory c subunit of the AMP-activated protein kinase ( AMPK). The AMPK plays a major role in the regulation of energy metabolism and mutations affecting the genes encoding the gamma subunits have been shown to influence AMPK activity. The gamma 3 subunit is involved in the regulation of AMPK activity in skeletal muscle and strongly inflences glycogen metabolism. Glycogen content in muscle is correlated to meat quality in livestock because it influences postmortem maturation process and ultimate pH. Naturally occurring mutations in the porcine PRKAG3 gene highly affect meat quality by influencing glycogen content before slaughter. We present the characterization of the bovine PRKAG3 gene and a polymorphism analysis in three cattle breeds. Thirty-two SNPs were identified among which 13 are in the coding region, one is in the 3' UTR, and 18 are in the introns. Five of them change an amino acid in the PRKAG3 protein sequence. Allelic frequencies were determined in the three breeds considered, and mutant alleles affecting the coding sequence are found at a very low frequency. Alternative splicing sites were identified at two positions of the gene, introducing heterogeneity in the population of proteins translated from the gene.
C1 Univ Limoges, Fac Sci & Tech, Unite Genet Mol Anim, UMR 1061,INRA, F-87060 Limoges, France.
   INRA, Qual Prod Anim, F-63122 St Genes Champanelle, France.
C3 Universite de Limoges; INRAE; INRAE
RP Univ Limoges, Fac Sci & Tech, Unite Genet Mol Anim, UMR 1061,INRA, 123 Av Albert Thomas, F-87060 Limoges, France.
EM valerie.amarger@unilim.fr
OI Amarger, Valerie/0000-0001-9258-6675
CR Amarger V, 2003, CYTOGENET GENOME RES, V102, P163, DOI 10.1159/000075743
   Andersson L, 2004, NAT REV GENET, V5, P202, DOI 10.1038/nrg1294
   Andersson L, 2003, BIOCHEM SOC T, V31, P232, DOI 10.1042/BST0310232
   Arad M, 2002, J CLIN INVEST, V109, P357, DOI 10.1172/JCI14571
   Barnes BR, 2004, J BIOL CHEM, V279, P38441, DOI 10.1074/jbc.M405533200
   Blair E, 2001, HUM MOL GENET, V10, P1215, DOI 10.1093/hmg/10.11.1215
   Cargill M, 1999, NAT GENET, V22, P231, DOI 10.1038/10290
   Carling D, 2004, TRENDS BIOCHEM SCI, V29, P18, DOI 10.1016/j.tibs.2003.11.005
   Cheung PCF, 2000, BIOCHEM J, V346, P659, DOI 10.1042/0264-6021:3460659
   Ciobanu D, 2001, GENETICS, V159, P1151
   Du M, 2005, J AGR FOOD CHEM, V53, P3235, DOI 10.1021/jf047913n
   Eggen A, 2001, GENET SEL EVOL, V33, P543, DOI 10.1051/gse:2001132
   Ferré P, 2003, BIOCHEM SOC T, V31, P220, DOI 10.1042/bst0310220
   Gollob MH, 2001, NEW ENGL J MED, V344, P1823, DOI 10.1056/NEJM200106143442403
   Halushka MK, 1999, NAT GENET, V22, P239, DOI 10.1038/10297
   Hardie DG, 2003, FEBS LETT, V546, P113, DOI 10.1016/S0014-5793(03)00560-X
   Heaton MP, 2001, MAMM GENOME, V12, P32, DOI 10.1007/s003350010223
   Immonen K, 2000, MEAT SCI, V55, P25, DOI 10.1016/S0309-1740(99)00121-7
   Kemp BE, 1999, TRENDS BIOCHEM SCI, V24, P22, DOI 10.1016/S0968-0004(98)01340-1
   Konfortov BA, 1999, MAMM GENOME, V10, P1142, DOI 10.1007/s003359901180
   Lareau LF, 2004, CURR OPIN STRUC BIOL, V14, P273, DOI 10.1016/j.sbi.2004.05.002
   MARIN A, 1989, NUCLEIC ACIDS RES, V17, P6181
   McKay SD, 2003, MAMM GENOME, V14, P853, DOI 10.1007/s00335-003-2276-x
   Milan D, 2000, SCIENCE, V288, P1248, DOI 10.1126/science.288.5469.1248
   Nelson MR, 2004, GENOME RES, V14, P1664, DOI 10.1101/gr.2421604
   Pickering J, 2002, NUCLEIC ACIDS RES, V30, DOI 10.1093/nar/gnf060
   PORTER TD, 1995, BBA-GENE STRUCT EXPR, V1261, P394, DOI 10.1016/0167-4781(95)00037-H
   Rouzaud F, 2000, GENET SEL EVOL, V32, P511, DOI 10.1051/gse:2000102
   Scott JW, 2004, J CLIN INVEST, V113, P274, DOI 10.1172/JCI200419874
   Stapleton D, 1996, J BIOL CHEM, V271, P611, DOI 10.1074/jbc.271.2.611
   Stephens JC, 2001, SCIENCE, V293, P489, DOI 10.1126/science.1059431
   Thornton C, 1998, J BIOL CHEM, V273, P12443, DOI 10.1074/jbc.273.20.12443
NR 32
TC 17
Z9 27
U1 0
U2 5
PU SPRINGER
PI NEW YORK
PA 233 SPRING ST, NEW YORK, NY 10013 USA
SN 0938-8990
EI 1432-1777
J9 MAMM GENOME
JI Mamm. Genome
PD JAN
PY 2006
VL 17
IS 1
BP 83
EP 92
DI 10.1007/s00335-005-0093-0
PG 10
WC Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology;
   Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology;
   Genetics & Heredity
GA 005MD
UT WOS:000234825800010
PM 16416094
DA 2025-04-10
ER

PT J
AU Chen, HJ
   Kronengold, J
   Yan, YY
   Gazula, VR
   Brown, MR
   Ma, LQ
   Ferreira, G
   Yang, YS
   Bhattacharjee, A
   Sigworth, FJ
   Salkoff, L
   Kaczmarek, LK
AF Chen, Haijun
   Kronengold, Jack
   Yan, Yangyang
   Gazula, Valeswara-Rao
   Brown, Maile R.
   Ma, Liqun
   Ferreira, Gonzalo
   Yang, Youshan
   Bhattacharjee, Arin
   Sigworth, Fred J.
   Salkoff, Larry
   Kaczmarek, Leonard K.
TI The N-Terminal Domain of Slack Determines the Formation and Trafficking
   of Slick/Slack Heteromeric Sodium-Activated Potassium Channels
SO JOURNAL OF NEUROSCIENCE
LA English
DT Article
ID K+ CHANNELS; VENTRICULAR MYOCYTES; NA+; NEURONS; RAT; CONDUCTANCE;
   SUBUNIT; SLICK; ATP; STOICHIOMETRY
AB Potassium channels activated by intracellular Na+ ions (K-Na) play several distinct roles in regulating the firing patterns of neurons, and, at the single channel level, their properties are quite diverse. Two known genes, Slick and Slack, encode K-Na channels. We have now found that Slick and Slack subunits coassemble to form heteromeric channels that differ from the homomers in their unitary conductance, kinetic behavior, subcellular localization, and response to activation of protein kinase C. Heteromer formation requires the N-terminal domain of Slack-B, one of the alternative splice variants of the Slack channel. This cytoplasmic N-terminal domain of Slack-B also facilitates the localization of heteromeric K-Na channels to the plasma membrane. Immunocytochemical studies indicate that Slick and Slack-B subunits are coexpressed in many central neurons. Our findings provide a molecular explanation for some of the diversity in reported properties of neuronal K-Na channels.
C1 [Chen, Haijun; Kronengold, Jack; Gazula, Valeswara-Rao; Brown, Maile R.; Kaczmarek, Leonard K.] Yale Univ, Sch Med, Dept Pharmacol, New Haven, CT 06510 USA.
   [Chen, Haijun; Ma, Liqun] SUNY Albany, Dept Biol Sci, Albany, NY 12222 USA.
   [Yan, Yangyang; Yang, Youshan; Sigworth, Fred J.; Kaczmarek, Leonard K.] Yale Univ, Sch Med, Dept Cellular & Mol Physiol, New Haven, CT 06510 USA.
   [Ferreira, Gonzalo] Univ Republica, Sch Med, Dept Biophys, Montevideo 11800, Uruguay.
   [Bhattacharjee, Arin] SUNY Buffalo, Dept Pharmacol & Toxicol, Buffalo, NY 14214 USA.
   [Salkoff, Larry] Washington Univ, Sch Med, Dept Anat & Neurobiol, St Louis, MO 63110 USA.
C3 Yale University; State University of New York (SUNY) System; University
   at Albany, SUNY; Yale University; Universidad de la Republica, Uruguay;
   State University of New York (SUNY) System; University at Buffalo, SUNY;
   Washington University (WUSTL)
RP Kaczmarek, LK (corresponding author), Yale Univ, Sch Med, Dept Pharmacol, New Haven, CT 06510 USA.
EM leonard.kaczmarek@yale.edu
RI Ferreira, Gonzalo/AAF-5749-2019; Chen, Haijun/C-7334-2011; Ma,
   Liqun/IXW-8762-2023
OI Ferreira, Gonzalo/0000-0002-4518-8698
FU American Heart Association (AHA) Scientist Development [0635125N];
   National Institutes of Health (NIH) [DC01919, GM067154-01A1, GM067154,
   U24NS05060]; American Heart Association (AHA) [0635125N] Funding Source:
   American Heart Association (AHA)
FX This work was supported by American Heart Association (AHA) Scientist
   Development Grant 0635125N (H. C.) and AHA and National Institutes of
   Health (NIH) Grants DC01919 (L. K. K.) and GM067154-01A1 and GM067154
   (F.J.S., L. S.). We thank Drs. Hongmei Li and Elizabeth A. Jonas for
   technical advice. We thank Drs. Steve Goldstein and Dan Levy (University
   of Chicago, Chicago, IL) for pMAX vectors and valuable discussions. We
   thank Gonzalo Budelli and Alice Butler for their kind help. The mouse
   monoclonal anti-Slack antibody was developed by and obtained from the
   University of California Davis/National Institute of Neurological
   Disorders and Stroke/National Institute of Mental Health NeuroMab
   Facility, supported by NIH Grant U24NS05060.
CR BADER CR, 1985, NATURE, V317, P540, DOI 10.1038/317540a0
   Bähring R, 2001, J BIOL CHEM, V276, P23888, DOI 10.1074/jbc.M101320200
   Bhattacharjee A, 2005, TRENDS NEUROSCI, V28, P422, DOI 10.1016/j.tins.2005.06.003
   Bhattacharjee A, 2003, J NEUROSCI, V23, P11681
   Bhattacharjee A, 2002, J COMP NEUROL, V454, P241, DOI 10.1002/cne.10439
   Bischoff U, 1998, J PHYSIOL-LONDON, V510, P743, DOI 10.1111/j.1469-7793.1998.743bj.x
   Brattacharjee A, 2005, J COMP NEUROL, V484, P80, DOI 10.1002/cne.20462
   Brelidze TI, 2003, P NATL ACAD SCI USA, V100, P9017, DOI 10.1073/pnas.1532257100
   Brown MR, 2008, J PHYSIOL-LONDON, V586, P5161, DOI 10.1113/jphysiol.2008.160861
   Callsen B, 2005, J PHYSIOL-LONDON, V568, P397, DOI 10.1113/jphysiol.2005.094359
   Cooper EC, 2003, ARCH NEUROL-CHICAGO, V60, P496, DOI 10.1001/archneur.60.4.496
   DRYER SE, 1989, J PHYSIOL-LONDON, V410, P283, DOI 10.1113/jphysiol.1989.sp017533
   Dryer SE, 2003, NEURON, V37, P727, DOI 10.1016/S0896-6273(03)00119-3
   EGAN TM, 1992, BRAIN RES, V584, P319, DOI 10.1016/0006-8993(92)90913-T
   EGAN TM, 1992, J NEUROSCI, V12, P1964
   Gulbis JM, 2000, SCIENCE, V289, P123, DOI 10.1126/science.289.5476.123
   HAIMANN C, 1992, PFLUG ARCH EUR J PHY, V422, P287, DOI 10.1007/BF00376215
   Hess D, 2007, J NEUROPHYSIOL, V97, P3484, DOI 10.1152/jn.00742.2006
   Hofherr A, 2005, J CELL SCI, V118, P1935, DOI 10.1242/jcs.02322
   Joiner WJ, 1998, NAT NEUROSCI, V1, P462, DOI 10.1038/2176
   KAMEYAMA M, 1984, NATURE, V309, P354, DOI 10.1038/309354a0
   Kim YC, 2007, J KOREAN MED SCI, V22, P57, DOI 10.3346/jkms.2007.22.1.57
   KOH DS, 1994, J PHYSIOL-LONDON, V479, P183, DOI 10.1113/jphysiol.1994.sp020287
   Mao JZ, 2004, P NATL ACAD SCI USA, V101, P1087, DOI 10.1073/pnas.0304827101
   Nimigean CM, 2003, BIOCHEMISTRY-US, V42, P9263, DOI 10.1021/bi0348720
   Niu XW, 2000, J PHYSIOL-LONDON, V526, P81, DOI 10.1111/j.1469-7793.2000.00081.x
   Paulais M, 2006, J GEN PHYSIOL, V127, P205, DOI 10.1085/jgp.200509360
   Pessia M, 1996, EMBO J, V15, P2980, DOI 10.1002/j.1460-2075.1996.tb00661.x
   Phartiyal P, 2008, J BIOL CHEM, V283, P3702, DOI 10.1074/jbc.M708999200
   Rajan S, 2005, CELL, V121, P37, DOI 10.1016/j.cell.2005.01.019
   RODRIGO GC, 1990, EXP PHYSIOL, V75, P839, DOI 10.1113/expphysiol.1990.sp003465
   Safronov BV, 1996, J PHYSIOL-LONDON, V497, P727, DOI 10.1113/jphysiol.1996.sp021803
   Santi CM, 2006, J NEUROSCI, V26, P5059, DOI 10.1523/JNEUROSCI.3372-05.2006
   Schwake M, 2000, J BIOL CHEM, V275, P13343, DOI 10.1074/jbc.275.18.13343
   Tucker SJ, 1997, NATURE, V387, P179, DOI 10.1038/387179a0
   Wang HS, 1998, SCIENCE, V282, P1890, DOI 10.1126/science.282.5395.1890
   Wang LT, 2007, J HIGH ENERGY PHYS, DOI 10.1088/1126-6708/2007/04/032
   WANG Z, 1991, J PHYSIOL-LONDON, V433, P241, DOI 10.1113/jphysiol.1991.sp018424
   Yang B, 2007, J NEUROSCI, V27, P2617, DOI 10.1523/JNEUROSCI.5308-06.2007
   Yuan A, 2003, NEURON, V37, P765, DOI 10.1016/S0896-6273(03)00096-5
   Zerangue N, 1999, NEURON, V22, P537, DOI 10.1016/S0896-6273(00)80708-4
   Zerangue N, 2000, P NATL ACAD SCI USA, V97, P3591, DOI 10.1073/pnas.060016797
   Zhang Y, 2007, AM J PHYSIOL-GASTR L, V292, pG1600, DOI 10.1152/ajpgi.00561.2005
   Zheng J, 1998, J GEN PHYSIOL, V112, P457, DOI 10.1085/jgp.112.4.457
   Zhou MO, 2004, CELL PHYSIOL BIOCHEM, V14, P225, DOI 10.1159/000080331
NR 45
TC 63
Z9 79
U1 1
U2 5
PU SOC NEUROSCIENCE
PI WASHINGTON
PA 11 DUPONT CIRCLE, NW, STE 500, WASHINGTON, DC 20036 USA
SN 0270-6474
J9 J NEUROSCI
JI J. Neurosci.
PD APR 29
PY 2009
VL 29
IS 17
BP 5654
EP 5665
DI 10.1523/JNEUROSCI.5978-08.2009
PG 12
WC Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA 439QL
UT WOS:000265642000029
PM 19403831
OA hybrid, Green Published, Green Accepted
DA 2025-04-10
ER

PT J
AU Ciomborowska-Basheer, J
   Staszak, K
   Kubiak, MR
   Makalowska, I
AF Ciomborowska-Basheer, Joanna
   Staszak, Klaudia
   Kubiak, Magdalena Regina
   Makalowska, Izabela
TI Not So Dead Genes-Retrocopies as Regulators of Their Disease-Related
   Progenitors and Hosts
SO CELLS
LA English
DT Review
DE retrocopies; retroposition; lncRNA; disease; parental gene; host gene;
   regulation
ID LONG-NONCODING-RNA; COMPETING ENDOGENOUS RNA; HEPATOCELLULAR-CARCINOMA;
   PARKINSONS-DISEASE; BREAST-CANCER; UP-REGULATION; NEURODEGENERATIVE
   DISEASES; MITOCHONDRIAL DYSFUNCTION; INTELLECTUAL DISABILITY; POTENTIAL
   MECHANISMS
AB Retroposition is RNA-based gene duplication leading to the creation of single exon nonfunctional copies. Nevertheless, over time, many of these duplicates acquire transcriptional capabilities. In human in most cases, these so-called retrogenes do not code for proteins but function as regulatory long noncoding RNAs (lncRNAs). The mechanisms by which they can regulate other genes include microRNA sponging, modulation of alternative splicing, epigenetic regulation and competition for stabilizing factors, among others. Here, we summarize recent findings related to lncRNAs originating from retrocopies that are involved in human diseases such as cancer and neurodegenerative, mental or cardiovascular disorders. Special attention is given to retrocopies that regulate their progenitors or host genes. Presented evidence from the literature and our bioinformatics analyses demonstrates that these retrocopies, often described as unimportant pseudogenes, are significant players in the cell's molecular machinery.
C1 [Ciomborowska-Basheer, Joanna; Staszak, Klaudia; Kubiak, Magdalena Regina; Makalowska, Izabela] Adam Mickiewicz Univ, Fac Biol, Inst Human Biol & Evolut, PL-61614 Poznan, Poland.
C3 Adam Mickiewicz University
RP Makalowska, I (corresponding author), Adam Mickiewicz Univ, Fac Biol, Inst Human Biol & Evolut, PL-61614 Poznan, Poland.
EM joannac@amu.edu.pl; klaudia.staszak@amu.edu.pl;
   magdalena.kubiak@amu.edu.pl; izabel@amu.edu.pl
RI Kubiak, Magdalena/AAW-2797-2020; Makalowska, Izabela/AAU-2682-2021
OI Ciomborowska-Basheer, Joanna/0000-0003-1166-3777; Kubiak,
   Magdalena/0000-0002-7253-228X; Staszak, Klaudia/0000-0002-7027-4790;
   Makalowska, Izabela/0000-0002-8144-5671
FU National Science Centre of Poland [2017/27/N/NZ2/00174]
FX This work was supported by the National Science Centre of Poland grant
   number 2017/27/N/NZ2/00174 to M.R.K.
CR Abegglen LM, 2015, JAMA-J AM MED ASSOC, V314, P1850, DOI 10.1001/jama.2015.13134
   Al-Saif A, 2012, ANN NEUROL, V72, P510, DOI 10.1002/ana.23641
   Amberger JS, 2019, NUCLEIC ACIDS RES, V47, pD1038, DOI 10.1093/nar/gky1151
   Andreozzi M, 2016, NEOPLASIA, V18, P724, DOI 10.1016/j.neo.2016.10.002
   Angelopoulou E, 2020, J MOL MED, V98, P325, DOI 10.1007/s00109-020-01885-z
   Bai MZ, 2015, ONCOL REP, V33, P1745, DOI 10.3892/or.2015.3763
   Bai YS, 2007, GENOME BIOL, V8, DOI 10.1186/gb-2007-8-1-r11
   Bai YS, 2008, BMC GENOMICS, V9, DOI 10.1186/1471-2164-9-241
   Bergman O, 2020, MOL PSYCHIATR, V25, P805, DOI 10.1038/s41380-018-0309-9
   Betrán E, 2002, GENOME RES, V12, P1854, DOI 10.1101/gr.6049
   Betrán E, 2002, MOL BIOL EVOL, V19, P654, DOI 10.1093/oxfordjournals.molbev.a004124
   Bier A, 2009, MOL CANCER THER, V8, P786, DOI 10.1158/1535-7163.MCT-08-0930
   Brosius J, 1999, GENE, V238, P115, DOI 10.1016/S0378-1119(99)00227-9
   Bryzghalov O, 2016, ACTA BIOCHIM POL, V63, P825, DOI 10.18388/abp.2016_1354
   Cao SW, 2017, ONCOTARGET, V8, P65370, DOI 10.18632/oncotarget.18524
   Carelli FN, 2016, GENOME RES, V26, P301, DOI 10.1101/gr.198473.115
   Casola C, 2017, GENOME BIOL EVOL, V9, P1351, DOI 10.1093/gbe/evx081
   Chen BH, 2018, CANCER CELL INT, V18, DOI 10.1186/s12935-018-0652-6
   Chen XJ, 2016, ONCOTARGET, V7, P55518, DOI 10.18632/oncotarget.10833
   Chiefari E, 2010, NAT COMMUN, V1, DOI 10.1038/ncomms1040
   Ciomborowska J, 2013, MOL BIOL EVOL, V30, P384, DOI 10.1093/molbev/mss235
   Costa Valerio, 2012, Frontiers in Genetics, V3, P231, DOI 10.3389/fgene.2012.00231
   Csobonyeiova M, 2020, INT J MOL SCI, V21, DOI 10.3390/ijms21062239
   Devor EJ, 2006, J HERED, V97, P186, DOI 10.1093/jhered/esj022
   DeWitt JJ, 2016, GENES-BASEL, V7, DOI 10.3390/genes7100076
   Driver JA, 2012, BRIT MED J, V344, DOI 10.1136/bmj.e1442
   Erkkinen MG, 2018, CSH PERSPECT BIOL, V10, DOI 10.1101/cshperspect.a033118
   Esnault C, 2000, NAT GENET, V24, P363, DOI 10.1038/74184
   Esposito F, 2014, ONCOTARGET, V5, P8341, DOI 10.18632/oncotarget.2202
   Fang P, 2012, MOL NEUROBIOL, V45, P499, DOI 10.1007/s12035-012-8264-y
   Fisher RA, 1935, AM NAT, V69, P446, DOI 10.1086/280618
   Force A, 1999, GENETICS, V151, P1531
   Gao XL, 2020, J BIOL CHEM, V295, P468, DOI 10.1074/jbc.RA119.010616
   Glenfield C, 2018, MOL BIOL EVOL, V35, P2886, DOI 10.1093/molbev/msy183
   Griffiths-Jones S, 2006, NUCLEIC ACIDS RES, V34, pD140, DOI 10.1093/nar/gkj112
   Grzeskowiak CL, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-04572-3
   Haldane JBS, 1933, AM NAT, V67, P5, DOI 10.1086/280465
   Hawkins PG, 2010, TRANSCR-AUSTIN, V1, P165, DOI 10.4161/trns.1.3.13332
   Howe KL, 2021, NUCLEIC ACIDS RES, V49, pD884, DOI 10.1093/nar/gkaa942
   Hu S, 2019, ONCOTARGETS THER, V12, P147, DOI 10.2147/OTT.S182537
   Javitt DC, 2004, MOL PSYCHIATR, V9, P984, DOI 10.1038/sj.mp.4001551
   Jeganathan J, 2017, ANN THORAC SURG, V104, P1547, DOI 10.1016/j.athoracsur.2017.04.060
   Jin LF, 2017, CELL PHYSIOL BIOCHEM, V41, P987, DOI 10.1159/000460836
   Johnsson P, 2013, NAT STRUCT MOL BIOL, V20, P440, DOI 10.1038/nsmb.2516
   Kadakkuzha BM, 2015, FRONT CELL NEUROSCI, V9, DOI 10.3389/fncel.2015.00063
   Kaer K, 2011, PLOS ONE, V6, DOI 10.1371/journal.pone.0026099
   Keeney PM, 2006, J NEUROSCI, V26, P5256, DOI 10.1523/JNEUROSCI.0984-06.2006
   Kerin T, 2012, SCI TRANSL MED, V4, DOI 10.1126/scitranslmed.3003479
   Kim P, 2019, NUCLEIC ACIDS RES, V47, pD994, DOI 10.1093/nar/gky1067
   Kinsella RJ, 2011, DATABASE-OXFORD, DOI 10.1093/database/bar030
   Kong Y, 2017, CANCER LETT, V407, P76, DOI 10.1016/j.canlet.2017.07.031
   Konradi C, 2017, SCHIZOPHR RES, V187, P1, DOI 10.1016/j.schres.2017.07.007
   Krasnov AN, 2005, NUCLEIC ACIDS RES, V33, P6654, DOI 10.1093/nar/gki969
   Kubiak MR, 2020, GENES-BASEL, V11, DOI 10.3390/genes11050542
   Kubiak MR, 2017, VIRUSES-BASEL, V9, DOI 10.3390/v9040080
   Lai YX, 2019, CLIN SCI, V133, P1439, DOI 10.1042/CS20190156
   Lathia J, 2020, ONCOLOGIST, V25, P123, DOI 10.1634/theoncologist.2019-0517
   Lelieveld SH, 2016, NAT NEUROSCI, V19, P1194, DOI 10.1038/nn.4352
   Li W, 2020, ONCOTARGETS THER, V13, P323, DOI 10.2147/OTT.S226770
   Liu FQ, 2018, BMC CANCER, V18, DOI 10.1186/s12885-018-4804-9
   Liu GY, 2015, LANCET NEUROL, V14, P679, DOI 10.1016/S1474-4422(15)00131-3
   Liu YS, 2018, PATHOL ONCOL RES, V24, P223, DOI 10.1007/s12253-017-0224-4
   LONG MY, 1993, SCIENCE, V260, P91, DOI 10.1126/science.7682012
   López L, 2018, J MOL NEUROSCI, V66, P462, DOI 10.1007/s12031-018-1195-y
   Lou WY, 2020, FRONT CELL DEV BIOL, V8, DOI 10.3389/fcell.2020.00085
   Lou WY, 2019, MOL THER-ONCOLYTICS, V14, P15, DOI 10.1016/j.omto.2019.03.006
   Luo T, 2020, AUTISM RES, V13, P2073, DOI 10.1002/aur.2413
   Lv H, 2018, HYPERTENSION, V71, P648, DOI 10.1161/HYPERTENSIONAHA.117.10084
   Marciniak P, 2018, MASTERS THESIS
   Matsumata M, 2012, STEM CELLS, V30, P1532, DOI 10.1002/stem.1124
   Mauri M., 2017, ACM INT C P SERIES, DOI [DOI 10.1145/3125571.3125585, 10.1145/3125571.3125585]
   MAYEDA A, 1994, EMBO J, V13, P5483, DOI 10.1002/j.1460-2075.1994.tb06883.x
   Mei DY, 2013, MED ONCOL, V30, DOI 10.1007/s12032-013-0709-2
   Meng H, 2017, NAT COMMUN, V8, DOI 10.1038/ncomms15500
   Mercer TR, 2008, P NATL ACAD SCI USA, V105, P716, DOI 10.1073/pnas.0706729105
   Mighell AJ, 2000, FEBS LETT, V468, P109, DOI 10.1016/S0014-5793(00)01199-6
   Miyoshi N, 2018, SURG TODAY, V48, P709, DOI 10.1007/s00595-018-1644-9
   Montaigne D, 2013, J AM COLL CARDIOL, V62, P1466, DOI 10.1016/j.jacc.2013.03.061
   NEI M, 1969, NATURE, V221, P40, DOI 10.1038/221040a0
   Nuerzhati Y, 2019, INT J MOL MED, V43, P739, DOI 10.3892/ijmm.2018.4023
   Nuzziello N, 2019, CELLS-BASEL, V8, DOI 10.3390/cells8101193
   O'Connor MD, 2011, EXP HEMATOL, V39, P866, DOI 10.1016/j.exphem.2011.05.008
   Ohno S., 1970, Evolution by gene duplication.
   Palumbo A Jr, 2019, GENES-BASEL, V10, DOI 10.3390/genes10050372
   Pan Y, 2014, J BIOMED RES, V28, P194, DOI 10.7555/JBR.28.20140052
   Parker HG, 2009, SCIENCE, V325, P995, DOI 10.1126/science.1173275
   Peng HR, 2015, ONCOTARGET, V6, P5666, DOI 10.18632/oncotarget.3290
   Pliarchopoulou K, 2013, CANCER CHEMOTH PHARM, V71, P245, DOI 10.1007/s00280-012-2002-z
   Poliseno L, 2010, NATURE, V465, P1033, DOI 10.1038/nature09144
   Pon JR, 2015, ANNU REV PATHOL-MECH, V10, P25, DOI 10.1146/annurev-pathol-012414-040312
   Qian YY, 2017, ONCOTARGET, V8, P107859, DOI 10.18632/oncotarget.22305
   Rappaport N, 2017, NUCLEIC ACIDS RES, V45, pD877, DOI 10.1093/nar/gkw1012
   Riva P, 2016, CURR ALZHEIMER RES, V13, P1219, DOI 10.2174/1567205013666160622112234
   Rosikiewicz W, 2017, DATABASE-OXFORD, DOI 10.1093/database/bax038
   Rowe VL, 2000, J VASC SURG, V31, P567
   Rutnam ZJ, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms3914
   Sarda S, 2018, TRANSCR-AUSTIN, V9, P171, DOI 10.1080/21541264.2017.1373209
   Scarola M, 2015, NAT COMMUN, V6, DOI 10.1038/ncomms8631
   Scola G, 2013, BIOL PSYCHIAT, V73, pE4, DOI 10.1016/j.biopsych.2012.06.028
   Seo J, 2020, CELL MOL LIFE SCI, V77, P2659, DOI 10.1007/s00018-019-03428-3
   Shashi V, 2015, CLIN GENET, V88, P386, DOI 10.1111/cge.12511
   Shearwin KE, 2005, TRENDS GENET, V21, P339, DOI 10.1016/j.tig.2005.04.009
   Shoshan-Barmatz V, 2018, PHARMACOL RES, V131, P87, DOI 10.1016/j.phrs.2018.03.010
   Stambolic V, 1998, CELL, V95, P29, DOI 10.1016/S0092-8674(00)81780-8
   Staszak K, 2021, LIFE-BASEL, V11, DOI 10.3390/life11010072
   Sulak M, 2016, ELIFE, V5, DOI [10.7554/eLife.11994, 10.7554/eLife.24307]
   Szczesniak MW, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0150353
   Tang J, 2017, CNS NEUROSCI THER, V23, P645, DOI 10.1111/cns.12710
   Tong J, 2018, PREGNANCY HYPERTENS, V13, P37, DOI 10.1016/j.preghy.2018.05.003
   Tsend-Ayush E, 2005, DEV DYNAM, V234, P682, DOI 10.1002/dvdy.20432
   Uwatoko H, 2019, MOL BRAIN, V12, DOI 10.1186/s13041-019-0471-2
   VANIN EF, 1985, ANNU REV GENET, V19, P253, DOI 10.1146/annurev.genet.19.1.253
   Vitiello M, 2020, J HEMATOL ONCOL, V13, DOI 10.1186/s13045-020-00894-2
   Wang CJ, 2018, CANCER SCI, V109, P84, DOI 10.1111/cas.13434
   Wang L, 2013, CARCINOGENESIS, V34, P1773, DOI 10.1093/carcin/bgt139
   Wang MY, 2019, CELL DEATH DIS, V10, DOI 10.1038/s41419-019-1666-2
   Wang QS, 2019, DIS MARKERS, V2019, DOI 10.1155/2019/9267046
   Wang RM, 2018, J CELL MOL MED, V22, P4068, DOI 10.1111/jcmm.13679
   Wang SL, 2019, ONCOL LETT, V18, P4583, DOI 10.3892/ol.2019.10806
   Wang YQ, 2014, CANCER LETT, V342, P130, DOI 10.1016/j.canlet.2013.08.044
   Waters AM, 2018, CSH PERSPECT MED, V8, DOI 10.1101/cshperspect.a031435
   Wu B, 2012, CELL PROLIFERAT, V45, P189, DOI 10.1111/j.1365-2184.2012.00820.x
   Wu N, 2020, HEART LUNG CIRC, V29, pE157, DOI 10.1016/j.hlc.2019.10.018
   Wu SS, 2020, J CELL MOL MED, V24, P3108, DOI 10.1111/jcmm.14977
   Xu H, 2019, ONCOL REP, V41, P3435, DOI 10.3892/or.2019.7128
   Xu TB, 2018, ONCOL LETT, V16, P4361, DOI 10.3892/ol.2018.9195
   Yamanaka S, 2008, CELL PROLIFERAT, V41, P51, DOI 10.1111/j.1365-2184.2008.00493.x
   Yan W, 2018, BIOCHEM BIOPH RES CO, V496, P1019, DOI 10.1016/j.bbrc.2017.12.149
   Yildirim Y, 2011, HUM MOL GENET, V20, P1886, DOI 10.1093/hmg/ddr070
   Yin L, 2020, AGING-US, V12, P8261, DOI 10.18632/aging.103137
   Zhang HH, 2014, SCI REP-UK, V4, DOI 10.1038/srep05416
   Zhou DM, 2021, MOL ONCOL, V15, P543, DOI 10.1002/1878-0261.12866
NR 132
TC 9
Z9 9
U1 0
U2 11
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
EI 2073-4409
J9 CELLS-BASEL
JI Cells
PD APR
PY 2021
VL 10
IS 4
AR 912
DI 10.3390/cells10040912
PG 20
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA RR1IQ
UT WOS:000642860900001
PM 33921034
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Liang, HF
   Li, J
   Li, XD
AF Liang, H. -F.
   Li, J.
   Li, X. -D.
TI Identification and characterization of troponin genes in Locusta
   migratoria
SO INSECT MOLECULAR BIOLOGY
LA English
DT Article
DE calcium; Locusta migratoria; muscle contraction; striated muscle;
   troponin
ID CARDIAC TROPONIN; FLIGHT MUSCLES; ALTERNATIVE EXON; C ISOFORMS;
   CONTRACTION; METABOLISM; ACTIVATION; EXCHANGE; ROLES
AB Troponin complex comprises three subunits, namely troponin C (TpnC), troponin I (TpnI) and troponin T (TpnT), and regulates the contraction of striated muscle. We found that the locust Locusta migratoria genome has one TpnT gene (LmTpnT), one TpnI gene (LmTpnI) and three TpnC genes (LmTpnC1, LmTpnC2 and LmTpnC3). Through alternative splicing, LmTpnT and LmTpnI potentially encode two and eight isoforms, respectively. The flight muscle and the jump muscle of L. migratoria express an identical LmTpnT isoform, but different LmTpnC isoforms and LmTpnI isoforms. LmTpnC2 and LmTpnC3 both contain highly conserved residues essential for calcium binding in the EF-hand II and IV, thus belonging two-site isoform. LmTpnC1 contains non-conserved substitutions in the EF-hand II and all highly conserved residues for calcium binding in the EF-hand IV. Mutagenesis and tyrosine fluorescence spectroscopic analysis show that both the EF-hand II and IV of LmTpnC1 can serve as calcium-binding site. Therefore, all three LmTpnC isoforms belong to two-site isoform. This is in contrast to the situation in the insect with asynchronous flight muscle, which expresses both one-site isoform and two-site isoform of TpnC. Those results suggest that the origination of insect asynchronous flight muscle is associated with the emergence of one-site isoform of TpnC.
C1 [Liang, H. -F.; Li, J.; Li, X. -D.] Chinese Acad Sci, State Key Lab Integrated Management Insect Pests, Inst Zool, Beijing 100101, Peoples R China.
   [Liang, H. -F.; Li, X. -D.] Univ Chinese Acad Sci, Beijing, Peoples R China.
C3 Chinese Academy of Sciences; Institute of Zoology, CAS; Chinese Academy
   of Sciences; University of Chinese Academy of Sciences, CAS
RP Li, XD (corresponding author), Chinese Acad Sci, State Key Lab Integrated Management Insect Pests, Inst Zool, Beijing 100101, Peoples R China.
EM lixd@ioz.ac.cn
RI Li, XD/JZT-1147-2024; Liang, Huifang/IZQ-4814-2023
FU National Natural Science Foundation of China [31672359, 31970657,
   31702066]
FX This work was supported by the National Natural Science Foundation of
   China (31672359, 31970657 and 31702066).
CR Agianian B, 2004, EMBO J, V23, P772, DOI 10.1038/sj.emboj.7600097
   Ayali A, 1996, PHYSIOL ENTOMOL, V21, P1, DOI 10.1111/j.1365-3032.1996.tb00828.x
   Ayme-Southgate A, 2015, INSECT BIOCHEM MOLEC, V62, P174, DOI 10.1016/j.ibmb.2015.02.008
   BABU A, 1992, J BIOL CHEM, V267, P15469
   Baylor SM, 2012, J GEN PHYSIOL, V139, P261, DOI 10.1085/jgp.201210773
   BOETTIGER EG, 1960, ANNU REV ENTOMOL, V5, P1, DOI 10.1146/annurev.en.05.010160.000245
   Bullard B, 2011, J MUSCLE RES CELL M, V32, P303, DOI 10.1007/s10974-011-9278-1
   Cao TX, 2019, ARCH BIOCHEM BIOPHYS, V666, P40, DOI 10.1016/j.abb.2019.03.013
   Chao E, 2010, COMP BIOCHEM PHYS B, V157, P88, DOI 10.1016/j.cbpb.2010.05.007
   Chechenova MB, 2017, MOL BIOL CELL, V28, P760, DOI 10.1091/mbc.E16-07-0498
   Eldred CC, 2014, J MUSCLE RES CELL M, V35, P211, DOI 10.1007/s10974-014-9387-8
   FARAH CS, 1995, FASEB J, V9, P755, DOI 10.1096/fasebj.9.9.7601340
   GUSEV NB, 1984, BIOCHEM J, V220, P315, DOI 10.1042/bj2200315
   Herranz R, 2005, J MOL EVOL, V60, P31, DOI 10.1007/s00239-004-0031-x
   Katrukha IA, 2013, BIOCHEMISTRY-MOSCOW+, V78, P1447, DOI 10.1134/S0006297913130063
   Kirkton SD, 2005, J EXP BIOL, V208, P3003, DOI 10.1242/jeb.01747
   Krzic U, 2010, J MOL BIOL, V397, P110, DOI 10.1016/j.jmb.2010.01.039
   Li J, 2016, INSECT MOL BIOL, V25, P689, DOI 10.1111/imb.12254
   Marden JH, 2001, J EXP BIOL, V204, P3457
   Nongthomba U, 2007, GENETICS, V177, P295, DOI 10.1534/genetics.106.056812
   Pflüger HJ, 2011, PHYSIOLOGY, V26, P293, DOI 10.1152/physiol.00002.2011
   Pillmann H, 2011, BMC BIOINFORMATICS, V12, DOI 10.1186/1471-2105-12-270
   Piroddi N, 2003, J PHYSIOL-LONDON, V552, P917, DOI 10.1113/jphysiol.2003.051615
   Qiu F, 2003, BIOCHEM J, V371, P811, DOI 10.1042/BJ20021814
   Snelling EP, 2012, J EXP BIOL, V215, P3388, DOI 10.1242/jeb.072769
   Snelling EP, 2012, J EXP BIOL, V215, P3324, DOI 10.1242/jeb.072975
   Tanaka H, 2013, FEBS LETT, V587, P2612, DOI 10.1016/j.febslet.2013.06.042
   Tobacman LS, 1996, ANNU REV PHYSIOL, V58, P447, DOI 10.1146/annurev.ph.58.030196.002311
   Vibert P, 1997, J MOL BIOL, V266, P8, DOI 10.1006/jmbi.1996.0800
   WEST JM, 1992, J MUSCLE RES CELL M, V13, P668, DOI 10.1007/BF01738256
   Yang K, 2017, ELIFE, V6, DOI [10.7554/eLife.29100, 10.7554/elife.29100]
   ZOT AS, 1987, ANNU REV BIOPHYS BIO, V16, P535
NR 32
TC 5
Z9 5
U1 0
U2 35
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0962-1075
EI 1365-2583
J9 INSECT MOL BIOL
JI Insect Mol. Biol.
PD AUG
PY 2020
VL 29
IS 4
BP 391
EP 403
DI 10.1111/imb.12644
EA MAY 2020
PG 13
WC Biochemistry & Molecular Biology; Entomology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Entomology
GA MG6AF
UT WOS:000530516200001
PM 32338426
DA 2025-04-10
ER

PT J
AU Yu, GS
   Lu, YC
   Gulick, T
AF Yu, GS
   Lu, YC
   Gulick, T
TI Co-regulation of tissue-specific alternative human carnitine
   palmitoyltransferase Iβ gene promoters by fatty acid enzyme substrate
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID PROLIFERATOR-ACTIVATED RECEPTORS; TRANSCRIPTION FACTORS; MALONYL-COA;
   RETINOIC ACID; EXPRESSION; OXIDATION; HEART; RAT; MUSCLE; CARBOXYLASE
AB Carnitine palmitoyltransferase I (CPT-I) catalyzes the rate-determining step in mitochondrial fatty acid beta-oxidation. CPT-I has two structural genes (alpha and beta) that are differentially expressed among tissues. Our CPT-I beta isolates from a human cardiac cDNA library contained two different extreme 5'-sequences derived from short alternative first untranslated exons that utilize a common splice acceptor site in exon 2. Primer extension identified single dominant start sites for each transcript, and ribonuclease protection assays showed the presence of one 5'-exon in liver, muscle, and heart mRNAs, indicating that the cognate promoter U (upstream/ubiquitous) is active in each of these tissues. By contrast, mRNAs containing the alternative 5'-exon were present only in muscle and heart, indicating a muscle-specific promoter M (muscle). CPT-I beta mRNA levels increased markedly in tissues of fasted rats, when circulating free fatty acid concentrations are elevated. Using CPT-I beta promoter/reporter transient transfection of murine C2C12 myotubes and HepG2 hepatocyte, fatty acids were found to increase promoter activity in a peroxisome proliferator-activated receptor alpha (PPAR alpha)-dependent fashion. A promoter fatty acid response element (FARE) was mapped, mutation of which ablated fatty acid-mediated production of both transcripts. PPAR alpha/retinoid X receptor a formed specific complexes with oligonucleotides containing the FARE, and anti-PPAR alpha antibody shifted nuclear protein-DNA complexes, confirming the role of this factor in regulating the expression of this critical metabolic enzyme gene. The constitutive repressor chicken ovalbumin upstream promoter transcription factor competitively binds at the FARE and modulates fatty acid induction of the promoters.
C1 Massachusetts Gen Hosp, Diabet Res Lab, Diabet Unit, Charlestown, MA 02129 USA.
   Massachusetts Gen Hosp, Med Serv, Charlestown, MA 02129 USA.
   Harvard Univ, Sch Med, Dept Med, Boston, MA 02115 USA.
C3 Harvard University; Harvard University Medical Affiliates; Massachusetts
   General Hospital; Harvard University; Harvard University Medical
   Affiliates; Massachusetts General Hospital; Harvard University; Harvard
   Medical School
RP Gulick, T (corresponding author), Massachusetts Gen Hosp, Diabet Res Lab, Diabet Unit, MGH E,CNY 149 8218,149 13th St, Charlestown, MA 02129 USA.
EM gulick@helix.mgh.harvard.edu
FU NICHD NIH HHS [HD35685] Funding Source: Medline
CR AssimacopoulosJeannet F, 1997, J BIOL CHEM, V272, P1659, DOI 10.1074/jbc.272.3.1659
   Ausubel F.M., 1992, Current Protocols in Molecular Biology, V2, p13.1
   BOEHM MF, 1994, J MED CHEM, V37, P408, DOI 10.1021/jm00029a013
   Brandt JM, 1998, J BIOL CHEM, V273, P23786, DOI 10.1074/jbc.273.37.23786
   BROWN NF, 1995, J BIOL CHEM, V270, P8952, DOI 10.1074/jbc.270.15.8952
   CARTER ME, 1994, MOL CELL BIOL, V14, P4360, DOI 10.1128/MCB.14.7.4360
   CASTELEIN H, 1994, J BIOL CHEM, V269, P26754
   Chatelain F, 1996, EUR J BIOCHEM, V235, P789, DOI 10.1111/j.1432-1033.1996.00789.x
   FORMAN BM, 1995, CELL, V83, P803, DOI 10.1016/0092-8674(95)90193-0
   Fraser F, 1997, BIOCHEM J, V323, P711, DOI 10.1042/bj3230711
   Gamble J, 1997, METABOLISM, V46, P1270, DOI 10.1016/S0026-0495(97)90229-8
   Glass CK, 1997, CURR OPIN CELL BIOL, V9, P222, DOI 10.1016/S0955-0674(97)80066-X
   GOTTLICHER M, 1992, P NATL ACAD SCI USA, V89, P4653, DOI 10.1073/pnas.89.10.4653
   GRANTHAM BD, 1986, BIOCHEM J, V239, P485, DOI 10.1042/bj2390485
   GREEN MR, 1991, ANNU REV CELL BIOL, V7, P559, DOI 10.1146/annurev.cellbio.7.1.559
   GULICK T, 1994, P NATL ACAD SCI USA, V91, P11012, DOI 10.1073/pnas.91.23.11012
   Horwitz KB, 1996, MOL ENDOCRINOL, V10, P1167, DOI 10.1210/me.10.10.1167
   Kallen CB, 1996, P NATL ACAD SCI USA, V93, P5793, DOI 10.1073/pnas.93.12.5793
   KELLY DP, 1989, J BIOL CHEM, V264, P18921
   KLIEWER SA, 1994, P NATL ACAD SCI USA, V91, P7355, DOI 10.1073/pnas.91.15.7355
   Kliewer SA, 1997, P NATL ACAD SCI USA, V94, P4318, DOI 10.1073/pnas.94.9.4318
   KLIEWER SA, 1992, NATURE, V358, P771, DOI 10.1038/358771a0
   KUROKAWA R, 1995, NATURE, V377, P451, DOI 10.1038/377451a0
   LEHMANN JM, 1995, J BIOL CHEM, V270, P12953, DOI 10.1074/jbc.270.22.12953
   LOPASCHUK GD, 1994, J BIOL CHEM, V269, P25871
   MANGELSDORF DJ, 1995, CELL, V83, P841, DOI 10.1016/0092-8674(95)90200-7
   Mascaró C, 1998, J BIOL CHEM, V273, P8560, DOI 10.1074/jbc.273.15.8560
   MCGARRY JD, 1989, DIABETES METAB REV, V5, P271, DOI 10.1002/dmr.5610050305
   MCGARRY JD, 1978, J BIOL CHEM, V253, P4128
   McGarry JD, 1997, EUR J BIOCHEM, V244, P1, DOI 10.1111/j.1432-1033.1997.00001.x
   MCMILLIN JB, 1994, ARCH BIOCHEM BIOPHYS, V312, P375, DOI 10.1006/abbi.1994.1322
   MUSCAT GEO, 1995, NUCLEIC ACIDS RES, V23, P1311, DOI 10.1093/nar/23.8.1311
   Neville C, 1997, METHOD CELL BIOL, V52, P85, DOI 10.1016/S0091-679X(08)60375-1
   NOTHIAS JY, 1995, J BIOL CHEM, V270, P22077, DOI 10.1074/jbc.270.38.22077
   PALMER CNA, 1995, J BIOL CHEM, V270, P16114, DOI 10.1074/jbc.270.27.16114
   PRENTKI M, 1992, J BIOL CHEM, V267, P5802
   Prowse DM, 1997, J BIOL CHEM, V272, P1308, DOI 10.1074/jbc.272.2.1308
   RANDLE PJ, 1994, DIABETOLOGIA, V37, pS155, DOI 10.1007/BF00400839
   Sack MN, 1997, P NATL ACAD SCI USA, V94, P6438, DOI 10.1073/pnas.94.12.6438
   SADDIK M, 1993, J BIOL CHEM, V268, P25836
   SAGGERSON ED, 1981, FEBS LETT, V129, P229, DOI 10.1016/0014-5793(81)80171-8
   SAGGERSON ED, 1982, FEBS LETT, V150, P177
   THUMELIN S, 1994, BIOCHEM J, V300, P583, DOI 10.1042/bj3000583
   Treuter E, 1998, MOL ENDOCRINOL, V12, P864, DOI 10.1210/me.12.6.864
   Tsai SY, 1997, ENDOCR REV, V18, P229, DOI 10.1210/er.18.2.229
   vanderLeij FR, 1997, BBA-GENE STRUCT EXPR, V1352, P123, DOI 10.1016/S0167-4781(97)00037-7
   WILEY SR, 1992, P NATL ACAD SCI USA, V89, P5814, DOI 10.1073/pnas.89.13.5814
   Yamazaki N, 1997, FEBS LETT, V409, P401, DOI 10.1016/S0014-5793(97)00561-9
   YAMAZAKI N, 1995, FEBS LETT, V363, P41, DOI 10.1016/0014-5793(95)00277-G
   Yu GS, 1998, BIOCHEM J, V334, P225, DOI 10.1042/bj3340225
   Yu GS, 1998, BBA-LIPID LIPID MET, V1393, P166, DOI 10.1016/S0005-2760(98)00075-7
   YU K, 1995, J BIOL CHEM, V270, P23975, DOI 10.1074/jbc.270.41.23975
NR 52
TC 91
Z9 102
U1 0
U2 2
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA
SN 0021-9258
J9 J BIOL CHEM
JI J. Biol. Chem.
PD DEC 4
PY 1998
VL 273
IS 49
BP 32901
EP 32909
DI 10.1074/jbc.273.49.32901
PG 9
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 144RP
UT WOS:000077329100079
PM 9830040
OA hybrid
DA 2025-04-10
ER

PT J
AU Santama, N
   Li, KW
   Geraerts, WPM
   Benjamin, PR
   Burke, JF
AF Santama, N
   Li, KW
   Geraerts, WPM
   Benjamin, PR
   Burke, JF
TI Post-translational processing of the alternative neuropeptide precursor
   encoded by the FMRFamide gene in the pulmonate snail Lymnaea stagnalis
SO EUROPEAN JOURNAL OF NEUROSCIENCE
LA English
DT Article
DE invertebrate neuron; neuropeptide precursor; post-translational
   processing; mass spectrometry; tetrabasic cleavage motif
ID CENTRAL NERVOUS-SYSTEM; POND SNAIL; NEUROSECRETORY-CELLS; PEPTIDES;
   PROTEIN; HEART; MOTONEURONS; NEURONS; BRAIN
AB The neuropeptide gene encoding FMRFamide-like peptides in the pulmonate mollusc Lymnaea is subject to alternative splicing that generates cell-specific expression of distinct sets of peptides in the CNS. In this paper, we analyse the post-translational processing of the alternative protein precursor encoded by the exon I, III-V transcript (type 2 transcript). We raised anti-peptide antisera specific to distinct segments of the precursor in order to address the pattern of endoproteolytic cleavages, specifically around the tetrabasic site RRKR. We first showed that not all peptides predicted by the precursor structure are generated as final steady-state products. We then identified a novel peptide by biochemical purification, amino acid sequencing and mass spectrometry-the 35 amino acid SDPFFRFGKQQVATDDSGELDDEILSRVSDDDKNI, which we termed the acidic peptide, previously not predicted on the basis of the precursor structure, This novel peptide, abundant in the snail brain (0.7 pmol per central nervous system), includes the N-terminal sequence SDPFFRF, which was previously considered to be a variant of the known heptapeptide SDPFLRFamide, also encoded within the same protein precursor. We showed by in situ hybridization and immunocytochemistry that the acidic peptide is produced in all cells that transcribe type 2 FMRFamide mRNA. We mapped the expression of this novel peptide in the CNS and localized it mainly in three identifiable neuronal clusters-the E, F and B groups of cells-and some additional neurons, all situated in three of the eleven central ganglia. Immunoreactive neurons included the single identifiable visceral white interneuron (VWI or VD4), a key cell of the cardiorespiratory network.
C1 UNIV SUSSEX,SCH BIOL SCI,SUSSEX CTR NEUROSCI,BRIGHTON BN1 9QG,E SUSSEX,ENGLAND.
   FREE UNIV AMSTERDAM,FAC BIOL,NEUROSCI RES INST,GRAD SCH NEUROSCI AMSTERDAM,1081 HV AMSTERDAM,NETHERLANDS.
C3 University of Sussex; University of Amsterdam; Vrije Universiteit
   Amsterdam
RI Santama, Niovi/GLR-7648-2022
OI Santama, Niovi/0000-0002-8370-8674
CR BENJAMIN PR, 1994, BIOESSAYS, V16, P335, DOI 10.1002/bies.950160508
   BENJAMIN PR, 1984, J EXP BIOL, V113, P165
   BREZDEN BL, 1991, J PHYSIOL-LONDON, V443, P727, DOI 10.1113/jphysiol.1991.sp018860
   BRIGHT K, 1993, J NEUROSCI, V13, P2719, DOI 10.1523/JNEUROSCI.13-06-02719.1993
   BRUSSAARD AB, 1989, PEPTIDES, V10, P289, DOI 10.1016/0196-9781(89)90032-6
   BRUSSAARD AB, 1988, BRAIN RES, V447, P35, DOI 10.1016/0006-8993(88)90963-8
   BUCKETT KJ, 1990, J NEUROPHYSIOL, V63, P1413, DOI 10.1152/jn.1990.63.6.1413
   BUCKETT KJ, 1990, J NEUROPHYSIOL, V63, P1426, DOI 10.1152/jn.1990.63.6.1426
   BUCKETT KJ, 1990, J NEUROPHYSIOL, V63, P1436, DOI 10.1152/jn.1990.63.6.1436
   CHOU PY, 1978, ANNU REV BIOCHEM, V47, P251, DOI 10.1146/annurev.bi.47.070178.001343
   CROLL RP, 1989, J COMP NEUROL, V280, P122, DOI 10.1002/cne.902800109
   DEWITH ND, 1992, NEUROREPORT, V3, P612, DOI 10.1097/00001756-199207000-00017
   EBBERINK RHM, 1987, PEPTIDES, V8, P515, DOI 10.1016/0196-9781(87)90018-0
   ELLIOTT CJH, 1985, J NEUROPHYSIOL, V54, P1396, DOI 10.1152/jn.1985.54.6.1396
   FISHER JM, 1988, CELL, V54, P813, DOI 10.1016/S0092-8674(88)91131-2
   Greenberg M J, 1988, Peptides, V9 Suppl 1, P125, DOI 10.1016/0196-9781(88)90236-7
   GREENBERG MJ, 1992, PROG BRAIN RES, V92, P25, DOI 10.1016/S0079-6123(08)61162-0
   Harlow ED, 1988, ANTIBODIES LAB MANUA
   KELLETT E, 1994, J NEUROSCI, V14, P6564
   LI KW, 1988, ANAL BIOCHEM, V174, P97, DOI 10.1016/0003-2697(88)90523-4
   LINACRE A, 1990, J NEUROSCI, V10, P412
   PRICE DA, 1977, SCIENCE, V197, P670, DOI 10.1126/science.877582
   ROST B, 1994, PROTEINS, V19, P55, DOI 10.1002/prot.340190108
   ROST B, 1993, J MOL BIOL, V232, P584, DOI 10.1006/jmbi.1993.1413
   SANTAMA N, 1994, J COMP NEUROL, V342, P335, DOI 10.1002/cne.903420303
   SANTAMA N, 1993, EUR J NEUROSCI, V5, P1003, DOI 10.1111/j.1460-9568.1993.tb00952.x
   SANTAMA N, 1995, EUR J NEUROSCI, V7, P234, DOI 10.1111/j.1460-9568.1995.tb01059.x
   SANTAMA N, 1995, EUR J NEUROSCI, V7, P65, DOI 10.1111/j.1460-9568.1995.tb01021.x
   SAUNDERS SE, 1991, J NEUROSCI, V11, P740
   SAUNDERS SE, 1992, J NEUROSCI, V12, P1033
   SCHOT LPC, 1984, HISTOCHEMISTRY, V81, P373, DOI 10.1007/BF00514332
   SOSSIN WS, 1989, NEURON, V2, P1407, DOI 10.1016/0896-6273(89)90186-4
   SOSSIN WS, 1990, P NATL ACAD SCI USA, V87, P4845, DOI 10.1073/pnas.87.12.4845
   SYED NI, 1990, SCIENCE, V250, P282, DOI 10.1126/science.2218532
NR 34
TC 21
Z9 23
U1 0
U2 8
PU OXFORD UNIV PRESS UNITED KINGDOM
PI OXFORD
PA WALTON ST JOURNALS DEPT, OXFORD, ENGLAND OX2 6DP
SN 0953-816X
J9 EUR J NEUROSCI
JI Eur. J. Neurosci.
PD MAY
PY 1996
VL 8
IS 5
BP 968
EP 977
DI 10.1111/j.1460-9568.1996.tb01584.x
PG 10
WC Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA UM788
UT WOS:A1996UM78800013
PM 8743745
DA 2025-04-10
ER

PT J
AU Kargapolova, Y
   Levin, M
   Lackner, K
   Danckwardt, S
AF Kargapolova, Yulia
   Levin, Michal
   Lackner, Karl
   Danckwardt, Sven
TI sCLIP-an integrated platform to study RNA-protein interactomes in
   biomedical research: identification of CSTF2tau in alternative
   processing of small nuclear RNAs
SO NUCLEIC ACIDS RESEARCH
LA English
DT Article
ID PRE-MESSENGER-RNA; BINDING PROTEIN; SITES; END; DEGRADATION; POLY(A);
   SNRNA; CLIP; AMPLIFICATION; PRENYLATION
AB RNA-binding proteins (RBPs) are central for gene expression by controlling the RNA fate from birth to decay. Various disorders arising from perturbations of RNA-protein interactions document their critical function. However, deciphering their function is complex, limiting the general functional elucidation of this growing class of proteins and their contribution to (patho) physiology. Here, we present sCLIP, a simplified and robust platform for genome-wide interrogation of RNA-protein interactomes based on crosslinking-immunoprecipitation and high-throughput sequencing. sCLIP exploits linear amplification of the immunoprecipitated RNA improving the complexity of the sequencing-library despite significantly reducing the amount of input material and omitting several purification steps. Additionally, it permits a radiolabel-free visualization of immunoprecipitated RNA. In a proof of concept, we identify that CSTF2tau binds many previously not recognized RNAs including histone, snoRNA and snRNAs. CSTF2tau-binding is associated with internal oligoadenylation resulting in shortened snRNA isoforms subjected to rapid degradation. We provide evidence for a new mechanism whereby CSTF2tau controls the abundance of snRNAs resulting in alternative splicing of several RNAs including ANK2 with critical roles in tumorigenesis and cardiac function. Combined with a bioinformatic pipeline sCLIP thus uncovers new functions for established RBPs and fosters the illumination of RBP-protein interaction landscapes in health and disease.
C1 [Kargapolova, Yulia; Levin, Michal; Lackner, Karl; Danckwardt, Sven] Univ Med Ctr Mainz, Inst Clin Chem & Lab Med, Mainz, Germany.
   [Kargapolova, Yulia; Levin, Michal; Danckwardt, Sven] Univ Med Ctr Mainz, CTH, Mainz, Germany.
   [Lackner, Karl; Danckwardt, Sven] German Ctr Cardiovasc Res DZHK, Mainz, Germany.
C3 Johannes Gutenberg University of Mainz; Johannes Gutenberg University of
   Mainz; German Centre for Cardiovascular Research
RP Danckwardt, S (corresponding author), Univ Med Ctr Mainz, Inst Clin Chem & Lab Med, Mainz, Germany.; Danckwardt, S (corresponding author), Univ Med Ctr Mainz, CTH, Mainz, Germany.; Danckwardt, S (corresponding author), German Ctr Cardiovasc Res DZHK, Mainz, Germany.
EM Sven.Danckwardt@unimedizin-mainz.de
RI Danckwardt, Sven/JRX-3763-2023
OI Levin, Michal/0000-0003-3484-890X
FU DFG [DA 1189/2-1, GRK 1591]; Federal Ministry of Education and Research
   [BMBF 01EO1003]; Hella Buhler Prize for Cancer Research; DGKL; Institute
   of Clinical Chemistry, University Medical Center Mainz; Humboldt
   Research Fellowship; BMBF
FX DFG [DA 1189/2-1 to S.D., GRK 1591]; Federal Ministry of Education and
   Research [BMBF 01EO1003]; Hella Buhler Prize for Cancer Research; DGKL
   and the Institute of Clinical Chemistry, University Medical Center
   Mainz; Humboldt Research Fellowship (to M.L.). Funding for open access
   charge: DFG, BMBF.
CR Anders S, 2012, GENOME RES, V22, P2008, DOI 10.1101/gr.133744.111
   Andresen K, 2015, HEPATOLOGY, V61, P1651, DOI 10.1002/hep.27707
   Baltz AG, 2012, MOL CELL, V46, P674, DOI 10.1016/j.molcel.2012.05.021
   Battle DJ, 2006, COLD SPRING HARB SYM, V71, P313, DOI 10.1101/sqb.2006.71.001
   Baugh LR, 2001, NUCLEIC ACIDS RES, V29, DOI 10.1093/nar/29.5.e29
   Beckmann BM, 2015, NAT COMMUN, V6, DOI 10.1038/ncomms10127
   Berg TJ, 2010, J BIOL CHEM, V285, P35255, DOI 10.1074/jbc.M110.129916
   Blume LC, 2015, CELL SIGNAL, V27, P716, DOI 10.1016/j.cellsig.2014.11.006
   Bohnsack MT, 2009, MOL CELL, V36, P583, DOI 10.1016/j.molcel.2009.09.039
   Brooks AN, 2015, GENOME RES, V25, P1771, DOI 10.1101/gr.192518.115
   Castello A, 2015, TRENDS ENDOCRIN MET, V26, P746, DOI 10.1016/j.tem.2015.09.012
   Castello A, 2013, TRENDS GENET, V29, P318, DOI 10.1016/j.tig.2013.01.004
   Castello A, 2012, CELL, V149, P1393, DOI 10.1016/j.cell.2012.04.031
   Chari A, 2009, CURR OPIN CELL BIOL, V21, P387, DOI 10.1016/j.ceb.2009.02.004
   CHENG GH, 1989, P NATL ACAD SCI USA, V86, P7002, DOI 10.1073/pnas.86.18.7002
   Cunha SR, 2008, J MOL CELL CARDIOL, V45, P724, DOI 10.1016/j.yjmcc.2008.08.005
   Danckwardt S, 2011, MOL CELL, V41, P298, DOI 10.1016/j.molcel.2010.12.032
   Dass B, 2007, P NATL ACAD SCI USA, V104, P20374, DOI 10.1073/pnas.0707589104
   Eckmann CR, 2011, WIRES RNA, V2, P348, DOI 10.1002/wrna.56
   Flynn RA, 2015, RNA, V21, P135, DOI 10.1261/rna.047803.114
   Hafner M, 2010, CELL, V141, P129, DOI 10.1016/j.cell.2010.03.009
   Harnisch C, 2016, RNA, V22, P428, DOI 10.1261/rna.053942.115
   Hashimshony T, 2012, CELL REP, V2, P666, DOI 10.1016/j.celrep.2012.08.003
   He HL, 2011, SCIENCE, V332, P238, DOI 10.1126/science.1200587
   Hoeijmakers WAM, 2011, NAT PROTOC, V6, P1026, DOI 10.1038/nprot.2011.345
   Hu J, 2005, RNA, V11, P1485, DOI 10.1261/rna.2107305
   Huberts DHEW, 2010, BBA-MOL CELL RES, V1803, P520, DOI 10.1016/j.bbamcr.2010.01.022
   Huppertz I, 2014, METHODS, V65, P274, DOI 10.1016/j.ymeth.2013.10.011
   Ishikawa H, 2014, NUCLEIC ACIDS RES, V42, P2708, DOI 10.1093/nar/gkt1271
   Islam S, 2014, NAT METHODS, V11, P163, DOI [10.1038/NMETH.2772, 10.1038/nmeth.2772]
   Iwakawa R, 2015, CARCINOGENESIS, V36, P616, DOI 10.1093/carcin/bgv026
   Jänicke A, 2012, RNA, V18, P1289, DOI 10.1261/rna.031898.111
   Jenkins PM, 2015, P NATL ACAD SCI USA, V112, P957, DOI 10.1073/pnas.1416544112
   Jia YC, 2012, CELL, V148, P296, DOI 10.1016/j.cell.2011.11.057
   Keene JD, 2007, NAT REV GENET, V8, P533, DOI 10.1038/nrg2111
   Konig J, 2011, JOVE-J VIS EXP, DOI 10.3791/2638
   Kwon SC, 2013, NAT STRUCT MOL BIOL, V20, P1122, DOI 10.1038/nsmb.2638
   Lestrade L, 2006, NUCLEIC ACIDS RES, V34, pD158, DOI 10.1093/nar/gkj002
   Liao Y, 2016, CELL REP, V16, P1456, DOI 10.1016/j.celrep.2016.06.084
   Licatalosi DD, 2008, NATURE, V456, P464, DOI 10.1038/nature07488
   Lukong KE, 2008, TRENDS GENET, V24, P416, DOI 10.1016/j.tig.2008.05.004
   Martin G, 2012, CELL REP, V1, P753, DOI 10.1016/j.celrep.2012.05.003
   Mohler PJ, 2007, CIRCULATION, V115, P432, DOI 10.1161/CIRCULATIONAHA.106.656512
   Ntantie E, 2013, SCI SIGNAL, V6, DOI 10.1126/scisignal.2003374
   Nunes NM, 2010, EMBO J, V29, P1523, DOI 10.1038/emboj.2010.42
   Ogorodnikov A, 2016, PFLUG ARCH EUR J PHY, V468, P993, DOI 10.1007/s00424-016-1828-3
   Ruepp MD, 2011, MOL BIOL CELL, V22, P91, DOI 10.1091/mbc.E10-06-0543
   Saulière J, 2015, METHODS MOL BIOL, V1296, P151, DOI 10.1007/978-1-4939-2547-6_14
   Slomovic S, 2010, P NATL ACAD SCI USA, V107, P7407, DOI 10.1073/pnas.0910621107
   Ule J, 2005, METHODS, V37, P376, DOI 10.1016/j.ymeth.2005.07.018
   Van Nostrand EL, 2016, NAT METHODS, V13, P508, DOI [10.1038/NMETH.3810, 10.1038/nmeth.3810]
   Yang XC, 2013, MOL CELL BIOL, V33, P28, DOI 10.1128/MCB.00653-12
   Yang XC, 2009, MOL CELL, V36, P267, DOI 10.1016/j.molcel.2009.08.016
   Yao CG, 2013, RNA, V19, P1781, DOI 10.1261/rna.042317.113
   Yao CG, 2012, P NATL ACAD SCI USA, V109, P18773, DOI 10.1073/pnas.1211101109
   Yehudai-Resheff S, 2000, NUCLEIC ACIDS RES, V28, P1139, DOI 10.1093/nar/28.5.1139
   Zarnegar BJ, 2016, NAT METHODS, V13, P489, DOI [10.1038/NMETH.3840, 10.1038/nmeth.3840]
   Zhuang FL, 2012, NUCLEIC ACIDS RES, V40, DOI 10.1093/nar/gkr1263
NR 58
TC 32
Z9 37
U1 0
U2 8
PU OXFORD UNIV PRESS
PI OXFORD
PA GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND
SN 0305-1048
EI 1362-4962
J9 NUCLEIC ACIDS RES
JI Nucleic Acids Res.
PD JUN 2
PY 2017
VL 45
IS 10
BP 6074
EP 6086
DI 10.1093/nar/gkx152
PG 13
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA EW4YH
UT WOS:000402510700052
PM 28334977
OA gold, Green Published, Green Submitted
DA 2025-04-10
ER

PT J
AU O'Reilly, M
   Marshall, E
   Speirs, HJL
   Brown, RW
AF O'Reilly, M
   Marshall, E
   Speirs, HJL
   Brown, RW
TI WNK1, a gene within a novel blood pressure control pathway,
   tissue-specifically generates radically different isoforms with and
   without a kinase domain
SO JOURNAL OF THE AMERICAN SOCIETY OF NEPHROLOGY
LA English
DT Article
ID INHERITED HYPERTENSION; HYPERKALEMIA; CL; REABSORPTION; KIDNEY
AB WNK1 is a member of a novel serine/threonine kinase family, With-No-K, (lysine). Intronic deletions in the encoding gene cause Gordon syndrome, an autosomal dominant, hypertensive, hyperkalemic disorder particularly responsive to thiazide diuretics, a first-line treatment in essential hypertension. To elucidate the novel WNK1 BP control pathway active in distal nephron, WNK1 expression in mouse was studied. It was found that WNK1 is highly expressed in testis > heart, lung, kidney, placenta > skeletal muscle, brain, and widely at low levels. Several WNK1 transcript classes are demonstrated, showing tissue-, developmental-, and nephron-segment-specific expression. Importantly, in kidney, the most prominent transcripts are smaller than elsewhere, having the first four exons replaced by an alternative 5'-exon, deleting the kinase domain, and showing strong distal nephron expression, whereas larger transcripts show low-level widespread distribution. Alternative splicing of exons I I and 12 is prominent-for example, transcripts containing exon I I are abundant in neural tissues, testis, and secondary renal transcripts but are predominantly absent in placenta. The transcriptional diversity generated by these events would produce proteins greatly differing in both structure and function. These findings help further define and clarify the role of WNK1 and the thiazide-responsive pathway relevant to essential hypertension in which it participates.
C1 Univ Edinburgh, Edinburgh EH8 9YL, Midlothian, Scotland.
C3 University of Edinburgh
RP Brown, RW (corresponding author), Western Gen Hosp, Mol Med Ctr, Edinburgh EH4 2XU, Midlothian, Scotland.
CR Bonny O, 2002, J AM SOC NEPHROL, V13, P2399, DOI 10.1097/01.ASN.0000028641.59030.B2
   Brown RW, 1996, BIOCHEM J, V313, P1007, DOI 10.1042/bj3131007
   Choate KA, 2003, P NATL ACAD SCI USA, V100, P663, DOI 10.1073/pnas.242728499
   Estévez R, 2001, NATURE, V414, P558, DOI 10.1038/35107099
   GORDON RD, 1986, HYPERTENSION, V8, P93, DOI 10.1161/01.HYP.8.2.93
   Gordon Richard D., 1995, P2111
   Hübner CA, 2002, HUM MOL GENET, V11, P2435, DOI 10.1093/hmg/11.20.2435
   Lifton RP, 2001, CELL, V104, P545, DOI 10.1016/S0092-8674(01)00241-0
   Liu WG, 1997, NAT GENET, V16, P328, DOI 10.1038/ng0897-328
   MacDonald P, 2000, J ENDOCRINOL, V165, P25, DOI 10.1677/joe.0.1650025
   Meneton P, 2001, SEMIN NEPHROL, V21, P81, DOI 10.1053/snep.2001.21210
   Pagani F, 2002, NAT GENET, V30, P426, DOI 10.1038/ng858
   Rossier BC, 2003, J CLIN INVEST, V111, P947, DOI 10.1172/JCI200318232
   SCHAMBELAN M, 1981, KIDNEY INT, V19, P716, DOI 10.1038/ki.1981.72
   Veríssimo F, 2001, ONCOGENE, V20, P5562, DOI 10.1038/sj.onc.1204726
   Wilson FH, 2001, SCIENCE, V293, P1107, DOI 10.1126/science.1062844
   Wilson FH, 2003, P NATL ACAD SCI USA, V100, P680, DOI 10.1073/pnas.242735399
   Xu BE, 2002, J BIOL CHEM, V277, P48456, DOI 10.1074/jbc.M207917200
   Xu BE, 2000, J BIOL CHEM, V275, P16795, DOI 10.1074/jbc.275.22.16795
   Xu Q, 2002, NUCLEIC ACIDS RES, V30, P3754, DOI 10.1093/nar/gkf492
   Yang CL, 2003, J CLIN INVEST, V111, P1039, DOI 10.1172/JCI200317443
NR 21
TC 153
Z9 167
U1 0
U2 1
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA 530 WALNUT ST, PHILADELPHIA, PA 19106-3621 USA
SN 1046-6673
J9 J AM SOC NEPHROL
JI J. Am. Soc. Nephrol.
PD OCT
PY 2003
VL 14
IS 10
BP 2447
EP 2456
DI 10.1097/01.ASN.0000089830.97681.3B
PG 10
WC Urology & Nephrology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Urology & Nephrology
GA 725JR
UT WOS:000185540800006
PM 14514722
DA 2025-04-10
ER

PT J
AU Mannon, RB
   Coffman, TM
   Mannon, PJ
AF Mannon, RB
   Coffman, TM
   Mannon, PJ
TI Distribution of binding sites for thromboxane A(2) in the mouse kidney
SO AMERICAN JOURNAL OF PHYSIOLOGY-RENAL PHYSIOLOGY
LA English
DT Article
DE glomerulus; medulla; eicosanoid; receptor autoradiography
ID MURINE LUPUS NEPHRITIS; GLOMERULAR MESANGIAL CELLS; PROSTAGLANDIN-E
   RECEPTOR; RAT-KIDNEY; SIGNAL-TRANSDUCTION; CDNA CLONING; EXPRESSION;
   LOCALIZATION; PLATELETS; HEMODYNAMICS
AB Thromboxane A(2) (TxA(2)) is a potent vasoconstrictor eicosanoid that has been implicated in the pathogenesis of both human and experimental renal diseases. The biological actions of TxA(2) in the kidney are mediated through specific cell-surface receptors. In this report, we characterize the distribution of thromboxane receptors (TxR) within the normal mouse kidney by receptor autoradiography. With the iodinated TxR agonist [I-125]BOP, TxA(2) binding sites were detected throughout the kidney. Competitive inhibition curves of whole kidney binding demonstrated a half-maximal inhibitory concentration of 6.5 nM. When Scatchard analysis was performed on anatomically discrete regions, the [I-125]BOP binding in the medulla was best fit by a one-site model, with a dissociation constant (K-d) of 8.2 +/- 2.2 nM. In contrast, [I-125]BOP binding in the cortex was better described by a two-site model, with estimated K-d Of 262 +/- 16 pM for a higher affinity site and 16.9 +/- 1.3 nM for a lower affinity site. These sites do not appear to represent receptor isoforms that arise from alternative splicing of mRNA. The lower affinity binding sites may represent a novel TxR or an alternative affinity state for the previously characterized high-affinity binding site.
C1 DUKE UNIV, DEPT MED, DIV NEPHROL, DURHAM, NC 27705 USA.
   DUKE UNIV, DEPT MED, DIV GASTROENTEROL, DURHAM, NC 27705 USA.
C3 Duke University; Duke University
RP VET ADM MED CTR, NEPHROL SECT 111I, RM B3002, 508 FULTON ST, DURHAM, NC 27705 USA.
CR ABE T, 1995, J CLIN INVEST, V96, P657, DOI 10.1172/JCI118108
   BAYLIS C, 1987, RENAL PHYSIOL BIOCH, V10, P110
   BRUGGEMAN LA, 1991, AM J PHYSIOL, V261, pF488, DOI 10.1152/ajprenal.1991.261.3.F488
   CHAZIANTONIOU C, 1991, AM J PHYSIOL, V261, pF238
   COFFMAN TM, 1989, KIDNEY INT, V35, P24, DOI 10.1038/ki.1989.4
   COFFMAN TM, 1994, J AM SOC NEPHROL, V5, P678
   DORN GW, 1989, J CLIN INVEST, V84, P1883, DOI 10.1172/JCI114375
   ERIKSSON LO, 1990, ACTA PHYSIOL SCAND, V139, P405, DOI 10.1111/j.1748-1716.1990.tb08941.x
   FOLGER WH, 1992, EUR J PHARM-MOLEC PH, V227, P71, DOI 10.1016/0922-4106(92)90144-K
   FUKUNAGA M, 1993, AM J PHYSIOL, V264, pC1619, DOI 10.1152/ajpcell.1993.264.6.C1619
   GERBER JG, 1979, EUR J PHARMACOL, V53, P239, DOI 10.1016/0014-2999(79)90129-8
   HIRATA M, 1991, NATURE, V349, P617, DOI 10.1038/349617a0
   ITO M, 1995, P NATL ACAD SCI USA, V92, P3521, DOI 10.1073/pnas.92.8.3521
   LIANOS EA, 1983, J CLIN INVEST, V72, P1439, DOI 10.1172/JCI111100
   MAIS DE, 1985, J PHARMACOL EXP THER, V233, P418
   MANNON PJ, 1993, PEPTIDES, V14, P567, DOI 10.1016/0196-9781(93)90146-8
   MORINELLI TA, 1989, J PHARMACOL EXP THER, V251, P557
   MUNSON PJ, 1980, ANAL BIOCHEM, V107, P220, DOI 10.1016/0003-2697(80)90515-1
   NAMBA T, 1992, BIOCHEM BIOPH RES CO, V184, P1197, DOI 10.1016/S0006-291X(05)80009-9
   NAMBA T, 1994, J BIOL CHEM, V269, P9986
   NAMBA T, 1993, NATURE, V365, P166, DOI 10.1038/365166a0
   NARUMIYA S, 1994, ANN NY ACAD SCI, V744, P126, DOI 10.1111/j.1749-6632.1994.tb52729.x
   PERICO N, 1986, AM J PHYSIOL, V251, pF581, DOI 10.1152/ajprenal.1986.251.4.F581
   RAYCHOWDHURY MK, 1994, J BIOL CHEM, V269, P19256
   Russell DW., 2001, Molecular Cloning: ALaboratory Manual, V1
   SAMUELSSON B, 1978, ANNU REV BIOCHEM, V47, P997, DOI 10.1146/annurev.bi.47.070178.005025
   SMITH WL, 1992, AM J PHYSIOL, V263, pF181
   SPURNEY RF, 1991, PROSTAG OTH LIPID M, V42, P15, DOI 10.1016/0090-6980(91)90090-3
   SPURNEY RF, 1992, KIDNEY INT, V41, P973, DOI 10.1038/ki.1992.149
   SPURNEY RF, 1993, J PHARMACOL EXP THER, V264, P584
   SPURNEY RF, 1993, AM J PHYSIOL, V264, pF292, DOI 10.1152/ajprenal.1993.264.2.F292
   SPURNEY RF, 1994, AM J PHYSIOL, V267, pF467, DOI 10.1152/ajprenal.1994.267.3.F467
   STUDER RK, 1993, KIDNEY INT, V44, P58, DOI 10.1038/ki.1993.213
   SUGIMOTO Y, 1994, AM J PHYSIOL, V266, pF823, DOI 10.1152/ajprenal.1994.266.5.F823
   TAKAHASHI K, 1992, J CLIN INVEST, V90, P136, DOI 10.1172/JCI115826
   WELCH WJ, 1992, J CLIN INVEST, V89, P1857, DOI 10.1172/JCI115790
   White T. J., 1990, PCRProtocols and ApplicationsA Laboratory Manual, P315
   WILCOX CS, 1985, KIDNEY INT, V28, P43, DOI 10.1038/ki.1985.116
   WILKES BM, 1989, AM J PHYSIOL, V256, pF1111, DOI 10.1152/ajprenal.1989.256.6.F1111
NR 39
TC 16
Z9 16
U1 0
U2 0
PU AMER PHYSIOLOGICAL SOC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA
SN 1931-857X
EI 1522-1466
J9 AM J PHYSIOL-RENAL
JI Am. J. Physiol.-Renal Physiol.
PD DEC
PY 1996
VL 271
IS 6
BP F1131
EP F1138
DI 10.1152/ajprenal.1996.271.6.F1131
PG 8
WC Physiology; Urology & Nephrology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Physiology; Urology & Nephrology
GA WA678
UT WOS:A1996WA67800004
DA 2025-04-10
ER

PT J
AU Wang, J
   Zhu, MC
   Pan, J
   Chen, CC
   Xia, SJ
   Song, YL
AF Wang, Jian
   Zhu, Mengchan
   Pan, Jue
   Chen, Cuicui
   Xia, Shijin
   Song, Yuanlin
TI Circular RNAs: a rising star in respiratory diseases
SO RESPIRATORY RESEARCH
LA English
DT Review
DE Circular RNAs; Non-coding RNA; miRNA sponge; Alternative splicing;
   Respiratory diseases
ID BLOOD MONONUCLEAR-CELLS; ACUTE LUNG INJURY; EXPRESSION; EFFICIENT;
   SEQUENCE; TRANSLATION; PROGRESSION; ABUNDANT; REVEALS; TISSUES
AB Circular RNAs (CircRNAs), as a new class of non-coding RNA molecules that, unlike linear RNAs, have covalently closed loop structures from the ligation of exons, introns, or both. CircRNAs are widely expressed in various organisms in a specie-, tissue-, disease- and developmental stage-specific manner, and have been demonstrated to play a vital role in the pathogenesis and progression of human diseases. An increasing number of recent studies has revealed that circRNAs are intensively associated with different respiratory diseases, including lung cancer, acute respiratory distress syndrome, pulmonary hypertension, pulmonary tuberculosis, and silicosis. However, to the best of our knowledge, there has been no systematic review of studies on the role of circRNAs in respiratory diseases. In this review, we elaborate on the biogenesis, functions, and identification of circRNAs and focus particularly on the potential implications of circRNAs in respiratory diseases.
C1 [Wang, Jian; Zhu, Mengchan; Chen, Cuicui; Song, Yuanlin] Fudan Univ, Zhongshan Hosp, Dept Pulm Med, 180 Fenglin Rd, Shanghai 200032, Peoples R China.
   [Zhu, Mengchan; Pan, Jue] Fudan Univ, Zhongshan Hosp, Dept Infect Dis, 180 Fenglin Rd, Shanghai 200032, Peoples R China.
   [Xia, Shijin] Fudan Univ, Huadong Hosp, Shanghai Inst Geriatr, Dept Geriatr, 221 West Yan An Rd, Shanghai 200040, Peoples R China.
C3 Fudan University; Fudan University; Fudan University
RP Song, YL (corresponding author), Fudan Univ, Zhongshan Hosp, Dept Pulm Med, 180 Fenglin Rd, Shanghai 200032, Peoples R China.; Xia, SJ (corresponding author), Fudan Univ, Huadong Hosp, Shanghai Inst Geriatr, Dept Geriatr, 221 West Yan An Rd, Shanghai 200040, Peoples R China.
EM xiashijinhd@163.com; ylsong70@163.com
FU State Key Basic Research Program [2015CB553404]; National Natural
   Science Foundation of China [81870044, 81770075, 81500026]; Shanghai
   Science and Technology Committee grant [15DZ1930600/15DZ1930602];
   Shanghai Municipal Commission of Health and Family Planning [201540370];
    [81630001];  [81490533]
FX This study was supported by the State Key Basic Research Program project
   (2015CB553404), the National Natural Science Foundation of China
   (81870044, 81770075, 81500026), key grant (81630001, 81490533), Shanghai
   Science and Technology Committee grant (15DZ1930600/15DZ1930602), and
   Shanghai Municipal Commission of Health and Family Planning (201540370).
CR ARNBERG AC, 1980, CELL, V19, P313, DOI 10.1016/0092-8674(80)90505-X
   Ashwal-Fluss R, 2014, MOL CELL, V56, P55, DOI 10.1016/j.molcel.2014.08.019
   Barrett SP, 2016, DEVELOPMENT, V143, P1838, DOI 10.1242/dev.128074
   CHEN CY, 1995, SCIENCE, V268, P415, DOI 10.1126/science.7536344
   Chen LL, 2015, RNA BIOL, V12, P381, DOI 10.1080/15476286.2015.1020271
   Chen W, 2016, TRENDS NEUROSCI, V39, P597, DOI 10.1016/j.tins.2016.06.006
   Chuang TJ, 2016, NUCLEIC ACIDS RES, V44, DOI 10.1093/nar/gkv1013
   Conn SJ, 2015, CELL, V160, P1125, DOI 10.1016/j.cell.2015.02.014
   Dai X, 2018, CARCINOGENESIS, V39, P981, DOI 10.1093/carcin/bgy061
   Danan M, 2012, NUCLEIC ACIDS RES, V40, P3131, DOI 10.1093/nar/gkr1009
   Dong R, 2017, RNA BIOL, V14, P1064, DOI 10.1080/15476286.2016.1269999
   Du WW, 2017, EUR HEART J, V38, P1402, DOI 10.1093/eurheartj/ehw001
   Du WW, 2016, NUCLEIC ACIDS RES, V44, P2846, DOI 10.1093/nar/gkw027
   Fan XM, 2017, BIOMED RES INT, V2017, DOI 10.1155/2017/5135781
   Fang SC, 2018, CELL DEATH DIS, V9, DOI 10.1038/s41419-018-0432-1
   Gao Y, 2018, BRIEF BIOINFORM, V19, P803, DOI 10.1093/bib/bbx014
   Gao Y, 2015, GENOME BIOL, V16, DOI 10.1186/s13059-014-0571-3
   Guo ZL, 2013, J IMMUNOL, V190, P4337, DOI 10.4049/jimmunol.1203233
   Hansen TB, 2016, NUCLEIC ACIDS RES, V44, DOI 10.1093/nar/gkv1458
   Hansen TB, 2013, NATURE, V495, P384, DOI 10.1038/nature11993
   Haque S, 2017, GENES-BASEL, V8, DOI 10.3390/genes8120353
   He J, 2017, CANCER LETT, V396, P138, DOI 10.1016/j.canlet.2017.03.027
   Hoffmann S, 2014, GENOME BIOL, V15, DOI 10.1186/gb-2014-15-2-r34
   Hu W, 2018, CANCER LETT, V427, P18, DOI 10.1016/j.canlet.2018.04.006
   Huang ZK, 2018, CELL PHYSIOL BIOCHEM, V45, P1230, DOI 10.1159/000487454
   Hurgobin B, 2018, RESPIROLOGY, V23, P1117, DOI 10.1111/resp.13401
   Jeck WR, 2014, NAT BIOTECHNOL, V32, P453, DOI 10.1038/nbt.2890
   Jeck WR, 2013, RNA, V19, P141, DOI 10.1261/rna.035667.112
   Khan MAF, 2016, CIRC RES, V119, P996, DOI 10.1161/CIRCRESAHA.116.309568
   Legnini I, 2017, MOL CELL, V66, P22, DOI 10.1016/j.molcel.2017.02.017
   Li F, 2015, ONCOTARGET, V6, P6001, DOI 10.18632/oncotarget.3469
   Liu J, 2017, MOL CANCER, V16, DOI 10.1186/s12943-017-0630-y
   Liu X, 2018, MOL THER-NUCL ACIDS, V13, P312, DOI 10.1016/j.omtn.2018.09.010
   Luo YH, 2017, BIOMED PHARMACOTHER, V96, P892, DOI 10.1016/j.biopha.2017.12.015
   Memczak S, 2013, NATURE, V495, P333, DOI 10.1038/nature11928
   Miao R, 2017, MEDICINE, V96, DOI 10.1097/MD.0000000000007354
   NIGRO JM, 1991, CELL, V64, P607, DOI 10.1016/0092-8674(91)90244-S
   Pamudurti NR, 2017, MOL CELL, V66, P9, DOI 10.1016/j.molcel.2017.02.021
   Pan JY, 2017, MOL THER NUCL ACIDS, V6, P140, DOI 10.1016/j.omtn.2016.11.003
   Panda AC, 2017, WIRES RNA, V8, DOI 10.1002/wrna.1386
   Petkovic S, 2015, NUCLEIC ACIDS RES, V43, P2454, DOI 10.1093/nar/gkv045
   Qian ZQ, 2018, EBIOMEDICINE, V27, P18, DOI 10.1016/j.ebiom.2017.12.007
   Qu SB, 2015, CANCER LETT, V365, P141, DOI 10.1016/j.canlet.2015.06.003
   Rybak-Wolf A, 2015, MOL CELL, V58, P870, DOI 10.1016/j.molcel.2015.03.027
   Salzman J, 2016, TRENDS GENET, V32, P309, DOI 10.1016/j.tig.2016.03.002
   Salzman J, 2013, PLOS GENET, V9, DOI 10.1371/journal.pgen.1003777
   Salzman J, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0030733
   SANGER HL, 1976, P NATL ACAD SCI USA, V73, P3852, DOI 10.1073/pnas.73.11.3852
   Song XF, 2016, NUCLEIC ACIDS RES, V44, DOI 10.1093/nar/gkw075
   Starke S, 2015, CELL REP, V10, P103, DOI 10.1016/j.celrep.2014.12.002
   Szabo L, 2016, NAT REV GENET, V17, P679, DOI 10.1038/nrg.2016.114
   Szabo L, 2015, GENOME BIOL, V16, DOI [10.1186/s13059-015-0690-5, 10.1186/s13059-016-1123-9]
   Tan SY, 2018, CELL RES, V28, P693, DOI 10.1038/s41422-018-0033-7
   Tian F, 2017, BIOCHEM BIOPH RES CO, V493, P1260, DOI 10.1016/j.bbrc.2017.09.136
   Wan L, 2016, BIOMED RES INT, V2016, DOI 10.1155/2016/1579490
   Wan QQ, 2017, BIOCHEM BIOPH RES CO, V493, P684, DOI 10.1016/j.bbrc.2017.08.131
   Wang J, 2018, INT J MOL MED, V42, P1353, DOI 10.3892/ijmm.2018.3740
   Wang K, 2010, NUCLEIC ACIDS RES, V38, DOI 10.1093/nar/gkq622
   WANG KS, 1986, NATURE, V323, P508, DOI 10.1038/323508a0
   Wang K, 2017, CELL DEATH DIFFER, V24, P1111, DOI 10.1038/cdd.2017.61
   Wang Y, 2015, RNA, V21, P172, DOI 10.1261/rna.048272.114
   Werfel S, 2016, J MOL CELL CARDIOL, V98, P103, DOI 10.1016/j.yjmcc.2016.07.007
   Wesselhoeft RA, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-05096-6
   Westholm JO, 2014, CELL REP, V9, P1966, DOI 10.1016/j.celrep.2014.10.062
   Xu ZJ, 2014, BIOCHEM BIOPH RES CO, V445, P48, DOI 10.1016/j.bbrc.2014.01.108
   Yang F, 2017, J THORAC DIS, V9, P5382, DOI 10.21037/jtd.2017.10.143
   Yang XY, 2018, FASEB J, V32, P3264, DOI 10.1096/fj.201701118R
   Yang Y, 2017, CELL RES, V27, P626, DOI 10.1038/cr.2017.31
   Ye ZQ, 2018, J PHYSIOL BIOCHEM, V74, P25, DOI 10.1007/s13105-017-0598-5
   Yi ZJ, 2018, J CELL MOL MED, V22, P4076, DOI 10.1111/jcmm.13684
   Zeng XX, 2017, PLOS COMPUT BIOL, V13, DOI 10.1371/journal.pcbi.1005420
   Zhang X, 2017, ONCOTARGET, V8
   Zhang XO, 2014, CELL, V159, P134, DOI 10.1016/j.cell.2014.09.001
   Zhang XF, 2018, ONCOTARGETS THER, V11, P3979, DOI 10.2147/OTT.S158316
   Zhang Y, 2013, MOL CELL, V51, P792, DOI 10.1016/j.molcel.2013.08.017
   Zhang YN, 2018, MOL MED REP, V17, P7692, DOI 10.3892/mmr.2018.8830
   Zhou ZW, 2018, THERANOSTICS, V8, P575, DOI 10.7150/thno.21648
   Zhuang ZG, 2017, MOL IMMUNOL, V90, P264, DOI 10.1016/j.molimm.2017.08.008
NR 78
TC 72
Z9 79
U1 2
U2 21
PU BMC
PI LONDON
PA CAMPUS, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
EI 1465-993X
J9 RESP RES
JI Respir. Res.
PD JAN 5
PY 2019
VL 20
AR 3
DI 10.1186/s12931-018-0962-1
PG 10
WC Respiratory System
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Respiratory System
GA HG3UC
UT WOS:000454899200001
PM 30611252
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Bogdanov, VY
   Versteeg, HH
AF Bogdanov, Vladimir Y.
   Versteeg, Henri H.
TI "Soluble Tissue Factor" in the 21st Century: Definitions, Biochemistry,
   and Pathophysiological Role in Thrombus Formation
SO SEMINARS IN THROMBOSIS AND HEMOSTASIS
LA English
DT Article
DE tissue factor; thrombosis; microparticle; alternative splicing;
   atherosclerosis
ID FACTOR-POSITIVE MICROPARTICLES; PROCOAGULANT ACTIVITY;
   PANCREATIC-CANCER; BLOOD-COAGULATION; ENDOTHELIAL-CELLS; FACTOR
   EXPRESSION; ACTIVATION; GROWTH; ANGIOGENESIS; PLASMA
AB Tissue factor (TF), the main trigger of blood coagulation, is essential for normal hemostasis. Over the past 20 years, heightened intravascular levels and activity of TF have been increasingly perceived as an entity that significantly contributes to venous as well as arterial thrombosis. Various forms of the TF protein in the circulation have been described and proposed to be thrombogenic. Aside from cell and vessel wall-associated TF, several forms of non-cell-associated TF circulate in plasma and may serve as a causative factor in thrombosis. At the present time, no firm consensus exists regarding the extent, the vascular setting(s), and/or the mechanisms by which such TF forms contribute to thrombus initiation and propagation. Here, we summarize the existing paradigms and recent, sometimes paradigm-shifting findings elucidating the structural, mechanistic, and pathophysiological characteristics of plasma-borne TF.
C1 [Bogdanov, Vladimir Y.] Univ Cincinnati, Div Hematol Oncol, Dept Internal Med, Coll Med, Cincinnati, OH 45267 USA.
   [Versteeg, Henri H.] Leiden Univ, Med Ctr, Sect Thrombosis & Hemostasis, Dept Internal Med, Leiden, Netherlands.
C3 University System of Ohio; University of Cincinnati; Leiden University;
   Leiden University Medical Center (LUMC); Leiden University - Excl LUMC
RP Bogdanov, VY (corresponding author), Univ Cincinnati, Div Hematol Oncol, Dept Internal Med, Coll Med, 3125 Eden Ave,Suite 1316, Cincinnati, OH 45267 USA.
EM vladimir.bogdanov@uc.edu
RI ; Versteeg, Henri/G-1783-2018
OI Bogdanov, Vladimir/0000-0003-4968-1129; Versteeg,
   Henri/0000-0003-4294-175X
FU NIH/NCI [R21CA160293, R01CA190717]
FX We are grateful to Dusten Unruh (University of Cincinnati, Ohio) for his
   help with the drawings, and to Prof. John-Bjarne Hansen (University of
   Tromso, Norway) for his insightful suggestions. This work was supported
   in part by NIH/NCI grants R21CA160293 and R01CA190717 to V.Y.B. The
   content is solely the responsibility of the authors and does not
   necessarily represent the official views of the National Institutes of
   Health.
CR Arraud N, 2014, J THROMB HAEMOST, V12, P614, DOI 10.1111/jth.12554
   Ashcroft BA, 2012, BIOMED MICRODEVICES, V14, P641, DOI 10.1007/s10544-012-9642-y
   Balasubramanian V, 2002, BLOOD, V100, P2787, DOI 10.1182/blood-2002-03-0902
   Banner DW, 1996, NATURE, V380, P41, DOI 10.1038/380041a0
   Berckmans RJ, 2001, THROMB HAEMOSTASIS, V85, P639
   Biró É, 2003, J THROMB HAEMOST, V1, P2561, DOI 10.1046/j.1538-7836.2003.00456.x
   Bogdanov VY, 2006, CURR MOL MED, V6, P859, DOI 10.2174/156652406779010821
   Bogdanov VY, 2006, J THROMB HAEMOST, V4, P158, DOI 10.1111/j.1538-7836.2005.01680.x
   Bogdanov VY, 2003, NAT MED, V9, P458, DOI 10.1038/nm841
   Borissoff JI, 2010, CIRCULATION, V122, P821, DOI 10.1161/CIRCULATIONAHA.109.907121
   Camera M, 2012, THROMB RES, V129, P279, DOI 10.1016/j.thromres.2011.11.028
   Chandradas S, 2010, J LEUKOCYTE BIOL, V87, P147, DOI 10.1189/jlb.0409252
   Chen VM, 2013, J THROMB HAEMOST, V11, P277, DOI 10.1111/jth.12228
   CLOWES AW, 1989, J CARDIOVASC PHARM, V14, pS12, DOI 10.1097/00005344-198900146-00005
   Davila M, 2014, J THROMB HAEMOST, V12, P186, DOI 10.1111/jth.12475
   del Conde I, 2005, BLOOD, V106, P1604, DOI 10.1182/blood-2004-03-1095
   Diamant M, 2002, CIRCULATION, V106, P2442, DOI 10.1161/01.CIR.0000036596.59665.C6
   Eisenreich A, 2009, CIRC RES, V104, P589, DOI 10.1161/CIRCRESAHA.108.183905
   Eisenreichi A, 2013, ONCOL REP, V30, P462, DOI 10.3892/or.2013.2413
   Ettelaie C, 2014, J EXTRACELL VESICLES, V3, DOI 10.3402/jev.v3.23592
   Fareed J, 2015, NAT REV CARDIOL, V12, P70, DOI 10.1038/nrcardio.2014.222
   FIORE MM, 1994, J BIOL CHEM, V269, P143
   Fogelson AL, 1998, J THEOR BIOL, V193, P1, DOI 10.1006/jtbi.1998.0670
   Giannarelli C, 2014, CIRCULATION, V130, P1274, DOI 10.1161/CIRCULATIONAHA.114.006614
   Giesen PLA, 1999, P NATL ACAD SCI USA, V96, P2311, DOI 10.1073/pnas.96.5.2311
   Godby RC, 2012, MOL MED, V18, P771, DOI 10.2119/molmed.2011.00416
   Gruber A, 2014, THROMB RES, V133, pS45, DOI 10.1016/j.thromres.2014.03.019
   Haas SL, 2006, WORLD J GASTROENTERO, V12, P4843
   Himber J, 2002, BLOOD, V99, P4249, DOI 10.1182/blood-2002-02-0557
   Hobbs JE, 2007, THROMB RES, V120, pS13, DOI 10.1016/S0049-3848(07)70126-3
   Jakubowski JA, 2014, THROMB RES, V133, P190, DOI 10.1016/j.thromres.2013.12.008
   Johansson H, 2005, DIABETES, V54, P1755, DOI 10.2337/diabetes.54.6.1755
   Joop K, 2001, THROMB HAEMOSTASIS, V85, P810
   Karnicki K, 2002, ARTERIOSCL THROM VAS, V22, P1495, DOI 10.1161/01.ATV.0000029968.34056.94
   Key NS, 1998, BLOOD, V91, P4216, DOI 10.1182/blood.V91.11.4216.411k15_4216_4223
   Khan MMH, 2006, THROMB HAEMOSTASIS, V95, P462, DOI 10.1160/TH05-06-0432
   Khorana AA, 2007, CLIN CANCER RES, V13, P2870, DOI 10.1158/1078-0432.CCR-06-2351
   Kocatürk B, 2013, J THROMB HAEMOST, V11, P285, DOI 10.1111/jth.12222
   Kocatürk B, 2013, P NATL ACAD SCI USA, V110, P11517, DOI 10.1073/pnas.1307100110
   Kooiman J, 2015, J THROMB THROMBOLYS, V40, P323, DOI 10.1007/s11239-015-1180-z
   Leiderman K, 2014, THROMB RES, V133, pS12, DOI 10.1016/j.thromres.2014.03.005
   Lind C, 2014, CIRCULATION, V129, P855, DOI 10.1161/CIRCULATIONAHA.113.004168
   Mallat Z, 1999, CIRCULATION, V99, P348, DOI 10.1161/01.CIR.99.3.348
   Marmur JD, 1996, CIRCULATION, V94, P1226, DOI 10.1161/01.CIR.94.6.1226
   Muhlfelder TW, 1999, THROMB HAEMOSTASIS, V81, P146
   OSTERUD B, 1982, SCAND J HAEMATOL, V29, P175
   Owens AP, 2010, THROMB HAEMOSTASIS, V104, P432, DOI 10.1160/TH09-11-0771
   Palmerini T, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0081501
   PRAGER NA, 1995, CIRCULATION, V92, P962, DOI 10.1161/01.CIR.92.4.962
   Puy C, 2015, BLOOD, V125, P1488, DOI 10.1182/blood-2014-10-604587
   Rauch U, 2000, BLOOD, V96, P170, DOI 10.1182/blood.V96.1.170.013k42_170_175
   Rauch U, 2000, TRENDS CARDIOVAS MED, V10, P139, DOI 10.1016/S1050-1738(00)00049-9
   Schecter AD, 2000, CIRC RES, V87, P126, DOI 10.1161/01.RES.87.2.126
   Shet AS, 2003, BLOOD, V102, P2678, DOI 10.1182/blood-2003-03-0693
   SILBERBERG JM, 1989, CANCER RES, V49, P5443
   SPICER EK, 1987, P NATL ACAD SCI USA, V84, P5148, DOI 10.1073/pnas.84.15.5148
   Srinivasan R, 2011, J THROMB HAEMOST, V9, P2087, DOI 10.1111/j.1538-7836.2011.04454.x
   Stavrou EX, 2015, BLOOD, V125, P710, DOI 10.1182/blood-2014-01-550285
   Szotowski B, 2005, CIRC RES, V96, P1233, DOI 10.1161/01.RES.0000171805.24799.fa
   Thaler J, 2014, THROMB RES, V134, P1093, DOI 10.1016/j.thromres.2014.07.041
   Thaler J, 2014, TRANSL RES, V163, P145, DOI 10.1016/j.trsl.2013.06.009
   Toschi V, 1997, CIRCULATION, V95, P594, DOI 10.1161/01.CIR.95.3.594
   Unruh D, 2015, J THROMB HAEMOST, V13, P111
   Unruh D, ANN SURG ONCOL
   Unruh D, 2014, INT J CANCER, V134, P9, DOI 10.1002/ijc.28327
   van den Berg YW, 2009, P NATL ACAD SCI USA, V106, P19497, DOI 10.1073/pnas.0905325106
   van den Berg YW, 2012, BLOOD, V119, P924, DOI 10.1182/blood-2011-06-317685
   Walenga JM, 2014, CLIN APPL THROMB-HEM, V20, P678, DOI 10.1177/1076029614545212
   Wang JG, 2012, BLOOD, V119, P5543, DOI 10.1182/blood-2012-01-402156
   Wang JT, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0090146
   Willemze R, 2014, THROMB RES, V133, P187, DOI 10.1016/j.thromres.2013.11.027
   Ye RY, 2012, THROMB RES, V130, P253, DOI 10.1016/j.thromres.2011.10.014
   Zwaal RFA, 1997, BLOOD, V89, P1121, DOI 10.1182/blood.V89.4.1121
NR 73
TC 29
Z9 31
U1 0
U2 7
PU THIEME MEDICAL PUBL INC
PI NEW YORK
PA 333 SEVENTH AVE, NEW YORK, NY 10001 USA
SN 0094-6176
EI 1098-9064
J9 SEMIN THROMB HEMOST
JI Semin. Thromb. Hemost.
PD OCT
PY 2015
VL 41
IS 7
BP 700
EP 707
DI 10.1055/s-0035-1556049
PG 8
WC Hematology; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Hematology; Cardiovascular System & Cardiology
GA CT0NW
UT WOS:000362494200005
PM 26408917
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Kraev, A
   Chumakov, I
   Carafoli, E
AF Kraev, A
   Chumakov, I
   Carafoli, E
TI The organization of the human gene NCX1 encoding the sodium-calcium
   exchanger
SO GENOMICS
LA English
DT Article
ID SARCOLEMMAL NA+-CA2+ EXCHANGER; TISSUE-SPECIFIC EXPRESSION; NA+/CA2+
   EXCHANGER; FUNCTIONAL EXPRESSION; GEL-ELECTROPHORESIS;
   MOLECULAR-CLONING; NA/CA EXCHANGER; DNA; ISOFORMS; LOCALIZATION
AB The intron-exon organization of the human Na/Ca-exchanger gene NCX1 and of the N-terminal half of the related gene NCX2 has been determined. The NCX1 gene consists of 12 exons spread over 200 kb on chromosome 2 close to STS D2S2328 and encodes a 6.2-kb transcript. Both NCX1 and NCX2 feature an unusual 1,8-kb exon, containing two-thirds of the protein coding sequence and a similar area of the coding sequences split into several small exons, displaying tissue-specific alternative splicing. The similar intron positions in the ''cardiac'' (NCX1) and ''brain'' (NCX2) mammalian exchanger genes suggest their origin from the recent duplication and translocation of a common ancestral gene, a putative precursor of which has been identified in the nematode Caenorhabditis elegans. (C) 1996 Academic Press, Inc.
C1 ETH ZURICH, LAB BIOCHEM 3, INST BIOCHEM, CH-8092 ZURICH, SWITZERLAND.
   FDN JEAN DAUSSET, CEPH, F-75010 PARIS, FRANCE.
C3 Swiss Federal Institutes of Technology Domain; ETH Zurich; Foundation
   Jean Dausset-CEPH
RI Carafoli, Ernesto/K-5192-2016
OI Carafoli, Ernesto/0000-0002-7826-0094
CR ADAMS MD, 1993, NAT GENET, V4, P256, DOI 10.1038/ng0793-256
   ALTSCHUL SF, 1990, J MOL BIOL, V215, P403, DOI 10.1016/S0022-2836(05)80360-2
   AUSUBEL FM, 2003, CURRENT PROTOCOLS MO
   BAKER PF, 1969, J PHYSIOL-LONDON, V200, P431, DOI 10.1113/jphysiol.1969.sp008702
   BENTON WD, 1977, SCIENCE, V196, P180, DOI 10.1126/science.322279
   BROWNSTEIN BH, 1989, SCIENCE, V244, P1348, DOI 10.1126/science.2544027
   CARLE GF, 1987, METHOD ENZYMOL, V155, P468
   CHENG S, 1994, P NATL ACAD SCI USA, V91, P5695, DOI 10.1073/pnas.91.12.5695
   CHEON J, 1989, ARCH BIOCHEM BIOPHYS, V267, P736
   CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
   CHURCH GM, 1984, P NATL ACAD SCI-BIOL, V81, P1991, DOI 10.1073/pnas.81.7.1991
   COHEN D, 1993, NATURE, V366, P698, DOI 10.1038/366698a0
   COOK PR, 1984, EMBO J, V3, P1837, DOI 10.1002/j.1460-2075.1984.tb02056.x
   DEVEREUX J, 1984, NUCLEIC ACIDS RES, V12, P387, DOI 10.1093/nar/12.1Part1.387
   DEVON RS, 1995, NUCLEIC ACIDS RES, V23, P1644, DOI 10.1093/nar/23.9.1644
   DOMINGUEZ JH, 1992, AM J PHYSIOL, V263, pF945, DOI 10.1152/ajprenal.1992.263.5.F945
   FEINBERG AP, 1983, ANAL BIOCHEM, V132, P6, DOI 10.1016/0003-2697(83)90418-9
   FRANK JS, 1992, J CELL BIOL, V117, P337, DOI 10.1083/jcb.117.2.337
   FURMAN I, 1993, FEBS LETT, V319, P105, DOI 10.1016/0014-5793(93)80046-W
   GABELLINI N, 1995, J BIOL CHEM, V270, P6917, DOI 10.1074/jbc.270.12.6917
   GROSS-BELLARD MM, 1973, EUR J BIOCHEM, V36, P32, DOI 10.1111/j.1432-1033.1973.tb02881.x
   JUHASZOVA M, 1994, AM J PHYSIOL, V266, pC234, DOI 10.1152/ajpcell.1994.266.1.C234
   KIMURA M, 1993, J BIOL CHEM, V268, P6874
   KOFUJI P, 1993, AM J PHYSIOL, V265, pF598, DOI 10.1152/ajprenal.1993.265.4.F598
   KOFUJI P, 1994, J BIOL CHEM, V269, P5145
   KOFUJI P, 1992, AM J PHYSIOL, V263, pC1241, DOI 10.1152/ajpcell.1992.263.6.C1241
   KOMURO I, 1992, P NATL ACAD SCI USA, V89, P4769, DOI 10.1073/pnas.89.10.4769
   LEE SL, 1994, J BIOL CHEM, V269, P14849
   LI ZP, 1994, J BIOL CHEM, V269, P17434
   LUTHER PW, 1992, J NEUROSCI, V12, P4898
   MATSUOKA S, 1993, P NATL ACAD SCI USA, V90, P3870, DOI 10.1073/pnas.90.9.3870
   MICHAELIS ML, 1991, ANN NY ACAD SCI, V639, P250, DOI 10.1111/j.1749-6632.1991.tb17313.x
   NAKASAKI Y, 1993, J BIOCHEM-TOKYO, V114, P528, DOI 10.1093/oxfordjournals.jbchem.a124211
   NICOLL DA, 1990, SCIENCE, V250, P562, DOI 10.1126/science.1700476
   Philipson K D, 1993, Int Rev Cytol, V137C, P199
   REED KC, 1985, NUCLEIC ACIDS RES, V13, P7207, DOI 10.1093/nar/13.20.7207
   REILANDER H, 1992, EMBO J, V11, P1689, DOI 10.1002/j.1460-2075.1992.tb05219.x
   REILLY RF, 1993, AM J PHYSIOL, V265, pF327, DOI 10.1152/ajprenal.1993.265.2.F327
   REILLY RF, 1992, AM J PHYSIOL, V262, pF1105, DOI 10.1152/ajprenal.1992.262.6.F1105
   REUTER H, 1995, NEURON, V15, P1077, DOI 10.1016/0896-6273(95)90096-9
   SHIEH BH, 1992, GENOMICS, V12, P616, DOI 10.1016/0888-7543(92)90459-6
   SOUTHERN EM, 1975, J MOL BIOL, V98, P503, DOI 10.1016/S0022-2836(75)80083-0
   VOLLOCH VZ, 1994, NUCLEIC ACIDS RES, V22, P5302, DOI 10.1093/nar/22.24.5302
   Voss H., 1992, Methods in Molecular and Cellular Biology, V3, P153
   WILIMZIG M, 1985, TRENDS GENET, V1, P185
NR 45
TC 45
Z9 48
U1 0
U2 0
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0888-7543
EI 1089-8646
J9 GENOMICS
JI Genomics
PD OCT 1
PY 1996
VL 37
IS 1
BP 105
EP 112
DI 10.1006/geno.1996.0526
PG 8
WC Biotechnology & Applied Microbiology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biotechnology & Applied Microbiology; Genetics & Heredity
GA VL371
UT WOS:A1996VL37100014
PM 8921376
DA 2025-04-10
ER

PT J
AU Lee, J
   Baldwin, WM
   Lee, CY
   Desiderio, S
AF Lee, Jihyun
   Baldwin, William M., III
   Lee, Chih-Yuan
   Desiderio, Stephen
TI Stat3β mitigates development of atherosclerosis in apolipoprotein
   E-deficient mice
SO JOURNAL OF MOLECULAR MEDICINE-JMM
LA English
DT Article
DE Stat3; Atherosclerosis; Inflammation; Acute phase response
ID C-REACTIVE PROTEIN; FUTURE MYOCARDIAL-INFARCTION;
   CORONARY-ARTERY-DISEASE; APPARENTLY HEALTHY-MEN; T-CELL; REDUCED
   ATHEROSCLEROSIS; CARDIOVASCULAR-DISEASE; PLASMA-CONCENTRATION;
   HEART-DISEASE; MOUSE MODELS
AB The transcription factor Stat3 is an activator of systemic inflammatory genes. Two isoforms of Stat3 are generated by alternative splicing, Stat3 alpha and Stat3 beta. The beta isoform lacks the transactivation domain but retains other functions, including dimerization and DNA binding. Stat3 beta-deficient mice exhibit elevated expression of systemic inflammatory genes and are hyperresponsive to lipopolysaccharide, suggesting that Stat3 beta functions predominantly as a suppressor of systemic inflammation. To test whether Stat3 beta deficiency would provoke pathologic effects associated with chronic inflammation, we asked whether selective removal of Stat3 beta would exacerbate the development of atherosclerosis in apolipoprotein E-deficient mice. In apoE(-/-)Stat3 beta(-/-) mice atherosclerotic plaque formation was significantly enhanced relative to apoE(-/-)Stat3 beta(+/+) controls. The ability of Stat3 beta deficiency to promote atherosclerosis was more pronounced in female mice, but could be unmasked in males by feeding a high fat diet. Infiltrating macrophages were not increased in aortas of apoE(-/-)Stat3 beta(-/-) mice. In contrast, the proportion of pro-inflammatory T(H)17 cells was significantly elevated in aortic infiltrates from apoE(-/-)Stat3 beta(-/-) mice, relative to paired apoE(-/-)Stat3 beta(+/+) littermates. These observations indicate that Stat3 beta can suppress pathologic sequelae associated with chronic inflammation. Our findings further suggest that in Stat3 beta-deficient mice the unopposed action of Stat3 alpha may enhance atherogenesis in part by promoting differentiation of T(H)17 cells.
C1 [Lee, Jihyun; Desiderio, Stephen] Johns Hopkins Univ, Sch Med, Dept Mol Biol & Genet, Baltimore, MD 21205 USA.
   [Lee, Jihyun; Desiderio, Stephen] Johns Hopkins Univ, Sch Med, Inst Cell Engn, Baltimore, MD 21205 USA.
   [Baldwin, William M., III] Cleveland Clin Fdn, Lerner Res Inst, Dept Immunol, Cleveland, OH 44195 USA.
   [Lee, Chih-Yuan] Natl Taiwan Univ Hosp, Dept Surg, Taipei 100, Taiwan.
   [Lee, Jihyun] Univ Penn, Perelman Sch Med, Abramson Family Canc Res Inst, Philadelphia, PA 19104 USA.
C3 Johns Hopkins University; Johns Hopkins University; Cleveland Clinic
   Foundation; National Taiwan University; National Taiwan University
   Hospital; University of Pennsylvania
RP Desiderio, S (corresponding author), Johns Hopkins Univ, Sch Med, Dept Mol Biol & Genet, Room 619,733 N Broadway, Baltimore, MD 21205 USA.
EM sdesider@jhmi.edu
RI Lee, Yu-Ching/H-4914-2017
OI Lee, Chih-Yuan/0000-0001-5034-3544
FU National Institutes of Health [HL073971]; National Institute of General
   Medical Sciences training grant [5T32GM008752]
FX We are grateful to Dominic Dordai for expert technical support and Karen
   Fox-Talbot for preparation and staining of aortic root samples. The work
   was supported by National Institutes of Health grant HL073971 and by a
   gift to the Johns Hopkins Institute for Cell Engineering. J.L. was
   supported in part by National Institute of General Medical Sciences
   training grant 5T32GM008752. The authors have no commercial or other
   associations that would pose a conflict of interest in connection with
   this manuscript.
CR Asanuma Y, 2003, NEW ENGL J MED, V349, P2407, DOI 10.1056/NEJMoa035611
   AUSTIN MA, 1989, AM J EPIDEMIOL, V129, P249, DOI 10.1093/oxfordjournals.aje.a115130
   AUSTYN JM, 1981, EUR J IMMUNOL, V11, P805, DOI 10.1002/eji.1830111013
   Avagyan S, 2011, BLOOD, V118, P6078, DOI 10.1182/blood-2011-07-365080
   Bates SH, 2003, NATURE, V421, P856, DOI 10.1038/nature01388
   Björkbacka H, 2004, NAT MED, V10, P416, DOI 10.1038/nm1008
   Blankenberg S, 2003, ATHEROSCLEROSIS, V170, P191, DOI 10.1016/S0021-9150(03)00097-2
   Breslow JL, 1996, SCIENCE, V272, P685, DOI 10.1126/science.272.5262.685
   Butcher MJ, 2012, CIRC RES, V110, P675, DOI 10.1161/CIRCRESAHA.111.261784
   Caldenhoven E, 1996, J BIOL CHEM, V271, P13221, DOI 10.1074/jbc.271.22.13221
   Caligiuri G, 1999, ATHEROSCLEROSIS, V145, P301, DOI 10.1016/S0021-9150(99)00081-7
   Cernkovich ER, 2008, ENDOCRINOLOGY, V149, P1581, DOI 10.1210/en.2007-1148
   Chang X, 2005, J EXP MED, V202, P1141, DOI 10.1084/jem.20050157
   Chiba T, 2008, ATHEROSCLEROSIS, V196, P68, DOI 10.1016/j.atherosclerosis.2007.01.040
   Desiderio S, 2003, ANN NY ACAD SCI, V987, P280, DOI 10.1111/j.1749-6632.2003.tb06062.x
   Durant L, 2010, IMMUNITY, V32, P605, DOI 10.1016/j.immuni.2010.05.003
   Erbel C, 2009, J IMMUNOL, V183, P8167, DOI 10.4049/jimmunol.0901126
   Gao Q, 2010, J IMMUNOL, V185, P5820, DOI 10.4049/jimmunol.1000116
   Gotto AM, 1998, AM J CARDIOL, V82, p22Q
   Hansson GK, 2006, NAT REV IMMUNOL, V6, P508, DOI 10.1038/nri1882
   Harris TJ, 2007, J IMMUNOL, V179, P4313, DOI 10.4049/jimmunol.179.7.4313
   Ivanov II, 2006, CELL, V126, P1121, DOI 10.1016/j.cell.2006.07.035
   Kirii H, 2003, ARTERIOSCL THROM VAS, V23, P656, DOI 10.1161/01.ATV.0000064374.15232.C3
   Koenig W, 1999, CIRCULATION, V99, P237, DOI 10.1161/01.CIR.99.2.237
   Korn T, 2009, ANNU REV IMMUNOL, V27, P485, DOI 10.1146/annurev.immunol.021908.132710
   KRAAL G, 1987, SCAND J IMMUNOL, V26, P653, DOI 10.1111/j.1365-3083.1987.tb02301.x
   Lesina M, 2011, CANCER CELL, V19, P456, DOI 10.1016/j.ccr.2011.03.009
   Lyngdorf LG, 2003, CARDIOVASC RES, V59, P854, DOI 10.1016/S0008-6363(03)00506-6
   Ma YL, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0035835
   Mallat Z, 1999, CIRC RES, V85, pE17, DOI 10.1161/01.RES.85.8.e17
   Maritano D, 2004, NAT IMMUNOL, V5, P401, DOI 10.1038/ni1052
   Moore KJ, 2011, CELL, V145, P341, DOI 10.1016/j.cell.2011.04.005
   NAKASHIMA Y, 1994, ARTERIOSCLER THROMB, V14, P133, DOI 10.1161/01.ATV.14.1.133
   Ray Jenna Lynn, 2001, Methods in Cell Science, V23, P185
   REDDICK RL, 1994, ARTERIOSCLER THROMB, V14, P141, DOI 10.1161/01.ATV.14.1.141
   Ridker PM, 2000, CIRCULATION, V101, P1767, DOI 10.1161/01.CIR.101.15.1767
   Ridker PM, 1998, LANCET, V351, P88, DOI 10.1016/S0140-6736(97)09032-6
   Ridker PM, 2000, NEW ENGL J MED, V342, P836, DOI 10.1056/NEJM200003233421202
   Riikola A, 2009, ATHEROSCLEROSIS, V207, P466, DOI 10.1016/j.atherosclerosis.2009.06.004
   Schaefer TS, 1997, MOL CELL BIOL, V17, P5307, DOI 10.1128/MCB.17.9.5307
   SCHAEFER TS, 1995, P NATL ACAD SCI USA, V92, P9097, DOI 10.1073/pnas.92.20.9097
   Schönbeck U, 2001, CIRCULATION, V104, P2266, DOI 10.1161/hc4401.099447
   Smith E, 2010, CIRCULATION, V121, P1746, DOI 10.1161/CIRCULATIONAHA.109.924886
   Speidl WS, 2002, AM HEART J, V144, P449, DOI 10.1067/mhj.2002.124353
   Stewart FA, 2006, AM J PATHOL, V168, P649, DOI 10.2353/ajpath.2006.050409
   Taleb S, 2009, J EXP MED, V206, P2067, DOI 10.1084/jem.20090545
   TANGIRALA RK, 1995, J LIPID RES, V36, P2320
   van Es T, 2009, BIOCHEM BIOPH RES CO, V388, P261, DOI 10.1016/j.bbrc.2009.07.152
   Yang XO, 2008, IMMUNITY, V29, P44, DOI 10.1016/j.immuni.2008.05.007
   Yang XXO, 2007, J BIOL CHEM, V282, P9358, DOI 10.1074/jbc.C600321200
   Yoo JY, 2002, CELL, V108, P331, DOI 10.1016/S0092-8674(02)00636-0
   Zadelaar S, 2007, ARTERIOSCL THROM VAS, V27, P1706, DOI 10.1161/ATVBAHA.107.142570
   Zhou LA, 2007, NAT IMMUNOL, V8, P967, DOI 10.1038/ni1488
NR 53
TC 13
Z9 14
U1 0
U2 8
PU SPRINGER
PI NEW YORK
PA 233 SPRING ST, NEW YORK, NY 10013 USA
SN 0946-2716
J9 J MOL MED
JI J. Mol. Med.
PD AUG
PY 2013
VL 91
IS 8
BP 965
EP 976
DI 10.1007/s00109-013-1013-5
PG 12
WC Genetics & Heredity; Medicine, Research & Experimental
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity; Research & Experimental Medicine
GA 193SM
UT WOS:000322581800007
PM 23619910
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Falcione, S
   Kamtchum-Tatuene, J
   Sykes, G
   Jickling, GC
AF Falcione, Sarina
   Kamtchum-Tatuene, Joseph
   Sykes, Gina
   Jickling, Glen C.
TI RNA expression studies in stroke: what can they tell us about stroke
   mechanism?
SO CURRENT OPINION IN NEUROLOGY
LA English
DT Review
DE biomarker; gene expression; immune response; ischemic stroke; microRNA;
   RNA; stroke
ID LONG NONCODING RNAS; ISCHEMIC-STROKE; GENE-EXPRESSION; BLOOD;
   BIOMARKERS; PREDICTION; PROFILES; LACUNAR
AB Purpose of review Diagnosis of stroke and understanding the mechanism of stroke is critical to implement optimal treatment. RNA expressed in peripheral blood cells is emerging as a precision biomarker to aid in stroke diagnosis and prediction of stroke cause. In this review, we summarize available data regarding the role of RNA to predict stroke, the rationale for these changes, and a discussion of novel mechanistic insight and clinical applications. Recent findings Differences in RNA gene expression in blood have been identified in patients with stroke, including differences to distinguish ischemic from hemorrhagic stroke, and differences between cardioembolic, large vessel atherosclerotic, and small vessel lacunar stroke cause. Gene expression differences show promise as novel stroke biomarkers to predict stroke of unclear cause (cryptogenic stroke). The differences in RNA expression provide novel insight to stroke mechanism, including the role of immune response and thrombosis in human stroke. Important insight to regulation of gene expression in stroke and its causes are being acquired, including alternative splicing, noncoding RNA, and microRNA. Improved diagnosis of stroke and determination of stroke cause will improve stroke treatment and prevention. RNA biomarkers show promise to aid in the diagnosis of stroke and cause determination, as well as providing novel insight to mechanism of stroke in patients. While further study is required, an RNA profile may one day be part of the stroke armamentarium with utility to guide acute stroke therapy and prevention strategies and refine stroke phenotype.
C1 [Falcione, Sarina; Kamtchum-Tatuene, Joseph; Sykes, Gina; Jickling, Glen C.] Univ Alberta, Div Neurol, Dept Med, 114 St & 87 Ave, Edmonton, AB T6G 2E1, Canada.
C3 University of Alberta
RP Falcione, S (corresponding author), Univ Alberta, Div Neurol, Dept Med, 114 St & 87 Ave, Edmonton, AB T6G 2E1, Canada.
EM sfalcion@ualberta.ca
RI Jickling, Glen/J-8790-2019; KAMTCHUM TATUENE, Joseph/W-3028-2017
OI KAMTCHUM TATUENE, Joseph/0000-0002-1041-4202; Jickling,
   Glen/0000-0003-3543-0820
FU CIHR; NIH; Heart and Stroke Foundation of Canada; Hypertension Canada;
   CFI; UHF
FX G.J. receives research support to study RNA in stroke from CIHR, NIH,
   Heart and Stroke Foundation of Canada, Hypertension Canada, CFI, UHF.
CR Bao MH, 2018, CELL DEATH DIS, V9, DOI 10.1038/s41419-018-0282-x
   Barr TL, 2010, NEUROLOGY, V75, P1009, DOI 10.1212/WNL.0b013e3181f2b37f
   Dharap A, 2012, STROKE, V43, P2800, DOI 10.1161/STROKEAHA.112.669465
   Dykstra-Aiello C, 2016, STROKE, V47, P2896, DOI 10.1161/STROKEAHA.116.013869
   Dykstra-Aiello C, 2015, TRANSL STROKE RES, V6, P284, DOI 10.1007/s12975-015-0407-9
   Feigin VL, 2014, LANCET, V383, P245, DOI 10.1016/S0140-6736(13)61953-4
   Garcia-Berrocoso T, 2019, TRANSL STROKE RES
   Guo XJ, 2018, CELL PHYSIOL BIOCHEM, V50, P2157, DOI 10.1159/000495058
   Hansen TB, 2013, NATURE, V495, P384, DOI 10.1038/nature11993
   Hedhli N, 2014, CURR PHARM DESIGN, V20, P4899
   Huang YJ, 2019, FRONT NEUROL, V10, DOI [10.3389/fphar.2019.01225, 10.3389/fneur.2019.00032]
   Jickling GC, 2016, NEUROLOGY, V87, P2198, DOI 10.1212/WNL.0000000000003354
   Jickling GC, 2015, STROKE, V46, P915, DOI 10.1161/STROKEAHA.114.005604
   Jickling GC, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0099283
   Jickling GC, 2012, STROKE, V43, P2036, DOI 10.1161/STROKEAHA.111.648725
   Jickling GC, 2011, ANN NEUROL, V70, P477, DOI 10.1002/ana.22497
   Jickling GC, 2011, NEUROTHERAPEUTICS, V8, P349, DOI 10.1007/s13311-011-0050-4
   Jickling GC, 2010, ANN NEUROL, V68, P681, DOI 10.1002/ana.22187
   Kamel H, 2017, CIRC RES, V120, P514, DOI 10.1161/CIRCRESAHA.116.308407
   Kamtchum-Tatuene J, 2019, NEUROMOL MED, P1
   Kaur H, 2018, ANN NY ACAD SCI, V1421, P19, DOI 10.1111/nyas.13612
   Liu DZ, 2010, J CEREBR BLOOD F MET, V30, P92, DOI 10.1038/jcbfm.2009.186
   Lloyd-Jones D, 2009, CIRCULATION, V119, pE21, DOI 10.1161/CIRCULATIONAHA.108.191261
   Mick E, 2017, STROKE, V48, P828, DOI 10.1161/STROKEAHA.116.015140
   Mirzaei H., 2017, J CELLULAR PHYSL, V233, P856
   Montes M, 2019, TRENDS GENET, V35, P68, DOI 10.1016/j.tig.2018.10.002
   Moore DF, 2005, CIRCULATION, V111, P212, DOI 10.1161/01.CIR.0000152105.79665.C6
   Moreno-Ramírez CE, 2018, J STROKE CEREBROVASC, V27, P3336, DOI 10.1016/j.jstrokecerebrovasdis.2018.07.035
   O'Connell GC, 2019, TRANSL STROKE RES, V10, P26, DOI 10.1007/s12975-018-0623-1
   Ren WM, 2018, FRONT MOL NEUROSCI, V11, DOI 10.3389/fnmol.2018.00096
   Rennert RC, 2019, NEUROSURGERY, V85, pS4, DOI 10.1093/neuros/nyz042
   Stamova B, 2010, STROKE, V41, P2171, DOI 10.1161/STROKEAHA.110.588335
   Sun P, 2018, J CEREBR BLOOD F MET, V38, P1125, DOI 10.1177/0271678X18773871
   Tan JR, 2017, PLOS ONE, V12, DOI 10.1371/journal.pone.0172131
   Tang Y, 2006, J CEREBR BLOOD F MET, V26, P1089, DOI 10.1038/sj.jcbfm.9600264
   Tiedt S, 2017, CIRC RES, V121, P970, DOI 10.1161/CIRCRESAHA.117.311572
   Wang J, 2017, STROKE, V48, P2211, DOI 10.1161/STROKEAHA.117.017387
   Wang SW, 2018, CELL TRANSPLANT, V27, P1763, DOI 10.1177/0963689718806818
   Weimar C, 2016, CURR OPIN NEUROL, V29, P4, DOI 10.1097/WCO.0000000000000280
   Xiao X, 2018, MOL PSYCHIATR, V23, DOI 10.1038/mp.2017.243
   Xu WL, 2018, CELL TRANSPLANT, V27, P1778, DOI 10.1177/0963689718773361
   Zhang XJ, 2019, NEUROSCIENTIST, V25, P22, DOI 10.1177/1073858418769556
NR 42
TC 24
Z9 24
U1 0
U2 58
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA TWO COMMERCE SQ, 2001 MARKET ST, PHILADELPHIA, PA 19103 USA
SN 1350-7540
EI 1473-6551
J9 CURR OPIN NEUROL
JI Curr. Opin. Neurol.
PD FEB
PY 2020
VL 33
IS 1
BP 24
EP 29
DI 10.1097/WCO.0000000000000786
PG 6
WC Clinical Neurology; Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA LC0GM
UT WOS:000525009200005
PM 31809333
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Imanaka-Yoshida, K
   Hiroe, M
   Yasutomi, Y
   Toyozaki, T
   Tsuchiya, T
   Noda, N
   Maki, T
   Nishikawa, T
   Sakakura, T
   Yoshida, T
AF Imanaka-Yoshida, K
   Hiroe, M
   Yasutomi, Y
   Toyozaki, T
   Tsuchiya, T
   Noda, N
   Maki, T
   Nishikawa, T
   Sakakura, T
   Yoshida, T
TI Tenascin-C is a useful marker for disease activity in myocarditis
SO JOURNAL OF PATHOLOGY
LA English
DT Article
DE tenascin-C; extracellular matrix; myocarditis; mouse; autoimmune
ID DILATED CARDIOMYOPATHY; EXPRESSION; CYTOKINES
AB Tenascin-C (TNC) is an extracellular matrix protein which appears at active sites of tissue remodelling during embryogenesis or cancer invasion. In normal heart, TNC is only present during the early stages of development but reappears in pathological states. This study examined the diagnostic value of TNC for assessing disease activity of myocarditis. Expression of TNC was examined in myosin-induced autoimmune myocarditis mouse models. Sequential changes in amount, localization and the producing cells were analysed by reverse transcriptase-polymerase chain reaction, western blotting. immunohistochemistry and in situ hybridization and compared with the histological picture. The expression of TNC was upregulated at a very early stage of myocarditis. Immunostaining was detectable before cell infiltration and myocytolysis became histologically apparent, remained during the active stage while cell infiltration and necrosis continued, and disappeared in sear tissue with healing. TNC immunostaining was always observed at the periphery of necrotic or degenerating cardiomyocytes in foci of inflammation, the expression level correlating with histological evidence of inflammatory activity. Interstitial fibroblasts were the major source of TNC, expressing the large isoform containing alternative splicing sites. These data demonstrate that TNC is a useful marker for evaluation of disease activity in myocarditis. Copyright (C) 2002 John Wiley Sons, Ltd.
C1 Mie Univ, Sch Med, Dept Pathol, Tsu, Mie 5148507, Japan.
   Int Med Ctr Japan, Dept Nephrol & Cardiol, Tokyo, Japan.
   Mie Univ, Sch Med, Dept Bioregulat, Tsu, Mie, Japan.
   Chiba Univ, Sch Med, Inst Pulm Canc Res, Div Pathol, Chiba 280, Japan.
   Tokyo Womens Med Univ, Dept Pathol, Tokyo, Japan.
C3 Mie University; National Center for Global Health & Medicine - Japan;
   Mie University; Chiba University; Tokyo Women's Medical University
RP Mie Univ, Sch Med, Dept Pathol, 2-174 Edobashi, Tsu, Mie 5148507, Japan.
EM imanaka@doc.medic.rme-u.ac.jp
RI Yoshida, Toshimichi/H-6204-2013
OI Yoshida, Toshimichi/0000-0001-8935-8217
CR ABELMANN WH, 1989, J AM COLL CARDIOL, V13, P1219, DOI 10.1016/0735-1097(89)90293-3
   Aretz T., 1986, Am J Cardiovasc Pathol, V1, P3
   Badorff C, 1997, J AM COLL CARDIOL, V29, P429, DOI 10.1016/S0735-1097(96)00475-5
   CHIQUETEHRISMANN R, 1988, CELL, V53, P383, DOI 10.1016/0092-8674(88)90158-4
   DEE GW, 1985, NEW ENGL J MED, V312, P885
   Erickson HP, 1993, CURR OPIN CELL BIOL, V5, P869, DOI 10.1016/0955-0674(93)90037-Q
   Felker GM, 1999, MEDICINE, V78, P270, DOI 10.1097/00005792-199907000-00005
   FENOGLIO JJ, 1983, NEW ENGL J MED, V308, P12, DOI 10.1056/NEJM198301063080103
   Imanaka-Yoshida K, 2001, VIRCHOWS ARCH, V439, P185, DOI 10.1007/s004280000390
   Imanaka-Yoshida K, 2001, LAB INVEST, V81, P1015, DOI 10.1038/labinvest.3780313
   IMANANAKYOSHIDA K, 2000, ETIOLOGY MORPHOGENES, P185
   KaarteenahoWiik R, 1996, AM J RESP CRIT CARE, V154, P511, DOI 10.1164/ajrccm.154.2.8756830
   Kuhl U, 1996, HEART, V75, P295, DOI 10.1136/hrt.75.3.295
   Latijnhouwers MAHE, 1998, ACTA DERM-VENEREOL, V78, P331
   Masaki T, 1998, CLIN NEPHROL, V50, P205
   Matsumori A, 1997, JPN CIRC J, V61, P275, DOI 10.1253/jcj.61.275
   Namba T, 1997, CIRCULATION, V95, P2448, DOI 10.1161/01.CIR.95.10.2448
   NEU N, 1987, J IMMUNOL, V139, P3630
   Noda N, 2000, BIOL REPROD, V63, P1713, DOI 10.1095/biolreprod63.6.1713
   Noutsias M, 1999, CIRCULATION, V99, P2124, DOI 10.1161/01.CIR.99.16.2124
   RETTIG WJ, 1994, J CELL SCI, V107, P487
   Rose NR, 1996, INT J CARDIOL, V54, P171, DOI 10.1016/0167-5273(96)02595-8
   SAGA Y, 1992, GENE DEV, V6, P1821, DOI 10.1101/gad.6.10.1821
   Straub V, 1997, J CELL BIOL, V139, P375, DOI 10.1083/jcb.139.2.375
   Tamura A, 1996, HEART, V75, P291, DOI 10.1136/hrt.75.3.291
   Willems IEMG, 1996, J PATHOL, V179, P321
   YAMADA S, 1992, LIVER, V12, P10
   Yoshimura E, 1999, HISTOCHEM CELL BIOL, V111, P259, DOI 10.1007/s004180050356
NR 28
TC 115
Z9 118
U1 0
U2 6
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0022-3417
EI 1096-9896
J9 J PATHOL
JI J. Pathol.
PD JUL
PY 2002
VL 197
IS 3
BP 388
EP 394
DI 10.1002/path.1131
PG 7
WC Oncology; Pathology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Oncology; Pathology
GA 573ZV
UT WOS:000176864600016
PM 12115886
DA 2025-04-10
ER

PT J
AU Liao, P
   Soong, TW
AF Liao, Ping
   Soong, Tuck Wah
TI CaV1.2 channelopathies: from arrhythmias to autism, bipolar
   disorder, and immunodeficiency
SO PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY
LA English
DT Article
DE Ca2+ channels; Immune response; Electrophysiology; Arrhythmia; Central
   nervous system
ID GATED CALCIUM-CHANNELS; TIMOTHY-SYNDROME MUTATION; CA2+ CHANNELS;
   DEPENDENT INACTIVATION; CONDITIONED FEAR; GENE-EXPRESSION; C-TERMINUS;
   VOLTAGE; SUBUNIT; MUSCLE
AB Mutations of human Ca(V)1.2 channel gene were identified only recently. The gain-of-function mutations were found at two mutually exclusive exons in patients with Timothy syndrome (TS). These patients exhibit prolonged QT interval and lethal cardiac arrhythmias. In contrast, the loss-of-function mutations of Ca(V)1.2 channel in patients with Brugada syndrome produce short QT interval that could result in sudden cardiac death. TS patients also suffer from multi-organ dysfunction that includes neurological disorder such as autism and mental retardation reflecting the wide tissue distribution of Ca(V)1.2 channel. Mutations found on different mutually exclusive exons determine the severity of the disease. Unexpectedly, TS patients may develop recurrent infections and bronchitis that suggests a role of Ca(V)1.2 channel in the immune system. Furthermore, recent reports revealed a linkage of Ca(V)1.2 channel polymorphism with multiple central nervous system disorders including bipolar disorder, depression, and schizophrenia. Here, we will discuss how alternative splicing modulates Ca(V)1.2 channelopathy and the role of Ca(V)1.2 channel in both excitable and non-excitable tissues.
C1 [Liao, Ping; Soong, Tuck Wah] Natl Inst Neurosci, Singapore 308433, Singapore.
   [Soong, Tuck Wah] Natl Univ Singapore, Yong Loo Lin Sch Med, Dept Physiol, Singapore 117597, Singapore.
C3 National Neuroscience Institute (NNI); National University of Singapore
RP Liao, P (corresponding author), Natl Inst Neurosci, 11 Jalan Tan Tock Seng, Singapore 308433, Singapore.
EM Ping_LIAO@nni.com.sg
RI Liao, Ping/LBI-1504-2024
OI Liao, Ping/0000-0002-6205-4042
FU National Medical Research Council; Biomedical Research Council of
   Singapore
FX This work was supported by grants from National Medical Research Council
   and Biomedical Research Council of Singapore.
CR Abernethy DR, 2002, J PHARMACOL EXP THER, V300, P724, DOI 10.1124/jpet.300.3.724
   Abrahams BS, 2008, NAT REV GENET, V9, P341, DOI 10.1038/nrg2346
   Adams B, 1997, J GEN PHYSIOL, V110, P379, DOI 10.1085/jgp.110.4.379
   Antzelevitch C, 2007, CIRCULATION, V115, P442, DOI 10.1161/CIRCULATIONAHA.106.668392
   Barrett CF, 2008, P NATL ACAD SCI USA, V105, P2157, DOI 10.1073/pnas.0710501105
   Busquet P, 2008, LEARN MEMORY, V15, P378, DOI 10.1101/lm.886208
   Cens T, 1999, J BIOL CHEM, V274, P5483, DOI 10.1074/jbc.274.9.5483
   Chen XG, 2007, J COSMOL ASTROPART P, DOI 10.1088/1475-7516/2007/01/002
   Das R, 2009, CIRC RES, V105, P167, DOI 10.1161/CIRCRESAHA.109.200311
   Erxleben C, 2006, P NATL ACAD SCI USA, V103, P3932, DOI 10.1073/pnas.0511322103
   Ferreira MAR, 2008, NAT GENET, V40, P1056, DOI 10.1038/ng.209
   GIDHJAIN M, 1995, BIOCHEM BIOPH RES CO, V216, P892, DOI 10.1006/bbrc.1995.2705
   Gomez-Ospina N, 2006, CELL, V127, P591, DOI 10.1016/j.cell.2006.10.017
   Green EK, 2010, MOL PSYCHIATR, V15, P1016, DOI 10.1038/mp.2009.49
   Gupta S, 2009, PLOS ONE, V4, DOI 10.1371/journal.pone.0005305
   HALLING DB, 2006, SCI STKE, pER1, DOI DOI 10.1126/STKE.3152005RE15
   Jacobs A, 2006, HEART RHYTHM, V3, P967, DOI 10.1016/j.hrthm.2006.04.024
   Kim J, 2004, NEURON, V41, P745, DOI 10.1016/S0896-6273(04)00081-9
   Krug A, 2010, NEUROIMAGE, V49, P1831, DOI 10.1016/j.neuroimage.2009.09.028
   Liao P, 2005, CARDIOVASC RES, V68, P197, DOI 10.1016/j.cardiores.2005.06.024
   Liao P, 2004, J BIOL CHEM, V279, P50329, DOI 10.1074/jbc.M409436200
   Liao P, 2007, J BIOL CHEM, V282, P35133, DOI 10.1074/jbc.M705478200
   Liao P, 2009, PFLUG ARCH EUR J PHY, V458, P701, DOI 10.1007/s00424-009-0652-4
   Liao P, 2009, PFLUG ARCH EUR J PHY, V458, P481, DOI 10.1007/s00424-009-0635-5
   MARKS ML, 1995, J AM COLL CARDIOL, V25, P59, DOI 10.1016/0735-1097(94)00318-K
   MARKS ML, 1995, AM J CARDIOL, V76, P744, DOI 10.1016/S0002-9149(99)80216-1
   Matza D, 2009, IMMUNOL REV, V231, P257, DOI 10.1111/j.1600-065X.2009.00805.x
   McKinney BC, 2008, LEARN MEMORY, V15, P326, DOI 10.1101/lm.893808
   McQuillin A, 2007, PHARMACOGENET GENOM, V17, P605, DOI 10.1097/FPC.0b013e328011b5b2
   Reichenbach H, 1992, Kinderarztl Prax, V60, P54
   Schroder E, 2009, CIRC RES, V104, P1373, DOI 10.1161/CIRCRESAHA.108.191387
   Seisenberger C, 2000, J BIOL CHEM, V275, P39193, DOI 10.1074/jbc.M006467200
   Sicouri S, 2007, HEART RHYTHM, V4, P638, DOI 10.1016/j.hrthm.2006.12.046
   Sinnegger-Brauns MJ, 2004, J CLIN INVEST, V113, P1430, DOI 10.1172/JCI200420208
   Sklar P, 2008, MOL PSYCHIATR, V13, P558, DOI 10.1038/sj.mp.4002151
   Splawski I, 2004, CELL, V119, P19, DOI 10.1016/j.cell.2004.09.011
   Splawski I, 2005, P NATL ACAD SCI USA, V102, P8089, DOI 10.1073/pnas.0502506102
   Stotz SC, 2000, J BIOL CHEM, V275, P24575, DOI 10.1074/jbc.M000399200
   Tang ZZ, 2008, BBA-MOL CELL RES, V1783, P118, DOI 10.1016/j.bbamcr.2007.11.003
   Tang ZZ, 2007, CELL CALCIUM, V41, P417, DOI 10.1016/j.ceca.2006.08.002
   Tang ZZ, 2004, J BIOL CHEM, V279, P44335, DOI 10.1074/jbc.M407023200
   Thiel WH, 2008, CIRCULATION, V118, P2225, DOI 10.1161/CIRCULATIONAHA.108.788067
   Tiwari S, 2006, P NATL ACAD SCI USA, V103, P17024, DOI 10.1073/pnas.0606539103
   Wang K, 2009, NATURE, V459, P528, DOI 10.1038/nature07999
   Welling A, 1997, CIRC RES, V81, P526, DOI 10.1161/01.RES.81.4.526
   White JA, 2008, LEARN MEMORY, V15, P1, DOI 10.1101/lm.773208
   Yang YB, 2000, J MOL CELL CARDIOL, V32, P973, DOI 10.1006/jmcc.2000.1138
   Yarotskyy V, 2009, J PHYSIOL-LONDON, V587, P551, DOI 10.1113/jphysiol.2008.161737
NR 48
TC 70
Z9 88
U1 0
U2 24
PU SPRINGER
PI NEW YORK
PA 233 SPRING ST, NEW YORK, NY 10013 USA
SN 0031-6768
J9 PFLUG ARCH EUR J PHY
JI Pflugers Arch.
PD JUL
PY 2010
VL 460
IS 2
BP 353
EP 359
DI 10.1007/s00424-009-0753-0
PG 7
WC Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Physiology
GA 609YH
UT WOS:000278694200012
PM 19916019
DA 2025-04-10
ER

PT J
AU Kim, MS
   Merlo, X
   Wilson, C
   Lough, J
AF Kim, Min-Su
   Merlo, Xanthi
   Wilson, Catherine
   Lough, John
TI Co-activation of atrial natriuretic factor promoter by Tip60 and serum
   response factor
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID HISTONE-ACETYLTRANSFERASE ACTIVITY; INTERACTIVE PROTEIN TIP60;
   GENE-EXPRESSION; RECEPTOR COACTIVATOR; ANDROGEN RECEPTOR; TAT;
   IDENTIFICATION; ACETYLATION; ACTIVATION; COMPLEX
AB Tat-interactive protein 60 (Tip60) is a member of the MYST family of histone acetyltransferases (HATs). In addition to its HAT domain, Tip contains a heterochromatin-associated protein 1-like chromodomain and a zinc finger-like domain. Several alternative splice variants of Tip60 have been characterized, including full-length Tip60 alpha, Tip60 beta (which lacks exon V encoded by the Tip60 gene), and Tip55 ( which encodes a novel 103-amino-acid C terminus). We report here that isoproteins recognized by a pan-Tip60 antibody are strongly and transiently expressed between embryonic days 8 and 11 in the embryonic mouse myocardium. A functional role for Tip60 isoproteins in cardiac myocyte differentiation is suggested by immunoprecipitation experiments showing that Tip60 alpha, Tip60 alpha, and Tip55 can bind serum response factor (SRF) and by transient transfection assessments showing that Tip60 and SRF cooperatively activate the atrial natriuretic factor promoter. Although this combinatorial activity is inhibited by histone deacetylase 7, it was unexpectedly enhanced by point mutation of the HAT domain. Ablation of the chromodomain from Tip60 beta caused derepression. These findings suggest that Tip60 modulates expression of SRF-dependent cardiac genes.
C1 Med Coll Wisconsin, Dept Cell Biol Neurobiol & Anat, Milwaukee, WI 53226 USA.
   Med Coll Wisconsin, Ctr Cardiovasc, Milwaukee, WI 53226 USA.
C3 Medical College of Wisconsin; Medical College of Wisconsin
RP Lough, J (corresponding author), Med Coll Wisconsin, Dept Cell Biol Neurobiol & Anat, 8701 Watertown Plank Rd, Milwaukee, WI 53226 USA.
EM jlough@mcw.edu
RI Kim, Chang/H-4759-2011; Wilson, Catherine/JWB-0289-2024
CR Barron MR, 2005, J BIOL CHEM, V280, P11816, DOI 10.1074/jbc.M412408200
   Belaguli NS, 2000, MOL CELL BIOL, V20, P7550, DOI 10.1128/MCB.20.20.7550-7558.2000
   Brady ME, 1999, J BIOL CHEM, V274, P17599, DOI 10.1074/jbc.274.25.17599
   Cao XW, 2001, SCIENCE, V293, P115, DOI 10.1126/science.1058783
   Chen CY, 1996, MOL CELL BIOL, V16, P6372
   Chen HW, 1999, CELL, V98, P675, DOI 10.1016/S0092-8674(00)80054-9
   Creaven M, 1999, BIOCHEMISTRY-US, V38, P8826, DOI 10.1021/bi9907274
   Gaughan L, 2002, J BIOL CHEM, V277, P25904, DOI 10.1074/jbc.M203423200
   Gavaravarapu S, 2000, BIOCHEM BIOPH RES CO, V269, P758, DOI 10.1006/bbrc.2000.2358
   Halkidou K, 2003, ONCOGENE, V22, P2466, DOI 10.1038/sj.onc.1206342
   Hass MR, 2005, J BIOL CHEM, V280, P36895, DOI 10.1074/jbc.M502861200
   Hecht A, 2000, EMBO J, V19, P1839, DOI 10.1093/emboj/19.8.1839
   Hlubek F, 2001, J BIOCHEM-TOKYO, V129, P635, DOI 10.1093/oxfordjournals.jbchem.a002901
   Houweling AC, 2002, ANAT RECORD, V266, P93, DOI 10.1002/ar.10042
   Ikura T, 2000, CELL, V102, P463, DOI 10.1016/S0092-8674(00)00051-9
   Jacobs SA, 2002, SCIENCE, V295, P2080, DOI 10.1126/science.1069473
   Jones DO, 2000, BIOESSAYS, V22, P124, DOI 10.1002/(SICI)1521-1878(200002)22:2<124::AID-BIES4>3.0.CO;2-E
   Kamine J, 1996, VIROLOGY, V216, P357, DOI 10.1006/viro.1996.0071
   Kao HY, 2000, GENE DEV, V14, P55
   Kioussi C, 2002, CELL, V111, P673, DOI 10.1016/S0092-8674(02)01084-X
   Kusch T, 2004, SCIENCE, V306, P2084, DOI 10.1126/science.1103455
   Lee HJ, 2001, J BIOL CHEM, V276, P16597, DOI 10.1074/jbc.C000909200
   Lough JW, 2002, DEV DYNAM, V223, P419, DOI 10.1002/dvdy.10058
   McAllister D, 2002, GENE, V289, P169, DOI 10.1016/S0378-1119(02)00546-2
   Morin S, 2001, MOL CELL BIOL, V21, P1036, DOI 10.1128/MCB.21.4.1036-1044.2001
   Ran QT, 2000, GENE, V258, P141, DOI 10.1016/S0378-1119(00)00410-8
   SEIDMAN CE, 1988, P NATL ACAD SCI USA, V85, P4104, DOI 10.1073/pnas.85.11.4104
   Sheridan AM, 2001, MOL CELL BIOL, V21, P4470, DOI 10.1128/MCB.21.14.4470-4481.2001
   Sliva D, 1999, BIOCHEM BIOPH RES CO, V263, P149, DOI 10.1006/bbrc.1999.1083
   Wang DZ, 2001, CELL, V105, P851, DOI 10.1016/S0092-8674(01)00404-4
   Xiao H, 2003, J BIOL CHEM, V278, P11197, DOI 10.1074/jbc.M210816200
   Yamamoto T, 1997, J BIOL CHEM, V272, P30595, DOI 10.1074/jbc.272.49.30595
NR 32
TC 14
Z9 16
U1 0
U2 4
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD JUN 2
PY 2006
VL 281
IS 22
BP 15082
EP 15089
DI 10.1074/jbc.M513593200
PG 8
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 048BI
UT WOS:000237922200010
PM 16597624
OA hybrid
DA 2025-04-10
ER

PT J
AU Hong, CS
   Kwak, YG
   Ji, JH
   Chae, SW
   Kim, DH
AF Hong, CS
   Kwak, YG
   Ji, JH
   Chae, SW
   Kim, DH
TI Molecular cloning and characterization of mouse cardiac junctate
   Isoforms
SO BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
LA English
DT Article
ID JUNCTIONAL SARCOPLASMIC-RETICULUM; SLOW CALCIUM CURRENT;
   SKELETAL-MUSCLE; RYANODINE RECEPTOR; CA2+ RELEASE; COMPLEMENTARY-DNA;
   CALSEQUESTRIN; PURIFICATION; TRIADIN; BINDING
AB Junctate is a newly identified integral ER/SR membrane calcium binding protein, which is an alternative splicing form of the same gene generating aspartyl beta-hydroxylase and junctin. Screening a mouse heart cDNA library using canine junctin cDNA as a probe yielded three complete mouse heart cDNAs. One of the cDNAs is homologous to the previously reported human junctate. The three mouse junctate proteins are composed of 270, 259, and 215 amino acids (we named them junctate-1, -2, and -3). The apparent molecular masses of the mouse junctates in SDS-PAGE were in the range between 40 and 53 kDa. Northern and Western blot analyses indicate that mouse junctates are expressed in heart, brain, spleen, lung, liver, kidney, and stomach, but not in skeletal muscle. The apparent molecular weights of junctates from heart and brain were somewhat different from those from the other tissues tested, suggesting that there are tissue-specific expression patterns of the different junctate isoforms. Immunohistochemical studies showed that junctates were expressed both in ventricular and atrial tissues. This is the first study that shows the presence of 3 distinct cardiac junctate isoforms expressed in various mammalian tissues. (C) 2001 Elsevier Science.
C1 Kwangju Inst Sci & Technol, Dept Life Sci, Kwangju 500712, South Korea.
   Chonbuk Natl Univ, Sch Med, Dept Pharmacol, Chonju 561182, South Korea.
C3 Gwangju Institute of Science & Technology (GIST); Jeonbuk National
   University
RP Kwangju Inst Sci & Technol, Dept Life Sci, 1 Oryong Dong, Kwangju 500712, South Korea.
EM dhkim@kjist.ac.kr
CR ANDERSON K, 1995, J GEN PHYSIOL, V105, P363, DOI 10.1085/jgp.105.3.363
   BEAM KG, 1986, NATURE, V320, P168, DOI 10.1038/320168a0
   BLOCK BA, 1988, J CELL BIOL, V107, P2587, DOI 10.1083/jcb.107.6.2587
   BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
   CAMPBELL KP, 1983, J BIOL CHEM, V258, P1197
   Dinchuk JE, 2000, J BIOL CHEM, V275, P39543, DOI 10.1074/jbc.M006753200
   Donoso P, 1996, BIOCHEMISTRY-US, V35, P13419, DOI 10.1021/bi9616209
   FLEISCHER S, 1989, ANNU REV BIOPHYS BIO, V18, P333, DOI 10.1146/annurev.bb.18.060189.002001
   FRANZINIARMSTRONG C, 1994, ANNU REV PHYSIOL, V56, P509, DOI 10.1146/annurev.ph.56.030194.002453
   Guo W, 1996, J BIOL CHEM, V271, P458, DOI 10.1074/jbc.271.1.458
   GUO W, 1995, J BIOL CHEM, V270, P9027, DOI 10.1074/jbc.270.16.9027
   HSU SM, 1981, J HISTOCHEM CYTOCHEM, V29, P1349, DOI 10.1177/29.11.6172466
   INUI M, 1987, J BIOL CHEM, V262, P1740
   Jones LR, 1995, J BIOL CHEM, V270, P30787, DOI 10.1074/jbc.270.51.30787
   KIM DH, 1994, J MOL CELL CARDIOL, V26, P1505, DOI 10.1006/jmcc.1994.1169
   LAEMMLI UK, 1970, NATURE, V227, P680, DOI 10.1038/227680a0
   Lee HG, 2001, J BIOL CHEM, V276, P39533, DOI 10.1074/jbc.M010664200
   Lim KY, 2000, GENE, V255, P35, DOI 10.1016/S0378-1119(00)00299-7
   MACLENNAN DH, 1985, NATURE, V316, P696, DOI 10.1038/316696a0
   MEISSNER G, 1994, ANNU REV PHYSIOL, V56, P485, DOI 10.1146/annurev.ph.56.030194.002413
   Palermo J, 1996, CIRC RES, V78, P504, DOI 10.1161/01.RES.78.3.504
   RIOS E, 1987, NATURE, V325, P717, DOI 10.1038/325717a0
   RIOS E, 1991, PHYSIOL REV, V71, P849, DOI 10.1152/physrev.1991.71.3.849
   TANABE T, 1988, NATURE, V336, P134, DOI 10.1038/336134a0
   Treves S, 2000, J BIOL CHEM, V275, P39555, DOI 10.1074/jbc.M005473200
   YANO K, 1994, MOL CELL BIOCHEM, V135, P61, DOI 10.1007/BF00925961
   Zhang L, 1997, J BIOL CHEM, V272, P23389, DOI 10.1074/jbc.272.37.23389
NR 27
TC 20
Z9 22
U1 0
U2 3
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0006-291X
EI 1090-2104
J9 BIOCHEM BIOPH RES CO
JI Biochem. Biophys. Res. Commun.
PD DEC 14
PY 2001
VL 289
IS 4
BP 882
EP 887
DI 10.1006/bbrc.2001.6056
PG 6
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA 510MQ
UT WOS:000173212200018
PM 11735129
DA 2025-04-10
ER

PT J
AU Chen, J
   Liu, HF
   Qiao, LB
   Wang, FB
   Wang, L
   Lin, Y
   Liu, J
AF Chen, Juan
   Liu, Hui-fang
   Qiao, Li-bo
   Wang, Fang-bin
   Wang, Lu
   Lin, Yan
   Liu, Jian
TI Global RNA editing identification and characterization during human
   pluripotent-to-cardiomyocyte differentiation
SO MOLECULAR THERAPY NUCLEIC ACIDS
LA English
DT Article
ID COMPREHENSIVE ANALYSIS; CIRCULAR RNA; EXPRESSION; DATABASE; INVASION;
   MUTATION; TECRL
AB RNA editing is widely involved in stem cell differentiation and development; however, RNA editing events during human cardiomyocyte differentiation have not yet been characterized and elucidated. Here, we identified genome-wide RNA editing sites and systemically characterized their genomic distribution during four stages of human cardiomyocyte differentiation. It was found that the expression level of ADAR1 affected the global number of adenosine to inosine (A-to-I) editing sites but not the editing degree. Next, we identified 43, 163, 544, and 141 RNA editing sites that contribute to changes in amino acid sequences, variation in alternative splicing, alterations in miRNA-target binding, and changes in gene expression, respectively. Generally, RNA editing showed a stage-specific pattern with 211 stage-shared editing sites. Interestingly, cardiac muscle contraction and heart-disease-related pathways were enriched by cardio-specific editing genes, emphasizing the connection between cardiomyocyte differentiation and heart diseases from the perspective of RNA editing. Finally, it was found that these RNA editing sites are also related to our study provides a new perspective on cardiomyocyte differentiation and offers more opportunities to understand the mechanisms underlying cell fate determination, which can promote the development of cardiac regenerative medicine and therapies for human heart diseases.
C1 [Chen, Juan; Qiao, Li-bo; Wang, Fang-bin; Wang, Lu; Lin, Yan; Liu, Jian] Hefei Univ Technol, Sch Food & Biol Engn, Hefei 230009, Anhui, Peoples R China.
   [Liu, Hui-fang] Huazhong Univ Sci & Technol, Cent Hosp Wuhan, Tongji Med Coll, Dept Endocrinol, Wuhan 430014, Hubei, Peoples R China.
   [Liu, Jian] Hefei Univ Technol, Engn Res Ctr Bioproc, Minist Educ, Hefei 230009, Anhui, Peoples R China.
C3 Hefei University of Technology; Huazhong University of Science &
   Technology; Hefei University of Technology
RP Chen, J; Liu, J (corresponding author), Hefei Univ Technol, Sch Food & Biol Engn, Hefei 230009, Anhui, Peoples R China.
EM chenjuan901105@hfut.edu.cn; liujian509@hfut.edu.cn
OI qiao, li bo/0000-0001-7633-4398; Chen, Juan/0009-0000-3141-8491; Juan,
   Chen/0000-0002-7959-335X
FU National Natural Science Foundation of China [31801114, 32070757,
   31671485, 11804072]; Natural Science Foundation of Anhui Province
   [1908085QC98]; University Syn-ergy Innovation Program of Anhui Province
   [GXXT-2019-026]
FX This work was supported by the National Natural Science Foundation of
   China (grant nos. 31801114 to J.C., 32070757 and 31671485 to J.L.,and
   11804072 to F.-b.W.) , the Natural Science Foundation of Anhui Province
   (grant no. 1908085QC98 to J.C.) , and the University Syn-ergy Innovation
   Program of Anhui Province (grant no. GXXT-2019-026 to J.L.) .
CR [Anonymous], 2012, Nature, DOI DOI 10.1038/nature11632
   Auwera G A., 2013, Curr. Protoc. Bioinforma., V43
   Berna MJ, 2007, ANAL CHEM, V79, P4199, DOI 10.1021/ac070051f
   Borik S, 2011, INTENS CARE MED, V37, P1664, DOI 10.1007/s00134-011-2296-z
   Chen CX, 2000, RNA, V6, P755, DOI 10.1017/S1355838200000170
   Chen J, 2020, FRONT ONCOL, V10, DOI 10.3389/fonc.2020.00037
   Chen LL, 2013, NAT MED, V19, P209, DOI 10.1038/nm.3043
   Chong JJH, 2014, NATURE, V510, P273, DOI 10.1038/nature13233
   Devalla HD, 2016, EMBO MOL MED, V8, P1390, DOI 10.15252/emmm.201505719
   el Azzouzi H, 2020, FRONT CARDIOVASC MED, V7, DOI 10.3389/fcvm.2020.00030
   Enright AJ, 2004, GENOME BIOL, V5
   Frankish A, 2019, NUCLEIC ACIDS RES, V47, pD766, DOI 10.1093/nar/gky955
   Fu L, 2017, P NATL ACAD SCI USA, V114, pE4631, DOI 10.1073/pnas.1703178114
   Gao C, 2020, PHYSIOL REV, V100, P673, DOI 10.1152/physrev.00007.2019
   Gong J, 2014, RNA BIOL, V11, P1375, DOI 10.1080/15476286.2014.996465
   Griffiths-Jones S, 2008, NUCLEIC ACIDS RES, V36, pD154, DOI 10.1093/nar/gkm952
   Han L, 2015, CANCER CELL, V28, DOI 10.1016/j.ccell.2015.08.013
   Han SW, 2014, J EXP MED, V211, P613, DOI 10.1084/jem.20132209
   Higuchi M, 2000, NATURE, V406, P78, DOI 10.1038/35017558
   Hwang T, 2016, NAT NEUROSCI, V19, P1093, DOI 10.1038/nn.4337
   Kadota S, 2020, J CARDIOL, V76, P459, DOI 10.1016/j.jjcc.2020.03.013
   Kitani T, 2020, CIRC RES, V126, P923, DOI 10.1161/CIRCRESAHA.119.315653
   Kuhn RM, 2013, BRIEF BIOINFORM, V14, P144, DOI 10.1093/bib/bbs038
   Li D, 2019, MITOCHONDRION, V46, P313, DOI 10.1016/j.mito.2018.08.005
   Li H, 2009, BIOINFORMATICS, V25, P1754, DOI [10.1093/bioinformatics/btp698, 10.1093/bioinformatics/btp324, 10.1093/bioinformatics/btp352]
   Li SS, 2018, STEM CELL REP, V10, P808, DOI 10.1016/j.stemcr.2018.01.013
   Li Y, 2020, NAT COMMUN, V11, DOI 10.1038/s41467-020-14802-2
   Li YS, 2019, MOL CANCER, V18, DOI 10.1186/s12943-019-1066-3
   Li YS, 2019, HEPATOLOGY, V70, P532, DOI 10.1002/hep.30242
   Li YS, 2018, TRENDS BIOCHEM SCI, V43, P576, DOI 10.1016/j.tibs.2018.05.002
   Li YS, 2017, EBIOMEDICINE, V24, P137, DOI 10.1016/j.ebiom.2017.09.015
   Liberzon A, 2014, METHODS MOL BIOL, V1150, P153, DOI 10.1007/978-1-4939-0512-6_9
   Lin ZH, 2021, J CELL MOL MED, V25, P2572, DOI 10.1111/jcmm.16251
   Long YD, 2020, J CELL MOL MED, V24, P7115, DOI 10.1111/jcmm.15073
   Moore JB, 2020, CIRC RES, V127, P550, DOI 10.1161/CIRCRESAHA.120.316932
   Nishikura K, 2010, ANNU REV BIOCHEM, V79, P321, DOI 10.1146/annurev-biochem-060208-105251
   Pan GJ, 2007, CELL RES, V17, P42, DOI 10.1038/sj.cr.7310125
   Peng ZY, 2012, NAT BIOTECHNOL, V30, P253, DOI 10.1038/nbt.2122
   Perry MD, 2016, EMBO MOL MED, V8, P1364, DOI 10.15252/emmm.201606967
   Pertea M, 2015, NAT BIOTECHNOL, V33, P290, DOI 10.1038/nbt.3122
   Qiu S, 2016, BMC GENOMICS, V17, DOI 10.1186/s12864-016-3115-2
   Quinlan AR, 2010, BIOINFORMATICS, V26, P841, DOI 10.1093/bioinformatics/btq033
   Ramaswami G, 2014, NUCLEIC ACIDS RES, V42, pD109, DOI 10.1093/nar/gkt996
   Rossetti C, 2017, LEUKEMIA, V31, P2824, DOI 10.1038/leu.2017.134
   Rueter SM, 1999, NATURE, V399, P75, DOI 10.1038/19992
   Sagredo EA, 2018, BIOL RES, V51, DOI 10.1186/s40659-018-0185-4
   She L, 2019, CARDIOVASC DRUG THER, V33, P13, DOI 10.1007/s10557-018-06848-8
   Sherry ST, 2001, NUCLEIC ACIDS RES, V29, P308, DOI 10.1093/nar/29.1.308
   Shtrichman R, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0041576
   Stellos K, 2016, NAT MED, V22, P1140, DOI 10.1038/nm.4172
   Szabo L, 2015, GENOME BIOL, V16, DOI [10.1186/s13059-015-0690-5, 10.1186/s13059-016-1123-9]
   Tan FL, 2002, P NATL ACAD SCI USA, V99, P11387, DOI 10.1073/pnas.162370099
   Uchida S, 2018, CIRC RES, V122, P399, DOI 10.1161/CIRCRESAHA.117.312512
   Wahlstedt H, 2009, GENOME RES, V19, P978, DOI 10.1101/gr.089409.108
   Wang K, 2010, NUCLEIC ACIDS RES, V38, DOI 10.1093/nar/gkq603
   Wang QD, 2004, J BIOL CHEM, V279, P4952, DOI 10.1074/jbc.M310162200
   Yao YC, 2012, BLOOD, V119, P5037, DOI 10.1182/blood-2011-10-385906
   Yu Y, 2016, PLOS GENET, V12, DOI 10.1371/journal.pgen.1006191
   Zaidan H, 2018, BMC GENOMICS, V19, DOI 10.1186/s12864-017-4409-8
   Zhao XL, 2020, J CELL MOL MED, V24, P9898, DOI 10.1111/jcmm.15584
   Zhu H, 2021, REDOX BIOL, V38, DOI 10.1016/j.redox.2020.101777
NR 61
TC 9
Z9 10
U1 1
U2 8
PU CELL PRESS
PI CAMBRIDGE
PA 50 HAMPSHIRE ST, FLOOR 5, CAMBRIDGE, MA 02139 USA
SN 2162-2531
J9 MOL THER NUCL ACIDS
JI Mol. Ther. Nucl. Acids
PD DEC 3
PY 2021
VL 26
BP 879
EP 891
DI 10.1016/j.omtn.2021.10.001
EA OCT 2021
PG 13
WC Medicine, Research & Experimental
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Research & Experimental Medicine
GA XO4TH
UT WOS:000730179100012
PM 34760335
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Chen, XC
   Wang, JN
   Tahir, M
   Zhang, FF
   Ran, YY
   Liu, ZJ
   Wang, J
AF Chen, Xuechai
   Wang, Jianan
   Tahir, Muhammad
   Zhang, Fangfang
   Ran, Yuanyuan
   Liu, Zongjian
   Wang, Juan
TI Current insights into the implications of m6A RNA methylation and
   autophagy interaction in human diseases
SO CELL AND BIOSCIENCE
LA English
DT Review
DE m6A; RNA methylation; Autophagy; Obesity; Azoospermatism; Ischemic heart
   disease; Cancer
ID MESSENGER-RNA; REGULATES ADIPOGENESIS; LYSOSOMAL DYSFUNCTION; BIOLOGICAL
   FUNCTIONS; M(6)A METHYLATION; CELL BIOLOGY; NUCLEAR-RNA;
   N-6-METHYLADENOSINE; EXPRESSION; OBESITY
AB Autophagy is a conserved degradation process crucial to maintaining the primary function of cellular and organismal metabolism. Impaired autophagy could develop numerous diseases, including cancer, cardiomyopathy, neurodegenerative disorders, and aging. N6-methyladenosine (m6A) is the most common RNA modification in eukaryotic cells, and the fate of m6A modified transcripts is controlled by m6A RNA binding proteins. m6A modification influences mRNA alternative splicing, stability, translation, and subcellular localization. Intriguingly, recent studies show that m6A RNA methylation could alter the expression of essential autophagy-related (ATG) genes and influence the autophagy function. Thus, both m6A modification and autophagy could play a crucial role in the onset and progression of various human diseases. In this review, we summarize the latest studies describing the impact of m6A modification in autophagy regulation and discuss the role of m6A modification-autophagy axis in different human diseases, including obesity, heart disease, azoospermatism or oligospermatism, intervertebral disc degeneration, and cancer. The comprehensive understanding of the m6A modification and autophagy interplay may help in interpreting their impact on human diseases and may aid in devising future therapeutic strategies.
C1 [Chen, Xuechai; Wang, Jianan; Tahir, Muhammad; Zhang, Fangfang; Wang, Juan] Beijing Univ Technol, Ctr Excellence Environm Safety & Biol Effects, Beijing Int Sci & Technol Cooperat Base Antiviral, Fac Environm & Life, 100 Ping Yuan, Beijing 100124, Peoples R China.
   [Ran, Yuanyuan; Liu, Zongjian] Capital Med Univ, Beijing Rehabil Hosp, Dept Rehabil, Beijing 100144, Peoples R China.
C3 Beijing University of Technology; Capital Medical University
RP Wang, J (corresponding author), Beijing Univ Technol, Ctr Excellence Environm Safety & Biol Effects, Beijing Int Sci & Technol Cooperat Base Antiviral, Fac Environm & Life, 100 Ping Yuan, Beijing 100124, Peoples R China.; Liu, ZJ (corresponding author), Capital Med Univ, Beijing Rehabil Hosp, Dept Rehabil, Beijing 100144, Peoples R China.
EM liuzj888@ccmu.edu.cn; juanwang@bjut.edu.cn
RI Wang, Jianan/P-4094-2019
OI liu, zong jian/0000-0002-8528-8992; Wang, Juan/0009-0002-9208-7985; Ran,
   Yuanyuan/0000-0002-6760-5173
FU National Natural Science Foundation of China [91854115, 31970044,
   31771571, 81400935]; Beijing Municipal Natural Science Foundation
   [7202001]; Scientific Research Project of Beijing Educational Committee
   [KM202010005022]
FX This work was supported by the National Natural Science Foundation of
   China (No. 91854115, 31970044, 31771571 to JW, and No. 81400935 to XC),
   the Beijing Municipal Natural Science Foundation (No.7202001 to XC), and
   the Scientific Research Project of Beijing Educational Committee (No.
   KM202010005022 to XC).
CR Aas A, 2017, PLOS ONE, V12, DOI 10.1371/journal.pone.0168182
   Bhatia D, 2020, PROG MOL BIOL TRANSL, V172, P107, DOI 10.1016/bs.pmbts.2020.01.008
   Bhol CS, 2020, SEMIN CANCER BIOL, V66, P22, DOI 10.1016/j.semcancer.2019.05.020
   BOKAR JA, 1994, J BIOL CHEM, V269, P17697
   Chen J, 2018, CELL DEATH DIS, V9, DOI 10.1038/s41419-017-0085-5
   Chen JX, 2019, AM J CANCER RES, V9, P752
   Chen XY, 2019, MOL CANCER, V18, DOI 10.1186/s12943-019-1033-z
   Chen X, 2019, BRIEF BIOINFORM, V20, P896, DOI 10.1093/bib/bbx142
   Chen XC, 2019, ACS CHEM NEUROSCI, V10, P2355, DOI 10.1021/acschemneuro.8b00657
   Cheng YL, 2020, AVIAN PATHOL, V49, P507, DOI 10.1080/03079457.2020.1783433
   Cheung MK, 2013, INT J OBESITY, V37, P744, DOI 10.1038/ijo.2012.77
   Chooi YC, 2019, METABOLISM, V92, P6, DOI 10.1016/j.metabol.2018.09.005
   Codogno P, 2010, CELL METAB, V11, P449, DOI 10.1016/j.cmet.2010.05.006
   Cui YH, 2021, NAT COMMUN, V12, DOI 10.1038/s41467-021-22469-6
   Dermentzaki G, 2020, FRONT MOL BIOSCI, V7, DOI 10.3389/fmolb.2020.555372
   Dominissini D, 2012, NATURE, V485, P201, DOI 10.1038/nature11112
   Dorn LE, 2019, J MOL CELL CARDIOL, V129, P272, DOI 10.1016/j.yjmcc.2019.03.010
   Du H, 2016, NAT COMMUN, V7, DOI 10.1038/ncomms12626
   Engel M, 2018, GENES BRAIN BEHAV, V17, DOI 10.1111/gbb.12428
   Fu Y, 2014, NAT REV GENET, V15, P293, DOI 10.1038/nrg3724
   Gao FY, 2018, J CELL BIOL, V217, P2103, DOI 10.1083/jcb.201710078
   Gulati P, 2013, P NATL ACAD SCI USA, V110, P2557, DOI 10.1073/pnas.1222796110
   Guo F, 2018, BRAIN PATHOL, V28, P3, DOI 10.1111/bpa.12545
   Guo JW, 2018, ONCOGENESIS, V7, DOI 10.1038/s41389-018-0054-6
   Han M, 2020, FRONT NEUROSCI-SWITZ, V14, DOI 10.3389/fnins.2020.00098
   He CC, 2009, ANNU REV GENET, V43, P67, DOI 10.1146/annurev-genet-102808-114910
   Hsu PJ, 2017, CELL RES, V27, P1115, DOI 10.1038/cr.2017.99
   Huang H, 2020, ENEURO, V7, DOI 10.1523/ENEURO.0125-20.2020
   Huang HL, 2018, NAT CELL BIOL, V20, P285, DOI 10.1038/s41556-018-0045-z
   Huang Q, 2021, AUTOPHAGY, V17, P1753, DOI 10.1080/15548627.2020.1783822
   Ianniello Z, 2018, INT J MOL SCI, V19, DOI 10.3390/ijms19082345
   Jia GF, 2011, NAT CHEM BIOL, V7, P885, DOI [10.1038/NCHEMBIO.687, 10.1038/nchembio.687]
   Jiao Y, 2016, NUTRIENTS, V8, DOI 10.3390/nu8020102
   Jin SH, 2018, CELL RES, V28, P955, DOI 10.1038/s41422-018-0069-8
   Kleene KC, 2013, REPRODUCTION, V146, pR1, DOI 10.1530/REP-12-0362
   Klionsky DJ, 2000, SCIENCE, V290, P1717, DOI 10.1126/science.290.5497.1717
   Kopp F, 2018, CELL, V172, P393, DOI 10.1016/j.cell.2018.01.011
   Leidal AM, 2018, NAT CELL BIOL, V20, P1338, DOI 10.1038/s41556-018-0235-8
   Levine B, 2004, DEV CELL, V6, P463, DOI 10.1016/S1534-5807(04)00099-1
   Levine B, 2019, CELL, V176, P11, DOI 10.1016/j.cell.2018.09.048
   Li A, 2017, CELL RES, V27, P444, DOI 10.1038/cr.2017.10
   Li BW, 2020, DRUG RESIST UPDATE, V53, DOI 10.1016/j.drup.2020.100720
   Li GC, 2020, CELL DEATH DIS, V11, DOI 10.1038/s41419-020-2284-8
   Li MM, 2018, GENOME BIOL, V19, DOI 10.1186/s13059-018-1436-y
   Li Q, 2021, SIGNAL TRANSDUCT TAR, V6, DOI 10.1038/s41392-020-00453-8
   Li WR, 2011, ASIAN J ANDROL, V13, P881, DOI 10.1038/aja.2011.85
   Lin Z, 2019, BBA-GENE REGUL MECH, V1862, P403, DOI 10.1016/j.bbagrm.2018.10.016
   Lin Z, 2017, CELL RES, V27, P1216, DOI 10.1038/cr.2017.117
   Lin ZY, 2020, EMBO J, V39, DOI 10.15252/embj.2019103181
   Linder B, 2015, NAT METHODS, V12, P767, DOI [10.1038/nmeth.3453, 10.1038/NMETH.3453]
   Liu HY, 2017, AUTOPHAGY, V13, P1952, DOI 10.1080/15548627.2017.1368596
   Liu JZ, 2014, NAT CHEM BIOL, V10, P93, DOI 10.1038/nchembio.1432
   Liu J, 2018, NAT CELL BIOL, V20, P1074, DOI 10.1038/s41556-018-0174-4
   Liu SP, 2020, CELL DEATH DIS, V11, DOI 10.1038/s41419-020-03148-8
   Liu SP, 2020, BIOMED PHARMACOTHER, V127, DOI 10.1016/j.biopha.2020.110098
   Luo RC, 2020, AUTOPHAGY, V16, P52, DOI 10.1080/15548627.2019.1596488
   Ma XC, 2019, J AM HEART ASSOC, V8, DOI 10.1161/JAHA.118.010866
   Mathiyalagan P, 2019, CIRCULATION, V139, P518, DOI 10.1161/CIRCULATIONAHA.118.033794
   Matsui Y, 2007, CIRC RES, V100, P914, DOI 10.1161/01.RES.0000261924.76669.36
   Mauer J, 2017, NATURE, V541, P371, DOI 10.1038/nature21022
   Meyer KD, 2014, NAT REV MOL CELL BIO, V15, P313, DOI 10.1038/nrm3785
   Meyer KD, 2012, CELL, V149, P1635, DOI 10.1016/j.cell.2012.05.003
   Mizunoe Y, 2017, AUTOPHAGY, V13, P642, DOI 10.1080/15548627.2016.1274850
   Mizushima N, 2020, NEW ENGL J MED, V383, P1564, DOI 10.1056/NEJMra2022774
   Tran NV, 2019, NUCLEIC ACIDS RES, V47, P7719, DOI 10.1093/nar/gkz619
   Otomo C, 2013, NAT STRUCT MOL BIOL, V20, P59, DOI 10.1038/nsmb.2431
   Patil DP, 2016, NATURE, V537, P369, DOI 10.1038/nature19342
   Ping XL, 2014, CELL RES, V24, P177, DOI 10.1038/cr.2014.3
   Piya S, 2017, AUTOPHAGY, V13, P214, DOI 10.1080/15548627.2016.1245263
   Puertollano R, 2018, EMBO J, V37, DOI 10.15252/embj.201798804
   Qin YH, 2020, INT J MOL MED, V46, P1958, DOI 10.3892/ijmm.2020.4746
   Qiu XH, 2020, NEUROSCI LETT, V737, DOI 10.1016/j.neulet.2020.135315
   Rosen ED, 2006, NAT REV MOL CELL BIO, V7, P885, DOI 10.1038/nrm2066
   Rottman F M, 1976, Prog Nucleic Acid Res Mol Biol, V19, P21
   Roundtree IA, 2017, ELIFE, V6, DOI 10.7554/eLife.31311
   Roundtree IA, 2016, TRENDS GENET, V32, P320, DOI 10.1016/j.tig.2016.03.006
   Saftig P, 2008, AUTOPHAGY, V4, P510, DOI 10.4161/auto.5724
   Saha S, 2018, BIOMED PHARMACOTHER, V104, P485, DOI 10.1016/j.biopha.2018.05.007
   Saito T, 2019, J CLIN INVEST, V129, P802, DOI 10.1172/JCI122035
   Schwartz S, 2014, CELL REP, V8, P284, DOI 10.1016/j.celrep.2014.05.048
   Sciarretta S, 2018, J AM COLL CARDIOL, V71, P1999, DOI 10.1016/j.jacc.2018.02.066
   Shi HL, 2018, NATURE, V563, P249, DOI 10.1038/s41586-018-0666-1
   Shi HL, 2017, CELL RES, V27, P315, DOI 10.1038/cr.2017.15
   Singh R, 2009, J CLIN INVEST, V119, P3329, DOI 10.1172/JCI39228
   SKINNER MK, 1985, J CELL BIOL, V100, P1941, DOI 10.1083/jcb.100.6.1941
   Song HW, 2019, AUTOPHAGY, V15, P1419, DOI 10.1080/15548627.2019.1586246
   Song TX, 2019, NUCLEIC ACIDS RES, V47, P6130, DOI 10.1093/nar/gkz312
   Sui XB, 2015, CANCER LETT, V360, P106, DOI 10.1016/j.canlet.2015.02.009
   Sung H, 2019, CA-CANCER J CLIN, V69, P88, DOI 10.3322/caac.21499
   Tang HW, 2021, P NATL ACAD SCI USA, V118, DOI 10.1073/pnas.2021945118
   Tian JB, 2020, GUT, V69, P2180, DOI 10.1136/gutjnl-2019-320179
   Trivedi PC, 2020, BBA-MOL BASIS DIS, V1866, DOI 10.1016/j.bbadis.2020.165832
   Vojinovic D, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-06234-w
   Vu LP, 2017, NAT MED, V23, P1369, DOI 10.1038/nm.4416
   Walker William H, 2011, Spermatogenesis, V1, P116
   Wang CY, 2020, BIOCHEM BIOPH RES CO, V527, P953, DOI 10.1016/j.bbrc.2020.04.138
   Wang X, 2015, CELL, V161, P1388, DOI 10.1016/j.cell.2015.05.014
   Wang XX, 2020, AUTOPHAGY, V16, P1221, DOI 10.1080/15548627.2019.1659617
   Wang XX, 2018, INT J OBESITY, V42, P1912, DOI 10.1038/s41366-018-0027-z
   Wang XX, 2015, BIOCHEM BIOPH RES CO, V459, P201, DOI 10.1016/j.bbrc.2015.02.048
   Wang Y, 2019, MOL CANCER, V18, DOI 10.1186/s12943-019-1105-0
   Warda AS, 2017, EMBO REP, V18, P2004, DOI 10.15252/embr.201744940
   Wesselborg S, 2015, CELL MOL LIFE SCI, V72, P4721, DOI 10.1007/s00018-015-2034-8
   Wu RF, 2018, BBA-MOL CELL BIOL L, V1863, P1323, DOI 10.1016/j.bbalip.2018.08.008
   Wu RF, 2016, MOL BIOTECHNOL, V58, P450, DOI 10.1007/s12033-016-9947-9
   Yamamoto T, 2017, J AM SOC NEPHROL, V28, P1534, DOI 10.1681/ASN.2016070731
   Yang S, 2019, NAT COMMUN, V10, DOI 10.1038/s41467-019-10669-0
   Yeo GSH, 2014, MOL CELL ENDOCRINOL, V397, P34, DOI 10.1016/j.mce.2014.09.012
   Yorimitsu T, 2005, CELL DEATH DIFFER, V12, P1542, DOI 10.1038/sj.cdd.4401765
   Yue YN, 2015, GENE DEV, V29, P1343, DOI 10.1101/gad.262766.115
   Zhao X, 2014, CELL RES, V24, P1403, DOI 10.1038/cr.2014.151
   Zheng GQ, 2013, MOL CELL, V49, P18, DOI 10.1016/j.molcel.2012.10.015
   Zhitomirsky B, 2015, ONCOTARGET, V6, P1143, DOI 10.18632/oncotarget.2732
   Zhu HT, 2019, J EXP CLIN CANC RES, V38, DOI 10.1186/s13046-019-1159-2
   Zhu LY, 2019, CELL DEATH DIS, V10, DOI 10.1038/s41419-019-1585-2
NR 115
TC 44
Z9 46
U1 3
U2 57
PU BMC
PI LONDON
PA CAMPUS, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
EI 2045-3701
J9 CELL BIOSCI
JI Cell Biosci.
PD JUL 27
PY 2021
VL 11
IS 1
AR 147
DI 10.1186/s13578-021-00661-x
PG 15
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA TS1FO
UT WOS:000679403500001
PM 34315538
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Ruble, CL
   Smith, RM
   Calley, J
   Munsie, L
   Airey, DC
   Gao, Y
   Shin, JH
   Hyde, TM
   Straub, RE
   Weinberger, DR
   Nisenbaum, LK
AF Ruble, Cara L.
   Smith, Ryan M.
   Calley, John
   Munsie, Leanne
   Airey, David C.
   Gao, Yuan
   Shin, Joo Heon
   Hyde, Thomas M.
   Straub, Richard E.
   Weinberger, Daniel R.
   Nisenbaum, Laura K.
TI Genomic structure and expression of the human serotonin 2A receptor gene
   (HTR2A) locus: identification of novel HTR2A and antisense
   (HTR2A-AS1) exons
SO BMC GENETICS
LA English
DT Article
DE Serotonin; HTR2A; Alternative splicing; Antisense RNA; mRNA expression;
   Regulatory polymorphism; Allelic expression; Comparative genomics; Long
   non-coding RNA; 5-HT2A
ID LONG NONCODING RNAS; MESSENGER-RNA; DIFFERENTIAL EXPRESSION; 5-HT2A
   RECEPTOR; SPLICE VARIANTS; HUMAN BRAIN; PREDICTION; BINDING; FAMILY;
   POLYMORPHISM
AB Background: The serotonin 2A receptor is widely implicated in genetic association studies and remains an important drug target for psychiatric, neurological, and cardiovascular conditions. RNA sequencing redefined the architecture of the serotonin 2A receptor gene (HTR2A), revealing novel mRNA transcript isoforms utilizing unannotated untranslated regions of the gene. Expression of these untranslated regions is modulated by common single nucleotide polymorphisms (SNPs), namely rs6311. Previous studies did not fully capture the complexity of the sense-and antisense-encoded transcripts with respect to novel exons in the HTR2A gene locus. Here, we comprehensively catalogued exons and RNA isoforms for both HTR2A and HTR2A-AS1 using RNA-Seq from human prefrontal cortex and multiple mouse tissues. We subsequently tested associations between expression of newfound gene features and common SNPs in humans.
   Results: We find that the human HTR2A gene spans similar to 66 kilobases and consists of 7, rather than 4 exons. Furthermore, the revised human HTR2A-AS1 gene spans similar to 474 kilobases and consists of 18, rather than 3 exons. Three HTR2A exons directly overlap with HTR2A-AS1 exons, suggesting potential for complementary nucleotide interactions. The repertoire of possible mouse Htr2a splice isoforms is remarkably similar to humans and we also find evidence for overlapping sense-antisense transcripts in the same relative positions as the human transcripts. rs6311 and SNPs in high linkage disequilibrium are associated with HTR2A-AS1 expression, in addition to previously described associations with expression of the extended 5' untranslated region of HTR2A.
   Conclusions: Our proposed HTR2A and HTR2A-AS1 gene structures dramatically differ from current annotations, now including overlapping exons on the sense and anti-sense strands. We also find orthologous transcript isoforms expressed in mice, providing opportunities to elucidate the biological roles of the human isoforms using a model system. Associations between rs6311 and expression of HTR2A and HTR2A-AS1 suggest this polymorphism is capable of modulating the expression of the sense or antisense transcripts. Still unclear is whether these SNPs act directly on the expression of the sense or antisense transcripts and whether overlapping exons are capable of interacting through complimentary base-pairing. Additional studies are necessary to determine the extent and nature of interactions between the SNPs and the transcripts prior to interpreting these findings in the context of phenotypes associated with HTR2A.
C1 [Ruble, Cara L.; Smith, Ryan M.; Calley, John; Munsie, Leanne; Airey, David C.; Nisenbaum, Laura K.] Eli Lilly & Co, Lilly Corp Ctr, Tailored Therapeut, Indianapolis, IN 46285 USA.
   [Gao, Yuan; Shin, Joo Heon; Hyde, Thomas M.; Straub, Richard E.; Weinberger, Daniel R.] Lieber Inst Brain Dev, Baltimore, MD USA.
   [Hyde, Thomas M.] Johns Hopkins Univ, Sch Med, Dept Neurol, Baltimore, MD USA.
   [Hyde, Thomas M.] Johns Hopkins Univ, Sch Med, Dept Psychiat, Baltimore, MD USA.
   [Hyde, Thomas M.] Johns Hopkins Univ, Sch Med, Dept Behav Sci, Baltimore, MD USA.
   [Weinberger, Daniel R.] Johns Hopkins Univ, Sch Med, Dept Psychiat, Baltimore, MD 21205 USA.
   [Weinberger, Daniel R.] Johns Hopkins Univ, Sch Med, Dept Neurol, Baltimore, MD 21205 USA.
   [Weinberger, Daniel R.] Johns Hopkins Univ, Sch Med, Dept Neurosci, Baltimore, MD 21205 USA.
   [Weinberger, Daniel R.] Johns Hopkins Univ, Sch Med, Inst Med Genet, Baltimore, MD USA.
C3 Eli Lilly; Lilly Research Laboratories; Johns Hopkins University; Johns
   Hopkins University; Johns Hopkins University; Johns Hopkins University;
   Johns Hopkins University; Johns Hopkins University; Johns Hopkins
   University
RP Nisenbaum, LK (corresponding author), Eli Lilly & Co, Lilly Corp Ctr, Tailored Therapeut, Indianapolis, IN 46285 USA.
EM nisenbaum_laura_k@lilly.com
RI Gao, Yuan/MGA-0610-2025
FU Eli Lilly and Company
FX This study was funded by Eli Lilly and Company.
CR Abdolmaleky HM, 2011, SCHIZOPHR RES, V129, P183, DOI 10.1016/j.schres.2011.04.007
   Anders S, 2010, GENOME BIOL, V11, DOI 10.1186/gb-2010-11-10-r106
   [Anonymous], 2014, DISGENET DISC PLATF
   Barrie ES, 2012, MOL PHARMACOL, V81, P620, DOI 10.1124/mol.111.076604
   Belgard TG, 2011, NEURON, V71, P605, DOI 10.1016/j.neuron.2011.06.039
   Bray NJ, 2004, MOL PSYCHIATR, V9, P109, DOI 10.1038/sj.mp.4001366
   Bullard JH, 2010, BMC BIOINFORMATICS, V11, DOI 10.1186/1471-2105-11-94
   BURNET PWJ, 1995, BRAIN RES, V676, P157, DOI 10.1016/0006-8993(95)00104-X
   Calebiro D, 2010, TRENDS PHARMACOL SCI, V31, P221, DOI 10.1016/j.tips.2010.02.002
   Cartharius K, 2005, BIOINFORMATICS, V21, P2933, DOI 10.1093/bioinformatics/bti473
   Cech TR, 2014, CELL, V157, P77, DOI 10.1016/j.cell.2014.03.008
   Celada P, 2013, FRONT INTEGR NEUROSC, V7, DOI 10.3389/fnint.2013.00025
   CHEN K, 1992, MOL BRAIN RES, V14, P20, DOI 10.1016/0169-328X(92)90005-V
   ClinicalTrials, STUD EV EFF RCN3028
   COHEN ML, 1981, J PHARMACOL EXP THER, V218, P421
   Córdoba-Chacón J, 2011, ANN NY ACAD SCI, V1220, P6, DOI 10.1111/j.1749-6632.2011.05985.x
   Cummings J, 2014, LANCET, V383, P533, DOI 10.1016/S0140-6736(13)62106-6
   DECLERCK F, 1984, BIOCHEM PHARMACOL, V33, P2807, DOI 10.1016/0006-2952(84)90699-3
   Derrien T, 2012, GENOME RES, V22, P1775, DOI 10.1101/gr.132159.111
   Desmet FO, 2009, NUCLEIC ACIDS RES, V37, DOI 10.1093/nar/gkp215
   Down TA, 2002, GENOME RES, V12, P458, DOI 10.1101/gr.216102
   Einstein R, 2008, P NATL ACAD SCI USA, V105, P5230, DOI 10.1073/pnas.0801319105
   Fairbrother WG, 2002, SCIENCE, V297, P1007, DOI 10.1126/science.1073774
   Fukuda Y, 2006, BIOL PSYCHIAT, V60, P1331, DOI 10.1016/j.biopsych.2006.06.024
   Gao XY, 2008, GENET EPIDEMIOL, V32, P361, DOI 10.1002/gepi.20310
   Gasque Gabriel, 2013, Sci Rep, V3, psrep02120, DOI 10.1038/srep02120
   Gentles AJ, 1999, TRENDS GENET, V15, P47, DOI 10.1016/S0168-9525(98)01648-5
   Guest PC, 2000, BRAIN RES, V876, P238, DOI 10.1016/S0006-8993(00)02664-0
   Jaffe AE, 2015, NAT NEUROSCI, V18, P154, DOI 10.1038/nn.3898
   Jakab RL, 1998, P NATL ACAD SCI USA, V95, P735, DOI 10.1073/pnas.95.2.735
   JULIUS D, 1990, P NATL ACAD SCI USA, V87, P928, DOI 10.1073/pnas.87.3.928
   Kim D, 2013, GENOME BIOL, V14, DOI 10.1186/gb-2013-14-4-r36
   Li H, 2009, BIOINFORMATICS, V25, P1094, DOI [10.1093/bioinformatics/btp100, 10.1093/bioinformatics/btp324]
   Lianoglou S, 2013, GENE DEV, V27, P2380, DOI 10.1101/gad.229328.113
   Lin S, 2014, P NATL ACAD SCI USA, V111, P17224, DOI 10.1073/pnas.1413624111
   Lipska BK, 2006, BIOL PSYCHIAT, V60, P650, DOI 10.1016/j.biopsych.2006.06.019
   Liu W, 2012, PHARMACOGENOMICS J, V12, P246, DOI 10.1038/tpj.2010.90
   Lonsdale J, 2013, NAT GENET, V45, P580, DOI 10.1038/ng.2653
   Maginnis MS, 2010, J VIROL, V84, P9677, DOI 10.1128/JVI.00978-10
   Majumdar S, 2011, P NATL ACAD SCI USA, V108, P19778, DOI 10.1073/pnas.1115231108
   Maple AM, 2015, ACS CHEM NEUROSCI, V6, P1137, DOI 10.1021/acschemneuro.5b00031
   Markovic D, 2009, CELL MOL LIFE SCI, V66, P3337, DOI 10.1007/s00018-009-0093-4
   MCLENNAN PL, 1984, EUR J PHARMACOL, V104, P313, DOI 10.1016/0014-2999(84)90407-2
   MIYAKE A, 1995, BIOCHEM BIOPH RES CO, V208, P230, DOI 10.1006/bbrc.1995.1328
   Moldofsky H, 2011, J RHEUMATOL, V38, P2653, DOI 10.3899/jrheum.110194
   Nag K, 2007, BIOCHEM BIOPH RES CO, V362, P1037, DOI 10.1016/j.bbrc.2007.08.107
   Nagalakshmi U, 2008, SCIENCE, V320, P1344, DOI 10.1126/science.1158441
   Nau F, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0075426
   Necsulea A, 2014, NATURE, V505, P635, DOI 10.1038/nature12943
   Pan YX, 1998, FEBS LETT, V435, P65, DOI 10.1016/S0014-5793(98)01039-4
   Paralkar VR, 2014, BLOOD, V123, P1927, DOI 10.1182/blood-2013-12-544494
   Paz I, 2010, NUCLEIC ACIDS RES, V38, pW281, DOI 10.1093/nar/gkq444
   Piva F, 2012, HUM MUTAT, V33, P81, DOI 10.1002/humu.21609
   Rice P, 2000, TRENDS GENET, V16, P276, DOI 10.1016/S0168-9525(00)02024-2
   Robinson MD, 2007, BIOINFORMATICS, V23, P2881, DOI 10.1093/bioinformatics/btm453
   Robinson MD, 2010, BIOINFORMATICS, V26, P139, DOI 10.1093/bioinformatics/btp616
   Runte M, 2001, HUM MOL GENET, V10, P2687, DOI 10.1093/hmg/10.23.2687
   Sáiz PA, 2008, PSYCHIAT GENET, V18, P213, DOI 10.1097/YPG.0b013e3283050ada
   SALTZMAN AG, 1991, BIOCHEM BIOPH RES CO, V181, P1469, DOI 10.1016/0006-291X(91)92105-S
   Schubert CR, 2015, NEURON, V88, P1078, DOI 10.1016/j.neuron.2015.10.047
   SHIRE D, 1995, J BIOL CHEM, V270, P3726, DOI 10.1074/jbc.270.8.3726
   Smith RM, 2014, AUTISM RES, V7, P459, DOI 10.1002/aur.1383
   Smith RM, 2013, BIOL PSYCHIAT, V73, P546, DOI 10.1016/j.biopsych.2012.09.028
   Turecki G, 1999, AM J PSYCHIAT, V156, P1456
   Van de Kar LD, 2001, J NEUROSCI, V21, P3572, DOI 10.1523/JNEUROSCI.21-10-03572.2001
   Walther DJ, 2003, CELL, V115, P851, DOI 10.1016/S0092-8674(03)01014-6
   Wang ET, 2008, NATURE, V456, P470, DOI 10.1038/nature07509
   Wang M, 2006, GENE, V366, P219, DOI 10.1016/j.gene.2005.07.015
   Wang ZF, 2004, CELL, V119, P831, DOI 10.1016/j.cell.2004.11.010
   Williams AA, 2012, NEUROPSYCHOPHARMACOL, V37, P2285, DOI 10.1038/npp.2012.81
   Wu TD, 2010, BIOINFORMATICS, V26, P873, DOI 10.1093/bioinformatics/btq057
   Yamada K, 2007, P NATL ACAD SCI USA, V104, P2815, DOI 10.1073/pnas.0610765104
   Yeo GW, 2005, P NATL ACAD SCI USA, V102, P2850, DOI 10.1073/pnas.0409742102
   Yu W, 2010, BIOINFORMATICS, V26, P145, DOI 10.1093/bioinformatics/btp618
   Zhang Y, 2014, J NEUROSCI, V34, P11929, DOI [10.1523/JNEUROSCI.1860-14.2014, 10.11772/j.issn.1001-9081.2014.07.1929]
NR 75
TC 24
Z9 28
U1 0
U2 10
PU BMC
PI LONDON
PA CAMPUS, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
SN 1471-2156
J9 BMC GENET
JI BMC Genet.
PD JAN 6
PY 2016
VL 17
AR 16
DI 10.1186/s12863-015-0325-6
PG 15
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA DA2SA
UT WOS:000367645100001
PM 26738766
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU van der Meer, DLM
   Marques, IJ
   Leito, JTD
   Besser, J
   Bakkers, J
   Schoonheere, E
   Bagowski, CP
AF van der Meer, David L. M.
   Marques, Ines J.
   Leito, Jelani T. D.
   Besser, Jaya
   Bakkers, Jeroen
   Schoonheere, Edwige
   Bagowski, Christoph P.
TI Zebrafish cypher is important for somite formation and heart
   development
SO DEVELOPMENTAL BIOLOGY
LA English
DT Article
DE cypher; somites; ZASP; Z-line; PDZ; myopathy; heart development; LIM
   domain
ID TUMOR-SUPPRESSOR PROTEIN; DILATED CARDIOMYOPATHY; SEPTATE JUNCTIONS;
   ADULT ZEBRAFISH; DANIO-RERIO; PDZ DOMAINS; WILD-TYPE; KINASE-C; NO TAIL;
   MUSCLE
AB Mammalian CYPHER (Oracle, KIA0613), a member of the PDZ-LIM family of proteins (Enigma/LMP-1, ENH, ZASP/Cypher, RIL, ALP, and CLP-36), has been associated with cardiac and muscular myopathies. Targeted deletion of Cypher in mice is neonatal lethal possibly caused by myopathies.
   To further investigate the role of cypher in development, we have cloned the zebrafish orthologue. We present here the gene, domain structure, and expression pattern of zebrafish cypher during development. Cypher was not present as a maternal mRNA and was absent during early development. Cypher mRNA was first detected at the 3-somite stage in adaxial somites, and as somites matured, cypher expression gradually enveloped the whole somite. Later, cypher expression was also found in the heart, in head and jaw musculature, and in the brain.
   We further identified 13 alternative spliced forms of cypher from zebrafish heart and skeletal muscle tissue, among them a very short form containing the PDZ domain but lacking the ZM (ZASP-like) motif and the LIM domains.
   Targeted gene knock-down experiments using cypher antisense morpholinos led to severe defects, including truncation of the embryo, deformation of somites, dilatation of the pericardium, and thinning of the ventricular wall. The phenotype could be rescued by a cypher form, which contains the PDZ domain and the ZM motif, but lacks all three LIM domains.
   These findings indicate that a PDZ domain protein is important for normal somite formation and in normal heart development. Treatment of zebrafish embryos with cyclopamine, which disrupts hedgehog signaling, abolished cypher expression in 9 somite and 15-somite stage embryos. Taken together, our data suggest that cypher may play a role downstream of sonic hedgehog, in a late stage of somite development, when slow muscle fibers differentiate and migrate from the adaxial cells. (c) 2006 Elsevier Inc. All rights reserved.
C1 Leiden Univ, NL-2333 AL Leiden, Netherlands.
   Leiden Univ, Inst Biol, Dept Integrat Zool, NL-2311 GN Leiden, Netherlands.
   Hubrecht Labs NIOB, NL-3584 CT Utrecht, Netherlands.
C3 Leiden University; Leiden University - Excl LUMC; Leiden University -
   Excl LUMC; Leiden University; Royal Netherlands Academy of Arts &
   Sciences; Hubrecht Institute (KNAW)
RP Bagowski, CP (corresponding author), Leiden Univ, Wassenaarseweg 64, NL-2333 AL Leiden, Netherlands.
EM bagowski@rulbim.leidenuniv.nl
RI Marques, Ines/X-6325-2019; Marques, Ines Joao/L-8392-2014; Bakkers,
   Jeroen/H-5551-2011
OI Marques, Ines Joao/0000-0003-1254-9394; Bakkers,
   Jeroen/0000-0002-9418-0422
CR Anderson RH., 1992, The heart: Structure in health and disease
   Arimura T, 2004, J BIOL CHEM, V279, P6746, DOI 10.1074/jbc.M311849200
   Au YH, 2004, STRUCTURE, V12, P611, DOI 10.1016/j.str.2004.02.019
   Barresi MJF, 2001, CURR BIOL, V11, P1432, DOI 10.1016/S0960-9822(01)00428-6
   Bassett DI, 2003, DEVELOPMENT, V130, P5851, DOI 10.1242/dev.00799
   Brenman JE, 1996, J NEUROSCI, V16, P7407
   Chambers SP, 2001, BIOCHEM BIOPH RES CO, V286, P478, DOI 10.1006/bbrc.2001.5424
   Chen JN, 1996, DEVELOPMENT, V122, P3809
   CHO KO, 1992, NEURON, V9, P929, DOI 10.1016/0896-6273(92)90245-9
   Cortés F, 2003, DEV CELL, V5, P865, DOI 10.1016/S1534-5807(03)00362-9
   Elmasri H, 2004, MECH DEVELOP, V121, P659, DOI 10.1016/j.mod.2004.04.003
   Faulkner G, 1999, J CELL BIOL, V146, P465, DOI 10.1083/jcb.146.2.465
   Faulkner G, 2001, IUBMB LIFE, V51, P275, DOI 10.1080/152165401317190761
   Galbiati F, 2000, J BIOL CHEM, V275, P23368, DOI 10.1074/jbc.M002020200
   Haffter P, 1996, DEVELOPMENT, V123, P1
   Henry CA, 2005, DEV BIOL, V287, P346, DOI 10.1016/j.ydbio.2005.08.049
   Holley SA, 2000, GENE DEV, V14, P1678
   Huang CQ, 2003, J BIOL CHEM, V278, P7360, DOI 10.1074/jbc.M211875200
   Jelen F, 2003, ACTA BIOCHIM POL, V50, P985
   Jülich D, 2005, DEV BIOL, V286, P391, DOI 10.1016/j.ydbio.2005.06.040
   Jülich D, 2005, DEV CELL, V8, P575, DOI 10.1016/j.devcel.2005.01.016
   KENNEDY MB, 1995, TRENDS BIOCHEM SCI, V20, P350, DOI 10.1016/S0968-0004(00)89074-X
   KIMMEL CB, 1995, DEV DYNAM, V203, P253, DOI 10.1002/aja.1002030302
   Kornau HC, 1997, NAT BIOTECHNOL, V15, P319, DOI 10.1038/nbt0497-319
   Koshida S, 2005, DEV CELL, V8, P587, DOI 10.1016/j.devcel.2005.03.006
   Lefebvre JL, 2004, DEVELOPMENT, V131, P2605, DOI 10.1242/dev.01123
   Passier R, 2000, MECH DEVELOP, V92, P277, DOI 10.1016/S0925-4773(99)00330-5
   Sehnert AJ, 2002, NAT GENET, V31, P106, DOI 10.1038/ng875
   Selcen D, 2005, ANN NEUROL, V57, P269, DOI 10.1002/ana.20376
   Sieger D, 2004, DEV GENES EVOL, V214, P393, DOI 10.1007/s00427-004-0427-z
   Sierralta J, 2004, BRAIN RES REV, V47, P105, DOI 10.1016/j.brainresrev.2004.06.002
   Stickney HL, 2000, DEV DYNAM, V219, P287
   Takke C, 1999, DEVELOPMENT, V126, P3005
   THISSE C, 1993, DEVELOPMENT, V119, P1203
   Tsang M, 2004, DEVELOPMENT, V131, P2769, DOI 10.1242/dev.01157
   van der Meer DLM, 2005, AM J PHYSIOL-REG I, V289, pR1512, DOI 10.1152/ajpregu.00089.2005
   Van Eeden FJM, 1998, DEV GENET, V23, P65
   vanEeden FJM, 1996, DEVELOPMENT, V123, P153
   Vatta M, 2003, J AM COLL CARDIOL, V42, P2014, DOI 10.1016/j.jacc.2003.10.021
   Weinberg ES, 1996, DEVELOPMENT, V122, P271
   WILLOTT E, 1993, P NATL ACAD SCI USA, V90, P7834, DOI 10.1073/pnas.90.16.7834
   WOODS DF, 1991, CELL, V66, P451, DOI 10.1016/0092-8674(81)90009-X
   WU RY, 1994, J BIOL CHEM, V269, P25085
   Xu XL, 2002, NAT GENET, V30, P205, DOI 10.1038/ng816
   Yelon D, 1999, DEV BIOL, V214, P23, DOI 10.1006/dbio.1999.9406
   Zhou Q, 1999, J BIOL CHEM, V274, P19807, DOI 10.1074/jbc.274.28.19807
   Zhou Q, 2001, J CELL BIOL, V155, P605, DOI 10.1083/jcb.200107092
NR 47
TC 48
Z9 62
U1 0
U2 7
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0012-1606
J9 DEV BIOL
JI Dev. Biol.
PD NOV 15
PY 2006
VL 299
IS 2
BP 356
EP 372
DI 10.1016/j.ydbio.2006.07.032
PG 17
WC Developmental Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Developmental Biology
GA 104BL
UT WOS:000241930800005
PM 16982050
OA Bronze
DA 2025-04-10
ER

PT J
AU Mavrommatis, E
   Shioura, KM
   Los, T
   Goldspink, PH
AF Mavrommatis, Evangelos
   Shioura, Krystyna M.
   Los, Tamara
   Goldspink, Paul H.
TI The E-domain region of mechano-growth factor inhibits cellular apoptosis
   and preserves cardiac function during myocardial infarction
SO MOLECULAR AND CELLULAR BIOCHEMISTRY
LA English
DT Article
DE IGF-1 isoforms; E-domain; Myocardial infarction; Cardiac function; Cell
   death
ID FACTOR-I; IGF-I; CARDIOMYOCYTE APOPTOSIS; HYPEROSMOTIC STRESS;
   GENE-EXPRESSION; WALL STRESS; MUSCLE; PEPTIDE; HYPERTROPHY; HEART
AB Insulin-like growth factor-1 (IGF-1) isoforms are expressed via alternative splicing. Expression of the minor isoform IGF-1Eb [also known as mechano-growth factor (MGF)] is responsive to cell stress. Since IGF-1 isoforms differ in their E-domain regions, we are interested in determining the biological function of the MGF E-domain. To do so, a synthetic peptide analog was used to gain mechanistic insight into the actions of the E-domain. Treatment of H9c2 cells indicated a rapid cellular uptake mechanism that did not involve IGF-1 receptor activation but resulted in a nuclear localization. Peptide treatment inhibited the intrinsic apoptotic pathway in H9c2 cells subjected to cell stress with sorbitol by preventing the collapse of the mitochondrial membrane potential and inhibition of caspase-3 activation. Therefore, we administered the peptide at the time of myocardial infarction (MI) in mice. At 2 weeks post-MI cardiac function, gene expression and cell death were assayed. A significant decline in both systolic and diastolic function was evident in untreated mice based on PV loop analysis. Delivery of the E-peptide ameliorated the decline in function and resulted in significant preservation of cardiac contractility. Associated with these changes were an inhibition of pathologic hypertrophy and significantly fewer apoptotic nuclei in the viable myocardium of E-peptide-treated mice post-MI. We conclude that administration of the MGF E-domain peptide may provide a means of modulating local tissue IGF-1 autocrine/paracrine actions to preserve cardiac function, prevent cell death, and pathologic remodeling in the heart.
C1 [Mavrommatis, Evangelos; Shioura, Krystyna M.; Los, Tamara] Univ Illinois, Cardiovasc Res Ctr, Chicago, IL USA.
   [Goldspink, Paul H.] Med Coll Wisconsin, Dept Physiol, Milwaukee, WI 53226 USA.
   [Goldspink, Paul H.] Med Coll Wisconsin, Cardiovasc Res Ctr, Milwaukee, WI 53226 USA.
C3 University of Illinois System; University of Illinois Chicago;
   University of Illinois Chicago Hospital; Medical College of Wisconsin;
   Medical College of Wisconsin
RP Goldspink, PH (corresponding author), Med Coll Wisconsin, Dept Physiol, 8701 Watertown Plank Rd,POB 26509, Milwaukee, WI 53226 USA.
EM pgoldspink@mcw.edu
FU National Institutes Health, Heart Lung and Blood Institutes [R01
   HL090523]
FX This study was supported by the National Institutes Health, Heart Lung
   and Blood Institutes R01 HL090523 (PHG).
CR Barton ER, 2010, J APPL PHYSIOL, V108, P1069, DOI 10.1152/japplphysiol.01308.2009
   Carpenter V, 2008, HEART LUNG CIRC, V17, P33, DOI 10.1016/j.hlc.2007.04.013
   Cheema U, 2003, CELL MOTIL CYTOSKEL, V54, P226, DOI 10.1002/cm.10095
   Cheng W, 1996, EXP CELL RES, V226, P316, DOI 10.1006/excr.1996.0232
   Chiong M, 2010, APOPTOSIS, V15, P887, DOI 10.1007/s10495-010-0505-9
   Colao A, 2004, HORM RES, V62, P42, DOI 10.1159/000080498
   Conti E, 2001, J AM COLL CARDIOL, V38, P26, DOI 10.1016/S0735-1097(01)01367-5
   Dluzniewska J, 2005, FASEB J, V19, P1896, DOI 10.1096/fj.05-3786fje
   Donath MY, 1998, EUR J ENDOCRINOL, V139, P109, DOI 10.1530/eje.0.1390109
   DUERR RL, 1995, J CLIN INVEST, V95, P619, DOI 10.1172/JCI117706
   Duerr RL, 1996, CIRCULATION, V93, P2188, DOI 10.1161/01.CIR.93.12.2188
   DUGUAY SJ, 1995, J BIOL CHEM, V270, P17566, DOI 10.1074/jbc.270.29.17566
   FOYT HL, 1991, J BIOL CHEM, V266, P7300
   Galvez A, 2001, CELL TISSUE RES, V304, P279, DOI 10.1007/s004410100358
   Galvez AS, 2003, J BIOL CHEM, V278, P38484, DOI 10.1074/jbc.M211824200
   Goldspink G, 2004, ADV GENET, V52, P23, DOI 10.1016/S0065-2660(04)52002-3
   Goldspink PH, 2004, CIRC RES, V95, P424, DOI 10.1161/01.RES.0000138299.85648.92
   Hill M, 2003, J PHYSIOL-LONDON, V549, P409, DOI 10.1113/jphysiol.2002.035832
   Kajstura J, 1996, LAB INVEST, V74, P86
   Li Q, 1997, J CLIN INVEST, V100, P1991, DOI 10.1172/JCI119730
   Loennechen JP, 2001, AM J PHYSIOL-HEART C, V280, pH2902, DOI 10.1152/ajpheart.2001.280.6.H2902
   Mao YW, 2004, CELL DEATH DIFFER, V11, P512, DOI 10.1038/sj.cdd.4401384
   Matthews KG, 1999, J ENDOCRINOL, V163, P433, DOI 10.1677/joe.0.1630433
   McKoy G, 1999, J PHYSIOL-LONDON, V516, P583, DOI 10.1111/j.1469-7793.1999.0583v.x
   Moor AN, 2000, J MOL CELL CARDIOL, V32, P925, DOI 10.1006/jmcc.2000.1133
   Morales MP, 2000, BIOCHEM BIOPH RES CO, V270, P1029, DOI 10.1006/bbrc.2000.2550
   Morrison LE, 2003, CIRC RES, V92, P203, DOI 10.1161/01.RES.0000052989.83995.A5
   MUTA K, 1993, J CELL PHYSIOL, V156, P264, DOI 10.1002/jcp.1041560207
   Nagy N, 2006, AM J PHYSIOL-HEART C, V291, pH2636, DOI 10.1152/ajpheart.00399.2006
   Napier JR, 1999, J ENDOCRINOL, V163, P63
   OLIVETTI G, 1994, CARDIOVASC RES, V28, P1199, DOI 10.1093/cvr/28.8.1199
   Osterziel KJ, 1998, LANCET, V351, P1233, DOI 10.1016/S0140-6736(97)11329-0
   Quesada A, 2011, J NEUROSCI RES, V89, P394, DOI 10.1002/jnr.22543
   Quesada A, 2009, EXP NEUROL, V220, P255, DOI 10.1016/j.expneurol.2009.08.029
   REISS K, 1994, EXP CELL RES, V213, P463, DOI 10.1006/excr.1994.1224
   Sánchez-Más J, 2010, REV ESP CARDIOL, V63, P779, DOI 10.1016/S0300-8932(10)70180-9
   Santini MP, 2007, CIRC RES, V100, P1732, DOI 10.1161/CIRCRESAHA.107.148791
   SHIMATSU A, 1987, J BIOL CHEM, V262, P7894
   Shioura KM, 2007, AM J PHYSIOL-HEART C, V293, pH2870, DOI 10.1152/ajpheart.00585.2007
   SIEGFRIED JM, 1992, P NATL ACAD SCI USA, V89, P8107, DOI 10.1073/pnas.89.17.8107
   Stavropoulou A, 2009, MOL MED, V15, P127, DOI 10.2119/molmed.2009.00012
   Tanaka N, 1998, AM J PHYSIOL-HEART C, V275, pH393, DOI 10.1152/ajpheart.1998.275.2.H393
   Welch S, 2002, CIRC RES, V90, P641, DOI 10.1161/01.RES.0000013780.77774.75
   Yang SY, 1996, J MUSCLE RES CELL M, V17, P487, DOI 10.1007/BF00123364
   Yang SY, 2002, FEBS LETT, V522, P156, DOI 10.1016/S0014-5793(02)02918-6
NR 45
TC 18
Z9 22
U1 0
U2 7
PU SPRINGER
PI DORDRECHT
PA VAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDS
SN 0300-8177
EI 1573-4919
J9 MOL CELL BIOCHEM
JI Mol. Cell. Biochem.
PD SEP
PY 2013
VL 381
IS 1-2
BP 69
EP 83
DI 10.1007/s11010-013-1689-4
PG 15
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA 187XV
UT WOS:000322155900008
PM 23712705
OA hybrid, Green Published
DA 2025-04-10
ER

PT J
AU Miura, T
   Ohnishi, Y
   Kurushima, H
   Horie, H
   Kadoya, T
   Nakabeppu, Y
AF Miura, T
   Ohnishi, Y
   Kurushima, H
   Horie, H
   Kadoya, T
   Nakabeppu, Y
TI Regulation of the neuronal fate by AFosB and its downstream target,
   galectin-1
SO CURRENT DRUG TARGETS
LA English
DT Review
DE AP-1; alternative splicing; AFosB; galectin-1; redox regulation; cell
   fate; neuronal fate
ID PROMOTES AXONAL REGENERATION; GALACTOSIDE-BINDING LECTIN; FOSB-LIKE
   IMMUNOREACTIVITY; EMBRYO CELL-LINE; DELTA-FOSB; PERIPHERAL-NERVES;
   GENE-EXPRESSION; RAT-1A CELLS; DNA-BINDING; TRANSCRIPTIONAL ACTIVATION
AB In mammals, the regulation of the cell fate to either proliferate, differentiate, arrest cell growth, or initiate programmed cell death is the most fundamental mechanism for maintaining normal cell function and tissue homeostasis. Under multiple signaling pathways, Jun and Fos family proteins are known to play important roles as components of an AP-1 (activator protein-1) complex, to regulate the transcription of various genes involved in cell proliferation, differentiation and programmed cell death. Delta FosB, one of the AP-1 subunits encoded by alternatively spliced fosB mRNA, triggers one round of proliferation in quiescent rat embryo cell lines, followed by a different cell fate such as morphological alteration or delayed cell death. As one of the downstream targets of the Delta FosB in rat3Y1 cell line, we identified rat galectin-1 and its novel variant, galectin-1 beta, and demonstrated that the expression of galectin-1 is required for the proliferative activation of quiescent rat1A cells by Delta FosB, thus indicating that galectin-1 is one of functional targets of Delta FosB. The expression of Delta FosB is highly inducible in the adult brain in response to various insults such as ischemic reperfusion injury, seizure induced by electric stimulation or cocaine administration. On the other hand, galectin-1 has also been shown to be involved in the regeneration of damaged axons in the peripheral nerve, as well as in neurite outgrowth or synaptic connectivity in the olfactory system during development. We herein propose that Delta FosB together with galectin-1, may therefore mediate neuroprotection and neurogenesis in response to brain damage.
C1 Kyushu Univ, Div Neurofunct Genom, Dept Immunobiol & Neurosci, Med Inst Bioregulat,Higashi Ku, Fukuoka 8128582, Japan.
   Waseda Univ, Adv Res Ctr Biol Sci, Tokyo 2020021, Japan.
   Kirin Brewery Co Ltd, CMC R&D Labs, Div Pharmaceut, Takasaki, Gumma 3700013, Japan.
C3 Kyushu University; Waseda University; Kirin Brewery Company Limited
RP Kyushu Univ, Div Neurofunct Genom, Dept Immunobiol & Neurosci, Med Inst Bioregulat,Higashi Ku, 3-1-1 Maidashi, Fukuoka 8128582, Japan.
EM yusaku@bioreg.kyushu-u.ac.jp
RI Nakabeppu, Yusaku/A-8902-2011
OI Nakabeppu, Yusaku/0000-0002-6739-242X
CR Akazawa C, 2004, NEUROSCIENCE, V125, P171, DOI 10.1016/j.neuroscience.2004.01.034
   BOURNE Y, 1994, J MOL BIOL, V235, P787, DOI 10.1006/jmbi.1994.1034
   BROWN HJ, 1995, EMBO J, V14, P124, DOI 10.1002/j.1460-2075.1995.tb06982.x
   Chen CP, 1997, PRENATAL DIAG, V17, P13, DOI 10.1002/(SICI)1097-0223(199701)17:1<13::AID-PD18>3.0.CO;2-#
   CHEN JS, 1995, MOL PHARMACOL, V48, P880
   Chen JS, 2000, J NEUROSCI, V20, P8965
   Chinenov Y, 2001, ONCOGENE, V20, P2438, DOI 10.1038/sj.onc.1204385
   Cho M, 1996, BIOCHEMISTRY-US, V35, P13081, DOI 10.1021/bi961181d
   Crocker SJ, 1998, MOL BRAIN RES, V53, P69, DOI 10.1016/S0169-328X(97)00281-7
   DOBRZANSKI P, 1991, MOL CELL BIOL, V11, P5470, DOI 10.1128/MCB.11.11.5470
   Doucet JP, 1996, EUR J NEUROSCI, V8, P365, DOI 10.1111/j.1460-9568.1996.tb01220.x
   Hayes JD, 2001, CANCER LETT, V174, P103, DOI 10.1016/S0304-3835(01)00695-4
   Herdegen T, 1998, BRAIN RES REV, V28, P370, DOI 10.1016/S0165-0173(98)00018-6
   Hollen KM, 1997, MOL BRAIN RES, V47, P31, DOI 10.1016/S0169-328X(97)00034-X
   HOPE BT, 1994, NEURON, V13, P1235, DOI 10.1016/0896-6273(94)90061-2
   Horie H, 1999, J NEUROSCI, V19, P9964
   Horie H, 2004, J NEUROSCI, V24, P1873, DOI 10.1523/JNEUROSCI.4483-03.2004
   Imbe H, 2003, BRAIN RES, V993, P72, DOI 10.1016/j.brainres.2003.08.064
   Inagaki Y, 2000, EUR J BIOCHEM, V267, P2955, DOI 10.1046/j.1432-1327.2000.01311.x
   Jochum W, 2001, ONCOGENE, V20, P2401, DOI 10.1038/sj.onc.1204389
   JOOSS KU, 1994, EMBO J, V13, P1467, DOI 10.1002/j.1460-2075.1994.tb06401.x
   KOVARY K, 1991, NEW BIOL, V3, P870
   Mandelzys A, 1997, J NEUROSCI, V17, P5407
   McClung CA, 2003, NAT NEUROSCI, V6, P1208, DOI 10.1038/nn1143
   McGahan L, 1998, MOL BRAIN RES, V56, P146, DOI 10.1016/S0169-328X(98)00039-4
   McGraw J, 2004, EUR J NEUROSCI, V20, P2872, DOI 10.1111/j.1460-9568.2004.03802.x
   McGraw J, 2004, NEUROSCIENCE, V128, P713, DOI 10.1016/j.neuroscience.2004.06.075
   METZ R, 1994, EMBO J, V13, P3832, DOI 10.1002/j.1460-2075.1994.tb06694.x
   Miura T, 2004, CELL DEATH DIFFER, V11, P1076, DOI 10.1038/sj.cdd.4401462
   NAKABEPPU Y, 1991, CELL, V64, P751, DOI 10.1016/0092-8674(91)90504-R
   NAKABEPPU Y, 1993, MOL CELL BIOL, V13, P4157, DOI 10.1128/MCB.13.7.4157
   NAKABEPPU Y, 1988, CELL, V55, P907, DOI 10.1016/0092-8674(88)90146-8
   NAKABEPPU Y, 1989, EMBO J, V8, P3833, DOI 10.1002/j.1460-2075.1989.tb08561.x
   Nishioka T, 2002, J BIOCHEM, V131, P653, DOI 10.1093/oxfordjournals.jbchem.a003148
   Novotny V, 1998, NUCLEIC ACIDS RES, V26, P5480, DOI 10.1093/nar/26.23.5480
   ODA S, 1995, ONCOGENE, V10, P1343
   Ogita K, 2004, NEUROPHARMACOLOGY, V46, P580, DOI 10.1016/j.neuropharm.2003.11.002
   Perillo NL, 1998, J MOL MED, V76, P402, DOI 10.1007/s001090050232
   Puche AC, 1996, DEV BIOL, V179, P274, DOI 10.1006/dbio.1996.0257
   Robertson GS, 2004, EUR J NEUROSCI, V20, P3189, DOI 10.1111/j.1460-9568.2004.03774.x
   Rodríguez JJ, 2001, SYNAPSE, V39, P122, DOI 10.1002/1098-2396(200102)39:2<122::AID-SYN3>3.0.CO;2-R
   Sabatakos G, 2000, NAT MED, V6, P985, DOI 10.1038/79683
   Shaulian E, 2001, ONCOGENE, V20, P2390, DOI 10.1038/sj.onc.1204383
   Skinner M, 1997, MOL CELL BIOL, V17, P2372, DOI 10.1128/MCB.17.5.2372
   Tahara K, 2003, CELL DEATH DIFFER, V10, P496, DOI 10.1038/sj.cdd.4401173
   Tkach V, 2003, ONCOGENE, V22, P5045, DOI 10.1038/sj.onc.1206570
   TRACEY BM, 1992, J BIOL CHEM, V267, P10342
   VahidAnsari F, 1996, EUR J NEUROSCI, V8, P927, DOI 10.1111/j.1460-9568.1996.tb01579.x
   WISDOM R, 1992, GENE DEV, V6, P667, DOI 10.1101/gad.6.4.667
   YEN J, 1991, P NATL ACAD SCI USA, V88, P5077, DOI 10.1073/pnas.88.12.5077
   Zhang DS, 2002, J NEUROCHEM, V82, P1453, DOI 10.1046/j.1471-4159.2002.01089.x
NR 51
TC 16
Z9 16
U1 0
U2 6
PU BENTHAM SCIENCE PUBL LTD
PI SHARJAH
PA EXECUTIVE STE Y-2, PO BOX 7917, SAIF ZONE, 1200 BR SHARJAH, U ARAB
   EMIRATES
SN 1389-4501
EI 1873-5592
J9 CURR DRUG TARGETS
JI Curr. Drug Targets
PD JUN
PY 2005
VL 6
IS 4
BP 437
EP 444
DI 10.2174/1389450054021963
PG 8
WC Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Pharmacology & Pharmacy
GA 939TT
UT WOS:000230096000008
PM 16026262
DA 2025-04-10
ER

PT J
AU Takimoto, K
   Li, DQ
   Hershman, KM
   Li, P
   Jackson, EK
   Levitan, ES
AF Takimoto, K
   Li, DQ
   Hershman, KM
   Li, P
   Jackson, EK
   Levitan, ES
TI Decreased expression of Kv4.2 and novel Kv4.3 K+ channel subunit mRNAs
   in ventricles of renovascular hypertensive rats
SO CIRCULATION RESEARCH
LA English
DT Article
DE K+ channel; alternative splicing; transient outward current;
   renovascular hypertension; ventricular hypertrophy
ID GATED POTASSIUM CHANNEL; TRANSIENT OUTWARD CURRENT; DIFFERENTIAL
   EXPRESSION; BETA-SUBUNIT; GENE-EXPRESSION; MYOCYTES; HEART; CLONING;
   BRAIN; DEXAMETHASONE
AB Hypertension-induced cardiac hypertrophy is associated with alterations in ventricular action potentials. To understand molecular mechanisms underlying this electrical abnormality, expression of cardiac voltage-gated K+ channel subunit genes was examined in ventricles of renovascular hypertensive rats. While generating a rat Kv4.3 probe, we discovered a previously unreported 19-amino acid insertion in the C-terminal intracellular region of the channel subunit. RNase protection assays indicated that this novel isoform is predominant in rat lung and heart. Effects of renovascular hypertension were then determined by using renal artery clipping models: two-kidney, one clip (2K-1C) rats, a model of high-renin hypertension with a normal plasma volume, and one-kidney, one clip (1K-1C) rats, a model of normal renin with a raised plasma volume. Expression of Kv4.2 and Kv4.3 mRNAs was diminished by >50% in ventricles of 2K-1C rats; however, no changes in the expression of Kv1.2, Kv1.4, Kv1.5, Kv2.1, or KvLQT1 mRNAs were detected. Similar downregulation of Kv4.2 and Kv4.3 mRNAs was detected in 1K-1C rats. Chronic administration of captopril, an angiotensin-converting enzyme inhibitor, blocked the development of hypertension and the suppression of Kv4 subfamily channel mRNA expression in 2K-1C rats. Furthermore, captopril administration to sham-operated rats significantly increased Kv4.2 mRNA. These results indicate that renovascular hypertension causes specific reductions in Kv4 subfamily channel mRNA expression and that this effect is likely to be mediated primarily by an increase in cardiac afterload.
C1 UNIV PITTSBURGH, DEPT PHARMACOL, PITTSBURGH, PA 15261 USA.
   UNIV PITTSBURGH, CTR CLIN PHARMACOL, PITTSBURGH, PA USA.
C3 Pennsylvania Commonwealth System of Higher Education (PCSHE); University
   of Pittsburgh; Pennsylvania Commonwealth System of Higher Education
   (PCSHE); University of Pittsburgh
OI Jackson, Edwin/0000-0002-8101-6009
FU NHLBI NIH HHS [HL-35909, HL-55314, HL-55312] Funding Source: Medline
CR ASMAN DC, 1993, J BIOL CHEM, V268, P12530
   ATTARDI B, 1993, RECEPTOR CHANNEL, V1, P287
   BALDWIN TJ, 1991, NEURON, V7, P471, DOI 10.1016/0896-6273(91)90299-F
   Barhanin J, 1996, NATURE, V384, P78, DOI 10.1038/384078a0
   BARRY DM, 1995, CIRC RES, V77, P361, DOI 10.1161/01.RES.77.2.361
   BENITAH JP, 1993, J PHYSIOL-LONDON, V469, P111, DOI 10.1113/jphysiol.1993.sp019807
   BOYDEN PA, 1995, CARDIOVASC RES, V29, P312, DOI 10.1016/0008-6363(96)88586-5
   BROOKSBY P, 1993, J HYPERTENS, V11, P611, DOI 10.1097/00004872-199306000-00005
   CERBAI E, 1994, CARDIOVASC RES, V28, P1180, DOI 10.1093/cvr/28.8.1180
   CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
   COULOMBE A, 1994, PFLUG ARCH EUR J PHY, V427, P47, DOI 10.1007/BF00585941
   DEMIERA EVS, 1992, P ROY SOC LOND B BIO, P9
   Dixon JE, 1996, CIRC RES, V79, P659, DOI 10.1161/01.RES.79.4.659
   DIXON JE, 1994, CIRC RES, V75, P252, DOI 10.1161/01.RES.75.2.252
   ENGLAND SK, 1995, P NATL ACAD SCI USA, V92, P6309, DOI 10.1073/pnas.92.14.6309
   FRECH GC, 1989, NATURE, V340, P642, DOI 10.1038/340642a0
   GidhJain M, 1996, CIRC RES, V79, P669, DOI 10.1161/01.RES.79.4.669
   JOHNSON DB, 1996, CURR OPIN NEPHROL HY, V5, P189
   KANNEL WB, 1991, J HYPERTENS, V9, pS3, DOI 10.1097/00004872-199112002-00002
   KEUNG EC, 1989, CIRC RES, V64, P753, DOI 10.1161/01.RES.64.4.753
   KLEINMAN RB, 1988, AM J PHYSIOL, V255, pH1413
   Levitan ES, 1996, NEUROPHARMACOLOGY, V35, P1001, DOI 10.1016/0028-3908(96)00095-0
   LIP GYH, 1994, BRIT MED BULL, V50, P299, DOI 10.1093/oxfordjournals.bmb.a072893
   LUNEAU CJ, 1991, P NATL ACAD SCI USA, V88, P3932, DOI 10.1073/pnas.88.9.3932
   MAJUMDER K, 1995, FEBS LETT, V361, P13, DOI 10.1016/0014-5793(95)00120-X
   MATSUBARA H, 1993, J CLIN INVEST, V92, P1659, DOI 10.1172/JCI116751
   MORALES MJ, 1995, J BIOL CHEM, V270, P6272, DOI 10.1074/jbc.270.11.6272
   MORI Y, 1993, J BIOL CHEM, V268, P26482
   PICKERING TJ, 1990, PATHOPHYSIOLOGY DIAG, P1539
   POTREAU D, 1995, CARDIOVASC RES, V30, P440, DOI 10.1016/S0008-6363(95)00073-9
   Qiu DY, 1996, CIRC RES, V79, P461, DOI 10.1161/01.RES.79.3.461
   ROBERDS SL, 1991, P NATL ACAD SCI USA, V88, P1798, DOI 10.1073/pnas.88.5.1798
   RUDY B, 1992, P NATL ACAD SCI USA, V89, P4603, DOI 10.1073/pnas.89.10.4603
   Sanguinetti MC, 1996, NATURE, V384, P80, DOI 10.1038/384080a0
   SERODIO P, 1994, J NEUROPHYSIOL, V72, P1516, DOI 10.1152/jn.1994.72.4.1516
   STUHMER W, 1989, EMBO J, V8, P3235, DOI 10.1002/j.1460-2075.1989.tb08483.x
   SWANSON R, 1990, NEURON, V4, P929, DOI 10.1016/0896-6273(90)90146-7
   TAKIMOTO K, 1994, CIRC RES, V75, P1006, DOI 10.1161/01.RES.75.6.1006
   TAKIMOTO K, 1993, NEURON, V11, P359, DOI 10.1016/0896-6273(93)90191-S
   TOMITA F, 1994, CIRC RES, V75, P296, DOI 10.1161/01.RES.75.2.296
   Wang Q, 1996, NAT GENET, V12, P17, DOI 10.1038/ng0196-17
   Wymore RS, 1997, CIRC RES, V80, P261, DOI 10.1161/01.RES.80.2.261
   XU W, 1991, AM J PHYSIOL, V260, pH935
   Yeola S. W., 1996, Biophysical Journal, V70, pA308
NR 44
TC 92
Z9 99
U1 0
U2 1
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA TWO COMMERCE SQ, 2001 MARKET ST, PHILADELPHIA, PA 19103 USA
SN 0009-7330
EI 1524-4571
J9 CIRC RES
JI Circ.Res.
PD OCT
PY 1997
VL 81
IS 4
BP 533
EP 539
DI 10.1161/01.RES.81.4.533
PG 7
WC Cardiac & Cardiovascular Systems; Hematology; Peripheral Vascular
   Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology; Hematology
GA XZ012
UT WOS:A1997XZ01200010
PM 9314834
DA 2025-04-10
ER

PT J
AU Vizirianakis, IS
   Yao, CC
   Chen, YQ
   Ziober, BL
   Tsiftsoglou, AS
   Kramer, RH
AF Vizirianakis, IS
   Yao, CC
   Chen, YQ
   Ziober, BL
   Tsiftsoglou, AS
   Kramer, RH
TI Transfection of MCF-7 carcinoma cells with human integrin α7 cDNA
   promotes adhesion to laminin
SO ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
LA English
DT Article
DE cDNA; cell adhesion assays; cloning; expression; human integrin alpha 7;
   monoclonal antibodies; transfection; tumor cells
ID SKELETAL-MUSCLE; NEUROMUSCULAR-JUNCTION; EXTRACELLULAR DOMAIN;
   MUSCULAR-DYSTROPHY; BINDING INTEGRINS; SPLICED VARIANTS; RECEPTOR;
   EXPRESSION; MYOBLASTS; IDENTIFICATION
AB The laminin-binding alpha7 beta1 integrin receptor is highly expressed by skeletal and cardiac muscles, and has been suggested to be a crucial molecule during myogenic cell migration and differentiation. Absence of integrin alpha7 subunit contributes to a form of muscular dystrophy in integrin alpha7 null mice, whereas specific mutations in the alpha7 gene are associated in humans with congenital myopathy, To examine in more detail the potential role of integrin alpha7 in human-related muscular disorders, we cloned alpha7 cDNA by RT-PCR from human skeletal muscle mRNA and then expressed the full-length human integrin alpha7 cDNA by transfection in several cell lines including MCF-7, COS-7, and NIH3T3 cells. The isolated cDNA corresponds to the human alpha 7X2B alternative splice form. Expression of human alpha7 was further confirmed by transfection of chimeric human/mouse alpha7 cDNA constructs. To demonstrate the functionality of expressed human alpha7, adhesion experiments with transfected MCF-7 cells have confirmed the specific binding of human alpha7 to laminin, In addition, mouse polyclonal and monoclonal antibodies were generated against the extracellular domain of human alpha7 and used to analyze by flow cytometry MCF-7 and NIH3T3 cells transfected with the full-length of human alpha7 cDNA. These results show for the first time the exogenous expression of functional full-length human alpha7 cDNA, as well. as the development of monoclonal antibodies against the human alpha7 extracellular domain. Antibodies developed will be useful for further analysis of human disorders involving alpha7 dysfunction and facilitate isolation of muscle stem cells (satellite cells) and thereby expand the opportunities for genetically modified transplantation treatment of human disease. (C) 2001 Academic Press.
C1 Univ Calif San Francisco, Dept Stomatol, San Francisco, CA 94143 USA.
   Univ Calif San Francisco, Dept Anat, San Francisco, CA 94143 USA.
   Aristotelian Univ Salonika, Dept Pharmaceut Sci, Pharmacol Lab, GR-54006 Salonika, Greece.
C3 University of California System; University of California San Francisco;
   University of California System; University of California San Francisco;
   Aristotle University of Thessaloniki
RP Kramer, RH (corresponding author), Univ Calif San Francisco, Dept Stomatol, HSW-604,Box 0512, San Francisco, CA 94143 USA.
RI Vizirianakis, Ioannis/AAK-6067-2020; Yao, Chung-Chen/D-1470-2018
OI Vizirianakis, Ioannis/0000-0003-1459-9774; YAO, CHUNG-CHEN
   JANE/0000-0002-2293-7000
CR Alameddine H S, 1991, Neuromuscul Disord, V1, P143, DOI 10.1016/0960-8966(91)90062-W
   BAKER RS, 1993, J PEDIATR OPHTHALMOL, V30, P113
   BAO ZZ, 1993, J CELL SCI, V106, P579
   Burkin DJ, 1998, J CELL BIOL, V143, P1067, DOI 10.1083/jcb.143.4.1067
   COLLO G, 1993, J BIOL CHEM, V268, P19019
   Fornaro M, 1997, MATRIX BIOL, V16, P185, DOI 10.1016/S0945-053X(97)90007-X
   Frisch SM, 1997, CURR OPIN CELL BIOL, V9, P701, DOI 10.1016/S0955-0674(97)80124-X
   GEORGEWEINSTEIN M, 1993, DEV BIOL, V156, P209, DOI 10.1006/dbio.1993.1071
   Hayashi YK, 1998, NAT GENET, V19, P94, DOI 10.1038/ng0598-94
   Hemler ME, 1998, CURR OPIN CELL BIOL, V10, P578, DOI 10.1016/S0955-0674(98)80032-X
   Hodges BL, 1997, J CELL SCI, V110, P2873
   Howe A, 1998, CURR OPIN CELL BIOL, V10, P220, DOI 10.1016/S0955-0674(98)80144-0
   HUGHES SM, 1990, NATURE, V345, P350, DOI 10.1038/345350a0
   HUNTER DD, 1989, NATURE, V338, P229, DOI 10.1038/338229a0
   HYNES RO, 1992, CELL, V69, P11, DOI 10.1016/0092-8674(92)90115-S
   KRAMER RH, 1991, CELL REGUL, V2, P805, DOI 10.1091/mbc.2.10.805
   KRAMER RH, 1994, METHOD ENZYMOL, V245, P129
   KRAMER RH, 1989, J BIOL CHEM, V264, P15642
   Leung E, 1998, BIOCHEM BIOPH RES CO, V243, P317, DOI 10.1006/bbrc.1998.8092
   Mayer U, 1997, NAT GENET, V17, P318, DOI 10.1038/ng1197-318
   Porter JC, 1998, TRENDS CELL BIOL, V8, P390, DOI 10.1016/S0962-8924(98)01344-0
   Sanders RJ, 1998, CANCER INVEST, V16, P329, DOI 10.3109/07357909809084653
   SANES JR, 1990, J CELL BIOL, V111, P1685, DOI 10.1083/jcb.111.4.1685
   SCHULTZ E, 1994, REV PHYSIOL BIOCH P, V123, P213, DOI 10.1007/BFb0030904
   SONG WK, 1992, J CELL BIOL, V117, P643, DOI 10.1083/jcb.117.3.643
   Tomatis D, 1999, EXP CELL RES, V246, P421, DOI 10.1006/excr.1998.4315
   Vachon PH, 1997, J CLIN INVEST, V100, P1870, DOI 10.1172/JCI119716
   Vachon PH, 1996, J CELL BIOL, V134, P1483, DOI 10.1083/jcb.134.6.1483
   VANDERMARK H, 1991, J BIOL CHEM, V266, P23593
   VANSWEARINGEN J, 1995, DEV BIOL, V170, P321, DOI 10.1006/dbio.1995.1218
   Vignier N, 1999, BIOCHEM BIOPH RES CO, V260, P357, DOI 10.1006/bbrc.1999.0916
   Yao CC, 1996, J CELL SCI, V109, P3139
   Yao CC, 1996, J BIOL CHEM, V271, P25598, DOI 10.1074/jbc.271.41.25598
   Yao CC, 1998, MOL BIOL CELL, V9, p416A
   Ziober BL, 1996, SEMIN CANCER BIOL, V7, P119, DOI 10.1006/scbi.1996.0017
   Ziober BL, 1996, J BIOL CHEM, V271, P22915, DOI 10.1074/jbc.271.37.22915
   Ziober BL, 1997, MOL BIOL CELL, V8, P1723, DOI 10.1091/mbc.8.9.1723
   ZIOBER BL, 1993, J BIOL CHEM, V268, P26773
NR 38
TC 22
Z9 22
U1 0
U2 0
PU ACADEMIC PRESS INC
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0003-9861
J9 ARCH BIOCHEM BIOPHYS
JI Arch. Biochem. Biophys.
PD JAN 1
PY 2001
VL 385
IS 1
BP 108
EP 116
DI 10.1006/abbi.2000.2134
PG 9
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA 391VA
UT WOS:000166375700015
PM 11361006
DA 2025-04-10
ER

PT J
AU Wada, J
   Kanwar, YS
AF Wada, J
   Kanwar, YS
TI Identification and characterization of galectin-9, a novel
   beta-galactoside-binding mammalian lectin
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID AMINO-ACID-SEQUENCE; GROWTH-FACTOR; MUSCLE LECTIN; PROTEIN; EXPRESSION;
   CLONING; LAMININ; FAMILY; GENE; IGE
AB A 36-kDa beta-galactoside mammalian lectin protein, designated as galectin-9, was isolated from mouse embryonic kidney by using a degenerate primer polymerase chain reaction and cloning strategy. Its deduced amino acid sequence had the characteristic conserved sequence motif of galectins. Endogenous galectin-9, extracted from liver and thymus, as well as recombinant galectin-9 exhibited specific binding activity for the lactosyl group. It had two distinct N- and C-terminal carbohydrate-binding domains connected by a link peptide, with no homology to any other protein. Galectin-9 had an alternate splicing isoform, exclusively expressed in the small intestine with a 31-amino acid insertion between the N-terminal domain and link peptide. Sequence homology analysis revealed that the C-terminal carbohydrate-binding domain of mouse galectin-9 had extensive similarity to that of monomeric rat galectin-5. The presence of galectin-5 in the mouse could not be demonstrated by polymerase chain reaction or by Northern or Southern blot genomic DNA analyses. Sequence comparison of rat galectin-5 and rat galectin-9 cDNA did not reveal identical nucleotide sequences in the overlapping C-terminal carbohydrate-binding domain, indicating that galectin-9 is not an alternative splicing isoform of galectin-5. However, galectin-9 had a sequence identical with that of its intestinal isoform in the overlapping regions in both species. Southern blot genomic DNA analyses, using the galectin-9 specific probe derived from the N-terminal carbohydrate-binding domain, indicated the presence of a novel gene encoding galectin-9 in both mice and rats. In contrast to galectin-5, which is mainly expressed in erythrocytes, galectin-9 was found to be widely distributed, i.e. in Liver, small intestine, thymus > kidney, spleen, lung cardiac and skeletal muscle > reticulocyte, brain. Collectively, these data indicate that galectin-9 is a new member of the galectin gene family and has a unique intestinal isoform.
C1 NORTHWESTERN UNIV, SCH MED, DEPT PATHOL, CHICAGO, IL 60611 USA.
C3 Northwestern University
RI Wada, Jun/B-2023-2011
OI Wada, Jun/0000-0003-1468-5170
FU NIDDK NIH HHS [DK28492] Funding Source: Medline
CR BARNES WM, 1994, P NATL ACAD SCI USA, V91, P2216, DOI 10.1073/pnas.91.6.2216
   BARONDES SH, 1994, CELL, V76, P597, DOI 10.1016/0092-8674(94)90498-7
   BARONDES SH, 1994, J BIOL CHEM, V269, P20807
   Borson N D, 1992, PCR Methods Appl, V2, P144
   Chenchik A., 1995, CLONTECHNIQUES, V10, P5
   CHENG S, 1994, P NATL ACAD SCI USA, V91, P5695, DOI 10.1073/pnas.91.12.5695
   CHERAYIL BJ, 1989, J EXP MED, V170, P1959, DOI 10.1084/jem.170.6.1959
   CHIRGWIN JM, 1979, BIOCHEMISTRY-US, V18, P5294, DOI 10.1021/bi00591a005
   Chou P Y, 1978, Adv Enzymol Relat Areas Mol Biol, V47, P45
   CHUI DHK, 1980, BRIT J HAEMATOL, V44, P431, DOI 10.1111/j.1365-2141.1980.tb05913.x
   COOPER DNW, 1991, J CELL BIOL, V115, P1437, DOI 10.1083/jcb.115.5.1437
   COOPER DNW, 1990, J CELL BIOL, V110, P1681, DOI 10.1083/jcb.110.5.1681
   COURAUD PO, 1989, J BIOL CHEM, V264, P1310
   EKBLOM P, 1995, MOL CELLULAR ASPECTS, P359
   ENGVALL E, 1971, IMMUNOCHEMISTRY, V8, P871, DOI 10.1016/0019-2791(71)90454-X
   FRIGERI LG, 1990, J BIOL CHEM, V265, P20763
   GITT MA, 1992, J BIOL CHEM, V267, P10601
   GITT MA, 1995, J BIOL CHEM, V270, P5032, DOI 10.1074/jbc.270.10.5032
   GITT MA, 1991, BIOCHEMISTRY-US, V30, P82, DOI 10.1021/bi00215a013
   GU MJ, 1994, J CELL SCI, V107, P175
   GUBLER U, 1983, GENE, V25, P263, DOI 10.1016/0378-1119(83)90230-5
   HADARI YR, 1995, J BIOL CHEM, V270, P3447, DOI 10.1074/jbc.270.7.3447
   HIRABAYASHI J, 1992, J BIOL CHEM, V267, P15485
   JUNG SK, 1994, J BIOCHEM-TOKYO, V116, P547, DOI 10.1093/oxfordjournals.jbchem.a124560
   KANWAR YS, 1995, KIDNEY INT, V48, P1646, DOI 10.1038/ki.1995.460
   KEREN DF, 1992, DIAGN IMMUNOL, P291
   Kuwabara I, 1996, J IMMUNOL, V156, P3939
   KYTE J, 1982, J MOL BIOL, V157, P105, DOI 10.1016/0022-2836(82)90515-0
   LAEMMLI UK, 1970, NATURE, V227, P680, DOI 10.1038/227680a0
   LIPMAN DJ, 1985, SCIENCE, V227, P1435, DOI 10.1126/science.2983426
   LIU ZZ, 1993, KIDNEY INT, V44, P1242, DOI 10.1038/ki.1993.375
   MADSEN P, 1995, J BIOL CHEM, V270, P5823, DOI 10.1074/jbc.270.11.5823
   MAGNALDO T, 1995, DEV BIOL, V168, P259, DOI 10.1006/dbio.1995.1078
   MASSA SM, 1993, BIOCHEMISTRY-US, V32, P260, DOI 10.1021/bi00052a033
   MIGNATTI P, 1991, J CELL BIOCHEM, V47, P201, DOI 10.1002/jcb.240470303
   ODA Y, 1993, J BIOL CHEM, V268, P5929
   POIRIER F, 1992, DEVELOPMENT, V115, P143
   QUN Z, 1993, ARCH BIOCHEM BIOPHYS, V300, P6, DOI 10.1006/abbi.1993.1002
   ROBERTSON MW, 1990, BIOCHEMISTRY-US, V29, P8093, DOI 10.1021/bi00487a015
   ROSENBERG IM, 1993, J BIOL CHEM, V268, P12393
   SAHIN U, 1995, P NATL ACAD SCI USA, V92, P11810, DOI 10.1073/pnas.92.25.11810
   SATO S, 1992, J BIOL CHEM, V267, P6983
   Saxen L., 1987, Organogenesis of the Kidney, DOI 10.1017/CBO9780511565083
   SHELNESS GS, 1988, J BIOL CHEM, V263, P17063
   SIDERS WM, 1993, J BIOL CHEM, V268, P22170
   SIEBERT PD, 1995, NUCLEIC ACIDS RES, V23, P1087, DOI 10.1093/nar/23.6.1087
   VARKI A, 1993, GLYCOBIOLOGY, V3, P97, DOI 10.1093/glycob/3.2.97
   Wada J, 1996, J CELL BIOL, V132, P1161, DOI 10.1083/jcb.132.6.1161
   WELLS V, 1991, CELL, V64, P91, DOI 10.1016/0092-8674(91)90211-G
   WHITNEY PL, 1986, BIOCHEM J, V238, P683, DOI 10.1042/bj2380683
NR 50
TC 301
Z9 352
U1 0
U2 14
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
SN 0021-9258
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD FEB 28
PY 1997
VL 272
IS 9
BP 6078
EP 6086
DI 10.1074/jbc.272.9.6078
PG 9
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA WK747
UT WOS:A1997WK74700101
PM 9038233
OA hybrid
DA 2025-04-10
ER

PT J
AU Hennessy, E
   O'Callaghan, J
   Mooij, MJ
   Legendre, C
   Camacho-Vanegas, O
   Camacho, SC
   Adams, C
   Martignetti, JA
   O'Gara, F
AF Hennessy, Emma
   O'Callaghan, Julie
   Mooij, Marlies J.
   Legendre, Claire
   Camacho-Vanegas, Olga
   Camacho, Sandra C.
   Adams, Claire
   Martignetti, John A.
   O'Gara, Fergal
TI The Impact of Simvastatin on Pulmonary Effectors of Pseudomonas
   aeruginosa Infection
SO PLOS ONE
LA English
DT Article
ID NITRIC-OXIDE SYNTHASE; KRUPPEL-LIKE FACTOR-2; COA REDUCTASE INHIBITORS;
   TUMOR-SUPPRESSOR GENE; EPITHELIAL-CELLS; IN-VITRO; TRANSCRIPTION FACTOR;
   ENDOTHELIAL-CELLS; PROSTATE-CANCER; HEPATOCELLULAR-CARCINOMA
AB The statin family of cholesterol-lowering drugs is known to have pleiotropic properties which include anti-inflammatory and immunomodulatory effects. Statins exert their pleiotropic effects by altering expression of human immune regulators including pro-inflammatory cytokines. Previously we found that statins modulate virulence phenotypes of the human pathogen Pseudomonas aeruginosa, and sought to investigate if simvastatin could alter the host response to this organism in lung epithelial cells. Simvastatin increased the expression of the P. aeruginosa target genes KLF2, KLF6, IL-8 and CCL20. Furthermore, both simvastatin and P. aeruginosa induced alternative splicing of KLF6. The novel effect of simvastatin on wtKLF6 expression was found to be responsible for induction of the KLF6 regulated genes CCL20 and iNOS. Simvastatin also increased the adhesion of P. aeruginosa to host cells, without altering invasion or cytotoxicity. This study demonstrated that simvastatin had several novel effects on the pulmonary cellular immune response.
C1 [Hennessy, Emma; O'Callaghan, Julie; Mooij, Marlies J.; Legendre, Claire; Adams, Claire; O'Gara, Fergal] Natl Univ Ireland, Sch Microbiol, BIOMERIT Res Ctr, Cork, Ireland.
   [Camacho-Vanegas, Olga; Camacho, Sandra C.; Martignetti, John A.] Icahn Sch Med Mt Sinai, Dept Genet & Genom Sci, New York, NY 10029 USA.
   [O'Gara, Fergal] Curtin Univ, Sch Biomed Sci, Perth, WA 6845, Australia.
C3 University College Cork; Icahn School of Medicine at Mount Sinai; Curtin
   University
RP O'Gara, F (corresponding author), Natl Univ Ireland, Sch Microbiol, BIOMERIT Res Ctr, Cork, Ireland.
EM f.ogara@ucc.ie
OI O'Gara, Fergal/0000-0002-2659-0673; Hennessy, Emma/0000-0003-0511-0797;
   Claire, LEGENDRE/0000-0003-0248-1111
FU European Commission [607786, CP-TP-312184, 311975, 287589, 256596];
   Science Foundation Ireland [SSPC-2, 07/IN.1/B948, 12/TIDA/B2411,
   12/TIDA/B2405, 09/RFP/BMT2350]; Department of Agriculture and Food
   (FIRM/RSF/CoFoRD) [FIRM 08/RDC/629]; Irish Research Council for Science,
   Engineering and Technology [PD/2011/2414, RS/2010/2413]; Health Research
   Board [RP/2006/271, RP/2007/290, HRA/2009/146]; Environmental Protection
   Agency [EPA2006-PhD-S-21, EPA2008-PhD-S-2]; Marine Institute [C2CRA
   2007/082]; Higher Education Authority of Ireland [PRTLI4]; Society For
   General Microbiology President's Fund for Research Visits; Science
   Foundation Ireland (SFI) [12/TIDA/B2405, 09/RFP/BMT2350, 07/IN.1/B948,
   12/TIDA/B2411] Funding Source: Science Foundation Ireland (SFI)
FX This research was supported in part by grants awarded by the European
   Commission (http://ec.europa.eu/index_en.htm)(FP7-PEOPLE-2013-ITN,
   607786; FP7-KBBE-2012-6, CP-TP-312184; FP7-KBBE-2012-6, 311975; OCEAN
   2011-2, 287589; Marie Curie 256596), Science Foundation Ireland
   (www.sfi.ie)(SSPC-2; 07/IN.1/B948; 12/TIDA/B2411; 12/TIDA/B2405;
   09/RFP/BMT2350), the Department of Agriculture and Food
   (www.agriculture.gov.ie/) (FIRM/RSF/CoFoRD; FIRM 08/RDC/629), the Irish
   Research Council for Science, Engineering and Technology
   (www.research.ie/) (PD/2011/2414; RS/2010/2413), the Health Research
   Board (www.hrb.ie)(RP/2006/271; RP/2007/290; HRA/2009/146), the
   Environmental Protection Agency (www.epa.ie) (EPA2006-PhD-S-21;
   EPA2008-PhD-S-2), the Marine Institute (https://www.marine.ie) (Beaufort
   award C2CRA 2007/082) Teagasc (www.teagasc.ie) (Walsh Fellowship 2013),
   the Higher Education Authority of Ireland (www.hea.ie)(PRTLI4) and the
   Society For General Microbiology President's Fund for Research Visits
   (www.sgm.ac.uk). The funders had no role in study design, data
   collection and analysis, decision to publish, or preparation of the
   manuscript.
CR Almog Y, 2004, CIRCULATION, V110, P880, DOI 10.1161/01.CIR.0000138932.17956.F1
   Bieker JJ, 2001, J BIOL CHEM, V276, P34355, DOI 10.1074/jbc.R100043200
   Bove PF, 2006, FREE RADICAL BIO MED, V41, P515, DOI 10.1016/j.freeradbiomed.2006.05.011
   Burns JL, 1996, INFECT IMMUN, V64, P4054, DOI 10.1128/IAI.64.10.4054-4059.1996
   Chalmers JD, 2008, AM J MED, V121, P1002, DOI 10.1016/j.amjmed.2008.06.030
   Coward WR, 2006, J IMMUNOL, V176, P5284, DOI 10.4049/jimmunol.176.9.5284
   Dach K, 2009, INFECT IMMUN, V77, P5583, DOI 10.1128/IAI.00121-09
   Darling KEA, 2003, INFECT IMMUN, V71, P2341, DOI 10.1128/IAI.71.5.2341-2349.2003
   Das H, 2006, P NATL ACAD SCI USA, V103, P6653, DOI 10.1073/pnas.0508235103
   Difeo A, 2008, CANCER RES, V68, P965, DOI 10.1158/0008-5472.CAN-07-2604
   Difeo A, 2006, CLIN CANCER RES, V12, P3730, DOI 10.1158/1078-0432.CCR-06-0054
   Difeo A, 2009, DRUG RESIST UPDATE, V12, P1, DOI 10.1016/j.drup.2008.11.001
   Dulak J, 2005, CURR CANCER DRUG TAR, V5, P579, DOI 10.2174/156800905774932824
   Edwards LA, 2011, PLOS ONE, V6, DOI 10.1371/journal.pone.0027030
   Erkkilä L, 2005, ANTIMICROB AGENTS CH, V49, P3959, DOI 10.1128/AAC.49.9.3959-3962.2005
   Gewirtz AT, 2001, J IMMUNOL, V167, P1882, DOI 10.4049/jimmunol.167.4.1882
   Grassmé H, 2003, NAT MED, V9, P322, DOI 10.1038/nm823
   Hayashi F, 2001, NATURE, V410, P1099, DOI 10.1038/35074106
   Hennessy E, 2013, J ANTIBIOT, V66, P99, DOI 10.1038/ja.2012.95
   Hernández-Perera O, 1998, J CLIN INVEST, V101, P2711, DOI 10.1172/JCI1500
   HOLLOWAY BW, 1979, MICROBIOL REV, V43, P73, DOI 10.1128/MMBR.43.1.73-102.1979
   Ito G, 2004, CANCER RES, V64, P3838, DOI 10.1158/0008-5472.CAN-04-0185
   Iwata A, 2012, CLIN EXP IMMUNOL, V168, P234, DOI 10.1111/j.1365-2249.2012.04564.x
   Jain MK, 2005, NAT REV DRUG DISCOV, V4, P977, DOI 10.1038/nrd1901
   Jendrossek V, 2001, INFECT IMMUN, V69, P2675, DOI 10.1128/IAI.69.4.2675-2683.2001
   Jouneau S, 2011, PLOS ONE, V6, DOI 10.1371/journal.pone.0022655
   Khan MA, 2008, INFECT IMMUN, V76, P1410, DOI 10.1128/IAI.01141-07
   Kiener PA, 2001, INT IMMUNOPHARMACOL, V1, P105, DOI 10.1016/S0162-3109(00)00272-1
   Kim TG, 2011, EXP DERMATOL, V20, P855, DOI 10.1111/j.1600-0625.2011.01343.x
   Kouroumichakis I, 2011, EUR J INTERN MED, V22, P125, DOI 10.1016/j.ejim.2010.12.004
   Kremer-Tal S, 2007, J HEPATOL, V46, P645, DOI 10.1016/j.jhep.2006.10.012
   LAW RE, 1992, MOL CELL BIOL, V12, P103, DOI 10.1128/MCB.12.1.103
   Lee VT, 2005, INFECT IMMUN, V73, P1695, DOI 10.1128/IAI.73.3.1695-1705.2005
   LEONARD S, 1990, J BIOL CHEM, V265, P5157
   Li CB, 2012, CLIN EXP PHARMACOL P, V39, P759, DOI 10.1111/j.1440-1681.2012.05730.x
   Lin TJ, 2003, INFECT IMMUN, V71, P365, DOI 10.1128/IAI.71.1.365-373.2003
   Mahabeleshwar GH, 2011, IMMUNITY, V34, P715, DOI 10.1016/j.immuni.2011.04.014
   Masamura K, 2003, ARTERIOSCL THROM VAS, V23, P512, DOI 10.1161/01.ATV.0000060461.64771.F0
   MASSION PP, 1994, J CLIN INVEST, V93, P26, DOI 10.1172/JCI116954
   Matsuda N, 2006, J PHARMACOL EXP THER, V319, P1348, DOI 10.1124/jpet.106.109785
   McGuffie EM, 1998, INFECT IMMUN, V66, P2607, DOI 10.1128/IAI.66.6.2607-2613.1998
   Mermis JD, 2012, CURR INFECT DIS REP, V14, P484, DOI 10.1007/s11908-012-0277-1
   Mgbemena V, 2013, CELL IMMUNOL, V283, P1, DOI 10.1016/j.cellimm.2013.06.002
   Mgbemena V, 2012, J IMMUNOL, V189, P606, DOI 10.4049/jimmunol.1102742
   Moreilhon C, 2005, PHYSIOL GENOMICS, V20, P244, DOI 10.1152/physiolgenomics.00135.2004
   Narla G, 2005, CANCER RES, V65, P5761, DOI 10.1158/0008-5472.CAN-05-0217
   Narla G, 2005, CANCER RES, V65, P1213, DOI 10.1158/0008-5472.CAN-04-4249
   Narla G, 2001, SCIENCE, V294, P2563, DOI 10.1126/science.1066326
   O'Grady E, 2007, NAT REV MICROBIOL, V5, P337, DOI 10.1038/nrmicro1641
   O'Grady EP, 2006, INFECT IMMUN, V74, P5893, DOI 10.1128/IAI.00489-06
   Parihar SP, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0075490
   Park JH, 2005, BBA-GENE STRUCT EXPR, V1732, P82, DOI 10.1016/j.bbaexp.2006.01.002
   Parker D, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0059932
   Qi WE, 2011, INT J BIOCHEM CELL B, V43, P383, DOI 10.1016/j.biocel.2010.11.008
   Quist-Paulsen P, 2010, CURR OPIN CARDIOL, V25, P399, DOI 10.1097/HCO.0b013e3283398e53
   Sauvonnet N, 2002, J BIOL CHEM, V277, P25133, DOI 10.1074/jbc.M203239200
   Schlienger RG, 2007, PHARMACOTHERAPY, V27, P325, DOI 10.1592/phco.27.3.325
   Sen-Banerjee S, 2005, CIRCULATION, V112, P720, DOI 10.1161/CIRCULATIONAHA.104.525774
   Teichgräber V, 2008, NAT MED, V14, P382, DOI 10.1038/nm1748
   Tuomisto TT, 2008, CARDIOVASC RES, V78, P175, DOI 10.1093/cvr/cvn007
   Urtasun R, 2012, ALCOHOL CLIN EXP RES, V36, P1851, DOI 10.1111/j.1530-0277.2012.01798.x
   Vetter D, 2012, HEPATOLOGY, V56, P1361, DOI 10.1002/hep.25810
   Warke VG, 2003, J BIOL CHEM, V278, P14812, DOI 10.1074/jbc.M300787200
   Yea S, 2008, GASTROENTEROLOGY, V134, P1521, DOI 10.1053/j.gastro.2008.02.015
   Zhang J, 2003, INVEST OPHTH VIS SCI, V44, P4247, DOI 10.1167/iovs.03-0219
NR 65
TC 8
Z9 8
U1 0
U2 0
PU PUBLIC LIBRARY SCIENCE
PI SAN FRANCISCO
PA 1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA
SN 1932-6203
J9 PLOS ONE
JI PLoS One
PD JUL 10
PY 2014
VL 9
IS 7
AR e102200
DI 10.1371/journal.pone.0102200
PG 12
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA AK9RG
UT WOS:000338763800081
PM 25010049
OA Green Published, gold, Green Submitted
DA 2025-04-10
ER

PT J
AU Gereben, B
   Salvatore, D
AF Gereben, B
   Salvatore, D
TI Pretranslational regulation of type 2 deiodinase
SO THYROID
LA English
DT Article
ID II IODOTHYRONINE DEIODINASE; MESSENGER-RIBONUCLEIC-ACID; PITUITARY-TUMOR
   CELLS; PROTEIN-KINASE-C; CARDIAC-SPECIFIC THYROTOXICOSIS; BROWN
   ADIPOSE-TISSUE; HEART TUBE FORMATION; TRANSCRIPTION FACTOR;
   THYROID-HORMONE; RAT-BRAIN
AB Type 2 deiodinase (D2) is a highly potent selenoenzyme that catalyzes the first step of thyroid hormone action and its expression is under close, multilevel control. D2 expression is tissue specific and can be regulated by transcriptional and posttranscriptional mechanisms. There is now compelling evidence that D2 is critically important in triiodothyronine (T3) homeostasis as well as in several biologic processes in which thyroid hormone is involved. A host of factors are known to influence dio2 mRNA including the transcription factors that regulate the dio2 gene in different cell types. In particular, cyclic adenosine monophosphate (CAMP) and two homeodomain-containing proteins are relevant for its defined and highly dynamic expression pattern. Single nucleotide polymorphisms of the dio2 gene and other pre-translational events such as alternative splicing can potentially modulate D2 expression and ultimately T-3 generation. Given the wealth of data accumulated over the past two decades, we have attempted in this review to provide a comprehensive update on the pre-translational regulation of D2.
C1 Univ Naples Federico II, Fac Med & Chirurg, Dept Endocrinol & Mol & Clin Oncol, I-80131 Naples, Italy.
   Hungarian Acad Sci, Inst Expt Med, Lab Endocrine Neurobiol, Budapest, Hungary.
C3 University of Naples Federico II; HUN-REN; HUN-REN Institute of
   Experimental Medicine; Hungarian Academy of Sciences
RP Univ Naples Federico II, Fac Med & Chirurg, Dept Endocrinol & Mol & Clin Oncol, Via S Pansini 5, I-80131 Naples, Italy.
EM domsalva@unina.it
RI Salvatore, Domenico/D-4881-2013
OI SALVATORE, DOMENICO/0000-0002-4556-7620
CR Ambroziak M, 2003, THYROID, V13, P141, DOI 10.1089/105072503321319440
   AMBROZIAK M, 2002, 28 ANN M EUR THYR AS, pP47
   AMBROZIAK M, 2004, 12 INT C END LISB PO, P851
   Araki O, 1999, CYTOGENET CELL GENET, V84, P73, DOI 10.1159/000015218
   Araki O, 2003, ENDOCRINOLOGY, V144, P4459, DOI 10.1210/en.2003-0419
   Araki O, 1998, LIFE SCI, V63, P1843, DOI 10.1016/S0024-3205(98)00471-8
   Bartha T, 2000, ENDOCRINOLOGY, V141, P229, DOI 10.1210/en.141.1.229
   Baumgartner A, 1998, J NEUROCHEM, V71, P817
   Baur A, 2000, J ENDOCRINOL, V167, P505, DOI 10.1677/joe.0.1670505
   Bianco AC, 2002, ENDOCR REV, V23, P38, DOI 10.1210/er.23.1.38
   Boelen A, 2004, J ENDOCRINOL, V182, P315, DOI 10.1677/joe.0.1820315
   Buettner C, 1998, J BIOL CHEM, V273, P33374, DOI 10.1074/jbc.273.50.33374
   Burmeister LA, 1997, ENDOCRINOLOGY, V138, P5231, DOI 10.1210/en.138.12.5231
   Campos-Barros A, 2000, P NATL ACAD SCI USA, V97, P1287, DOI 10.1073/pnas.97.3.1287
   Canettieri G, 2004, J MOL ENDOCRINOL, V33, P51, DOI 10.1677/jme.0.0330051
   Canettieri G, 2000, ENDOCRINOLOGY, V141, P1804, DOI 10.1210/en.141.5.1804
   Carvalho-Bianco SD, 2004, MOL ENDOCRINOL, V18, P1840, DOI 10.1210/me.2003-0125
   Celi FS, 1998, MOL CELL ENDOCRINOL, V141, P49, DOI 10.1016/S0303-7207(98)00093-8
   COURTIN F, 1989, ENDOCRINOLOGY, V125, P1277, DOI 10.1210/endo-125-3-1277
   Croteau W, 1996, J CLIN INVEST, V98, P405, DOI 10.1172/JCI118806
   Dentice M, 2003, MOL ENDOCRINOL, V17, P1508, DOI 10.1210/me.2002-0348
   Diano S, 1998, ENDOCRINOLOGY, V139, P2879, DOI 10.1210/en.139.6.2879
   DRUST DS, 1984, J BIOL CHEM, V259, P4520
   Fekete C, 2000, BRAIN RES, V862, P154, DOI 10.1016/S0006-8993(00)02105-3
   Fekete C, 2004, ENDOCRINOLOGY, V145, P1649, DOI 10.1210/en.2003-1439
   Galton VA, 1999, J CLIN INVEST, V103, P979, DOI 10.1172/JCI6073
   Galton VA, 2001, ENDOCRINOLOGY, V142, P2123, DOI 10.1210/en.142.5.2123
   Gereben B, 2000, MOL ENDOCRINOL, V14, P1697, DOI 10.1210/me.14.11.1697
   Gereben B, 2004, ENDOCRINOLOGY, V145, P3619, DOI 10.1210/en.2004-0229
   Gereben B, 2002, MOL ENDOCRINOL, V16, P1667, DOI 10.1210/me.16.7.1667
   Gereben B, 1999, J BIOL CHEM, V274, P13768, DOI 10.1074/jbc.274.20.13768
   Gereben B, 2001, MOL ENDOCRINOL, V15, P112, DOI 10.1210/me.15.1.112
   GUAZZI S, 1990, EMBO J, V9, P3631, DOI 10.1002/j.1460-2075.1990.tb07574.x
   Guo TW, 2004, J MED GENET, V41, P585, DOI 10.1136/jmg.2004.019190
   Hosoi Y, 1999, J CLIN ENDOCR METAB, V84, P3293, DOI 10.1210/jc.84.9.3293
   Imai Y, 2001, THYROID, V11, P899, DOI 10.1089/105072501753210957
   KADOBAYASHI T, 1999, 72 ANN M AM THYR ASS, P86
   Kamiya Y, 1999, ENDOCRINOLOGY, V140, P1272, DOI 10.1210/en.140.3.1272
   Kim SW, 1998, ENDOCRINOLOGY, V139, P4895, DOI 10.1210/en.139.12.4895
   KOENIG RJ, 1986, ENDOCRINOLOGY, V118, P1491, DOI 10.1210/endo-118-4-1491
   Kong WM, 2004, ENDOCRINOLOGY, V145, P5252, DOI 10.1210/en.2004-0545
   Kuo CT, 1997, GENE DEV, V11, P1048, DOI 10.1101/gad.11.8.1048
   Larsen P.Reed., 2003, WILLIAMS TXB ENDOCRI, V10th
   LAZZARO D, 1991, DEVELOPMENT, V113, P1093
   LEONARD JL, 1981, SCIENCE, V214, P571, DOI 10.1126/science.7291997
   LEONARD JL, 1988, BIOCHEM BIOPH RES CO, V151, P1164, DOI 10.1016/S0006-291X(88)80488-1
   Li WW, 2001, NEUROSCIENCE, V107, P507, DOI 10.1016/S0306-4522(01)00362-1
   LYONS I, 1995, GENE DEV, V9, P1654, DOI 10.1101/gad.9.13.1654
   Mentuccia D, 2002, DIABETES, V51, P880, DOI 10.2337/diabetes.51.3.880
   Mentuccia D., 2004, END SOC 86 ANN M NEW, pP3
   Molkentin JD, 1997, GENE DEV, V11, P1061, DOI 10.1101/gad.11.8.1061
   MORLEY JE, 1981, ENDOCR REV, V2, P396, DOI 10.1210/edrv-2-4-396
   Murakami M, 2001, ENDOCRINOLOGY, V142, P1195, DOI 10.1210/en.142.3.1195
   Nadeau S, 1999, NEUROSCIENCE, V93, P1449, DOI 10.1016/S0306-4522(99)00225-0
   Ohba KI, 2001, MOL CELL ENDOCRINOL, V172, P169, DOI 10.1016/S0303-7207(00)00368-3
   Orozco A, 2002, GEN COMP ENDOCR, V128, P162, DOI 10.1016/S0016-6480(02)00071-0
   Pachucki J, 2001, ENDOCRINOLOGY, V142, P13, DOI 10.1210/en.142.1.13
   Peeters R, 2001, AM J PHYSIOL-ENDOC M, V281, pE54, DOI 10.1152/ajpendo.2001.281.1.E54
   Peeters RP, 2003, J CLIN ENDOCR METAB, V88, P2880, DOI 10.1210/jc.2002-021592
   ROSS DS, 1987, METABOLISM, V36, P799, DOI 10.1016/0026-0495(87)90120-X
   Salvatore D, 1996, ENDOCRINOLOGY, V137, P3308, DOI 10.1210/en.137.8.3308
   Salvatore D, 1996, J CLIN INVEST, V98, P962, DOI 10.1172/JCI118880
   Schott JJ, 1998, SCIENCE, V281, P108, DOI 10.1126/science.281.5373.108
   SILVA JE, 1983, NATURE, V305, P712, DOI 10.1038/305712a0
   SILVA JE, 1982, J CLIN INVEST, V70, P1110, DOI 10.1172/JCI110699
   Smith PL, 2002, ISSI SCI RPT, V2, P21
   Song S, 2000, MOL CELL ENDOCRINOL, V165, P189, DOI 10.1016/S0303-7207(00)00246-X
   STGERMAIN DL, 1986, ENDOCRINOLOGY, V119, P840
   STGERMAIN DL, 1985, J CLIN INVEST, V76, P890, DOI 10.1172/JCI112049
   STGERMAIN DL, 1988, ENDOCRINOLOGY, V122, P1860, DOI 10.1210/endo-122-5-1860
   Tanaka M, 1999, DEVELOPMENT, V126, P1269
   Tu HM, 1997, ENDOCRINOLOGY, V138, P3359, DOI 10.1210/en.138.8.3359
   Van der Geyten S, 2001, MOL CELL ENDOCRINOL, V183, P1, DOI 10.1016/S0303-7207(01)00644-X
   Wasco EC, 2003, ENDOCRINOLOGY, V144, P4253, DOI 10.1210/en.2003-0490
   Watanabe M, 2004, ENDOCRINOLOGY, V145, P1546, DOI 10.1210/en.2003-1593
   Yoshimura T, 2003, NATURE, V426, P178, DOI 10.1038/nature02117
   ZANNINI M, 1992, MOL CELL BIOL, V12, P4230, DOI 10.1128/MCB.12.9.4230
   Zou LL, 1998, J NEUROCHEM, V71, P887
NR 78
TC 40
Z9 52
U1 0
U2 6
PU MARY ANN LIEBERT, INC
PI NEW ROCHELLE
PA 140 HUGUENOT STREET, 3RD FL, NEW ROCHELLE, NY 10801 USA
SN 1050-7256
EI 1557-9077
J9 THYROID
JI Thyroid
PD AUG
PY 2005
VL 15
IS 8
BP 855
EP 864
DI 10.1089/thy.2005.15.855
PG 10
WC Endocrinology & Metabolism
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism
GA 966TL
UT WOS:000232044700012
PM 16131328
DA 2025-04-10
ER

PT J
AU Endo-Umeda, K
   Uno, S
   Fujimori, K
   Naito, Y
   Saito, K
   Yamagishi, K
   Jeong, Y
   Miyachi, H
   Tokiwa, H
   Yamada, S
   Makishima, M
AF Endo-Umeda, Kaori
   Uno, Shigeyuki
   Fujimori, Ko
   Naito, Yoshikazu
   Saito, Koichi
   Yamagishi, Kenji
   Jeong, Yangsik
   Miyachi, Hiroyuki
   Tokiwa, Hiroaki
   Yamada, Sachiko
   Makishima, Makoto
TI Differential Expression and Function of Alternative Splicing Variants of
   Human Liver X Receptor α
SO MOLECULAR PHARMACOLOGY
LA English
DT Article
ID BILE-ACID METABOLISM; NUCLEAR RECEPTORS; CRYSTAL-STRUCTURE; LXR-ALPHA;
   GENE-EXPRESSION; IMMUNE-RESPONSE; MOLECULAR-BASIS; CANCER CELLS;
   PROLIFERATION; CHOLESTEROL
AB The liver X receptor alpha (LXR alpha) is a nuclear receptor that is involved in regulation of lipid metabolism, cellular proliferation and apoptosis, and immunity. In this report, we characterize three human LXR alpha isoforms with variation in the ligand-binding domain (LBD). While examining the expression of LXR alpha 3, which lacks 60 amino acids within the LBD, we identified two novel transcripts that encode LXR alpha-LBD variants (LXR alpha 4 and LXR alpha 5). LXR alpha 4 has an insertion of 64 amino acids in helix 4/5, and LXR alpha 5 lacks the C-terminal helices 7 to 12 due to a termination codon in an additional exon that encodes an intron in the LXR alpha 1 mRNA. LXR alpha 3, LXR alpha 4, and LXR alpha 5 were expressed at lower levels compared with LXR alpha 1 in many human tissues and cell lines. We also observed weak expression of LXR alpha 3 and LXR alpha 4 in several tissues of mice. LXR ligand treatment induced differential regulation of LXR alpha isoform mRNA expression in a cell type-dependent manner. Whereas LXR alpha 3 had no effect, LXR alpha 4 has weak transactivation, retinoid X receptor (RXR) heterodimerization, and coactivator recruitment activities. LXR alpha 5 interacted with a corepressor in a ligand-independent manner and inhibited LXR alpha 1 transactivation and target gene expression when overexpressed. Combination of LXR alpha 5 cotransfection and LXR alpha antagonist treatment produced additive effects on the inhibition of ligand-dependent LXR alpha 1 activation. We constructed structural models of the LXR alpha 4-LBD and its complexes with ligand, RXR-LBD, and coactivator peptide. The models showed that the insertion in the LBD can be predicted to disrupt RXR heterodimerization. Regulation of LXR alpha pre-mRNA splicing may be involved in the pathogenesis of LXR alpha-related diseases.
C1 [Makishima, Makoto] Nihon Univ, Dept Biomed Sci, Div Biochem, Sch Med,Itabashi Ku, Tokyo 1738610, Japan.
   [Fujimori, Ko] Osaka Univ Pharmaceut Sci, Lab Biodef & Regulat, Osaka 580, Japan.
   [Naito, Yoshikazu; Saito, Koichi] Sumitomo Chem Co Ltd, Environm Hlth Sci Lab, Osaka, Japan.
   [Yamagishi, Kenji] Rikkyo Univ, Fac Sci, Res Informat Ctr Extremophile, Tokyo 171, Japan.
   [Tokiwa, Hiroaki] Rikkyo Univ, Fac Sci, Dept Chem, Tokyo 171, Japan.
   [Jeong, Yangsik] Yonsei Univ, Wonju Coll Med, Dept Biochem, Inst Lifestyle Med, Gangwon Do, South Korea.
   [Jeong, Yangsik] Yonsei Univ, Wonju Coll Med, Nucl Receptor Res Consortium, Gangwon Do, South Korea.
   [Miyachi, Hiroyuki] Okayama Univ, Grad Sch Med Dent & Pharmaceut Sci, Okayama 7008530, Japan.
C3 Nihon University; Osaka Medical & Pharmaceutical University; Sumitomo
   Chem Co Ltd; Rikkyo University; Rikkyo University; Yonsei University;
   Yonsei University; Okayama University
RP Makishima, M (corresponding author), Nihon Univ, Dept Biomed Sci, Div Biochem, Sch Med,Itabashi Ku, 30-1 Oyaguchi Kamicho, Tokyo 1738610, Japan.
EM makishima.makoto@nihon-u.ac.jp
RI Fujimori, Ko/AAD-5428-2021; Jeong, Yangsik/AFQ-0172-2022
OI Saito, Koichi/0000-0001-6497-5286; Fujimori, Ko/0000-0002-2506-0769
FU Ministry of Education, Culture, Sports, Science, and Technology of Japan
   [18077005]; Grants-in-Aid for Scientific Research [18077005, 21570151]
   Funding Source: KAKEN
FX This work was supported in part by the Ministry of Education, Culture,
   Sports, Science, and Technology of Japan [Grant-in-Aid for Scientific
   Research on Priority Areas 18077005] (to M. M.).
CR Adachi R, 2004, MOL ENDOCRINOL, V18, P43, DOI 10.1210/me.2003-0244
   Bensinger SJ, 2008, CELL, V134, P97, DOI 10.1016/j.cell.2008.04.052
   Blaschke F, 2004, CIRC RES, V95, pE110, DOI 10.1161/01.RES.0000150368.56660.4f
   Chandra V, 2008, NATURE, V456, P350, DOI 10.1038/nature07413
   Chang YF, 2007, ANNU REV BIOCHEM, V76, P51, DOI 10.1146/annurev.biochem.76.050106.093909
   Chen MY, 2005, J LIPID RES, V46, P2570, DOI 10.1194/jlr.M500157-JLR200
   Cooper TA, 2009, CELL, V136, P777, DOI 10.1016/j.cell.2009.02.011
   Fukuchi J, 2004, CANCER RES, V64, P7686, DOI 10.1158/0008-5472.CAN-04-2332
   Gampe RT, 2000, MOL CELL, V5, P545, DOI 10.1016/S1097-2765(00)80448-7
   Inaba Y, 2007, MOL PHARMACOL, V71, P1298, DOI 10.1124/mol.106.032318
   Ishizawa M, 2008, J LIPID RES, V49, P763, DOI 10.1194/jlr.M700293-JLR200
   Joseph SB, 2004, CELL, V119, P299, DOI 10.1016/j.cell.2004.09.032
   Kaneko E, 2003, J BIOL CHEM, V278, P36091, DOI 10.1074/jbc.M304153200
   Laffitte BA, 2001, MOL CELL BIOL, V21, P7558, DOI 10.1128/MCB.21.22.7558-7568.2001
   Li Y, 2002, MOL ENDOCRINOL, V16, P506, DOI 10.1210/me.16.3.506
   Lu TT, 2000, MOL CELL, V6, P507, DOI 10.1016/S1097-2765(00)00050-2
   Makishima M, 2005, J PHARMACOL SCI, V97, P177, DOI 10.1254/jphs.FMJ04008X4
   Noguchi-Yachide T, 2007, BIOORG MED CHEM LETT, V17, P3957, DOI 10.1016/j.bmcl.2007.04.090
   Ou JF, 2001, P NATL ACAD SCI USA, V98, P6027, DOI 10.1073/pnas.111138698
   Peet DJ, 1998, CELL, V93, P693, DOI 10.1016/S0092-8674(00)81432-4
   Repa JJ, 2002, NAT MED, V8, P1243, DOI 10.1038/nm1102-1243
   Repa JJ, 2000, SCIENCE, V289, P1524, DOI 10.1126/science.289.5484.1524
   Rosenfeld MG, 2006, GENE DEV, V20, P1405, DOI 10.1101/gad.1424806
   Schultz JR, 2000, GENE DEV, V14, P2831, DOI 10.1101/gad.850400
   Shin C, 2004, NAT REV MOL CELL BIO, V5, P727, DOI 10.1038/nrm1467
   Spencer TA, 2001, J MED CHEM, V44, P886, DOI 10.1021/jm0004749
   Svensson S, 2003, EMBO J, V22, P4625, DOI 10.1093/emboj/cdg456
   Tontonoz P, 2003, MOL ENDOCRINOL, V17, P985, DOI 10.1210/me.2003-0061
   Uno S, 2009, BIOCHEM PHARMACOL, V77, P186, DOI 10.1016/j.bcp.2008.10.007
   Valledor AF, 2004, P NATL ACAD SCI USA, V101, P17813, DOI 10.1073/pnas.0407749101
   Vedin LL, 2009, CARCINOGENESIS, V30, P575, DOI 10.1093/carcin/bgp029
   Wahl MC, 2009, CELL, V136, P701, DOI 10.1016/j.cell.2009.02.009
   Williams S, 2003, J BIOL CHEM, V278, P27138, DOI 10.1074/jbc.M302260200
   WILLY PJ, 1995, GENE DEV, V9, P1033, DOI 10.1101/gad.9.9.1033
   Yoshikawa T, 2001, MOL CELL BIOL, V21, P2991, DOI 10.1128/MCB.21.9.2991-3000.2001
NR 35
TC 23
Z9 27
U1 0
U2 8
PU AMER SOC PHARMACOLOGY EXPERIMENTAL THERAPEUTICS
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3995 USA
SN 0026-895X
J9 MOL PHARMACOL
JI Mol. Pharmacol.
PD JUN
PY 2012
VL 81
IS 6
BP 800
EP 810
DI 10.1124/mol.111.077206
PG 11
WC Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Pharmacology & Pharmacy
GA 961MW
UT WOS:000305469500005
PM 22399489
DA 2025-04-10
ER

PT J
AU Stennard, FA
   Costa, MW
   Elliott, DA
   Rankin, S
   Haast, SJP
   Lai, D
   McDonald, LPA
   Niederreither, K
   Dolle, P
   Bruneau, BG
   Zorn, AM
   Harvey, RP
AF Stennard, FA
   Costa, MW
   Elliott, DA
   Rankin, S
   Haast, SJP
   Lai, D
   McDonald, LPA
   Niederreither, K
   Dolle, P
   Bruneau, BG
   Zorn, AM
   Harvey, RP
TI Cardiac T-box factor Tbx20 directly interacts with Nkx2-5, GATA4, and
   GATA5 in regulation of gene expression in the developing heart
SO DEVELOPMENTAL BIOLOGY
LA English
DT Review
DE T-box; Tbx20; Tbx5; Tbx genes; Nkx2-5; GATA; heart development;
   embryonic development; transcription factor; Xenopus; cell migration
ID HOLT-ORAM-SYNDROME; TRANSCRIPTION FACTOR; HOMEOBOX GENES; MESODERM
   FORMATION; MATERNAL VEGT; DNA-BINDING; BRACHYURY; PROTEIN; MUTATIONS;
   XENOPUS
AB Tbx20 is a member of the T-box transcription factor family expressed in the forming hearts of vertebrate and invertebrate embryos. We report here analysis of Tbx20 expression during murine cardiac development and assessment of DNA-binding and transcriptional properties of Tbx20 isoforms. Tbx20 was expressed in myocardium and endocardium, including high levels in endocardial cushions. cDNAs generated by alternative splicing encode at least four Tbx20 isoforms, and Tbx20a uniquely carried strong transactivation and transrepression domains in its C terminus. Isoforms with an intact T-box bound specifically to DNA sites resembling the consensus brachyury half site, although with less avidity compared with the related factor, Tbx5. Tbx20 physically interacted with cardiac transcription factors Nkx2-5, GATA4, and GATA5, collaborating to synergistically activate cardiac gene expression. Among cardiac GATA factors, there was preferential synergy with GATA5, implicated in endocardial differentiation. In Xenopus embryos, enforced expression of Tbx20a, but not Tbx20b, led to induction of mesodermal and endodermal lineage markers as well as cell migration, indicating that the long Tbx20a isoform uniquely bears functional domains that can alter gene expression and developmental behaviour in an in vivo context. We propose that Tbx20 plays an integrated role in the ancient myogenic program of the heart, and has been additionally coopted during evolution of vertebrates for endocardial cushion development. (C) 2003 Elsevier Inc. All rights reserved.
C1 Victor Chang Cardiac Res Inst, Sydney, NSW 2010, Australia.
   Childrens Hosp, Med Ctr, Div Dev Biol, Cincinnati, OH 45229 USA.
   Univ Amsterdam, Acad Med Ctr, Dept Anat & Embryol, NL-1105 AZ Amsterdam, Netherlands.
   Baylor Coll Med, Ctr Cardiovasc Dev, Dept Med, Houston, TX 77030 USA.
   Baylor Coll Med, Ctr Cardiovasc Dev, Dept Mol & Cellular Biol, Houston, TX 77030 USA.
   Coll France, ULP, Inst Genet & Biol Mol & Cellulaire, CNRS,INSERM, F-67404 Illkirch Graffenstaden, CU Strasbourg, France.
   Hosp Sick Children, Programme Cardiovasc Res, Toronto, ON M5G 1X8, Canada.
   Hosp Sick Children, Programme Dev Biol, Toronto, ON M5G 1X8, Canada.
   Univ Toronto, Dept Mol & Med Genet, Toronto, ON M5G 1X8, Canada.
   Univ New S Wales, Fac Med, Kensington, NSW 2052, Australia.
   Univ New S Wales, Fac Life Sci, Kensington, NSW 2052, Australia.
C3 Victor Chang Cardiac Research Institute; Cincinnati Children's Hospital
   Medical Center; University of Amsterdam; Academic Medical Center
   Amsterdam; Baylor College of Medicine; Baylor College of Medicine;
   Institut National de la Sante et de la Recherche Medicale (Inserm);
   Centre National de la Recherche Scientifique (CNRS); Universite PSL;
   College de France; Universites de Strasbourg Etablissements Associes;
   Universite de Strasbourg; University of Toronto; Hospital for Sick
   Children (SickKids); University of Toronto; Hospital for Sick Children
   (SickKids); University of Toronto; University of New South Wales Sydney;
   University of New South Wales Sydney
RP Victor Chang Cardiac Res Inst, 384 Victoria St, Sydney, NSW 2010, Australia.
EM r.harvey@victorchang.unsw.edu.au
RI Dolle, Pascal/A-8037-2010; Costa, Mauro/S-9219-2018; Elliott,
   David/H-3334-2012
OI Dolle, Pascal/0000-0002-9294-9090; Bruneau, Benoit/0000-0002-0804-7597;
   Costa, Mauro/0000-0003-3579-8625; Harvey, Richard/0000-0002-9950-9792;
   Zorn, Aaron/0000-0003-3217-3590; Elliott, David/0000-0003-1052-7407
FU NICHD NIH HHS [R01 HD042572, HD042572-01] Funding Source: Medline
CR ARCECI RJ, 1993, MOL CELL BIOL, V13, P2235, DOI 10.1128/MCB.13.4.2235
   Ausubel F.M., 1996, CURRENT PROTOCOLS MO, V2, p9.11.11
   Basson CT, 1997, NAT GENET, V15, P30, DOI 10.1038/ng0197-30
   Biben C, 1997, COLD SPRING HARB SYM, V62, P395, DOI 10.1101/SQB.1997.062.01.047
   Biben C, 1997, GENE DEV, V11, P1357, DOI 10.1101/gad.11.11.1357
   Bodmer R, 1998, DEV GENET, V22, P181, DOI 10.1002/(SICI)1520-6408(1998)22:3<181::AID-DVG1>3.0.CO;2-2
   Brown J, 2000, MT RES DEV, V20, P212, DOI 10.1659/0276-4741(2000)020[0212:CANITP]2.0.CO;2
   Bruneau BG, 1999, DEV BIOL, V211, P100, DOI 10.1006/dbio.1999.9298
   Bruneau BG, 2001, CELL, V106, P709, DOI 10.1016/S0092-8674(01)00493-7
   Carreira S, 1998, MOL CELL BIOL, V18, P5099, DOI 10.1128/MCB.18.9.5099
   Carson CT, 2000, MECH DEVELOP, V96, P137, DOI 10.1016/S0925-4773(00)00376-2
   Casey ES, 1998, DEVELOPMENT, V125, P3887
   Chapman DL, 1998, NATURE, V391, P695, DOI 10.1038/35624
   Charron F, 1999, SEMIN CELL DEV BIOL, V10, P85, DOI 10.1006/scdb.1998.0281
   Chen CY, 1996, MOL CELL BIOL, V16, P6372
   Chen F, 2002, CELL, V110, P713, DOI 10.1016/S0092-8674(02)00932-7
   CHEN WS, 1995, ONCOL REP, V2, P5
   Christoffels VM, 2000, DEV BIOL, V223, P266, DOI 10.1006/dbio.2000.9753
   Ciruna B, 2001, DEV CELL, V1, P37, DOI 10.1016/S1534-5807(01)00017-X
   Clamp M, 2003, NUCLEIC ACIDS RES, V31, P38, DOI 10.1093/nar/gkg083
   Coll M, 2002, STRUCTURE, V10, P343, DOI 10.1016/S0969-2126(02)00722-0
   Conlon FL, 2001, DEVELOPMENT, V128, P3749
   Cripps RM, 2002, DEV BIOL, V246, P14, DOI 10.1006/dbio.2002.0666
   CUNLIFFE V, 1992, NATURE, V358, P427, DOI 10.1038/358427a0
   Delorme B, 1997, CIRC RES, V81, P423, DOI 10.1161/01.RES.81.3.423
   Durocher D, 1996, MOL CELL BIOL, V16, P4648, DOI 10.1128/mcb.16.9.4648
   Durocher D, 1997, EMBO J, V16, P5687, DOI 10.1093/emboj/16.18.5687
   ELLIOTT DA, 2003, IN PRESS J AM COLL C
   Engleka MJ, 2001, DEV BIOL, V237, P159, DOI 10.1006/dbio.2001.0366
   Ghosh TK, 2001, HUM MOL GENET, V10, P1983, DOI 10.1093/hmg/10.18.1983
   GibsonBrown JJ, 1996, MECH DEVELOP, V56, P93, DOI 10.1016/0925-4773(96)00514-X
   Goldmuntz E, 2001, CIRCULATION, V104, P2565, DOI 10.1161/hc4601.098427
   Griffin KJP, 2000, DEV BIOL, V218, P235, DOI 10.1006/dbio.1999.9571
   Griffin KJP, 1998, DEVELOPMENT, V125, P3379
   Grow MW, 1998, DEV BIOL, V204, P187, DOI 10.1006/dbio.1998.9080
   Habets PEMH, 2002, GENE DEV, V16, P1234, DOI 10.1101/gad.222902
   Harvey R.P., 2002, MOL DETERMINANTS CAR, P331
   Harvey RP, 1996, DEV BIOL, V178, P203, DOI 10.1006/dbio.1996.0212
   Harvey RP, 1999, HEART DEV, P111
   Hatcher CJ, 2000, DEV DYNAM, V219, P90, DOI 10.1002/1097-0177(200009)219:1<90::AID-DVDY1033>3.0.CO;2-L
   Hatcher CJ, 2001, DEV BIOL, V230, P177, DOI 10.1006/dbio.2000.0134
   He ML, 1999, P NATL ACAD SCI USA, V96, P10212, DOI 10.1073/pnas.96.18.10212
   Hiroi Y, 2001, NAT GENET, V28, P276, DOI 10.1038/90123
   Horb ME, 1999, DEVELOPMENT, V126, P1739
   Hsueh YP, 2000, NATURE, V404, P298, DOI 10.1038/35005118
   Isaac A, 1998, DEVELOPMENT, V125, P1867
   Jerome LA, 2001, NAT GENET, V27, P286, DOI 10.1038/85845
   Jeyaseelan R, 1997, J BIOL CHEM, V272, P22800, DOI 10.1074/jbc.272.36.22800
   Kasahara H, 2000, J CLIN INVEST, V106, P299, DOI 10.1172/JCI9860
   Kasahara H, 1998, CIRC RES, V82, P936, DOI 10.1161/01.RES.82.9.936
   Kasahara H, 2001, J BIOL CHEM, V276, P4570, DOI 10.1074/jbc.M004995200
   Kelly RG, 2002, TRENDS GENET, V18, P210, DOI 10.1016/S0168-9525(02)02642-2
   KISPERT A, 1995, EMBO J, V14, P4763, DOI 10.1002/j.1460-2075.1995.tb00158.x
   KISPERT A, 1993, EMBO J, V12, P3211, DOI 10.1002/j.1460-2075.1993.tb05990.x
   Kofron M, 1999, DEVELOPMENT, V126, P5759
   Koshiba-Takeuchi K, 2000, SCIENCE, V287, P134, DOI 10.1126/science.287.5450.134
   Kraus F, 2001, MECH DEVELOP, V100, P87, DOI 10.1016/S0925-4773(00)00499-8
   Kraus F, 2001, MECH DEVELOP, V100, P83, DOI 10.1016/S0925-4773(00)00494-9
   Lee Y, 1998, MOL CELL BIOL, V18, P3120, DOI 10.1128/MCB.18.6.3120
   Lei EP, 2002, DEV CELL, V2, P261, DOI 10.1016/S1534-5807(02)00134-X
   Li QY, 1997, NAT GENET, V15, P21
   Liberatore CM, 2000, DEV BIOL, V223, P169, DOI 10.1006/dbio.2000.9748
   Lindsay EA, 2001, NATURE, V410, P97, DOI 10.1038/35065105
   Logan M, 1999, SCIENCE, V283, P1736, DOI 10.1126/science.283.5408.1736
   LYONS I, 1995, GENE DEV, V9, P1654, DOI 10.1101/gad.9.13.1654
   Mattaj IW, 1998, ANNU REV BIOCHEM, V67, P265, DOI 10.1146/annurev.biochem.67.1.265
   Meins M, 2000, GENOMICS, V67, P317, DOI 10.1006/geno.2000.6249
   Merscher S, 2001, CELL, V104, P619, DOI 10.1016/S0092-8674(01)00247-1
   Moorman AFM, 1998, CIRC RES, V82, P629, DOI 10.1161/01.RES.82.6.629
   Morin S, 2001, MOL CELL BIOL, V21, P1036, DOI 10.1128/MCB.21.4.1036-1044.2001
   Muller CW, 1997, NATURE, V389, P884, DOI 10.1038/39929
   Nakajima Y, 2000, ANAT RECORD, V258, P119, DOI 10.1002/(SICI)1097-0185(20000201)258:2<119::AID-AR1>3.0.CO;2-U
   Nemer G, 2002, DEVELOPMENT, V129, P4045
   Niederreither K, 2001, DEVELOPMENT, V128, P1019
   Packham EA, 2003, HUM MOL GENET, V12, pR37, DOI 10.1093/hmg/ddg077
   Palmer S, 2001, J CELL BIOL, V153, P985, DOI 10.1083/jcb.153.5.985
   Papaioannou VE, 1998, BIOESSAYS, V20, P9, DOI 10.1002/(SICI)1521-1878(199801)20:1<9::AID-BIES4>3.0.CO;2-Q
   Pasumarthi KBS, 2002, CIRC RES, V90, P1044, DOI 10.1161/01.RES.0000020201.44772.67
   Paxton C, 2002, GENE, V283, P117, DOI 10.1016/S0378-1119(01)00878-2
   Prall OWJ, 2002, ANN MED, V34, P148
   Ranganayakulu G, 1998, DEVELOPMENT, V125, P3037
   Redkar A, 2001, DEVELOPMENT, V128, P2269
   Ross SA, 2000, PHYSIOL REV, V80, P1021, DOI 10.1152/physrev.2000.80.3.1021
   Russ AP, 2000, NATURE, V404, P95, DOI 10.1038/35003601
   SADOWSKI I, 1989, NUCLEIC ACIDS RES, V17, P7539, DOI 10.1093/nar/17.18.7539
   SETH A, 1992, J BIOL CHEM, V267, P24796
   Shiojima I, 1999, J BIOL CHEM, V274, P8231, DOI 10.1074/jbc.274.12.8231
   Sinha S, 2000, GENE, V258, P15, DOI 10.1016/S0378-1119(00)00417-0
   Smith J, 1999, TRENDS GENET, V15, P154, DOI 10.1016/S0168-9525(99)01693-5
   Stennard F, 1996, DEVELOPMENT, V122, P4179
   Szeto DP, 2002, DEVELOPMENT, V129, P5093
   Tada M, 2000, DEVELOPMENT, V127, P2227
   Takeuchi JK, 1999, NATURE, V398, P810, DOI 10.1038/19762
   Tanaka M, 1999, DEVELOPMENT, V126, P1269
   van den Hoff MJB, 1999, DEV BIOL, V212, P477, DOI 10.1006/dbio.1999.9366
   Vaughan CJ, 2000, AM J MED GENET, V97, P304, DOI 10.1002/1096-8628(200024)97:4<304::AID-AJMG1281>3.0.CO;2-#
   Watada H, 2000, P NATL ACAD SCI USA, V97, P9443, DOI 10.1073/pnas.97.17.9443
   Webb S, 1998, CIRC RES, V82, P645, DOI 10.1161/01.RES.82.6.645
   Wolberger C, 1999, ANNU REV BIOPH BIOM, V28, P29, DOI 10.1146/annurev.biophys.28.1.29
   Xanthos JB, 2001, DEVELOPMENT, V128, P167
   Yamamoto A, 1998, DEVELOPMENT, V125, P3389
   Zaffran S, 2002, CIRC RES, V91, P457, DOI 10.1161/01.RES.0000034152.74523.A8
   Zou YM, 1997, DEVELOPMENT, V124, P793
NR 103
TC 228
Z9 282
U1 0
U2 31
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0012-1606
EI 1095-564X
J9 DEV BIOL
JI Dev. Biol.
PD OCT 15
PY 2003
VL 262
IS 2
BP 206
EP 224
DI 10.1016/S0012-1606(03)00385-3
PG 19
WC Developmental Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Developmental Biology
GA 733RC
UT WOS:000186013600002
PM 14550786
DA 2025-04-10
ER

PT J
AU Misquitta, CM
   Ghosh, P
   Mwanjewe, J
   Grover, AK
AF Misquitta, CM
   Ghosh, P
   Mwanjewe, J
   Grover, AK
TI Role of cis-acting elements in the control of SERCA2b
   Ca<SUP>2+</SUP> pump mRNA decay by nuclear proteins
SO BIOCHEMICAL JOURNAL
LA English
DT Article
DE ATPase; calcium pump; nuclear protein; RNA stability; SERCA2b;
   Y-untranslated region
ID A+U-RICH ELEMENTS; MAMMALIAN-CELLS; SMOOTH-MUSCLE; C-FOS; STABILITY;
   DEGRADATION; TRANSLATION; REGION; DESTABILIZATION; EUKARYOTES
AB Alternative splicing at position 3495 b yields SERCA2 (sarco/endoplasmic reticulum Ca2+ pump 2) RNA species, namely SERCA2a and SERCA2b which differ in 3'-end regions. This results in SERCA2b RNA being less stable. In vitro decay experiments show that, in the presence of protein extracts from nuclei of LVMs (left ventricular myocytes), the rate of decay of both SERCA2b RNA and synthetic RNA from its 3'-region is greater than that of the corresponding SERCA2a RNA. To search for cis-acting instability elements in the 3'-region of SERCA2b, we examined the effects of LVM nuclear protein extracts on the in vitro decay of six short overlapping capped [m(7)G(5')ppp(5')Gm] and polyadenylated (A(40)) RNA fragments from the 3'-end region (3444-4472) of SERCA2b. The proximal fragment 2B1 (3444-3753) was the most unstable. 213 1 RNA without a cap or a polyadenylated tail was analysed further in electrophoretic mobility-shift assays, and was observed to bind to protein(s) in the nuclear extracts. Based on competition for binding to nuclear proteins between radiolabelled 2B1 RNA and short unlabelled RNA fragments, the cis-acting element involved in this binding was the sequence 2B1-4.2B1-4 is a 35-base (3521-3555, CCAGUCCUGCUCGUUGUGGGCGUGCACCGAGGGGG) GC-rich region just past the splice site (3495). Nuclear extracts decreased the electrophoretic mobility of the radiolabelled 2B1-4 RNA which bound to two proteins (19 and 21 kDa) in cross-linking experiments. Excess 2B1-4 RNA decreased the decay of the 2B1 RNA by the nuclear protein extract. 2B1-del 4 RNA (2B1 with the 2B1-4 domain deleted) also decayed more slowly than the control 2B1 RNA. Thus SERCA2b contains a novel GC-rich cis-acting element involved in its decay by nuclear proteins.
C1 McMaster Univ, Dept Biol, Hamilton, ON L8N 3Z5, Canada.
   McMaster Univ, Dept Med, Hamilton, ON L8N 3Z5, Canada.
C3 McMaster University; McMaster University
RP McMaster Univ, Dept Biol, HSC 4N41,1200 Main St W, Hamilton, ON L8N 3Z5, Canada.
EM groverak@mcmaster.ca
CR AHARON T, 1993, MOL CELL BIOL, V13, P1971, DOI 10.1128/MCB.13.3.1971
   BRAWERMAN G, 1989, CELL, V57, P9, DOI 10.1016/0092-8674(89)90166-9
   BREWER G, 1990, METHOD ENZYMOL, V181, P202
   Buzby JS, 1999, J BIOL CHEM, V274, P33973, DOI 10.1074/jbc.274.48.33973
   CHEN CYA, 1995, MOL CELL BIOL, V15, P5777
   CHEN CYA, 1995, TRENDS BIOCHEM SCI, V20, P465, DOI 10.1016/S0968-0004(00)89102-1
   CLAPHAM DE, 1995, CELL, V80, P259, DOI 10.1016/0092-8674(95)90408-5
   DeMaria CT, 1996, J BIOL CHEM, V271, P12179, DOI 10.1074/jbc.271.21.12179
   Dode L, 1996, BIOCHEM J, V318, P689, DOI 10.1042/bj3180689
   East JM, 2000, MOL MEMBR BIOL, V17, P189, DOI 10.1080/09687680010009646
   EGGERMONT JA, 1991, BIOCHIM BIOPHYS ACTA, V1088, P448, DOI 10.1016/0167-4781(91)90143-A
   Fan XHC, 1997, GENE DEV, V11, P2557, DOI 10.1101/gad.11.19.2557
   Fan XHC, 1998, EMBO J, V17, P3448, DOI 10.1093/emboj/17.12.3448
   KHAN I, 1990, BIOCHEM J, V268, P415, DOI 10.1042/bj2680415
   LYTTON J, 1989, J BIOL CHEM, V264, P7059
   Misquitta CM, 1999, CELL CALCIUM, V25, P277, DOI 10.1054/ceca.1999.0032
   Misquitta CM, 2002, AM J PHYSIOL-CELL PH, V283, pC560, DOI 10.1152/ajpcell.00527.2001
   Misquitta CM, 2001, MOL CELL BIOCHEM, V224, P53, DOI 10.1023/A:1011982932645
   Moore MJ, 2002, CELL, V108, P431, DOI 10.1016/S0092-8674(02)00645-1
   Pande A, 1996, J BIOL CHEM, V271, P8493, DOI 10.1074/jbc.271.14.8493
   Pennisi E, 1998, SCIENCE, V279, P1129, DOI 10.1126/science.279.5354.1129
   PIECHACZYK M, 1988, GENE, V72, P287, DOI 10.1016/0378-1119(88)90154-0
   Ross J, 1997, BIOESSAYS, V19, P527, DOI 10.1002/bies.950190612
   Ross J, 1996, TRENDS GENET, V12, P171, DOI 10.1016/0168-9525(96)10016-0
   ROSS J, 1995, MICROBIOL REV, V59, P423, DOI 10.1128/MMBR.59.3.423-450.1995
   SACHS AB, 1993, CELL, V74, P413, DOI 10.1016/0092-8674(93)80043-E
   SAVANTBHONSALE S, 1992, GENE DEV, V6, P1927, DOI 10.1101/gad.6.10.1927
   Wilson GM, 1999, J BIOL CHEM, V274, P33374, DOI 10.1074/jbc.274.47.33374
   Wilson GM, 1999, METHODS, V17, P74, DOI 10.1006/meth.1998.0709
   Wilson GM, 1999, PROG NUCLEIC ACID RE, V62, P257
NR 30
TC 6
Z9 6
U1 0
U2 1
PU PORTLAND PRESS LTD
PI LONDON
PA CHARLES DARWIN HOUSE, 12 ROGER STREET, LONDON WC1N 2JU, ENGLAND
SN 0264-6021
EI 1470-8728
J9 BIOCHEM J
JI Biochem. J.
PD MAY 15
PY 2005
VL 388
BP 291
EP 297
DI 10.1042/BJ20041568
PN 1
PG 7
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 931DA
UT WOS:000229464800032
PM 15656788
OA Green Published
DA 2025-04-10
ER

PT J
AU Wang, C
   JeBailey, L
   Ridgway, ND
AF Wang, C
   JeBailey, L
   Ridgway, ND
TI Oxysterol-binding-protein (OSBP)-related protein 4 binds
   25-hydroxycholesterol and interacts with vimentin intermediate filaments
SO BIOCHEMICAL JOURNAL
LA English
DT Article
DE cholesterol esterification; mRNA alternative splicing; tissue expression
ID HAMSTER OVARY CELLS; LOW-DENSITY-LIPOPROTEIN; GOLGI LOCALIZATION;
   LIPID-METABOLISM; CHOLESTEROL; HOMOLOGY; PHOSPHORYLATION; SPHINGOMYELIN;
   GLYCOSPHINGOLIPIDS; ASSOCIATION
AB Oxysterol-binding protein (OSBP) is the prototypical member of a class of phospholipid and oxysterol-binding proteins that interacts with the Golgi apparatus and regulates lipid and cholesterol metabolism. As a result of recent sequencing efforts, eleven other OSBP-related proteins (ORPs) have been identified in humans. We have investigated the structure, oxysterol-binding activity, cellular localization and function of ORP4 (also designated OSBP2 or HLM), a homologue that shares the highest degree of similarity with OSBP. Two ORP4 cDNAs were identified: a full-length ORP4 containing a pleckstrin homology (PH) domain and an oxysterol-binding region (designated ORP4-L), and a splice variant in which the PH domain and part of the oxysterol-binding domain were deleted (designated ORP4-S). ORP4 mRNA and protein expression overlapped partially with OSBP and were restricted to brain, heart, muscle and kidney. Like OSBP, ORP4-L bound [H-3]25-hydroxycholesterol with high affinity and specificity. In contrast, ORP4-S did not bind [H-3]25-hydroxycholesterol or [H-3]7-ketocholesterol. Immunofluorescence localization in stably transfected Chinese hamster ovary cells showed that ORP4-S co-localized with vimentin and caused the intermediate filament network to bundle or aggregate. ORP4-L displayed a diffuse staining pattern that did not overlap with vimentin except when the microtubule network was disrupted with nocodazole. Oxysterols had no effect on the localization of either ORP4. Cells overexpressing ORP4-S had a 40% reduction in the esterification of low-density-lipoprotein-derived cholesterol, demonstrating that ORP4 interaction with intermediate filaments inhibits an intracellular cholesterol-transport pathway mediated by vimentin. These studies elucidate a hitherto unknown relationship between OSBPs and the intermediate filament network that influences cholesterol transport.
C1 Dalhousie Univ, Dept Pediat, Atlantic Res Ctr, Halifax, NS B3H 4H7, Canada.
   Dalhousie Univ, Dept Biochem & Mol Biol, Halifax, NS B3H 4H7, Canada.
C3 Dalhousie University; Dalhousie University
RP Dalhousie Univ, Dept Pediat, Atlantic Res Ctr, Halifax, NS B3H 4H7, Canada.
EM nridgway@is.dal.ca
OI Ridgway, Neale/0000-0002-0441-6228
CR Beh CT, 2001, GENETICS, V157, P1117
   Chou YH, 1997, CURR OPIN CELL BIOL, V9, P49, DOI 10.1016/S0955-0674(97)80151-2
   COLUCCIGUYON E, 1994, CELL, V79, P679, DOI 10.1016/0092-8674(94)90553-3
   Daum G, 1999, YEAST, V15, P601, DOI 10.1002/(SICI)1097-0061(199905)15:7<601::AID-YEA390>3.0.CO;2-N
   DAWSON PA, 1989, J BIOL CHEM, V264, P16798
   Dunham I, 1999, NATURE, V402, P489, DOI 10.1038/990031
   Eckes B, 1998, J CELL SCI, V111, P1897
   ESSER V, 1988, J BIOL CHEM, V263, P13282
   Faigle W, 2000, MOL BIOL CELL, V11, P3485, DOI 10.1091/mbc.11.10.3485
   Fang M, 1998, BBA-MOL CELL RES, V1404, P85, DOI 10.1016/S0167-4889(98)00049-4
   Fang M, 1996, EMBO J, V15, P6447, DOI 10.1002/j.1460-2075.1996.tb01036.x
   FOURIER MV, 1999, CANCER RES, V59, P1748
   FUCHS E, 1994, ANNU REV BIOCHEM, V63, P345, DOI 10.1146/annurev.bi.63.070194.002021
   Gao YS, 2001, J CELL BIOL, V152, P877, DOI 10.1083/jcb.152.5.877
   Gillard BK, 1998, EXP CELL RES, V242, P561, DOI 10.1006/excr.1998.4126
   GILLARD BK, 1994, J CELL SCI, V107, P3545
   GOLDSTEIN JL, 1983, METHOD ENZYMOL, V98, P241
   GURLAND G, 1995, J CELL BIOL, V131, P1275, DOI 10.1083/jcb.131.5.1275
   Holwell TA, 1999, J LIPID RES, V40, P1440
   JIANG B, 1994, YEAST, V10, P341, DOI 10.1002/yea.320100307
   KANDUTSCH AA, 1980, J BIOL CHEM, V255, P813
   KANDUTSCH AA, 1981, J BIOL CHEM, V256, P3068
   Lagace TA, 1997, BIOCHEM J, V326, P205, DOI 10.1042/bj3260205
   Lagace TA, 1999, J LIPID RES, V40, P109
   Lehto M, 2001, J LIPID RES, V42, P1203
   Levine TP, 1998, CURR BIOL, V8, P729, DOI 10.1016/S0960-9822(98)70296-9
   LIN JJC, 1981, CELL, V24, P185, DOI 10.1016/0092-8674(81)90514-6
   Liscum L, 1999, BBA-MOL CELL BIOL L, V1438, P19, DOI 10.1016/S1388-1981(99)00043-8
   Mohammadi A, 2001, J LIPID RES, V42, P1062
   Moreira EF, 2001, J BIOL CHEM, V276, P18570, DOI 10.1074/jbc.M011259200
   Rameh LE, 1997, J BIOL CHEM, V272, P22059, DOI 10.1074/jbc.272.35.22059
   Ridgway ND, 1998, J BIOL CHEM, V273, P31621, DOI 10.1074/jbc.273.47.31621
   RIDGWAY ND, 1992, J CELL BIOL, V116, P307, DOI 10.1083/jcb.116.2.307
   Rivas MP, 1999, MOL BIOL CELL, V10, P2235, DOI 10.1091/mbc.10.7.2235
   Russell RL, 2001, J BIOL CHEM, V276, P13302, DOI 10.1074/jbc.M008512200
   SARRIA AJ, 1992, J BIOL CHEM, V267, P19455
   SPUDICH A, 1992, CELL MOTIL CYTOSKEL, V22, P250, DOI 10.1002/cm.970220405
   Storey MK, 1998, BIOCHEM J, V336, P247, DOI 10.1042/bj3360247
   Xu YQ, 2001, J BIOL CHEM, V276, P18407, DOI 10.1074/jbc.M101204200
NR 39
TC 104
Z9 114
U1 0
U2 7
PU PORTLAND PRESS LTD
PI LONDON
PA 5TH FLR, 90 HIGH HOLBORN, LONDON WC1V 6LJ, ENGLAND
SN 0264-6021
EI 1470-8728
J9 BIOCHEM J
JI Biochem. J.
PD FEB 1
PY 2002
VL 361
BP 461
EP 472
DI 10.1042/0264-6021:3610461
PN 3
PG 12
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 523XK
UT WOS:000173982700006
PM 11802775
OA Green Published
DA 2025-04-10
ER

PT J
AU Yi, XZ
   Liu, JL
   Zang, E
   Tian, Y
   Liu, JX
   Shi, LC
AF Yi, Xiaozhe
   Liu, Jiali
   Zang, Erhuan
   Tian, Yu
   Liu, Jinxin
   Shi, Linchun
TI Exploring a Hirudin variant from nonhematophagous leeches: Unraveling
   full-length sequence, alternative splicing, function, and potential as a
   novel anticoagulant polypeptide
SO JOURNAL OF ETHNOPHARMACOLOGY
LA English
DT Article
DE Anticoagulant active peptide; Hirudin variant; Medicinal leeches;
   Thrombin inhibitor drugs; Whitmania pigra
ID MEDICINAL LEECH; PROTEIN; PURIFICATION; DOMAIN
AB Ethnopharmacological relevance: Leeches exhibit robust anticoagulant activity, making them useful for treating cardiovascular diseases in traditional Chinese medicine. Whitmania pigra, , the primary source species of leech-derived medicinal compounds in China, has been demonstrated to possess formidable anticoagulant properties. Hirudin-like peptides, recognized as potent thrombin inhibitors, are prevalent in hematophagous leeches. Considering that W. pigra is a nonhematophagic leech, the following question arises: does a hirudin variant exist in this species? Aim of the study: In this study we identified the hirudin-encoding gene (WP_HV1) in the W. pigra genome. The goal of this study was to assess its anticoagulant activity and analyze the related mechanisms. Materials and methods: In this study, a hirudin-encoding gene, WP_HV1, was identified from the W. pigra genome, and its accurate coding sequence (CDS) was validated through cloning from cDNA extracted from fresh W. pigra specimens. The structure of WP_HV1 and the amino acids associated with its anticoagulant activity were determined by sequence and structural analysis and prediction of its binding energy to thrombin. E. coli was used for the expression of WP_HV1 and recombinant proteins with various structures and mutants. The anticoagulant activity of the synthesized recombinant proteins was then confirmed using thrombin time (TT). Results: Validation of the WP_HV1 gene was accomplished, and three alternative splices were discovered. The TT of the blank sample exceeded that of the recombinant WP_HV1 sample by 1.74 times (0.05 mg/ml), indicating positive anticoagulant activity. The anticoagulant activity of WP_HV1 was found to be associated with its Cterminal tyrosine, along with the presence of 9 acidic amino acids on both the left and right sides. A significant reduction in the corresponding TT was observed for the mutated amino acids compared to those of the wild type, with decreases of 4.8, 6.6, and 3.9 s, respectively. In addition, the anticoagulant activity of WP_HV1 was enhanced and prolonged for 2.7 s when the lysine-67 residue was mutated to tryptophan. Conclusion: Only one hirudin-encoding variant was identified in W. pigra. The active amino acids associated with anticoagulation in WP_HV1 were resolved and validated, revealing a novel source for screening and developing new anticoagulant drugs.
C1 [Yi, Xiaozhe; Liu, Jiali; Zang, Erhuan; Tian, Yu; Liu, Jinxin; Shi, Linchun] Chinese Acad Med Sci & Peking Union Med Coll, Inst Med Plant Dev, State Key Lab Qual Ensurance & Sustainable Use Dao, Beijing 100193, Peoples R China.
   [Yi, Xiaozhe; Liu, Jiali; Zang, Erhuan; Liu, Jinxin; Shi, Linchun] Minist Educ, State Adm Tradit Chinese Med Peoples Republ China, Engn Res Ctr Chinese Med Resource, Key Lab Chinese Med Resources Conservat, Beijing 100193, Peoples R China.
   [Tian, Yu] Chengde Med Univ, Hebei Key Lab Study & Exploitat Chinese Med, Chengde 067000, Peoples R China.
C3 Chinese Academy of Medical Sciences - Peking Union Medical College;
   Peking Union Medical College; Institute of Medicinal Plant Development -
   CAMS; Chengde Medical University
RP Liu, JX; Shi, LC (corresponding author), Chinese Acad Med Sci & Peking Union Med Coll, Inst Med Plant Dev, State Key Lab Qual Ensurance & Sustainable Use Dao, Beijing 100193, Peoples R China.
EM liujx_23@163.com; lcshi@implad.ac.cn
RI Liu, Jinxin/AAB-5109-2019
FU CAMS Innovation Fund for Medical Sciences (CIFMS) [2021-I2M-1-029];
   National Natural Science Foundation of China [81703659]; Key project at
   central government level: The ability establishment of sustainable use
   for valuable Chinese medicine resources [2060302]
FX This work was supported by the CAMS Innovation Fund for Medical Sciences
   (CIFMS) (2021-I2M-1-029), National Natural Science Foundation of China
   (81703659), Key project at central government level: The ability
   establishment of sustainable use for valuable Chinese medicine resources
   (2060302).
CR Corral-Rodríguez MA, 2011, BLOOD, V117, P7164, DOI 10.1182/blood-2010-10-315309
   Corral-Rodriguez MA, 2010, J MED CHEM, V53, P3847, DOI 10.1021/jm901743x
   Babenko VV, 2020, BMC GENOMICS, V21, DOI 10.1186/s12864-020-6748-0
   Barlow KA, 2018, J PHYS CHEM B, V122, P5389, DOI 10.1021/acs.jpcb.7b11367
   Baskova IP, 2004, BIOCHEMISTRY-MOSCOW+, V69, P770, DOI 10.1023/B:BIRY.0000040202.21965.2a
   Baskova IP, 2001, BIOCHEMISTRY-MOSCOW+, V66, P703, DOI 10.1023/A:1010223325313
   Bateman A, 2023, NUCLEIC ACIDS RES, V51, pD523, DOI 10.1093/nar/gkac1052
   Chen CJ, 2023, MOL PLANT, V16, P1733, DOI 10.1016/j.molp.2023.09.010
   Chen JR, 2021, FRONT PHARMACOL, V12, DOI 10.3389/fphar.2021.660757
   Cramer P, 2021, NAT STRUCT MOL BIOL, V28, P704, DOI 10.1038/s41594-021-00650-1
   DEFILIPPIS V, 1995, BIOCHEMISTRY-US, V34, P9552, DOI 10.1021/bi00029a032
   Dong XN, 2018, EUR J PHARM SCI, V121, P166, DOI 10.1016/j.ejps.2018.05.025
   Gu XJ, 2022, CHIN HERB MED, V14, P171, DOI 10.1016/j.chmed.2022.03.004
   Hall G, 2017, SCI REP-UK, V7, DOI 10.1038/srep39933
   Hall SW, 2001, THROMB HAEMOSTASIS, V86, P1466, DOI 10.1055/s-0037-1616750
   JOHNSON PH, 1989, SEMIN THROMB HEMOST, V15, P302, DOI 10.1055/s-2007-1002723
   Kumar S, 2016, MOL BIOL EVOL, V33, P1870, DOI [10.1093/molbev/msw054, 10.1093/molbev/msv279]
   Leman JK, 2020, NAT METHODS, V17, P665, DOI 10.1038/s41592-020-0848-2
   Lemke S, 2020, BIOMEDICINES, V8, DOI 10.3390/biomedicines8050099
   Li P, 2021, J THROMB THROMBOLYS, V52, P59, DOI 10.1007/s11239-020-02337-8
   Li WZ, 2006, BIOINFORMATICS, V22, P1658, DOI 10.1093/bioinformatics/btl158
   Li YR, 2020, ACTA PHARMACOL SIN, V41, P753, DOI 10.1038/s41401-019-0347-0
   Liu Celina, 2015, Nursing, V45, P25, DOI 10.1097/01.NURSE.0000472561.41030.2d
   Liu JL, 2023, BMC GENOMICS, V24, DOI 10.1186/s12864-023-09286-5
   MARKWARDT F, 1994, THROMB RES, V74, P1, DOI 10.1016/0049-3848(94)90032-9
   Monigatti F, 2002, BIOINFORMATICS, V18, P769, DOI 10.1093/bioinformatics/18.5.769
   Montinari MR, 2022, BIOMED PHARMACOTHER, V149, DOI 10.1016/j.biopha.2022.112878
   Müller C, 2022, J THROMB HAEMOST, V20, P1808, DOI 10.1111/jth.15762
   Nowak G, 2002, SEMIN THROMB HEMOST, V28, P415, DOI 10.1055/s-2002-35293
   Nowak G, 2007, THROMB HAEMOSTASIS, V98, P116, DOI 10.1160/Th07-05-0364
   Pettersen EF, 2021, PROTEIN SCI, V30, P70, DOI 10.1002/pro.3943
   Ripoll-Rozada J, 2022, BIOCHEM SOC T, V50, P387, DOI 10.1042/BST20210600
   Shakouri A, 2021, ADV PHARM BULL, V11, P261, DOI 10.34172/apb.2021.038
   Shen LH, 2019, EUR J PHARMACOL, V852, P77, DOI 10.1016/j.ejphar.2019.03.001
   Siddall ME, 2016, J PARASITOL, V102, P143, DOI 10.1645/15-802
   Sig AK, 2017, INTEGR MED RES, V6, P337, DOI 10.1016/j.imr.2017.08.001
   STUBBS MT, 1995, TRENDS BIOCHEM SCI, V20, P23, DOI 10.1016/S0968-0004(00)88945-8
   Sun Y, 2022, BRIT J PHARMACOL, V179, P3740, DOI 10.1111/bph.15816
   Waterhouse AM, 2009, BIOINFORMATICS, V25, P1189, DOI 10.1093/bioinformatics/btp033
   Wilkins MR, 1999, METH MOL B, V112, P531
   Xin XJ, 2015, MOL MED REP, V11, P3774, DOI 10.3892/mmr.2015.3194
   Yao XL, 2020, J SURG RES, V245, P441, DOI 10.1016/j.jss.2019.07.094
   Zhang YJ, 2022, J ETHNOPHARMACOL, V288, DOI 10.1016/j.jep.2022.114990
   Zhong S, 2007, BIOMED CHROMATOGR, V21, P439, DOI 10.1002/bmc.739
NR 44
TC 0
Z9 0
U1 6
U2 10
PU ELSEVIER IRELAND LTD
PI CLARE
PA ELSEVIER HOUSE, BROOKVALE PLAZA, EAST PARK SHANNON, CO, CLARE, 00000,
   IRELAND
SN 0378-8741
EI 1872-7573
J9 J ETHNOPHARMACOL
JI J. Ethnopharmacol.
PD AUG 10
PY 2024
VL 330
AR 118257
DI 10.1016/j.jep.2024.118257
EA MAY 2024
PG 10
WC Plant Sciences; Chemistry, Medicinal; Integrative & Complementary
   Medicine; Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Plant Sciences; Pharmacology & Pharmacy; Integrative & Complementary
   Medicine
GA H7V8N
UT WOS:001325492200001
PM 38677578
DA 2025-04-10
ER

PT J
AU Reimann, F
   Ashcroft, FM
   Gribble, FM
AF Reimann, F
   Ashcroft, FM
   Gribble, FM
TI Structural basis for the interference between nicorandil and
   sulfonylurea action
SO DIABETES
LA English
DT Article
ID K-ATP CHANNEL; TRANSMEMBRANE CONDUCTANCE REGULATOR; SENSITIVE POTASSIUM
   CHANNELS; BETA-CELL; DISTINCT FUNCTIONS; INSULIN-SECRETION; XENOPUS
   OOCYTES; SKELETAL-MUSCLE; SMOOTH-MUSCLE; RECEPTOR
AB Nicorandil is a new antianginal agent that potentially may be used to treat the cardiovascular side effects of diabetes. It is both a nitric oxide donor and an opener of ATP-sensitive K+ (K-ATP) channels in muscle and thereby causes vasodilation of the coronary vasculature. The aim of this study was to investigate the domains of the K-ATP channel involved in nicorandil activity and to determine whether nicorandil interacts with hypoglycemic sulfonylureas that target K-ATP channels in pancreatic beta -cells. K-ATP channels in muscle and beta -cells share a common pore-forming subunit, Kir6.2, but possess alternative sulfonylurea receptors (SURs; SUR1 in beta -cells, SUR2A in cardiac muscle, and SUR2B in smooth muscle). We expressed recombinant K-ATP channels in Xenopus oocytes and measured the effects of drugs and nucleotides by recording macroscopic currents in excised membrane patches. Nicorandil activated Kir6.2/SUR2A and Kir6.2/SUR2B but not Kir6.2/SUR1 currents, consistent with its specificity for cardiac and smooth muscle K-ATP channels. Drug activity depended on the presence of intracellular nucleotides and was impaired when the Walker A lysine residues were mutated in either nucleotide-binding domain of SUR2. Chimeric studies showed that the COOH-terminal group of transmembrane helices (TMs), especially TM 17, is responsible for the specificity of nicorandil for channels containing SUR2. The splice variation between SUR2A and SUR2B altered the off-rate of the nicorandil response. Finally, we showed. that nicorandil activity was unaffected by gliclazide.. which specifically blocks SUR1-type K-ATP channels, but; was severely impaired by glibenclamide and glimepiride, which target both SUR1 and SUR2-type K-ATP channels.
C1 Addenbrookes Hosp, Dept Clin Biochem, Cambridge CB2 2QR, England.
   Univ Oxford, Physiol Lab, Oxford, England.
C3 Cambridge University Hospitals NHS Foundation Trust; Addenbrooke's
   Hospital; University of Cambridge; University of Oxford
RP Gribble, FM (corresponding author), Addenbrookes Hosp, Dept Clin Biochem, Box 232,Hills Rd, Cambridge CB2 2QR, England.
OI Gribble, Fiona/0000-0002-4232-2898; Reimann, Frank/0000-0001-9399-6377
CR Aguilar-Bryan L, 1999, ENDOCR REV, V20, P101, DOI 10.1210/er.20.2.101
   AGUILARBRYAN L, 1995, SCIENCE, V268, P423, DOI 10.1126/science.7716547
   Ashcroft FM, 2000, TRENDS PHARMACOL SCI, V21, P439
   Ashcroft FM, 1999, DIABETOLOGIA, V42, P903, DOI 10.1007/s001250051247
   Ashfield R, 1999, DIABETES, V48, P1341, DOI 10.2337/diabetes.48.6.1341
   AZZARIA M, 1989, MOL CELL BIOL, V9, P5289, DOI 10.1128/MCB.9.12.5289
   Babenko AP, 2000, J BIOL CHEM, V275, P717, DOI 10.1074/jbc.275.2.717
   Bienengraeber M, 2000, FASEB J, V14, P1943, DOI 10.1096/fj.00-0027com
   CARSON MR, 1995, J BIOL CHEM, V270, P1711, DOI 10.1074/jbc.270.4.1711
   Cogolludo AL, 1999, BRIT J PHARMACOL, V126, P1025, DOI 10.1038/sj.bjp.0702375
   D'Hahan N, 1999, MOL PHARMACOL, V56, P308, DOI 10.1124/mol.56.2.308
   D'hahan N, 1999, P NATL ACAD SCI USA, V96, P12162, DOI 10.1073/pnas.96.21.12162
   Gribble FM, 2000, MOL PHARMACOL, V57, P1256
   Gribble FM, 1997, J PHYSIOL-LONDON, V504, P35, DOI 10.1111/j.1469-7793.1997.00035.x
   Gribble FM, 1997, J PHYSIOL-LONDON, V498, P87, DOI 10.1113/jphysiol.1997.sp021843
   Gribble FM, 1997, EMBO J, V16, P1145, DOI 10.1093/emboj/16.6.1145
   Gribble FM, 1998, DIABETES, V47, P1412, DOI 10.2337/diabetes.47.9.1412
   Gribble FM, 1999, DIABETOLOGIA, V42, P845, DOI 10.1007/s001250051236
   Hambrock A, 1999, MOL PHARMACOL, V55, P832
   INAGAKI N, 1995, SCIENCE, V270, P1166, DOI 10.1126/science.270.5239.1166
   INAGAKI N, 1995, J BIOL CHEM, V270, P5691, DOI 10.1074/jbc.270.11.5691
   Inagaki N, 1996, NEURON, V16, P1011, DOI 10.1016/S0896-6273(00)80124-5
   Isomoto S, 1996, J BIOL CHEM, V271, P24321, DOI 10.1074/jbc.271.40.24321
   KO YH, 1995, J BIOL CHEM, V270, P22093, DOI 10.1074/jbc.270.38.22093
   Liss B, 1999, EMBO J, V18, P833, DOI 10.1093/emboj/18.4.833
   Matsuo M, 2000, J BIOL CHEM, V275, P28757, DOI 10.1074/jbc.M004818200
   Moreau C, 2000, EMBO J, V19, P6644, DOI 10.1093/emboj/19.24.6644
   NICHOLS CG, 1991, AM J PHYSIOL, V261, pH1675, DOI 10.1152/ajpheart.1991.261.6.H1675
   Okuyama Y, 1998, PFLUG ARCH EUR J PHY, V435, P595, DOI 10.1007/s004240050559
   Patel DJ, 1999, EUR HEART J, V20, P51, DOI 10.1053/euhj.1998.1354
   Quayle JM, 1997, PHYSIOL REV, V77, P1165, DOI 10.1152/physrev.1997.77.4.1165
   Reimann F, 2000, MOL PHARMACOL, V58, P1318, DOI 10.1124/mol.58.6.1318
   Rorsman P, 1997, DIABETOLOGIA, V40, P487, DOI 10.1007/s001250050706
   Sakura H, 1995, FEBS LETT, V377, P338, DOI 10.1016/0014-5793(95)01369-5
   Schwanstecher M, 1998, EMBO J, V17, P5529, DOI 10.1093/emboj/17.19.5529
   Shindo T, 1998, BRIT J PHARMACOL, V124, P985, DOI 10.1038/sj.bjp.0701927
   Shyng SL, 1997, J GEN PHYSIOL, V110, P643, DOI 10.1085/jgp.110.6.643
   Song DK, 2001, BRIT J PHARMACOL, V133, P193, DOI 10.1038/sj.bjp.0704062
   TERZIC A, 1995, AM J PHYSIOL-CELL PH, V269, pC525, DOI 10.1152/ajpcell.1995.269.3.C525
   Tucker SJ, 1997, NATURE, V387, P179, DOI 10.1038/387179a0
   Tusnady GE, 1997, FEBS LETT, V402, P1, DOI 10.1016/S0014-5793(96)01478-0
   Ueda K, 1999, P NATL ACAD SCI USA, V96, P1268, DOI 10.1073/pnas.96.4.1268
   Ueda K, 1997, J BIOL CHEM, V272, P22983, DOI 10.1074/jbc.272.37.22983
   Uhde I, 1999, J BIOL CHEM, V274, P28079, DOI 10.1074/jbc.274.40.28079
NR 44
TC 40
Z9 45
U1 0
U2 3
PU AMER DIABETES ASSOC
PI ALEXANDRIA
PA 1660 DUKE ST, ALEXANDRIA, VA 22314 USA
SN 0012-1797
J9 DIABETES
JI Diabetes
PD OCT
PY 2001
VL 50
IS 10
BP 2253
EP 2259
DI 10.2337/diabetes.50.10.2253
PG 7
WC Endocrinology & Metabolism
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism
GA 477KR
UT WOS:000171283200011
PM 11574406
OA Bronze
DA 2025-04-10
ER

PT J
AU Gomez-Sanchez, EP
AF Gomez-Sanchez, Elise P.
TI The mammalian mineralocorticoid receptor: tying down a promiscuous
   receptor
SO EXPERIMENTAL PHYSIOLOGY
LA English
DT Article
ID ALDOSTERONE-SENSITIVE NEURONS; 11-BETA-HYDROXYSTEROID DEHYDROGENASE
   TYPE-1; SALT-INDUCED HYPERTENSION; HEXOSE-6-PHOSPHATE DEHYDROGENASE;
   SOLITARY TRACT; BINDING; BRAIN; CORTICOSTERONE; LOCALIZATION; EXPRESSION
AB The mineralocorticoid receptor (MR) has been called a promiscuous receptor because its intrinsic affinity for aldosterone, cortisol and corticosterone is similar. Since glucocorticoids circulate in concentrations 100- to 1000-fold those of aldosterone, stoichiometry dictates that MR should be activated by glucocorticoids, not aldosterone, yet MRs are expressed in many tissues and regulate diverse functions, many of them under the regulation of the renin-angiotensin-aldosterone system. A relatively small number of brain MRs are aldosterone selective and modulate blood pressure. Evidence for possible mechanisms conferring ligand specificity in the context of mineralocorticoid-induced hypertension and the brain are discussed. These include factors (or mechanisms) intrinsic to the receptor, such as alternative splice variants and translation start sites, and extrinsic to the MR, including differential access through the blood-brain barrier, differential recruitment of co-regulators and scaffolding proteins, 11 beta-steroid dehydrogenase activity, synthesis of potent acylated aldosterone derivatives and the synthesis of relevant amounts of aldosterone in areas of the brain that modulate blood pressure.
C1 [Gomez-Sanchez, Elise P.] GV Sonny Montgomery VA Med Ctr, Res Serv, Jackson, MS 39216 USA.
   [Gomez-Sanchez, Elise P.] Univ Mississippi, Med Ctr, Dept Med, Div Endocrinol, Jackson, MS 39216 USA.
   [Gomez-Sanchez, Elise P.] Univ Mississippi, Med Ctr, Dept Pharmacol, Jackson, MS 39216 USA.
C3 University of Mississippi; University of Mississippi Medical Center;
   University of Mississippi; University of Mississippi Medical Center
RP Gomez-Sanchez, EP (corresponding author), GV Sonny Montgomery VA Med Ctr, Res Serv, Jackson, MS 39216 USA.
EM egomez-sanchez@medicine.umsmed.edu
FU Department of Veterans Affairs; NIH [HL27255, HL75321]
FX This work was supported by Medical Research funds from the Department of
   Veterans Affairs and NIH grants HL27255 and HL75321.
CR ARRIZA JL, 1987, SCIENCE, V237, P268, DOI 10.1126/science.3037703
   Atanasov AG, 2004, FEBS LETT, V571, P129, DOI 10.1016/j.febslet.2004.06.065
   BIRMINGHAM MK, 1984, NEUROCHEM RES, V9, P333, DOI 10.1007/BF00963982
   BRODY MJ, 1991, HYPERTENSION S3, V18, P7
   Connell JMC, 2005, J ENDOCRINOL, V186, P1, DOI 10.1677/joe.1.06017
   de Kloet ER, 2000, KIDNEY INT, V57, P1329, DOI 10.1046/j.1523-1755.2000.00971.x
   DEKLOET ER, 1983, BRAIN RES, V264, P323, DOI 10.1016/0006-8993(83)90834-X
   DEKLOET ER, 1991, FRONT NEUROENDOCRIN, V12, P95
   EDWARDS CRW, 1988, LANCET, V2, P986, DOI 10.1016/S0140-6736(88)90742-8
   Felder RB, 2010, EXP PHYSIOL, V95, P19, DOI 10.1113/expphysiol.2008.045948
   Fuller PJ, 2005, HYPERTENSION, V46, P1227, DOI 10.1161/01.HYP.0000193502.77417.17
   FUNDER JW, 1973, ENDOCRINOLOGY, V92, P994, DOI 10.1210/endo-92-4-994
   FUNDER JW, 1995, CARDIOVASC RES, V30, P177, DOI 10.1016/S0008-6363(96)88515-4
   Geerling JC, 2006, J NEUROSCI, V26, P411, DOI 10.1523/JNEUROSCI.3115-05.2006
   Geerling JC, 2005, BRAIN RES, V1065, P142, DOI 10.1016/j.brainres.2005.10.044
   Geerling JC, 2006, J COMP NEUROL, V494, P515, DOI 10.1002/cne.20808
   Geerling JC, 2006, J COMP NEUROL, V497, P646, DOI 10.1002/cne.21019
   Geerling JC, 2006, J COMP NEUROL, V497, P223, DOI 10.1002/cne.20993
   Gomez-Sanchez CE, 2006, ENDOCRINOLOGY, V147, P1343, DOI 10.1210/en.2005-0860
   Gomez-Sanchez CE, 2001, AM J HYPERTENS, V14, p200S, DOI 10.1016/S0895-7061(01)02089-1
   Gomez-Sanchez CE, 2001, J CLIN ENDOCR METAB, V86, P5118, DOI 10.1210/jc.86.11.5118
   Gomez-Sanchez EP, 2008, ENDOCRINOLOGY, V149, P525, DOI 10.1210/en.2007-0328
   Gomez-Sanchez EP, 2005, AM J PHYSIOL-ENDOC M, V288, pE342, DOI 10.1152/ajpendo.00355.2004
   Gomez-Sanchez EP, 2005, AM J PHYSIOL-REG I, V288, pR389, DOI 10.1152/ajpregu.00441.2004
   Gomez-Sanchez EP, 2004, CURR OPIN NEPHROL HY, V13, P191, DOI 10.1097/00041552-200403000-00007
   Gomez-Sanchez EP, 2003, AM J PHYSIOL-ENDOC M, V285, pE272, DOI 10.1152/ajpendo.00409.2002
   GomezSanchez CE, 1996, ENDOCR RES, V22, P463, DOI 10.1080/07435809609043732
   GomezSanchez CE, 1997, ENDOCRINOLOGY, V138, P3369, DOI 10.1210/en.138.8.3369
   GomezSanchez EP, 1997, STEROIDS, V62, P444, DOI 10.1016/S0039-128X(97)00011-1
   GOMEZSANCHEZ EP, 1992, AM J PHYSIOL, V263, pE1125
   GOTO A, 1981, CLIN SCI, V61, pS53, DOI 10.1042/cs061053s
   Grossmann C, 2005, MOL ENDOCRINOL, V19, P1697, DOI 10.1210/me.2004-0469
   HOLMES MC, 2006, ANN NY ACAD SCI, V1007, P357
   Huang BS, 2006, CURR OPIN CARDIOL, V21, P295, DOI 10.1097/01.hco.0000231398.64362.94
   JANIAK PC, 1990, AM J PHYSIOL, V259, pR1025, DOI 10.1152/ajpregu.1990.259.5.R1025
   KNOWLTON AI, 1949, ENDOCRINOLOGY, V45, P435, DOI 10.1210/endo-45-4-435
   KROZOWSKI ZS, 1983, P NATL ACAD SCI-BIOL, V80, P6056, DOI 10.1073/pnas.80.19.6056
   LANGFORD HG, 1959, AM J PHYSIOL, V196, P449, DOI 10.1152/ajplegacy.1959.196.2.449
   LASSMAN MN, 1974, ENDOCRINOLOGY, V94, P1541, DOI 10.1210/endo-94-6-1541
   LOCKETT MF, 1969, ISRAEL J MED SCI, V5, P525
   MARK AL, 1991, HYPERTENSION, V17, pI86, DOI 10.1161/01.HYP.17.1_Suppl.I86
   MELLON SH, 1994, J CLIN ENDOCR METAB, V78, P1003, DOI 10.1210/jc.78.5.1003
   MOISAN MP, 1990, ENDOCRINOLOGY, V127, P1450, DOI 10.1210/endo-127-3-1450
   PACHA J, 1993, ACTA PHYSIOL SCAND, V148, P69, DOI 10.1111/j.1748-1716.1993.tb09533.x
   Pascual-Le Tallec L, 2005, MOL ENDOCRINOL, V19, P2211, DOI 10.1210/me.2005-0089
   RAPP JP, 1985, HYPERTENSION, V7, P340, DOI 10.1161/01.HYP.7.3_Pt_1.340
   Seckl J. R., 1993, Journal of Endocrinology, V137, pS9
   Seckl JR, 2001, ENDOCRINOLOGY, V142, P1371, DOI 10.1210/en.142.4.1371
   Selye H, 1944, AM HEART J, V27, P338, DOI 10.1016/S0002-8703(44)90823-9
   Stumpf WE., 1979, Within the Brain-Pituitary- Adrenocortical System, P137
   TAKESHITA A, 1979, AM J PHYSIOL, V236, pH48, DOI 10.1152/ajpheart.1979.236.1.H48
   Uhr M, 2002, J NEUROENDOCRINOL, V14, P753, DOI 10.1046/j.1365-2826.2002.00836.x
   Viengchareun Say, 2007, Nucl Recept Signal, V5, pe012, DOI 10.1621/nrs.05012
   Yu L, 2002, MOL CELL ENDOCRINOL, V190, P9, DOI 10.1016/S0303-7207(02)00041-2
   Zhou MY, 2000, MOL CELL ENDOCRINOL, V159, P125, DOI 10.1016/S0303-7207(99)00198-7
NR 55
TC 31
Z9 36
U1 0
U2 1
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0958-0670
EI 1469-445X
J9 EXP PHYSIOL
JI Exp. Physiol.
PD JAN 1
PY 2010
VL 95
IS 1
BP 13
EP 18
DI 10.1113/expphysiol.2008.045914
PG 6
WC Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Physiology
GA 533PI
UT WOS:000272836300003
PM 19648477
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Kojima, D
   Mano, H
   Fukada, Y
AF Kojima, D
   Mano, H
   Fukada, Y
TI Vertebrate ancient-long opsin: A green-sensitive photoreceptive molecule
   present in zebrafish deep brain and retinal horizontal cells
SO JOURNAL OF NEUROSCIENCE
LA English
DT Article
DE VAL-opsin; VA-opsin; deep brain photoreceptor; horizontal cell;
   alternative splicing; zebrafish
ID BOVINE RHODOPSIN; EXTRARETINAL PHOTORECEPTORS; ACTIVITY RHYTHMS;
   CYPRINUS-CARPIO; SILURUS-ASOTUS; TELEOST FISH; PINEAL; PROTEIN;
   IMMUNOCYTOCHEMISTRY; PIGMENTS
AB Nonretinal/nonpineal photosensitivity has been found in the brain of vertebrates, but the molecular basis for such a "deep brain" photoreception system remains unclear. We conducted an extensive search for brain opsin cDNAs of the zebrafish (Danio rerio), a useful animal model for genetic studies, and we have isolated a partial cDNA clone encoding an ortholog of vertebrate ancient (VA) opsin, the function of which is unknown. Subsequent characterization revealed the occurrence of two kinds of mRNAs encoding putative splicing variants, VA and VA-Long (VAL) opsin, the latter of which is a novel variant of the former. Both opsins shared a common core sequence in the membrane-spanning domains, but VAL-opsin had a C-terminal tail much longer than that of VA-opsin. Functional reconstitution experiments on the recombinant proteins showed that VAL-opsin with bound 11-cis-retinal is a green-sensitive pigment (lambda max similar to 500 nm), whereas VA-opsin exhibited no photosensitivity even in the presence of 11-cis-retinal. Immunoreactivity specific to this functionally active VAL-opsin was localized at a limited number of cells surrounding the diencephalic ventricle of central thalamus, and these cells were distributed over similar to 200 mm along the rostrocaudal axis. Taken together with the previous study on the locus of the teleost brain photosensitivity (von Frisch K, 1911), it is strongly suggested that the VAL-positive cells in the zebrafish brain represent the deep brain photoreceptors. The VAL-specific immunoreactivity was also detected in a subset of non-GABAergic horizontal cells in the zebrafish retina. The existence of VAL-opsin, a new member of the rhodopsin superfamily, in these tissues may indicate its multiple roles in visual and nonvisual photosensory physiology.
C1 Univ Tokyo, Grad Sch Sci, Dept Biophys & Biochem, Bunkyo Ku, Tokyo 1130033, Japan.
   Japan Sci & Technol Corp, CREST, Tokyo, Japan.
C3 University of Tokyo; Japan Science & Technology Agency (JST)
RP Fukada, Y (corresponding author), Univ Tokyo, Grad Sch Sci, Dept Biophys & Biochem, Bunkyo Ku, Hongo 7-3-1, Tokyo 1130033, Japan.
RI 吉孝, 深田/G-5090-2014; Kojima, Daisuke/G-4958-2014
OI Kojima, Daisuke/0000-0003-2658-780X
CR ALUBAIDI MR, 1990, J BIOL CHEM, V265, P20563
   BALDRIDGE WH, 1991, VISUAL NEUROSCI, V7, P441, DOI 10.1017/S0952523800009731
   BarPeled M, 1996, ANAL BIOCHEM, V241, P140, DOI 10.1006/abio.1996.0390
   BARTHEL LK, 1990, J HISTOCHEM CYTOCHEM, V38, P1383, DOI 10.1177/38.9.2201738
   Blackshaw S, 1997, J NEUROSCI, V17, P8083
   Blackshaw S, 1999, J NEUROSCI, V19, P3681
   Cahill GM, 1996, BRAIN RES, V708, P177, DOI 10.1016/0006-8993(95)01365-2
   Connaughton VP, 1999, VISUAL NEUROSCI, V16, P483, DOI 10.1017/S0952523899163090
   DEGUCHI T, 1981, NATURE, V290, P706, DOI 10.1038/290706a0
   Dowling J, 1987, RETINA APPROACHABLE
   ECHTELER SM, 1984, J COMP NEUROL, V230, P536, DOI 10.1002/cne.902300405
   ECHTELER SM, 1985, J COMP PHYSIOL A, V156, P267, DOI 10.1007/BF00610868
   Elshourbagy NA, 1996, J BIOL CHEM, V271, P25300, DOI 10.1074/jbc.271.41.25300
   FOSTER RG, 1985, NATURE, V313, P50, DOI 10.1038/313050a0
   FOSTER RG, 1993, J COMP PHYSIOL A, V172, P33, DOI 10.1007/BF00214713
   Freedman MS, 1999, SCIENCE, V284, P502, DOI 10.1126/science.284.5413.502
   HARTWIG HG, 1979, J COMP PHYSIOL, V130, P277, DOI 10.1007/BF00614615
   KAVALIERS M, 1980, BEHAV NEURAL BIOL, V30, P56, DOI 10.1016/S0163-1047(80)90884-5
   KAWATA A, 1992, PHOTOCHEM PHOTOBIOL, V56, P1157, DOI 10.1111/j.1751-1097.1992.tb09740.x
   KAYADA S, 1995, COMP BIOCHEM PHYS B, V110, P599, DOI 10.1016/0305-0491(94)00179-X
   Kojima D, 1996, BIOCHEMISTRY-US, V35, P2625, DOI 10.1021/bi9511548
   LAM DMK, 1979, NATURE, V278, P565, DOI 10.1038/278565a0
   Lucas RJ, 1999, SCIENCE, V284, P505, DOI 10.1126/science.284.5413.505
   LYTHGOE JN, 1984, NATURE, V308, P83, DOI 10.1038/308083a0
   Mano H, 1999, MOL BRAIN RES, V73, P110, DOI 10.1016/S0169-328X(99)00242-9
   MASUDA H, 1994, TISSUE CELL, V26, P101, DOI 10.1016/0040-8166(94)90086-8
   MAX M, 1995, SCIENCE, V267, P1502, DOI 10.1126/science.7878470
   Miyamoto Y, 1998, P NATL ACAD SCI USA, V95, P6097, DOI 10.1073/pnas.95.11.6097
   MURAKAMI M, 1995, PROG RETIN EYE RES, V14, P197, DOI 10.1016/1350-9462(95)90003-4
   NAMBA T, 1993, NATURE, V365, P166, DOI 10.1038/365166a0
   NATHANS J, 1983, CELL, V34, P807, DOI 10.1016/0092-8674(83)90537-8
   NATHANS J, 1986, SCIENCE, V232, P193, DOI 10.1126/science.2937147
   OKANO T, 1994, NATURE, V372, P94, DOI 10.1038/372094a0
   OKSCHE A., 1975, BRAIN ENDOCRINE INTE, P40
   Piccolino M., 1986, PROGR RETINAL RES, V5, P147
   Provencio I, 2000, J NEUROSCI, V20, P600, DOI 10.1523/JNEUROSCI.20-02-00600.2000
   Provencio I, 1998, P NATL ACAD SCI USA, V95, P340, DOI 10.1073/pnas.95.1.340
   SCHARRER E., 1928, ZEITSCHR VERGLEICH PHYSIOL, V7, P1, DOI 10.1007/BF00341151
   SHIMAMOTO A, 1993, FEBS LETT, V333, P61, DOI 10.1016/0014-5793(93)80375-5
   Soni BG, 1997, FEBS LETT, V406, P279, DOI 10.1016/S0014-5793(97)00287-1
   Soni BG, 1998, NATURE, V394, P27, DOI 10.1038/27794
   STRIEDTER GF, 1991, J COMP NEUROL, V312, P311, DOI 10.1002/cne.903120213
   TABATA M, 1989, J COMP PHYSIOL A, V164, P797, DOI 10.1007/BF00616751
   TABATA M, 1988, EXP BIOL, V47, P219
   THOMPSON JD, 1994, NUCLEIC ACIDS RES, V22, P4673, DOI 10.1093/nar/22.22.4673
   UMINO O, 1991, VISUAL NEUROSCI, V7, P451, DOI 10.1017/S0952523800009743
   VANVEEN T, 1976, J COMP PHYSIOL, V111, P209, DOI 10.1007/BF00605532
   von Frisch K, 1911, PFLUG ARCH GES PHYS, V138, P319
   Wada Y, 1998, FEBS LETT, V424, P53, DOI 10.1016/S0014-5793(98)00138-0
   WEISS ER, 1994, BIOCHEMISTRY-US, V33, P7587, DOI 10.1021/bi00190a011
   Yoshikawa T, 1998, FEBS LETT, V424, P69, DOI 10.1016/S0014-5793(98)00139-2
   Yoshikawa T, 1998, COMP BIOCHEM PHYS B, V119, P65, DOI 10.1016/S0305-0491(97)00290-3
NR 52
TC 131
Z9 147
U1 0
U2 11
PU SOC NEUROSCIENCE
PI WASHINGTON
PA 11 DUPONT CIRCLE, NW, STE 500, WASHINGTON, DC 20036 USA
SN 0270-6474
J9 J NEUROSCI
JI J. Neurosci.
PD APR 15
PY 2000
VL 20
IS 8
BP 2845
EP 2851
PG 7
WC Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA 303FR
UT WOS:000086412100014
PM 10751436
DA 2025-04-10
ER

PT J
AU Suzuki, S
   Li, AJ
   Ikemoto, M
   Imamura, T
AF Suzuki, S
   Li, AJ
   Ikemoto, M
   Imamura, T
TI Expression of tenascin-C long isoforms is induced in the hypothalamus by
   FGF-1
SO NEUROREPORT
LA English
DT Article
DE alternative splicing; anti-adhesive protein; ependymal cell; fibroblast
   growth factor-1; fibronectin type III domain; hypothalamus; long
   isoforms; rat; shortest isoform; tenascin-C
ID FIBROBLAST GROWTH-FACTOR; CENTRAL-NERVOUS-SYSTEM; NEURAL TISSUES;
   CELL-ADHESION; FOOD-INTAKE; FACTOR-I; BRAIN; ASTROCYTES; MOUSE; RATS
AB Fibroblast growth factor (FGF)-1 modulates various brain functions, such as the hypothalamic control of feeding. In the rat, we examined the effect of intracerebroventricularly infused FGF-1 on the hypothalamic expression of tenascin-C, a selective mediator of neuron-glial interaction. In situ hybridization revealed little tenascin-C mRNA expression in control brains, but greatly increased expression in ependymal cells around the third ventricle in the FGF-1-infused rats. Reverse transcription-linked PCR analysis of hypothalamic mRNA revealed an FGF-1-induced expression not of the shortest isoform of tenascin-C, but of the long isoforms (with additional fibronectin type Ill-domain insertions). Quantitative analysis by real time PCR revealed that this induction was transient and dose-dependent. Specific modulation of hypothalamic neuron-glial interactions by tenascin-C may mediate FGF-1-induced feeding suppression.
C1 AIST, Gene Discovery Res Ctr, Tsukuba, Ibaraki 3058566, Japan.
C3 National Institute of Advanced Industrial Science & Technology (AIST)
RP Imamura, T (corresponding author), AIST, Gene Discovery Res Ctr, AIST Cent 6,1-1-1 Higashi, Tsukuba, Ibaraki 3058566, Japan.
RI IKEMOTO, Mitsushi/L-8861-2018
OI IKEMOTO, Mitsushi/0000-0001-5799-0672
CR FAISSNER A, 1995, GLIA, V13, P233, DOI 10.1002/glia.440130402
   GRUMET M, 1985, P NATL ACAD SCI USA, V82, P8075, DOI 10.1073/pnas.82.23.8075
   HANAI K, 1989, AM J PHYSIOL, V256, pR217, DOI 10.1152/ajpregu.1989.256.1.R217
   HILAIRE ZD, 1992, BRAIN RES BULL, V29, P525, DOI 10.1016/0361-9230(92)90094-E
   HOEBEL BG, 1989, ANN NY ACAD SCI, V575, P171
   IKOMOTO M, 2000, NAT MED, V6, P910
   Joester A, 1999, J BIOL CHEM, V274, P17144, DOI 10.1074/jbc.274.24.17144
   KRUSE J, 1985, NATURE, V316, P146, DOI 10.1038/316146a0
   Meiners S, 1999, J NEUROSCI, V19, P8443
   MEINERS S, 1993, DEV BIOL, V160, P480, DOI 10.1006/dbio.1993.1322
   MENDIS DB, 1995, BRAIN RES, V676, P69, DOI 10.1016/0006-8993(95)00101-U
   Murphy-Ullrich JE, 2001, J CLIN INVEST, V107, P785, DOI 10.1172/JCI12609
   OOMURA Y, 1992, American Journal of Clinical Nutrition, V55, p278S, DOI 10.1093/ajcn/55.1.278s
   Ozawa K, 1996, MOL BRAIN RES, V41, P279, DOI 10.1016/0169-328X(96)00108-8
   Paxinos G, 1986, RAT BRAIN STEREOTAXI
   SASAKI K, 1994, PHYSIOL BEHAV, V56, P211, DOI 10.1016/0031-9384(94)90186-4
   SASAKI K, 1991, BRAIN RES BULL, V27, P327, DOI 10.1016/0361-9230(91)90120-9
   ScottDrew S, 1997, J NEUROSCI RES, V50, P202, DOI 10.1002/(SICI)1097-4547(19971015)50:2<202::AID-JNR9>3.0.CO;2-J
   Suzuki S, 2001, EUR J NEUROSCI, V13, P2299, DOI 10.1046/j.0953-816x.2001.01606.x
   Suzuki S, 2001, NEUROSCI LETT, V300, P29, DOI 10.1016/S0304-3940(01)01535-X
   TUCKER RP, 1993, J CELL SCI, V104, P69
   Wittwer CT, 1997, BIOTECHNIQUES, V22, P130, DOI 10.2144/97221bi01
NR 22
TC 7
Z9 8
U1 0
U2 0
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA 530 WALNUT ST, PHILADELPHIA, PA 19106-3621 USA
SN 0959-4965
J9 NEUROREPORT
JI Neuroreport
PD JUN 12
PY 2002
VL 13
IS 8
BP 1041
EP 1045
DI 10.1097/00001756-200206120-00013
PG 5
WC Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA 573HN
UT WOS:000176823600020
PM 12060805
DA 2025-04-10
ER

PT J
AU Madugundu, AK
   Na, CH
   Nirujogi, RS
   Renuse, S
   Kim, KP
   Burns, KH
   Wilks, C
   Langmead, B
   Ellis, SE
   Collado-Torres, L
   Halushka, MK
   Kim, MS
   Pandey, A
AF Madugundu, Anil K.
   Na, Chan Hyun
   Nirujogi, Raja Sekhar
   Renuse, Santosh
   Kim, Kwang Pyo
   Burns, Kathleen H.
   Wilks, Christopher
   Langmead, Ben
   Ellis, Shannon E.
   Collado-Torres, Leonardo
   Halushka, Marc K.
   Kim, Min-Sik
   Pandey, Akhilesh
TI Integrated Transcriptomic and Proteomic Analysis of Primary Human
   Umbilical Vein Endothelial Cells
SO PROTEOMICS
LA English
DT Article
DE allelic expression; coding SNP; mass-spectrometry; RNA-seq; proteoform;
   proteogenomics; splice variants; transcriptome
ID ADHESION MOLECULES; GENOME ANNOTATION; QUALITY-CONTROL; NONCODING RNAS;
   IDENTIFICATION; TRANSLATION; EXPRESSION; PROTEINS; DRAFT; QUANTIFICATION
AB Understanding the molecular profile of every human cell type is essential for understanding its role in normal physiology and disease. Technological advancements in DNA sequencing, mass spectrometry, and computational methods allow us to carry out multiomics analyses although such approaches are not routine yet. Human umbilical vein endothelial cells (HUVECs) are a widely used model system to study pathological and physiological processes associated with the cardiovascular system. In this study, next-generation sequencing and high-resolution mass spectrometry to profile the transcriptome and proteome of primary HUVECs is employed. Analysis of 145 million paired-end reads from next-generation sequencing confirmed expression of 12 186 protein-coding genes (FPKM >= 0.1), 439 novel long non-coding RNAs, and revealed 6089 novel isoforms that were not annotated in GENCODE. Proteomics analysis identifies 6477 proteins including confirmation of N-termini for 1091 proteins, isoforms for 149 proteins, and 1034 phosphosites. A database search to specifically identify other post-translational modifications provide evidence for a number of modification sites on 117 proteins which include ubiquitylation, lysine acetylation, and mono-, di- and tri-methylation events. Evidence for 11 "missing proteins," which are proteins for which there was insufficient or no protein level evidence, is provided. Peptides supporting missing protein and novel events are validated by comparison of MS/MS fragmentation patterns with synthetic peptides. Finally, 245 variant peptides derived from 207 expressed proteins in addition to alternate translational start sites for seven proteins and evidence for novel proteoforms for five proteins resulting from alternative splicing are identified. Overall, it is believed that the integrated approach employed in this study is widely applicable to study any primary cell type for deeper molecular characterization.
C1 [Madugundu, Anil K.; Pandey, Akhilesh] Natl Inst Mental Hlth & Neurosci, Ctr Mol Med, Hosur Rd, Bangalore 560029, Karnataka, India.
   [Madugundu, Anil K.] Inst Bioinformat, Int Technol Pk, Bangalore 560066, Karnataka, India.
   [Madugundu, Anil K.] Manipal Acad Higher Educ, Manipal 576104, Karnataka, India.
   [Madugundu, Anil K.; Na, Chan Hyun; Nirujogi, Raja Sekhar; Renuse, Santosh; Burns, Kathleen H.; Pandey, Akhilesh] Johns Hopkins Univ, Sch Med, McKusick Nathans Inst Genet Med, Baltimore, MD 21205 USA.
   [Madugundu, Anil K.; Renuse, Santosh; Pandey, Akhilesh] Mayo Clin, Ctr Individualized Med, Rochester, MN 55905 USA.
   [Madugundu, Anil K.; Renuse, Santosh; Pandey, Akhilesh] Mayo Clin, Dept Lab Med & Pathol, Rochester, MN 55905 USA.
   [Na, Chan Hyun; Pandey, Akhilesh] Johns Hopkins Univ, Sch Med, Inst Cell Engn, Neurol, Baltimore, MD 21205 USA.
   [Kim, Kwang Pyo; Kim, Min-Sik] Kyung Hee Univ, Dept Appl Chem, Yongin 17104, Gyeonggi, South Korea.
   [Burns, Kathleen H.; Halushka, Marc K.; Pandey, Akhilesh] Johns Hopkins Univ, Sch Med, Dept Pathol, Baltimore, MD 21205 USA.
   [Burns, Kathleen H.] Johns Hopkins Univ, Sch Med, Sidney Kimmel Comprehens Canc Ctr, Baltimore, MD 21205 USA.
   [Burns, Kathleen H.] Johns Hopkins Univ, Sch Med, High Throughput Biol Ctr, Baltimore, MD 21205 USA.
   [Wilks, Christopher; Langmead, Ben] Johns Hopkins Univ, Dept Comp Sci, Baltimore, MD 21218 USA.
   [Wilks, Christopher; Langmead, Ben; Ellis, Shannon E.; Collado-Torres, Leonardo] Johns Hopkins Univ, Ctr Computat Biol, Baltimore, MD 21205 USA.
   [Ellis, Shannon E.] Johns Hopkins Bloomberg Sch Publ Hlth, Dept Biostat, Baltimore, MD 21205 USA.
   [Collado-Torres, Leonardo] Johns Hopkins Med Campus, Lieber Inst Brain Dev, Baltimore, MD 21205 USA.
   [Kim, Min-Sik] DGIST, Dept New Biol, Daegu 42988, South Korea.
   [Pandey, Akhilesh] Johns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA.
   [Pandey, Akhilesh] Johns Hopkins Univ, Sch Med, Dept Oncol, Baltimore, MD 21205 USA.
C3 National Institute of Mental Health & Neurosciences - India; Manipal
   Academy of Higher Education (MAHE); Johns Hopkins University; Mayo
   Clinic; Mayo Clinic; Johns Hopkins University; Kyung Hee University;
   Johns Hopkins University; Johns Hopkins University; Johns Hopkins
   Medicine; Johns Hopkins University; Johns Hopkins University; Johns
   Hopkins University; Johns Hopkins University; Johns Hopkins Bloomberg
   School of Public Health; Johns Hopkins University; Johns Hopkins
   Medicine; Daegu Gyeongbuk Institute of Science & Technology (DGIST);
   Johns Hopkins University; Johns Hopkins University
RP Pandey, A (corresponding author), Natl Inst Mental Hlth & Neurosci, Ctr Mol Med, Hosur Rd, Bangalore 560029, Karnataka, India.; Pandey, A (corresponding author), Johns Hopkins Univ, Sch Med, McKusick Nathans Inst Genet Med, Baltimore, MD 21205 USA.; Pandey, A (corresponding author), Mayo Clin, Ctr Individualized Med, Rochester, MN 55905 USA.; Pandey, A (corresponding author), Mayo Clin, Dept Lab Med & Pathol, Rochester, MN 55905 USA.; Pandey, A (corresponding author), Johns Hopkins Univ, Sch Med, Inst Cell Engn, Neurol, Baltimore, MD 21205 USA.; Pandey, A (corresponding author), Johns Hopkins Univ, Sch Med, Dept Pathol, Baltimore, MD 21205 USA.; Pandey, A (corresponding author), Johns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA.; Pandey, A (corresponding author), Johns Hopkins Univ, Sch Med, Dept Oncol, Baltimore, MD 21205 USA.
EM akhilesh.pandey@mayo.edu
RI Kim, Kwang Pyo/AAG-1815-2020; Burns, Kathleen/A-3360-2011; Renuse,
   Santosh/ABA-6792-2020; Pandey, Akhilesh/CAI-9458-2022; Langmead,
   Ben/F-4218-2012; Madugundu, Anil/ABE-2128-2021; Kim,
   Min-Sik/KFS-9148-2024; Kim, Min-Sik/M-3488-2016; Langmead,
   Benjamin/C-1354-2009; Pandey, Akhilesh/B-4127-2009
OI Kim, Min-Sik/0000-0001-7317-5360; Madugundu, Anil/0000-0003-4274-7316;
   RENUSE, SANTOSH/0000-0002-4051-5637; Collado-Torres,
   Leonardo/0000-0003-2140-308X; Langmead, Benjamin/0000-0003-2437-1976;
   Kim, Kwang Pyo/0000-0003-0095-3787; Pandey,
   Akhilesh/0000-0001-9943-6127; Nirujogi, Raja Sekhar/0000-0002-3177-8566
FU DBT-Wellcome Trust India Alliance [IA/M/15/1/502023] Funding Source:
   Medline; NCI NIH HHS [R01 CA184165, U24 CA210985] Funding Source:
   Medline; NIGMS NIH HHS [R01 GM124531] Funding Source: Medline; NIH HHS
   [P50NS038377, R01CA184165, S10 OD021844, R01GM124531, S10OD021844,
   U24CA210985] Funding Source: Medline; NINDS NIH HHS [P50 NS038377]
   Funding Source: Medline; Wellcome Trust Funding Source: Medline
CR Bassenge E, 1996, PROG CARDIOVASC DIS, V39, P209, DOI 10.1016/S0033-0620(96)80002-8
   Bruneel A, 2005, PROTEOMICS, V5, P3876, DOI 10.1002/pmic.200401239
   Bruneel A, 2003, PROTEOMICS, V3, P714, DOI 10.1002/pmic.200300409
   Cabili MN, 2011, GENE DEV, V25, P1915, DOI 10.1101/gad.17446611
   Collado-Torres L, 2017, NAT BIOTECHNOL, V35, P319, DOI 10.1038/nbt.3838
   COLLINS T, 1995, FASEB J, V9, P899, DOI 10.1096/fasebj.9.10.7542214
   Data KK, 2016, METHODS MOL BIOL, V1410, P77, DOI 10.1007/978-1-4939-3524-6_5
   DAVIES MJ, 1993, J PATHOL, V171, P223, DOI 10.1002/path.1711710311
   DeLuca DS, 2012, BIOINFORMATICS, V28, P1530, DOI 10.1093/bioinformatics/bts196
   Deutsch EW, 2016, J PROTEOME RES, V15, P3961, DOI 10.1021/acs.jproteome.6b00392
   Eren E, 2013, CHOLESTEROL, DOI 10.1155/2013/792090
   Etzioni A, 1996, PEDIATR RES, V39, P191, DOI 10.1203/00006450-199602000-00001
   Gaudet P, 2017, NUCLEIC ACIDS RES, V45, pD177, DOI 10.1093/nar/gkw1062
   Gautier V, 2012, MOL CELL PROTEOMICS, V11, P527, DOI 10.1074/mcp.M111.015230
   GEARING AJH, 1993, IMMUNOL TODAY, V14, P506, DOI 10.1016/0167-5699(93)90267-O
   Gonzàlez-Porta M, 2013, GENOME BIOL, V14, DOI 10.1186/gb-2013-14-7-r70
   Haft DH, 2018, NUCLEIC ACIDS RES, V46, pD851, DOI 10.1093/nar/gkx1068
   Harrow J, 2012, GENOME RES, V22, P1760, DOI 10.1101/gr.135350.111
   Hatakeyama K, 2011, PROTEOMICS, V11, P2275, DOI 10.1002/pmic.201100016
   Haznedaroglu IC, 1998, ACTA HAEMATOL-BASEL, V99, P236
   Hon CC, 2017, NATURE, V543, P199, DOI 10.1038/nature21374
   Ingolia NT, 2009, SCIENCE, V324, P218, DOI 10.1126/science.1168978
   JAFFE EA, 1973, J CLIN INVEST, V52, P2745, DOI 10.1172/JCI107470
   Jorge I, 2009, MOL CELL PROTEOMICS, V8, P1130, DOI 10.1074/mcp.M800260-MCP200
   Kelkar DS, 2014, MOL CELL PROTEOMICS, V13, P3184, DOI 10.1074/mcp.M114.038299
   Kim D, 2015, NAT METHODS, V12, P357, DOI [10.1038/NMETH.3317, 10.1038/nmeth.3317]
   Kim MS, 2014, NATURE, V509, P575, DOI 10.1038/nature13302
   KOC Y, 1992, J RHEUMATOL, V19, P402
   Kulak NA, 2014, NAT METHODS, V11, P319, DOI [10.1038/NMETH.2834, 10.1038/nmeth.2834]
   Lee S, 2012, P NATL ACAD SCI USA, V109, pE2424, DOI 10.1073/pnas.1207846109
   Letunic I, 2009, NUCLEIC ACIDS RES, V37, pD229, DOI 10.1093/nar/gkn808
   Li H, 2009, BIOINFORMATICS, V25, P1754, DOI [10.1093/bioinformatics/btp698, 10.1093/bioinformatics/btp324, 10.1093/bioinformatics/btp352]
   Li YX, 2016, J PROTEOME RES, V15, P2309, DOI 10.1021/acs.jproteome.6b00344
   Low TY, 2013, CELL REP, V5, P1469, DOI 10.1016/j.celrep.2013.10.041
   Lundberg E, 2010, MOL SYST BIOL, V6, DOI 10.1038/msb.2010.106
   Maruhashi T, 2018, J HYPERTENS, V36, P1460, DOI 10.1097/HJH.0000000000001750
   McLaren W, 2016, GENOME BIOL, V17, DOI 10.1186/s13059-016-0974-4
   Melé M, 2015, SCIENCE, V348, P660, DOI 10.1126/science.aaa0355
   Michalik KM, 2014, CIRC RES, V114, P1389, DOI 10.1161/CIRCRESAHA.114.303265
   Mirsafian H, 2016, GENOMICS, V108, P37, DOI 10.1016/j.ygeno.2016.01.002
   Mitchell CJ, 2015, BMC SYST BIOL, V9, DOI 10.1186/s12918-015-0225-4
   Mohr T, 2017, PLOS ONE, V12, DOI 10.1371/journal.pone.0179065
   Molina H, 2005, MOL CELL PROTEOMICS, V4, P637, DOI 10.1074/mcp.M500042-MCP200
   Münzel T, 2008, ANN MED, V40, P180, DOI 10.1080/07853890701854702
   Na CH, 2018, GENOME RES, V28, P25, DOI 10.1101/gr.226050.117
   Nagaraj N, 2011, MOL SYST BIOL, V7, DOI 10.1038/msb.2011.81
   Nielsen H, 2017, METHODS MOL BIOL, V1611, P59, DOI 10.1007/978-1-4939-7015-5_6
   Omenn GS, 2017, J PROTEOME RES, V16, P4281, DOI 10.1021/acs.jproteome.7b00375
   Onat D, 2011, CURR DIABETES REP, V11, P193, DOI 10.1007/s11892-011-0182-2
   Or Nick H. K., 2017, POLICY STUD J, V45, pS67
   Ou K, 2008, J PROTEOME RES, V7, P1518, DOI 10.1021/pr700820g
   Oyama M, 2007, MOL CELL PROTEOMICS, V6, P1000, DOI 10.1074/mcp.M600297-MCP200
   Pandey A, 2000, NATURE, V405, P837, DOI 10.1038/35015709
   Patella F, 2016, J PROTEOME RES, V15, P2187, DOI 10.1021/acs.jproteome.6b00166
   Pertea M, 2015, NAT BIOTECHNOL, V33, P290, DOI 10.1038/nbt.3122
   Ping PP, 2005, PROTEOMICS, V5, P3506, DOI 10.1002/pmic.200500140
   Piskol R, 2013, AM J HUM GENET, V93, P641, DOI 10.1016/j.ajhg.2013.08.008
   Prasad TSK, 2017, GENOME RES, V27, P133, DOI 10.1101/gr.201368.115
   Prasad TSK, 2009, NUCLEIC ACIDS RES, V37, pD767, DOI 10.1093/nar/gkn892
   Ramsköld D, 2009, PLOS COMPUT BIOL, V5, DOI 10.1371/journal.pcbi.1000598
   Reid SE, 2017, EMBO J, V36, P2373, DOI 10.15252/embj.201694912
   Renuse S, 2011, PROTEOMICS, V11, P620, DOI 10.1002/pmic.201000615
   Schwanhäusser B, 2011, NATURE, V473, P337, DOI 10.1038/nature10098
   Tunica DG, 2009, PROTEOMICS, V9, P4991, DOI 10.1002/pmic.200900065
   Van Damme P, 2014, MOL CELL PROTEOMICS, V13, P1245, DOI 10.1074/mcp.M113.036442
   van Zijl F, 2011, MUTAT RES-REV MUTAT, V728, P23, DOI 10.1016/j.mrrev.2011.05.002
   Wang LG, 2012, BIOINFORMATICS, V28, P2184, DOI 10.1093/bioinformatics/bts356
   Wilhelm M, 2014, NATURE, V509, P582, DOI 10.1038/nature13319
   Wilks C, 2018, BIOINFORMATICS, V34, P114, DOI 10.1093/bioinformatics/btx547
   Wu J, 2007, J PROTEOME RES, V6, P4728, DOI 10.1021/pr070537c
   Xiao SJ, 2010, BIOINFORMATICS, V26, P1273, DOI 10.1093/bioinformatics/btq109
   Zhang J, 2011, PLOS ONE, V6, DOI 10.1371/journal.pone.0014525
   Zhu YF, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-03311-y
NR 73
TC 13
Z9 14
U1 0
U2 17
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 1615-9853
EI 1615-9861
J9 PROTEOMICS
JI Proteomics
PD AUG
PY 2019
VL 19
IS 15
AR 1800315
DI 10.1002/pmic.201800315
PG 14
WC Biochemical Research Methods; Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA IM5YI
UT WOS:000478069500005
PM 30983154
OA Green Published, Green Accepted, hybrid
DA 2025-04-10
ER

PT J
AU Kuo, FC
   Neville, MJ
   Sabaratnam, R
   Wesolowska-Andersen, A
   Phillips, D
   Wittemans, LBL
   van Dam, AD
   Loh, NY
   Todorcevic, M
   Denton, N
   Kentistou, KA
   Joshi, PK
   Christodoulides, C
   Langenberg, C
   Collas, P
   Karpe, F
   Pinnick, KE
AF Kuo, Feng-Chih
   Neville, Matt J.
   Sabaratnam, Rugivan
   Wesolowska-Andersen, Agata
   Phillips, Daniel
   Wittemans, Laura B. L.
   van Dam, Andrea D.
   Loh, Nellie Y.
   Todorcevic, Marijana
   Denton, Nathan
   Kentistou, Katherine A.
   Joshi, Peter K.
   Christodoulides, Constantinos
   Langenberg, Claudia
   Collas, Philippe
   Karpe, Fredrik
   Pinnick, Katherine E.
TI HOTAIR interacts with PRC2 complex regulating the regional
   preadipocyte transcriptome and human fat distribution
SO CELL REPORTS
LA English
DT Article
ID LONG NONCODING RNA; CARDIOVASCULAR RISK-FACTORS; GENOME-WIDE
   ASSOCIATION; ADIPOSE-TISSUE; LNCRNA HOTAIR; MOLECULAR-MECHANISMS;
   ADIPOCYTE; POLYCOMB; BIOLOGY; DIFFERENTIATION
AB Mechanisms governing regional human adipose tissue (AT) development remain undefined. Here, we show that the long non-coding RNA HOTAIR (HOX transcript antisense RNA) is exclusively expressed in gluteofe-moral AT, where it is essential for adipocyte development. We find that HOTAIR interacts with polycomb repressive complex 2 (PRC2) and we identify core HOTAIR-PRC2 target genes involved in adipocyte lineage determination. Repression of target genes coincides with PRC2 promoter occupancy and H3K27 trimethyla-tion. HOTAIR is also involved in modifying the gluteal adipocyte transcriptome through alternative splicing. Gluteal-specific expression of HOTAIR is maintained by defined regions of open chromatin across the HO-TAIR promoter. HOTAIR expression levels can be modified by hormonal (estrogen, glucocorticoids) and ge-netic variation (rs1443512 is a HOTAIR eQTL associated with reduced gynoid fat mass). These data identify HOTAIR as a dynamic regulator of the gluteal adipocyte transcriptome and epigenome with functional impor-tance for human regional AT development.
C1 [Kuo, Feng-Chih; Neville, Matt J.; Sabaratnam, Rugivan; Phillips, Daniel; van Dam, Andrea D.; Loh, Nellie Y.; Todorcevic, Marijana; Denton, Nathan; Christodoulides, Constantinos; Karpe, Fredrik; Pinnick, Katherine E.] Univ Oxford, Oxford Ctr Diabet Endocrinol & Metab, Radcliffe Dept Med, Churchill Hosp, Headington OX3 7LE, England.
   [Kuo, Feng-Chih] Natl Def Med Ctr, Triserv Gen Hosp, Divis Endocrinol & Metab, Dept Internal Med, Taipei, Taiwan.
   [Neville, Matt J.; Karpe, Fredrik] OUH Fdn Trust, NIHR Oxford Biomed Res Ctr, Oxford, England.
   [Sabaratnam, Rugivan] Univ Southern Denmark, Inst Clin Res, DK-5000 Odense C, Denmark.
   [Sabaratnam, Rugivan] Odense Univ Hosp, Steno Diabet Ctr Odense, DK-5000 Odense C, Denmark.
   [Wesolowska-Andersen, Agata] Univ Oxford, Wellcome Trust Ctr Human Genet, Roosevelt Dr, Oxford OX3 7BN, England.
   [Wittemans, Laura B. L.; Langenberg, Claudia] Univ Cambridge, MRC Epidemiol Unit, Inst Metab Sci, Sch Clin Med, Cambridge CB2 0QQ, England.
   [Wittemans, Laura B. L.] Univ Oxford, Big Data Inst, Li Ka Shing Ctr Hlth Informat & Discovery, Oxford, England.
   [Kentistou, Katherine A.; Joshi, Peter K.] Univ Edinburgh, Ctr Global Hlth Res, Usher Inst, Teviot Pl, Edinburgh EH8 9AG, Midlothian, Scotland.
   [Kentistou, Katherine A.] Univ Edinburgh, Ctr Cardiovas Sci, Queens Med Res Inst, Edinburgh EH16 4TJ, Midlothian, Scotland.
   [Collas, Philippe] Univ Oslo, Dept Mol Med, Inst Basic Med Sci, Fac Med, Oslo, Norway.
   [Collas, Philippe] Oslo Univ Hosp, Dept Immunol, Oslo, Norway.
C3 University of Oxford; National Defense Medical Center; Tri-Service
   General Hospital; University of Oxford; University of Southern Denmark;
   University of Southern Denmark; Odense University Hospital; University
   of Oxford; Wellcome Centre for Human Genetics; University of Cambridge;
   University of Oxford; University of Edinburgh; University of Edinburgh;
   University of Oslo; University of Oslo
RP Karpe, F; Pinnick, KE (corresponding author), Univ Oxford, Oxford Ctr Diabet Endocrinol & Metab, Radcliffe Dept Med, Churchill Hosp, Headington OX3 7LE, England.; Karpe, F (corresponding author), OUH Fdn Trust, NIHR Oxford Biomed Res Ctr, Oxford, England.
EM fredrik.karpe@ocdem.ox.ac.uk; katherine.pinnick@ocdem.ox.ac.uk
RI Langenberg, Claudia/ABG-9067-2021; Sabaratnam, Rugivan/ABC-5668-2021;
   Todorcevic, Marijana/MAI-0936-2025; Neville, Matt/IUN-5855-2023;
   Pinnick, Katherine/B-7209-2012; Collas, Philippe/IRZ-5918-2023
OI Kuo, Feng-Chih/0000-0003-3513-2487; Todorcevic,
   Marijana/0000-0002-3100-8799; Kentistou, Katherine/0000-0002-5816-664X;
   Sabaratnam, Rugivan/0000-0002-4085-1083; Langenberg,
   Claudia/0000-0002-5017-7344
CR Ameres SL, 2007, CELL, V130, P101, DOI 10.1016/j.cell.2007.04.037
   Aprile M, 2014, PPAR RES, V2014, DOI 10.1155/2014/537865
   Arner E, 2010, DIABETES, V59, P105, DOI 10.2337/db09-0942
   ARNER P, 1990, J CLIN INVEST, V85, P893, DOI 10.1172/JCI114516
   Aulchenko YS, 2007, BIOINFORMATICS, V23, P1294, DOI 10.1093/bioinformatics/btm108
   Bagchi DP, 2021, DIABETES, V70, P1419, DOI 10.2337/dbi20-0015
   Ben-Porath I, 2008, NAT GENET, V40, P499, DOI 10.1038/ng.127
   Bhan A, 2015, BBA-REV CANCER, V1856, P151, DOI 10.1016/j.bbcan.2015.07.001
   Bhan A, 2013, J MOL BIOL, V425, P3707, DOI 10.1016/j.jmb.2013.01.022
   Bhatlekar S, 2018, STEM CELLS INT, V2018, DOI 10.1155/2018/3569493
   Blake JA, 2014, DEVELOPMENT, V141, P737, DOI 10.1242/dev.091785
   Brockdorff N, 2013, RNA, V19, P429, DOI 10.1261/rna.037598.112
   Bycroft C, 2017, bioRxiv, DOI [10.1101/166298, 10.1101/166298, DOI 10.1101/166298, :10.1101/166298]
   Cabili MN, 2011, GENE DEV, V25, P1915, DOI 10.1101/gad.17446611
   Christodoulides C, 2009, TRENDS ENDOCRIN MET, V20, P16, DOI 10.1016/j.tem.2008.09.002
   Chu C, 2011, MOL CELL, V44, P667, DOI 10.1016/j.molcel.2011.08.027
   Collins JM, 2010, J BIOL CHEM, V285, P6044, DOI 10.1074/jbc.M109.053280
   Davidovich C, 2013, NAT STRUCT MOL BIOL, V20, P1250, DOI 10.1038/nsmb.2679
   Day N, 1999, BRIT J CANCER, V80, P95
   Dehghan A, 2021, MENOPAUSE, V28, P400, DOI 10.1097/GME.0000000000001721
   Divoux A, 2018, CLIN EPIGENETICS, V10, DOI 10.1186/s13148-018-0582-0
   Divoux A, 2014, OBESITY, V22, P1781, DOI 10.1002/oby.20793
   Dobin A, 2013, BIOINFORMATICS, V29, P15, DOI 10.1093/bioinformatics/bts635
   Fuerer C, 2010, PLOS ONE, V5, DOI 10.1371/journal.pone.0009370
   Gehrke S, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0082516
   Guo WB, 2021, RNA BIOL, V18, P1574, DOI 10.1080/15476286.2020.1858253
   Hajjari Mohammadreza, 2017, Genomics & Informatics, V15, P170, DOI 10.5808/GI.2017.15.4.170
   Haller T, 2015, BRIEF BIOINFORM, V16, P39, DOI 10.1093/bib/bbt066
   Hauner H, 2000, METH MOL B, V155, P239
   Hernandez-Quiles M, 2021, FRONT ENDOCRINOL, V12, DOI 10.3389/fendo.2021.624112
   Hu WQ, 2012, EMBO REP, V13, P971, DOI 10.1038/embor.2012.145
   Kalwa M, 2016, NUCLEIC ACIDS RES, V44, P10631, DOI 10.1093/nar/gkw802
   Kang HM, 2018, NAT BIOTECHNOL, V36, P89, DOI 10.1038/nbt.4042
   Karastergiou K, 2013, J CLIN ENDOCR METAB, V98, P362, DOI 10.1210/jc.2012-2953
   Karpe F, 2018, INT J EPIDEMIOL, V47, P21, DOI 10.1093/ije/dyx132
   Karpe F, 2015, NAT REV ENDOCRINOL, V11, P90, DOI 10.1038/nrendo.2014.185
   Khan A, 2018, NUCLEIC ACIDS RES, V46, pD260, DOI [10.1093/nar/gkx1126, 10.1093/nar/gkx1188]
   Kuo FC, 2022, MOL METAB, V60, DOI 10.1016/j.molmet.2022.101473
   Lachmann A, 2010, BIOINFORMATICS, V26, P2438, DOI 10.1093/bioinformatics/btq466
   Langfelder P, 2008, BMC BIOINFORMATICS, V9, DOI 10.1186/1471-2105-9-559
   Laugesen A, 2019, MOL CELL, V74, P8, DOI 10.1016/j.molcel.2019.03.011
   Lee MJ, 2014, BBA-MOL BASIS DIS, V1842, P473, DOI 10.1016/j.bbadis.2013.05.029
   Lee TI, 2006, CELL, V125, P301, DOI 10.1016/j.cell.2006.02.043
   Lennox KA, 2016, NUCLEIC ACIDS RES, V44, P863, DOI 10.1093/nar/gkv1206
   Li N, 2003, GENETICS, V165, P2213
   Liao Y, 2014, BIOINFORMATICS, V30, P923, DOI 10.1093/bioinformatics/btt656
   Loh NY, 2015, CELL METAB, V21, P262, DOI 10.1016/j.cmet.2015.01.009
   Loh PR, 2015, NAT GENET, V47, P284, DOI 10.1038/ng.3190
   Lotta LA, 2018, JAMA-J AM MED ASSOC, V320, P2553, DOI 10.1001/jama.2018.19329
   Lotta LA, 2016, PLOS MED, V13, DOI 10.1371/journal.pmed.1002179
   Lotta LA, 2017, NAT GENET, V49, P17, DOI 10.1038/ng.3714
   Love MI, 2014, GENOME BIOL, V15, DOI 10.1186/s13059-014-0550-8
   Ma LN, 2013, RNA BIOL, V10, P925, DOI 10.4161/rna.24604
   Macotela Y, 2012, DIABETES, V61, P1691, DOI 10.2337/db11-1753
   Marchini J, 2007, NAT GENET, V39, P906, DOI 10.1038/ng2088
   Mazin PV, 2021, NAT GENET, V53, P925, DOI 10.1038/s41588-021-00851-w
   McQuillan R, 2008, AM J HUM GENET, V83, P359, DOI 10.1016/j.ajhg.2008.08.007
   Meissner A, 2008, NATURE, V454, P766, DOI 10.1038/nature07107
   Milevskiy MJG, 2016, HUM MOL GENET, V25, P3269, DOI 10.1093/hmg/ddw177
   Miller KL, 2016, NAT NEUROSCI, V19, P1523, DOI 10.1038/nn.4393
   Neville MJ, 2019, PLOS ONE, V14, DOI 10.1371/journal.pone.0217644
   Neville MJ, 2011, OBESITY, V19, P888, DOI 10.1038/oby.2010.257
   Nguyen ED, 2018, RNA BIOL, V15, P901, DOI 10.1080/15476286.2018.1474072
   Passaro A, 2017, BMC GENOMICS, V18, DOI 10.1186/s12864-017-3564-2
   Patro R, 2017, NAT METHODS, V14, P417, DOI 10.1038/nmeth.4197
   Pinnick KE, 2014, DIABETES, V63, P3785, DOI 10.2337/db14-0385
   Pisignano G, 2021, NON-CODING RNA, V7, DOI 10.3390/ncrna7010021
   Portoso M, 2017, EMBO J, V36, P981, DOI 10.15252/embj.201695335
   Raudvere U, 2019, NUCLEIC ACIDS RES, V47, pW191, DOI 10.1093/nar/gkz369
   Rinn JL, 2007, CELL, V129, P1311, DOI 10.1016/j.cell.2007.05.022
   Ritchie ME, 2015, NUCLEIC ACIDS RES, V43, DOI 10.1093/nar/gkv007
   Sarma Kavitha, 2010, Proc Natl Acad Sci U S A, V107, P22196, DOI 10.1073/pnas.1009785107
   Sherman BT, 2022, NUCLEIC ACIDS RES, V50, pW216, DOI 10.1093/nar/gkac194
   Shlyueva D, 2014, NAT REV GENET, V15, P272, DOI 10.1038/nrg3682
   Shungin D, 2015, NATURE, V518, P187, DOI 10.1038/nature14132
   Somarowthu S, 2015, MOL CELL, V58, P353, DOI 10.1016/j.molcel.2015.03.006
   Soneson Charlotte, 2015, F1000Res, V4, P1521, DOI 10.12688/f1000research.7563.2
   Sun L, 2019, DIABETES, V68, P887, DOI 10.2337/dbi18-0009
   Sun L, 2013, P NATL ACAD SCI USA, V110, P3387, DOI 10.1073/pnas.1222643110
   Tchkonia T, 2007, AM J PHYSIOL-ENDOC M, V292, pE298, DOI 10.1152/ajpendo.00202.2006
   Tchoukalova YD, 2010, P NATL ACAD SCI USA, V107, P18226, DOI 10.1073/pnas.1005259107
   Todorcevic M, 2017, ADIPOCYTE, V6, P40, DOI 10.1080/21623945.2016.1277052
   TOMIYAMA K, 1995, BIOCHEM BIOPH RES CO, V212, P263, DOI 10.1006/bbrc.1995.1965
   Trincado JL, 2018, GENOME BIOL, V19, DOI 10.1186/s13059-018-1417-1
   Tsai MC, 2010, SCIENCE, V329, P689, DOI 10.1126/science.1192002
   Ulitsky I, 2011, CELL, V147, P1537, DOI 10.1016/j.cell.2011.11.055
   Vazquez G, 2007, EPIDEMIOL REV, V29, P115, DOI 10.1093/epirev/mxm008
   Viechtbauer W, 2010, J STAT SOFTW, V36, P1, DOI 10.18637/jss.v036.i03
   WAHRENBERG H, 1989, J CLIN INVEST, V84, P458, DOI 10.1172/JCI114187
   Waldén TB, 2012, AM J PHYSIOL-ENDOC M, V302, pE19, DOI 10.1152/ajpendo.00249.2011
   Wan LX, 2018, MOL CELL, V69, P279, DOI 10.1016/j.molcel.2017.12.024
   Wang KC, 2011, MOL CELL, V43, P904, DOI 10.1016/j.molcel.2011.08.018
   Wang LF, 2010, P NATL ACAD SCI USA, V107, P7317, DOI 10.1073/pnas.1000031107
   Wang SS, 2019, CELL DEATH DIS, V10, DOI 10.1038/s41419-019-1742-7
   Wassef M, 2019, P NATL ACAD SCI USA, V116, P6075, DOI 10.1073/pnas.1814634116
   Watanabe K, 2017, NAT COMMUN, V8, DOI 10.1038/s41467-017-01261-5
   Wells JCK, 2007, BEST PRACT RES CL EN, V21, P415, DOI 10.1016/j.beem.2007.04.007
   Wiklund P, 2008, J CLIN ENDOCR METAB, V93, P4360, DOI 10.1210/jc.2008-0804
   Yusuf S, 2005, LANCET, V366, P1640, DOI 10.1016/S0140-6736(05)67663-5
   Zhang XH, 2019, MOL CELL BIOL, V39, DOI 10.1128/MCB.00251-19
NR 100
TC 27
Z9 28
U1 3
U2 8
PU CELL PRESS
PI CAMBRIDGE
PA 50 HAMPSHIRE ST, FLOOR 5, CAMBRIDGE, MA 02139 USA
SN 2211-1247
J9 CELL REP
JI Cell Reports
PD JUL 26
PY 2022
VL 40
IS 4
AR 111136
DI 10.1016/j.celrep.2022.111136
EA JUL 2022
PG 23
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA 3W5EE
UT WOS:000842366700006
PM 35905723
OA gold, Green Published, Green Submitted
DA 2025-04-10
ER

PT J
AU Hua, H
   Zhang, HY
   Kong, QB
   Jiang, YF
AF Hua, Hui
   Zhang, Hongying
   Kong, Qingbin
   Jiang, Yangfu
TI Mechanisms for estrogen receptor expression in human cancer
SO EXPERIMENTAL HEMATOLOGY & ONCOLOGY
LA English
DT Review
DE Cancer; Estrogen receptor; Transcription; Epigenetic modification
ID HUMAN BREAST-CANCER; ALPHA MESSENGER-RNA; AU-RICH ELEMENTS; ER-ALPHA;
   HEPATOCELLULAR-CARCINOMA; GENE-EXPRESSION; BETA ISOFORMS; TRANSCRIPTION
   FACTORS; CELL-LINES; 3'-UNTRANSLATED REGION
AB Estrogen is a steroid hormone that has critical roles in reproductive development, bone homeostasis, cardiovascular remodeling and brain functions. However, estrogen also promotes mammary, ovarian and endometrial tumorigenesis. Estrogen antagonists and drugs that reduce estrogen biosynthesis have become highly successful therapeutic agents for breast cancer patients. The effects of estrogen are largely mediated by estrogen receptor (ER) alpha and ER alpha, which are members of the nuclear receptor superfamily of transcription factors. The mechanisms underlying the aberrant expression of ER in breast cancer and other types of human tumors are complex, involving considerable alternative splicing of ER alpha and ER beta, transcription factors, epigenetic and post-transcriptional regulation of ER expression. Elucidation of mechanisms for ER expression may not only help understand cancer progression and evolution, but also shed light on overcoming endocrine therapy resistance. Herein, we review the complex mechanisms for regulating ER expression in human cancer.
C1 [Hua, Hui] Sichuan Univ, West China Hosp, Lab Stem Cell Biol, Chengdu, Sichuan, Peoples R China.
   [Zhang, Hongying; Kong, Qingbin; Jiang, Yangfu] Sichuan Univ, West China Hosp, Lab Oncogene, Chengdu, Sichuan, Peoples R China.
C3 Sichuan University; Sichuan University
RP Hua, H (corresponding author), Sichuan Univ, West China Hosp, Lab Stem Cell Biol, Chengdu, Sichuan, Peoples R China.
EM huahuihuaxi@163.com
RI Jiang, Yangfu/AAX-2645-2020
OI Jiang, Yangfu/0000-0002-8696-2651
CR Abdi J, 2017, J HEMATOL ONCOL, V10, DOI 10.1186/s13045-017-0538-4
   Adams BD, 2007, MOL ENDOCRINOL, V21, P1132, DOI 10.1210/me.2007-0022
   Adlanmerini M, 2014, P NATL ACAD SCI USA, V111, pE283, DOI 10.1073/pnas.1322057111
   Al-Nakhle H, 2010, CANCER RES, V70, P4778, DOI 10.1158/0008-5472.CAN-09-4104
   Alferez DG, 2018, CURR STEM CELL REP, V4, P81, DOI 10.1007/s40778-018-0114-z
   Allred DC, 2004, BREAST CANCER RES, V6, P240, DOI 10.1186/bcr938
   Anderson E, 1998, J MAMMARY GLAND BIOL, V3, P23, DOI 10.1023/A:1018718117113
   Andersson A, 2018, J ENDOCRINOL, V236, P99, DOI 10.1530/JOE-17-0372
   Arnal JF, 2017, PHYSIOL REV, V97, P1045, DOI 10.1152/physrev.00024.2016
   Asselin-Labat ML, 2007, NAT CELL BIOL, V9, P201, DOI 10.1038/ncb1530
   Backes FJ, 2016, GYNECOL ONCOL, V141, P312, DOI 10.1016/j.ygyno.2016.03.006
   Bertucci F, 2009, INT J CANCER, V124, P1338, DOI 10.1002/ijc.24055
   Bialesova L, 2017, ONCOTARGET, V8, P76622, DOI 10.18632/oncotarget.20635
   Bondesson M, 2015, BBA-GENE REGUL MECH, V1849, P142, DOI 10.1016/j.bbagrm.2014.06.005
   Bozovic A, 2013, MED ONCOL, V30, DOI 10.1007/s12032-013-0642-4
   Brufsky AM, 2018, ONCOLOGIST, V23, P528, DOI 10.1634/theoncologist.2017-0423
   BUDWITNOVOTNY DA, 1986, CANCER RES, V46, P5419
   Cai W, 2008, MOL CELL BIOL, V28, P784, DOI 10.1128/MCB.00233-07
   Castellano L, 2009, P NATL ACAD SCI USA, V106, P15732, DOI 10.1073/pnas.0906947106
   Chan KKL, 2008, OBSTET GYNECOL, V111, P144, DOI 10.1097/01.AOG.0000296715.07705.e9
   Chantalat E, 2016, BREAST CANCER RES, V18, DOI 10.1186/s13058-016-0780-7
   CHAPPEL SC, 1991, HUM REPROD, V6, P1206, DOI 10.1093/oxfordjournals.humrep.a137513
   CHEN CYA, 1995, MOL CELL BIOL, V15, P5777
   Chu I, 2007, J CLIN INVEST, V117, P2205, DOI 10.1172/JCI21739
   Cicatiello L, 2010, AM J PATHOL, V176, P2113, DOI 10.2353/ajpath.2010.090837
   Ciucci A, 2014, GYNECOL ONCOL, V132, P351, DOI 10.1016/j.ygyno.2013.12.027
   COMB M, 1990, NUCLEIC ACIDS RES, V18, P3975, DOI 10.1093/nar/18.13.3975
   Couse JF, 1999, ENDOCR REV, V20, P358, DOI 10.1210/er.20.3.358
   Cui J, 2013, TRENDS MOL MED, V19, P197, DOI 10.1016/j.molmed.2012.12.007
   Chuffa LGD, 2017, STEROIDS, V118, P93, DOI 10.1016/j.steroids.2016.12.011
   Demetriadou Christina, 2017, Critical Reviews in Oncogenesis, V22, P195, DOI 10.1615/CritRevOncog.2017024506
   Dey P, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0128239
   Di Leva G, 2010, JNCI-J NATL CANCER I, V102, P706, DOI 10.1093/jnci/djq102
   Duan RQ, 2008, MOL CELL ENDOCRINOL, V281, P9, DOI 10.1016/j.mce.2007.10.004
   Dubal DB, 2001, P NATL ACAD SCI USA, V98, P1952, DOI 10.1073/pnas.98.4.1952
   Dunnwald LK, 2007, BREAST CANCER RES, V9, DOI 10.1186/bcr1639
   Eeckhoute J, 2007, CANCER RES, V67, P6477, DOI 10.1158/0008-5472.CAN-07-0746
   Faria Michelle, 2018, Oncotarget, V9, P12201, DOI 10.18632/oncotarget.24134
   FERGUSON AT, 1995, CANCER RES, V55, P2279
   Finlay-Schultz J, 2017, CANCER RES, V77, P4934, DOI 10.1158/0008-5472.CAN-16-3541
   Flouriot G, 2000, EMBO J, V19, P4688, DOI 10.1093/emboj/19.17.4688
   Folkerd EJ, 2010, J CLIN ONCOL, V28, P4038, DOI 10.1200/JCO.2009.27.4290
   Fox EM, 2008, STEROIDS, V73, P1039, DOI 10.1016/j.steroids.2008.04.006
   Frasor J, 2015, MOL CELL ENDOCRINOL, V418, P235, DOI 10.1016/j.mce.2014.09.013
   Fujiwara T, 2017, TOHOKU J EXP MED, V242, P83, DOI 10.1620/tjem.242.83
   Gala K, 2018, ONCOGENE, V37, P4692, DOI 10.1038/s41388-018-0273-5
   Gee JMW, 2001, INT J CANCER, V95, P247, DOI 10.1002/1097-0215(20010720)95:4<247::AID-IJC1042>3.0.CO;2-S
   Grabinski N, 2014, CELL SIGNAL, V26, P1021, DOI 10.1016/j.cellsig.2014.01.018
   GREEN S, 1986, NATURE, V320, P134, DOI 10.1038/320134a0
   Guo YW, 2017, PLOS ONE, V12, DOI 10.1371/journal.pone.0174843
   Guttilla IK, 2012, TRENDS ENDOCRIN MET, V23, P73, DOI 10.1016/j.tem.2011.12.001
   Hadjimarkou MM, 2018, J STEROID BIOCHEM, V176, P57, DOI 10.1016/j.jsbmb.2017.04.012
   Hall JM, 1999, ENDOCRINOLOGY, V140, P5566, DOI 10.1210/en.140.12.5566
   Hall JM, 2001, J BIOL CHEM, V276, P36869, DOI 10.1074/jbc.R100029200
   Hamilton KJ, 2017, CURR TOP DEV BIOL, V125, P109, DOI 10.1016/bs.ctdb.2016.12.005
   Harris HA, 2003, ENDOCRINOLOGY, V144, P4241, DOI 10.1210/en.2003-0550
   Hastings MH, 2018, NAT REV NEUROSCI, V19, P453, DOI 10.1038/s41583-018-0026-z
   HATCH KD, 1991, CANCER, V68, P269, DOI 10.1002/1097-0142(19910715)68:2<269::AID-CNCR2820680209>3.0.CO;2-O
   Hattori Y, 2015, GENE, V571, P117, DOI 10.1016/j.gene.2015.06.086
   Hedges VL, 2018, ENDOCRINOLOGY, V159, P1328, DOI 10.1210/en.2018-00039
   Hewitt SC, 2018, ENDOCR REV, V39, P664, DOI 10.1210/er.2018-00087
   Hewitt SC, 2016, J MOL ENDOCRINOL, V56, pR55, DOI 10.1530/JME-15-0254
   Hirata S, 2001, J STEROID BIOCHEM, V78, P33, DOI 10.1016/S0960-0760(01)00071-1
   Hirschfeld M, 2015, BMC CANCER, V15, DOI 10.1186/s12885-015-1088-1
   Honma N, 2008, J CLIN ONCOL, V26, P3727, DOI 10.1200/JCO.2007.14.2968
   Hu XC, 2017, J HEMATOL ONCOL, V10, DOI 10.1186/s13045-017-0466-3
   Igarashi H, 2001, P NATL ACAD SCI USA, V98, P15131, DOI 10.1073/pnas.011513098
   Ikeda K, 2015, ACTA PHARMACOL SIN, V36, P24, DOI 10.1038/aps.2014.123
   Ikeda Y, 2006, BRAIN RES, V1083, P39, DOI 10.1016/j.brainres.2006.02.025
   Ing NH, 2008, J BIOL CHEM, V283, P1764, DOI 10.1074/jbc.M704745200
   Iorio MV, 2005, CANCER RES, V65, P7065, DOI 10.1158/0008-5472.CAN-05-1783
   Iyer JK, 2017, WORLD J GASTROENTERO, V23, P6802, DOI 10.3748/wjg.v23.i37.6802
   Jeng MH, 2000, BREAST CANCER RES TR, V62, P167, DOI 10.1023/A:1006406030612
   Jiang CF, 2018, MOL CANCER, V17, DOI 10.1186/s12943-018-0830-0
   Jiménez-Gardnno AM, 2017, BIOCHEM BIOPH RES CO, V490, P780, DOI 10.1016/j.bbrc.2017.06.117
   Johnson KE, 2017, ARTERIOSCL THROM VAS, V37, P664, DOI 10.1161/ATVBAHA.116.308791
   JOHNSTON SRD, 1995, CANCER RES, V55, P3331
   Kenealy MR, 2000, ENDOCRINOLOGY, V141, P2805, DOI 10.1210/en.141.8.2805
   Kewley RJ, 2004, INT J BIOCHEM CELL B, V36, P189, DOI 10.1016/S1357-2725(03)00211-5
   Knutson TP, 2017, J HEMATOL ONCOL, V10, DOI 10.1186/s13045-017-0462-7
   Kos M, 2001, MOL ENDOCRINOL, V15, P2057, DOI 10.1210/me.15.12.2057
   Krege JH, 1998, P NATL ACAD SCI USA, V95, P15677, DOI 10.1073/pnas.95.26.15677
   Kuiper GGJM, 1996, P NATL ACAD SCI USA, V93, P5925, DOI 10.1073/pnas.93.12.5925
   Laflamme N, 1998, J NEUROBIOL, V36, P357, DOI 10.1002/(SICI)1097-4695(19980905)36:3<357::AID-NEU5>3.0.CO;2-V
   Leung YK, 2006, P NATL ACAD SCI USA, V103, P13162, DOI 10.1073/pnas.0605676103
   Li XR, 2010, ENDOCRINOLOGY, V151, P2462, DOI 10.1210/en.2009-1150
   Liu JY, 2018, CANCER RES, V78, P3176, DOI 10.1158/0008-5472.CAN-17-3470
   Louie MC, 2017, AM J CANCER RES, V7, P1617
   Madureira PA, 2006, J BIOL CHEM, V281, P25167, DOI 10.1074/jbc.M603906200
   Mallepell S, 2006, P NATL ACAD SCI USA, V103, P2196, DOI 10.1073/pnas.0510974103
   McPherson LA, 1999, NUCLEIC ACIDS RES, V27, P4040, DOI 10.1093/nar/27.20.4040
   Millour J, 2010, ONCOGENE, V29, P2983, DOI 10.1038/onc.2010.47
   Moore JT, 1998, BIOCHEM BIOPH RES CO, V247, P75, DOI 10.1006/bbrc.1998.8738
   Morselli E, 2018, AM J PHYSIOL-ENDOC M, V315, pE7, DOI 10.1152/ajpendo.00473.2017
   Mungenast F, 2014, FRONT ENDOCRINOL, V5, DOI 10.3389/fendo.2014.00192
   Munzone E, 2006, BREAST CANCER RES, V8, DOI 10.1186/bcr1366
   Nebbioso A, 2018, PLOS GENET, V14, DOI 10.1371/journal.pgen.1007362
   Nilsson S, 2011, NAT REV DRUG DISCOV, V10, P778, DOI 10.1038/nrd3551
   Oh AS, 2001, MOL ENDOCRINOL, V15, P1344, DOI 10.1210/me.15.8.1344
   Ohe K, 2018, FRONT MOL BIOSCI, V5, DOI 10.3389/fmolb.2018.00052
   Ohe K, 2018, J STEROID BIOCHEM, V182, P21, DOI 10.1016/j.jsbmb.2018.04.007
   Ohshiro K, 2010, MOL ENDOCRINOL, V24, P914, DOI 10.1210/me.2009-0413
   Omarjee S, 2017, ONCOGENE, V36, P2503, DOI 10.1038/onc.2016.415
   Ormandy CJ, 2003, RECENT PROG HORM RES, V58, P297, DOI 10.1210/rp.58.1.297
   Pandey DP, 2009, MOL CELL BIOL, V29, P3783, DOI 10.1128/MCB.01875-08
   Paris O, 2012, ONCOGENE, V31, P4196, DOI 10.1038/onc.2011.583
   Pellikainen JM, 2007, INT J CANCER, V120, P2061, DOI 10.1002/ijc.22648
   Peng B, 2003, J MOL ENDOCRINOL, V30, P13, DOI 10.1677/jme.0.0300013
   Pfeffer U, 1996, J STEROID BIOCHEM, V56, P99, DOI 10.1016/0960-0760(95)00227-8
   Pink JJ, 1996, NUCLEIC ACIDS RES, V24, P962, DOI 10.1093/nar/24.5.962
   Pratt WB, 1997, ENDOCR REV, V18, P306, DOI 10.1210/er.18.3.306
   Pryzbylkowski P, 2008, BREAST CANCER RES TR, V111, P15, DOI 10.1007/s10549-007-9751-0
   Reese JM, 2014, BMC CANCER, V14, DOI 10.1186/1471-2407-14-749
   Repsold L, 2016, EXP HEMATOL ONCOL, V5, DOI 10.1186/s40164-016-0048-z
   Rooney AM, 2017, ANN NY ACAD SCI, V1410, P85, DOI 10.1111/nyas.13523
   Sanders DA, 2013, GENOME BIOL, V14, DOI 10.1186/gb-2013-14-1-r6
   Sas L, 2012, BREAST CANCER RES, V14, DOI 10.1186/bcr3196
   Schuur ER, 2001, J BIOL CHEM, V276, P15519, DOI 10.1074/jbc.M009001200
   Seto K, 2016, INT J BIOCHEM CELL B, V76, P115, DOI 10.1016/j.biocel.2016.04.018
   Sheng ML, 2014, HEPATO-GASTROENTEROL, V61, P146, DOI 10.5754/hge11859
   Shults CL, 2018, NEUROBIOL AGING, V61, P13, DOI 10.1016/j.neurobiolaging.2017.09.005
   Simpson ER, 2001, ENDOCRINOLOGY, V142, P4589, DOI 10.1210/en.142.11.4589
   Soderqvist G, 1997, AM J OBSTET GYNECOL, V176, P123, DOI 10.1016/S0002-9378(97)80024-5
   Sogon T, 2007, J STEROID BIOCHEM, V105, P106, DOI 10.1016/j.jsbmb.2006.12.104
   Stark K, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0074525
   Stevanato PR, 2018, PATHOL ONCOL RES, V24, P533, DOI 10.1007/s12253-017-0268-5
   Sukocheva OA, 2018, WORLD J GASTROENTERO, V24, P1, DOI 10.3748/wjg.v24.i1.1
   Sun Q, 2017, BIOCHEM BIOPH RES CO, V487, P625, DOI 10.1016/j.bbrc.2017.04.105
   Suzuki A, 2017, ONCOL LETT, V14, P891, DOI 10.3892/ol.2017.6216
   Suzuki F, 2008, CANCER SCI, V99, P2365, DOI 10.1111/j.1349-7006.2008.00988.x
   Tanimoto K, 1999, NUCLEIC ACIDS RES, V27, P903, DOI 10.1093/nar/27.3.903
   Tsuboi K, 2017, J STEROID BIOCHEM, V171, P209, DOI 10.1016/j.jsbmb.2017.04.001
   Turner BC, 1998, CANCER RES, V58, P5466
   Urano T, 2002, NATURE, V417, P871, DOI 10.1038/nature00826
   WALTER P, 1985, P NATL ACAD SCI USA, V82, P7889, DOI 10.1073/pnas.82.23.7889
   Wang J, 2015, BREAST CANCER RES TR, V152, P255, DOI 10.1007/s10549-015-3467-3
   Wang LQ, 2017, J HEMATOL ONCOL, V10, DOI 10.1186/s13045-017-0526-8
   Wang XB, 2009, MOL CELL BIOL, V29, P3832, DOI 10.1128/MCB.00032-09
   Wang ZY, 2006, P NATL ACAD SCI USA, V103, P9063, DOI 10.1073/pnas.0603339103
   Welboren WJ, 2009, EMBO J, V28, P1418, DOI 10.1038/emboj.2009.88
   Whitesell L, 2014, P NATL ACAD SCI USA, V111, P18297, DOI 10.1073/pnas.1421323111
   Wimberly H, 2014, BREAST CANCER RES TR, V146, P657, DOI 10.1007/s10549-014-3050-3
   Wu CS, 2016, J HEMATOL ONCOL, V9, DOI 10.1186/s13045-016-0349-z
   Xu HX, 2017, J HEMATOL ONCOL, V10, DOI 10.1186/s13045-017-0467-2
   Xu NH, 1997, MOL CELL BIOL, V17, P4611, DOI 10.1128/MCB.17.8.4611
   Xu Y, 2018, MOL METAB, V15, P104, DOI 10.1016/j.molmet.2018.05.012
   Yan L, 2003, CANCER BIOL THER, V2, P552, DOI 10.4161/cbt.2.5.469
   Yang XW, 2001, CANCER RES, V61, P7025
   Yoshida T, 2000, CARCINOGENESIS, V21, P2193, DOI 10.1093/carcin/21.12.2193
   You H, 2018, STEROIDS, V134, P78, DOI 10.1016/j.steroids.2018.02.007
   Yu SN, 2017, EXP HEMATOL ONCOL, V6, DOI 10.1186/s40164-017-0091-4
   Zhang J, 2016, BMC CANCER, V16, DOI 10.1186/s12885-016-2928-3
   Zhang JB, 2017, CELL DEATH DIS, V8, DOI 10.1038/cddis.2017.154
   Zhang WJ, 2018, CANCER RES, V78, P4915, DOI 10.1158/0008-5472.CAN-18-0069
   Zhang X, 2007, ONCOGENE, V26, P7346, DOI 10.1038/sj.onc.1210537
   Zhao CY, 2003, ONCOGENE, V22, P7600, DOI 10.1038/sj.onc.1207100
   Zheng B, 2017, SCI CHINA LIFE SCI, V60, P575, DOI 10.1007/s11427-016-9043-9
   Zhou Y, 2016, J MOL MED, V94, P887, DOI 10.1007/s00109-016-1396-1
   Zhu L, 2018, MOL METAB, V8, P106, DOI 10.1016/j.molmet.2017.12.012
   Zou YY, 2008, BREAST CANCER RES, V10, DOI 10.1186/bcr1872
NR 160
TC 148
Z9 162
U1 4
U2 37
PU BMC
PI LONDON
PA CAMPUS, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
EI 2162-3619
J9 EXP HEMATOL ONCOL
JI Exp. Hematol. Oncol.
PD SEP 19
PY 2018
VL 7
AR 24
DI 10.1186/s40164-018-0116-7
PG 11
WC Oncology; Hematology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Oncology; Hematology
GA GU3BM
UT WOS:000445148700001
PM 30250760
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Davies, WL
   Vandenberg, JI
   Sayeed, RA
   Trezise, AEO
AF Davies, WL
   Vandenberg, JI
   Sayeed, RA
   Trezise, AEO
TI Cardiac expression of the cystic fibrosis transmembrane conductance
   regulator involves novel Exon 1 usage to produce a unique amino-terminal
   protein
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID CFTR CHLORIDE CHANNELS; OPEN READING FRAME; DECARBOXYLASE MESSENGER-RNA;
   SECONDARY STRUCTURE; MULTIDRUG-RESISTANCE; CL-CHANNELS; ANTISENSE
   OLIGODEOXYNUCLEOTIDE; DEVELOPMENTAL REGULATION; TRANSLATIONAL CONTROL;
   VENTRICULAR MYOCYTES
AB Cystic fibrosis is caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene, which encodes a chloride channel present in many cells. In cardiomyocytes, we report that multiple exon 1 usage and alternative splicing produces four CFTR transcripts, with different 5'-untranslated regions, CFTRTRAD-139, CFTR-1C/-1A, CFTR-1C, and CFTR-1B. CFTR transcripts containing the novel upstream exons (exons -1C, -1B, and -1A) represent more than 90% of cardiac expressed CFTR mRNA. Regulation of cardiac CFTR expression, in response to developmental and pathological stimuli, is exclusively due to the modulation of CFTR-1C and CFTR-1C/-1A expression. Upstream open reading frames have been identified in the 5'-untranslated regions of all CFTR transcripts that, in conjunction with adjacent stem-loop structures, modulate the efficiency of translation initiation at the AUG codon of the main CFTR coding region in CFTRTRAD-139 and CFTR-1C/-1A transcripts. Exon(-1A), only present in CFTR-1C/-1A transcripts, encodes an AUG codon that is in-frame with the main CFTR open reading frame, the efficient translation of which produces a novel CFTR protein isoform with a curtailed amino terminus. As the expression of this CFTR transcript parallels the spatial and temporal distribution of the cAMP-activated whole-cell current density in normal and diseased hearts, we suggest that CFTR-1C/-1A provides the molecular basis for the cardiac cAMP-activated chloride channel. Our findings provide further insight into the complex nature of in vivo CFTR expression, to which multiple mRNA transcripts, protein isoforms, and post-transcriptional regulatory mechanisms are now added.
C1 Univ Queensland, Sch Biomed Sci, Brisbane, Qld 4072, Australia.
   Univ Cambridge, Dept Biochem, Cambridge CB2 1QW, England.
   Victor Chang Cardiac Res Inst, Sydney, NSW 2010, Australia.
C3 University of Queensland; University of Cambridge; Victor Chang Cardiac
   Research Institute
RP Univ Queensland, Sch Biomed Sci, Brisbane, Qld 4072, Australia.
EM ann.trezise@uq.edu.au
RI Vandenberg, Jamie/B-6608-2013; Sayeed, Rana Ahmed/S-7736-2019; Davies,
   Wayne/I-1547-2014
OI Vandenberg, Jamie/0000-0002-3859-3716; Sayeed, Rana
   Ahmed/0000-0002-2887-1874; Davies, Wayne/0000-0003-0232-1812
CR ANDERSON MP, 1991, SCIENCE, V253, P202, DOI 10.1126/science.1712984
   [Anonymous], 1999, RNA BIOCH BIOTECHNOL
   Antzelevitch C, 1995, CARDIAC ELECTROPHYSI
   BAHINSKI A, 1989, NATURE, V340, P718, DOI 10.1038/340718a0
   BEAR CE, 1992, CELL, V68, P809, DOI 10.1016/0092-8674(92)90155-6
   CARROLL TP, 1995, J BIOL CHEM, V270, P11941, DOI 10.1074/jbc.270.20.11941
   Chang G, 2001, SCIENCE, V293, P1793, DOI 10.1126/science.293.5536.1793
   CHERON G, 1984, ACTA PAEDIATR SCAND, V73, P697, DOI 10.1111/j.1651-2227.1984.tb09999.x
   CHIEN KR, 1993, ANNU REV PHYSIOL, V55, P77, DOI 10.1146/annurev.ph.55.030193.000453
   CHIEN KR, 1991, FASEB J, V5, P3037, DOI 10.1096/fasebj.5.15.1835945
   Child SJ, 1999, J BIOL CHEM, V274, P24335, DOI 10.1074/jbc.274.34.24335
   CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
   DAVIES W, 2002, THESIS U CAMBRIDGE C
   GADSBY DC, 1995, ANNU REV PHYSIOL, V57, P387
   Ganeshan R, 2003, J BIOL CHEM, V278, P2876, DOI 10.1074/jbc.M211790200
   Guarnieri C, 1985, Adv Myocardiol, V5, P191
   Guhaniyogi J, 2001, GENE, V265, P11, DOI 10.1016/S0378-1119(01)00350-X
   HART G, 1994, CARDIOVASC RES, V28, P933, DOI 10.1093/cvr/28.7.933
   Hart P, 1996, P NATL ACAD SCI USA, V93, P6343, DOI 10.1073/pnas.93.13.6343
   HILL JR, 1993, J BIOL CHEM, V268, P726
   HOROWITZ B, 1993, AM J PHYSIOL, V264, pH2214, DOI 10.1152/ajpheart.1993.264.6.H2214
   HYDE SC, 1990, NATURE, V346, P362, DOI 10.1038/346362a0
   James AF, 1996, CIRC RES, V79, P201, DOI 10.1161/01.RES.79.2.201
   Jin XP, 2003, J BIOL CHEM, V278, P25716, DOI 10.1074/jbc.M300316200
   Jones DT, 1999, J MOL BIOL, V292, P195, DOI 10.1006/jmbi.1999.3091
   KEREM BS, 1989, SCIENCE, V245, P1073, DOI 10.1126/science.2570460
   KOPELMAN H, 1993, J CLIN INVEST, V91, P1253, DOI 10.1172/JCI116289
   KOZAK M, 1987, NUCLEIC ACIDS RES, V15, P8125, DOI 10.1093/nar/15.20.8125
   KOZAK M, 1986, P NATL ACAD SCI USA, V83, P2850, DOI 10.1073/pnas.83.9.2850
   Kozak M, 2000, GENOMICS, V70, P396, DOI 10.1006/geno.2000.6412
   KOZAK M, 1991, J CELL BIOL, V115, P887, DOI 10.1083/jcb.115.4.887
   KOZAK M, 1989, MOL CELL BIOL, V9, P5134, DOI 10.1128/MCB.9.11.5134
   KYTE J, 1982, J MOL BIOL, V157, P105, DOI 10.1016/0022-2836(82)90515-0
   Lee J, 2002, NUCLEIC ACIDS RES, V30, P5110, DOI 10.1093/nar/gkf664
   LEVESQUE PC, 1995, CARDIOVASC RES, V29, P336, DOI 10.1016/S0008-6363(96)88590-7
   LEVESQUE PC, 1992, CIRC RES, V71, P1002, DOI 10.1161/01.RES.71.4.1002
   Liu L, 1999, NAT GENET, V21, P128, DOI 10.1038/5082
   LYDFORD S, 2001, 44 MOL DEV
   MARBAN E, 1999, MOL BASIS CARDIOVASC
   Mathews DH, 1999, J MOL BIOL, V288, P911, DOI 10.1006/jmbi.1999.2700
   MCGOWN E, 1999, 30 MOL DEV
   Mendell JT, 2001, CELL, V107, P411, DOI 10.1016/S0092-8674(01)00583-9
   Mize GJ, 1998, J BIOL CHEM, V273, P32500, DOI 10.1074/jbc.273.49.32500
   Mouchel N, 2003, HUM MOL GENET, V12, P759, DOI 10.1093/hmg/ddg079
   MOUNT SM, 1982, NUCLEIC ACIDS RES, V14, P1319
   MULBERG AE, 1994, NEUROREPORT, V5, P1684, DOI 10.1097/00001756-199408150-00035
   Naren AP, 1999, SCIENCE, V286, P544, DOI 10.1126/science.286.5439.544
   Naren AP, 1998, P NATL ACAD SCI USA, V95, P10972, DOI 10.1073/pnas.95.18.10972
   Naren AP, 2000, NEWS PHYSIOL SCI, V15, P57
   OLENYCH SG, 1999, PEDIATR PULM, V19, P185
   Pesole G, 2001, GENE, V276, P73, DOI 10.1016/S0378-1119(01)00674-6
   RIORDAN JR, 1989, SCIENCE, V245, P1066
   Roden DM, 2002, ANNU REV PHYSIOL, V64, P431, DOI 10.1146/annurev.physiol.64.083101.145105
   ROMMENS JM, 1989, SCIENCE, V245, P1059, DOI 10.1126/science.2772657
   SOROTA S, 1991, J MOL CELL CARDIOL, V23, P1191, DOI 10.1016/0022-2828(91)90207-3
   SORSCHER EJ, 1991, P NATL ACAD SCI USA, V88, P7759, DOI 10.1073/pnas.88.17.7759
   SULLIVAN MM, 1986, CHEST, V90, P239, DOI 10.1378/chest.90.2.239
   TAKANO M, 1992, PFLUG ARCH EUR J PHY, V420, P223, DOI 10.1007/BF00374995
   TOMASELLI GF, 1994, CIRCULATION, V90, P2534, DOI 10.1161/01.CIR.90.5.2534
   TREZISE AEO, 1991, NATURE, V353, P434, DOI 10.1038/353434a0
   TREZISE AEO, 1993, HUM MOL GENET, V2, P801, DOI 10.1093/hmg/2.6.801
   TREZISE AEO, 1993, HUM MOL GENET, V2, P213, DOI 10.1093/hmg/2.3.213
   TREZISE AEO, 1992, EMBO J, V11, P4291, DOI 10.1002/j.1460-2075.1992.tb05528.x
   Vega Laso Maria R., 1993, Journal of Biological Chemistry, V268, P6453
   Vilela C, 1999, EMBO J, V18, P3139, DOI 10.1093/emboj/18.11.3139
   Vuillaumier S, 1997, MOL BIOL EVOL, V14, P372, DOI 10.1093/oxfordjournals.molbev.a025773
   WAGNER JA, 1992, P NATL ACAD SCI USA, V89, P6785, DOI 10.1073/pnas.89.15.6785
   Wallis W., 2001, Archives of Physiology and Biochemistry, V109, P117, DOI 10.1076/apab.109.2.117.4266
   Wang XQ, 2001, J BIOL CHEM, V276, P1311, DOI 10.1074/jbc.M005191200
   Warth JD, 1996, CARDIOVASC RES, V31, P615
   WELSH MJ, 1995, METABOLIC BASIS INHE
   Weyler RT, 1999, AM J PHYSIOL-CELL PH, V277, pC563, DOI 10.1152/ajpcell.1999.277.3.C563
   White NL, 1998, HUM MOL GENET, V7, P363, DOI 10.1093/hmg/7.3.363
   Wiestner A, 1998, NAT GENET, V18, P49, DOI 10.1038/ng0198-49
   Wong KR, 2000, BIOCHEM BIOPH RES CO, V278, P144, DOI 10.1006/bbrc.2000.3754
   Wong KR, 2000, MECH DEVELOP, V94, P195, DOI 10.1016/S0925-4773(00)00312-9
   Wong KR, 1999, AM J PHYSIOL-HEART C, V277, pH1403, DOI 10.1152/ajpheart.1999.277.4.H1403
   ZHANG K, 1994, CIRC RES, V75, P133, DOI 10.1161/01.RES.75.1.133
NR 78
TC 18
Z9 20
U1 0
U2 3
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
SN 0021-9258
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD APR 16
PY 2004
VL 279
IS 16
BP 15877
EP 15887
DI 10.1074/jbc.M313628200
PG 11
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 811BR
UT WOS:000220747900024
PM 14754881
OA hybrid
DA 2025-04-10
ER

PT J
AU Girard, TJ
   Grunz, K
   Lasky, NM
   Malone, JP
   Broze, GJ
AF Girard, T. J.
   Grunz, K.
   Lasky, N. M.
   Malone, J. P.
   Broze, G. J., Jr.
TI Re-evaluation of mouse tissue factor pathway inhibitor and comparison of
   mouse and human tissue factor pathway inhibitor physiology
SO JOURNAL OF THROMBOSIS AND HAEMOSTASIS
LA English
DT Article
DE alternative splicing; hemostasis; mice; protein isoforms; thrombosis
ID FACTOR-FACTOR-VIIA; FACTOR-INDUCED COAGULATION; FACTOR XA; PROTEIN-S;
   ENDOTHELIAL-CELLS; GENE-EXPRESSION; HUMAN PLASMA; TFPI-ALPHA; MICE;
   THROMBOSIS
AB Background: Mouse models can provide insight into the pathophysiology of human thrombosis and hemostasis. Tissue factor pathway inhibitor (TFPI) regulates coagulation through protein S (PS)-enhanced factor (F) Xa inhibition and FXa-dependent inhibition of FVIIa/tissue factor (TF) activity. TFPI is expressed as isoforms alpha and beta in man, and alpha, beta and gamma in the mouse. Objective: Assess the reliability of extending TFPI-related studies in mice to humans. Method: Compare mouse and human TFPI physiology using a variety of methods. Results: Mouse TFPI and human TFPI are similar in regard to: (i) the mechanisms for FVIIa/TF and FXa inhibition; (ii) TFPI alpha is a soluble form and TFP beta is glycosyl phosphatidyl inositol (GPI) membrane anchored; (iii) the predominant circulating form of TFPI in plasma is lipoprotein-associated; (iv) low levels of TFPI alpha circulate in plasma and increase following heparin treatment; and (v) TFPI alpha is the isoform in platelets. They differ in that: (i) mouse TFPI circulates at a similar to 20-fold higher concentration; (ii) mouse lines with isolated isoform deletions show this circulating mouse TFPI is derived from TFPI gamma; (iii) sequences homologous to the mouse TFPI gamma exon are present in many species, including man, but in primates are unfavorable for splicing; and (iv) tandem mass spectrometry (MS/MS) detects sequences for TFPI isoforms alpha and beta in human plasma and alpha and gamma in mouse plasma. Conclusion: To dissect the pathophysiological roles of human TFPI alpha and TFPI beta, studies in TFPI gamma null mice, expressing only alpha and beta, only alpha or only beta should better reflect the human situation.
C1 [Girard, T. J.; Grunz, K.; Lasky, N. M.; Broze, G. J., Jr.] Washington Univ, Sch Med, Dept Med, Div Hematol, Campus Box 8125,660 S Euclid Ave, St Louis, MO 63110 USA.
   [Malone, J. P.] Washington Univ, Sch Med, Inst Clin & Translat Sci, Prote Core Lab, St Louis, MO USA.
C3 Washington University (WUSTL); Washington University (WUSTL)
RP Broze, GJ (corresponding author), Washington Univ, Sch Med, Dept Med, Div Hematol, Campus Box 8125,660 S Euclid Ave, St Louis, MO 63110 USA.
EM gbroze@wustl.edu
FU National Institutes of Health [HL077193, HL112303];  [UL1 TR000448]; 
   [P41GM103422-35]
FX We recognize the Washington University School of Medicine Genomic
   Engineering and iPC (GEiC) Center for the design and production of the
   CRISPR reagents and J. M. White and the Pathology Microinjection Core
   for production of the TFPI exon-deleted mouse strains. The laboratory of
   Reed Townsend, Washington University, St. Louis, MO, USA, conducted the
   tandem MS/MS analyses with support from grants UL1 TR000448 and
   P41GM103422-35. Our work was supported by National Institutes of Health
   grants HL077193 and HL112303.
CR Augustsson C, 2018, J THROMB HAEMOST, V16, P893, DOI 10.1111/jth.14000
   BAJAJ MS, 1990, P NATL ACAD SCI USA, V87, P8869, DOI 10.1073/pnas.87.22.8869
   BROZE GJ, 1994, BLOOD COAGUL FIBRIN, V5, P551
   BROZE GJ, 1988, BLOOD, V71, P335
   BROZE GJ, 1987, BLOOD, V69, P150
   Camerer E, 2000, P NATL ACAD SCI USA, V97, P5255, DOI 10.1073/pnas.97.10.5255
   Chang JY, 1998, THROMB HAEMOSTASIS, V79, P306
   Chang JY, 1999, THROMB HAEMOSTASIS, V81, P45
   Chu AJ, 2006, FRONT BIOSCI-LANDMRK, V11, P256, DOI 10.2741/1796
   Dahm AEA, 2005, J THROMB HAEMOST, V3, P651, DOI 10.1111/j.1538-7836.2005.01237.x
   Dockal M, 2014, J BIOL CHEM, V289, P1732, DOI 10.1074/jbc.M113.533836
   Eitzman DT, 2002, CIRCULATION, V105, P2139, DOI 10.1161/01.CIR.0000017361.39256.82
   Girard TJ, 2013, J THROMB HAEMOST, V11, P375, DOI 10.1111/jth.12084
   Girard TJ, 2012, BLOOD, V119, P1256, DOI 10.1182/blood-2011-10-388512
   GIRARD TJ, 1993, METHOD ENZYMOL, V222, P195
   GIRARD TJ, 1989, NATURE, V338, P518, DOI 10.1038/338518a0
   Hackeng TM, 2006, P NATL ACAD SCI USA, V103, P3106, DOI 10.1073/pnas.0504240103
   HAMAMOTO T, 1993, J BIOL CHEM, V268, P8704
   Hansen JB, 1997, THROMB RES, V85, P413, DOI 10.1016/S0049-3848(97)00029-7
   Hemker HC, 2013, THROMB RES, V131, P3, DOI 10.1016/j.thromres.2012.10.011
   HIGUCHI DA, 1992, BLOOD, V79, P1712
   Huang ZF, 1997, BLOOD, V90, P944, DOI 10.1182/blood.V90.3.944.944_944_951
   HUBBARD AR, 1986, THROMB RES, V42, P489, DOI 10.1016/0049-3848(86)90212-4
   Lindhout T, 1996, HAEMOSTASIS, V26, P89
   Livak KJ, 2001, METHODS, V25, P402, DOI 10.1006/meth.2001.1262
   Maroney SA, 2008, J THROMB HAEMOST, V6, P1344, DOI 10.1111/j.1538-7836.2008.03033.x
   Maroney SA, 2009, J THROMB HAEMOST, V7, P1106, DOI 10.1111/j.1538-7836.2009.03454.x
   Maroney SA, 2006, J THROMB HAEMOST, V4, P1114, DOI 10.1111/j.1538-7836.2006.01873.x
   Maroney SA, 2012, P NATL ACAD SCI USA, V109, P3927, DOI 10.1073/pnas.1119858109
   Maroney SA, 2011, ARTERIOSCL THROM VAS, V31, P821, DOI 10.1161/ATVBAHA.110.220293
   Mast AE, 2002, ARTERIOSCL THROM VAS, V22, P2099, DOI 10.1161/01.ATV.0000042456.84190.F0
   Mast AE, 2016, ARTERIOSCL THROM VAS, V36, P9, DOI 10.1161/ATVBAHA.115.305996
   Muth H, 2005, THROMB HAEMOSTASIS, V94, P1028, DOI 10.1160/TH05-01-0002
   Ndonwi M, 2010, BLOOD, V116, P1344, DOI 10.1182/blood-2009-10-246686
   NOVOTNY WF, 1991, BLOOD, V78, P394
   NOVOTNY WF, 1988, BLOOD, V72, P2020
   Ott I, 2000, ARTERIOSCL THROM VAS, V20, P874, DOI 10.1161/01.ATV.20.3.874
   Parikh BA, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0116484
   Pawlinski R, 2004, BLOOD, V103, P1342, DOI 10.1182/blood-2003-09-3051
   Peraramelli S, 2012, THROMB HAEMOSTASIS, V108, P266, DOI 10.1160/TH11-12-0902
   PETERSEN LC, 1992, THROMB HAEMOSTASIS, V67, P537
   Piro O, 2005, J THROMB HAEMOST, V3, P2677, DOI 10.1111/j.1538-7836.2005.01636.x
   Prince R, 2018, BLOOD, V131, P1360, DOI 10.1182/blood-2017-09-800326
   Rao LVM, 2005, ARTERIOSCL THROM VAS, V25, P47, DOI 10.1161/01.ATV.0000151624.45775.13
   RAO LVM, 1987, BLOOD, V69, P645
   Riewald M, 2001, P NATL ACAD SCI USA, V98, P7742, DOI 10.1073/pnas.141126698
   Rosales C, 2009, BIOCHEMISTRY-US, V48, P8070, DOI 10.1021/bi901087z
   Saller F, 2009, BLOOD, V114, P2307, DOI 10.1182/blood-2009-03-209031
   SANDERS NL, 1985, BLOOD, V66, P204
   SANDSET PM, 1988, THROMB RES, V50, P803, DOI 10.1016/0049-3848(88)90340-4
   Sethi AS, 2005, CLIN SCI, V108, P255, DOI 10.1042/CS20040237
   Singh R, 2003, THROMB HAEMOSTASIS, V89, P747, DOI 10.1055/s-0037-1613582
   Uusitalo-Jarvinen H, 2007, ARTERIOSCL THROM VAS, V27, P1456, DOI 10.1161/ATVBAHA.107.142539
   Valentin S, 1995, THROMB HAEMOSTASIS, V74, P1478
   Versteeg HH, 2006, SEMIN THROMB HEMOST, V32, P24, DOI 10.1055/s-2006-933337
   Wang JP, 2016, MOL CARCINOGEN, V55, P882, DOI 10.1002/mc.22329
   WEINSTEIN DB, 1979, CIRCULATION, V60, P54
   WESSELSCHMIDT R, 1993, BLOOD COAGUL FIBRIN, V4, P661, DOI 10.1097/00001721-199304050-00001
   Westrick RJ, 2001, CIRCULATION, V103, P3044, DOI 10.1161/hc2501.092492
   White TA, 2010, BLOOD, V116, P1787, DOI 10.1182/blood-2009-10-250910
   Winckers K, 2017, PLOS ONE, V12, DOI 10.1371/journal.pone.0168273
   Wood JP, 2014, BLOOD, V123, P2934, DOI 10.1182/blood-2013-11-512764
   Wood JP, 2014, ARTERIOSCL THROM VAS, V34, P169, DOI 10.1161/ATVBAHA.113.302655
   WUN TC, 1988, J BIOL CHEM, V263, P6001
   Zhang J, 2003, CIRCULATION, V108, P623, DOI 10.1161/01.CIR.0000078642.45127.7B
   Zhang MQ, 1998, HUM MOL GENET, V7, P919, DOI 10.1093/hmg/7.5.919
NR 66
TC 15
Z9 16
U1 0
U2 0
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 1538-7933
EI 1538-7836
J9 J THROMB HAEMOST
JI J. Thromb. Haemost.
PD NOV
PY 2018
VL 16
IS 11
BP 2246
EP 2257
DI 10.1111/jth.14288
PG 12
WC Hematology; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Hematology; Cardiovascular System & Cardiology
GA HB2EU
UT WOS:000450850600016
PM 30194803
OA Green Accepted, Bronze
DA 2025-04-10
ER

PT J
AU Hsu, SY
   Chen, CH
   Mukda, S
   Leu, S
AF Hsu, Shu-Yuan
   Chen, Chih-Hung
   Mukda, Sujira
   Leu, Steve
TI Neuronal Pnn Deficiency Increases Oxidative Stress and Exacerbates
   Cerebral Ischemia/Reperfusion Injury in Mice
SO ANTIOXIDANTS
LA English
DT Article
DE Pnn; neuron; ischemia; reperfusion; mRNA alternative splicing; oxidative
   stress
ID BINDING-PROTEINS; ISCHEMIC-STROKE; APOPTOSIS; EXPRESSION; PININ;
   INVOLVEMENT; GENE
AB Cerebral stroke remains one of the leading causes of death worldwide. Ischemic stroke caused by the sudden loss of blood flow in brain is the major type of cerebral stroke. In addition to necrotic cell death in the ischemic core region, neuronal apoptosis is usually observed in the ischemic penumbra. Pnn, a multi-functional protein, participates in cellular proliferation, migration, differentiation, apoptosis as well as cell-cell interaction through its abilities in regulating gene transcription and mRNA processing. Our recent studies have demonstrated that Pnn has a cell type-specific distribution manner in neural cells under ischemic injury and plays a protective role in astrocytes against ischemic stress. In this study, we generated an inducible neuron-specific Pnn deficiency mouse model to further investigate the physiological role of Pnn in neurons. To directly examine the role of neuronal Pnn in ischemic stress, four weeks after induction of Pnn deficiency in neurons, middle cerebral artery occlusion (MCAO) was applied to induce cerebral ischemia/reperfusion in mice. In the cerebrum and hippocampus with neuronal Pnn depletion, the expression of SRSF2, a mRNA splicing regulator, was increased, while the expression of SRSF1, a functional antagonist of SRSF2, was reduced. Expression levels of ROS generators (NOX-1 and NOX-2) and antioxidant proteins (GR, HO-1, NQO-1) were upregulated in brain tissue with loss of neuronal Pnn, echoing an increase in oxidized proteins in cortical and hippocampal neurons. Furthermore, the expression of DNA damage marker, p53bp1, was found in the choroid plexus of mice with neuronal Pnn depletion. In mice with MCAO, compared to wild type mice, both increased cerebral infarcted area and elevated expressions of proapoptotic proteins were found in mice with neuronal Pnn depletion. In conclusion, Pnn deficiency increases oxidative stress in neurons and exacerbates cerebral ischemia/reperfusion injury in mice.
C1 [Hsu, Shu-Yuan] Chang Gung Univ, Coll Med, Grad Inst Biomed Sci, Dept Anat, Taoyuan 33302, Taiwan.
   [Hsu, Shu-Yuan; Leu, Steve] Kaohsiung Chang Gung Mem Hosp, Inst Translat Res Biomed, Kaohsiung 833401, Taiwan.
   [Chen, Chih-Hung] Kaohsiung Chang Gung Mem Hosp, Dept Internal Med, Div Gen Med, Kaohsiung 833401, Taiwan.
   [Chen, Chih-Hung] Chang Gung Univ, Coll Med, Kaohsiung 833401, Taiwan.
   [Mukda, Sujira] Mahidol Univ, Res Ctr Neurosci, Inst Mol Biosci, Salaya 73170, Nakhon Pathom, Thailand.
   [Leu, Steve] Kaohsiung Med Univ, Coll Life Sci, Dept Biotechnol, Kaohsiung 807378, Taiwan.
C3 Chang Gung University; Chang Gung Memorial Hospital; Chang Gung Memorial
   Hospital; Mahidol University; Kaohsiung Medical University
RP Leu, S (corresponding author), Kaohsiung Chang Gung Mem Hosp, Inst Translat Res Biomed, Kaohsiung 833401, Taiwan.; Leu, S (corresponding author), Kaohsiung Med Univ, Coll Life Sci, Dept Biotechnol, Kaohsiung 807378, Taiwan.
EM hsusy@mail.cgu.edu.tw; totoro@adm.cgmh.org.tw; sujira.muk@mahidol.ac.th;
   leu@mail.cgu.edu.tw
RI Leu, Steve/D-6807-2011
OI Leu, Steve/0000-0002-1738-1028; Mukda, Sujira/0000-0002-9646-2394
FU Chang Gung Medical Research Program Grant [CMRPG 8J1181-2, CMRPD1F0181,
   CMRPD1G0071]; Ministry of Science and Technology, Taiwan [MOST
   110-2320-B-182A-005]
FX This research was funded by a Chang Gung Medical Research Program Grant
   (Grant number: CMRPG 8J1181-2; CMRPD1F0181, CMRPD1G0071) and from the
   Ministry of Science and Technology, Taiwan (MOST 110-2320-B-182A-005).
CR Abdelmohsen K, 2008, BIOL CHEM, V389, P243, DOI 10.1515/BC.2008.022
   Amadio M, 2008, CURR PHARM DESIGN, V14, P2651, DOI 10.2174/138161208786264052
   Anczuków O, 2012, NAT STRUCT MOL BIOL, V19, P220, DOI 10.1038/nsmb.2207
   Baldwin K, 2010, PHARMACOTHERAPY, V30, P493, DOI 10.1592/phco.30.5.493
   Broughton BRS, 2009, STROKE, V40, pE331, DOI 10.1161/STROKEAHA.108.531632
   Chelluboina B, 2014, MOL NEUROBIOL, V49, P50, DOI 10.1007/s12035-013-8486-7
   Chen LL, 2017, CELL REP, V21, P3406, DOI 10.1016/j.celrep.2017.11.091
   Cheng YM, 2016, MOL CELL BIOL, V36, P1628, DOI 10.1128/MCB.01071-15
   Gallego ME, 1997, EMBO J, V16, P1772, DOI 10.1093/emboj/16.7.1772
   Harley J, 2021, ANTIOXIDANTS-BASEL, V10, DOI 10.3390/antiox10040552
   Harley J, 2020, INT J MOL SCI, V21, DOI 10.3390/ijms21218346
   Hsu SY, 2020, BRAIN SCI, V10, DOI 10.3390/brainsci10100708
   Hsu SY, 2012, HISTOCHEM CELL BIOL, V138, P127, DOI 10.1007/s00418-012-0950-3
   Hsu SY, 2011, HISTOCHEM CELL BIOL, V135, P361, DOI 10.1007/s00418-011-0795-1
   Infante SK, 2013, J NEUROSCI RES, V91, P1152, DOI 10.1002/jnr.23224
   Joo JH, 2014, MOL VIS, V20, P1629
   Joo JH, 2007, DEV DYNAM, V236, P2147, DOI 10.1002/dvdy.21243
   Joo JH, 2010, DEV BIOL, V345, P191, DOI 10.1016/j.ydbio.2010.07.009
   Joo JH, 2010, INVEST OPHTH VIS SCI, V51, P1927, DOI 10.1167/iovs.09-4591
   Kedzierska H, 2016, INT J MOL SCI, V17, DOI 10.3390/ijms17101598
   Lattanzi S, 2021, BRAIN SCI, V11, DOI 10.3390/brainsci11091164
   Leu S, 2021, BIOCHEM PHARMACOL, V192, DOI 10.1016/j.bcp.2021.114672
   Leu S, 2012, J CELL SCI, V125, P3164, DOI 10.1242/jcs.100859
   Loh Kok Poh, 2006, Current Alzheimer Research, V3, P327
   Merdzhanova G, 2008, CELL DEATH DIFFER, V15, P1815, DOI 10.1038/cdd.2008.135
   Moon H, 2017, BMB REP, V50, P423, DOI 10.5483/BMBRep.2017.50.8.103
   Skliris A, 2015, CELL DEATH DIFFER, V22, P703, DOI 10.1038/cdd.2014.158
   Slegtenhorst Bendix R, 2014, Curr Transplant Rep, V1, P147
   Wang P, 2002, BIOCHEM BIOPH RES CO, V294, P448, DOI 10.1016/S0006-291X(02)00495-3
   Wee CD, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0115205
   Zhang YL, 2016, ONCOTARGET, V7, P11397, DOI 10.18632/oncotarget.7242
NR 31
TC 7
Z9 9
U1 0
U2 6
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
EI 2076-3921
J9 ANTIOXIDANTS-BASEL
JI Antioxidants
PD MAR
PY 2022
VL 11
IS 3
AR 466
DI 10.3390/antiox11030466
PG 12
WC Biochemistry & Molecular Biology; Chemistry, Medicinal; Food Science &
   Technology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Pharmacology & Pharmacy; Food Science
   & Technology
GA 0D4WY
UT WOS:000775998700001
PM 35326115
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Unlap, MT
   Peti-Peterdi, J
   Bell, PD
AF Unlap, MT
   Peti-Peterdi, J
   Bell, PD
TI Cloning of mesangial cell Na<SUP>+</SUP>/Ca<SUP>2+</SUP> exchangers from
   Dahl/Rapp salt-sensitive/resistant rats
SO AMERICAN JOURNAL OF PHYSIOLOGY-RENAL PHYSIOLOGY
LA English
DT Article
DE sodium-calcium exchanger; cytosolic calcium concentration; genetic
   hypertension
ID SMOOTH-MUSCLE CELLS; PROTEIN-KINASE-C; ALTERNATIVELY SPLICED ISOFORMS;
   TISSUE-SPECIFIC EXPRESSION; FUNCTIONAL EXPRESSION; NA+-CA-2+ EXCHANGER;
   NA/CA EXCHANGER; CYTOSOLIC CA2+; HELA-CELLS; ACTIVATION
AB The Dahl/Rapp rat model of hypertension is characterized by a marked increase in blood pressure and a progressive fall in glomerular filtration rate when salt-sensitive (S) rats are placed on an 8% NaCl diet. On the same diet, the salt-resistant (R) rat does not exhibit these changes. In previous studies we found that protein kinase C (PKC) upregulates Na+/Ca2+ exchanger activity in afferent arterioles and mesangial cells from R but not S rats. One possible reason for the difference in PKC sensitivity may be due to differences in the S and R Na+/Ca2+ exchanger protein. We now report the cloning of Na+/Ca2+ exchangers from R (RNCX1) and S (SNCX1) mesangial cells. At the amino acid level, SNCX1 differs from RNCX1 at position 218 in the NH2-terminal domain where it is isoleucine in RNCX1 but phenylalanine in SNCX1. These two exchangers also differ by 23 amino acids at the alternative splice site within the cytosolic domain. RNCX1 and SNCX1 were expressed in OK-PTH cells and Ca-45(2+)-uptake studies were performed. Acute phorbol 12-myristate13-acetate (PMA) treatment (300 nM, 20 min) upregulated exchanger activity in cells expressing RNCX1 but failed to stimulate exchanger activity in SNCX1 expressing cells. Upregulation of RNCX1 could be prevented by prior 24-h pretreatment with PMA, which downregulates PKC. These results demonstrate a difference in PKC-Na+/Ca2+ exchange activity between the isoform of the exchanger cloned from the R vs. the S rat. Lack of PKC activation of SNCX1 may contribute to a dysregulation of intracellular Ca2+ concentration and enhanced renal vasoreactivity in this model of hypertension.
C1 Univ Alabama, UAB Stn, Nephrol Res & Training Ctr, Dept Med,Div Nephrol, Birmingham, AL 35294 USA.
   Univ Alabama, UAB Stn, Nephrol Res & Training Ctr, Dept Physiol,Div Nephrol, Birmingham, AL 35294 USA.
C3 University of Alabama System; University of Alabama Birmingham;
   University of Alabama System; University of Alabama Birmingham
RP Bell, PD (corresponding author), Univ Alabama, UAB Stn, Nephrol Res & Training Ctr, Dept Med,Div Nephrol, 865 Sparks Ctr, Birmingham, AL 35294 USA.
EM DBELL@NRTC.DOM.UAB.EDU
FU NHLBI NIH HHS [HL-50163] Funding Source: Medline; NIDDK NIH HHS
   [3RO1-DK-32032] Funding Source: Medline
CR BATLLE DC, 1991, AM J PHYSIOL, V261, pC845, DOI 10.1152/ajpcell.1991.261.5.C845
   CHEN PY, 1993, LAB INVEST, V68, P174
   Fowler BC, 1996, KIDNEY INT, V50, P1856, DOI 10.1038/ki.1996.506
   FRIEDMAN PA, 1981, AM J PHYSIOL, V240, pF558, DOI 10.1152/ajprenal.1981.240.6.F558
   FURMAN I, 1993, FEBS LETT, V319, P105, DOI 10.1016/0014-5793(93)80046-W
   He SW, 1998, J NEUROSCI, V18, P4833
   Ikari A, 1998, EUR J PHARMACOL, V360, P91, DOI 10.1016/S0014-2999(98)00659-1
   IKEDA M, 1995, NEUROLOGY, V45, P2038, DOI 10.1212/WNL.45.11.2038
   IWAMOTO T, 1995, J BIOL CHEM, V270, P8996, DOI 10.1074/jbc.270.15.8996
   Iwamoto T, 1996, J BIOL CHEM, V271, P13609, DOI 10.1074/jbc.271.23.13609
   KAMENDULIS LM, 1992, TOXICOL LETT, V63, P277, DOI 10.1016/0378-4274(92)90090-7
   KOFUJI P, 1993, AM J PHYSIOL, V265, pF598, DOI 10.1152/ajprenal.1993.265.4.F598
   KOFUJI P, 1994, J BIOL CHEM, V269, P5145
   KOFUJI P, 1992, AM J PHYSIOL, V263, pC1241, DOI 10.1152/ajpcell.1992.263.6.C1241
   LEE SL, 1994, J BIOL CHEM, V269, P14849
   Linck B, 1998, AM J PHYSIOL-CELL PH, V274, pC415, DOI 10.1152/ajpcell.1998.274.2.C415
   LOVETT DH, 1983, J IMMUNOL, V130, P1796
   LOW W, 1993, FEBS LETT, V316, P63, DOI 10.1016/0014-5793(93)81737-K
   Mashburn NA, 1999, AM J PHYSIOL-RENAL, V276, pF574, DOI 10.1152/ajprenal.1999.276.4.F574
   MENE P, 1991, AM J PHYSIOL, V261, pF466, DOI 10.1152/ajprenal.1991.261.3.F466
   MISRA RP, 1972, AM J CLIN PATHOL, V58, P135
   NAKASAKI Y, 1993, J BIOCHEM-TOKYO, V114, P528, DOI 10.1093/oxfordjournals.jbchem.a124211
   Nelson LD, 1999, AM J PHYSIOL-RENAL, V276, pF567, DOI 10.1152/ajprenal.1999.276.4.F567
   NICOLL DA, 1991, ANN NY ACAD SCI, V639, P181, DOI 10.1111/j.1749-6632.1991.tb17305.x
   NICOLL DA, 1990, SCIENCE, V250, P562, DOI 10.1126/science.1700476
   Omelchenko A, 1998, J GEN PHYSIOL, V111, P691, DOI 10.1085/jgp.111.5.691
   Quednau BD, 1997, AM J PHYSIOL-CELL PH, V272, pC1250, DOI 10.1152/ajpcell.1997.272.4.C1250
   RAPP JP, 1985, HYPERTENSION, V7, P340, DOI 10.1161/01.HYP.7.3_Pt_1.340
   REILLY RF, 1992, AM J PHYSIOL, V262, pF1105, DOI 10.1152/ajprenal.1992.262.6.F1105
   TOMATSU S, 1995, AM J HUM GENET, V57, P556
   VIGNE P, 1988, J BIOL CHEM, V263, P8078
   VONHEIJNE G, 1986, NUCLEIC ACIDS RES, V14, P4683, DOI 10.1093/nar/14.11.4683
   White KE, 1996, ANN NY ACAD SCI, V779, P115, DOI 10.1111/j.1749-6632.1996.tb44776.x
   ZHU L, 1995, AM J PATHOL, V147, P375
   ZHU ZM, 1994, AM J PHYSIOL, V266, pC794, DOI 10.1152/ajpcell.1994.266.3.C794
NR 35
TC 13
Z9 15
U1 0
U2 1
PU AMER PHYSIOLOGICAL SOC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA
SN 1931-857X
J9 AM J PHYSIOL-RENAL
JI Am. J. Physiol.-Renal Physiol.
PD JUL
PY 2000
VL 279
IS 1
BP F177
EP F184
DI 10.1152/ajprenal.2000.279.1.F177
PG 8
WC Physiology; Urology & Nephrology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Physiology; Urology & Nephrology
GA 333RM
UT WOS:000088144600018
PM 10894800
DA 2025-04-10
ER

PT J
AU Onkal, R
   Djamgoz, MBA
AF Onkal, Rustem
   Djamgoz, Mustafa B. A.
TI Molecular pharmacology of voltage-gated sodium channel expression in
   metastatic disease: Clinical potential of neonatal Nav1.5 in breast
   cancer
SO EUROPEAN JOURNAL OF PHARMACOLOGY
LA English
DT Review
DE Breast cancer; Metastasis; Oncofoetal; Voltage-gated sodium channel;
   Nav1.5; SCN5A; Cardiac; Development; Alternative splicing; Neonatal;
   Pharmacology; Antibody; siRNA; Neurotoxin
ID HUMAN PROSTATE-CANCER; TARGETING ION CHANNELS; RESISTANT NA+ CHANNELS;
   CURRENT ELECTRIC-FIELD; ALPHA-SUBUNIT GENES; LYLU CELL-LINE; FUNCTIONAL
   EXPRESSION; RNA INTERFERENCE; DEVELOPMENTAL-CHANGES;
   MONOCLONAL-ANTIBODIES
AB A variety of ion channels have been detected in cancer cells. In particular, upregulation of voltage-gated sodium channels (VGSCs) has been associated pathophysiologically with several strongly metastatic carcinomas. This review emphasises breast cancer. Inhibiting VGSC activity in a number of independent ways, using the highly selective tetrodotoxin (TTX), gene silencing and a blocking polyclonal antibody, suppressed a range of cellular behaviors, especially directional motility and invasion, integral to the metastatic cascade. Conversely, transfecting; a VGSC into a weakly invasive human prostate cancer cell line significantly increased invasiveness. In vivo, also, VGSC expression has been correlated positively with metastatic status. It has been suggested, therefore (i) that VGSC upregulation is an early event in metastatic progression and (ii) that VGSC expression is a 'switch,' necessary and sufficient for engaging cancer cells in a highly invasive state. Importantly, where studied, mainly prostate and breast cancers, the dominant VGSC (Nav1.7 and Nav1.5, respectively) was found to be an embryonic/neonatal splice variant, consistent with the gene expression being "oncofoetal." In breast cancer, the molecular difference between the adult and neonatal isoforms of the VGSC/Nav1.5 is largest (31 base pairs, generating 7 amino acid differences). We propose that neonatal Nav1.5 is a novel marker with significant clinical potential for management of metastatic breast cancer and describe a number of approaches which may enable tumour-specific targeting. These include various small-molecule drugs, small-interfering RNA, monoclonal antibody and natural neurotoxins. (C) 2009 Elsevier B.V. All rights reserved.
C1 [Onkal, Rustem; Djamgoz, Mustafa B. A.] Univ London Imperial Coll Sci Technol & Med, Div Cell & Mol Biol, Neurosci Solut Canc Res Grp, London SW7 2AZ, England.
   [Djamgoz, Mustafa B. A.] Cyprus Int Univ, Biotechnol Res Inst, TR-10 N Cyprus, Mersin, Turkey.
C3 Imperial College London; Cyprus International University
RP Djamgoz, MBA (corresponding author), Univ London Imperial Coll Sci Technol & Med, Div Cell & Mol Biol, Neurosci Solut Canc Res Grp, Sir Alexander Fleming Bldg,S Kensington Campus, London SW7 2AZ, England.
EM m.djamgoz@imperial.ac.uk
RI Djamgoz, Mustafa/KJL-8515-2024
FU Pro Cancer Research Fund (PCRF); MRC [G0501019] Funding Source: UKRI
FX We are grateful to the Pro Cancer Research Fund (PCRF) for the continued
   support. We thank Drs. Scott Fraser and Dongmin Shao for critical
   reading of the manuscript
CR Abdul M, 2002, CANCER LETT, V186, P99, DOI 10.1016/S0304-3835(02)00348-8
   Abdul M, 2002, ANTICANCER RES, V22, P1727
   Abdul M, 2001, ANTICANCER RES, V21, P2045
   Adachi K, 2004, ONCOGENE, V23, P7791, DOI 10.1038/sj.onc.1208067
   Ademuyiwa FO, 2008, CLIN BREAST CANCER, V8, pS151, DOI 10.3816/CBC.2008.s.011
   Allen DH, 1997, J MEMBRANE BIOL, V155, P27, DOI 10.1007/s002329900155
   [Anonymous], MOL CANC
   [Anonymous], 2003, CURRENT PROTOCOLS NE
   Ansiaux R, 2007, EXPERT OPIN INV DRUG, V16, P209, DOI 10.1517/13543784.16.2.209
   Arcangeli A, 2009, CURR MED CHEM, V16, P66, DOI 10.2174/092986709787002835
   Ariel I, 1997, J CLIN PATHOL-MOL PA, V50, P34, DOI 10.1136/mp.50.1.34
   Ashcroft FM, 2006, NATURE, V440, P440, DOI 10.1038/nature04707
   Bacac M, 2008, ANNU REV PATHOL-MECH, V3, P221, DOI 10.1146/annurev.pathmechdis.3.121806.151523
   Bedard PL, 2008, CLIN BREAST CANCER, V8, pS157, DOI 10.3816/CBC.2008.s.012
   Behlke MA, 2008, OLIGONUCLEOTIDES, V18, P305, DOI 10.1089/oli.2008.0164
   Belardinelli L, 2006, HEART, V92, P6, DOI 10.1136/hrt.2005.078790
   BELCHER SM, 1995, P NATL ACAD SCI USA, V92, P11034, DOI 10.1073/pnas.92.24.11034
   Ben-Porath I, 2008, NAT GENET, V40, P499, DOI 10.1038/ng.127
   Bennay M, 2008, GLIA, V56, P1138, DOI 10.1002/glia.20685
   Bennett ES, 2004, PFLUG ARCH EUR J PHY, V447, P908, DOI 10.1007/s00424-003-1205-x
   Berger JC, 2004, ANTI-CANCER DRUG, V15, P559, DOI 10.1097/01.cad.0000132233.36512.fa
   BLANDINO JKW, 1995, J MEMBRANE BIOL, V143, P153
   Brackenbury WJ, 2007, BREAST CANCER RES TR, V101, P149, DOI 10.1007/s10549-006-9281-1
   Brackenbury WJ, 2007, J CELL PHYSIOL, V210, P602, DOI 10.1002/jcp.20846
   Brackenbury WJ, 2006, J PHYSIOL-LONDON, V573, P343, DOI 10.1113/jphysiol.2006.106906
   Brackenbury WJ, 2008, NEUROSCIENTIST, V14, P571, DOI 10.1177/1073858408320293
   Carter P, 2001, NAT REV CANCER, V1, P118, DOI 10.1038/35101072
   Castillo C, 2003, DEV BRAIN RES, V144, P99, DOI 10.1016/S0165-3806(03)00164-0
   Catterall WA, 2000, NEURON, V26, P13, DOI 10.1016/S0896-6273(00)81133-2
   Catterall WA, 2003, PHARMACOL REV, V55, P579, DOI 10.1124/pr.55.4.8
   Catterall WA, 2007, TOXICON, V49, P124, DOI 10.1016/j.toxicon.2006.09.022
   Cestèle S, 2000, BIOCHIMIE, V82, P883, DOI 10.1016/S0300-9084(00)01174-3
   Chioni AM, 2005, J NEUROSCI METH, V147, P88, DOI 10.1016/j.jneumeth.2005.03.010
   Chioni AM, 2009, INT J BIOCHEM CELL B, V41, P1216, DOI 10.1016/j.biocel.2008.11.001
   Chuang YC, 2006, J UROLOGY, V176, P2375, DOI 10.1016/j.juro.2006.07.127
   Clare JJ, 2000, DRUG DISCOV TODAY, V5, P506, DOI 10.1016/S1359-6446(00)01570-1
   CLARKSON CW, 1988, J MOL CELL CARDIOL, V20, P1119, DOI 10.1016/0022-2828(88)90592-5
   Conti F, 1996, BIOPHYS J, V71, P1295, DOI 10.1016/S0006-3495(96)79330-X
   Conti M, 2007, CURR CLIN PHARMACOL, V2, P135, DOI 10.2174/157488407780598153
   Copley RR, 2004, TRENDS GENET, V20, P171, DOI 10.1016/j.tig.2004.02.001
   Cusdin FS, 2008, TRAFFIC, V9, P17, DOI 10.1111/j.1600-0854.2007.00673.x
   Diaz D, 2007, J CELL PHYSIOL, V210, P469, DOI 10.1002/jcp.20871
   Diaz ME, 1998, JPN HEART J, V39, P199
   Ding Y, 2004, INT J BIOCHEM CELL B, V36, P1249, DOI 10.1016/j.biocel.2003.10.010
   Ding YN, 2008, J CELL PHYSIOL, V215, P77, DOI 10.1002/jcp.21289
   Diss JKJ, 2008, PROSTATE CANCER P D, V11, P325, DOI 10.1038/sj.pcan.4501012
   Diss JKJ, 2005, PROSTATE CANCER P D, V8, P266, DOI 10.1038/sj.pcan.4500796
   Diss JKJ, 2001, PROSTATE, V48, P165, DOI 10.1002/pros.1095
   Diss JKJ, 2004, EUR BIOPHYS J BIOPHY, V33, P180, DOI 10.1007/s00249-004-0389-0
   Djamgoz MBA, 2001, J CELL SCI, V114, P2697
   Djamgoz MBA, 2006, TURK J BIOCHEM, V31, P57
   Drizin I, 2008, BIOORGAN MED CHEM, V16, P6379, DOI 10.1016/j.bmc.2008.05.003
   Dykxhoorn DM, 2005, ANNU REV MED, V56, P401, DOI 10.1146/annurev.med.56.082103.104606
   Edwards BK, 2005, JNCI-J NATL CANCER I, V97, P1407, DOI 10.1093/jnci/dji289
   Elbashir SM, 2001, NATURE, V411, P494, DOI 10.1038/35078107
   England S, 2008, EXPERT OPIN INV DRUG, V17, P1849, DOI 10.1517/13543780802514559 
   Fidler IJ, 2003, NAT REV CANCER, V3, P453, DOI 10.1038/nrc1098
   Fidler IJ, 2002, SEMIN CANCER BIOL, V12, P89, DOI 10.1006/scbi.2001.0416
   Fidler IJ, 2002, DIFFERENTIATION, V70, P498, DOI 10.1046/j.1432-0436.2002.700904.x
   Fiske JL, 2006, CANCER METAST REV, V25, P493, DOI 10.1007/s10555-006-9017-z
   Fraser S.P., 2007, EUR BIOPHYS J BIOPHY, V36, pS228
   Fraser SP, 2008, EMBO REP, V9, P512, DOI 10.1038/embor.2008.75
   Fraser SP, 2003, J CELL PHYSIOL, V195, P479, DOI 10.1002/jcp.10312
   Fraser SP, 1999, CELL TISSUE RES, V295, P505, DOI 10.1007/s004410051256
   Fraser SP, 2005, CLIN CANCER RES, V11, P5381, DOI 10.1158/1078-0432.CCR-05-0327
   Fraser SP, 2004, FEBS LETT, V569, P191, DOI 10.1016/j.febslet.2004.05.063
   Fulgenzi G, 2006, INT J BIOCHEM CELL B, V38, P1146, DOI 10.1016/j.biocel.2005.12.003
   GALPER JB, 1978, DEV BIOL, V65, P216, DOI 10.1016/0012-1606(78)90191-4
   Gao R, 2009, J HUAZHONG U SCI-MED, V29, P64, DOI 10.1007/s11596-009-0113-5
   GELLENS ME, 1992, P NATL ACAD SCI USA, V89, P554, DOI 10.1073/pnas.89.2.554
   Gillet L, 2009, J BIOL CHEM, V284, P8671, DOI 10.1074/jbc.M806891200
   Goldin AL, 2001, ANNU REV PHYSIOL, V63, P871, DOI 10.1146/annurev.physiol.63.1.871
   Gómez-Varela D, 2007, CANCER RES, V67, P7343, DOI 10.1158/0008-5472.CAN-07-0107
   Grimes JA, 1998, J CELL PHYSIOL, V175, P50, DOI 10.1002/(SICI)1097-4652(199804)175:1<50::AID-JCP6>3.0.CO;2-B
   GRIMES JA, 1995, FEBS LETT, V369, P290, DOI 10.1016/0014-5793(95)00772-2
   Gurel B, 2008, ADV ANAT PATHOL, V15, P319, DOI 10.1097/PAP.0b013e31818a5c19
   GUSTAFSON TA, 1993, J BIOL CHEM, V268, P18648
   Hagel C, 2007, PROG EXP TUMOR RES, V39, P64, DOI 10.1159/000100047
   Hanahan D, 2000, CELL, V100, P57, DOI 10.1016/S0092-8674(00)81683-9
   Harnmarström AKM, 2002, EUR BIOPHYS J BIOPHY, V31, P323, DOI 10.1007/s00249-002-0218-2
   Herfst LJ, 2004, J MOL CELL CARDIOL, V36, P185, DOI 10.1016/j.yjmcc.2003.11.014
   Hille B, 1992, IONIC CHANNELS EXCIT
   Hoang BX, 2007, MED HYPOTHESES, V68, P832, DOI 10.1016/j.mehy.2006.09.005
   Hoang BX, 2007, EUR J CANCER PREV, V16, P55, DOI 10.1097/01.cej.0000220636.15976.4c
   HOFFMAN EP, 1995, ANNU REV MED, V46, P431
   Huang C, 2008, EXPERT OPIN THER TAR, V12, P637, DOI [10.1517/14728222.12.5.637, 10.1517/14728222.12.5.637 ]
   Hunter Kent W, 2008, Breast Cancer Res, V10 Suppl 1, pS2, DOI 10.1186/bcr1988
   Hunter KW, 2004, BRIT J CANCER, V90, P752, DOI 10.1038/sj.bjc.6601590
   Isbilen B, 2006, INT J BIOCHEM CELL B, V38, P2173, DOI 10.1016/j.biocel.2006.06.014
   Isom LL, 2002, FRONT BIOSCI, V7, P12
   Isom LL, 2001, NEUROSCIENTIST, V7, P42, DOI 10.1177/107385840100700108
   Jarvis MF, 2007, P NATL ACAD SCI USA, V104, P8520, DOI 10.1073/pnas.0611364104
   Jean-Yves L, 2007, RECENT PAT ANTI-CANC, V2, P189, DOI 10.2174/157489207782497244
   Jemal A, 2008, CA-CANCER J CLIN, V58, P71, DOI 10.3322/CA.2007.0010
   Kaczmarek LK, 2006, NAT REV NEUROSCI, V7, P761, DOI 10.1038/nrn1988
   KIM YI, 1988, SCIENCE, V239, P405, DOI 10.1126/science.2447652
   KLUGBAUER N, 1995, EMBO J, V14, P1084, DOI 10.1002/j.1460-2075.1995.tb07091.x
   Kort ME, 2008, J MED CHEM, V51, P407, DOI 10.1021/jm070637u
   Kostrzewa RM, 2007, NEUROTOX RES, V12, P275, DOI 10.1007/BF03033911
   Krasowska M, 2004, EUR BIOPHYS J BIOPHY, V33, P535, DOI 10.1007/s00249-004-0394-3
   Laniado ME, 1997, AM J PATHOL, V150, P1213
   Leipold E, 2006, MOL PHARMACOL, V70, P340, DOI 10.1124/mol.106.024034
   Leippold T, 2003, EUR UROL, V44, P165, DOI 10.1016/S0302-2838(03)00250-1
   Leung SWS, 2007, CLIN EXP PHARMACOL P, V34, P822, DOI 10.1111/j.1440-1681.2007.04686.x
   Liao YJ, 2008, P NATL ACAD SCI USA, V105, P2705, DOI 10.1073/pnas.0710771105
   Liotta LA, 2000, NATURE, V405, P287, DOI 10.1038/35012728
   Lu Y, 2002, LIFE SCI, V71, P1465, DOI 10.1016/S0024-3205(02)01922-7
   Maertens C, 2006, MOL PHARMACOL, V70, P405, DOI 10.1124/mol.106.022970
   Marbán E, 2002, NATURE, V415, P213, DOI 10.1038/415213a
   Martin SE, 2007, ANNU REV GENOM HUM G, V8, P81, DOI 10.1146/annurev.genom.8.080706.092424
   Masiero M, 2007, MOL ASPECTS MED, V28, P143, DOI 10.1016/j.mam.2006.12.004
   Medvedeva YV, 2009, NEUROSCIENCE, V159, P559, DOI 10.1016/j.neuroscience.2008.12.029
   MEIRI H, 1989, METHOD ENZYMOL, V178, P714
   Meisler MH, 2002, NOVART FDN SYMP, V241, P72
   Mellstedt H, 2003, DRUG TODAY, V39, P1
   Monk M, 2001, ONCOGENE, V20, P8085, DOI 10.1038/sj.onc.1205088
   MORTON ME, 1988, J BIOL CHEM, V263, P613
   Mycielska ME, 2005, J PHYSIOL-LONDON, V563, P393, DOI 10.1113/jphysiol.2004.079491
   Mycielska ME, 2004, J CELL SCI, V117, P1631, DOI 10.1242/jcs.01125
   Mycielska ME, 2003, J CELL PHYSIOL, V195, P461, DOI 10.1002/jcp.10265
   Nakajima T, 2009, BRIT J PHARMACOL, V156, P420, DOI 10.1111/j.1476-5381.2008.00059.x
   Newsome BW, 2008, BRIT J CLIN PHARMACO, V66, P6, DOI 10.1111/j.1365-2125.2008.03187.x
   Nguyen DX, 2007, NAT REV GENET, V8, P341, DOI 10.1038/nrg2101
   Nikolaeva MA, 2005, J NEUROSCI, V25, P9960, DOI 10.1523/JNEUROSCI.2003-05.2005
   O'Rourke Brian, 2007, Drug Discov Today Dis Models, V4, P207, DOI 10.1016/j.ddmod.2007.11.003
   Ohya S, 2009, J PHARMACOL SCI, V109, P148, DOI 10.1254/jphs.08208SC
   Onganer PU, 2005, BRIT J CANCER, V93, P1197, DOI 10.1038/sj.bjc.6602857
   Onganer PU, 2005, J MEMBRANE BIOL, V204, P67, DOI 10.1007/s00232-005-0747-6
   Onkal R, 2008, J CELL PHYSIOL, V216, P716, DOI 10.1002/jcp.21451
   Ou SW, 2005, EUR J NEUROSCI, V22, P793, DOI 10.1111/j.1460-9568.2005.04280.x
   Ouwerkerk R, 2007, BREAST CANCER RES TR, V106, P151, DOI 10.1007/s10549-006-9485-4
   Palmer CP, 2008, EUR BIOPHYS J BIOPHY, V37, P359, DOI 10.1007/s00249-007-0219-2
   Pardo LA, 2008, EXPERT OPIN THER TAR, V12, P837, DOI 10.1517/14728222.12.7.837 
   Plummer NW, 1998, GENOMICS, V54, P287, DOI 10.1006/geno.1998.5550
   Plummer NW, 1999, GENOMICS, V57, P323, DOI 10.1006/geno.1998.5735
   Prevarskaya N, 2007, CELL DEATH DIFFER, V14, P1295, DOI 10.1038/sj.cdd.4402162
   Priest BT, 2007, TOXICON, V49, P194, DOI 10.1016/j.toxicon.2006.09.014
   Prossnitz ER, 2008, ANNU REV PHYSIOL, V70, P165, DOI 10.1146/annurev.physiol.70.113006.100518
   Ragsdale DS, 1996, P NATL ACAD SCI USA, V93, P9270, DOI 10.1073/pnas.93.17.9270
   Ramírez ML, 2008, PROSTATE CANCER P D, V11, P216, DOI 10.1038/pcan.2008.2
   Raymond CK, 2004, J BIOL CHEM, V279, P46234, DOI 10.1074/jbc.M406387200
   Ribeiro MA, 2003, DEV BRAIN RES, V146, P59, DOI 10.1016/j.devbrainres.2003.09.011
   Roberts R, 2003, ANNU REV MED, V54, P257, DOI 10.1146/annurev.med.54.073002.182112
   Roger S, 2003, BBA-BIOMEMBRANES, V1616, P107, DOI 10.1016/j.bbamem.2003.07.001
   Roger S, 2007, INT J BIOCHEM CELL B, V39, P774, DOI 10.1016/j.biocel.2006.12.007
   Roger S, 2006, CURR PHARM DESIGN, V12, P3681, DOI 10.2174/138161206778522047
   Rosker C, 2007, AM J PHYSIOL-CELL PH, V293, pC783, DOI 10.1152/ajpcell.00070.2007
   Ruan YF, 2009, NAT REV CARDIOL, V6, P337, DOI 10.1038/nrcardio.2009.44
   Saint David A, 2006, J Cardiovasc Electrophysiol, V17 Suppl 1, pS96, DOI 10.1111/j.1540-8167.2006.00390.x
   Santen RJ, 2008, ADV EXP MED BIOL, V630, P19
   Santen RJ, 2005, ENDOCR-RELAT CANCER, V12, pS61, DOI 10.1677/erc.1.01018
   SARAO R, 1991, NUCLEIC ACIDS RES, V19, P5673, DOI 10.1093/nar/19.20.5673
   Schwirzke M, 1999, ANTICANCER RES, V19, P1801
   Shao DM, 2009, INT J BIOCHEM CELL B, V41, P1471, DOI 10.1016/j.biocel.2009.01.016
   Sikes Robert A, 2003, Clin Prostate Cancer, V2, P181, DOI 10.3816/CGC.2003.n.028
   Smith P, 1998, FEBS LETT, V423, P19, DOI 10.1016/S0014-5793(98)00050-7
   Son DJ, 2007, MOL CANCER THER, V6, P675, DOI 10.1158/1535-7163.MCT-06-0328
   Soroceanu L, 1998, CANCER RES, V58, P4871
   Vaidya KS, 2007, J MAMMARY GLAND BIOL, V12, P175, DOI 10.1007/s10911-007-9049-1
   Ventura AC, 2008, ANNU REV MED, V59, P199, DOI 10.1146/annurev.med.59.060106.184830
   Wall NR, 2003, LANCET, V362, P1401, DOI 10.1016/S0140-6736(03)14637-5
   Wang J, 2008, J NEUROGENET, V22, P57, DOI 10.1080/01677060701672077
   Wang MC, 2008, BIOCHEM PHARMACOL, V76, P1716, DOI 10.1016/j.bcp.2008.09.008
   Wang WX, 2005, J NEURO-ONCOL, V73, P1, DOI 10.1007/s11060-004-4205-6
   WANG Y, 2009, BIOORGAN MED CHEM, V17, P7964
   Waxman SG, 2001, NEUROLOGY, V56, P1621, DOI 10.1212/WNL.56.12.1621
   Waxman SG, 2007, NAT NEUROSCI, V10, P405, DOI 10.1038/nn1857
   Weigelt B, 2005, CANCER RES, V65, P9155, DOI 10.1158/0008-5472.CAN-05-2553
   Welch DR, 2000, BREAST CANCER RES, V2, P408, DOI 10.1186/bcr87
   Welch DR, 2004, BREAST CANCER RES, V6, P61, DOI 10.1186/bcr736
   Welch DR., 2006, BREAST DIS, V26, P3
   Williams BS, 2007, BIOCHEMISTRY-US, V46, P14693, DOI 10.1021/bi7018207
   Williams EL, 2005, BIOESSAYS, V27, P1228, DOI 10.1002/bies.20324
   Xiao XH, 1999, CIRC RES, V85, P723, DOI 10.1161/01.RES.85.8.723
   Xiao YC, 2008, J BIOL CHEM, V283, P27300, DOI 10.1074/jbc.M708447200
   Xu SZ, 2005, NAT BIOTECHNOL, V23, P1289, DOI 10.1038/nbt1148
   XU YQ, 1992, J PHARMACOL EXP THER, V262, P670
   XU YQ, 1991, CIRC RES, V69, P644, DOI 10.1161/01.RES.69.3.644
   Zangemeister-Wittke U, 2005, PATHOBIOLOGY, V72, P279, DOI 10.1159/000091325
   Zhou BY, 1998, J GEN PHYSIOL, V111, P555, DOI 10.1085/jgp.111.4.555
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TC 107
Z9 128
U1 0
U2 37
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
SN 0014-2999
EI 1879-0712
J9 EUR J PHARMACOL
JI Eur. J. Pharmacol.
PD DEC 25
PY 2009
VL 625
IS 1-3
SI SI
BP 206
EP 219
DI 10.1016/j.ejphar.2009.08.040
PG 14
WC Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Pharmacology & Pharmacy
GA 532LA
UT WOS:000272748300024
PM 19835862
DA 2025-04-10
ER

PT J
AU Dahlbäck, B
AF Dahlback, B.
TI Novel insights into the regulation of coagulation by factor V isoforms,
   tissue factor pathway inhibitorα, and protein S
SO JOURNAL OF THROMBOSIS AND HAEMOSTASIS
LA English
DT Article
DE blood coagulation; factor V; factor Xa; protein C; protein S; TFPI alpha
ID C-MEDIATED CLEAVAGES; TEXAS BLEEDING DISORDER; XA-BINDING-SITE;
   BLOOD-COAGULATION; EAST TEXAS; B-DOMAIN; THROMBIN GENERATION; VENOUS
   THROMBOSIS; COFACTOR ACTIVITY; TFPI-ALPHA
AB Factor V (FV) is a regulator of both pro- and anticoagulant pathways. It circulates as a single-chain procofactor, which is activated by thrombin or FXa to FVa that serves as cofactor for FXa in prothrombin activation. The cofactor function of FVa is regulated by activated protein C (APC) and protein S. FV can also function as an anticoagulant APC cofactor in the inhibition of FVIIIa in the membrane-bound tenase complex (FIXa/FVIIIa). In recent years, it has become clear that FV also functions in multiple ways in the tissue factor pathway inhibitor (TFPI) anticoagulant pathway. Of particular importance is a FV splice variant (FV-Short) that serves as a carrier and cofactor to TFPI alpha in the inhibition of FXa. FV-Short is generated through alternative splicing of exon 13 that encodes the large activation B domain. A highly negatively charged binding site for TFPI alpha is exposed in the C-terminus of the FV-Short B domain, which binds the positively charged C-terminus of TFPI alpha, thus keeping TFPIa in circulation. The binding of TFPI alpha to FV-Short is also instrumental in localizing the inhibitor to the surface of negatively charged phospholipids, where TFPI alpha inhibits FXa in process that is stimulated by protein S. Plasma FV activation intermediates and partially proteolyzed platelet FV similarly bind TFPI alpha with high affinity and regulate formation of prothrombinase. The novel insights gained into the interaction between FV isoforms, TFPI alpha, and protein S have opened a new avenue for research about the mechanisms of coagulation regulation and also for future development of therapeutics aimed at modulating coagulation.
C1 [Dahlback, B.] Lund Univ, Univ Hosp SUS, Dept Translat Med, Inga Marie Nilssons St 53, S-20502 Malmo, Sweden.
C3 Lund University
RP Dahlbäck, B (corresponding author), Lund Univ, Univ Hosp SUS, Dept Translat Med, Inga Marie Nilssons St 53, S-20502 Malmo, Sweden.
EM bjorn.dahlback@med.lu.se
OI Dahlback, Bjorn/0000-0003-1546-0328
CR Ahnström J, 2012, BLOOD, V120, P5059, DOI 10.1182/blood-2012-05-432005
   Asselta R, 2009, SEMIN THROMB HEMOST, V35, P382, DOI 10.1055/s-0029-1225760
   Autin L, 2006, PROTEINS, V63, P440, DOI 10.1002/prot.20848
   Ayombil F, 2013, J THROMB HAEMOST, V11, P1532, DOI 10.1111/jth.12307
   Baugh RJ, 1998, J BIOL CHEM, V273, P4378, DOI 10.1074/jbc.273.8.4378
   Bendz B, 2000, BLOOD COAGUL FIBRIN, V11, P343, DOI 10.1097/00001721-200006000-00005
   BERTINA RM, 1994, NATURE, V369, P64, DOI 10.1038/369064a0
   Bos MHA, 2012, J BIOL CHEM, V287, P26342, DOI 10.1074/jbc.M112.377168
   Broze GJ, 2013, J CLIN INVEST, V123, P3710, DOI 10.1172/JCI71220
   Broze GJ, 2012, FRONT BIOSCI-LANDMRK, V17, P262, DOI 10.2741/3926
   Bunce MW, 2013, J BIOL CHEM, V288, P30151, DOI 10.1074/jbc.M113.506840
   Camire RM, 2016, HAEMOPHILIA, V22, P3, DOI 10.1111/hae.13004
   Camire RM, 2009, J THROMB HAEMOST, V7, P1951, DOI 10.1111/j.1538-7836.2009.03622.x
   Castoldi E, 2004, CURR OPIN HEMATOL, V11, P176, DOI 10.1097/01.moh.0000130315.41033.32
   Castoldi E, 2004, BLOOD, V103, P4173, DOI 10.1182/blood-2003-10-3578
   Castoldi E, 2010, J THROMB HAEMOST, V8, P445, DOI 10.1111/j.1538-7836.2009.03711.x
   Castoldi E, 2010, J THROMB HAEMOST, V8, P294, DOI 10.1111/j.1538-7836.2009.03712.x
   Cunha MLR, 2015, BLOOD, V125, P1822, DOI 10.1182/blood-2014-08-592733
   DAHLBACK B, 1993, P NATL ACAD SCI USA, V90, P1004, DOI 10.1073/pnas.90.3.1004
   Dahlbäck B, 2005, ARTERIOSCL THROM VAS, V25, P1311, DOI 10.1161/01.ATV.0000168421.13467.82
   Dahlbäck B, 2003, J THROMB HAEMOST, V1, P3, DOI 10.1046/j.1538-7836.2003.00016.x
   DAHLBACK B, 1994, P NATL ACAD SCI USA, V91, P1396, DOI 10.1073/pnas.91.4.1396
   Dahlbäck B, 2008, BLOOD, V112, P19, DOI 10.1182/blood-2008-01-077909
   Dahlbäck B, 2016, INT J LAB HEMATOL, V38, P4, DOI 10.1111/ijlh.12508
   Duckers C, 2008, BLOOD, V112, P3615, DOI 10.1182/blood-2008-06-162453
   Duckers C, 2010, BLOOD, V115, P879, DOI 10.1182/blood-2009-08-237719
   Duckers C, 2009, BRIT J HAEMATOL, V146, P17, DOI 10.1111/j.1365-2141.2009.07708.x
   Esmon CT, 2009, BLOOD REV, V23, P225, DOI 10.1016/j.blre.2009.07.002
   Fager AM, 2010, ARTERIOSCL THROM VAS, V30, P2400, DOI 10.1161/ATVBAHA.110.216531
   Girard TJ, 2012, BLOOD, V119, P1256, DOI 10.1182/blood-2011-10-388512
   GRIFFIN JH, 1993, BLOOD, V82, P1989
   Griffin JH, 2012, INT J HEMATOL, V95, P333, DOI 10.1007/s12185-012-1059-0
   Hackeng TM, 2009, J THROMB HAEMOST, V7, P165, DOI 10.1111/j.1538-7836.2009.03363.x
   Hackeng TM, 2006, P NATL ACAD SCI USA, V103, P3106, DOI 10.1073/pnas.0504240103
   Ivanciu L, 2014, BLOOD, V124, P1705, DOI 10.1182/blood-2014-03-565010
   JENNY RJ, 1987, P NATL ACAD SCI USA, V84, P4846, DOI 10.1073/pnas.84.14.4846
   Kalafatis M, 2003, J BIOL CHEM, V278, P33550, DOI 10.1074/jbc.M303153200
   KANE WH, 1986, P NATL ACAD SCI USA, V83, P6800, DOI 10.1073/pnas.83.18.6800
   KANE WH, 1987, BIOCHEMISTRY-US, V26, P6508, DOI 10.1021/bi00394a033
   KELLER FG, 1995, BIOCHEMISTRY-US, V34, P4118, DOI 10.1021/bi00012a030
   Krishnaswamy S, 2013, J THROMB HAEMOST, V11, P265, DOI 10.1111/jth.12217
   Kuang SQ, 2001, BLOOD, V97, P1549, DOI 10.1182/blood.V97.6.1549
   Lechtenberg BC, 2013, BLOOD, V122, P2777, DOI 10.1182/blood-2013-06-511733
   Livaja-Koshiar R, 2015, J THROMB HAEMOST, V13, P54
   Maroney SA, 2015, J THROMB HAEMOST, V13, pS200, DOI 10.1111/jth.12897
   Maroney SA, 2012, THROMB RES, V129, pS21, DOI 10.1016/j.thromres.2012.02.023
   Mast AE, 2016, ARTERIOSCL THROM VAS, V36, P9, DOI 10.1161/ATVBAHA.115.305996
   MONKOVIC DD, 1990, BIOCHEMISTRY-US, V29, P1118, DOI 10.1021/bi00457a004
   Morrissey JH, 2015, J THROMB HAEMOST, V13, pS92, DOI 10.1111/jth.12896
   Nakayama D, 2011, FEBS LETT, V585, P3020, DOI 10.1016/j.febslet.2011.08.022
   Ndonwi M, 2012, J THROMB HAEMOST, V10, P1944, DOI 10.1111/j.1538-7836.2012.04834.x
   Ndonwi M, 2010, BLOOD, V116, P1344, DOI 10.1182/blood-2009-10-246686
   Nicolaes GAF, 2002, ARTERIOSCL THROM VAS, V22, P530, DOI 10.1161/01.ATV.0000012665.51263.B7
   Nogami K, 2014, BLOOD, V123, P2420, DOI 10.1182/blood-2013-10-530089
   Norstrom EA, 2003, J BIOL CHEM, V278, P24904, DOI 10.1074/jbc.M303829200
   Norstrom EA, 2006, J BIOL CHEM, V281, P31486, DOI 10.1074/jbc.M606441200
   Peraramelli S, 2015, THROMB HAEMOSTASIS, P115
   Peraramelli S, 2012, THROMB RES, V129, pS23, DOI 10.1016/j.thromres.2012.02.024
   Pezeshkpoor B, 2016, J THROMB HAEMOST, V14, P1353, DOI 10.1111/jth.13339
   ROSING J, 1995, J BIOL CHEM, V270, P27852, DOI 10.1074/jbc.270.46.27852
   SANDSET PM, 1988, THROMB RES, V50, P803, DOI 10.1016/0049-3848(88)90340-4
   Segers K, 2007, THROMB HAEMOSTASIS, V98, P530, DOI 10.1160/TH07-02-0150
   SHEN L, 1994, J BIOL CHEM, V269, P18735
   Steen M, 2002, J BIOL CHEM, V277, P38424, DOI 10.1074/jbc.M204972200
   Steen M, 2008, J BIOL CHEM, V283, P20805, DOI 10.1074/jbc.M802703200
   SVENSSON PJ, 1994, NEW ENGL J MED, V330, P517, DOI 10.1056/NEJM199402243300801
   Thalji N, 2013, SEMIN THROMB HEMOST, V39, P607, DOI 10.1055/s-0033-1349224
   Thorelli E, 1998, J BIOL CHEM, V273, P16140, DOI 10.1074/jbc.273.26.16140
   Thorelli E, 1997, EUR J BIOCHEM, V247, P12, DOI 10.1111/j.1432-1033.1997.00012.x
   Thorelli E, 1998, THROMB HAEMOSTASIS, V80, P92, DOI 10.1055/s-0037-1615145
   Toso R, 2014, BLOOD, V124, DOI 10.1182/blood.V124.21.578.578
   Tran S, 2008, J BIOL CHEM, V283, P6648, DOI 10.1074/jbc.M708036200
   van Doorn P, 2017, J THROMB HAEMOST, V15, P140, DOI 10.1111/jth.13559
   Vincent LM, 2013, J CLIN INVEST, V123, P3777, DOI 10.1172/JCI69091
   Wood JP, 2014, ARTERIOSCL THROM VAS, V34, P169, DOI 10.1161/ATVBAHA.113.302655
   Wood JP, 2013, P NATL ACAD SCI USA, V110, P17838, DOI 10.1073/pnas.1310444110
NR 76
TC 55
Z9 58
U1 0
U2 6
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 1538-7933
EI 1538-7836
J9 J THROMB HAEMOST
JI J. Thromb. Haemost.
PD JUL
PY 2017
VL 15
IS 7
BP 1241
EP 1250
DI 10.1111/jth.13665
PG 10
WC Hematology; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Hematology; Cardiovascular System & Cardiology
GA EZ3IX
UT WOS:000404605700003
PM 28671348
OA hybrid
DA 2025-04-10
ER

PT J
AU Horiuchi, H
   Inoue, T
   Furusawa, S
   Matsuda, H
AF Horiuchi, H
   Inoue, T
   Furusawa, S
   Matsuda, H
TI Characterization and expression of three forms of cDNA encoding chicken
   platelet-derived growth factor-A chain
SO GENE
LA English
DT Article
DE cDNA; chicken; splicing; PDGF-A chains; thrombocyte
ID TUMOR-CELL LINES; PDGF-A; SEQUENCE; ESTABLISHMENT; RECEPTOR;
   DIFFERENTIATION; IDENTIFICATION; THROMBOCYTES; EMBRYO; SITES
AB Platelet-derived growth factor (PDGF) affects cell proliferation and differentiation during mammalian embryogenesis. In a number of avian species, PDGF-a receptors and PDGF-A chain (PDGF-A) are present during chicken limb and lens development. However, little is understood about the chicken PDGF-A gene. The present study identified short form type 1 (S1), long form (L) and short form type 2 (S2) cDNA clones encoding chicken PDGF-A chain (PDGF-A). These clones were isolated from a chicken hepatoma cell line (LMH) mRNA by reverse transcriptase-polymerase chain reaction (RT-PCR) and cDNA library cloning. Genomic sequencing and Southern blotting revealed that these forms were generated by alternative splicing. The mRNAs of S1 and L contained two transcription start sites on one exon. At the amino acid level, the mature protein encoded by the L clone showed 90 and 85% homology with the processed coding regions of the long form of human and Xenopus PDGF-A, respectively. The putative mature peptides of all forms of chicken PDGF-A encompassed the eight cysteine residues conserved in all known forms of PDGF. We examined the expression of the three forms in chicken tissues and cells using RT-PCR. Expression of these forms varied among tissues and cells. Levels of PDGF mRNAs were very low in chicken thrombocytes, which are analogous to mammalian platelets. However, the level of PDGF-A chain mRNA expression in chicken thrombocytes peaked 4 h after exposure to type 1 collagen or thrombin, and then decreased gradually with continued incubation. These results suggest that chicken PDGF in thrombocytes plays an important role in the vascular system and in healing damaged tissue. (C) 2001 Elsevier Science B.V. All rights reserved.
C1 Hiroshima Univ, Fac Appl Biol Sci, Dept Immunobiol, Higashihiroshima 7398528, Japan.
C3 Hiroshima University
RP Hiroshima Univ, Fac Appl Biol Sci, Dept Immunobiol, Higashihiroshima 7398528, Japan.
EM hhori10@hiroshima-u.ac.jp
RI Inoue, Takeshi/S-5623-2019; Horiuchi, Hiroyuki/G-6138-2019
OI Horiuchi, Hiroyuki/0000-0002-4844-348X; Inoue,
   Takeshi/0000-0003-3289-4478
CR Afrakhte M, 1996, INT J CANCER, V68, P802
   AKIYAMA Y, 1974, BIKEN J, V17, P105
   ALTSCHUL SF, 1990, J MOL BIOL, V215, P403, DOI 10.1016/S0022-2836(05)80360-2
   [Anonymous], METHOD ENZYMOL
   Ataliotis P, 2000, MECH DEVELOP, V94, P13, DOI 10.1016/S0925-4773(00)00321-X
   BETSHOLTZ C, 1986, NATURE, V320, P695, DOI 10.1038/320695a0
   BEUG H, 1979, CELL, V18, P375, DOI 10.1016/0092-8674(79)90057-6
   BONTHRON DT, 1988, P NATL ACAD SCI USA, V85, P1492, DOI 10.1073/pnas.85.5.1492
   COLLINS T, 1987, NATURE, V328, P621, DOI 10.1038/328621a0
   DEUEL TF, 1981, J BIOL CHEM, V263, P16493
   FENSTERMAKER RA, 1993, J BIOL CHEM, V268, P10482
   HIHARA H, 1974, NATL I ANIM HEALTH Q, V14, P163
   HOPPE J, 1987, FEBS LETT, V223, P243, DOI 10.1016/0014-5793(87)80297-1
   HORIUCHI H, 1990, JPN J VET SCI, V52, P559
   INOUE M, 1988, JPN J VET SCI, V50, P648
   KATAYOSE D, 1993, AM J PHYSIOL, V264, P100
   KAWAGUCHI T, 1987, CANCER RES, V47, P4460
   KOZAK M, 1986, CELL, V44, P283, DOI 10.1016/0092-8674(86)90762-2
   KUNICKI TJ, 1985, P NATL ACAD SCI USA, V82, P7319, DOI 10.1073/pnas.82.21.7319
   MERCOLA M, 1990, DEV BIOL, V138, P114, DOI 10.1016/0012-1606(90)90181-H
   MERCOLA M, 1988, SCIENCE, V241, P1223, DOI 10.1126/science.3413486
   Nielsen H, 1997, PROTEIN ENG, V10, P1, DOI 10.1093/protein/10.1.1
   ORRURTREGER A, 1992, DEVELOPMENT, V115, P1045
   PANABIERES F, 1984, BIOCHEM BIOPH RES CO, V118, P767, DOI 10.1016/0006-291X(84)91461-X
   ROSS R, 1986, CELL, V46, P155, DOI 10.1016/0092-8674(86)90733-6
   Russell DW., 2001, Molecular Cloning: ALaboratory Manual, V1
NR 26
TC 8
Z9 11
U1 0
U2 0
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 0378-1119
EI 1879-0038
J9 GENE
JI Gene
PD JUL 11
PY 2001
VL 272
IS 1-2
BP 181
EP 190
DI 10.1016/S0378-1119(01)00542-X
PG 10
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA 467WR
UT WOS:000170727200021
PM 11470524
DA 2025-04-10
ER

PT J
AU Noetzli, L
   Lo, RW
   Lee-Sherick, AB
   Callaghan, M
   Noris, P
   Savoia, A
   Rajpurkar, M
   Jones, K
   Gowan, K
   Balduini, CL
   Pecci, A
   Gnan, C
   De Rocco, D
   Doubek, M
   Li, L
   Lu, L
   Leung, R
   Landolt-Marticorena, C
   Hunger, S
   Heller, P
   Gutierrez-Hartmann, A
   Liang, XY
   Pluthero, FG
   Rowley, JW
   Weyrich, AS
   Kahr, WHA
   Porter, CC
   Di Paola, J
AF Noetzli, Leila
   Lo, Richard W.
   Lee-Sherick, Alisa B.
   Callaghan, Michael
   Noris, Patrizia
   Savoia, Anna
   Rajpurkar, Madhvi
   Jones, Kenneth
   Gowan, Katherine
   Balduini, Carlo L.
   Pecci, Alessandro
   Gnan, Chiara
   De Rocco, Daniela
   Doubek, Michael
   Li, Ling
   Lu, Lily
   Leung, Richard
   Landolt-Marticorena, Carolina
   Hunger, Stephen
   Heller, Paula
   Gutierrez-Hartmann, Arthur
   Liang Xiayuan
   Pluthero, Fred G.
   Rowley, Jesse W.
   Weyrich, Andrew S.
   Kahr, Walter H. A.
   Porter, Christopher C.
   Di Paola, Jorge
TI Germline mutations in ETV6 are associated with thrombocytopenia,
   red cell macrocytosis and predisposition to lymphoblastic leukemia
SO NATURE GENETICS
LA English
DT Article
ID FAMILIAL THROMBOCYTOPENIA; MEGAKARYOCYTE DEVELOPMENT; TEL ETV6; PROTEIN;
   FUSION; HEMATOPOIESIS; TRANSCRIPTION; INDUCTION; TEL/ETV6; BINDING
AB Some familial platelet disorders are associated with predisposition to leukemia, myelodysplastic syndrome (MDS) or dyserythropoietic anemia(1,2). We identified a family with autosomal dominant thrombocytopenia, high erythrocyte mean corpuscular volume (MCV) and two occurrences of B cell-precursor acute lymphoblastic leukemia (ALL). Whole-exome sequencing identified a heterozygous single-nucleotide change in ETV6 (ets variant 6), c.641C>T, encoding a p.Pro214Leu substitution in the central domain, segregating with thrombocytopenia and elevated MCV. A screen of 23 families with similar phenotypes identified 2 with ETV6 mutations. One family also had a mutation encoding p.Pro214Leu and one individual with ALL. The other family had a c.1252A>G transition producing a p.Arg418Gly substitution in the DNA-binding domain, with alternative splicing and exon skipping. Functional characterization of these mutations showed aberrant cellular localization of mutant and endogenous ETV6, decreased transcriptional repression and altered megakaryocyte maturation. Our findings underscore a key role for ETV6 in platelet formation and leukemia predisposition.
C1 [Noetzli, Leila; Lee-Sherick, Alisa B.; Hunger, Stephen; Porter, Christopher C.; Di Paola, Jorge] Univ Colorado, Dept Pediat, Aurora, CO 80045 USA.
   [Noetzli, Leila; Di Paola, Jorge] Univ Colorado AMC, Human Med Genet & Genom Program, Aurora, CO USA.
   [Lo, Richard W.; Li, Ling; Lu, Lily; Leung, Richard; Pluthero, Fred G.; Kahr, Walter H. A.] Hosp Sick Children, Res Inst, Program Cell Biol, Toronto, ON M5G 1X8, Canada.
   [Lo, Richard W.; Kahr, Walter H. A.] Univ Toronto, Dept Biochem, Toronto, ON, Canada.
   [Callaghan, Michael; Rajpurkar, Madhvi] Wayne State Univ, Dept Pediat, Childrens Hosp Michigan, Detroit, MI 48202 USA.
   [Noris, Patrizia; Balduini, Carlo L.; Pecci, Alessandro] Univ Pavia, Dept Internal Med, IRCCS Policlin San Matteo Fdn, I-27100 Pavia, Italy.
   [Savoia, Anna; Gnan, Chiara; De Rocco, Daniela] Univ Trieste, Dept Med Sci, Trieste, Italy.
   [Savoia, Anna; Gnan, Chiara; De Rocco, Daniela] IRCCS Burlo Garofolo, Inst Maternal & Child Hlth, Trieste, Italy.
   [Jones, Kenneth; Gowan, Katherine; Gutierrez-Hartmann, Arthur] Univ Colorado AMC, Dept Biochem & Mol Genet, Aurora, CO USA.
   [Doubek, Michael] Univ Hosp Brno, Dept Internal Med, Haematol Oncol, Brno, Czech Republic.
   [Landolt-Marticorena, Carolina] Univ Toronto, Dept Med, Div Rheumatol, Univ Hlth Network, Toronto, ON, Canada.
   [Heller, Paula] Univ Buenos Aires, Inst Invest Med Alfredo Lanar, Buenos Aires, DF, Argentina.
   [Gutierrez-Hartmann, Arthur] Univ Colorado AMC, Dept Med, Aurora, CO USA.
   [Liang Xiayuan] Univ Colorado AMC, Dept Pathol, Aurora, CO USA.
   [Rowley, Jesse W.; Weyrich, Andrew S.] Univ Utah, Dept Internal Med, Salt Lake City, UT 84112 USA.
   [Rowley, Jesse W.; Weyrich, Andrew S.] Univ Utah, Mol Med Program, Salt Lake City, UT USA.
   [Kahr, Walter H. A.] Univ Toronto, Dept Paediat, Div Haematol Oncol, Toronto, ON M5S 1A1, Canada.
   [Kahr, Walter H. A.] Hosp Sick Children, Toronto, ON M5G 1X8, Canada.
C3 University of Colorado System; University of Colorado Anschutz Medical
   Campus; AMC Cancer Research Center; University of Toronto; Hospital for
   Sick Children (SickKids); University of Toronto; Wayne State University;
   Children's Hospital of Michigan; University of Pavia; IRCCS Fondazione
   San Matteo; University of Trieste; IRCCS Burlo Garofolo; AMC Cancer
   Research Center; University Hospital Brno; University of Toronto;
   University Health Network Toronto; University of Buenos Aires; AMC
   Cancer Research Center; AMC Cancer Research Center; Utah System of
   Higher Education; University of Utah; Utah System of Higher Education;
   University of Utah; University of Toronto; University of Toronto;
   Hospital for Sick Children (SickKids)
RP Di Paola, J (corresponding author), Univ Colorado, Dept Pediat, Anschutz Med Campus AMC, Aurora, CO 80045 USA.
EM walter.kahr@sickkids.ca; chris.porter@ucdenver.edu;
   jorge.dipaola@ucdenver.edu
RI Porter, Christopher/AAE-8918-2020; Gutierrez-Hartmann,
   Arthur/HTP-8292-2023; Jones, Kenneth/GXF-4945-2022; Callaghan,
   Michael/AAH-2059-2019; Balduini, Carlo/D-9299-2015; Kahr,
   Walter/K-9040-2019; Savoia, Anna/AIC-4560-2022; Doubek,
   Michael/J-7011-2018; Pluthero, Fred/T-8593-2019; PECCI,
   ALESSANDRO/E-9288-2012; Savoia, Anna/B-6463-2014; De Rocco,
   Daniela/K-6753-2016
OI Pluthero, Fred/0000-0002-0451-5840; Heller, Paula
   G./0000-0002-6829-1313; Weyrich, Andrew/0000-0001-9622-4647; Lee
   Sherick, Alisa/0000-0002-1177-7208; Lu, Lily/0000-0001-9306-1563; PECCI,
   ALESSANDRO/0000-0001-9202-7013; Savoia, Anna/0000-0002-2407-2696; Lu,
   Lily/0009-0004-6146-9504; Lo, Richard/0000-0001-5325-5590; Noris,
   Patrizia/0000-0002-5035-3707; De Rocco, Daniela/0000-0002-4536-9798
FU Postle Family Chair in Pediatric Cancer and Blood Disorders; US National
   Institutes of Health [HL112311, GM103806]; Canadian Institutes of Health
   Research (CIHR) [MOP-81208, MOP-259952]; Telethon Foundation [GGP13082]
FX We are grateful to the families studied for their contribution to this
   project. We are also grateful to T. Shaikh, R. Spritz and J. Murray for
   their insightful comments. This work was supported by the Postle Family
   Chair in Pediatric Cancer and Blood Disorders (J.D.P.) and by US
   National Institutes of Health grants HL112311 (A.S.W.) and GM103806
   (J.W.R.). W.H.A.K. was supported by operating grants from the Canadian
   Institutes of Health Research (CIHR; MOP-81208 and MOP-259952). P.N. and
   A.S. were supported by grant GGP13082 from the Telethon Foundation.
CR Bejar R, 2011, NEW ENGL J MED, V364, P2496, DOI 10.1056/NEJMoa1013343
   Fenrick R, 2000, MOL CELL BIOL, V20, P5828, DOI 10.1128/MCB.20.16.5828-5839.2000
   Ge HY, 2011, BIOINFORMATICS, V27, P1922, DOI 10.1093/bioinformatics/btr310
   Green SM, 2010, J BIOL CHEM, V285, P18496, DOI 10.1074/jbc.M109.096958
   Hock H, 2004, GENE DEV, V18, P2336, DOI 10.1101/gad.1239604
   Kahr WHA, 2013, BLOOD, V122, P3349, DOI 10.1182/blood-2013-04-499491
   Kar A, 2013, CRIT REV BIOCHEM MOL, V48, P522, DOI 10.3109/10409238.2013.838202
   Kim D, 2011, GENOME BIOL, V12, DOI 10.1186/gb-2011-12-8-r72
   Kwiatkowski BA, 1998, J BIOL CHEM, V273, P17525, DOI 10.1074/jbc.273.28.17525
   Liu XM, 2011, HUM MUTAT, V32, P894, DOI 10.1002/humu.21517
   Lopez R, 1999, J BIOL CHEM, V274, P30132, DOI 10.1074/jbc.274.42.30132
   Love MI, 2014, GENOME BIOL, V15, DOI 10.1186/s13059-014-0550-8
   Machlus KR, 2013, J CELL BIOL, V201, P785, DOI 10.1083/jcb.201304054
   McKenna A, 2010, GENOME RES, V20, P1297, DOI 10.1101/gr.107524.110
   Million RP, 2004, MOL CELL BIOL, V24, P4685, DOI 10.1128/MCB.24.11.4685-4695.2004
   Mullighan CG, 2007, NATURE, V446, P758, DOI 10.1038/nature05690
   Nichols KE, 2000, NAT GENET, V24, P266, DOI 10.1038/73480
   ORKIN SH, 1982, NATURE, V300, P768, DOI 10.1038/300768a0
   Patel N, 2003, BRIT J HAEMATOL, V122, P94, DOI 10.1046/j.1365-2141.2003.04399.x
   Pereira CF, 2013, CELL STEM CELL, V13, P205, DOI 10.1016/j.stem.2013.05.024
   Rasighaemi P, 2015, HAEMATOLOGICA, V100, P23, DOI 10.3324/haematol.2014.104091
   Raslova H, 2004, J CLIN INVEST, V114, P77, DOI 10.1172/JCI200421197
   Romana SP, 1996, LEUKEMIA, V10, P167
   Roukens MG, 2008, MOL CELL BIOL, V28, P4394, DOI 10.1128/MCB.01914-07
   Rowley JW, 2011, BLOOD, V118, pE101, DOI 10.1182/blood-2011-03-339705
   Song WJ, 1999, NAT GENET, V23, P166, DOI 10.1038/13793
   Strehl S, 2003, LEUKEMIA, V17, P1121, DOI 10.1038/sj.leu.2402923
   Subramanian A, 2005, P NATL ACAD SCI USA, V102, P15545, DOI 10.1073/pnas.0506580102
   Urban D, 2012, BLOOD, V120, P5032, DOI 10.1182/blood-2012-05-431205
   van Doorn-Khosrovani SBV, 2005, ONCOGENE, V24, P4129, DOI 10.1038/sj.onc.1208588
   Van Vlierberghe P, 2011, J EXP MED, V208, P2571, DOI 10.1084/jem.20112239
   Wang K, 2010, NUCLEIC ACIDS RES, V38, DOI 10.1093/nar/gkq603
   Wang LC, 1997, EMBO J, V16, P4374, DOI 10.1093/emboj/16.14.4374
   Wang LC, 1998, GENE DEV, V12, P2392, DOI 10.1101/gad.12.15.2392
   Wilcox DA, 2003, J THROMB HAEMOST, V1, P2477, DOI 10.1111/j.1538-7836.2003.00534.x
   Wu TD, 2010, BIOINFORMATICS, V26, P873, DOI 10.1093/bioinformatics/btq057
   Zhang MY, 2015, NAT GENET, V47, P180, DOI 10.1038/ng.3177
NR 37
TC 221
Z9 240
U1 1
U2 23
PU NATURE PUBLISHING GROUP
PI NEW YORK
PA 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA
SN 1061-4036
EI 1546-1718
J9 NAT GENET
JI Nature Genet.
PD MAY
PY 2015
VL 47
IS 5
BP 535
EP U143
DI 10.1038/ng.3253
PG 6
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA CG9LE
UT WOS:000353635800018
PM 25807284
OA Green Accepted, Green Submitted
DA 2025-04-10
ER

PT J
AU Park, Y
   Kim, YJ
   Dupriez, V
   Adams, ME
AF Park, Y
   Kim, YJ
   Dupriez, V
   Adams, ME
TI Two subtypes of ecdysis-triggering hormone receptor in Drosophila
   melanogaster
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID CRUSTACEAN CARDIOACTIVE PEPTIDE; IDENTIFICATION; SEQUENCE; NEURONS
AB Insect ecdysis is a hormonally programmed physiological sequence that enables insects to escape their old cuticle at the end of each developmental stage. The immediate events leading to ecdysis, which are initiated upon release of ecdysis-triggering hormones (ETH) into the bloodstream, include respiratory inflation and sequential stereotypic behaviors that facilitate shedding of the cuticle. Here we report that the Drosophila gene CG5911 encodes two functionally distinct subtypes of G protein-coupled receptors through alternative splicing (CG5911a and CG5911b) that respond preferentially to ecdysis-triggering hormones of flies and moths. These subtypes show differences in ligand sensitivity and specificity, suggesting that they may play separate roles in ETH signaling. At significantly higher concentrations (> 100-fold), certain insect and vertebrate peptides also activate these receptors, providing evidence that CG5911 is evolutionarily related to the thyrotropin-releasing hormone and neuromedin U receptors. The ETH signaling system in insects is a vital system that provides opportunities for the construction of models for the molecular basis of stereotypic animal behavior as well as a target for the design of more sophisticated insect-selective pest control strategies.
C1 Univ Calif Riverside, Dept Cell Biol & Neurosci, Riverside, CA 92521 USA.
   Univ Calif Riverside, Dept Entomol, Riverside, CA 92521 USA.
   Euroscreen SA, B-6041 Gosselies, Belgium.
C3 University of California System; University of California Riverside;
   University of California System; University of California Riverside
RP Univ Calif Riverside, Dept Cell Biol & Neurosci, 5429 Boyce Hall, Riverside, CA 92521 USA.
EM adams@mail.ucr.edu
RI Kim, Young-Joon/JEO-4995-2023; Adams, Michael/ABF-6728-2020; Park,
   Yoonseong/J-5861-2013
OI Park, Yoonseong/0000-0003-1191-7335; Kim, Young-Joon/0000-0002-7990-754X
FU NIAID NIH HHS [AI-40555] Funding Source: Medline
CR Adams MD, 2000, SCIENCE, V287, P2185, DOI 10.1126/science.287.5461.2185
   Adams ME, 1997, BIOCHEM BIOPH RES CO, V230, P188, DOI 10.1006/bbrc.1996.5915
   Aguinaldo AMA, 1997, NATURE, V387, P489, DOI 10.1038/387489a0
   Ewer J, 1996, J COMP NEUROL, V370, P330
   Gammie SC, 1999, J EXP BIOL, V202, P343
   Hewes RS, 2001, GENOME RES, V11, P1126, DOI 10.1101/gr.169901
   HUESMANN GR, 1995, FEBS LETT, V371, P311, DOI 10.1016/0014-5793(95)00929-4
   Iversen A, 2002, BIOCHEM BIOPH RES CO, V299, P924, DOI 10.1016/S0006-291X(02)02798-5
   Jespersen T, 2002, BIOTECHNIQUES, V32, P536, DOI 10.2144/02323st05
   Le Poul E, 2002, J BIOMOL SCREEN, V7, P57, DOI 10.1089/108705702753520341
   MATSUMOTO S, 1990, J INSECT PHYSIOL, V36, P427, DOI 10.1016/0022-1910(90)90060-S
   McNabb SL, 1997, NEURON, V19, P813, DOI 10.1016/S0896-6273(00)80963-0
   Meng XJ, 2002, MECH DEVELOP, V117, P5, DOI 10.1016/S0925-4773(02)00175-2
   MORRIS HR, 1982, NATURE, V300, P643, DOI 10.1038/300643a0
   O'Brien MA, 1998, J EXP BIOL, V201, P193
   OFFERMANNS S, 1995, J BIOL CHEM, V270, P15175, DOI 10.1074/jbc.270.25.15175
   Park Y, 1999, FEBS LETT, V463, P133, DOI 10.1016/S0014-5793(99)01622-1
   Park Y, 2002, DEVELOPMENT, V129, P493
   Park Y, 2002, P NATL ACAD SCI USA, V99, P11423, DOI 10.1073/pnas.162276199
   RAINA AK, 1989, SCIENCE, V244, P796, DOI 10.1126/science.244.4906.796
   RIZZUTO R, 1992, NATURE, V358, P325, DOI 10.1038/358325a0
   Truman JW, 1996, J EXP BIOL, V199, P749
   Zitnan D, 2000, J EXP BIOL, V203, P1329
   Zitnan D, 1999, NEURON, V23, P523, DOI 10.1016/S0896-6273(00)80805-3
   Zitnan D, 1996, SCIENCE, V271, P88, DOI 10.1126/science.271.5245.88
NR 25
TC 71
Z9 88
U1 1
U2 18
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD MAY 16
PY 2003
VL 278
IS 20
BP 17710
EP 17715
DI 10.1074/jbc.M301119200
PG 6
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 677YX
UT WOS:000182838300017
PM 12586820
OA hybrid
DA 2025-04-10
ER

PT J
AU Kaur, S
   Angrish, N
   Vasudevan, M
   Khare, G
AF Kaur, Simran
   Angrish, Nupur
   Vasudevan, Madavan
   Khare, Garima
TI Global proteomics reveals pathways of mesenchymal stem cells altered by
   Mycobacterium tuberculosis
SO SCIENTIFIC REPORTS
LA English
DT Article
DE Host-directed therapeutics; Mesenchymal stem cells; Mycobacterium
   tuberculosis; Proteomics; Pathway analysis
ID THROMBOSPONDIN-2; DIFFERENTIATION; FIBULIN-1; NICHE
AB Mycobacterium tuberculosis (M. tb) has a remarkable ability to persist inside host cells. Several studies showed that M. tb infects and survives inside bone marrow mesenchymal stem cells (BM-MSCs) escaping the host immune system. Here, we have identified various cellular pathways that are modulated in human BM-MSCs upon infection with virulent M. tb and the proteomic profile of these cells varies from that of avirulent M. tb infected cells. We found that virulent M. tb infection reshapes host pathways such as stem cell differentiation, alternative splicing, cytokine production, mitochondrial function etc., which might be modulated by M. tb to persist inside this unconventional niche of human BM-MSCs. Additionally, we observed that virulent M. tb infection suppresses various cellular processes. This study uncovers the differences in the host proteomic profiles resulting from the virulent versus avirulent M. tb infection that can pave the way to identify host-directed therapeutic targets for the treatment of tuberculosis.
C1 [Kaur, Simran; Angrish, Nupur; Khare, Garima] Univ Delhi South Campus, Dept Biochem, New Delhi 110021, India.
   [Vasudevan, Madavan] Theom Int Pvt Ltd, Genom & Data Sci Unit, Bangalore 560038, India.
   [Kaur, Simran] Childrens Hosp Eastern Ontario Res Inst, Ottawa, ON, Canada.
C3 University of Delhi; University of Ottawa; Children's Hospital of
   Eastern Ontario
RP Khare, G (corresponding author), Univ Delhi South Campus, Dept Biochem, New Delhi 110021, India.
EM garimakhare@south.du.ac.in
FU Council of Scientific and Industrial Research, India; BSL3 facility at
   the University of Delhi South Campus (UDSC), New Delhi, India
FX We acknowledge BSL3 facility at the University of Delhi South Campus
   (UDSC), New Delhi, India for providing necessary facilities for
   conducting experiments related to the use of M. tb. We thank UDSC-CIF
   for the mass spectrometry and confocal services. We are also thankful to
   UDSC-Microarray facility and Prof. Amit Gupta for providing us generous
   access of equipment for conducting real-time PCR studies. We acknowledge
   Prof. Anil K. Tyagi and Dr. Prachi Nangpal for critical reading of the
   manuscript. We are thankful to Apoorva Mishra for providing help in
   preparation of the figures related to analysis of proteomics data.
CR [Anonymous], 2023, WHO global TB report
   Arbués A, 2021, FRONT IMMUNOL, V12, DOI 10.3389/fimmu.2021.727508
   Barbera S, 2019, CELL COMMUN SIGNAL, V17, DOI 10.1186/s12964-019-0375-x
   Beamer G, 2014, AM J PATHOL, V184, P3170, DOI 10.1016/j.ajpath.2014.08.024
   Boro M, 2017, J IMMUNOL, V199, P1660, DOI 10.4049/jimmunol.1700129
   Buravkova LB, 2013, BBA-GEN SUBJECTS, V1830, P4418, DOI 10.1016/j.bbagen.2013.05.029
   Celebi Saltik B., 2011, Adv. Mater. Res., V409, P111, DOI [10.4028/www.scientific.net/AMR.409.111, DOI 10.4028/WWW.SCIENTIFIC.NET/AMR.409.111]
   Chauhan K, 2019, J MOL BIOL, V431, P1565, DOI 10.1016/j.jmb.2019.03.001
   Chen YF, 2022, CIRC RES, V131, P1037, DOI 10.1161/CIRCRESAHA.122.321614
   Colonne PM, 2016, FRONT CELL INFECT MI, V6, DOI 10.3389/fcimb.2016.00107
   Cooley MA, 2014, BONE, V69, P30, DOI 10.1016/j.bone.2014.07.038
   Das B, 2013, SCI TRANSL MED, V5, DOI 10.1126/scitranslmed.3004912
   Denzer L, 2020, INT J MOL SCI, V21, DOI 10.3390/ijms21103730
   Diao MQ, 2019, FRONT IMMUNOL, V10, DOI 10.3389/fimmu.2019.02763
   Didusch S, 2022, BMC GENOMICS, V23, DOI 10.1186/s12864-022-09058-7
   Domingo-Gonzalez R, 2018, TUBERCULOSIS AND THE TUBERCLE BACILLUS, 2 EDITION, P33, DOI 10.1128/microbiolspec.TBTB2-0018-2016
   Fatima S, 2020, J CLIN INVEST, V130, P655, DOI 10.1172/JCI128043
   Fernandes H, 2009, TISSUE ENG PT A, V15, P3857, DOI 10.1089/ten.tea.2009.0011
   Forrellad MA, 2013, VIRULENCE, V4, P3, DOI 10.4161/viru.22329
   Friendly M, 2002, AM STAT, V56, P316, DOI 10.1198/000313002533
   Gao XF, 2011, FRONT MICROBIOL, V2, DOI 10.3389/fmicb.2011.00137
   Gao XF, 2009, PLOS PATHOG, V5, DOI 10.1371/journal.ppat.1000708
   Garcia EJ, 2021, AUTOPHAGY, V17, P2363, DOI 10.1080/15548627.2020.1826691
   Garhyan J, 2015, AM J PATHOL, V185, P1924, DOI 10.1016/j.ajpath.2015.03.028
   Gattazzo F, 2014, BBA-GEN SUBJECTS, V1840, P2506, DOI 10.1016/j.bbagen.2014.01.010
   Hankenson KD, 2002, J BONE MINER RES, V17, P415, DOI 10.1359/jbmr.2002.17.3.415
   Heinrichs MT, 2018, INT J MYCOBACT, V7, P156, DOI 10.4103/ijmy.ijmy_33_18
   Huang HY, 2022, P NATL ACAD SCI USA, V119, DOI 10.1073/pnas.2105228119
   Jain N, 2020, NAT COMMUN, V11, DOI 10.1038/s41467-020-16877-3
   Jeong SY, 2015, STEM CELLS, V33, P3291, DOI 10.1002/stem.2120
   Jeong SY, 2013, STEM CELLS, V31, P2136, DOI 10.1002/stem.1471
   Jiang X, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0168387
   Kalam H, 2017, PLOS PATHOG, V13, DOI 10.1371/journal.ppat.1006236
   Kaufmann SHE, 2002, ANN RHEUM DIS, V61, P54
   Kaur S, 2021, INFECT GENET EVOL, V87, DOI 10.1016/j.meegid.2020.104662
   Khan A, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-15290-z
   Khare G, 2013, ANTIMICROB AGENTS CH, V57, P6372, DOI 10.1128/AAC.01444-13
   Krummenauer F, 2002, KLIN MONATSBL AUGENH, V219, P613, DOI 10.1055/s-2002-34420
   Kumar R, 2019, FRONT MOL BIOSCI, V6, DOI 10.3389/fmolb.2019.00105
   Lee JH, 2002, P NATL ACAD SCI USA, V99, P16689, DOI 10.1073/pnas.262569399
   Li H, 2017, ACTA BIOCH BIOPH SIN, V49, P835, DOI 10.1093/abbs/gmx080
   Li P, 2017, FRONT CELL INFECT MI, V7, DOI 10.3389/fcimb.2017.00065
   Li S, 2021, J EXP CLIN CANC RES, V40, DOI 10.1186/s13046-021-02078-3
   Liu HN, 2021, CONNECT TISSUE RES, V62, P325, DOI 10.1080/03008207.2020.1736054
   Lombard R, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0149455
   Longo A, 2014, BIOLOGICALS, V42, P294, DOI 10.1016/j.biologicals.2014.07.002
   Maphasa RE, 2021, FRONT CELL INFECT MI, V10, DOI 10.3389/fcimb.2020.618414
   Menon D, 2019, ACS INFECT DIS, V5, P559, DOI 10.1021/acsinfecdis.8b00301
   Mishra M, 2019, SCI REP-UK, V9, DOI 10.1038/s41598-019-49343-2
   Monin L, 2014, SEMIN IMMUNOL, V26, P552, DOI 10.1016/j.smim.2014.09.004
   Naik SK, 2017, INFECT IMMUN, V85, DOI 10.1128/IAI.00471-17
   Novoseletskaya E, 2020, FRONT CELL DEV BIOL, V8, DOI 10.3389/fcell.2020.555378
   Park JH, 2021, FRONT CELL INFECT MI, V11, DOI 10.3389/fcimb.2021.635335
   Patashnik O, 2020, COMPUT VIS MEDIA, V6, P385, DOI 10.1007/s41095-020-0197-1
   Penn BH, 2018, MOL CELL, V71, P637, DOI 10.1016/j.molcel.2018.07.010
   Pham LBH, 2017, J BIOMED MATER RES A, V105, P2291, DOI 10.1002/jbm.a.36095
   Rai A, 2016, CELL, V164, P722, DOI 10.1016/j.cell.2015.12.054
   Rigaud VOC, 2020, CELLS-BASEL, V9, DOI 10.3390/cells9112490
   Roy S, 2017, AUTOPHAGY, V13, P2013, DOI 10.1080/15548627.2017.1371397
   Shui WQ, 2009, J PROTEOME RES, V8, P282, DOI 10.1021/pr800422e
   Singh VK, 2020, MICROBES INFECT, V22, P423, DOI 10.1016/j.micinf.2020.05.015
   Somaiah C, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0145068
   Squeglia F, 2018, BIOCHEM J, V475, P3123, DOI 10.1042/BCJ20180482
   Su ZP, 2020, MED SCI MONITOR, V26, DOI 10.12659/MSM.920122
   Tang DD, 2023, PLOS ONE, V18, DOI 10.1371/journal.pone.0294236
   Upadhyay S, 2018, PATHOG DIS, V76, DOI 10.1093/femspd/fty037
   Wan J, 2022, ADV CLIN EXP MED, V31, P889, DOI 10.17219/acem/147271
   Wang RX, 2022, CURR BIOL, V32, P1262, DOI 10.1016/j.cub.2022.01.040
   Zhang W, 2018, BIOENGINEERED, V9, P203, DOI 10.1080/21655979.2017.1387692
   Zheng HJ, 2008, PLOS ONE, V3, DOI 10.1371/journal.pone.0002375
   Zouhar J, 2009, PLANT PHYSIOL, V149, P1668, DOI 10.1104/pp.108.134361
NR 71
TC 0
Z9 0
U1 1
U2 1
PU NATURE PORTFOLIO
PI BERLIN
PA HEIDELBERGER PLATZ 3, BERLIN, 14197, GERMANY
SN 2045-2322
J9 SCI REP-UK
JI Sci Rep
PD DEC 28
PY 2024
VL 14
IS 1
AR 30677
DI 10.1038/s41598-024-75722-5
PG 15
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA Q6Z6J
UT WOS:001386137300007
PM 39730375
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Damas, C
   Vink, T
   Nieuwenhuis, HK
   Sixma, JJ
AF Damas, C
   Vink, T
   Nieuwenhuis, HK
   Sixma, JJ
TI The 33-kDa platelet α-granule membrane protein (GMP-33) is an N-terminal
   proteolytic fragment of thrombospondin
SO THROMBOSIS AND HAEMOSTASIS
LA English
DT Article
DE thrombospondin; platelet alpha-granule; platelet activation; platelet
   membrane
ID HEPARIN-BINDING FRAGMENT; AGGREGATION; SURFACE; AMPLIFICATION;
   EXPRESSION; ACTIVATION; SECRETION; PEPTIDES; INVITRO; INHIBIT
AB GMP-33 is a platelet membrane associated protein that is recognised by RUU-SP 1.77, an antibody raised against activated platelets. GMP-33 is predominantly associated with the membrane of platelet alpha -granules and it is translocated to the plasma membrane upon platelet activation (Metzelaar et al. Blood 1992; 79: 372-9). In this study we have isolated the protein by immunoaffinity chromatography. The N-terminus was sequenced and was identical to the N-terminal sequence of human thrombospondin, The protein was N-glycosylated and bound to heparin as would be expected of the N-terminal part of thrombospondin. RUU-SP 1.77 reacted only with reduced thrombospondin. Plasmin and trypsin digestion of thrombospondin yielded fragments of approximately the same size as GMP 33 that reacted with RUU-SP 1.77 after reduction. No evidence for alternative splicing was found. We postulate that GMP 33 is an N-terminal proteolytic fragment of thrombospondin that is membrane associated.
C1 Univ Utrecht, Dept Haematol, Utrecht, Netherlands.
   Univ Utrecht, Grad Sch Biomembranes, Utrecht, Netherlands.
C3 Utrecht University; Utrecht University
RP Sixma, JJ (corresponding author), Univ Utrecht Hosp, Dept Haematol G03647, POB 85-500, NL-3508 GA Utrecht, Netherlands.
CR AGBANYO FR, 1993, J CLIN INVEST, V92, P288, DOI 10.1172/JCI116563
   AIKEN ML, 1987, BLOOD, V69, P58
   ALTSCHUL SF, 1990, J MOL BIOL, V215, P403, DOI 10.1016/S0022-2836(05)80360-2
   BORNSTEIN P, 1995, J CELL BIOL, V130, P503, DOI 10.1083/jcb.130.3.503
   BORNSTEIN P, 1991, J BIOL CHEM, V266, P12821
   BORNSTEIN P, 1994, METHOD ENZYMOL, V245, P62
   CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
   DIXIT VM, 1984, J BIOL CHEM, V259, P100
   EDMAN P, 1967, EUR J BIOCHEM, V1, P80, DOI 10.1111/j.1432-1033.1967.tb00047.x
   FAUVEL J, 1986, BIOCHIM BIOPHYS ACTA, V856, P155, DOI 10.1016/0005-2736(86)90022-2
   FEINBERG AP, 1983, ANAL BIOCHEM, V132, P6, DOI 10.1016/0003-2697(83)90418-9
   FROHMAN MA, 1988, P NATL ACAD SCI USA, V85, P8998, DOI 10.1073/pnas.85.23.8998
   FUGMAN DA, 1990, BLOOD, V75, P1252
   GARTNER TK, 1984, BIOCHEM BIOPH RES CO, V124, P290, DOI 10.1016/0006-291X(84)90950-1
   Gawaz M, 1996, ARTERIOSCL THROM VAS, V16, P621, DOI 10.1161/01.ATV.16.5.621
   GEORGE JN, 1980, J CLIN INVEST, V66, P1, DOI 10.1172/JCI109821
   GOOD DJ, 1990, P NATL ACAD SCI USA, V87, P6624, DOI 10.1073/pnas.87.17.6624
   LAEMMLI UK, 1970, NATURE, V227, P680, DOI 10.1038/227680a0
   LAWLER J, 1986, J CELL BIOL, V103, P1635, DOI 10.1083/jcb.103.5.1635
   LAWLER J, 1986, BLOOD, V67, P555
   LAWLER J, 1986, BLOOD, V67, P1197
   LEGRAND C, 1992, BLOOD, V79, P1995
   LEGRAND C, 1994, ARTERIOSCLER THROMB, V14, P1784, DOI 10.1161/01.ATV.14.11.1784
   METZELAAR MJ, 1993, J LAB CLIN MED, V121, P579
   METZELAAR MJ, 1992, BLOOD, V79, P372
   MORANDI V, 1994, FEBS LETT, V346, P156, DOI 10.1016/0014-5793(94)00460-9
   MURPHYULLRICH JE, 1993, J BIOL CHEM, V268, P26784
   RabhiSabile S, 1996, BLOOD COAGUL FIBRIN, V7, P237, DOI 10.1097/00001721-199603000-00032
   REED MJ, 1995, AM J PATHOL, V147, P1068
   Sambrook J, 1989, MOL CLONING LAB MANU
   SCHAEFER BC, 1995, ANAL BIOCHEM, V227, P255, DOI 10.1006/abio.1995.1279
NR 31
TC 15
Z9 17
U1 0
U2 1
PU F K SCHATTAUER VERLAG GMBH
PI STUTTGART
PA P O BOX 10 45 43, LENZHALDE 3, D-70040 STUTTGART, GERMANY
SN 0340-6245
J9 THROMB HAEMOSTASIS
JI Thromb. Haemost.
PD SEP
PY 2001
VL 86
IS 3
BP 887
EP 893
DI 10.1055/s-0037-1616152
PG 7
WC Hematology; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Hematology; Cardiovascular System & Cardiology
GA 472PL
UT WOS:000170992600025
PM 11583323
DA 2025-04-10
ER

PT J
AU Hiltunen, TP
   Gough, PJ
   Greaves, DR
   Gordon, S
   Ylä-Herttuala, S
AF Hiltunen, TP
   Gough, PJ
   Greaves, DR
   Gordon, S
   Ylä-Herttuala, S
TI Rabbit atherosclerotic lesions express scavenger receptor AIII mRNA, a
   naturally occurring splice variant that encodes a non-functional,
   dominant negative form of the macrophage scavenger receptor
SO ATHEROSCLEROSIS
LA English
DT Article
DE macrophage scavenger receptor; reverse transcription polymerase chain
   reaction; alternative splicing; atherogenesis
ID MESSENGER-RNA; LIGAND-BINDING; LDL RECEPTOR; PROTEIN; GENE;
   15-LIPOXYGENASE; INDUCTION
AB Macrophage class A scavenger receptor types I and II (SR-AI and II) mediate the uptake of oxidized LDL in atherosclerotic lesions. The recently described type III receptor (SR-AIII), which lacks amino acids encoded by exon 10 of the SR-A gene. is unable to mediate the uptake of ligands and acts as a dominant negative regulator in the trimeric SR-A molecule. To find out whether SR-AIII might play a role in the regulation of SR-A activity in the arterial wall, we studied its expression in normal and atherosclerotic aortic intima-medias of Watanabe heritable hyperlipidemic (WHHL) and cholesterol-fed New Zealand white (NZW) rabbits. SR-A mRNA was amplified by reverse transcription-polymerase chain reaction (RT-PCR) with a SR-AIII-specific primer pair and with a primer pair suitable for both SR-AI and III. Very low SR-AI expression and no SR-AIII expression was found in the lesion-free aortic intima-medias of WHHL rabbits and control NZW rabbits. WHHL rabbit fatty streaks contained abundant SR-AI expression and low-level SR-AIII expression. In contrast. the numerous fatty streaks and fatty plaques appearing in the aortas of cholesterol-fed (14 weeks) NZW rabbits, and the fatty plaques of WHHL rabbits contained clearly detectable SR-AIII expression in addition to the abundant SR-AI expression. In addition, SR-AIII mRNA was detected in NZW and WHHL rabbit livers. The results suggest that in advanced atherosclerotic lesions, cells may protect themselves from the excessive uptake of oxidized lipoproteins by generating SR-A molecules which cannot bind modified LDL. (C) 2001 Elsevier Science Ireland Ltd. All rights reserved.
C1 Univ Kuopio, AI Virtanen Inst, FIN-70211 Kuopio, Finland.
   Univ Kuopio, Dept Med, FIN-70211 Kuopio, Finland.
   Univ Helsinki, Cent Hosp, Dept Med, Helsinki, Finland.
   Univ Tampere, Sch Med, FIN-33101 Tampere, Finland.
   Univ Washington, Dept Pathol, Seattle, WA 98195 USA.
   Univ Oxford, Sir William Dunn Sch Pathol, Oxford OX1 3RE, England.
C3 University of Eastern Finland; University of Eastern Finland; University
   of Helsinki; Helsinki University Central Hospital; Tampere University;
   University of Washington; University of Washington Seattle; University
   of Oxford
RP Ylä-Herttuala, S (corresponding author), Univ Kuopio, AI Virtanen Inst, POB 1627, FIN-70211 Kuopio, Finland.
RI ; Hiltunen, Timo/B-9436-2008
OI Yla-Herttuala, Seppo/0000-0001-7593-2708; Hiltunen,
   Timo/0000-0001-7011-0422; Greaves, David/0000-0003-2856-9410
CR ASHKENAS J, 1993, J LIPID RES, V34, P983
   EMI M, 1993, J BIOL CHEM, V268, P2120
   GOLDSTEIN JC, 1979, P NATL ACAD SCI USA, V76, P168
   Gough PJ, 1998, J LIPID RES, V39, P531
   Gough PJ, 1999, ARTERIOSCL THROM VAS, V19, P461, DOI 10.1161/01.ATV.19.3.461
   HILTUNEN T, 1995, CIRCULATION, V92, P3297, DOI 10.1161/01.CIR.92.11.3297
   Hiltunen TP, 1998, CIRCULATION, V97, P1079, DOI 10.1161/01.CIR.97.11.1079
   KINGSTON RE, 1991, CURRENT PROTOCOLS MO
   KODAMA T, 1990, NATURE, V343, P531, DOI 10.1038/343531a0
   KRIEGER M, 1994, ANNU REV BIOCHEM, V63, P601, DOI 10.1146/annurev.bi.63.070194.003125
   LUOMA J, 1994, J CLIN INVEST, V93, P2014, DOI 10.1172/JCI117195
   MATSUMOTO A, 1990, P NATL ACAD SCI USA, V87, P9133, DOI 10.1073/pnas.87.23.9133
   MCCULLOCH RK, 1995, PCR METH APPL, V4, P219
   ROHRER L, 1990, NATURE, V343, P570, DOI 10.1038/343570a0
   YLAHERTTUALA S, 1991, J CLIN INVEST, V87, P1146, DOI 10.1172/JCI115111
NR 15
TC 5
Z9 5
U1 0
U2 4
PU ELSEVIER SCI IRELAND LTD
PI CLARE
PA CUSTOMER RELATIONS MANAGER, BAY 15, SHANNON INDUSTRIAL ESTATE CO, CLARE,
   IRELAND
SN 0021-9150
J9 ATHEROSCLEROSIS
JI Atherosclerosis
PD FEB 1
PY 2001
VL 154
IS 2
BP 415
EP 419
DI 10.1016/S0021-9150(00)00519-0
PG 5
WC Cardiac & Cardiovascular Systems; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology
GA 401TY
UT WOS:000166945400018
PM 11166774
DA 2025-04-10
ER

PT J
AU Koppens, PFJ
   Hoogenboezem, T
   Drop, SLS
   de Muinck, SMPF
   Keizer-Schrama
   Degenhart, HJ
AF Koppens, PFJ
   Hoogenboezem, T
   Drop, SLS
   de Muinck, SMPF
   Keizer-Schrama
   Degenhart, HJ
TI Aldosterone production despite absence or defectiveness of the CYP21
   genes in two patients with salt-losing congenital adrenal hyperplasia
   caused by steroid 21-hydroxylase deficiency
SO CLINICAL ENDOCRINOLOGY
LA English
DT Article
ID HUMAN-FETUS; 21-DEOXYALDOSTERONE; DEOXYCORTICOSTERONE; MUTATION;
   GENOTYPE; HYPERTENSION; PROGESTERONE; CONVERSION; PSEUDOGENE; COMPLEMENT
AB Aldosterone and cortisol were found in plasma samples from two patients with salt-losing congenital adrenal hyperplasia caused by steroid 21-hydroxylase deficiency. One patient had a CYP21 gene deletion on one chromosome and a mutation causing erroneous mRNA splicing on the other. The other patient had a CYP21 gene deletion on one chromosome and a large scale conversion of CYP21 to CYP21P on the other. All CYP21P-like genes in these patients were defective, since they carried a deleterious 8 bp deletion in the third exon, After HPLC purification of the patients' plasma samples, cortisol was no longer detectable in the radioimmunoassay, but aldosterone levels were still within or slightly above the normal reference range. Aldosterone dropped to very low levels after steroid replacement therapy had taken effect. In at least one of these patients, the genetic defect rules out normal functioning of the adrenocortical steroid 21-hydroxylase, which implies involvement of an alternative enzyme system.
C1 Erasmus Univ, Paediat Lab, NL-3000 DR Rotterdam, Netherlands.
   Univ Rotterdam Hosp, Sophia Childrens Hosp, Dept Paediat, Rotterdam, Netherlands.
C3 Erasmus University Rotterdam - Excl Erasmus MC; Erasmus University
   Rotterdam; Erasmus University Rotterdam; Erasmus MC - Sophia Children's
   Hospital; Erasmus MC
RP Degenhart, HJ (corresponding author), Erasmus Univ, Paediat Lab, POB 1738, NL-3000 DR Rotterdam, Netherlands.
CR ABDELHAMID S, 1994, J STEROID BIOCHEM, V50, P319, DOI 10.1016/0960-0760(94)90138-4
   ANTONIPILLAI I, 1983, J CLIN ENDOCR METAB, V57, P580, DOI 10.1210/jcem-57-3-580
   BORMANN M, 1992, ACTA ENDOCRINOL-COP, V126, P7, DOI 10.1530/acta.0.1260007
   BROTHERTON J, 1990, J STEROID BIOCHEM, V36, P641, DOI 10.1016/0022-4731(90)90183-S
   CASEY ML, 1983, J STEROID BIOCHEM, V18, P449, DOI 10.1016/0022-4731(83)90064-X
   DELANGE WE, 1980, ACTA ENDOCRINOL-COP, V93, P488, DOI 10.1530/acta.0.0930488
   EGFJORD M, 1992, AM J PHYSIOL, V262, pE488, DOI 10.1152/ajpendo.1992.262.4.E488
   FRANKLIN SO, 1987, J STEROID BIOCHEM, V28, P749, DOI 10.1016/0022-4731(87)90408-0
   HIGASHI Y, 1991, J BIOCHEM-TOKYO, V109, P638, DOI 10.1093/oxfordjournals.jbchem.a123433
   Hoffman WH, 1996, CLIN ENDOCRINOL, V45, P103, DOI 10.1046/j.1365-2265.1996.00736.x
   HORNER JM, 1979, J CLIN ENDOCR METAB, V48, P776, DOI 10.1210/jcem-48-5-776
   JACOBS DR, 1961, J CLIN ENDOCR METAB, V21, P909, DOI 10.1210/jcem-21-8-909
   JAMES VHT, 1978, ENDOCRINE FUNCTION H, P179
   KILLEEN AA, 1991, J STEROID BIOCHEM, V38, P677, DOI 10.1016/0960-0760(91)90078-J
   KOHN B, 1995, AM J MED GENET, V57, P450, DOI 10.1002/ajmg.1320570318
   KOPPENS PFJ, 1995, CLIN GENET, V48, P109
   KOPPENS PFJ, 1992, EUR J PEDIATR, V151, P885, DOI 10.1007/BF01954123
   LAJIC S, 1995, J STEROID BIOCHEM, V52, P181, DOI 10.1016/0960-0760(94)00158-I
   LAND M, 1987, J STEROID BIOCHEM, V26, P207, DOI 10.1016/0022-4731(87)90073-2
   LEWICKA S, 1987, J CLIN ENDOCR METAB, V64, P771, DOI 10.1210/jcem-64-4-771
   LEWICKA S, 1990, ACTA ENDOCRINOL-COP, V123, P225, DOI 10.1530/acta.0.1230225
   MELLON SH, 1989, J CLIN INVEST, V84, P1497, DOI 10.1172/JCI114325
   MORNET E, 1991, AM J HUM GENET, V48, P79
   SCHONESHOFER M, 1983, J STEROID BIOCHEM, V18, P65, DOI 10.1016/0022-4731(83)90332-1
   SCHULZE E, 1995, ENDOCR RES, V21, P359, DOI 10.3109/07435809509030452
   SHACKLETON C H L, 1987, Steroids, V49, P295, DOI 10.1016/0039-128X(87)90006-7
   SINNOTT PJ, 1989, J MED GENET, V26, P10, DOI 10.1136/jmg.26.1.10
   SPEISER PW, 1991, NEW ENGL J MED, V324, P145, DOI 10.1056/NEJM199101173240302
   SPEISER PW, 1992, J CLIN INVEST, V90, P584, DOI 10.1172/JCI115897
   STONER E, 1986, CLIN ENDOCRINOL, V24, P9, DOI 10.1111/j.1365-2265.1986.tb03249.x
   VANVLIET AA, 1992, J HEPATOL, V15, P40, DOI 10.1016/0168-8278(92)90009-E
   VOUTILAINEN R, 1986, J CLIN ENDOCR METAB, V63, P1145, DOI 10.1210/jcem-63-5-1145
   WHITE PC, 1985, P NATL ACAD SCI USA, V82, P1089, DOI 10.1073/pnas.82.4.1089
   WHITMORE MW, 1994, J LOSS PREVENT PROC, V7, P49, DOI 10.1016/0950-4230(94)80016-2
   WILLARD HH, 1965, INSTRUMENTAL METHODS, P342
   WILSON RC, 1995, J CLIN ENDOCR METAB, V80, P2322, DOI 10.1210/jc.80.8.2322
   WINKEL CA, 1980, J CLIN INVEST, V66, P803, DOI 10.1172/JCI109918
NR 37
TC 5
Z9 5
U1 0
U2 0
PU BLACKWELL SCIENCE LTD
PI OXFORD
PA P O BOX 88, OSNEY MEAD, OXFORD OX2 0NE, OXON, ENGLAND
SN 0300-0664
J9 CLIN ENDOCRINOL
JI Clin. Endocrinol.
PD DEC
PY 1998
VL 49
IS 6
BP 815
EP 822
DI 10.1046/j.1365-2265.1998.00431.x
PG 8
WC Endocrinology & Metabolism
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism
GA 149LR
UT WOS:000077607200017
PM 10209571
DA 2025-04-10
ER

PT J
AU Kudo, M
   Takayama, E
   Tadakuma, T
   Shiokawa, K
AF Kudo, M
   Takayama, E
   Tadakuma, T
   Shiokawa, K
TI Molecular cloning of ssd-form neural cell adhesion molecules (N-CAMs) as
   the major form in Xenopus heart
SO BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
LA English
DT Article
ID POLYSIALIC ACID; MESSENGER-RNA; EXTRACELLULAR DOMAIN; MEMBRANE
   ATTACHMENT; SURFACE MODULATION; SKELETAL-MUSCLE; CDNA CLONES; EXON
   USAGE; NCAM; EXPRESSION
AB Different forms of neural cell adhesion molecule (N-CAM) are generated by alternative splicing of primary transcripts and considered to have distinct biological functions. We cloned cDNAs encoding a new form of N-CAMs from the Xenopus heart cDNA library. Comparison of the sequences with chicken and mouse NCAMs revealed that these clones code for ssd-form N-CAM. We demonstrate by Northern blot analysis that the ssd form is the major form expressed in the Xenopus adult heart. We obtained two types of ssd-form N-CAM, which are transcripts from N-CAM 1 and N-CAM 2 genes. Both types contain muscle specific domain (MSD) but not pi domain. Northern blot analysis also indicated that this form is not expressed in adult brain, in which ld-form N-CAM is the main N-CAM expressed, It is possible that high levels of specific expression of ssd-form N-CAM. are related with the differentiation of cardiac muscles. (C) 1998 Academic Press.
C1 Univ Tokyo, Grad Sch Sci, Dept Biol Sci, Bunkyo Ku, Tokyo 113, Japan.
   Natl Def Med Coll, Dept Parasitol, Tokorozawa, Saitama 359, Japan.
C3 University of Tokyo; National Defense Medical College - Japan
RP Shiokawa, K (corresponding author), Univ Tokyo, Grad Sch Sci, Dept Biol Sci, Bunkyo Ku, Hongo 7-3-1, Tokyo 113, Japan.
RI Kudo, Masatoshi/AAA-9744-2019
CR ACHESON A, 1991, J CELL BIOL, V114, P143, DOI 10.1083/jcb.114.1.143
   AVIV H, 1972, P NATL ACAD SCI USA, V69, P1408, DOI 10.1073/pnas.69.6.1408
   BARTON CH, 1988, DEVELOPMENT, V104, P165
   CHIRGWIN JM, 1979, BIOCHEMISTRY-US, V18, P5294, DOI 10.1021/bi00591a005
   CUNNINGHAM BA, 1987, SCIENCE, V236, P799, DOI 10.1126/science.3576199
   DICKSON G, 1987, CELL, V50, P1119, DOI 10.1016/0092-8674(87)90178-4
   EDELMAN GM, 1991, ANNU REV BIOCHEM, V60, P155, DOI 10.1146/annurev.biochem.60.1.155
   EDELMAN GM, 1985, ANNU REV BIOCHEM, V54, P135, DOI 10.1146/annurev.bi.54.070185.001031
   FREDETTE B, 1993, J CELL BIOL, V123, P1867, DOI 10.1083/jcb.123.6.1867
   GORIDIS C, 1988, NEUROCHEM INT, V12, P269, DOI 10.1016/0197-0186(88)90164-7
   GOWER HJ, 1988, CELL, V55, P955, DOI 10.1016/0092-8674(88)90241-3
   HE HT, 1987, J CELL BIOL, V105, P2489, DOI 10.1083/jcb.105.6.2489
   HE HT, 1986, EMBO J, V5, P2489, DOI 10.1002/j.1460-2075.1986.tb04526.x
   HEMPERLY JJ, 1986, P NATL ACAD SCI USA, V83, P9822, DOI 10.1073/pnas.83.24.9822
   HESSION C, 1992, BIOCHEM BIOPH RES CO, V183, P163, DOI 10.1016/0006-291X(92)91623-X
   KNUDSEN KA, 1990, DEV BIOL, V138, P159, DOI 10.1016/0012-1606(90)90185-L
   KRIEG PA, 1989, NUCLEIC ACIDS RES, V17, P10321, DOI 10.1093/nar/17.24.10321
   KRUSE J, 1984, NATURE, V311, P153, DOI 10.1038/311153a0
   LACKIE PM, 1991, DIFFERENTIATION, V47, P85, DOI 10.1111/j.1432-0436.1991.tb00226.x
   LEVI G, 1987, J CELL BIOL, V105, P2359, DOI 10.1083/jcb.105.5.2359
   LEVI G, 1990, DEVELOPMENT, V109, P681
   MARGOLIS RK, 1983, BIOCHEM BIOPH RES CO, V116, P889, DOI 10.1016/S0006-291X(83)80225-3
   MURRAY BA, 1986, J CELL BIOL, V103, P1431, DOI 10.1083/jcb.103.4.1431
   OWENS GC, 1987, P NATL ACAD SCI USA, V84, P294, DOI 10.1073/pnas.84.1.294
   PECK D, 1993, J CELL BIOL, V123, P1587, DOI 10.1083/jcb.123.6.1587
   PROBSTMEIER R, 1994, J NEUROSCI RES, V37, P324, DOI 10.1002/jnr.490370305
   RUTISHAUSER U, 1988, SCIENCE, V240, P53, DOI 10.1126/science.3281256
   RUTISHAUSER U, 1989, NEUROBIOLOGY GLYCOCO, P367
   Sambrook J, 1989, MOL CLONING LAB MANU
   SANTONI MJ, 1989, EMBO J, V8, P385, DOI 10.1002/j.1460-2075.1989.tb03389.x
   SANTONI MJ, 1987, NUCLEIC ACIDS RES, V15, P8621, DOI 10.1093/nar/15.21.8621
   SMALL SJ, 1988, NEURON, V1, P1007, DOI 10.1016/0896-6273(88)90158-4
   SORKIN BC, 1984, SCIENCE, V225, P1476, DOI 10.1126/science.6474186
   TAKEBE Y, 1988, MOL CELL BIOL, V8, P466, DOI 10.1128/MCB.8.1.466
   THOMPSON J, 1989, GENE DEV, V3, P348, DOI 10.1101/gad.3.3.348
   TONISSEN KF, 1993, GENE, V127, P243, DOI 10.1016/0378-1119(93)90727-K
   WATANABE M, 1992, DEV DYNAM, V194, P128, DOI 10.1002/aja.1001940206
   YANG PF, 1992, J CELL BIOL, V116, P1487, DOI 10.1083/jcb.116.6.1487
   ZORN AM, 1992, DEV BIOL, V149, P197, DOI 10.1016/0012-1606(92)90276-M
NR 39
TC 2
Z9 2
U1 0
U2 0
PU ACADEMIC PRESS INC
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0006-291X
J9 BIOCHEM BIOPH RES CO
JI Biochem. Biophys. Res. Commun.
PD APR 7
PY 1998
VL 245
IS 1
BP 127
EP 132
DI 10.1006/bbrc.1998.8347
PG 6
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA ZK045
UT WOS:000073279400023
PM 9535795
DA 2025-04-10
ER

PT J
AU Chin, K
   Yu, XB
   Beleslin-Cokic, B
   Liu, C
   Shen, K
   Mohrenweiser, HW
   Noguchi, CT
AF Chin, K
   Yu, XB
   Beleslin-Cokic, B
   Liu, C
   Shen, K
   Mohrenweiser, HW
   Noguchi, CT
TI Production and processing of erythropoietin receptor transcripts in
   brain
SO MOLECULAR BRAIN RESEARCH
LA English
DT Article
DE erythropoietin receptor; brain transcript; alternative splicing;
   upstream transcription; anemic stress; induced expression
ID CENTRAL-NERVOUS-SYSTEM; ENDOTHELIAL-CELLS; GENE-EXPRESSION;
   NITRIC-OXIDE; IN-VITRO; RAT HIPPOCAMPAL; MICE LACKING; MOUSE-BRAIN;
   FACTOR AP-2; NEURONS
AB The expression of erythropoietin receptor (EpoR) in brain and neuronal cells, and hypoxia-responsive production of erythropoietin (Epo) in the brain suggests that the function of Epo as a survival or viability factor may extend beyond hematopoietic tissue and erythroid progenitor cells. Epo, produced by astrocytes and neurons, can be induced by hypoxia by severalfold, and in animal models Epo administration is neuroprotective to ischemic challenge. We characterized the human EpoR transcript in brain and neuronal cells to determine its contribution in regulating the Epo response in brain. Screening of a human brain cDNA library and quantitative analysis of EpoR transcripts indicate that the EpoR gene locus is transcriptionally active in brain. In addition to the proximal promoter that is active in hematopoietic cells, a significant proportion of transcripts originates far upstream from the EpoR coding region. Unlike erythroid cells with efficient splicing of EpoR transcripts to its mature form, brain EpoR transcripts are inefficiently or alternately processed with a bias towards the 3' coding region. In human EpoR transgenic mice, anemic stress induces expression of the transgene and endogenous EpoR gene in hematopoietic tissue and brain. In culture of neuronal cells, hypoxia induces EpoR expression and increases sensitivity to Epo. Induction of EpoR expression appears to be a consequence of increased transcription from the upstream region and proximal promoter, and a shift towards increased processing efficiency. These data suggest that in contrast to erythropoiesis where erythroid progenitor cells express high levels of EpoR and are directly responsive to Epo stimulation, the neuroprotective effect of Epo and its receptor may require two molecular events: the induction of Epo production by hypoxia and an increase in EpoR expression in neuronal cells resulting in increased sensitivity to Epo. (C) 2000 Elsevier Science B.V. All rights reserved.
C1 NIDDK, Biol Chem Lab, NIH, Bethesda, MD 20892 USA.
   Lawrence Livermore Natl Lab, Biol & Biotechnol Res Program, Livermore, CA 94550 USA.
C3 National Institutes of Health (NIH) - USA; NIH National Institute of
   Diabetes & Digestive & Kidney Diseases (NIDDK); United States Department
   of Energy (DOE); Lawrence Livermore National Laboratory
RP NIDDK, Biol Chem Lab, NIH, Bethesda, MD 20892 USA.
EM cnoguchi@helix.nih.gov
CR ANAGNOSTOU A, 1990, P NATL ACAD SCI USA, V87, P5978, DOI 10.1073/pnas.87.15.5978
   ANAGNOSTOU A, 1994, P NATL ACAD SCI USA, V91, P3974, DOI 10.1073/pnas.91.9.3974
   Assandri R, 1999, J PHYSIOL-LONDON, V516, P343, DOI 10.1111/j.1469-7793.1999.0343v.x
   BARRON C, 1994, GENE, V147, P263, DOI 10.1016/0378-1119(94)90078-7
   Bernaudin M, 1999, J CEREBR BLOOD F MET, V19, P643, DOI 10.1097/00004647-199906000-00007
   Centeno JM, 1999, BRAIN RES, V836, P62, DOI 10.1016/S0006-8993(99)01610-8
   CHIBA T, 1991, NUCLEIC ACIDS RES, V19, P3843, DOI 10.1093/nar/19.14.3843
   CHIN K, 1995, NUCLEIC ACIDS RES, V23, P3041, DOI 10.1093/nar/23.15.3041
   DAVIS LG, 1986, BASIC METHODS MOL BI, P136
   DIGICAYLIOGLU M, 1995, P NATL ACAD SCI USA, V92, P3717, DOI 10.1073/pnas.92.9.3717
   FIBACH E, 1989, BLOOD, V73, P100
   IOANNOU PA, 1994, NAT GENET, V6, P84, DOI 10.1038/ng0194-84
   Iyer NV, 1998, GENE DEV, V12, P149, DOI 10.1101/gad.12.2.149
   Juul SE, 1999, PEDIATR DEVEL PATHOL, V2, P148, DOI 10.1007/s100249900103
   Juul SE, 1998, EARLY HUM DEV, V52, P235, DOI 10.1016/S0378-3782(98)00030-9
   Juul SE, 1998, PEDIATR RES, V43, P40, DOI 10.1203/00006450-199801000-00007
   KONISHI Y, 1993, BRAIN RES, V609, P29, DOI 10.1016/0006-8993(93)90850-M
   Koshimura K, 1999, J NEUROCHEM, V72, P2565, DOI 10.1046/j.1471-4159.1999.0722565.x
   Li Y, 1996, PEDIATR RES, V40, P376, DOI 10.1203/00006450-199609000-00002
   Lin CS, 1996, GENE DEV, V10, P154, DOI 10.1101/gad.10.2.154
   Liu C, 1997, J BIOL CHEM, V272, P32395, DOI 10.1074/jbc.272.51.32395
   LIU ZY, 1994, DEV BIOL, V166, P159, DOI 10.1006/dbio.1994.1304
   Maltepe E, 1997, NATURE, V386, P403, DOI 10.1038/386403a0
   MAOUCHE L, 1991, BLOOD, V78, P2557
   Marti HH, 1997, KIDNEY INT, V51, P416, DOI 10.1038/ki.1997.55
   Marti HH, 1996, EUR J NEUROSCI, V8, P666, DOI 10.1111/j.1460-9568.1996.tb01252.x
   MASUDA S, 1992, FEBS LETT, V298, P169, DOI 10.1016/0014-5793(92)80048-L
   MASUDA S, 1994, J BIOL CHEM, V269, P19488
   MASUDA S, 1993, J BIOL CHEM, V268, P11208
   Morishita E, 1997, NEUROSCIENCE, V76, P105, DOI 10.1016/s0306-4522(96)00306-5
   Neubauer H, 1998, CELL, V93, P397, DOI 10.1016/S0092-8674(00)81168-X
   NOGUCHI CT, 1991, BLOOD, V78, P2548
   PANDOLFI PP, 1995, NAT GENET, V11, P40, DOI 10.1038/ng0995-40
   PAPAYANNOPOULOU T, 1988, BLOOD, V72, P1029
   Parganas E, 1998, CELL, V93, P385, DOI 10.1016/S0092-8674(00)81167-8
   PENNY LA, 1991, GENOMICS, V11, P974, DOI 10.1016/0888-7543(91)90022-7
   PLEASURE SJ, 1992, J NEUROSCI, V12, P1802
   ROSS RA, 1983, JNCI-J NATL CANCER I, V71, P741
   Sadamoto Y, 1998, BIOCHEM BIOPH RES CO, V253, P26, DOI 10.1006/bbrc.1998.9748
   Sakanaka M, 1998, P NATL ACAD SCI USA, V95, P4635, DOI 10.1073/pnas.95.8.4635
   Schorle H, 1996, NATURE, V381, P235, DOI 10.1038/381235a0
   Silva M, 1996, BLOOD, V88, P1576, DOI 10.1182/blood.V88.5.1576.1576
   TABIRA T, 1995, INT J DEV NEUROSCI, V13, P241, DOI 10.1016/0736-5748(94)00020-4
   Travers A, 1999, P NATL ACAD SCI USA, V96, P13634, DOI 10.1073/pnas.96.24.13634
   Utepbergenov DI, 1998, FEBS LETT, V424, P197, DOI 10.1016/S0014-5793(98)00173-2
   WICKREMA A, 1992, BLOOD, V80, P1940, DOI 10.1182/blood.V80.8.1940.1940
   Wu H, 1999, DEVELOPMENT, V126, P3597
   WU H, 1995, CELL, V83, P59, DOI 10.1016/0092-8674(95)90234-1
   Wu XC, 1999, CLIN SCI, V97, P413, DOI 10.1042/CS19990055
   YASUDA Y, 1993, DEV GROWTH DIFFER, V35, P711, DOI 10.1111/j.1440-169X.1993.00711.x
   YOUSSOUFIAN H, 1993, BLOOD, V81, P2223
   Zaman K, 1999, J NEUROSCI, V19, P9821
   Zhang JA, 1996, NATURE, V381, P238, DOI 10.1038/381238a0
   ZON LI, 1991, P NATL ACAD SCI USA, V88, P10638, DOI 10.1073/pnas.88.23.10638
NR 54
TC 115
Z9 128
U1 0
U2 4
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
SN 0169-328X
J9 MOL BRAIN RES
JI Mol. Brain Res.
PD SEP 30
PY 2000
VL 81
IS 1-2
BP 29
EP 42
DI 10.1016/S0169-328X(00)00157-1
PG 14
WC Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA 363LW
UT WOS:000089838000004
PM 11000476
DA 2025-04-10
ER

PT J
AU Regimbeau, M
   Mary, R
   Hermetet, F
   Girodon, F
AF Regimbeau, Mathilde
   Mary, Romain
   Hermetet, Francois
   Girodon, Francois
TI Genetic Background of Polycythemia Vera
SO GENES
LA English
DT Review
DE polycythemia vera; JAK2 mutation; erythrocytosis; myeloproliferative
   neoplasm; mutational landscape
ID JAK2 EXON-12 MUTATIONS; GAIN-OF-FUNCTION; TYROSINE KINASE JAK2;
   MYELOPROLIFERATIVE NEOPLASMS; ESSENTIAL THROMBOCYTHEMIA; SOMATIC
   MUTATIONS; ALLELE BURDEN; CHRONIC-PHASE; LEUKEMIC TRANSFORMATION;
   MICRORNA EXPRESSION
AB Polycythemia vera belongs to myeloproliferative neoplasms, essentially by affecting the erythroblastic lineage. JAK2 alterations have emerged as major driver mutations triggering PV-phenotype with the V617F mutation detected in nearly 98% of cases. That's why JAK2 targeting therapeutic strategies have rapidly emerged to counter the aggravation of the disease. Over decades of research, to go further in the understanding of the disease and its evolution, a wide panel of genetic alterations affecting multiple genes has been highlighted. These are mainly involved in alternative splicing, epigenetic, miRNA regulation, intracellular signaling, and transcription factors expression. If JAK2 mutation, irrespective of the nature of the alteration, is known to be a crucial event for the disease to initiate, additional mutations seem to be markers of progression and poor prognosis. These discoveries have helped to characterize the complex genomic landscape of PV, resulting in potentially new adapted therapeutic strategies for patients concerning all the genetic interferences.
C1 [Regimbeau, Mathilde; Mary, Romain; Hermetet, Francois; Girodon, Francois] Univ Bourgogne, Inserm U1231, F-21000 Dijon, France.
   [Mary, Romain] INSERM, Inst IMAGINE, U1163, F-75015 Paris, France.
   [Girodon, Francois] CHU Dijon, Serv Hematol Biol, Hop Bocage, F-21000 Dijon, France.
   [Girodon, Francois] Lab Excellence GR Ex Labex GR Ex, F-75015 Paris, France.
   [Girodon, Francois] France Intergrp Syndromes Myeloproliferatifs FIM, F-75010 Paris, France.
C3 Institut National de la Sante et de la Recherche Medicale (Inserm);
   Institut Agro; AgroSup Dijon; Universite de Bourgogne; Universite Paris
   Cite; Institut National de la Sante et de la Recherche Medicale
   (Inserm); CHU Dijon Bourgogne
RP Girodon, F (corresponding author), Univ Bourgogne, Inserm U1231, F-21000 Dijon, France.; Girodon, F (corresponding author), CHU Dijon, Serv Hematol Biol, Hop Bocage, F-21000 Dijon, France.; Girodon, F (corresponding author), Lab Excellence GR Ex Labex GR Ex, F-75015 Paris, France.; Girodon, F (corresponding author), France Intergrp Syndromes Myeloproliferatifs FIM, F-75010 Paris, France.
EM mathilde.regimbeau@gmail.com; romain.mary1@gmail.com;
   francois.hermetet@u-bourgogne.fr; francois.girodon@chu-dijon.fr
RI Hermetet, François/GPF-8614-2022
OI Hermetet, Francois/0000-0001-5549-1992; MARY, Romain/0000-0001-8876-7895
FU ANR (PRTS 2015 "GenRED"); labex GR-Ex [ANR-11-LABX-0051]
FX This study was supported by grants from the ANR (PRTS 2015 "GenRED");
   the labex GR-Ex. reference ANR-11-LABX-0051. The authors thank Suzanne
   RANKIN for the English revision.
CR Abdel-Wahab O, 2012, CANCER CELL, V22, P180, DOI 10.1016/j.ccr.2012.06.032
   Albiero E, 2008, BRIT J HAEMATOL, V142, P986, DOI 10.1111/j.1365-2141.2008.07180.x
   Aly M, 2019, BLOOD ADV, V3, P2164, DOI 10.1182/bloodadvances.2018028423
   An NF, 2018, BLOOD, V131, P2682, DOI 10.1182/blood-2017-10-810028
   Andrews NC, 1998, INT J BIOCHEM CELL B, V30, P429, DOI 10.1016/S1357-2725(97)00135-0
   Andrieux J, 2003, CANCER GENET CYTOGEN, V140, P118, DOI 10.1016/S0165-4608(02)00678-7
   Aral B, 2018, HAEMATOLOGICA, V103, pE372, DOI 10.3324/haematol.2018.188995
   Aranaz P, 2012, HAEMATOL-HEMATOL J, V97, P1234, DOI 10.3324/haematol.2011.052605
   Argetsinger LS, 2004, MOL CELL BIOL, V24, P4955, DOI 10.1128/MCB.24.11.4955-4967.2004
   Arteaga CL, 2014, CANCER CELL, V25, P282, DOI 10.1016/j.ccr.2014.02.025
   Bahar Burak, 2016, Leuk Res Rep, V6, P27
   Baxter EJ, 2005, LANCET, V365, P1054, DOI 10.1016/S0140-6736(05)71142-9
   Beer PA, 2010, BLOOD, V115, P2891, DOI 10.1182/blood-2009-08-236596
   Benati M, 2015, CLIN CHEM LAB MED, V53, P1005, DOI 10.1515/cclm-2014-0858
   Bergoug M, 2020, CELLS-BASEL, V9, DOI 10.3390/cells9112365
   BERK PD, 1986, SEMIN HEMATOL, V23, P132
   Bernardi M, 2009, AM J HEMATOL, V84, P258, DOI 10.1002/ajh.21357
   Bersenev A, 2008, J CLIN INVEST, V118, P2832, DOI 10.1172/JCI35808
   Bersenev A, 2010, J CLIN INVEST, V120, P2058, DOI 10.1172/JCI42032
   Birnbaum RA, 2000, MOL CELL, V5, P189, DOI 10.1016/S1097-2765(00)80415-3
   Boiocchi L, 2019, HUM PATHOL, V86, P1, DOI 10.1016/j.humpath.2018.11.022
   Bollag G, 1996, NAT GENET, V12, P144, DOI 10.1038/ng0296-144
   BOS JL, 1989, CANCER RES, V49, P4682
   Brecqueville M, 2012, GENE CHROMOSOME CANC, V51, P743, DOI 10.1002/gcc.21960
   Brooks SA, 2016, EXP HEMATOL, V44, P24, DOI 10.1016/j.exphem.2015.09.006
   Broséus J, 2014, BLOOD, V124, P3964, DOI 10.1182/blood-2014-06-583161
   Bruchova H, 2008, HAEMATOL-HEMATOL J, V93, P1009, DOI 10.3324/haematol.12706
   Bruchova H, 2007, EXP HEMATOL, V35, P1657, DOI 10.1016/j.exphem.2007.08.021
   Bruchova-Votavova H, 2010, LEUKEMIA LYMPHOMA, V51, P686, DOI 10.3109/10428191003629362
   Butcher CM, 2008, LEUKEMIA, V22, P870, DOI 10.1038/sj.leu.2404971
   Byun JM, 2019, ANTICANCER RES, V39, P6273, DOI 10.21873/anticanres.13837
   Campario H, 2020, LEUKEMIA, V34, P1210, DOI 10.1038/s41375-019-0636-0
   Campbell SL, 1998, ONCOGENE, V17, P1395, DOI 10.1038/sj.onc.1202174
   Carillo S, 2011, J MOL DIAGN, V13, P263, DOI 10.1016/j.jmoldx.2010.12.002
   Casolari DA, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-02655-7
   Cerquozzi S, 2015, BLOOD CANCER J, V5, DOI 10.1038/bcj.2015.95
   Chauveau A, 2017, HAEMATOLOGICA, V102, pE15, DOI 10.3324/haematol.2016.154799
   Chen Y, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0154183
   Chowdhury O, 2021, LEUKEMIA, V35, P1197, DOI 10.1038/s41375-020-0979-6
   Citri A, 2006, NAT REV MOL CELL BIO, V7, P505, DOI 10.1038/nrm1962
   Cleyrat C, 2010, LEUKEMIA, V24, P1069, DOI 10.1038/leu.2010.23
   Colaizzo D, 2007, BLOOD, V110, P2768, DOI 10.1182/blood-2007-05-092502
   Delhommeau F, 2009, NEW ENGL J MED, V360, P2289, DOI 10.1056/NEJMoa0810069
   Dinan AM, 2017, BIOL DIRECT, V12, DOI 10.1186/s13062-017-0195-0
   Ding Y, 2009, BLOOD, V114, P5201, DOI 10.1182/blood-2009-06-223982
   Donehower LA, 2019, CELL REP, V28, P1370, DOI 10.1016/j.celrep.2019.07.001
   Du TT, 2005, DEVELOPMENT, V132, P4645, DOI 10.1242/dev.02070
   Ernst T, 2010, NAT GENET, V42, P722, DOI 10.1038/ng.621
   Farnoud N, 2019, BLOOD, V134, DOI 10.1182/blood-2019-132014
   Feng YM, 2019, FRONT ONCOL, V9, DOI 10.3389/fonc.2019.00210
   Ferdowsi S, 2015, INT J LAB HEMATOL, V37, P661, DOI 10.1111/ijlh.12381
   Fisher CL, 2010, BLOOD, V115, P38, DOI 10.1182/blood-2009-07-230698
   Gebauer N, 2013, ACTA HAEMATOL-BASEL, V129, P251, DOI 10.1159/000345848
   Gery S, 2009, J LEUKOCYTE BIOL, V85, P957, DOI 10.1189/jlb.0908575
   Gill H, 2020, HEMATOLOGY, V25, P247, DOI 10.1080/16078454.2020.1780755
   Girardot M, 2010, BLOOD, V116, P437, DOI 10.1182/blood-2008-06-165985
   Goerttler PS, 2005, BRIT J HAEMATOL, V129, P138, DOI 10.1111/j.1365-2141.2005.05416.x
   Gold LI, 2010, FASEB J, V24, P665, DOI 10.1096/fj.09-145482
   Graubert TA, 2012, NAT GENET, V44, P53, DOI 10.1038/ng.1031
   Grinfeld J, 2018, NEW ENGL J MED, V379, P1416, DOI 10.1056/NEJMoa1716614
   Grinfeld J, 2017, HAEMATOLOGICA, V102, P7, DOI 10.3324/haematol.2014.113845
   Guglielmelli P, 2007, EXP HEMATOL, V35, P1708, DOI 10.1016/j.exphein.2007.08.020
   Guglielmelli P, 2020, AM J HEMATOL, V95, pE23, DOI 10.1002/ajh.25668
   Guglielmelli P, 2018, J CLIN ONCOL, V36, P310, DOI 10.1200/JCO.2017.76.4886
   Guglielmelli P, 2011, BLOOD, V118, P5227, DOI 10.1182/blood-2011-06-363424
   Harada H, 2004, BLOOD, V103, P2316, DOI 10.1182/blood-2003-09-3074
   Hirvonen EAM, 2017, HUM GENOMICS, V11, DOI 10.1186/s40246-017-0102-x
   Hock H, 2004, GENE DEV, V18, P2336, DOI 10.1101/gad.1239604
   Jäger R, 2010, HAEMATOL-HEMATOL J, V95, P526, DOI 10.3324/haematol.2009.019570
   James C, 2005, NATURE, V434, P1144, DOI 10.1038/nature03546
   Jovanovic JV, 2013, LEUKEMIA, V27, P2032, DOI 10.1038/leu.2013.219
   Jutzi JS, 2013, J EXP MED, V210, P1003, DOI 10.1084/jem.20120521
   Kahn JD, 2018, BLOOD, V132, P1095, DOI 10.1182/blood-2018-05-850339
   Kapralova K, 2014, BLOOD, V123, P391, DOI 10.1182/blood-2013-10-534222
   Kaufmann KB, 2012, J EXP MED, V209, P35, DOI 10.1084/jem.20110540
   Kelly LM, 2002, BLOOD, V99, P310, DOI 10.1182/blood.V99.1.310
   Klampfl T, 2013, NEW ENGL J MED, V369, P2379, DOI 10.1056/NEJMoa1311347
   Klampfl T, 2011, BLOOD, V118, P167, DOI 10.1182/blood-2011-01-331678
   Kleiblova P, 2013, J CELL BIOL, V201, P511, DOI 10.1083/jcb.201210031
   Kleppe M, 2015, CANCER DISCOV, V5, P316, DOI 10.1158/2159-8290.CD-14-0736
   Kouroupi E, 2008, BRIT J HAEMATOL, V142, P676, DOI 10.1111/j.1365-2141.2008.07223.x
   Kralovics R, 2005, NEW ENGL J MED, V352, P1779, DOI 10.1056/NEJMoa051113
   Kratz CP, 2006, LEUKEMIA, V20, P381, DOI 10.1038/sj.leu.2404060
   Kubesova B, 2018, LEUKEMIA, V32, P450, DOI 10.1038/leu.2017.230
   Langabeer SE, 2015, EUR J HAEMATOL, V95, P270, DOI 10.1111/ejh.12578
   Larsen TS, 2008, LEUKEMIA, V22, P194, DOI 10.1038/sj.leu.2404861
   Lasho TL, 2018, BLOOD ADV, V2, P370, DOI 10.1182/bloodadvances.2018015875
   Lebecque B, 2021, PEDIATR BLOOD CANCER, V68, DOI 10.1002/pbc.28816
   Lee TS, 2009, BMC STRUCT BIOL, V9, DOI 10.1186/1472-6807-9-58
   Levine RL, 2005, CANCER CELL, V7, P387, DOI 10.1016/j.ccr.2005.03.023
   Li S, 2008, BLOOD, V111, P3863, DOI 10.1182/blood-2007-09-111971
   Li Z, 2011, BLOOD, V118, P4509, DOI 10.1182/blood-2010-12-325241
   Lin P, 2006, AM J CLIN PATHOL, V126, P530, DOI 10.1309/JT5BE2L1FGG8P8Y6
   Link-Lenczowska D, 2018, ANN HEMATOL, V97, P2299, DOI 10.1007/s00277-018-3451-1
   Lippert E, 2006, BLOOD, V108, P1865, DOI 10.1182/blood-2006-01-013540
   Lippert E, 2009, HAEMATOL-HEMATOL J, V94, P38, DOI 10.3324/haematol.13486
   Loscocco GG, 2020, ONCOTARGETS THER, V13, P12367, DOI 10.2147/OTT.S287944
   Lundberg P, 2014, BLOOD, V123, P2220, DOI 10.1182/blood-2013-11-537167
   Luque Paz D, 2020, BLOOD ADV, V4, P4887, DOI 10.1182/bloodadvances.2020002271
   Ma WL, 2009, J MOL DIAGN, V11, P49, DOI 10.2353/jmoldx.2009.080114
   Makishima H, 2012, BLOOD, V119, P3203, DOI 10.1182/blood-2011-12-399774
   Makishima H, 2009, J CLIN ONCOL, V27, P6109, DOI 10.1200/JCO.2009.23.7503
   Mansier O, 2018, AM J HEMATOL, V93, pE84, DOI 10.1002/ajh.25014
   Marcellino BK, 2018, BLOOD ADV, V2, P3581, DOI 10.1182/bloodadvances.2018024018
   Martínez-Avilés L, 2007, HAEMATOLOGICA, V92, P1717, DOI 10.3324/haematol.12011
   Maslah N, 2017, LEUKEMIA, V31, P1661, DOI 10.1038/leu.2017.139
   McMullin MF, 2016, AM J HEMATOL, V91, P248, DOI 10.1002/ajh.24259
   Mikic TB, 2019, SCI REP-UK, V9, DOI 10.1038/s41598-019-56236-x
   Nakata Y, 2017, BLOOD, V129, P2148, DOI 10.1182/blood-2016-06-724658
   Nangalia J, 2017, HEMATOL-AM SOC HEMAT, P470, DOI 10.1182/asheducation-2017.1.470
   Nussenzveig RH, 2016, LEUKEMIA LYMPHOMA, V57, P1429, DOI 10.3109/10428194.2015.1091932
   Obeidi N, 2016, CELL J, V18
   Olcaydu D, 2009, LEUKEMIA, V23, P1924, DOI 10.1038/leu.2009.110
   Ortmann CA, 2015, NEW ENGL J MED, V372, P601, DOI 10.1056/NEJMoa1412098
   Panovska-Stavridis I, 2016, CL LYMPH MYELOM LEUK, V16, pE55, DOI 10.1016/j.clml.2016.02.039
   Pardanani A, 2007, LEUKEMIA, V21, P1960, DOI 10.1038/sj.leu.2404810
   Pardanani A, 2010, LEUKEMIA, V24, P1713, DOI 10.1038/leu.2010.163
   Pardanani A, 2010, LEUKEMIA, V24, P1146, DOI 10.1038/leu.2010.77
   Pardanani AD, 2006, BLOOD, V108, P3472, DOI 10.1182/blood-2006-04-018879
   Parikh C, 2007, CANCER RES, V67, P7139, DOI 10.1158/0008-5472.CAN-07-0778
   Passamonti F, 2006, BLOOD, V107, P3676, DOI 10.1182/blood-2005-09-3826
   Passamonti F, 2011, BLOOD, V117, P2813, DOI 10.1182/blood-2010-11-316810
   Percy MJ, 2007, HAEMATOLOGICA, V92, P1607, DOI 10.3324/haematol.11643
   Pietra D, 2008, BLOOD, V111, P1686, DOI 10.1182/blood-2007-07-101576
   Ramdzan ZM, 2014, NAT REV CANCER, V14, P673, DOI 10.1038/nrc3805
   Rao N, 2012, BRIT J HAEMATOL, V156, P268, DOI 10.1111/j.1365-2141.2011.08837.x
   Roller A, 2013, LEUKEMIA, V27, P1573, DOI 10.1038/leu.2013.65
   Rosnet O, 1996, LEUKEMIA, V10, P238
   ROSNET O, 1993, BLOOD, V82, P1110, DOI 10.1182/blood.V82.4.1110.bloodjournal8241110
   Rumi E, 2016, BLOOD, V128, P144, DOI 10.1182/blood-2016-04-711150
   Saez B, 2017, BLOOD, V129, P1260, DOI 10.1182/blood-2016-10-692400
   Sanada M, 2009, NATURE, V460, P904, DOI 10.1038/nature08240
   Santos FPS, 2020, LEUKEMIA, V34, P799, DOI 10.1038/s41375-019-0603-9
   Schnittger S, 2012, HAEMATOL-HEMATOL J, V97, P1890, DOI 10.3324/haematol.2012.065375
   Schnittger S, 2009, HAEMATOL-HEMATOL J, V94, P414, DOI 10.3324/haematol.13223
   Scott LM, 2007, NEW ENGL J MED, V356, P459, DOI 10.1056/NEJMoa065202
   Senin A, 2018, ANN HEMATOL, V97, P443, DOI 10.1007/s00277-017-3193-5
   Silver RT, 2011, LEUKEMIA RES, V35, P177, DOI 10.1016/j.leukres.2010.06.017
   Simon JA, 2008, MUTAT RES-FUND MOL M, V647, P21, DOI 10.1016/j.mrfmmm.2008.07.010
   Singh RK, 2012, TRENDS MOL MED, V18, P472, DOI 10.1016/j.molmed.2012.06.006
   Skoda RC, 2015, EXP HEMATOL, V43, P599, DOI 10.1016/j.exphem.2015.06.007
   Skov V, 2020, CANCERS, V12, DOI 10.3390/cancers12082194
   Stegelmann F, 2010, HAEMATOL-HEMATOL J, V95, P666, DOI 10.3324/haematol.2009.013623
   Stein BL, 2011, HAEMATOL-HEMATOL J, V96, P1462, DOI 10.3324/haematol.2011.045591
   Takaki S, 2002, J EXP MED, V195, P151, DOI 10.1084/jem.20011170
   Tan Y X, 2020, Zhonghua Xue Ye Xue Za Zhi, V41, P576, DOI 10.3760/cma.j.issn.0253-2727.2020.07.008
   Tefferi A, 2006, CANCER-AM CANCER SOC, V106, P631, DOI 10.1002/cncr.21645
   Tefferi A, 2010, LEUKEMIA, V24, P1302, DOI 10.1038/leu.2010.113
   Tefferi A, 2020, AM J HEMATOL, V95, P1599, DOI 10.1002/ajh.26008
   Tefferi A, 2020, BRIT J HAEMATOL, V189, P291, DOI 10.1111/bjh.16380
   Tefferi A, 2018, AM J HEMATOL, V93, P348, DOI 10.1002/ajh.24978
   Tefferi A, 2016, BLOOD ADV, V1, P105, DOI 10.1182/bloodadvances.2016000208
   Tefferi A, 2016, BLOOD ADV, V1, P21, DOI 10.1182/bloodadvances.2016000216
   Thoennissen NH, 2010, BLOOD, V115, P2882, DOI 10.1182/blood-2009-07-235119
   Tondeur S, 2021, LEUKEMIA, V35, P871, DOI 10.1038/s41375-020-0991-x
   Tong W, 2005, BLOOD, V105, P4604, DOI 10.1182/blood-2004-10-4093
   Tsuruta-Kishino T, 2017, ONCOGENE, V36, P3300, DOI 10.1038/onc.2016.478
   Vainchenker W, 2017, BLOOD, V129, P667, DOI 10.1182/blood-2016-10-695940
   Vainchenker W, 2011, BLOOD, V118, P1723, DOI 10.1182/blood-2011-02-292102
   Vannucchi AM, 2008, LEUKEMIA, V22, pCP5, DOI 10.1038/leu.2008.113
   Vannucchi AM, 2013, LEUKEMIA, V27, P1861, DOI 10.1038/leu.2013.119
   Vaquez H., 1892, CR SOC BIOL, V44, P384
   Velazquez L, 2002, J EXP MED, V195, P1599, DOI 10.1084/jem.20011883
   Viré E, 2006, NATURE, V439, P871, DOI 10.1038/nature04431
   Voice JK, 1999, J BIOL CHEM, V274, P17164, DOI 10.1074/jbc.274.24.17164
   Wang M, 2014, BIOMED RES INT-UK, V2014, DOI 10.1155/2014/485645
   Wang W, 2010, BLOOD, V116, P254, DOI 10.1182/blood-2009-11-254664
   Ward PS, 2010, CANCER CELL, V17, P225, DOI 10.1016/j.ccr.2010.01.020
   Warshawsky I, 2010, BLOOD, V115, P3175, DOI 10.1182/blood-2009-12-257501
   Williams DM, 2007, EXP HEMATOL, V35, P1641, DOI 10.1016/j.exphem.2007.08.010
   Wu J Y, 2020, Zhonghua Xue Ye Xue Za Zhi, V41, P989, DOI 10.3760/cma.j.issn.0253-2727.2020.12.004
   Yap YS, 2014, ONCOTARGET, V5, P5873, DOI 10.18632/oncotarget.2194
   Yarden Y, 2012, NAT REV CANCER, V12, P553, DOI 10.1038/nrc3309
   Zhan HC, 2013, BLOOD CELL MOL DIS, V50, P190, DOI 10.1016/j.bcmd.2012.11.009
   Zhan M, 2007, EXP HEMATOL, V35, P1015, DOI 10.1016/j.exphem.2007.03.014
   Zhang L, 2012, LEUKEMIA, V26, P2310, DOI 10.1038/leu.2012.137
   Zou HY, 2011, FEBS LETT, V585, P1007, DOI 10.1016/j.febslet.2011.02.032
NR 177
TC 15
Z9 16
U1 0
U2 5
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
EI 2073-4425
J9 GENES-BASEL
JI Genes
PD APR
PY 2022
VL 13
IS 4
AR 637
DI 10.3390/genes13040637
PG 29
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA 0Q9XK
UT WOS:000785261600001
PM 35456443
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Pascual-Le Tallec, L
   Lombès, M
AF Pascual-Le Tallec, L
   Lombès, M
TI The mineralocorticoid receptor:: A journey exploring its diversity and
   specificity of action
SO MOLECULAR ENDOCRINOLOGY
LA English
DT Review
ID GLUCOCORTICOID-INDUCED APOPTOSIS; MESSENGER-RIBONUCLEIC-ACID; ACTIVATED
   STAT PROTEINS; ANDROGEN RECEPTOR; SPLICE VARIANTS; TRANSCRIPTIONAL
   ACTIVATION; PROGESTERONE-RECEPTOR; ALTERNATIVE PROMOTERS;
   MOLECULAR-MECHANISMS; INHIBITORY FUNCTION
AB The mineralocorticoid receptor (MR) integrates hormonal signaling and activates the expression of aldosterone target genes, which control various physiological processes. In recent years, evidence has been provided for an important role of MR not only in the regulation of sodium and water homeostasis but also in cardiovascular function, neuronal fate, and adipocyte differentiation. MR belongs to the steroid receptor family that displays common mechanism of action. As a result, some apparent similarities with the glucocorticoid receptor (GR) have shaded MR's own specificities. The description of its gene structure, messenger isoforms, protein variants, functional domains, and posttranslational modifications ( phosphorylation, ubiquitinylation, sumoylation, acetylation) as well as a panel of interactions with coregulators, progressively depicted an original portrait of MR and shed light on its specific mechanism of action. In this review, after an overview of MR characteristics, the multiple levels of MR selectivity over other steroid receptors, in particular GR, will be described as well as the consequences for aldosterone-regulated gene expression.
C1 INSERM, Unite 693, Fac Med Paris Sud, F-94276 Le Kremlin Bicetre, France.
   NYU, Sch Med, Dept Microbiol, New York, NY 10016 USA.
C3 Institut National de la Sante et de la Recherche Medicale (Inserm);
   Universite Paris Saclay; New York University
RP INSERM, Unite 693, Fac Med Paris Sud, 63 Rue Gabriel Peri, F-94276 Le Kremlin Bicetre, France.
EM marc.lombes@kb.u-psud.fr
RI Lombes, Marc/L-5933-2018
CR Abdel-Hafiz H, 2002, J BIOL CHEM, V277, P33950, DOI 10.1074/jbc.M204573200
   ALNEMRI ES, 1991, J BIOL CHEM, V266, P18072
   ARRIZA JL, 1987, SCIENCE, V237, P268, DOI 10.1126/science.3037703
   Auboeuf D, 2002, SCIENCE, V298, P416, DOI 10.1126/science.1073734
   Auzou G, 2000, MOL PHARMACOL, V58, P684, DOI 10.1124/mol.58.4.684
   Bähr V, 2004, EUR J ENDOCRINOL, V151, P295, DOI 10.1530/eje.0.1510295
   Beggah AT, 2002, P NATL ACAD SCI USA, V99, P7160, DOI 10.1073/pnas.102673599
   Berger S, 1998, P NATL ACAD SCI USA, V95, P9424, DOI 10.1073/pnas.95.16.9424
   BINART N, 1991, P NATL ACAD SCI USA, V88, P10681, DOI 10.1073/pnas.88.23.10681
   Black BE, 2001, CURR BIOL, V11, P1749, DOI 10.1016/S0960-9822(01)00537-1
   BLOEM LJ, 1995, J STEROID BIOCHEM, V55, P159, DOI 10.1016/0960-0760(95)00162-S
   Chauchereau A, 2003, J BIOL CHEM, V278, P12335, DOI 10.1074/jbc.M207148200
   De Kloet ER, 1998, ENDOCR REV, V19, P269, DOI 10.1210/er.19.3.269
   Deroo BJ, 2002, MOL CELL BIOL, V22, P4113, DOI 10.1128/MCB.22.12.4113-4123.2002
   Desterro JMP, 1998, MOL CELL, V2, P233, DOI 10.1016/S1097-2765(00)80133-1
   Fagart J, 1998, EMBO J, V17, P3317, DOI 10.1093/emboj/17.12.3317
   Fan MY, 2002, MOL ENDOCRINOL, V16, P315, DOI 10.1210/me.16.2.315
   Farman N, 2001, AM J PHYSIOL-RENAL, V280, pF181, DOI 10.1152/ajprenal.2001.280.2.F181
   Freiman RN, 2003, CELL, V112, P11, DOI 10.1016/S0092-8674(02)01278-3
   Fu MF, 2004, BIOCHEM PHARMACOL, V68, P1199, DOI 10.1016/j.bcp.2004.05.037
   Fuse H, 2000, MOL ENDOCRINOL, V14, P889, DOI 10.1210/me.14.6.889
   Geller DS, 2000, SCIENCE, V289, P119, DOI 10.1126/science.289.5476.119
   Gross M, 2004, ONCOGENE, V23, P3059, DOI 10.1038/sj.onc.1207443
   Heery DM, 1997, NATURE, V387, P733, DOI 10.1038/42750
   Hellal-Levy C, 2000, MOL ENDOCRINOL, V14, P1210, DOI 10.1210/me.14.8.1210
   Hellal-Levy C, 2000, KIDNEY INT, V57, P1250, DOI 10.1046/j.1523-1755.2000.00958.x
   Hittelman AB, 1999, EMBO J, V18, P5380, DOI 10.1093/emboj/18.19.5380
   HOLLENBERG SM, 1988, CELL, V55, P899, DOI 10.1016/0092-8674(88)90145-6
   Hovland AR, 1998, J BIOL CHEM, V273, P5455, DOI 10.1074/jbc.273.10.5455
   Hu X, 1999, NATURE, V402, P93, DOI 10.1038/47069
   Iñiguez-Lluhí JA, 2000, MOL CELL BIOL, V20, P6040, DOI 10.1128/MCB.20.16.6040-6050.2000
   Ismaili N, 2004, ANN NY ACAD SCI, V1024, P86, DOI 10.1196/annals.1321.007
   JENSTER G, 1995, J BIOL CHEM, V270, P7341, DOI 10.1074/jbc.270.13.7341
   Jiménez-Lara AM, 2002, FEBS LETT, V526, P142, DOI 10.1016/S0014-5793(02)03154-X
   Kitagawa H, 2002, MOL CELL BIOL, V22, P3698, DOI 10.1128/MCB.22.11.3698-3706.2002
   Kotaja N, 2000, MOL ENDOCRINOL, V14, P1986, DOI 10.1210/me.14.12.1986
   Kotaja N, 2002, MOL CELL BIOL, V22, P5222, DOI 10.1128/MCB.22.14.5222-5234.2002
   Kressler D, 2002, J BIOL CHEM, V277, P13918, DOI 10.1074/jbc.M201134200
   KWAK SP, 1993, ENDOCRINOLOGY, V133, P2344, DOI 10.1210/en.133.5.2344
   Le Menuet D, 2000, J BIOL CHEM, V275, P7878, DOI 10.1074/jbc.275.11.7878
   Le Menuet D, 2001, J BIOL CHEM, V276, P38911, DOI 10.1074/jbc.M103984200
   Le Moëllic C, 2004, J AM SOC NEPHROL, V15, P1145
   Lifton RP, 2001, CELL, V104, P545, DOI 10.1016/S0092-8674(01)00241-0
   Lin DY, 2004, MOL CELL BIOL, V24, P10529, DOI 10.1128/MCB.24.24.10529-10541.2004
   Liu WH, 1995, P NATL ACAD SCI USA, V92, P12480, DOI 10.1073/pnas.92.26.12480
   LOMBES M, 1994, BIOCHEM J, V302, P191, DOI 10.1042/bj3020191
   LOMBES M, 1994, ENDOCRINOLOGY, V135, P834, DOI 10.1210/en.135.3.834
   Margueron R, 2004, BIOCHEM PHARMACOL, V68, P1239, DOI 10.1016/j.bcp.2004.04.031
   Marissal-Arvy N, 2004, EXP PHYSIOL, V89, P753, DOI 10.1113/expphysiol.2004.028621
   Marissal-Arvy N, 2004, J BIOL CHEM, V279, P39232, DOI 10.1074/jbc.M407436200
   Massaad C, 1999, MOL ENDOCRINOL, V13, P57, DOI 10.1210/me.13.1.57
   McKenna NJ, 1999, ENDOCR REV, V20, P321, DOI 10.1210/er.20.3.321
   Meijer OC, 2005, ENDOCRINOLOGY, V146, P1438, DOI 10.1210/en.2004-0411
   Métivier R, 2003, CELL, V115, P751, DOI 10.1016/S0092-8674(03)00934-6
   Moilanen AM, 1999, J BIOL CHEM, V274, P3700, DOI 10.1074/jbc.274.6.3700
   MORRISON N, 1990, HUM GENET, V85, P130
   Nishi M, 2001, MOL ENDOCRINOL, V15, P1077, DOI 10.1210/me.15.7.1077
   Nishida T, 2002, J BIOL CHEM, V277, P41311, DOI 10.1074/jbc.M206741200
   Obradovic D, 2004, MOL PHARMACOL, V65, P761, DOI 10.1124/mol.65.3.761
   Pascual-Le Tallec L, 2005, MOL ENDOCRINOL, V19, P1158, DOI 10.1210/me.2004-0331
   Pascual-Le Tallec L, 2003, MOL ENDOCRINOL, V17, P2529, DOI 10.1210/me.2003-0299
   PATEL PD, 1989, MOL ENDOCRINOL, V3, P1877, DOI 10.1210/mend-3-11-1877
   Pearce D, 2003, VITAM HORM, V66, P29, DOI 10.1016/S0083-6729(03)01002-1
   PEARCE D, 1993, SCIENCE, V259, P1161, DOI 10.1126/science.8382376
   Pitt B, 2004, MOL CELL ENDOCRINOL, V217, P53, DOI 10.1016/j.mce.2003.10.009
   Planey SL, 2002, J BIOL CHEM, V277, P42188, DOI 10.1074/jbc.M205085200
   Planey SL, 2000, BIOCHEM BIOPH RES CO, V279, P307, DOI 10.1006/bbrc.2000.3922
   Poukka H, 2000, P NATL ACAD SCI USA, V97, P14145, DOI 10.1073/pnas.97.26.14145
   Pratt WB, 1997, ENDOCR REV, V18, P306, DOI 10.1210/er.18.3.306
   Privalsky ML, 2004, ANNU REV PHYSIOL, V66, P315, DOI 10.1146/annurev.physiol.66.032802.155556
   Rafestin-Oblin ME, 2003, ENDOCRINOLOGY, V144, P528, DOI 10.1210/en.2002-220708
   Rogerson FM, 2004, MOL CELL ENDOCRINOL, V217, P203, DOI 10.1016/j.mce.2003.10.021
   Rogerson FM, 2003, MOL CELL ENDOCRINOL, V200, P45, DOI 10.1016/S0303-7207(02)00413-6
   Rogerson FM, 1999, J BIOL CHEM, V274, P36305, DOI 10.1074/jbc.274.51.36305
   RUPPRECHT R, 1993, MOL ENDOCRINOL, V7, P597, DOI 10.1210/me.7.4.597
   Sartorato P, 2004, MOL ENDOCRINOL, V18, P2151, DOI 10.1210/me.2003-0408
   Savory JGA, 1999, MOL CELL BIOL, V19, P1025
   Savory JGA, 2001, MOL CELL BIOL, V21, P781, DOI 10.1128/MCB.21.3.781-793.2001
   Schulz M, 2002, J BIOL CHEM, V277, P26238, DOI 10.1074/jbc.M203268200
   Seeler JS, 2003, NAT REV MOL CELL BIO, V4, P690, DOI 10.1038/nrm1200
   Shilatifard A, 1996, SCIENCE, V271, P1873, DOI 10.1126/science.271.5257.1873
   Shilatifard A, 1997, J BIOL CHEM, V272, P22355, DOI 10.1074/jbc.272.35.22355
   Sim RJ, 2004, GENE DEV, V18, P2437, DOI 10.1101/gad.1235904
   Stockand JD, 2002, AM J PHYSIOL-RENAL, V282, pF559, DOI 10.1152/ajprenal.00320.2001
   Sturm A, 2005, ENDOCRINOLOGY, V146, P47, DOI 10.1210/en.2004-0128
   Tajima T, 2000, J CLIN ENDOCR METAB, V85, P4690, DOI 10.1210/jc.85.12.4690
   Tallec LPL, 2004, EUR J ENDOCRINOL, V150, P585, DOI 10.1530/eje.0.1500585
   Tan JA, 2000, MOL ENDOCRINOL, V14, P14, DOI 10.1210/me.14.1.14
   Thomas M, 2004, J BIOL CHEM, V279, P8389, DOI 10.1074/jbc.M311761200
   Tirard M, 2004, J MOL ENDOCRINOL, V32, P825, DOI 10.1677/jme.0.0320825
   TSAI MJ, 1994, ANNU REV BIOCHEM, V63, P451, DOI 10.1146/annurev.bi.63.070194.002315
   Wallace AD, 2001, J BIOL CHEM, V276, P42714, DOI 10.1074/jbc.M106033200
   Wang Q, 2004, J STEROID BIOCHEM, V91, P197, DOI 10.1016/j.jsbmb.2004.04.007
   White PC, 1997, ENDOCR REV, V18, P135, DOI 10.1210/er.18.1.135
   Wickert L, 2000, J NEUROENDOCRINOL, V12, P867, DOI 10.1046/j.1365-2826.2000.00535.x
   Yudt MR, 2002, MOL ENDOCRINOL, V16, P1719, DOI 10.1210/me.2002-0106
   Yudt MR, 2001, MOL ENDOCRINOL, V15, P1093, DOI 10.1210/me.15.7.1093
   Zennaro MC, 2004, TRENDS ENDOCRIN MET, V15, P264, DOI 10.1016/j.tem.2004.06.003
   Zennaro MC, 1998, J CLIN INVEST, V101, P1254, DOI 10.1172/JCI1915
   ZENNARO MC, 1995, J BIOL CHEM, V270, P21016, DOI 10.1074/jbc.270.36.21016
   Zennaro MC, 2001, MOL ENDOCRINOL, V15, P1586, DOI 10.1210/me.15.9.1586
   Zennaro MC, 1997, J CLIN ENDOCR METAB, V82, P1345, DOI 10.1210/jc.82.5.1345
   Zennaro MC, 1996, MOL ENDOCRINOL, V10, P1549, DOI 10.1210/me.10.12.1549
   Zhou K, 2003, NUCLEIC ACIDS RES, V31, P2253, DOI 10.1093/nar/gkg328
   Zhou MY, 2000, MOL CELL ENDOCRINOL, V159, P125, DOI 10.1016/S0303-7207(99)00198-7
NR 105
TC 181
Z9 203
U1 0
U2 6
PU OXFORD UNIV PRESS INC
PI CARY
PA JOURNALS DEPT, 2001 EVANS RD, CARY, NC 27513 USA
SN 0888-8809
EI 1944-9917
J9 MOL ENDOCRINOL
JI Mol. Endocrinol.
PD SEP
PY 2005
VL 19
IS 9
BP 2211
EP 2221
DI 10.1210/me.2005-0089
PG 11
WC Endocrinology & Metabolism
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism
GA 958MY
UT WOS:000231453600001
PM 15802372
DA 2025-04-10
ER

PT J
AU Thevenon, D
   Smida-Rezgui, S
   Chevessier, F
   Groh, S
   Henry-Berger, J
   Romero, NB
   Villaz, M
   DeWaard, M
   Marty, I
AF Thevenon, D
   Smida-Rezgui, S
   Chevessier, F
   Groh, S
   Henry-Berger, J
   Romero, NB
   Villaz, M
   DeWaard, M
   Marty, I
TI Human skeletal muscle triadin: gene organization and cloning of the
   major isoform, Trisk 51
SO BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
LA English
DT Article
DE triadin; excitation-contraction coupling; ryanodine receptor;
   dihydropyridine receptor; calsequestrin; calcium release complex
ID CENTRAL CORE DISEASE; SARCOPLASMIC-RETICULUM MEMBRANE; JUNCTIONAL FOOT
   PROTEIN; RYANODINE RECEPTOR; MALIGNANT-HYPERTHERMIA; MOLECULAR-CLONING;
   DIHYDROPYRIDINE RECEPTOR; CALCIUM-CHANNEL; CARDIAC TRIADIN;
   CALSEQUESTRIN
AB We obtained the gene organization of human triadin gene by aligning the, DNA coding sequence of human 95-kDa triadin (Trisk 95) with human genomic database. We identified a novel human triadin isoform., a potential human homologue of rat Trisk 51. We show that both isoforms of triadin, Trisk 51 and Trisk 95, are alternative splice variants of the same gene. We demonstrated experimentally the existence of this Trisk 51 transcript in human skeletal muscle and cloned its full length cDNA. We further demonstrated that the protein encoded by this transcript is expressed in the human skeletal muscle. In addition, unlike other species, Trisk 51 is the major triadin isoform expressed in human skeletal muscle, whereas Trisk 95 is below the detection level in the two types of muscles tested. (C) 2003 Elsevier Science (USA). All rights reserved.
C1 CEA, DRDC, INSERM EMI 9931, Lab Canaux Ion & Signalisat, F-38054 Grenoble, France.
   Hop La Pitie Salpetriere, INSERM U523, Inst Myol, F-75651 Paris 13, France.
   CNRS, UMR 6547, F-63177 Aubiere, France.
C3 Institut National de la Sante et de la Recherche Medicale (Inserm); CEA;
   Institut National de la Sante et de la Recherche Medicale (Inserm);
   Assistance Publique Hopitaux Paris (APHP); Hopital Universitaire
   Pitie-Salpetriere - APHP; Sorbonne Universite; Centre National de la
   Recherche Scientifique (CNRS)
RP CEA, DRDC, INSERM EMI 9931, Lab Canaux Ion & Signalisat, 17 Rue Martyrs, F-38054 Grenoble, France.
EM imarty@cea.fr
RI Marty, Isabelle/N-7114-2017; De Waard, Michel/G-7406-2014
OI De Waard, Michel/0000-0002-2782-9615; Marty,
   Isabelle/0000-0003-3625-913X
CR Altschul SF, 1997, NUCLEIC ACIDS RES, V25, P3389, DOI 10.1093/nar/25.17.3389
   Avila G, 2001, P NATL ACAD SCI USA, V98, P4215, DOI 10.1073/pnas.071048198
   BRANDT NR, 1990, J MEMBRANE BIOL, V113, P237, DOI 10.1007/BF01870075
   Caswell AH, 1999, BIOCHEMISTRY-US, V38, P90, DOI 10.1021/bi981306+
   CASWELL AH, 1991, BIOCHEMISTRY-US, V30, P7507, DOI 10.1021/bi00244a020
   CHAUDHARI N, 1993, DEV BIOL, V155, P507, DOI 10.1006/dbio.1993.1048
   Groh S, 1999, J BIOL CHEM, V274, P12278, DOI 10.1074/jbc.274.18.12278
   Guo W, 1996, J BIOL CHEM, V271, P458, DOI 10.1074/jbc.271.1.458
   GUO W, 1995, J BIOL CHEM, V270, P9027, DOI 10.1074/jbc.270.16.9027
   Hong CS, 2001, GENE, V278, P193, DOI 10.1016/S0378-1119(01)00718-1
   KIM KC, 1990, BIOCHEMISTRY-US, V29, P9281, DOI 10.1021/bi00491a025
   KNUDSON CM, 1993, J BIOL CHEM, V268, P12646
   Kobayashi YM, 2000, J BIOL CHEM, V275, P17639, DOI 10.1074/jbc.M002091200
   Kobayashi YM, 1999, J BIOL CHEM, V274, P28660, DOI 10.1074/jbc.274.40.28660
   Lee HG, 2001, J BIOL CHEM, V276, P39533, DOI 10.1074/jbc.M010664200
   Louis CF, 2001, BIOSCIENCE REP, V21, P155, DOI 10.1023/A:1013644107519
   MacLennan DH, 2000, EUR J BIOCHEM, V267, P5291, DOI 10.1046/j.1432-1327.2000.01566.x
   MARTY I, 1995, BIOCHEM J, V307, P769, DOI 10.1042/bj3070769
   Marty I, 2000, J BIOL CHEM, V275, P8206, DOI 10.1074/jbc.275.11.8206
   McCarthy TV, 2000, HUM MUTAT, V15, P410, DOI 10.1002/(SICI)1098-1004(200005)15:5<410::AID-HUMU2>3.0.CO;2-D
   Monnier N, 2001, HUM MOL GENET, V10, P2581, DOI 10.1093/hmg/10.22.2581
   Monnier N, 1997, AM J HUM GENET, V60, P1316, DOI 10.1086/515454
   Ohkura M, 1998, BIOCHEMISTRY-US, V37, P12987, DOI 10.1021/bi972803d
   PENG M, 1994, FEBS LETT, V348, P17, DOI 10.1016/0014-5793(94)00556-7
   Shin DW, 2000, FEBS LETT, V486, P178, DOI 10.1016/S0014-5793(00)02246-8
   Tarroni P, 1997, J BIOL CHEM, V272, P19808, DOI 10.1074/jbc.272.32.19808
   TASKE NL, 1995, EUR J BIOCHEM, V233, P258, DOI 10.1111/j.1432-1033.1995.258_1.x
   Tilgen N, 2001, HUM MOL GENET, V10, P2879, DOI 10.1093/hmg/10.25.2879
   Tong JF, 1999, J BIOL CHEM, V274, P693, DOI 10.1074/jbc.274.2.693
   Zhang L, 1997, J BIOL CHEM, V272, P23389, DOI 10.1074/jbc.272.37.23389
NR 30
TC 30
Z9 34
U1 0
U2 1
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0006-291X
EI 1090-2104
J9 BIOCHEM BIOPH RES CO
JI Biochem. Biophys. Res. Commun.
PD APR 4
PY 2003
VL 303
IS 2
BP 669
EP 675
DI 10.1016/S0006-291X(03)00406-6
PG 7
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA 666LB
UT WOS:000182177800043
PM 12659871
DA 2025-04-10
ER

PT J
AU Zhang, XJ
   Hamblin, MH
   Yin, KJ
AF Zhang, Xuejing
   Hamblin, Milton H.
   Yin, Ke-Jie
TI The long noncoding RNA Malat1: Its physiological and pathophysiological
   functions
SO RNA BIOLOGY
LA English
DT Review
DE Long noncoding RNA; Malat1; cancer; neurologic disorder; stroke;
   cardiovascular disease
ID CELL LUNG-CANCER; RESISTANT PROSTATE-CANCER; COMPETING ENDOGENOUS RNA;
   ADENOCARCINOMA TRANSCRIPT 1; LNCRNA MALAT1; COLORECTAL-CANCER;
   BREAST-CANCER; UP-REGULATION; TRIPLE-HELIX; PROGNOSTIC-FACTOR
AB Recent studies suggest that in humans, DNA sequences responsible for protein coding regions comprise only 2% of the total genome. The rest of the transcripts result in RNA transcripts without protein-coding ability, including long noncoding RNAs (lncRNAs). Different from most members in the lncRNA family, the metastasis-associated lung adenocarcinoma transcript 1 (Malat1) is abundantly expressed and evolutionarily conserved throughout various mammalian species. Malat1 is one of the first identified lncRNAs associated with human disease, and cumulative studies have indicated that Malat1 plays critical roles in the development and progression of various cancers. Malat1 is also actively involved in various physiologic processes, including alternative splicing, epigenetic modification of gene expression, synapse formation, and myogenesis. Furthermore, extensive evidences show that Malat1 plays pivotal roles in multiple pathological conditions as well. In this review, we will summarize latest findings related to the physiologic and pathophysiological processes of Malat1 and discuss its therapeutic potentials.
C1 [Zhang, Xuejing; Yin, Ke-Jie] Univ Pittsburgh, Sch Med, Dept Neurol, Pittsburgh Inst Brain Disorders & Recovery, S518 BST,200 Lothrop St, Pittsburgh, PA 15213 USA.
   [Hamblin, Milton H.] Tulane Univ, Sch Med, Dept Pharmacol, New Orleans, LA 70112 USA.
C3 Pennsylvania Commonwealth System of Higher Education (PCSHE); University
   of Pittsburgh; Tulane University
RP Yin, KJ (corresponding author), Univ Pittsburgh, Sch Med, Dept Neurol, Pittsburgh Inst Brain Disorders & Recovery, S518 BST,200 Lothrop St, Pittsburgh, PA 15213 USA.
EM yink2@upmc.edu
RI Zhang, Xuejing/J-8857-2018
OI Zhang, Xuejing/0000-0003-2994-5502
FU National Institute of Health [NS094930, NS091175, NS086820]
FX This work was supported by the National Institute of Health Grants:
   NS094930, NS091175, NS086820 (K.J. Yin). The authors declare no
   competing financial interests.
CR Allen DL, 2011, MED SCI SPORT EXER, V43, P1828, DOI 10.1249/MSS.0b013e3182178bb4
   Argani P, 2012, AM J SURG PATHOL, V36, P1516, DOI 10.1097/PAS.0b013e3182613d8f
   Arun G, 2016, GENE DEV, V30, P34, DOI 10.1101/gad.270959.115
   Baker ML, 2008, STROKE, V39, P1371, DOI 10.1161/STROKEAHA.107.496091
   Barres BA, 2008, NEURON, V60, P430, DOI 10.1016/j.neuron.2008.10.013
   Bartel DP, 2009, CELL, V136, P215, DOI 10.1016/j.cell.2009.01.002
   Bennett MC, 2005, PHARMACOL THERAPEUT, V105, P311, DOI 10.1016/j.pharmthera.2004.10.010
   Bernard D, 2010, EMBO J, V29, P3082, DOI 10.1038/emboj.2010.199
   Blencowe BJ, 2006, CELL, V126, P37, DOI 10.1016/j.cell.2006.06.023
   Brown JA, 2016, P NATL ACAD SCI USA, V113, P14013, DOI 10.1073/pnas.1614759113
   Brown JA, 2016, RNA, V22, P743, DOI 10.1261/rna.055707.115
   Brown JA, 2014, NAT STRUCT MOL BIOL, V21, P633, DOI 10.1038/nsmb.2844
   Cech TR, 2014, CELL, V157, P77, DOI 10.1016/j.cell.2014.03.008
   Cesana M, 2011, CELL, V147, P358, DOI 10.1016/j.cell.2011.09.028
   Chaudhry MA, 2013, INT J MOL SCI, V14, P9099, DOI 10.3390/ijms14059099
   Cho SF, 2014, BMC CANCER, V14, DOI 10.1186/1471-2407-14-809
   Clark MB, 2012, GENOME RES, V22, P885, DOI 10.1101/gr.131037.111
   Clemson CM, 2009, MOL CELL, V33, P717, DOI 10.1016/j.molcel.2009.01.026
   Davis IJ, 2003, P NATL ACAD SCI USA, V100, P6051, DOI 10.1073/pnas.0931430100
   Eissmann M, 2012, RNA BIOL, V9, P1076, DOI 10.4161/rna.21089
   Ellis MJ, 2012, NATURE, V486, P353, DOI 10.1038/nature11143
   Engreitz JM, 2014, CELL, V159, P188, DOI 10.1016/j.cell.2014.08.018
   Fan Y, 2014, CLIN CANCER RES, V20, P1531, DOI 10.1158/1078-0432.CCR-13-1455
   Fang DF, 2015, BIOCHEM BIOPH RES CO, V457, P500, DOI 10.1016/j.bbrc.2014.12.114
   Gibbs RA, 2004, NATURE, V428, P493, DOI 10.1038/nature02426
   Grote P, 2015, TRENDS GENET, V31, P329, DOI 10.1016/j.tig.2015.02.002
   Guffanti A, 2009, BMC GENOMICS, V10, DOI 10.1186/1471-2164-10-163
   Guo FJ, 2010, ACTA BIOCH BIOPH SIN, V42, P224, DOI 10.1093/abbs/gmq008
   Gutschner T, 2013, J MOL MED, V91, P791, DOI 10.1007/s00109-013-1028-y
   Gutschner T, 2013, CANCER RES, V73, P1180, DOI 10.1158/0008-5472.CAN-12-2850
   Gutschner T, 2011, GENOME RES, V21, P1944, DOI 10.1101/gr.122358.111
   Han XR, 2015, FASEB J, V29, P3054, DOI 10.1096/fj.14-259952
   Han YH, 2013, FEBS LETT, V587, P3875, DOI 10.1016/j.febslet.2013.10.023
   Han YH, 2013, UROLOGY, V81, DOI 10.1016/j.urology.2012.08.044
   Hirata H, 2015, CANCER RES, V75, P1322, DOI 10.1158/0008-5472.CAN-14-2931
   Hu LW, 2015, J EXP CLIN CANC RES, V34, DOI 10.1186/s13046-015-0123-z
   Hübner MR, 2010, ANNU REV BIOPHYS, V39, P471, DOI 10.1146/annurev.biophys.093008.131348
   Hutchinson JN, 2007, BMC GENOMICS, V8, DOI 10.1186/1471-2164-8-39
   Hüttenhofer A, 2005, TRENDS GENET, V21, P289, DOI 10.1016/j.tig.2005.03.007
   Isin M, 2014, CLIN CHIM ACTA, V431, P255, DOI 10.1016/j.cca.2014.02.010
   Iyer MK, 2015, NAT GENET, V47, P199, DOI 10.1038/ng.3192
   Ji P, 2003, ONCOGENE, V22, P8031, DOI 10.1038/sj.onc.1206928
   Ji Q, 2014, BRIT J CANCER, V111, P736, DOI 10.1038/bjc.2014.383
   Ji Q, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0078700
   Jiang Y, 2014, ONCOL LETT, V7, P2135, DOI 10.3892/ol.2014.1996
   Joulia D, 2003, EXP CELL RES, V286, P263, DOI 10.1016/S0014-4827(03)00074-0
   Kandoth C, 2013, NATURE, V502, P333, DOI 10.1038/nature12634
   Kanduri C, 2016, BBA-GENE REGUL MECH, V1859, P102, DOI 10.1016/j.bbagrm.2015.05.006
   Kayaci S, 2014, NEUROL MED-CHIR, V54, P363, DOI 10.2176/nmc.oa.2013-0147
   Koshimizu T, 2010, LIFE SCI, V86, P455, DOI 10.1016/j.lfs.2010.02.001
   Kryger R, 2012, ALCOHOL, V46, P629, DOI 10.1016/j.alcohol.2012.04.002
   Kuiper RP, 2003, HUM MOL GENET, V12, P1661, DOI 10.1093/hmg/ddg178
   Kuo IY, 2014, INT J CANCER, V135, P563, DOI 10.1002/ijc.28695
   Leucci E, 2013, SCI REP-UK, V3, DOI 10.1038/srep02535
   Li BZ, 2014, J BIOL CHEM, V289, P29365, DOI 10.1074/jbc.M114.572693
   Li L, 2009, P NATL ACAD SCI USA, V106, P12956, DOI 10.1073/pnas.0906005106
   Li ZY, 2015, PITUITARY, V18, P42, DOI 10.1007/s11102-014-0554-0
   Lin R, 2007, ONCOGENE, V26, P851, DOI 10.1038/sj.onc.1209846
   Lin R, 2011, FEBS LETT, V585, P671, DOI 10.1016/j.febslet.2011.01.030
   Lipovich L, 2012, GENETICS, V192, P1133, DOI 10.1534/genetics.112.145128
   Liu JY, 2014, CELL DEATH DIS, V5, DOI 10.1038/cddis.2014.466
   Liu JH, 2017, FRONT BIOSCI-LANDMRK, V22, P66, DOI 10.2741/4472
   Liu N, 2015, NATURE, V518, P560, DOI 10.1038/nature14234
   Liu WT, 2014, WORLD J GASTROENTERO, V20, P6314, DOI 10.3748/wjg.v20.i20.6314
   Liu Y, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0035145
   Liu YK, 2013, BMC MOL BIOL, V14, DOI 10.1186/1471-2199-14-7
   Lopez-Ayllon BD, 2014, CANCER MED-US, V3, P1099, DOI 10.1002/cam4.291
   Lu L, 2015, TOXICOL APPL PHARM, V289, P276, DOI 10.1016/j.taap.2015.09.016
   Luo JH, 2006, HEPATOLOGY, V44, P1012, DOI 10.1002/hep.21328
   Ma J, 2016, BBA-GENE REGUL MECH, V1859, P324, DOI 10.1016/j.bbagrm.2015.11.008
   Macias S, 2012, NAT STRUCT MOL BIOL, V19, P760, DOI 10.1038/nsmb.2344
   Mehta SL, 2015, J NEUROSCI, V35, P16443, DOI 10.1523/JNEUROSCI.2943-15.2015
   Menon DU, 2015, RNA BIOL, V12, P1088, DOI 10.1080/15476286.2015.1086864
   Mercer TR, 2009, NAT REV GENET, V10, P155, DOI 10.1038/nrg2521
   Michalik KM, 2014, CIRC RES, V114, P1389, DOI 10.1161/CIRCRESAHA.114.303265
   Miyagawa R, 2012, RNA, V18, P738, DOI 10.1261/rna.028639.111
   Mohamadkhani A, 2014, HEPAT MON, V14, DOI 10.5812/hepatmon.18794
   Nagano T, 2011, CELL, V145, P178, DOI 10.1016/j.cell.2011.03.014
   Nakagawa S, 2012, RNA, V18, P1487, DOI 10.1261/rna.033217.112
   Nik-Zainal S, 2016, NATURE, V534, P47, DOI 10.1038/nature17676
   Okugawa Y, 2014, CARCINOGENESIS, V35, P2731, DOI 10.1093/carcin/bgu200
   Poliseno L, 2010, NATURE, V465, P1033, DOI 10.1038/nature09144
   Ponting CP, 2009, CELL, V136, P629, DOI 10.1016/j.cell.2009.02.006
   Puthanveetil P, 2015, J CELL MOL MED, V19, P1418, DOI 10.1111/jcmm.12576
   Rajaram V, 2007, GENE CHROMOSOME CANC, V46, P508, DOI 10.1002/gcc.20437
   Ren SC, 2013, J UROLOGY, V190, P2278, DOI 10.1016/j.juro.2013.07.001
   Salmena L, 2011, CELL, V146, P353, DOI 10.1016/j.cell.2011.07.014
   Sarver AL, 2012, BIOINFORMATION, V8, P731, DOI 10.6026/97320630008731
   Schmidt LH, 2011, J THORAC ONCOL, V6, P1984, DOI 10.1097/JTO.0b013e3182307eac
   Shen J, 2015, CANCERS, V7, P1847, DOI 10.3390/cancers7030865
   Shi XF, 2015, TUMOR BIOL, V36, P503, DOI 10.1007/s13277-015-3106-y
   Simon MD, 2011, P NATL ACAD SCI USA, V108, P20497, DOI 10.1073/pnas.1113536108
   Sowalsky AG, 2015, MOL CANCER RES, V13, P98, DOI 10.1158/1541-7786.MCR-14-0273
   Spector DL, 2011, CSH PERSPECT BIOL, V3, DOI 10.1101/cshperspect.a000646
   STEWARD O, 1991, J COMP NEUROL, V314, P545, DOI 10.1002/cne.903140311
   Tani H, 2012, GENOME RES, V22, P947, DOI 10.1101/gr.130559.111
   Tani H, 2010, DRUG DISCOV THER, V4, P235
   Taniguchi M, 2014, FEBS OPEN BIO, V4, P328, DOI 10.1016/j.fob.2014.03.004
   Tano K, 2010, FEBS LETT, V584, P4575, DOI 10.1016/j.febslet.2010.10.008
   Tee AE, 2014, ONCOTARGET, V5, P1793, DOI 10.18632/oncotarget.1785
   Tripathi V, 2013, PLOS GENET, V9, DOI 10.1371/journal.pgen.1003368
   Tripathi V, 2010, MOL CELL, V39, P925, DOI 10.1016/j.molcel.2010.08.011
   Tseng JJ, 2009, MOL HUM REPROD, V15, P725, DOI 10.1093/molehr/gap071
   Vausort M, 2014, CIRC RES, V115, P668, DOI 10.1161/CIRCRESAHA.115.303836
   Wang DJ, 2015, ONCOTARGET, V6, P41045, DOI 10.18632/oncotarget.5728
   Wang FB, 2014, ONCOTARGET, V5, P11091, DOI 10.18632/oncotarget.2691
   Wang XY, 2015, J BIOL CHEM, V290, P3925, DOI 10.1074/jbc.M114.596866
   Watts R, 2013, AM J PHYSIOL-CELL PH, V304, pC995, DOI 10.1152/ajpcell.00392.2012
   Weber Daniel Gilbert, 2013, BMC Res Notes, V6, P518, DOI 10.1186/1756-0500-6-518
   West JA, 2014, MOL CELL, V55, P791, DOI 10.1016/j.molcel.2014.07.012
   Wheeler TM, 2012, NATURE, V488, P111, DOI 10.1038/nature11362
   Wilusz JE, 2016, BBA-GENE REGUL MECH, V1859, P128, DOI 10.1016/j.bbagrm.2015.06.003
   Wilusz JE, 2008, CELL, V135, P919, DOI 10.1016/j.cell.2008.10.012
   Wu YT, 2015, CURR PHARM DESIGN, V21, P5017, DOI 10.2174/1381612821666150724115625
   Xiao HB, 2015, ONCOTARGET, V6, P38005, DOI 10.18632/oncotarget.5357
   Xie CY, 2014, NUCLEIC ACIDS RES, V42, pD98, DOI 10.1093/nar/gkt1222
   Xu CA, 2011, INT J ONCOL, V39, P169, DOI 10.3892/ijo.2011.1007
   Xu YT, 2012, PHARMACOL BIOCHEM BE, V101, P174, DOI 10.1016/j.pbb.2011.12.016
   Yan B, 2014, INVEST OPHTH VIS SCI, V55, P941, DOI 10.1167/iovs.13-13221
   Yang F, 2013, FEBS LETT, V587, P3175, DOI 10.1016/j.febslet.2013.07.048
   Yang LQ, 2011, CELL, V147, P773, DOI 10.1016/j.cell.2011.08.054
   Yao J, 2016, EMBO MOL MED, V8, P1113, DOI 10.15252/emmm.201606749
   Yao YB, 2012, BIOCHEM BIOPH RES CO, V423, P613, DOI 10.1016/j.bbrc.2012.06.050
   Yau JWY, 2012, DIABETES RES CLIN PR, V95, P265, DOI 10.1016/j.diabres.2011.10.027
   Yin KJ, 2014, NEUROCHEM INT, V77, P9, DOI 10.1016/j.neuint.2014.03.013
   Yoon JH, 2013, J MOL BIOL, V425, P3723, DOI 10.1016/j.jmb.2012.11.024
   Yoshimoto R, 2016, BBA-GENE REGUL MECH, V1859, P192, DOI 10.1016/j.bbagrm.2015.09.012
   Zhang B, 2012, CELL REP, V2, P111, DOI 10.1016/j.celrep.2012.06.003
   Zhang J, 2016, EXP NEUROL, V277, P162, DOI 10.1016/j.expneurol.2015.12.014
   Zhang J, 2015, INT J CLIN EXP MED, V8, P5499
   Zhang QS, 2016, BIOMED PHARMACOTHER, V83, P153, DOI 10.1016/j.biopha.2016.06.017
   Zhang XJ, 2017, J NEUROSCI, V37, P1797, DOI 10.1523/JNEUROSCI.3389-16.2017
   Zhao G, 2016, FEBS LETT, V590, P2884, DOI 10.1002/1873-3468.12315
   Zhao Y, 2014, CANCER RES, V74, P5103, DOI 10.1158/0008-5472.CAN-14-0427
   Zhao ZH, 2017, CELL BIOL INT, V41, P62, DOI 10.1002/cbin.10701
   Zhao ZY, 2014, BIOCHEM BIOPH RES CO, V445, P388, DOI 10.1016/j.bbrc.2014.02.006
   Zheng HT, 2014, INT J CLIN EXP PATHO, V7, P3174
NR 137
TC 384
Z9 418
U1 2
U2 51
PU TAYLOR & FRANCIS INC
PI PHILADELPHIA
PA 530 WALNUT STREET, STE 850, PHILADELPHIA, PA 19106 USA
SN 1547-6286
EI 1555-8584
J9 RNA BIOL
JI RNA Biol.
PY 2017
VL 14
IS 12
BP 1705
EP 1714
DI 10.1080/15476286.2017.1358347
PG 10
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA FT6VH
UT WOS:000423291400013
PM 28837398
OA Green Published, Bronze
DA 2025-04-10
ER

PT J
AU Maroney, SA
   Mast, AE
AF Maroney, S. A.
   Mast, A. E.
TI New insights into the biology of tissue factor pathway inhibitor
SO JOURNAL OF THROMBOSIS AND HAEMOSTASIS
LA English
DT Review
DE hemophilia; prothrombinase; TFPI; thrombosis; tissue factor
ID HUMAN ENDOTHELIAL-CELLS; FACTOR-XA; FACTOR-V; COAGULATION INHIBITOR;
   PROTEIN-S; FUNCTIONAL-CHARACTERIZATION; INTRAUTERINE LETHALITY;
   TFPI-ALPHA; SURFACE; MICE
AB Tissue factor pathway inhibitor (TFPI) dampens the initiation of blood coagulation by inhibiting two potent procoagulant complexes, tissue factor-factor VIIa (TF-FVIIa) and early forms of prothrombinase. TFPI isoforms, TFPI and TFPI, result from alternative splicing of mRNA, producing distinct C-terminal ends of the two proteins. Both isoforms inhibit TF-FVIIa, but only TFPI can inhibit early forms of prothrombinase by binding of its positively charged C-terminus with high affinity to the acidic B-domain exosite of FVa, which is generated upon activation by FXa. TFPI and TFPI are produced in cultured human endothelial cells, while platelets contain only TFPI. Knowledge of the anticoagulant mechanisms and tissue expression patterns of TFPI and TFPI have improved our understanding of the phenotypes observed in different mouse models of TFPI deficiency, the east Texas bleeding disorder, and the development of pharmaceutical agents that block TFPI function to treat hemophilia.
C1 [Maroney, S. A.; Mast, A. E.] Blood Ctr Wisconsin, Blood Res Inst, Milwaukee, WI 53201 USA.
   [Mast, A. E.] Med Coll Wisconsin, Dept Cell Biol Neurobiol & Anat, Milwaukee, WI 53226 USA.
C3 Versiti Blood Center of Wisconsin; Medical College of Wisconsin
RP Mast, AE (corresponding author), Blood Ctr Wisconsin, Blood Res Inst, POB 2178, Milwaukee, WI 53201 USA.
EM alan.mast@bcw.edu
FU NHLBI NIH HHS [R01 HL068835] Funding Source: Medline
CR AMERI A, 1992, BLOOD, V79, P3219
   Baugh RJ, 1998, J BIOL CHEM, V273, P4378, DOI 10.1074/jbc.273.8.4378
   BLOEMENKAMP KWM, 1995, LANCET, V346, P1593, DOI 10.1016/S0140-6736(95)91929-5
   Bos MHA, 2012, J BIOL CHEM, V287, P26342, DOI 10.1074/jbc.M112.377168
   BROZE GJ, 1994, BLOOD COAGUL FIBRIN, V5, P551
   BROZE GJ, 1988, BLOOD, V71, P335
   Brufatto N, 2003, J THROMB HAEMOST, V1, P1258, DOI 10.1046/j.1538-7836.2003.00254.x
   Chan JCY, 1999, J CLIN INVEST, V103, P475, DOI 10.1172/JCI5678
   Cunningham AC, 2002, BIOCHEM J, V367, P451, DOI 10.1042/BJ20020696
   Dockal M, 2014, J BIOL CHEM, V289, P1732, DOI 10.1074/jbc.M113.533836
   Donahue BS, 2006, J THROMB HAEMOST, V4, P1011, DOI 10.1111/j.1538-7836.2006.01896.x
   Eitzman DT, 2002, CIRCULATION, V105, P2139, DOI 10.1161/01.CIR.0000017361.39256.82
   Ellery PER, 2014, ARTERIOSCL THROM VAS, V34, P187, DOI 10.1161/ATVBAHA.113.302660
   ERHARDTSEN E, 1995, BLOOD COAGUL FIBRIN, V6, P388, DOI 10.1097/00001721-199507000-00004
   Girard TJ, 2012, BLOOD, V119, P1256, DOI 10.1182/blood-2011-10-388512
   GIRARD TJ, 1989, NATURE, V338, P518, DOI 10.1038/338518a0
   Hackeng TM, 2006, P NATL ACAD SCI USA, V103, P3106, DOI 10.1073/pnas.0504240103
   Han X, 2000, BLOOD, V96, P3049
   Hansen JB, 2000, THROMB HAEMOSTASIS, V83, P937
   Harris GM, 1999, AM J HEMATOL, V60, P175, DOI 10.1002/(SICI)1096-8652(199903)60:3<175::AID-AJH1>3.3.CO;2-O
   Hilden I, 2012, BLOOD, V119, P5871, DOI 10.1182/blood-2012-01-401620
   Huang ZF, 1997, BLOOD, V90, P944, DOI 10.1182/blood.V90.3.944.944_944_951
   Kempton CL, 2014, BLOOD, V124, P3365, DOI 10.1182/blood-2014-05-577643
   Lupu C, 2005, J BIOL CHEM, V280, P22308, DOI 10.1074/jbc.M503333200
   LUPU C, 1995, ARTERIOSCL THROM VAS, V15, P2055, DOI 10.1161/01.ATV.15.11.2055
   Maroney SA, 2008, J THROMB HAEMOST, V6, P1344, DOI 10.1111/j.1538-7836.2008.03033.x
   Maroney SA, 2008, J THROMB HAEMOST, V6, P111
   Maroney SA, 2013, J THROMB HAEMOST, V11, P911, DOI 10.1111/jth.12188
   Maroney SA, 2009, J THROMB HAEMOST, V7, P1106, DOI 10.1111/j.1538-7836.2009.03454.x
   Maroney SA, 2007, BLOOD, V109, P1931, DOI 10.1182/blood-2006-07-037283
   Maroney SA, 2012, BIOCHEM J, V443, P259, DOI 10.1042/BJ20111994
   Maroney SA, 2012, P NATL ACAD SCI USA, V109, P3927, DOI 10.1073/pnas.1119858109
   Maroney SA, 2011, ARTERIOSCL THROM VAS, V31, P821, DOI 10.1161/ATVBAHA.110.220293
   Maroney SA, 2010, THROMB RES, V125, pS52, DOI 10.1016/j.thromres.2010.01.038
   Mast AE, 1996, BLOOD, V87, P1845
   Moatti D, 2000, THROMB HAEMOSTASIS, V84, P244
   MONKOVIC DD, 1990, J BIOL CHEM, V265, P17132
   MONKOVIC DD, 1990, BIOCHEMISTRY-US, V29, P1118, DOI 10.1021/bi00457a004
   Ndonwi M, 2010, BLOOD, V116, P1344, DOI 10.1182/blood-2009-10-246686
   NOVOTNY WF, 1988, BLOOD, V72, P2020
   Oudot-Mellakh T, 2012, BRIT J HAEMATOL, V157, P230, DOI 10.1111/j.1365-2141.2011.09025.x
   Pedersen B, 2005, BLOOD, V105, P2777, DOI 10.1182/blood-2004-09-3724
   PETERSEN JGL, 1993, J BIOL CHEM, V268, P13344
   Piro O, 2005, J THROMB HAEMOST, V3, P2677, DOI 10.1111/j.1538-7836.2005.01636.x
   Prasad S, 2008, BLOOD, V111, P672, DOI 10.1182/blood-2007-07-098913
   Schuijt TJ, 2013, CIRCULATION, V128, P254, DOI 10.1161/CIRCULATIONAHA.113.003191
   Semeraro F, 2011, BLOOD, V118, P1952, DOI 10.1182/blood-2011-03-343061
   Smith SA, 2008, THROMB HAEMOSTASIS, V100, P160, DOI 10.1160/TH08-05-0275
   Tran S, 2008, J BIOL CHEM, V283, P6648, DOI 10.1074/jbc.M708036200
   Vincent LM, 2013, J CLIN INVEST, V123, P3777, DOI 10.1172/JCI69091
   Waters EK, 2011, BLOOD, V117, P5514, DOI 10.1182/blood-2010-10-311936
   WESSELSCHMIDT R, 1992, BLOOD, V79, P2004
   Willyard C, 2014, NATURE, V515, pS168, DOI 10.1038/515S168a
   Winckers K, 2013, BLOOD REV, V27, P119, DOI 10.1016/j.blre.2013.03.001
   Wood JP, 2014, ARTERIOSCL THROM VAS, V34, P169, DOI 10.1161/ATVBAHA.113.302655
   Wood JP, 2013, P NATL ACAD SCI USA, V110, P17838, DOI 10.1073/pnas.1310444110
   WUN TC, 1988, J BIOL CHEM, V263, P6001
   Zhang J, 2003, CIRCULATION, V108, P623, DOI 10.1161/01.CIR.0000078642.45127.7B
   Zhang ZQ, 2015, CARBOHYD POLYM, V115, P677, DOI 10.1016/j.carbpol.2014.09.001
NR 59
TC 73
Z9 80
U1 0
U2 11
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 1538-7933
EI 1538-7836
J9 J THROMB HAEMOST
JI J. Thromb. Haemost.
PD JUN
PY 2015
VL 13
SU 1
SI SI
BP S200
EP S207
DI 10.1111/jth.12897
PG 8
WC Hematology; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Hematology; Cardiovascular System & Cardiology
GA CL1BN
UT WOS:000356677500027
PM 26149025
OA Green Accepted, Bronze
DA 2025-04-10
ER

PT J
AU Lee, YA
   Na, W
   Lee, K
   Lee, HS
   Ju, BG
AF Lee, Young Ae
   Na, Wonho
   Lee, Kwanghyun
   Lee, HoSuk Sean
   Ju, Bong-Gun
TI Characterization of HDAC9 isoforms in brain microvessel bEnd.3 cells
   upon oxygen and glucose deprivation-reperfusion injury
SO GENES & GENOMICS
LA English
DT Article
DE HDRP; HDAC9; Transcription; Blood-brain barrier; Endothelial cell
ID DEACETYLASE-RELATED PROTEIN; SPINAL-CORD-INJURY; FUNCTIONAL RECOVERY;
   BARRIER DISRUPTION; RAT MODEL; DEATH; ANGIOGENESIS; REPRESSOR; ISCHEMIA;
   HYPOXIA
AB Histone deacetylases (HDACs) and their inhibitors affect the integrity of blood-brain barrier (BBB) which plays an important role in pathological conditions of the central nervous system (CNS). In this study, expression of HDACs was examined in bEnd.3 endothelial cells subjected to oxygen and glucose deprivation (OGD)-reperfusion injury. Expression of histone deacetylase-related protein (HDRP) produced by alternative splicing of HDAC9 was found to increase significantly in bEnd.3 cells upon OGD-reperfusion injury. HDRP was primarily localized in the nucleus. To investigate potential target genes of HDRP, its transcript was depleted by RNA interference and gene expression was determined. We found that FAS and GADD45a gene expression was up-regulated in HDRP-depleted bEnd.3 cells subjected to OGD-reperfusion injury. Interestingly, these genes are known to be involved in apoptosis and permeability of vascular endothelial cells. Our study suggests that HDRP may play a significant role in BBB integrity after CNS damage.
C1 [Lee, Young Ae; Na, Wonho; Lee, Kwanghyun; Lee, HoSuk Sean; Ju, Bong-Gun] Sogang Univ, Dept Life Sci, Seoul 121742, South Korea.
C3 Sogang University
RP Ju, BG (corresponding author), Sogang Univ, Dept Life Sci, Sinsoo Dong 1, Seoul 121742, South Korea.
EM bgju@sogang.ac.kr
RI Lee, Young-Ah/X-8919-2019
CR Bardai FH, 2012, J BIOL CHEM, V287, P35444, DOI 10.1074/jbc.M112.394544
   Chen JH, 2005, NAT MED, V11, P1188, DOI 10.1038/nm1307
   Dash PK, 2010, PLOS ONE, V5, DOI 10.1371/journal.pone.0011383
   Förster C, 2008, J PHYSIOL-LONDON, V586, P1937, DOI 10.1113/jphysiol.2007.146852
   Gloire G, 2008, BIOCHEM PHARMACOL, V76, P1451, DOI 10.1016/j.bcp.2008.06.023
   Green MichaelR., 2012, Molecular cloning: a laboratory manual, V1
   Guo G, 2007, NEUROCHEM RES, V32, P2160, DOI 10.1007/s11064-007-9408-8
   Hawkins BT, 2005, PHARMACOL REV, V57, P173, DOI 10.1124/pr.57.2.4
   Lavrik IN, 2012, CELL DEATH DIFFER, V19, P36, DOI 10.1038/cdd.2011.155
   Lee JY, 2012, J NEUROCHEM, V121, P818, DOI 10.1111/j.1471-4159.2012.07731.x
   Morrison BE, 2006, MOL CELL BIOL, V26, P3550, DOI 10.1128/MCB.26.9.3550-3564.2006
   Morrison BE, 2008, EXP BIOL MED, V233, P980, DOI 10.3181/0802-RM-48
   Nohda K, 2007, SPINE, V32, P1060, DOI 10.1097/01.brs.0000261560.53428.90
   Ogata T, 1996, J ORTHOPAED RES, V14, P504, DOI 10.1002/jor.1100140322
   Petrie K, 2003, J BIOL CHEM, V278, P16059, DOI 10.1074/jbc.M212935200
   Redzic Z, 2011, FLUIDS BARRIERS CNS, V8, DOI 10.1186/2045-8118-8-3
   Simard JM, 2007, J CLIN INVEST, V117, P2105, DOI 10.1172/JCI32041
   Sparrow DB, 1999, EMBO J, V18, P5085, DOI 10.1093/emboj/18.18.5085
   Stamatovic SM, 2008, CURR NEUROPHARMACOL, V6, P179, DOI 10.2174/157015908785777210
   Wang LY, 2011, BRAIN RES, V1372, P13, DOI 10.1016/j.brainres.2010.11.099
   Wang ZF, 2012, STROKE, V43, P2430, DOI 10.1161/STROKEAHA.112.652545
   Wang ZF, 2011, J CEREBR BLOOD F MET, V31, P52, DOI 10.1038/jcbfm.2010.195
   Wosik K, 2007, J NEUROL SCI, V259, P53, DOI 10.1016/j.jns.2006.08.018
   Yang XJ, 2007, ONCOGENE, V26, P5310, DOI 10.1038/sj.onc.1210599
   Yang XJ, 2008, NAT REV MOL CELL BIO, V9, P206, DOI 10.1038/nrm2346
   Yourick DL, 2003, BRAIN RES, V991, P56, DOI 10.1016/S0006-8993(03)03533-9
   Zhang CL, 2001, P NATL ACAD SCI USA, V98, P7354, DOI 10.1073/pnas.131198498
   Zhang XG, 2008, J NEUROSCI RES, V86, P2423, DOI 10.1002/jnr.21680
   Zhou XB, 2000, P NATL ACAD SCI USA, V97, P1056, DOI 10.1073/pnas.97.3.1056
NR 29
TC 0
Z9 0
U1 0
U2 9
PU SPRINGER
PI NEW YORK
PA 233 SPRING ST, NEW YORK, NY 10013 USA
SN 1976-9571
EI 2092-9293
J9 GENES GENOM
JI Genes Genom.
PD JUN
PY 2015
VL 37
IS 6
BP 537
EP 543
DI 10.1007/s13258-015-0282-5
PG 7
WC Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology;
   Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology;
   Genetics & Heredity
GA CI4JO
UT WOS:000354714700005
DA 2025-04-10
ER

PT J
AU Citterio, L
   Azzani, T
   Duga, S
   Bianchi, G
AF Citterio, L
   Azzani, T
   Duga, S
   Bianchi, G
TI Genomic organization of the human γ adducin gene
SO BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
LA English
DT Article
ID HUMAN ERYTHROCYTE ADDUCIN; HUMAN ALPHA-ADDUCIN; PROTEIN-KINASE-C;
   BETA-ADDUCIN; ESSENTIAL-HYPERTENSION; POINT MUTATIONS; DOMAIN;
   POLYMORPHISMS; EXPRESSION
AB We report the genomic structure of the human gamma adducin gene (ADD3). Adducin is a protein involved in cytoskeletal assembly and composed of alpha-beta or alpha-beta subunits which share a high degree of homology between human and rat. Mutations in cu subunit have been shown associated to both human and rat hypertension. The human ADD3 gene spans over 20 kb and is composed of at least 13 introns and 14 exons covering the entire coding region. The exon size ranges from 81 bp to greater than 293 bp and the intron size from 111 bp to longer than 3.2 kb. We also demonstrate the presence of an alternative splicing event around exon 13, whose sequence, position, and expression is analogous in rat Add3 gene. Moreover, human ADD3 amino acid sequence presents 91.9% of identity compared to rat sequence. Characterization of human ADD3 gene provides an important tool for mutation analysis. (C) 1999 Academic Press.
C1 Hosp San Raffaele, Div Nephrol Dialysis & Hypertens, I-20132 Milan, Italy.
   Univ Milan, Vet Physiol & Biochem Inst, Milan, Italy.
C3 Vita-Salute San Raffaele University; IRCCS Ospedale San Raffaele;
   University of Milan
RP Citterio, L (corresponding author), Hosp San Raffaele, Div Nephrol Dialysis & Hypertens, I-20132 Milan, Italy.
RI Citterio, Lorena/AAC-1589-2019; Duga, Stefano/F-8173-2014
OI Duga, Stefano/0000-0003-3457-1410; Citterio, Lorena/0000-0001-6455-2291;
   Bianchi, Giuseppe/0000-0002-8365-3618
CR Barber B. R., 1994, V16, P316
   BARLASSINA C, 1999, IN PRESS KIDNEY INT
   BIANCHI G, 1994, P NATL ACAD SCI USA, V91, P3999, DOI 10.1073/pnas.91.9.3999
   BREATHNACH R, 1981, ANNU REV BIOCHEM, V50, P349, DOI 10.1146/annurev.bi.50.070181.002025
   CASARI G, 1995, HYPERTENSION, V25, P320, DOI 10.1161/01.HYP.25.3.320
   Castellano M, 1997, J HYPERTENS, V15, P1707, DOI 10.1097/00004872-199715120-00076
   Cusi D, 1997, LANCET, V349, P1353, DOI 10.1016/S0140-6736(97)01029-5
   DONG LQ, 1995, J BIOL CHEM, V270, P25534, DOI 10.1074/jbc.270.43.25534
   Ferrandi M, 1996, HYPERTENSION, V28, P1018, DOI 10.1161/01.HYP.28.6.1018
   FERRANDI M, 1999, IN PRESS AM J PHYSL, V277
   Gilligan DM, 1997, GENOMICS, V43, P141, DOI 10.1006/geno.1997.4802
   HUGHES CA, 1995, J BIOL CHEM, V270, P18990, DOI 10.1074/jbc.270.32.18990
   JOSHI R, 1990, J BIOL CHEM, V265, P13130
   JOSHI R, 1991, J CELL BIOL, V115, P665, DOI 10.1083/jcb.115.3.665
   Katagiri T, 1996, CYTOGENET CELL GENET, V74, P90, DOI 10.1159/000134389
   LIN BY, 1995, GENOMICS, V25, P93, DOI 10.1016/0888-7543(95)80113-Z
   Manunta P, 1998, KIDNEY INT, V53, P1471, DOI 10.1046/j.1523-1755.1998.00931.x
   Matsuoka Y, 1996, J BIOL CHEM, V271, P25157, DOI 10.1074/jbc.271.41.25157
   Sambrook J, 1989, MOL CLONING LAB MANU
   SHYAMALA V, 1989, GENE, V84, P1, DOI 10.1016/0378-1119(89)90132-7
   Tripodi G, 1995, GENE, V166, P307, DOI 10.1016/0378-1119(95)00590-0
   Tripodi G, 1997, BIOCHEM BIOPH RES CO, V237, P685, DOI 10.1006/bbrc.1997.7173
   Tripodi G, 1996, J CLIN INVEST, V97, P2815, DOI 10.1172/JCI118737
NR 23
TC 14
Z9 17
U1 0
U2 2
PU ACADEMIC PRESS INC
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0006-291X
J9 BIOCHEM BIOPH RES CO
JI Biochem. Biophys. Res. Commun.
PD DEC 9
PY 1999
VL 266
IS 1
BP 110
EP 114
DI 10.1006/bbrc.1999.1769
PG 5
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA 263TF
UT WOS:000084140800020
PM 10581174
DA 2025-04-10
ER

PT J
AU Verkerk, AO
   Amin, AS
   Remme, CA
AF Verkerk, Arie O.
   Amin, Ahmad S.
   Remme, Carol Ann
TI Disease Modifiers of Inherited SCN5A Channelopathy
SO FRONTIERS IN CARDIOVASCULAR MEDICINE
LA English
DT Review
DE Na(V)1.5; LQT3; Brugada syndrome; conduction; co-morbidities
ID LONG QT SYNDROME; BRUGADA-SYNDROME; SODIUM CURRENT; DILATED
   CARDIOMYOPATHY; SYNDROME TYPE-3; SPLICE VARIANT; NA+ CHANNEL; MUTATION;
   CURRENTS; MICE
AB To date, a large number of mutations in SCN5A, the gene encoding the pore-forming a-subunit of the primary cardiac Na+ channel (Na(V)1.5), have been found in patients presenting with a wide range of ECG abnormalities and cardiac syndromes. Although these mutations all affect the same Na(V)1.5 channel, the associated cardiac syndromes each display distinct phenotypical and biophysical characteristics. Variable disease expressivity has also been reported, where one particular mutation in SCN5A may lead to either one particular symptom, a range of various clinical signs, or no symptoms at all, even within one single family. Additionally, disease severity may vary considerably between patients carrying the same mutation. The exact reasons are unknown, but evidence is increasing that various cardiac and non-cardiac conditions can influence the expressivity and severity of inherited SCN5A channelopathies. In this review, we provide a summary of identified disease entities caused by SCN5A mutations, and give an overview of co-morbidities and other (non)-genetic factors which may modify SCN5A channelopathies. A comprehensive knowledge of these modulatory factors is not only essential for a complete understanding of the diverse clinical phenotypes associated with SCN5A mutations, but also for successful development of effective risk stratification and (alternative) treatment paradigms.
C1 [Verkerk, Arie O.; Amin, Ahmad S.; Remme, Carol Ann] Acad Med Ctr, Heart Ctr, Dept Clin & Expt Cardiol, Amsterdam, Netherlands.
   [Verkerk, Arie O.] Acad Med Ctr, Dept Med Biol, Amsterdam, Netherlands.
C3 University of Amsterdam; Academic Medical Center Amsterdam; University
   of Amsterdam; Academic Medical Center Amsterdam
RP Remme, CA (corresponding author), Acad Med Ctr, Heart Ctr, Dept Clin & Expt Cardiol, Amsterdam, Netherlands.
EM c.a.remme@amc.uva.nl
RI Amin, Ahmad/Y-8107-2019; Verkerk, Arie/HQZ-9694-2023
OI Remme, Carol Ann/0000-0003-0095-0084; Verkerk, Arie/0000-0003-2140-834X;
   Amin, A.S./0000-0002-1600-7907
FU Innovational Research Incentives Scheme Vidi grant from ZonMw
   [91714371]; Netherlands CardioVascular Research Initiative; Dutch Heart
   Foundation [CVON2012-10, CVON2015-12]
FX This study was supported by an Innovational Research Incentives Scheme
   Vidi grant from ZonMw (grant no. 91714371, to CR), in addition to the
   Netherlands CardioVascular Research Initiative, an initiative with
   support from the Dutch Heart Foundation (CVON2012-10 PREDICT and
   CVON2015-12 e-DETECT).
CR Achaiah Andrew, 2016, JRSM Open, V7, p2054270416640153, DOI 10.1177/2054270416640153
   Ackerman MJ, 2004, HEART RHYTHM, V1, P600, DOI 10.1016/j.hrthm.2004.07.013
   Amin A S, 2010, Neth Heart J, V18, P165, DOI 10.1007/BF03091755
   Amin AS, 2005, ACTA PHYSIOL SCAND, V185, P291, DOI 10.1111/j.1365-201X.2005.01496.x
   Ton AT, 2017, ARCH TOXICOL, V91, P3947, DOI 10.1007/s00204-017-2006-x
   Aromolaran AS, 2017, FRONT PHYSIOL, V8, DOI 10.3389/fphys.2017.00431
   Aulbach F, 1999, CARDIOVASC RES, V42, P113, DOI 10.1016/S0008-6363(98)00307-1
   Baba S, 2006, AM J PHYSIOL-HEART C, V291, pH756, DOI 10.1152/ajpheart.00063.2006
   Balser JR, 1999, CARDIOVASC RES, V42, P327, DOI 10.1016/S0008-6363(99)00031-0
   Barajas-Martinez H, 2009, CARDIOVASC RES, V81, P82, DOI 10.1093/cvr/cvn255
   Baruscotti M, 2000, AM J PHYSIOL-HEART C, V279, pH2303, DOI 10.1152/ajpheart.2000.279.5.H2303
   Basso C, 2012, CIRC-ARRHYTHMIA ELEC, V5, P1233, DOI 10.1161/CIRCEP.111.962035
   Basso C, 2009, LANCET, V373, P1289, DOI 10.1016/S0140-6736(09)60256-7
   Beaufort-Krol GCM, 2005, J AM COLL CARDIOL, V46, P331, DOI 10.1016/j.jacc.2005.03.066
   Bebarova M, 2014, J PHYSIOL PHARMACOL, V65, P497
   Berecki G, 2010, PLOS ONE, V5, DOI 10.1371/journal.pone.0015772
   Bezzina C, 1999, CIRC RES, V85, P1206
   Bezzina CR, 2008, CIRC-ARRHYTHMIA ELEC, V1, P80, DOI 10.1161/CIRCEP.108.791434
   Bezzina CR, 2006, CIRCULATION, V113, P338, DOI 10.1161/CIRCULATIONAHA.105.580811
   Burashnikov A, 2008, CIRC-ARRHYTHMIA ELEC, V1, P202, DOI 10.1161/CIRCEP.107.691931
   Chadda KR, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-11210-3
   Chanavirut R, 2017, J Cardiol Curr Res, V8, DOI [10.15406/jccr.2017.08.00294, DOI 10.15406/JCCR.2017.08.00294]
   Chapalamadugu Kalyan, 2014, Recent Pat Biotechnol, V8, P123, DOI 10.2174/1872208309666140904123023
   Cheng JD, 2010, CTS-CLIN TRANSL SCI, V3, P287, DOI 10.1111/j.1752-8062.2010.00249.x
   Claes GRF, 2016, EUR HEART J, V37, P1815, DOI 10.1093/eurheartj/ehv522
   Coronel R, 2005, CIRCULATION, V112, P2769, DOI 10.1161/CIRCULATIONAHA.105.532614
   D'Souza A, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms4775
   Dallas ML, 2012, AM J RESP CRIT CARE, V186, P648, DOI 10.1164/rccm.201204-0688OC
   DEKKER JM, 1994, CIRCULATION, V90, P779, DOI 10.1161/01.CIR.90.2.779
   Diness JG, 2009, HEART RHYTHM, V6, P100, DOI 10.1016/j.hrthm.2008.10.020
   Dumaine R, 1999, CIRC RES, V85, P803, DOI 10.1161/01.RES.85.9.803
   Effinor PT, 2008, HEART RHYTHM, V5, P99, DOI 10.1016/j.hrthm.2007.09.015
   Egri C, 2012, CHANNELS, V6, P75, DOI 10.4161/chan.19827
   Fazio G, 2013, WORLD J CARDIOL, V5, P87, DOI 10.4330/wjc.v5.i4.87
   Fish JM, 2006, CIRCULATION, V113, P1393, DOI 10.1161/CIRCULATIONAHA.105.601690
   Gastaldelli A, 2000, AM J PHYSIOL-REG I, V279, pR2022, DOI 10.1152/ajpregu.2000.279.6.R2022
   Groenewegen WA, 2003, CIRC RES, V92, P14, DOI 10.1161/01.RES.0000050585.07097.D7
   Gui JH, 2010, J CARDIOVASC ELECTR, V21, P564, DOI 10.1111/j.1540-8167.2010.01762.x
   Guo JH, 2017, CHINESE MED J-PEKING, V130, P203, DOI 10.4103/0366-6999.198003
   Hahad O, 2018, INT J CARDIOL, V264, P79, DOI 10.1016/j.ijcard.2018.03.126
   Hansen PS, 2000, AM J PHYSIOL-CELL PH, V278, pC546, DOI 10.1152/ajpcell.2000.278.3.C546
   Hayashi H, 2018, J ARRYTHM, V34, P216, DOI 10.1002/joa3.12046
   Hershberger RE, 2013, NAT REV CARDIOL, V10, P531, DOI 10.1038/nrcardio.2013.105
   Hoogendijk MG, 2011, HEART RHYTHM, V8, P111, DOI 10.1016/j.hrthm.2010.09.066
   Hou JW, 2016, HEART RHYTHM, V13, P973, DOI 10.1016/j.hrthm.2015.12.023
   Huang HY, 2013, J MOL CELL CARDIOL, V59, P151, DOI 10.1016/j.yjmcc.2013.03.007
   Ikeda T, 2006, J CARDIOVASC ELECTR, V17, P602, DOI 10.1111/j.1540-8167.2006.00424.x
   Ioakeimidis NS, 2017, J BIOL RES-THESSALON, V24, DOI 10.1186/s40709-017-0063-1
   Kapplinger JD, 2011, J AM COLL CARDIOL, V57, P2317, DOI 10.1016/j.jacc.2010.12.036
   Klaver EC, 2011, INT J CARDIOL, V152, P162, DOI 10.1016/j.ijcard.2010.12.051
   Klein G, 2007, FORENSIC SCI INT, V171, P131, DOI 10.1016/j.forsciint.2006.10.012
   KOKUBUN S, 1982, PFLUG ARCH EUR J PHY, V393, P15, DOI 10.1007/BF00582385
   Kolder ICRM, 2012, J MOL CELL CARDIOL, V52, P620, DOI 10.1016/j.yjmcc.2011.12.014
   Korantzopoulos P, 2011, AM J CARDIOL, V107, P37, DOI 10.1016/j.amjcard.2010.08.038
   Kujime S, 2017, INTERNAL MED, V56, P129, DOI 10.2169/internalmedicine.56.7307
   Kyndt F, 2001, CIRCULATION, V104, P3081, DOI 10.1161/hc5001.100834
   Lei M, 2004, J PHYSIOL-LONDON, V559, P835, DOI 10.1113/jphysiol.2004.068643
   Li J, 2017, BIOMED RES INT, V2017, DOI 10.1155/2017/4615727
   Lieve KV, 2017, INT J CARDIOL, V236, P187, DOI 10.1016/j.ijcard.2017.01.113
   Lodder EM, 2012, PLOS GENET, V8, DOI 10.1371/journal.pgen.1003113
   Lu ZJ, 2013, DIABETES, V62, P4257, DOI 10.2337/db13-0420
   Macleod JC, 1998, EUR J PHARMACOL, V356, P261, DOI 10.1016/S0014-2999(98)00528-7
   Makielski JC, 2003, CIRC RES, V93, P821, DOI 10.1161/01.RES.0000096652.14509.96
   Marangoni S, 2011, CARDIOVASC RES, V91, P606, DOI 10.1093/cvr/cvr142
   Mascia G, 2018, J CARDIOVASC ELECTR, V29, P489, DOI 10.1111/jce.13410
   Mascia G, 2017, INT J SPORTS MED, V38, P573, DOI 10.1055/s-0043-107240
   Matsuo K, 2001, J AM COLL CARDIOL, V38, P765, DOI 10.1016/S0735-1097(01)01421-8
   McNair WP, 2004, CIRCULATION, V110, P2163, DOI 10.1161/01.CIR.0000144458.58660.BB
   Meregalli PG, 2009, HEART RHYTHM, V6, P341, DOI 10.1016/j.hrthm.2008.11.009
   Meregalli PG, 2005, CARDIOVASC RES, V67, P367, DOI 10.1016/j.cardiores.2005.03.005
   Minoura Y, 2013, HEART RHYTHM, V10, P1054, DOI 10.1016/j.hrthm.2013.03.011
   Mordukhovich I, 2016, EPIDEMIOLOGY, V27, P284, DOI 10.1097/EDE.0000000000000424
   Münzel T, 2018, ANTIOXID REDOX SIGN, V28, P873, DOI 10.1089/ars.2017.7118
   Nadruz W, 2015, J HUM HYPERTENS, V29, P1, DOI 10.1038/jhh.2014.36
   Nagatomo T, 1998, AM J PHYSIOL-HEART C, V275, pH2016, DOI 10.1152/ajpheart.1998.275.6.H2016
   Nishizaki M, 2008, HEART VESSELS, V23, P201, DOI 10.1007/s00380-007-1036-3
   Noda T, 2002, J AM COLL CARDIOL, V40, P1841, DOI 10.1016/S0735-1097(02)02494-4
   O'Leary ME, 2010, BRIT J CLIN PHARMACO, V69, P427, DOI 10.1111/j.1365-2125.2010.03629.x
   Ohkubo K, 2013, J ARRYTHM, V29, P211, DOI 10.1016/j.joa.2012.09.008
   Ong P, 2011, EUROPACE, V13, P1625, DOI 10.1093/europace/eur205
   Opdal SH, 2004, PEDIATRICS, V114, pE506, DOI 10.1542/peds.2004-0683
   Ozyilmaz I, 2017, PEDIATRICS, V140, DOI 10.1542/peds.2016-2485
   Paci M, 2017, HEART RHYTHM, V14, P1704, DOI 10.1016/j.hrthm.2017.07.026
   Parisi P, 2013, EPILEPSY RES, V105, P415, DOI 10.1016/j.eplepsyres.2013.02.024
   Pi-Sunyer FX, 2002, OBES RES, V10, p97S, DOI 10.1038/oby.2002.202
   Poelzing S, 2006, CIRCULATION, V114, P368, DOI 10.1161/CIRCULATIONAHA.105.601294
   Postema Pieter G, 2017, JACC Clin Electrophysiol, V3, P68, DOI 10.1016/j.jacep.2016.05.014
   Postema PG, 2013, EUROPACE, V15, P1042, DOI 10.1093/europace/eut018
   Postema PG, 2013, J GERIATR CARDIOL, V10, P75, DOI 10.3969/j.issn.1671-5411.2013.01.012
   Postema PG, 2009, HEART RHYTHM, V6, P1335, DOI 10.1016/j.hrthm.2009.07.002
   Potet F, 2015, CIRC-ARRHYTHMIA ELEC, V8, P933, DOI 10.1161/CIRCEP.115.002760
   Probst V, 2003, J AM COLL CARDIOL, V41, P643, DOI 10.1016/S0735-1097(02)02864-4
   Probst V, 2009, CIRC-CARDIOVASC GENE, V2, P552, DOI 10.1161/CIRCGENETICS.109.853374
   Remme CA, 2009, BASIC RES CARDIOL, V104, P511, DOI 10.1007/s00395-009-0012-8
   Remme CA, 2008, EUROPACE, V10, P1253, DOI 10.1093/europace/eun267
   Remme CA, 2006, CIRCULATION, V114, P2584, DOI 10.1161/CIRCULATIONAHA.106.653949
   Remme CA, 2013, J PHYSIOL-LONDON, V591, P4099, DOI 10.1113/jphysiol.2013.256461
   Remme CA, 2013, CARDIOVASC DRUG THER, V27, P91, DOI 10.1007/s10557-012-6433-x
   Remme CA, 2009, CIRC RES, V104, P1283, DOI 10.1161/CIRCRESAHA.109.194423
   Rivaud MR, 2018, INT J CARDIOL, V263, P54, DOI 10.1016/j.ijcard.2018.03.044
   Rivaud MR, 2018, EUR HEART J, V39, P2898, DOI 10.1093/eurheartj/ehy247
   Rizzo S, 2012, CARDIOVASC RES, V95, P409, DOI 10.1093/cvr/cvs219
   Royer A, 2005, CIRCULATION, V111, P1738, DOI 10.1161/01.CIR.0000160853.19867.61
   Salem KA, 2013, MOL CELL BIOCHEM, V380, P83, DOI 10.1007/s11010-013-1662-2
   Sartiani L, 2004, CIRCULATION, V109, P419, DOI 10.1161/01.CIR.0000109497.73223.4D
   Sasaki T, 2006, INTERNAL MED, V45, P77, DOI 10.2169/internalmedicine.45.1404
   Sato PY, 2009, CIRC RES, V105, P523, DOI 10.1161/CIRCRESAHA.109.201418
   Savio-Galimberti Eleonora, 2014, Card Electrophysiol Clin, V6, P741
   Savio-Galimberti E, 2012, FRONT PHARMACOL, V3, DOI 10.3389/fphar.2012.00124
   Schwartz PJ, 2006, J INTERN MED, V259, P39, DOI 10.1111/j.1365-2796.2005.01583.x
   Scicluna BP, 2011, J MOL CELL CARDIOL, V50, P380, DOI 10.1016/j.yjmcc.2010.09.009
   Shah SR, 2019, CURR PROB CARDIOLOGY, V44, P83, DOI 10.1016/j.cpcardiol.2018.04.002
   Shi YQ, 2015, CELL PHYSIOL BIOCHEM, V37, P284, DOI 10.1159/000430353
   Shinlapawittayatorn K, 2011, HEART RHYTHM, V8, P455, DOI 10.1016/j.hrthm.2010.11.034
   Signore S, 2015, NAT COMMUN, V6, DOI 10.1038/ncomms9803
   Skinner JR, 2014, CASE REP MED, V2014, DOI 10.1155/2014/647252
   Splawski I, 2000, CIRCULATION, V102, P1178, DOI 10.1161/01.CIR.102.10.1178
   Stables CL, 2014, J MOL CELL CARDIOL, V69, P24, DOI 10.1016/j.yjmcc.2013.12.031
   Stones R, 2009, BASIC RES CARDIOL, V104, P643, DOI 10.1007/s00395-009-0030-6
   Sze E, 2008, ANN NONINVAS ELECTRO, V13, P327, DOI 10.1111/j.1542-474X.2008.00250.x
   Tan BH, 2006, AM J PHYSIOL-HEART C, V291, pH1822, DOI 10.1152/ajpheart.00101.2006
   Tan HL, 2003, CARDIOVASC RES, V57, P961, DOI 10.1016/S0008-6363(02)00714-9
   Uyarel H, 2005, J STUD ALCOHOL, V66, P555, DOI 10.15288/jsa.2005.66.555
   van den Berg MP, 2001, J CARDIOVASC ELECTR, V12, P630
   van Hoorn F, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0042037
   Veerman CC, 2015, GENE, V573, P177, DOI 10.1016/j.gene.2015.08.062
   Veglio M, 1999, DIABETOLOGIA, V42, P68, DOI 10.1007/s001250051115
   Verkerk AO, 2006, ACTA PHYSIOL, V187, P459, DOI 10.1111/j.1748-1716.2006.01586.x
   Verkerk AO, 2015, INT J MOL SCI, V16, P3071, DOI 10.3390/ijms16023071
   Verstraelen TE, 2015, NEUROGASTROENT MOTIL, V27, P906, DOI 10.1111/nmo.12569
   Viswanathan PC, 2003, J CLIN INVEST, V111, P341, DOI 10.1172/JCI200316879
   WEIDMANN S, 1955, J PHYSIOL-LONDON, V127, P213, DOI 10.1113/jphysiol.1955.sp005250
   Wilde AAM, 2018, JACC-CLIN ELECTROPHY, V4, P569, DOI 10.1016/j.jacep.2018.03.006
   Wilde AAM, 2016, CIRCULATION, V134, P872, DOI 10.1161/CIRCULATIONAHA.116.021823
   Wilders R, 2018, FRONT CARDIOVASC MED, V5, DOI 10.3389/fcvm.2018.00106
   Wilders R, 2018, INT J MOL SCI, V19, DOI 10.3390/ijms19020634
   Wilders R, 2012, FRONT PHYSIOL, V3, DOI 10.3389/fphys.2012.00168
   Wu CC, 1997, LIFE SCI, V61, P1539, DOI 10.1016/S0024-3205(97)00733-9
   Wu MH, 2014, PFLUG ARCH EUR J PHY, V466, P937, DOI 10.1007/s00424-013-1352-7
   XIAO YF, 1995, P NATL ACAD SCI USA, V92, P11000, DOI 10.1073/pnas.92.24.11000
   Xue XL, 2013, PACE, V36, P732, DOI 10.1111/pace.12109
   Yagi S, 2017, INT HEART J, V58, P720, DOI 10.1536/ihj.16-278
   Yap YG, 2009, EUROPACE, V11, P989, DOI 10.1093/europace/eup114
   Ye B, 2003, PHYSIOL GENOMICS, V12, P187, DOI 10.1152/physiolgenomics.00117.2002
   Yu J, 2014, HERZ, V39, P271, DOI 10.1007/s00059-013-3998-5
   Yu P, 2018, INT J CARDIOL, V260, P74, DOI 10.1016/j.ijcard.2018.02.099
   Ziyadeh-Isleem A, 2014, HEART RHYTHM, V11, P1015, DOI 10.1016/j.hrthm.2014.02.021
   Zygmunt AC, 2001, AM J PHYSIOL-HEART C, V281, pH689, DOI 10.1152/ajpheart.2001.281.2.H689
NR 148
TC 28
Z9 29
U1 1
U2 5
PU FRONTIERS MEDIA SA
PI LAUSANNE
PA AVENUE DU TRIBUNAL FEDERAL 34, LAUSANNE, CH-1015, SWITZERLAND
SN 2297-055X
J9 FRONT CARDIOVASC MED
JI Front. Cardiovasc. Med.
PD OCT 1
PY 2018
VL 5
AR 137
DI 10.3389/fcvm.2018.00137
PG 13
WC Cardiac & Cardiovascular Systems
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology
GA VJ7XL
UT WOS:000625880900001
PM 30327767
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Cohen-Barak, G
   Hagiwara, N
   Arlt, MF
   Horton, JP
   Brilliant, MH
AF Cohen-Barak, G
   Hagiwara, N
   Arlt, MF
   Horton, JP
   Brilliant, MH
TI Cloning, characterization and chromosome mapping of the human
   SOX6 gene
SO GENE
LA English
DT Article
DE high mobility group box; leucine zipper; SRY; skeletal muscle;
   cardiomyopathy
ID ARCHITECTURAL TRANSCRIPTION FACTORS; SEX-DETERMINING REGION;
   DNA-BINDING; SRY; PROTEIN; MOUSE; EXPRESSION; SEQUENCE; FAMILY; MEMBER
AB The Sox gene family encodes an important group of transcription factors harboring the conserved high-mobility group (HMG) box originally identified in the mouse and human testis determining gene Sry. We have cloned and sequenced SOX6, a member of the human Sox gene family. SOX6 cDNAs isolated from a human myoblast cDNA library show 94.3% amino acid identity to mouse Sox6 throughout the gene, and 100% identity in the critical HMG box and coiled-coil domains. The human SOX6 gene was localized to chromosome 11p15.2-11p15.3 in a region of shared synteny with distal mouse chromosome 7. An analysis of the genomic structure of the human SOX6 gene revealed 16 exons. We identified three SOX6 cDNAs that are generated by alternative splicing. Northern blot analysis revealed that SOX6 is expressed in a wide variety of tissues, most abundantly in skeletal muscle, suggesting an important role for SOX6 in muscle. Mice homozygous for a null mutation of Sox6 (p(100H)) die suddenly within the first 2 weeks after birth, most likely from cardiac conduction defects (Hagiwara et al., 2000). Thus, there is a possibility that human SOX6 is similarly involved in an, as yet, unidentified human cardiac disorder. (C) 2001 Elsevier Science B.V. All rights reserved.
C1 Univ Arizona, Coll Med, Steel Mem Childrens Res Ctr, Dept Pediat, Tucson, AZ 85724 USA.
   Univ Michigan, Dept Human Genet, Ann Arbor, MI 48109 USA.
C3 University of Arizona; University of Michigan System; University of
   Michigan
RP Brilliant, MH (corresponding author), Univ Arizona, Coll Med, Steel Mem Childrens Res Ctr, Dept Pediat, 1501 N Campbell Ave, Tucson, AZ 85724 USA.
EM mhb@peds.arizona.edu
FU NIGMS NIH HHS [GM43840] Funding Source: Medline
CR [Anonymous], METHOD ENZYMOL
   Argentaro A, 2000, GENE, V250, P181, DOI 10.1016/S0378-1119(00)00157-8
   Barth PG, 1998, NEUROMUSCULAR DISORD, V8, P296, DOI 10.1016/S0960-8966(98)00028-5
   Bowles J, 2000, DEV BIOL, V227, P239, DOI 10.1006/dbio.2000.9883
   CLEPET C, 1993, HUM MOL GENET, V2, P2007, DOI 10.1093/hmg/2.12.2007
   Collignon J, 1996, DEVELOPMENT, V122, P509
   CONNER F, 1994, NUCLEIC ACIDS RES, V22, P3339, DOI 10.1093/nar/22.16.3339
   CONNOR F, 1995, NUCLEIC ACIDS RES, V23, P3365, DOI 10.1093/nar/23.17.3365
   DUGAICZYK A, 1975, J MOL BIOL, V96, P171, DOI 10.1016/0022-2836(75)90189-8
   FERRARI S, 1992, EMBO J, V11, P4497, DOI 10.1002/j.1460-2075.1992.tb05551.x
   GUBBAY J, 1990, NATURE, V346, P245, DOI 10.1038/346245a0
   HACKER A, 1995, DEVELOPMENT, V121, P1603
   Hagiwara N, 2000, P NATL ACAD SCI USA, V97, P4180, DOI 10.1073/pnas.97.8.4180
   Hargrave M, 2000, HUM GENET, V106, P432, DOI 10.1007/s004390000266
   Jay P, 1997, HUM MOL GENET, V6, P1069, DOI 10.1093/hmg/6.7.1069
   JAY P, 1995, GENOMICS, V29, P541, DOI 10.1006/geno.1995.9970
   Kanai Y, 1996, J CELL BIOL, V133, P667, DOI 10.1083/jcb.133.3.667
   KLEVER M, 1991, HUM GENET, V86, P484
   Lefebvre V, 1998, EMBO J, V17, P5718, DOI 10.1093/emboj/17.19.5718
   Morris GE, 1999, HUM MOL GENET, V8, P1847, DOI 10.1093/hmg/8.10.1847
   PABO CO, 1992, ANNU REV BIOCHEM, V61, P1053, DOI 10.1146/annurev.bi.61.070192.005201
   PEARSONWHITE SH, 1991, NUCLEIC ACIDS RES, V19, P1148, DOI 10.1093/nar/19.5.1148
   Pevny LH, 1997, CURR OPIN GENET DEV, V7, P338, DOI 10.1016/S0959-437X(97)80147-5
   Pingault V, 1998, NAT GENET, V18, P171, DOI 10.1038/ng0298-171
   Roose J, 1999, GENOMICS, V57, P301, DOI 10.1006/geno.1999.5779
   SCHILHAM MW, 1993, NUCLEIC ACIDS RES, V21, P2009, DOI 10.1093/nar/21.8.2009
   SHAPIRO MB, 1987, NUCLEIC ACIDS RES, V15, P7155, DOI 10.1093/nar/15.17.7155
   Shehata BM, 1998, PEDIATR DEVEL PATHOL, V1, P56, DOI 10.1007/s100249900007
   SINCLAIR AH, 1990, NATURE, V346, P240, DOI 10.1038/346240a0
   TAKAMATSU N, 1995, MOL CELL BIOL, V15, P3759
   VANDEWETERING M, 1993, EMBO J, V12, P3847, DOI 10.1002/j.1460-2075.1993.tb06063.x
   Wegner M, 1999, NUCLEIC ACIDS RES, V27, P1409, DOI 10.1093/nar/27.6.1409
   Werner MH, 1997, CELL, V88, P733, DOI 10.1016/S0092-8674(00)81917-0
   WHITFIELD LS, 1993, NATURE, V364, P713, DOI 10.1038/364713a0
   Wilke CM, 1996, HUM MOL GENET, V5, P187, DOI 10.1093/hmg/5.2.187
   WOLFFE AP, 1994, SCIENCE, V264, P1100, DOI 10.1126/science.8178167
   WRIGHT E, 1995, NAT GENET, V9, P15, DOI 10.1038/ng0195-15
   Wunderle VM, 1996, GENOMICS, V36, P354, DOI 10.1006/geno.1996.0474
   Yamashita A, 2000, FEBS LETT, V481, P147, DOI 10.1016/S0014-5793(00)01987-6
NR 39
TC 40
Z9 45
U1 0
U2 3
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 0378-1119
EI 1879-0038
J9 GENE
JI Gene
PD MAR 7
PY 2001
VL 265
IS 1-2
BP 157
EP 164
DI 10.1016/S0378-1119(01)00346-8
PG 8
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA 415WX
UT WOS:000167747500017
PM 11255018
DA 2025-04-10
ER

PT J
AU Franz, WM
   Müller, M
   Müller, OJ
   Herrmann, R
   Rothmann, T
   Cremer, M
   Cohn, RD
   Voit, T
   Katus, HA
AF Franz, WM
   Müller, M
   Müller, OJ
   Herrmann, R
   Rothmann, T
   Cremer, M
   Cohn, RD
   Voit, T
   Katus, HA
TI Association of nonsense mutation of dystrophin gene with disruption of
   sarcoglycan complex in X-linked dilated cardiomyopathy
SO LANCET
LA English
DT Article
ID DUCHENNE MUSCULAR-DYSTROPHY; GLYCOPROTEIN; IDENTIFICATION; ORGANIZATION;
   DEFICIENCY; COMPONENT; DELETION; LINKAGE; FAMILY; REGION
AB Background In a systematic analysis of inherited forms of cardiomyopathy, we previously identified a family with X-linked dilated cardiomyopathy characterised by a mutation in the rod region of dystrophin. We have now attempted to eludicate the genetic mechanism involved in this disease, as well as the role of dystrophin-associated glycoproteins.
   Methods The affected dystrophin epitope, which lacks binding to the dys-1 antibody, was analysed by single-strand conformation polymorphism analysis, reverse-transcription PCR, and DNA sequencing. Effects on dystrophin-associated glycoproteins were studied by immunohistochemistry and western blotting.
   Findings A translation-termination mutation (C4148T) in exon 29 of the dystrophin gene was found in all affected family members. Alternative splicing rescued the reading frame and led to the expression of a dystrophin molecule lacking 50 aminoacids both in cardiac and skeletal muscle. Immunohistochemical analysis of the dystrophin-associated proteins revealed a reduction of beta-sarcoglycan and delta-sarcoglycan in the sarcolemma of cardiac muscle but not skeletal muscle tissue. However, western blotting revealed similar amounts of sarcoglycan subunits in both tissues.
   Interpretation The molecular mechanism of this subtype of X-linked cardiomyopathy may be explained by a conformational change in exon-29-deleted dystrophin, resulting in disruption of the sarcoglycan assembly in heart muscle but not skeletal muscle.
C1 Med Univ Lubeck, Med Klin 2, Lubeck, Germany.
   Univ Essen Gesamthsch, Kinderklin, Essen, Germany.
   Deutsch Krebsforschungszentrum, Heidelberg, Germany.
   Univ Heidelberg, Dept Human Genet, D-6900 Heidelberg, Germany.
C3 University of Lubeck; University of Duisburg Essen; Helmholtz
   Association; German Cancer Research Center (DKFZ); Ruprecht Karls
   University Heidelberg
RP Franz, WM (corresponding author), Med Univ Lubeck, Med Klin 2, D-23538 Lubeck, Germany.
RI Cohn, Ronald/AAC-5835-2021; Müller, Oliver/H-4739-2016; Cremer,
   Marion/P-8524-2014
OI Cremer, Marion/0000-0002-1830-9589; Muller, Mathias/0000-0002-7879-3552
CR Badorff C, 1999, NAT MED, V5, P320, DOI 10.1038/6543
   Beggs AH, 1997, CIRCULATION, V95, P2344, DOI 10.1161/01.CIR.95.10.2344
   Bies RD, 1997, J MOL CELL CARDIOL, V29, P3175, DOI 10.1006/jmcc.1997.0568
   CAMPBELL KP, 1995, CELL, V80, P675, DOI 10.1016/0092-8674(95)90344-5
   Chan YM, 1998, J CELL BIOL, V143, P2033, DOI 10.1083/jcb.143.7.2033
   ENGLAND SB, 1990, NATURE, V343, P180, DOI 10.1038/343180a0
   ENGLAND SB, 1992, NEW ENGL J MED, V326, P77
   Fadic R, 1996, NEW ENGL J MED, V334, P362, DOI 10.1056/NEJM199602083340604
   Ferlini A, 1998, AM J HUM GENET, V63, P436, DOI 10.1086/301952
   FRANZ WM, 1995, ANN NY ACAD SCI, V752, P470, DOI 10.1111/j.1749-6632.1995.tb17457.x
   Grünig E, 1998, J AM COLL CARDIOL, V31, P186, DOI 10.1016/S0735-1097(97)00434-8
   HUNSAKER RH, 1982, AM J MED, V73, P235, DOI 10.1016/0002-9343(82)90184-X
   Jung D, 1996, J BIOL CHEM, V271, P32321, DOI 10.1074/jbc.271.50.32321
   KOENIG M, 1990, J BIOL CHEM, V265, P4560
   KOENIG M, 1987, CELL, V50, P509, DOI 10.1016/0092-8674(87)90504-6
   LIM LE, 1995, NAT GENET, V11, P257, DOI 10.1038/ng1195-257
   Melacini P, 1996, CIRCULATION, V94, P3168, DOI 10.1161/01.CIR.94.12.3168
   Meng HP, 1996, J BIOL CHEM, V271, P12364, DOI 10.1074/jbc.271.21.12364
   MUNTONI F, 1995, J CLIN INVEST, V96, P693, DOI 10.1172/JCI118112
   MUNTONI F, 1993, NEW ENGL J MED, V329, P921, DOI 10.1056/NEJM199309233291304
   Nigro V, 1996, HUM MOL GENET, V5, P1179, DOI 10.1093/hmg/5.8.1179
   Nigro V, 1997, HUM MOL GENET, V6, P601, DOI 10.1093/hmg/6.4.601
   Olson TM, 1998, SCIENCE, V280, P750, DOI 10.1126/science.280.5364.750
   OrtizLopez R, 1997, CIRCULATION, V95, P2434, DOI 10.1161/01.CIR.95.10.2434
   PALEK J, 1990, SEMIN HEMATOL, V27, P290
   PRIOR TW, 1995, AM J HUM GENET, V57, P22
   Rybakova IN, 1996, J CELL BIOL, V135, P661, DOI 10.1083/jcb.135.3.661
   Shiga N, 1997, J CLIN INVEST, V100, P2204, DOI 10.1172/JCI119757
   Stevenson S, 1997, CIRC RES, V80, P269, DOI 10.1161/01.RES.80.2.269
   TOWBIN JA, 1993, CIRCULATION, V87, P1854, DOI 10.1161/01.CIR.87.6.1854
   VOIT T, 1989, J NEUROL SCI, V89, P199, DOI 10.1016/0022-510X(89)90022-1
   WATAKABE A, 1993, GENE DEV, V7, P407, DOI 10.1101/gad.7.3.407
   YOSHIDA K, 1993, MUSCLE NERVE, V16, P1161, DOI 10.1002/mus.880161104
NR 33
TC 33
Z9 40
U1 0
U2 2
PU LANCET LTD
PI LONDON
PA 84 THEOBALDS RD, LONDON WC1X 8RR, ENGLAND
SN 0140-6736
J9 LANCET
JI Lancet
PD MAY 20
PY 2000
VL 355
IS 9217
BP 1781
EP 1785
DI 10.1016/S0140-6736(00)02266-2
PG 5
WC Medicine, General & Internal
WE Science Citation Index Expanded (SCI-EXPANDED)
SC General & Internal Medicine
GA 315RE
UT WOS:000087126100013
PM 10832829
DA 2025-04-10
ER

PT J
AU Zhang, KQ
   Demeure, O
   Belliard, A
   Goujon, JM
   Favreau, F
   Desurmont, T
   Mauco, G
   Barrière, M
   Carretier, M
   Milan, D
   Papadopoulos, V
   Hauet, T
AF Zhang, Keqiang
   Demeure, Olivier
   Belliard, Aude
   Goujon, Jean-Michel
   Favreau, Frederic
   Desurmont, Thibault
   Mauco, Gerard
   Barriere, Michel
   Carretier, Michel
   Milan, Denis
   Papadopoulos, Vassilios
   Hauet, Thierry
TI Cloning, sequencing, and chromosomal localization of pig peripheral
   benzodiazepine receptor:: three different forms produced by alternative
   splicing
SO MAMMALIAN GENOME
LA English
DT Article
ID CHOLESTEROL TRANSPORT; RAT-KIDNEY; EXPRESSION; BINDING; PORCINE;
   CONSTRUCTION; GENE
AB We report the molecular cloning of the cDNA sequence for pig peripheral benzodiazepine receptor (PBR) by using RT-PCR and 5'/3' terminal extension. Three different transcripts (long, middle, and short) are identified. The open reading frame (ORF) of the longest PBR mRNA encodes a deduced polypeptide of 169 amino acids with a calculated molecular weight of 18,609 Da and an estimated pI of 9.70, which corresponds to the authentic PBR of other mammalian species. The middle transcript (PBR-M) contains a 141-codon ORF, which is consistent with that of the authentic PBR, but lacks a region of 84 bp so that its encoded polypeptide lacks a region of 28 amino acids from 35 to 62 of the authentic PBR polypeptide. The short transcript (PBR-S) contains a 104-codon ORF, which overlaps that of the authentic PBR, but lacks a region of 211 bp so that its encoded polypeptide lacks a region of 65 amino acids of the N-terminal of the authentic PBR. The pig PBR gene was mapped to the telomeric end of SSC5p. In addition, PBR mRNA was the more abundant detected form in pig tissues and in warm kidney that underwent ischemia suggesting functional implications of PBR during the renal repair process.
C1 CHU Poitiers, ERM 324, INSERM, F-86021 Poitiers, France.
   Univ Poitiers, Fac Med, F-86000 Poitiers, France.
   INRA, Lab Genet Cellulaire, F-31326 Castanet Tolosan, France.
   INRA, Lab Transplantat Expt, F-17000 Surgeres, France.
   Georgetown Univ, Dept Biochem & Mol Biol, Sch Med, Washington, DC 20057 USA.
C3 Universite de Poitiers; CHU Poitiers; Institut National de la Sante et
   de la Recherche Medicale (Inserm); Universite de Poitiers; CHU Poitiers;
   INRAE; INRAE; Georgetown University
RP Hauet, T (corresponding author), CHU Poitiers, ERM 324, INSERM, Rue Miletrie,BP 577, F-86021 Poitiers, France.
EM t.hauet@chu-poitiers.fr
RI Zhang, Keqiang/P-7082-2019; Papadopoulos, Vassilios/AAI-2613-2019;
   Hauet, Thierry/AAC-9277-2021; Mauco, Gerard/A-3164-2016
OI Papadopoulos, Vassilios/0000-0002-1183-8568; Hauet,
   Thierry/0000-0002-0117-071X
CR ANHOLT RRH, 1986, J BIOL CHEM, V261, P576
   Bribes E, 2002, J AM SOC NEPHROL, V13, P1, DOI 10.1681/ASN.V1311
   Casellas P, 2002, NEUROCHEM INT, V40, P475, DOI 10.1016/S0197-0186(01)00118-8
   Dalla Valle L, 2004, J STEROID BIOCHEM, V91, P49, DOI 10.1016/j.jsbmb.2004.01.008
   Faure JP, 2002, J PHARMACOL EXP THER, V302, P861, DOI 10.1124/jpet.102.033688
   Gavish M, 1999, PHARMACOL REV, V51, P629
   Goureau A, 1996, GENOMICS, V36, P252, DOI 10.1006/geno.1996.0460
   Joseph-Liauzun E, 1998, J BIOL CHEM, V273, P2146, DOI 10.1074/jbc.273.4.2146
   KYTE J, 1982, J MOL BIOL, V157, P105, DOI 10.1016/0022-2836(82)90515-0
   Lacapère JJ, 2003, STEROIDS, V68, P569, DOI 10.1016/S0039-128X(03)00101-6
   Li H, 1998, ENDOCRINOLOGY, V139, P4991, DOI 10.1210/en.139.12.4991
   Li H, 2001, P NATL ACAD SCI USA, V98, P1267, DOI 10.1073/pnas.031461598
   LIN D, 1993, GENOMICS, V18, P643, DOI 10.1016/S0888-7543(05)80367-2
   LINDEMANN P, 1999, MOL STEROIDOGENESIS, P297
   MCENERY MW, 1992, P NATL ACAD SCI USA, V89, P3170, DOI 10.1073/pnas.89.8.3170
   Milan D, 2000, BIOINFORMATICS, V16, P558, DOI 10.1093/bioinformatics/16.6.558
   PAPADOPOULOS V, 1993, ENDOCR REV, V14, P222, DOI 10.1210/er.14.2.222
   Papadopoulos V, 2004, ENDOCR RES, V30, P677, DOI 10.1081/ERC-200043971
   Papadopoulos V, 1997, STEROIDS, V62, P21, DOI 10.1016/S0039-128X(96)00154-7
   PAROLA AL, 1991, J BIOL CHEM, V266, P14082
   Quintanilla R, 2003, J ANIM SCI, V81, P385
   Rink A, 2002, MAMM GENOME, V13, P578, DOI 10.1007/s00335-002-2192-5
   Rochard P, 2004, GENE EXPRESSION, V12, P13, DOI 10.3727/000000004783992170
   Rogel-Gaillard C, 1999, CYTOGENET CELL GENET, V85, P205, DOI 10.1159/000015294
   SPRENGEL R, 1989, J BIOL CHEM, V264, P20415
   TAKETANI S, 1994, J BIOL CHEM, V269, P7527
   Veenman L, 2006, PHARMACOL THERAPEUT, V110, P503, DOI 10.1016/j.pharmthera.2005.09.007
   Yeliseev AA, 2000, J BIOL CHEM, V275, P5657, DOI 10.1074/jbc.275.8.5657
   Yerle M, 1998, CYTOGENET CELL GENET, V82, P182, DOI 10.1159/000015095
NR 29
TC 8
Z9 11
U1 0
U2 1
PU SPRINGER
PI NEW YORK
PA ONE NEW YORK PLAZA, SUITE 4600, NEW YORK, NY, UNITED STATES
SN 0938-8990
EI 1432-1777
J9 MAMM GENOME
JI Mamm. Genome
PD OCT
PY 2006
VL 17
IS 10
BP 1050
EP 1062
DI 10.1007/s00335-006-0022-x
PG 13
WC Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology;
   Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology;
   Genetics & Heredity
GA 093JS
UT WOS:000241165200007
PM 17019653
DA 2025-04-10
ER

PT J
AU Pichiule, P
   Chávez, JC
   Xu, K
   LaManna, JC
AF Pichiule, P
   Chávez, JC
   Xu, K
   LaManna, JC
TI Vascular endothelial growth factor upregulation in transient global
   ischemia induced by cardiac arrest and resuscitation in rat brain
SO MOLECULAR BRAIN RESEARCH
LA English
DT Article
DE angiogenic factor; reperfusion injury; vascular permeability factor
ID MIDDLE CEREBRAL-ARTERY; FACTOR MESSENGER-RNA; PERMEABILITY FACTOR;
   FACTOR EXPRESSION; FACTOR GENE; IN-VIVO; TUMOR ANGIOGENESIS; BLOOD-FLOW;
   HYPOXIA; EDEMA
AB This study examined vascular endothelial growth factor (VEGF) expression in rat brain after reversible global cerebral ischemia produced by cardiac arrest and resuscitation. Three alternative splicing forms, VEGF(188), VEGF(164) and VEGF(120), were observed in cortex, hippocampus and brainstem by RT-PCR analysis. After 24 h of recovery from cardiac arrest, mRNA levels corresponding to VEGF(188) and VEGF(164) were significantly increased by about double in all the regions analyzed. These mRNA levels remained elevated at 24 and 48 h of recovery but returned to basal expression after 7 days of recovery. Changes in VEGF(120) expression after cardiac arrest did not reach statistical significance. VEGF protein expression measured by Western blot was also increased by about double at 24 and 48 h of recovery but returned to control levels after 7 days of recovery. VEGF immunohistochemistry localized this increased expression mostly associated with astrocytes. Considering its biological activity, VEGF induction after cardiac arrest and resuscitation may be responsible for the increased vascular permeability and the resultant vasogenic edema, found 24-48 h after reversible global ischemia. (C) 1999 Elsevier Science B.V. All rights reserved.
C1 Case Western Reserve Univ, Sch Med, Dept Neurol, Cleveland, OH 44106 USA.
   Case Western Reserve Univ, Sch Med, Dept Anat, Cleveland, OH 44106 USA.
C3 University System of Ohio; Case Western Reserve University; University
   System of Ohio; Case Western Reserve University
RP LaManna, JC (corresponding author), Case Western Reserve Univ, Sch Med, Dept Neurol, 10900 Euclid Ave, Cleveland, OH 44106 USA.
RI LaManna, Joseph/C-3347-2012; LaManna, Joseph Charles/D-3860-2013
OI LaManna, Joseph Charles/0000-0002-0159-4512
FU NINDS NIH HHS [NS37111] Funding Source: Medline
CR BACIC M, 1995, GROWTH FACTORS, V12, P11, DOI 10.3109/08977199509003209
   Cobbs CS, 1998, NEUROSCI LETT, V249, P79, DOI 10.1016/S0304-3940(98)00377-2
   CONN G, 1990, P NATL ACAD SCI USA, V87, P2628, DOI 10.1073/pnas.87.7.2628
   CRUMRINE RC, 1991, J CEREBR BLOOD F MET, V11, P272, DOI 10.1038/jcbfm.1991.59
   Dibbens JA, 1999, MOL BIOL CELL, V10, P907, DOI 10.1091/mbc.10.4.907
   Dobrogowska DH, 1998, J NEUROCYTOL, V27, P163, DOI 10.1023/A:1006907608230
   Feng D, 1996, J EXP MED, V183, P1981, DOI 10.1084/jem.183.5.1981
   Ferrara N, 1997, ENDOCR REV, V18, P4, DOI 10.1210/er.18.1.4
   Forsythe JA, 1996, MOL CELL BIOL, V16, P4604
   Goldman CK, 1997, NEUROSURGERY, V40, P1269, DOI 10.1097/00006123-199706000-00029
   Guo Y, 1997, J NEUROSCI RES, V49, P89, DOI 10.1002/(SICI)1097-4547(19970701)49:1<89::AID-JNR10>3.0.CO;2-#
   Hayashi T, 1997, STROKE, V28, P2039, DOI 10.1161/01.STR.28.10.2039
   Hippenstiel S, 1998, AM J PHYSIOL-LUNG C, V274, pL678, DOI 10.1152/ajplung.1998.274.5.L678
   Kalaria RN, 1998, MOL BRAIN RES, V62, P101, DOI 10.1016/S0169-328X(98)00190-9
   Kalkanis SN, 1996, J NEUROSURG, V85, P1095, DOI 10.3171/jns.1996.85.6.1095
   Kovacs Z, 1996, STROKE, V27, P1865, DOI 10.1161/01.STR.27.10.1865
   Kuo NT, 1999, J APPL PHYSIOL, V86, P260, DOI 10.1152/jappl.1999.86.1.260
   Kuroki M, 1996, J CLIN INVEST, V98, P1667, DOI 10.1172/JCI118962
   LAMANNA J C, 1985, Neurological Research, V7, P161
   LAMANNA JC, 1988, EXP NEUROL, V101, P234, DOI 10.1016/0014-4886(88)90007-6
   LAMANNA JC, 1995, BRAIN RES, V687, P175, DOI 10.1016/0006-8993(95)00516-S
   Lauro KL, 1999, BRAIN RES, V831, P64, DOI 10.1016/S0006-8993(99)01394-3
   Lennmyr F, 1998, J NEUROPATH EXP NEUR, V57, P874, DOI 10.1097/00005072-199809000-00009
   LEVY AP, 1995, J BIOL CHEM, V270, P13333, DOI 10.1074/jbc.270.22.13333
   Levy AP, 1996, J BIOL CHEM, V271, P2746, DOI 10.1074/jbc.271.5.2746
   Li J, 1996, AM J PHYSIOL-HEART C, V270, pH1803, DOI 10.1152/ajpheart.1996.270.5.H1803
   Marti HH, 1998, P NATL ACAD SCI USA, V95, P15809, DOI 10.1073/pnas.95.26.15809
   MILLER JW, 1994, AM J PATHOL, V145, P574
   MONACCI WT, 1993, AM J PHYSIOL, V264, pC995, DOI 10.1152/ajpcell.1993.264.4.C995
   MURATA T, 1995, OPHTHALMIC RES, V27, P48, DOI 10.1159/000267567
   Neufeld G, 1999, FASEB J, V13, P9, DOI 10.1096/fasebj.13.1.9
   PLUTA R, 1994, BRAIN RES, V633, P41, DOI 10.1016/0006-8993(94)91520-2
   Provias J, 1997, NEUROSURGERY, V40, P1016, DOI 10.1097/00006123-199705000-00027
   ROBERTS WG, 1995, J CELL SCI, V108, P2369
   Rosenstein JM, 1998, P NATL ACAD SCI USA, V95, P7086, DOI 10.1073/pnas.95.12.7086
   Satake S, 1998, BIOL CELL, V90, P161, DOI 10.1016/S0248-4900(98)80337-7
   Schmitz B, 1997, J CEREBR BLOOD F MET, V17, P1202, DOI 10.1097/00004647-199711000-00009
   SENGER DR, 1983, SCIENCE, V219, P983, DOI 10.1126/science.6823562
   SHWEIKI D, 1992, NATURE, V359, P843, DOI 10.1038/359843a0
   SHWEIKI D, 1995, P NATL ACAD SCI USA, V92, P768, DOI 10.1073/pnas.92.3.768
   STEIN I, 1995, MOL CELL BIOL, V15, P5363
   STRUGAR J, 1994, J NEUROSURG, V81, P560, DOI 10.3171/jns.1994.81.4.0560
   Thomas KA, 1996, J BIOL CHEM, V271, P603, DOI 10.1074/jbc.271.2.603
   Wang W, 1996, AM J PHYSIOL-CELL PH, V271, pC1973, DOI 10.1152/ajpcell.1996.271.6.C1973
   WISNIEWSKI HM, 1995, ACTA NEUROPATHOL, V90, P432
   Xu FP, 1998, J APPL PHYSIOL, V85, P53, DOI 10.1152/jappl.1998.85.1.53
NR 46
TC 50
Z9 61
U1 0
U2 0
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 0169-328X
J9 MOL BRAIN RES
JI Mol. Brain Res.
PD DEC 10
PY 1999
VL 74
IS 1-2
BP 83
EP 90
DI 10.1016/S0169-328X(99)00261-2
PG 8
WC Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA 269WA
UT WOS:000084499500008
PM 10640678
DA 2025-04-10
ER

PT J
AU Mori, M
   Yamagata, T
   Mori, Y
   Nokubi, M
   Saito, K
   Fukushima, Y
   Momoi, MY
AF Mori, M
   Yamagata, T
   Mori, Y
   Nokubi, M
   Saito, K
   Fukushima, Y
   Momoi, MY
TI Elastic fiber degeneration in Costello syndrome
SO AMERICAN JOURNAL OF MEDICAL GENETICS
LA English
DT Article
DE Costello syndrome; elastic fiber disruption; elastin; arrhythmia;
   rhabdomyolysis
ID CUTIS-LAXA; GENE-EXPRESSION; FIBROBLASTS; DELINEATION; PEPTIDE
AB Clinical and pathological observations of a 6-month-old-boy with Costello syndrome are reported. The main clinical findings were loose skin of the neck, hands, and feet, deep palmar and plantar creases, typical ''coarse'' face with thick lips and macroglossia, relative macrocephaly, mental retardation, short stature, arrhythmia, large size for gestational age, and poor feeding. At age 6 months he died of rhabdomyolysis. The major pathological findings were fine, disrupted, and loosely-constructed elastic fibers in the skin, tongue, pharynx, larynx, and upper esophagus, but not in the bronchi, alveoli, aorta, or coronary arteries. Hyperplasia of collagen fibers in the skin, hyperplasia of the mucous glands in the bronchus, narrowing of the pulmonary artery, degeneration of the atrial conduction system, calcification and ballooning of skeletal muscle fibers with infiltration of macrophages, and myoglobin depositions in the collecting ducts in the kidney were also observed. The degeneration of elastic fibers was confirmed in the skin of a second Costello syndrome patient. Expression of elastin mRNA in the patient's fibroblasts was normal in size and amount; Given that elastic fiber degeneration was observed in the tissues with clinical symptoms, we speculate that a defect of elastic fibers, possibly relating to alternative splicing in the elastin gene or to defects in elastin microfibrils, might be involved in the pathogenesis of Costello syndrome. (C) 1996 Wiley-Liss, Inc.
C1 JICHI MED SCH,DEPT PEDIAT,MINAMI KAWACHI,TOCHIGI 32904,JAPAN.
   JICHI MED SCH,DEPT PATHOL,MINAMI KAWACHI,TOCHIGI 32904,JAPAN.
   SAITAMA CHILDRENS MED CTR,DIV MED GENET,IWATSUKI,SAITAMA,JAPAN.
C3 Jichi Medical University; Jichi Medical University; Saitama Children's
   Medical Center
CR BERBERICH MS, 1991, P GREENWOOD GENET CT, V10, P78
   BLOOD CH, 1988, J CELL BIOL, V107, P1987, DOI 10.1083/jcb.107.5.1987
   BOROCHOWITZ Z, 1992, AM J MED GENET, V43, P678, DOI 10.1002/ajmg.1320430405
   COSTELLO JM, 1977, AUST PAEDIATR J, V13, P114
   DAVIES SJ, 1994, J MED GENET, V31, P486, DOI 10.1136/jmg.31.6.486
   DERKALOUSTIAN VM, 1991, AM J MED GENET, V41, P69, DOI 10.1002/ajmg.1320410118
   DIROCCO M, 1993, AM J MED GENET, V47, P1135
   EWART AK, 1993, NAT GENET, V5, P11, DOI 10.1038/ng0993-11
   HALL BB, 1990, P GREENWOOD GENET CT, V9, P103
   HATAMOCHI A, 1991, J INVEST DERMATOL, V97, P483, DOI 10.1111/1523-1747.ep12481519
   INDIK Z, 1987, P NATL ACAD SCI USA, V84, P5680, DOI 10.1073/pnas.84.16.5680
   IZUMIKAWA Y, 1993, JPN J HUM GENET, V38, P329, DOI 10.1007/BF01874143
   JOHNSON JP, 1993, P GREENWOOD GENET CT, V12, P96
   KONDO I, 1993, JPN J HUM GENET, V38, P433, DOI 10.1007/BF01907991
   LONG MM, 1988, BIOCHIM BIOPHYS ACTA, V968, P300, DOI 10.1016/0167-4889(88)90021-3
   MARTIN RA, 1991, AM J MED GENET, V41, P346, DOI 10.1002/ajmg.1320410316
   OKAMOTO N, 1994, HUM GENET, V93, P605
   OLSEN DR, 1988, J BIOL CHEM, V263, P6465
   PATTON MA, 1993, J MED GENET, V30, P622, DOI 10.1136/jmg.30.7.622
   PHILIP N, 1993, AM J MED GENET, V47, P174, DOI 10.1002/ajmg.1320470209
   POPE FM, 1993, HERITABLE DISORDERS, P253
   SAY B, 1993, AM J MED GENET, V47, P163, DOI 10.1002/ajmg.1320470203
   SENIOR RM, 1984, J CELL BIOL, V99, P870, DOI 10.1083/jcb.99.3.870
   SEPHEL GC, 1989, J INVEST DERMATOL, V93, P147, DOI 10.1111/1523-1747.ep12277389
   TEEBI AS, 1993, AM J MED GENET, V47, P166, DOI 10.1002/ajmg.1320470204
   YOSHIDA R, 1993, JPN J HUM GENET, V38, P437, DOI 10.1007/BF01907992
   ZAMPINO G, 1993, AM J MED GENET, V47, P176, DOI 10.1002/ajmg.1320470210
NR 27
TC 48
Z9 50
U1 0
U2 0
PU WILEY-LISS
PI NEW YORK
PA DIV JOHN WILEY & SONS INC 605 THIRD AVE, NEW YORK, NY 10158-0012
SN 0148-7299
J9 AM J MED GENET
JI Am. J. Med. Genet.
PD FEB 2
PY 1996
VL 61
IS 4
BP 304
EP 309
DI 10.1002/(SICI)1096-8628(19960202)61:4<304::AID-AJMG2>3.0.CO;2-U
PG 6
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA UP990
UT WOS:A1996UP99000002
PM 8834040
DA 2025-04-10
ER

PT J
AU Flück, CE
   Meyer-Böni, M
   Pandey, AV
   Kempná, P
   Miller, WL
   Schoenle, EJ
   Biason-Lauber, A
AF Flueck, Christa E.
   Meyer-Boeni, Monika
   Pandey, Amit V.
   Kempna, Petra
   Miller, Walter L.
   Schoenle, Eugen J.
   Biason-Lauber, Anna
TI Why Boys Will Be Boys: Two Pathways of Fetal Testicular Androgen
   Biosynthesis Are Needed for Male Sexual Differentiation
SO AMERICAN JOURNAL OF HUMAN GENETICS
LA English
DT Article
ID TYPE-3 3-ALPHA-HYDROXYSTEROID DEHYDROGENASE; KETO REDUCTASE SUPERFAMILY;
   ANTLEY-BIXLER-SYNDROME; CYTOCHROME-P450 OXIDOREDUCTASE DEFICIENCY;
   STEROID 17-ALPHA-HYDROXYLASE/17,20 LYASE; ISOLATED 17,20-LYASE
   DEFICIENCY; CONGENITAL ADRENAL-HYPERPLASIA; MUTANT P450 OXIDOREDUCTASE;
   DIHYDRODIOL DEHYDROGENASE; HYDROXYSTEROID DEHYDROGENASE
AB Human sexual determination is initiated by a cascade of genes that lead to the development of the fetal gonad. Whereas development of the female external genitalia does not require fetal ovarian hormones, male genital development requires the action of testicular testosterone and its more potent derivative dihydrotestosterone (DHT). The "classic" biosynthetic pathway from cholesterol to testosterone in the testis and the subsequent conversion of testosterone to DHT in genital skin is well established. Recently, an alternative pathway leading to DHT has been described in marsupials, but its potential importance to human development is unclear. AKR1C2 is an enzyme that participates in the alternative but not the classic pathway. Using a candidate gene approach, we identified AKR1C2 mutations with sex-limited recessive inheritance in four 46,XY individuals with disordered sexual development (DSD). Analysis of the inheritance of microsatellite markers excluded other candidate loci. Affected individuals had moderate to severe undervirilization at birth; when recreated by site-directed mutagenesis and expressed in bacteria, the mutant AKR1C2 had diminished but not absent catalytic activities. The 46,XY DSD individuals also carry a mutation causing aberrant splicing in AKR1C4, which encodes an enzyme with similar activity. This suggests a mode of inheritance where the severity of the developmental defect depends on the number of mutations in the two genes. An unrelated 46,XY DSD patient carried AKR1C2 mutations on both alleles, confirming the essential role of AKR1C2 and corroborating the hypothesis that both the classic and alternative pathways of testicular androgen biosynthesis are needed for normal human male sexual differentiation.
C1 [Flueck, Christa E.; Pandey, Amit V.; Kempna, Petra] Univ Bern, Univ Childrens Hosp Bern, Dept Pediat Endocrinol Diabetol & Metab, CH-3010 Bern, Switzerland.
   [Meyer-Boeni, Monika; Schoenle, Eugen J.; Biason-Lauber, Anna] Univ Childrens Hosp Zurich, Dept Pediat Endocrinol & Diabetol, CH-8032 Zurich, Switzerland.
   [Miller, Walter L.] Univ Calif San Francisco, Dept Pediat, Div Endocrinol, San Francisco, CA 94143 USA.
C3 University of Bern; University Hospital of Bern; University Children's
   Hospital Zurich; University of California System; University of
   California San Francisco
RP Flück, CE (corresponding author), Univ Bern, Univ Childrens Hosp Bern, Dept Pediat Endocrinol Diabetol & Metab, CH-3010 Bern, Switzerland.
EM christa.flueck@dkf.unibe.ch; anna.lauber@kispi.uzh.ch
RI Miller, Walter/J-3696-2012; Pandey, Amit/AAO-6442-2020; Pandey,
   Amit/A-7223-2008
OI Pandey, Amit/0000-0001-8331-5902; Flueck, Christa/0000-0002-4568-5504
FU Swiss National Science Foundation [31003A-130710, 320000-116636]; Swiss
   National Science Foundation (SNF) [31003A_130710] Funding Source: Swiss
   National Science Foundation (SNF)
FX This work was supported by the grants from the Swiss National Science
   Foundation (31003A-130710 to C.E.F. and 320000-116636 to A.B.L.). We
   thank Rock Breton for providing the human WT AKR1C2 expression vector,
   Synthia H Mellon for the generous gift of radiochemicals and George
   Thalmann for providing normal testes and adrenal tissues. We thank Gaby
   Hofer for excellent technical assistance.
CR Arlt W, 2004, LANCET, V363, P2128, DOI 10.1016/S0140-6736(04)16503-3
   Auchus RJ, 2004, TRENDS ENDOCRIN MET, V15, P432, DOI 10.1016/j.tem.2004.09.004
   Auchus RJ, 1998, J BIOL CHEM, V273, P3158, DOI 10.1074/jbc.273.6.3158
   Barbaccia ML, 1997, BRIT J PHARMACOL, V120, P1582, DOI 10.1038/sj.bjp.0701046
   Bennett MJ, 1996, BIOCHEMISTRY-US, V35, P10702, DOI 10.1021/bi9604688
   Bennett MJ, 1997, STRUCTURE, V5, P799, DOI 10.1016/S0969-2126(97)00234-7
   Biason-Lauber A, 2009, AM J HUM GENET, V84, P658, DOI 10.1016/j.ajhg.2009.03.016
   Biswas MG, 1997, J BIOL CHEM, V272, P15959, DOI 10.1074/jbc.272.25.15959
   Case DA, 2005, J COMPUT CHEM, V26, P1668, DOI 10.1002/jcc.20290
   CHUNG BC, 1987, P NATL ACAD SCI USA, V84, P407, DOI 10.1073/pnas.84.2.407
   Couture JF, 2005, PROTEIN SCI, V14, P1485, DOI 10.1110/ps.051353205
   Damborsky Jiri, 2007, Biotechnology Journal, V2, P62, DOI 10.1002/biot.200600208
   Desmet FO, 2009, NUCLEIC ACIDS RES, V37, DOI 10.1093/nar/gkp215
   Draper N, 2003, NAT GENET, V34, P434, DOI 10.1038/ng1214
   Dufort I, 1996, BIOCHEM BIOPH RES CO, V228, P474, DOI 10.1006/bbrc.1996.1684
   Dufort I, 2001, J CLIN ENDOCR METAB, V86, P841, DOI 10.1210/jc.86.2.841
   Flück CE, 2004, NAT GENET, V36, P228, DOI 10.1038/ng1300
   FRIEDRICH W, 1988, NIACIN NICOTINIC ACI
   Fukami M, 2005, J CLIN ENDOCR METAB, V90, P414, DOI 10.1210/jc.2004-0810
   Fukami M, 2009, J CLIN ENDOCR METAB, V94, P1723, DOI 10.1210/jc.2008-2816
   Geller DH, 1997, NAT GENET, V17, P201, DOI 10.1038/ng1097-201
   Ghayee Hans K., 2008, V13, P55, DOI 10.1159/000134780
   GLOCK GE, 1955, BIOCHEM J, V61, P388, DOI 10.1042/bj0610388
   GRINO PB, 1990, ENDOCRINOLOGY, V126, P1165, DOI 10.1210/endo-126-2-1165
   HAMMOND GL, 1977, J CLIN ENDOCR METAB, V45, P16, DOI 10.1210/jcem-45-1-16
   Hershkovitz E, 2008, J CLIN ENDOCR METAB, V93, P3584, DOI 10.1210/jc.2008-0051
   Homma K, 2006, J CLIN ENDOCR METAB, V91, P2643, DOI 10.1210/jc.2005-2460
   HOOG SS, 1994, P NATL ACAD SCI USA, V91, P2517, DOI 10.1073/pnas.91.7.2517
   Huang N, 2008, P NATL ACAD SCI USA, V105, P1733, DOI 10.1073/pnas.0711621105
   IMPERATOMCGINLEY J, 1991, CLIN ENDOCRINOL, V34, P293, DOI 10.1111/j.1365-2265.1991.tb03769.x
   ITO T, 1971, J CLIN INVEST, V50, P1621, DOI 10.1172/JCI106650
   Jin Y, 2001, BIOCHEMISTRY-US, V40, P10161, DOI 10.1021/bi010919a
   Jin Y, 2006, BIOCHEMISTRY-US, V45, P13054, DOI 10.1021/bi060591r
   KHANNA M, 1995, GENOMICS, V25, P588, DOI 10.1016/0888-7543(95)80066-U
   Kok RC, 2010, J CLIN ENDOCR METAB, V95, P994, DOI 10.1210/jc.2008-1745
   Královicová J, 2007, NUCLEIC ACIDS RES, V35, P6399, DOI 10.1093/nar/gkm680
   Krieger E, 2004, PROTEINS, V57, P678, DOI 10.1002/prot.20251
   Krieger E, 2006, J MOL GRAPH MODEL, V25, P481, DOI 10.1016/j.jmgm.2006.02.009
   Krieger E, 2009, PROTEINS, V77, P114, DOI 10.1002/prot.22570
   Kruglyak L, 1996, AM J HUM GENET, V58, P1347
   Lin HK, 1997, MOL ENDOCRINOL, V11, P1971, DOI 10.1210/me.11.13.1971
   Mahendroo M, 2004, MOL CELL ENDOCRINOL, V222, P113, DOI 10.1016/j.mce.2004.04.009
   Mendonca BB, 2009, CLIN ENDOCRINOL, V70, P173, DOI 10.1111/j.1365-2265.2008.03392.x
   Miller WL, 2011, ENDOCR REV, V32, P81, DOI 10.1210/er.2010-0013
   Ming JE, 2002, AM J HUM GENET, V71, P1017, DOI 10.1086/344412
   Nahoum V, 2001, J BIOL CHEM, V276, P42091, DOI 10.1074/jbc.M105610200
   NAKAJIN S, 1981, J BIOL CHEM, V256, P3871
   Pandey AV, 2007, MOL ENDOCRINOL, V21, P2579, DOI 10.1210/me.2007-0245
   Penning TM, 2000, BIOCHEM J, V351, P67, DOI 10.1042/0264-6021:3510067
   Penning TM, 2004, MOL CELL ENDOCRINOL, V215, P63, DOI 10.1016/j.mce.2003.11.006
   Penning TM, 1996, STEROIDS, V61, P508, DOI 10.1016/S0039-128X(96)00093-1
   PICADOLEONARD J, 1987, DNA-J MOLEC CELL BIO, V6, P439, DOI 10.1089/dna.1987.6.439
   Pollak N, 2007, J BIOL CHEM, V282, P33562, DOI 10.1074/jbc.M704442200
   QIN KN, 1993, J STEROID BIOCHEM, V46, P673, DOI 10.1016/0960-0760(93)90308-J
   QUIGLEY CA, 1992, J CLIN ENDOCR METAB, V74, P927, DOI 10.1210/jc.74.4.927
   Rizner TL, 2003, ENDOCRINOLOGY, V144, P2922, DOI 10.1210/en.2002-0032
   RUSSELL DW, 1994, ANNU REV BIOCHEM, V63, P25, DOI 10.1146/annurev.biochem.63.1.25
   Schneidman-Duhovny D, 2003, PROTEINS, V52, P107, DOI 10.1002/prot.10397
   Shackleton C, 2004, AM J MED GENET A, V129A, P105, DOI 10.1002/ajmg.a.30171
   Speiser PW, 2010, J CLIN ENDOCR METAB, V95, P4133, DOI 10.1210/jc.2009-2631
   Steckelbroeck S, 2004, J BIOL CHEM, V279, P10784, DOI 10.1074/jbc.M313308200
   Vockley J, 2000, MOL GENET METAB, V71, P10, DOI 10.1006/mgme.2000.3066
   Vollmer M, 1998, AM J HUM GENET, V63, P1724, DOI 10.1086/302162
   VRIEND G, 1990, J MOL GRAPHICS, V8, P52, DOI 10.1016/0263-7855(90)80070-V
   Wilson JD, 1999, BIOL REPROD, V61, P471, DOI 10.1095/biolreprod61.2.471
   Wilson JD, 1999, ENDOCR REV, V20, P726, DOI 10.1210/er.20.5.726
   Wilson JD, 2003, ENDOCRINOLOGY, V144, P575, DOI 10.1210/en.2002-220721
   WILSON JD, 1993, ENDOCR REV, V14, P577, DOI 10.1210/er.14.5.577
   WINTERS CJ, 1990, BIOCHEMISTRY-US, V29, P1080, DOI 10.1021/bi00456a034
   ZACHMANN M, 1972, Clinical Endocrinology, V1, P369, DOI 10.1111/j.1365-2265.1972.tb00407.x
   ZHANG LH, 1995, P NATL ACAD SCI USA, V92, P10619, DOI 10.1073/pnas.92.23.10619
NR 71
TC 176
Z9 185
U1 1
U2 16
PU CELL PRESS
PI CAMBRIDGE
PA 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA
SN 0002-9297
J9 AM J HUM GENET
JI Am. J. Hum. Genet.
PD AUG 12
PY 2011
VL 89
IS 2
BP 201
EP 218
DI 10.1016/j.ajhg.2011.06.009
PG 18
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA 810TA
UT WOS:000294148800001
PM 21802064
OA Bronze, Green Published
DA 2025-04-10
ER

PT J
AU Verma, SK
   Deshmukh, V
   Thatcher, K
   Belanger, KK
   Rhyner, AM
   Meng, S
   Holcomb, RJ
   Bressan, M
   Martin, JF
   Cooke, JP
   Wythe, JD
   Widen, SG
   Lincoln, J
   Kuyumcu-Martinez, MN
AF Verma, Sunil K.
   Deshmukh, Vaibhav
   Thatcher, Kaitlyn
   Belanger, KarryAnne K.
   Rhyner, Alexander M.
   Meng, Shu
   Holcomb, Richard Joshua
   Bressan, Michael
   Martin, James F.
   Cooke, John P.
   Wythe, Joshua D.
   Widen, Steven G.
   Lincoln, Joy
   Kuyumcu-Martinez, Muge N.
TI RBFOX2 is required for establishing RNA regulatory networks essential
   for heart development
SO NUCLEIC ACIDS RESEARCH
LA English
DT Article
ID CRYSTAL-STRUCTURE; RHO-GTPASES; COMPLEX; DEFECTS; ABI1; PROTEIN;
   ACTIVATION; MECHANISMS; REPRESSION; MYOCYTES
AB Human genetic studies identified a strong association between loss of function mutations in RBFOX2 and hypoplastic left heart syndrome (HLHS). There are currently no Rbfox2 mouse models that recapitulate HLHS. Therefore, it is still unknown how RBFOX2 as an RNA binding protein contributes to heart development. To address this, we conditionally deleted Rbfox2 in embryonic mouse hearts and found profound defects in cardiac chamber and yolk sac vasculature formation. Importantly, our Rbfox2 conditional knockout mouse model recapitulated several molecular and phenotypic features of HLHS. To determine the molecular drivers of these cardiac defects, we performed RNA-sequencing in Rbfox2 mutant hearts and identified dysregulated alternative splicing (AS) networks that affect cell adhesion to extracellular matrix (ECM) mediated by Rho GTPases. We identified two Rho GTPase cycling genes as targets of RBFOX2. Modulating AS of these two genes using antisense oligos led to cell cycle and cell-ECM adhesion defects. Consistently, Rbfox2 mutant hearts displayed cell cycle defects and inability to undergo endocardial-mesenchymal transition, processes dependent on cell-ECM adhesion and that are seen in HLHS. Overall, our work not only revealed that loss of Rbfox2 leads to heart development defects resembling HLHS, but also identified RBFOX2-regulated AS networks that influence cell-ECM communication vital for heart development.
C1 [Verma, Sunil K.; Belanger, KarryAnne K.; Holcomb, Richard Joshua; Widen, Steven G.; Kuyumcu-Martinez, Muge N.] Univ Texas Med Branch, Dept Biochem & Mol Biol, Galveston, TX 77555 USA.
   [Deshmukh, Vaibhav; Rhyner, Alexander M.; Martin, James F.; Wythe, Joshua D.] Baylor Coll Med, Dept Mol Physiol & Biophys, Houston, TX 77030 USA.
   [Thatcher, Kaitlyn; Lincoln, Joy] Med Coll Wisconsin, Herma Heart Inst, Dept Pediat, Div Pediat Cardiol,Childrens WI, Milwaukee, WI 53226 USA.
   [Rhyner, Alexander M.; Martin, James F.; Wythe, Joshua D.] Baylor Coll Med, Ctr Organ Repair & Renewal, Houston, TX 77030 USA.
   [Meng, Shu; Cooke, John P.] Houston Methodist Res Inst, Dept Cardiovasc Sci, Houston, TX 77030 USA.
   [Bressan, Michael] Univ N Carolina, Dept Cell Biol & Physiol, McAllister Heart Inst, Chapel Hill, NC 27599 USA.
   [Martin, James F.; Wythe, Joshua D.] Cardiomyocyte Renewal Lab, Houston, TX 77030 USA.
   [Martin, James F.; Wythe, Joshua D.] Texas Heart Inst, Houston, TX 77030 USA.
   [Kuyumcu-Martinez, Muge N.] Univ Texas Med Branch, Inst Translat Sci, Dept Neurosci Cell Biol & Anat, 301 Univ Blvd Galveston, Galveston, TX 77555 USA.
C3 University of Texas System; University of Texas Medical Branch
   Galveston; Baylor College of Medicine; Medical College of Wisconsin;
   Baylor College of Medicine; Houston Methodist; University of North
   Carolina; University of North Carolina Chapel Hill; Texas Heart
   Institute; University of Texas System; University of Texas Medical
   Branch Galveston
RP Kuyumcu-Martinez, MN (corresponding author), Univ Texas Med Branch, Dept Biochem & Mol Biol, Galveston, TX 77555 USA.; Kuyumcu-Martinez, MN (corresponding author), Univ Texas Med Branch, Inst Translat Sci, Dept Neurosci Cell Biol & Anat, 301 Univ Blvd Galveston, Galveston, TX 77555 USA.
EM nmmartin@utmb.edu
RI Deshmukh, Vaibhav/HPG-7012-2023; Wythe, Josh/IQW-7204-2023; Verma,
   Sunil/J-8838-2019
OI Wythe, Joshua/0000-0002-3225-2937; Holcomb, Richard
   Joshua/0000-0003-3455-4733
FU AHAGrant [15GRNT22830010, 20TPA35490206]; Additional Ventures Single
   Ventricle Research Fund [4873]; John Sealy Memorial Endowment Fund;
   NIH/NHLBI [1R01HL135031, 1R01HL132801, R01HL142685, R01HL146626,
   1R01HD099026-01, 1R01HL133254]; NIH [HL127717, HL130804, HL118761];
   Vivian L. Smith Foundation, Fondation LeDucq Transatlantic Networks of
   Excellence in Cardiovascular Research [14CVD01]; Cancer Prevention
   Institute of Texas grant [RP200619]; Eunice Kennedy Shriver National
   Institute of Child Health and Human Development [R01HD099026] Funding
   Source: NIH RePORTER; National Heart Lung and Blood Institute
   [R01HL133254, R01HL142685] Funding Source: NIH RePORTER; American Heart
   Association (AHA) [15GRNT22830010, 20TPA35490206] Funding Source:
   American Heart Association (AHA)
FX AHAGrant [15GRNT22830010, 20TPA35490206, in part], Additional Ventures
   Single Ventricle Research Fund [4873, in part], John Sealy Memorial
   Endowment Fund [in part] and [NIH/NHLBI [1R01HL135031 to M.N.K.-M.,
   1R01HL132801 and R01HL142685 to J.L., R01HL146626 to M.B,
   1R01HD099026-01, 1R01HL133254 to J.P.C.]; NIH [HL127717, HL130804,
   HL118761 to J.F.M.]; Vivian L. Smith Foundation, Fondation LeDucq
   Transatlantic Networks of Excellence in Cardiovascular Research
   [14CVD01] to J.F.M; Cancer Prevention Institute of Texas grant
   [RP200619, in part] to J.P.C; and Additional Ventures Single Ventricle
   Research Fund [4873, in part] to J.D.W. Funding for open access charge:
   John Sealy Memorial Endowment Fund.
CR Astrof S, 2007, DEV BIOL, V311, P11, DOI 10.1016/j.ydbio.2007.07.005
   Auweter SD, 2006, EMBO J, V25, P163, DOI 10.1038/sj.emboj.7600918
   Baraniak AP, 2006, MOL CELL BIOL, V26, P1209, DOI 10.1128/MCB.26.4.1209-1222.2006
   Benito-Jardón M, 2017, ELIFE, V6, DOI 10.7554/eLife.22264
   Bohlmeyer TJ, 2003, CARDIOVASC PATHOL, V12, P23, DOI 10.1016/S1054-8807(02)00127-8
   Braeutigam C, 2014, ONCOGENE, V33, P1082, DOI 10.1038/onc.2013.50
   Chen MR, 2020, P NATL ACAD SCI USA, V117, P1027, DOI 10.1073/pnas.1913054117
   Cibi DM, 2019, ELIFE, V8, DOI 10.7554/eLife.45418
   Cook Danielle R, 2011, Genes Cancer, V2, P932, DOI 10.1177/1947601912437035
   Daley WP, 2008, J CELL SCI, V121, P255, DOI 10.1242/jcs.006064
   Damianov A, 2016, CELL, V165, P606, DOI 10.1016/j.cell.2016.03.040
   Davis CA, 2018, NUCLEIC ACIDS RES, V46, pD794, DOI 10.1093/nar/gkx1081
   Debbache J, 2018, GENESIS, V56, DOI 10.1002/dvg.23105
   Dubielecka PM, 2011, P NATL ACAD SCI USA, V108, P7022, DOI 10.1073/pnas.1016811108
   Dunham I, 2012, NATURE, V489, P57, DOI 10.1038/nature11247
   Etienne-Manneville S, 2002, NATURE, V420, P629, DOI 10.1038/nature01148
   Feinstein JA, 2012, J AM COLL CARDIOL, V59, pS1, DOI 10.1016/j.jacc.2011.09.022
   Fukata M, 2001, NAT REV MOL CELL BIO, V2, P887, DOI 10.1038/35103068
   Gallagher TL, 2011, DEV BIOL, V359, P251, DOI 10.1016/j.ydbio.2011.08.025
   Garcia MD, 2014, FRONT PHYSIOL, V5, DOI 10.3389/fphys.2014.00308
   Gehman LT, 2012, GENE DEV, V26, P445, DOI 10.1101/gad.182477.111
   Geiger B, 2011, CSH PERSPECT BIOL, V3, DOI 10.1101/cshperspect.a005033
   GEORGE EL, 1993, DEVELOPMENT, V119, P1079
   Glessner JT, 2014, CIRC RES, V115, P884, DOI 10.1161/CIRCRESAHA.115.304458
   Harmon AW, 2013, GENESIS, V51, P862, DOI 10.1002/dvg.22721
   Homsy J, 2015, SCIENCE, V350, P1262, DOI 10.1126/science.aac9396
   Hu J, 2019, P NATL ACAD SCI USA, V116, P6172, DOI 10.1073/pnas.1822176116
   Hua YM, 2011, NATURE, V478, P123, DOI 10.1038/nature10485
   Innocenti M, 2004, NAT CELL BIOL, V6, P319, DOI 10.1038/ncb1105
   Innocenti M, 2003, J CELL BIOL, V160, P17, DOI 10.1083/jcb.200206079
   Kalsotra A, 2008, P NATL ACAD SCI USA, V105, P20333, DOI 10.1073/pnas.0809045105
   Katz Y, 2010, NAT METHODS, V7, P1009, DOI 10.1038/NMETH.1528
   Konstandin MH, 2013, BASIC RES CARDIOL, V108, DOI 10.1007/s00395-013-0375-8
   Kotula L, 2012, FEBS LETT, V586, P2790, DOI 10.1016/j.febslet.2012.05.015
   Kovacic JC, 2012, CIRCULATION, V125, P1795, DOI 10.1161/CIRCULATIONAHA.111.040352
   Kuo JC, 2011, NAT CELL BIOL, V13, P383, DOI 10.1038/ncb2216
   Leahy DJ, 1996, CELL, V84, P155, DOI 10.1016/S0092-8674(00)81002-8
   Liu XQ, 2017, NAT GENET, V49, P1152, DOI 10.1038/ng.3870
   MAYEDA A, 1994, EMBO J, V13, P5483, DOI 10.1002/j.1460-2075.1994.tb06883.x
   McKean DM, 2016, NAT COMMUN, V7, DOI 10.1038/ncomms12824
   Mendell JR, 2013, ANN NEUROL, V74, P637, DOI 10.1002/ana.23982
   Miao YF, 2020, CELL STEM CELL, V27, P574, DOI 10.1016/j.stem.2020.07.015
   Morris SA, 2014, CIRCULATION, V129, P285, DOI 10.1161/CIRCULATIONAHA.113.003711
   Moses Kelvin A., 2001, Genesis The Journal of Genetics and Development, V31, P176, DOI 10.1002/gene.10022
   Nakano H, 2013, NAT COMMUN, V4, DOI 10.1038/ncomms2569
   Nakashima Y, 2014, CIRC RES, V114, P1103, DOI 10.1161/CIRCRESAHA.114.303219
   Nutter CA, 2016, CELL REP, V15, P2200, DOI 10.1016/j.celrep.2016.05.002
   Padget RL, 2019, MECH DEVELOP, V156, P8, DOI 10.1016/j.mod.2019.02.002
   Parker SE, 2010, BIRTH DEFECTS RES A, V88, P1008, DOI 10.1002/bdra.20735
   Ricci M, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0029784
   Ryu JR, 2009, MOL CELL BIOL, V29, P1735, DOI 10.1128/MCB.01483-08
   Schiefner A, 2012, J BIOL CHEM, V287, P17578, DOI 10.1074/jbc.M111.303131
   Schneid S, 2021, CELL REP, V34, DOI 10.1016/j.celrep.2021.108805
   Sun SY, 2012, RNA, V18, P274, DOI 10.1261/rna.030486.111
   Tatsumoto T, 1999, J CELL BIOL, V147, P921, DOI 10.1083/jcb.147.5.921
   Tranchevent LC, 2017, GENOME RES, V27, P1087, DOI 10.1101/gr.212696.116
   Underwood JG, 2005, MOL CELL BIOL, V25, P10005, DOI 10.1128/MCB.25.22.10005-10016.2005
   Venables JP, 2013, MOL CELL BIOL, V33, P396, DOI 10.1128/MCB.01174-12
   Verma SK, 2016, SCI REP-UK, V6, DOI 10.1038/srep30896
   Verma SK, 2013, J BIOL CHEM, V288, P35372, DOI 10.1074/jbc.M113.507426
   Wang RP, 2020, SCI REP-UK, V10, DOI 10.1038/s41598-020-67781-1
   Wei CL, 2016, MOL CELL, V62, P875, DOI 10.1016/j.molcel.2016.04.013
   Wei CL, 2015, CELL REP, V10, P1521, DOI 10.1016/j.celrep.2015.02.013
   Windmueller R, 2020, CELL REP, V30, P3105, DOI 10.1016/j.celrep.2020.02.034
   Yagi H, 2018, PEDIATR CARDIOL, V39, P1069, DOI 10.1007/s00246-018-1861-4
   Yeo GW, 2009, NAT STRUCT MOL BIOL, V16, P130, DOI 10.1038/nsmb.1545
   Zhang H, 2018, CIRC RES, V122, P774, DOI 10.1161/CIRCRESAHA.117.312136
   Zou Y, 2014, FEBS LETT, V588, P2911, DOI 10.1016/j.febslet.2014.07.019
   Zudaire E, 2011, PLOS ONE, V6, DOI 10.1371/journal.pone.0027385
NR 69
TC 22
Z9 26
U1 1
U2 6
PU OXFORD UNIV PRESS
PI OXFORD
PA GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND
SN 0305-1048
EI 1362-4962
J9 NUCLEIC ACIDS RES
JI Nucleic Acids Res.
PD FEB 28
PY 2022
VL 50
IS 4
BP 2270
EP 2286
DI 10.1093/nar/gkac055
PG 17
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA ZS3XB
UT WOS:000768400500037
PM 35137168
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Glinghammar, B
   Rafter, I
   Lindström, AK
   Hedberg, JJ
   Andersson, HB
   Lindblom, P
   Berg, AL
   Cotgreavei, I
AF Glinghammar, Bjoern
   Rafter, Ingalill
   Lindstrom, Anna-Karin
   Hedberg, Jesper J.
   Andersson, Hakan B.
   Lindblom, Per
   Berg, Anna-Lena
   Cotgreavei, Ian
TI Detection of the mitochondrial and catalytically active alanine
   aminotransferase in human tissues and plasma
SO INTERNATIONAL JOURNAL OF MOLECULAR MEDICINE
LA English
DT Article
DE liver; hepatotoxicity; biomarker; ALT; ALAT; GPT2; serum; plasma; tissue
   expression
ID GLUTAMIC PYRUVIC TRANSAMINASE; ACUTE MYOCARDIAL-INFARCTION; RAT-LIVER;
   AMINO-TRANSFERASE; SERUM; EXPRESSION; ENZYMES; DEHYDROGENASE;
   METABOLISM; ISOENZYMES
AB Serum alanine aminotransferase (ALT) is used as a clinical marker of hepatotoxicity. Three forms of human ALT have been identified, ALT1 and 2 and an alternative splice variant of ALT2 (herein called ALT2_2). The standard ALT activity assay does not discriminate between ALT from different organs, or the isoforms measured in the plasma. Here, we show that ALT1 and 2 possess similar enzymatic activity for alanine and pyruvate but with different K-m and k(cat) values, while recombinant ALT2_2 protein does not possess any enzymatic activity. Isolation of organelles from cultured human skeletal muscle cells, showed localisation of ALT2 to the mitochondrial fraction and endoplasmatic reticulum (ER), but not to the cytosol. In human hepatocytes, on the other hand, ALT1 was only localised to the cytosol and ER, with no detection in mitochondria. ALT2 was not detected in cultured human hepatocytes, liver extract or tissue using Western blotting or immunohistochemistry. The islet of Langerhans and cardiomyocytes were other examples of cells with high expression of catalytic ALT2. A clinical method for selective measurement of ALT1 and 2 in human plasma is described, and both ALT1 and 2 were immunoprecipitated from human plasma and structurally detected using Western blotting techniques.
C1 [Glinghammar, Bjoern; Rafter, Ingalill; Hedberg, Jesper J.; Lindblom, Per; Cotgreavei, Ian] AstraZeneca, Mol Toxicol, Safety Assessment, S-15185 Sodertalje, Sweden.
   [Lindstrom, Anna-Karin; Berg, Anna-Lena] AstraZeneca, Pathology, Safety Assessment, S-15185 Sodertalje, Sweden.
   [Andersson, Hakan B.] AstraZeneca, Clin Pathol, Safety Assessment, S-15185 Sodertalje, Sweden.
C3 AstraZeneca; AstraZeneca; AstraZeneca
RP Glinghammar, B (corresponding author), AstraZeneca, Mol Toxicol, Safety Assessment, S-15185 Sodertalje, Sweden.
EM bjorn.glinghammar@astrazeneca.com
CR BANG NU, 1962, DIS CHEST, V41, P384
   Barshes NR, 2005, J AM COLL SURGEONS, V200, P353, DOI 10.1016/j.jamcollsurg.2004.10.021
   BRADY LJ, 1978, J NUTR, V108, P648, DOI 10.1093/jn/108.4.648
   DAVISON TF, 1975, COMP BIOCHEM PHYS A, V52, P645, DOI 10.1016/S0300-9629(75)80017-X
   DEROSA G, 1979, BIOCHIM BIOPHYS ACTA, V567, P116, DOI 10.1016/0005-2744(79)90178-5
   DEROSA G, 1975, J BIOL CHEM, V250, P7961
   DHAMI MSI, 1979, CLIN CHEM, V25, P1263
   DRAPER RP, 1994, ARCH TOXICOL, V69, P111, DOI 10.1007/s002040050145
   FUJIWARA S, 1994, ARCH BIOCHEM BIOPHYS, V310, P497, DOI 10.1006/abbi.1994.1198
   GIESEN PLA, 1989, CLIN CHEM, V35, P279
   GUBERN G, 1990, BIOCHEM SOC T, V18, P1288, DOI 10.1042/bst0181288
   HIRD FJR, 1950, NATURE, V166, P517, DOI 10.1038/166517a0
   ISHIGURO M, 1991, BIOCHEMISTRY-US, V30, P10451, DOI 10.1021/bi00107a013
   Jadaho SB, 2004, HEPATOLOGY, V39, P1297, DOI 10.1002/hep.20182
   KARMEN A, 1955, J CLIN INVEST, V34, P126, DOI 10.1172/JCI103055
   LADUE J S, 1956, Ann Intern Med, V45, P801
   Lindblom P, 2007, ARCH BIOCHEM BIOPHYS, V466, P66, DOI 10.1016/j.abb.2007.07.023
   LINDENA J, 1986, J CLIN CHEM CLIN BIO, V24, P35, DOI 10.1515/cclm.1986.24.1.35
   Liu L, 2008, PROTEIN EXPRES PURIF, V60, P225, DOI 10.1016/j.pep.2008.04.006
   Metón I, 2004, FEBS LETT, V566, P251, DOI 10.1016/j.febslet.2004.04.051
   Mukorah F, 1998, CRYOBIOLOGY, V37, P300, DOI 10.1006/cryo.1998.2125
   O'Brien PJ, 2002, LAB ANIM-UK, V36, P313, DOI 10.1258/002367702320162414
   PETTE D, 1962, BIOCHEM BIOPH RES CO, V8, P283, DOI 10.1016/0006-291X(62)90279-6
   Sohocki MM, 1997, GENOMICS, V40, P247, DOI 10.1006/geno.1996.4604
   SWICK RW, 1965, J BIOL CHEM, V240, P3341
   SWICK RW, 1965, J BIOL CHEM, V240, P3334
   TAKEDA Y, 1964, J BIOL CHEM, V239, P3590
   VALENTINE BA, 1990, J VET INTERN MED, V4, P140, DOI 10.1111/j.1939-1676.1990.tb00886.x
   Wada H, 1978, Med J Osaka Univ, V29, P181
   WANER T, 1991, VET RES COMMUN, V15, P73, DOI 10.1007/BF00497793
   WILLIAMSON DH, 1967, BIOCHEM J, V104, P497, DOI 10.1042/bj1040497
   YAMADA R H, 1984, Acta Vitaminologica et Enzymologica, V6, P289
   Yang RZ, 2002, GENOMICS, V79, P445, DOI 10.1006/geno.2002.6722
NR 33
TC 58
Z9 64
U1 0
U2 18
PU SPANDIDOS PUBL LTD
PI ATHENS
PA POB 18179, ATHENS, 116 10, GREECE
SN 1107-3756
EI 1791-244X
J9 INT J MOL MED
JI Int. J. Mol. Med.
PD MAY
PY 2009
VL 23
IS 5
BP 621
EP 631
DI 10.3892/ijmm_00000173
PG 11
WC Medicine, Research & Experimental
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Research & Experimental Medicine
GA 434FU
UT WOS:000265261400008
PM 19360321
OA Bronze
DA 2025-04-10
ER

PT J
AU Uslu, O
   Herold, J
   Kanse, SM
AF Uslu, Ozgur
   Herold, Joerg
   Kanse, Sandip M.
TI VEGF-A-Cleavage by FSAP and Inhibition of Neo-Vascularization
SO CELLS
LA English
DT Article
DE factor VII activating protease; HABP2; VEGF; matrigel;
   neo-vascularization; hind limb ischemia
ID VII-ACTIVATING PROTEASE; ENDOTHELIAL GROWTH-FACTOR; HYALURONAN-BINDING
   PROTEASE; MARBURG-I POLYMORPHISM; CELL-PROLIFERATION; VENOUS THROMBOSIS;
   RISK; ANGIOGENESIS; DEFICIENCY; MATRIGEL
AB Alternative splicing leads to the secretion of multiple forms of vascular endothelial growth factor-A (VEGF-A) that differ in their activity profiles with respect to neovascularization. FSAP (factor VII activating protease) is the zymogen form of a plasma protease that is activated (FSAPa) upon tissue injury via the release of histones. The purpose of the study was to determine if FSAPa regulates VEGF-A activity in vitro and in vivo. FSAP bound to VEGF(165), but not VEGF(121), and VEGF(165) was cleaved in its neuropilin/proteoglycan binding domain. VEGF(165) cleavage did not alter its binding to VEGF receptors but diminished its binding to neuropilin. The stimulatory effects of VEGF(165) on endothelial cell proliferation, migration, and signal transduction were not altered by FSAP. Similarly, proliferation of VEGF receptor-expressing BAF3 cells, in response to VEGF(165), was not modulated by FSAP. In the mouse matrigel model of angiogenesis, FSAP decreased the ability of VEGF(165), basic fibroblast growth factor (bFGF), and their combination, to induce neovascularization. Lack of endogenous FSAP in mice did not influence neovascularization. Thus, FSAP inhibited VEGF(165)-mediated angiogenesis in the matrigel model in vivo, where VEGF's interaction with the matrix and its diffusion are important.
C1 [Uslu, Ozgur] Justus Liebig Univ Giessen, Inst Biochem, D-35392 Giessen, Germany.
   [Herold, Joerg] Klinikum Darmstadt, Dept Angiol, Clin Vasc Med, D-64283 Darmstadt, Germany.
   [Kanse, Sandip M.] Univ Oslo, Inst Basic Med Sci, Sognvannsveien 9, N-0372 Oslo, Norway.
C3 Justus Liebig University Giessen; Klinikum Darmstadt; University of Oslo
RP Kanse, SM (corresponding author), Univ Oslo, Inst Basic Med Sci, Sognvannsveien 9, N-0372 Oslo, Norway.
EM Oezguer1975@gmx.de; joerg_herold@hotmail.com;
   Sandip.kanse@medisin.uio.no
RI herold, joerg/AAD-9745-2020; Kanse, Sandip/ABP-0755-2022
OI Kanse, Sandip/0000-0003-0782-9957
FU Deutscheforschungsgemeinschaft, Germany
FX Funding was from the Deutscheforschungsgemeinschaft, Germany.
CR Ahmad-Nejad P, 2012, THROMB RES, V130, P441, DOI 10.1016/j.thromres.2012.02.009
   Apte RS, 2019, CELL, V176, P1248, DOI 10.1016/j.cell.2019.01.021
   Armulik A, 2005, CIRC RES, V97, P512, DOI 10.1161/01.RES.0000182903.16652.d7
   Chen TT, 2010, J CELL BIOL, V188, P595, DOI 10.1083/jcb.200906044
   Daniel JM, 2016, J THROMB HAEMOST, V14, P2058, DOI 10.1111/jth.13417
   Ekker SC, 2009, BLOOD, V113, P2123, DOI 10.1182/blood-2008-11-189746
   Etscheid M, 2004, EUR J CELL BIOL, V82, P597, DOI 10.1078/0171-9335-00349
   Etscheid M, 2012, THROMB RES, V130, P935, DOI 10.1016/j.thromres.2012.07.023
   Gara SK, 2015, NEW ENGL J MED, V373, P448, DOI 10.1056/NEJMoa1502449
   Grasso S, 2018, THROMB RES, V161, P36, DOI 10.1016/j.thromres.2017.11.012
   Herold J, 2017, AM J TRANSL RES, V9, P3084
   Holmes DIR, 2005, GENOME BIOL, V6, DOI 10.1186/gb-2005-6-2-209
   Hoppe B, 2006, THROMB HAEMOSTASIS, V96, P465, DOI 10.1160/TH06-06-0312
   Hughes CS, 2010, PROTEOMICS, V10, P1886, DOI 10.1002/pmic.200900758
   Jeon JW, 2006, INT J ONCOL, V29, P209
   Joshi AU, 2015, EUR J NEUROSCI, V41, P963, DOI 10.1111/ejn.12830
   Kannemeier Christian, 2004, FASEB J, V18, P728
   Kano MR, 2005, J CELL SCI, V118, P3759, DOI 10.1242/jcs.02483
   Kanse SM, 2012, J IMMUNOL, V188, P2858, DOI 10.4049/jimmunol.1103029
   Kara E, 2017, THROMB HAEMOSTASIS, V117, P1750, DOI 10.1160/TH17-02-0081
   Keck RG, 1997, ARCH BIOCHEM BIOPHYS, V344, P103, DOI 10.1006/abbi.1997.0145
   Keyt BA, 1996, J BIOL CHEM, V271, P7788, DOI 10.1074/jbc.271.13.7788
   Kress JA, 2006, BIOL CHEM, V387, P1275, DOI 10.1515/BC.2006.158
   Lee S, 2005, J CELL BIOL, V169, P681, DOI 10.1083/jcb.200409115
   MAGEE JC, 1994, AM J PHYSIOL-LUNG C, V267, pL433, DOI 10.1152/ajplung.1994.267.4.L433
   Mambetsariev N, 2010, ARTERIOSCL THROM VAS, V30, P483, DOI 10.1161/ATVBAHA.109.200451
   Marsman G, 2017, BLOOD ADV, V1, P2491, DOI 10.1182/bloodadvances.2017010959
   Ngeow J, 2016, JNCI-J NATL CANCER I, V108, DOI 10.1093/jnci/djw013
   PAULY RR, 1992, CIRCULATION, V86, P68
   Peng KW, 2019, DRUG DISCOV TODAY, V24, P656, DOI 10.1016/j.drudis.2018.10.004
   Reiner AP, 2009, J THROMB HAEMOST, V7, P1499, DOI 10.1111/j.1538-7836.2009.03522.x
   Roedel EK, 2013, J BIOL CHEM, V288, P7193, DOI 10.1074/jbc.M112.433029
   Roth D, 2006, AM J PATHOL, V168, P670, DOI 10.2353/ajpath.2006.050372
   Sedding D, 2006, J EXP MED, V203, P2801, DOI 10.1084/jem.20052546
   Serpas L, 2019, P NATL ACAD SCI USA, V116, P641, DOI 10.1073/pnas.1815031116
   Trompet S, 2011, STROKE RES TREAT, V2011, DOI 10.4061/2011/424759
   Vempati P, 2014, CYTOKINE GROWTH F R, V25, P1, DOI 10.1016/j.cytogfr.2013.11.002
   Wake H, 2009, EUR J PHARMACOL, V623, P89, DOI 10.1016/j.ejphar.2009.09.010
   Wasmuth HE, 2009, HEPATOLOGY, V49, P775, DOI 10.1002/hep.22707
   Willeit J, 2003, CIRCULATION, V107, P667, DOI 10.1161/01.CIR.0000055189.18831.B1
   Yamamichi S, 2011, BIOCHEM BIOPH RES CO, V409, P483, DOI 10.1016/j.bbrc.2011.05.030
NR 41
TC 7
Z9 7
U1 1
U2 7
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
EI 2073-4409
J9 CELLS-BASEL
JI Cells
PD NOV
PY 2019
VL 8
IS 11
AR 1396
DI 10.3390/cells8111396
PG 17
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA JV3LB
UT WOS:000502266700094
PM 31698750
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Li, DX
   Bachinski, LL
   Roberts, R
AF Li, DX
   Bachinski, LL
   Roberts, R
TI Genomic organization and isoform-specific tissue expression of human
   NAPOR (CUGBP2) as a candidate gene for familial
   arrhythmogenic right ventricular dysplasia
SO GENOMICS
LA English
DT Article
ID RNA-BINDING PROTEIN; MESSENGER-RNA; CARDIOMYOPATHY; LOCUS; MAPS;
   APOPTOSIS; DYSTROPHY; DEATH
AB Neuroblastoma apoptosis-related RNA-binding protein (NAPOR; HGMW-approved symbol CUGBP2) is a newly discovered gene prominently induced during apoptosis, suggesting that: it plays a role during apoptosis, We have found that it is encoded by a gene located on chromosome 10p13-p14 between Genethon markers D10S547 and D10S223, a region to which we have recently localized a gene responsible for arrhythmogenic right ventricular dysplasia (ARVD). To examine its possible role in the pathogenesis of ARVD, we determined the genomic organization of the human NAPOR gene including its exon-intron boundaries and the putative promoter sequence, which provide a plausible mechanism for its alternative mRNA splicing. We also demonstrated that three isoforms of the NAPOR transcript were differently expressed, with NAPOR-3 being nearly neuron specific while the other two forms were ubiquitously expressed. The expression of NAPOR is differentially regulated during development. Finally, we screened the members of the ARVD family for mutations and identified two DNA sequence variants in the protein-coding exons of NAPOR, neither of which was responsible for ARVD, While the function of NAPOR remains to be elucidated, our current characterization of the NAPOR gene will be valuable for further clinical and functional study, (C) 2001 Academic Press.
C1 Baylor Coll Med, Cardiol Sect, Dept Med Cardiol, Houston, TX 77030 USA.
C3 Baylor College of Medicine
RP Baylor Coll Med, Cardiol Sect, Dept Med Cardiol, 6550 Fannin,MS SM677,1 Baylor Plaza, Houston, TX 77030 USA.
EM rroberts@bcm.tmc.edu
OI Diamandis, Eleftherios/0000-0002-1589-820X
FU NHLBI NIH HHS [T32-HL07706, P50-HL54313] Funding Source: Medline
CR Ahmad F, 1998, CIRCULATION, V98, P2791, DOI 10.1161/01.CIR.98.25.2791
   Aizencang G, 2000, GENOMICS, V70, P223, DOI 10.1006/geno.2000.6373
   Basso C, 1996, CIRCULATION, V94, P983, DOI 10.1161/01.CIR.94.5.983
   BREATHNACH R, 1981, ANNU REV BIOCHEM, V50, P349, DOI 10.1146/annurev.bi.50.070181.002025
   Choi DK, 1999, GENE, V237, P135, DOI 10.1016/S0378-1119(99)00312-1
   Choi DK, 1998, GENE, V223, P21, DOI 10.1016/S0378-1119(98)00364-3
   CORRADO D, 1990, AM J MED, V89, P588, DOI 10.1016/0002-9343(90)90176-E
   DECKER CJ, 1994, TRENDS BIOCHEM SCI, V19, P336, DOI 10.1016/0968-0004(94)90073-6
   Fontaine G, 1999, ANNU REV MED, V50, P17, DOI 10.1146/annurev.med.50.1.17
   Jensen KB, 2000, NEURON, V25, P359, DOI 10.1016/S0896-6273(00)80900-9
   KLAUSNER RD, 1993, CELL, V72, P19, DOI 10.1016/0092-8674(93)90046-S
   Li DX, 1999, CIRCULATION, V100, P461, DOI 10.1161/01.CIR.100.5.461
   Li DX, 2000, AM J HUM GENET, V66, P148, DOI 10.1086/302713
   Lu XH, 1999, HUM MOL GENET, V8, P53, DOI 10.1093/hmg/8.1.53
   Mallat Z, 1996, NEW ENGL J MED, V335, P1190, DOI 10.1056/NEJM199610173351604
   RAMPAZZO A, 1995, HUM MOL GENET, V4, P2151, DOI 10.1093/hmg/4.11.2151
   Rampazzo A, 1997, GENOMICS, V45, P259, DOI 10.1006/geno.1997.4927
   RAMPAZZO A, 1994, HUM MOL GENET, V3, P959, DOI 10.1093/hmg/3.6.959
   Roberts R, 1997, P NATL ACAD SCI USA, V94, P13221, DOI 10.1073/pnas.94.24.13221
   Severini GM, 1996, GENOMICS, V31, P193, DOI 10.1006/geno.1996.0031
   SHEN WK, 1995, AM J CARDIOL, V76, P148, DOI 10.1016/S0002-9149(99)80047-2
   TAUPIN JL, 1995, P NATL ACAD SCI USA, V92, P1629, DOI 10.1073/pnas.92.5.1629
   Thiene G, 1997, TRENDS CARDIOVAS MED, V7, P84, DOI 10.1016/S1050-1738(97)00011-X
   TIAN QS, 1991, CELL, V67, P629, DOI 10.1016/0092-8674(91)90536-8
   Timchenko LT, 1996, NUCLEIC ACIDS RES, V24, P4407, DOI 10.1093/nar/24.22.4407
   Valente M, 1998, AM J PATHOL, V152, P479
   Zhu JH, 2000, MOL CELL BIOL, V20, P5602, DOI 10.1128/MCB.20.15.5602-5618.2000
NR 27
TC 39
Z9 45
U1 0
U2 3
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0888-7543
EI 1089-8646
J9 GENOMICS
JI Genomics
PD JUN 15
PY 2001
VL 74
IS 3
BP 396
EP 401
DI 10.1006/geno.2001.6558
PG 6
WC Biotechnology & Applied Microbiology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biotechnology & Applied Microbiology; Genetics & Heredity
GA 449EJ
UT WOS:000169671100016
PM 11414768
DA 2025-04-10
ER

PT J
AU Tu, YH
   Hou, ST
   Huang, ZG
   Robertson, GS
   MacManus, JP
AF Tu, YH
   Hou, ST
   Huang, ZG
   Robertson, GS
   MacManus, JP
TI Increased Mdm2 expression in rat brain after transient middle cerebral
   artery occlusion
SO JOURNAL OF CEREBRAL BLOOD FLOW AND METABOLISM
LA English
DT Article
DE mdm2; p53; transient focal ischemia; apoptosis; gene expression
ID CENTRAL-NERVOUS-SYSTEM; P53 MESSENGER-RNA; TUMOR-SUPPRESSOR; DNA-DAMAGE;
   EMBRYONIC LETHALITY; MDM2-DEFICIENT MICE; FOREBRAIN ISCHEMIA; INDUCED
   APOPTOSIS; GENE-EXPRESSION; NEURONAL DEATH
AB The negative regulator of p53 transactivation, Mdm2, increased in the ischemic territory after 90 minutes of transient middle cerebral artery occlusion in spontaneously hypertensive rats compared to sham controls. Increased mdm2 mRNA was detected by semiquantitative reverse transcriptase polymerase chain reaction by 6 hours of reperfusion in the ipsilateral hemisphere. In situ hybridization histochemistry was used to localize increases in mdm2 mRNA which occurred in neurons of ischemic cortex and dorsolateral striatum. The number of labeled neurons increased by approximately 20-fold and the cells displayed five-fold increases of mdm2 mRNA in the cortex. Immunohistochemical staining for Mdm2 revealed that its mRNA was efficiently translated in the ischemic cortex, but not striatum, by 8 to 24 hours of reperfusion. Western blotting confirmed 30- to 40-fold increases in the full-length protein of 90 kd at these time points without evidence of alternative splicing. Because Mdm2 is a negative regulator of the apoptosis promoting activity of p53, increased expression of Mdm2 may be a component of a repair response in injured neurons, and supports Mdm2 being an indicator of DNA damage in the brain early after an ischemic insult in a similar way to Gadd45.
C1 Natl Res Council Canada, Inst Biol Sci, Montreal Rd Labs, Ottawa, ON K1A 0R6, Canada.
   Univ Ottawa, Dept Cellular & Mol Med, Ottawa, ON K1N 6N5, Canada.
C3 National Research Council Canada; University of Ottawa
RP MacManus, JP (corresponding author), Natl Res Council Canada, Inst Biol Sci, Montreal Rd Labs, Bldg M54, Ottawa, ON K1A 0R6, Canada.
RI Hou, Sheng/AAM-7756-2020
OI Robertson, George S./0000-0001-8411-7721; Hou, Sheng
   Tao/0000-0001-9736-342X
CR Akins PT, 1996, STROKE, V27, P1682, DOI 10.1161/01.STR.27.9.1682
   BUCHAN AM, 1992, STROKE, V23, P273, DOI 10.1161/01.STR.23.2.273
   CAHILLYSNYDER L, 1987, SOMAT CELL MOLEC GEN, V13, P235, DOI 10.1007/BF01535205
   CharriautMarlangue C, 1996, TRENDS NEUROSCI, V19, P109, DOI 10.1016/S0166-2236(96)80039-7
   Chen J, 1997, J NEUROCHEM, V69, P232
   Chen JD, 1996, MOL CELL BIOL, V16, P2445
   CHEN JD, 1993, MOL CELL BIOL, V13, P4107, DOI 10.1128/MCB.13.7.4107
   Choi DW, 1996, CURR OPIN NEUROBIOL, V6, P667, DOI 10.1016/S0959-4388(96)80101-2
   CHOPP M, 1992, BIOCHEM BIOPH RES CO, V182, P1201, DOI 10.1016/0006-291X(92)91859-O
   Chopp M, 1996, ACT NEUR S, V66, P21
   CORVI R, 1995, EUR J CANCER, V31A, P520, DOI 10.1016/0959-8049(95)00031-D
   CRUMRINE RC, 1994, J CEREBR BLOOD F MET, V14, P887, DOI 10.1038/jcbfm.1994.119
   DubsPoterszman MC, 1995, ONCOGENE, V11, P2445
   EBERT M, 1994, INT J ONCOL, V5, P1279
   Eizenberg O, 1996, MOL CELL BIOL, V16, P5178
   Enokido Y, 1996, EUR J NEUROSCI, V8, P1812, DOI 10.1111/j.1460-9568.1996.tb01325.x
   FAKHARZADEH SS, 1991, EMBO J, V10, P1565, DOI 10.1002/j.1460-2075.1991.tb07676.x
   Field SJ, 1996, CELL, V85, P549, DOI 10.1016/S0092-8674(00)81255-6
   GERFEN CR, 1991, J NEUROSCI, V11, P1016
   Gorgoulis VG, 1996, J PATHOL, V180, P129
   Guegan C, 1997, NEUROREPORT, V8, P1003, DOI 10.1097/00001756-199703030-00037
   HAINES DS, 1994, MOL CELL BIOL, V14, P1171, DOI 10.1128/MCB.14.2.1171
   Haupt Y, 1997, NATURE, V387, P296, DOI 10.1038/387296a0
   Haupt Y, 1996, EMBO J, V15, P1596, DOI 10.1002/j.1460-2075.1996.tb00504.x
   Holbrook N J., 1996, in Stress-Inducible Cellular Responses ed, P273
   Honkaniemi J, 1996, MOL BRAIN RES, V42, P79, DOI 10.1016/S0169-328X(96)00121-0
   Hou ST, 1997, BIOCHEM CELL BIOL, V75, P383, DOI 10.1139/bcb-75-4-383
   Hughes PE, 1996, NEUROSCIENCE, V74, P1143, DOI 10.1016/S0306-4522(96)00174-1
   Iadecola C, 1997, TRENDS NEUROSCI, V20, P132, DOI 10.1016/S0166-2236(96)10074-6
   JAYARAMAN L, 1995, CELL, V81, P1021, DOI 10.1016/S0092-8674(05)80007-8
   Jin KL, 1996, NEUROREPORT, V7, P1797, DOI 10.1097/00001756-199607290-00022
   JOHNSON EM, 1995, J NEUROTRAUM, V12, P843, DOI 10.1089/neu.1995.12.843
   JONES SN, 1995, NATURE, V378, P206, DOI 10.1038/378206a0
   JORDAN J, 1997, J NEUROSCI, V15, P1379
   KONDO S, 1995, ONCOGENE, V10, P2001
   KOWALIK TF, 1995, J VIROL, V69, P2491, DOI 10.1128/JVI.69.4.2491-2500.1995
   Kubbutat MHG, 1997, NATURE, V387, P299, DOI 10.1038/387299a0
   KUMAR K, 1995, MOL BRAIN RES, V30, P149, DOI 10.1016/0169-328X(94)00286-N
   Kussie PH, 1996, SCIENCE, V274, P948, DOI 10.1126/science.274.5289.948
   LAEMMLI UK, 1970, NATURE, V227, P680, DOI 10.1038/227680a0
   LANDANYI M, 1993, CANCER RES, V53, P16
   LEE S, 1995, CELL, V81, P1013, DOI 10.1016/S0092-8674(05)80006-6
   LENG P, 1995, ONCOGENE, V10, P1275
   Levine AJ, 1997, CELL, V88, P323, DOI 10.1016/S0092-8674(00)81871-1
   LI Y, 1994, STROKE, V25, P849, DOI 10.1161/01.STR.25.4.849
   Li Y, 1997, J CEREBR BLOOD F MET, V17, P846, DOI 10.1097/00004647-199708000-00003
   Linnik MD, 1996, RESTOR NEUROL NEUROS, V9, P219, DOI 10.3233/RNN-1996-9404
   Liu PK, 1996, J NEUROSCI, V16, P6795
   Liu W, 1996, NEUROREPORT, V7, P2785, DOI 10.1097/00001756-199611040-00076
   LUNA RMD, 1995, NATURE, V378, P203
   MacManus JP, 1997, J CEREBR BLOOD F MET, V17, P376, DOI 10.1097/00004647-199704000-00003
   MACMANUS JP, 1995, J CEREBR BLOOD F MET, V15, P728, DOI 10.1038/jcbfm.1995.93
   MacManus JP, 1997, J CEREBR BLOOD F MET, V17, P815, DOI 10.1038/aj.jcbfm.9590266
   MACMANUS JP, 1994, NEUROREPORT, V5, P493, DOI 10.1097/00001756-199401120-00031
   MARTIN K, 1995, NATURE, V375, P691, DOI 10.1038/375691a0
   Massa SM, 1996, CEREBROVAS BRAIN MET, V8, P95
   Momand J, 1997, J CELL BIOCHEM, V64, P343
   Morrison RS, 1996, J NEUROSCI, V16, P1337
   Nakagomi T, 1996, NEUROL RES, V18, P559
   NEVINS JR, 1992, SCIENCE, V258, P424
   NITATORI T, 1995, J NEUROSCI, V15, P1001
   OLINER JD, 1992, NATURE, V358, P80, DOI 10.1038/358080a0
   OLSON DC, 1993, ONCOGENE, V8, P2353
   PERRY ME, 1993, P NATL ACAD SCI USA, V90, P11623, DOI 10.1073/pnas.90.24.11623
   PRICE BD, 1994, CANCER RES, V54, P896
   ROBERTSON GS, 1995, NEUROSCIENCE, V67, P325, DOI 10.1016/0306-4522(95)00049-O
   Sakhi S, 1996, NEUROREPORT, V8, P233, DOI 10.1097/00001756-199612200-00047
   SAKHI S, 1994, P NATL ACAD SCI USA, V91, P7525, DOI 10.1073/pnas.91.16.7525
   SCHREIBER SS, 1994, EXP NEUROL, V130, P368, DOI 10.1006/exnr.1994.1216
   Sigalas I, 1996, NAT MED, V2, P912, DOI 10.1038/nm0896-912
   Slack RS, 1996, J CELL BIOL, V135, P1085, DOI 10.1083/jcb.135.4.1085
   TOBITA M, 1995, NEUROSCI LETT, V200, P129, DOI 10.1016/0304-3940(95)12097-N
   TOMASEVIC G, 1996, PHARM CEREBRAL ISCHE, P1
   VONWASIELEWSKI R, 1994, HISTOCHEMISTRY, V102, P65
   Wiessner C, 1996, NEUROSCIENCE, V72, P947, DOI 10.1016/0306-4522(95)00601-X
   WU XW, 1993, GENE DEV, V7, P1126, DOI 10.1101/gad.7.7a.1126
   Xiang H, 1996, J NEUROSCI, V16, P6753
   XIAO ZX, 1995, NATURE, V375, P694, DOI 10.1038/375694a0
NR 78
TC 30
Z9 34
U1 0
U2 0
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA 227 EAST WASHINGTON SQ, PHILADELPHIA, PA 19106 USA
SN 0271-678X
J9 J CEREBR BLOOD F MET
JI J. Cereb. Blood Flow Metab.
PD JUN
PY 1998
VL 18
IS 6
BP 658
EP 669
DI 10.1097/00004647-199806000-00008
PG 12
WC Endocrinology & Metabolism; Hematology; Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism; Hematology; Neurosciences & Neurology
GA ZT870
UT WOS:000074136600008
PM 9626190
DA 2025-04-10
ER

PT J
AU Thorsteinsdóttir, S
   Roelen, BAJ
   Goumans, MJ
   Ward-van Oostwaard, D
   Gaspar, AC
   Mummery, CL
AF Thorsteinsdóttir, S
   Roelen, BAJ
   Goumans, MJ
   Ward-van Oostwaard, D
   Gaspar, AC
   Mummery, CL
TI Expression of the α6A integrin splice variant in developing mouse
   embryonic stem cell aggregates and correlation with cardiac muscle
   differentiation
SO DIFFERENTIATION
LA English
DT Article
ID TRANSFORMING GROWTH-FACTOR; FACTOR-BETA; IN-VITRO; TRANSCRIPTION FACTOR;
   CYTOPLASMIC DOMAINS; LAMININ RECEPTOR; CARCINOMA-CELLS; CHROMOSOMAL
   LOCALIZATION; ENDODERM DIFFERENTIATION; EXTRACELLULAR-MATRIX
AB Mouse embryonic stem (ES) cells grown in aggregates give rise to several different cell types, including cardiac muscle. Given the lack of cardiac muscle cell lines, ES cells can be a useful tool in the study of cardiac muscle differentiation The laminin-binding integrin alpha 6 beta 1 exists in two different splice variant forms of the alpha chain (alpha 6A and alpha 6B), the alpha 6A form having been implicated as possibly playing a role in cardiac muscle development, based on its distribution pattern [4, 53]. In this study we characterise the ES cell model system in terms of the expression of the two different alpha 6 splice variants. We correlate their expression with that of muscle markers and the transcription factor GATA-4, using the reverse transcription-polymerase chain reaction (RT-PCR). We confirm that alpha 6B is constitutively expressed by ES cells. In contrast, alpha 6A expression appears later and overlaps in time with a period when the muscle marker myosin light chain-2V (MLC-2V) is expressed, but no MyoD is present, which indicates the presence of cardiac muscle cells in the aggregates. We further show that GATA-4 is present at the same time. Culturing the aggregates under conditions that stimulate (transforming growth factor beta 1 supplement) or inhibit (TGF beta 1 plus 10(-9) M retinoic acid supplement) cardiac muscle differentiation does not lead to any qualitative differences in the timing of expression of these genes, but quantitative changes cannot be excluded. The TGF beta 1 supplement does, however, lead to a relatively greater expression of alpha 6A compared to alpha 6B than the TGF beta 1 plus 10-9 M RA supplement after 6 days in culture, suggesting that alpha 6A expression is favoured under conditions that stimulate cardiac muscle differentiation. The switch towards alpha 6A expression in ES cell aggregates is paralleled by expression of the binding receptor for TGF beta (T beta RII). Stable expression of a mutated (dominant negative) T beta RII in ES cells, however, still resulted in (TGF beta-independent) upregulation of alpha 6A, demonstrating that these events were not causally related and that parallel or alternative regulatory pathways exist. The initial characterisation of differentiating ES cell aggregates in terms of alpha 6A integrin subunit expression suggests that this model system could be a valuable tool in the study of the role of the alpha 6 beta 1 integrin in cardiac muscle differentiation.
C1 Univ Lisbon, Fac Sci, Dept Zool, P-1749016 Lisbon, Portugal.
   Univ Lisbon, Fac Sci, Ctr Environm Biol, P-1749016 Lisbon, Portugal.
   Netherlands Inst Dev Biol, Hubrecht Lab, NL-3584 CT Utrecht, Netherlands.
C3 Universidade de Lisboa; Universidade de Lisboa; Royal Netherlands
   Academy of Arts & Sciences; Hubrecht Institute (KNAW)
RP Thorsteinsdóttir, S (corresponding author), Univ Lisbon, Fac Sci, Dept Zool, P-1749016 Lisbon, Portugal.
RI Goumans, Marie/U-1455-2019; Thorsteinsdottir, Solveig/M-3561-2013
OI Goumans, Marie Jose/0000-0001-9344-6746; Thorsteinsdottir,
   Solveig/0000-0002-9018-3431; Mummery, Christine/0000-0002-4549-6535
CR ADAMS JC, 1993, DEVELOPMENT, V117, P1183
   ARCECI RJ, 1993, MOL CELL BIOL, V13, P2235, DOI 10.1128/MCB.13.4.2235
   BALDWIN HS, 1994, DEVELOPMENT, V120, P2539
   COLLO G, 1995, CELL ADHES COMMUN, V3, P101, DOI 10.3109/15419069509081280
   COOPER HM, 1991, J CELL BIOL, V115, P843, DOI 10.1083/jcb.115.3.843
   DELWEL GO, 1995, ADHESION RECEPTORS T, P9
   DESIMONE DW, 1994, CURR OPIN CELL BIOL, V6, P747, DOI 10.1016/0955-0674(94)90103-1
   deWinter JP, 1997, ONCOGENE, V14, P1891, DOI 10.1038/sj.onc.1201017
   DOETSCHMAN TC, 1985, J EMBRYOL EXP MORPH, V87, P27
   Ekblom P., 1993, MOL CELLULAR ASPECTS, P359
   ENENSTEIN J, 1992, EXP CELL RES, V203, P499, DOI 10.1016/0014-4827(92)90028-7
   Goumans MJ, 1998, DIFFERENTIATION, V63, P101, DOI 10.1046/j.1432-0436.1998.6330101.x
   Grepin C, 1997, DEVELOPMENT, V124, P2387
   GREPIN C, 1994, MOL CELL BIOL, V14, P3115, DOI 10.1128/MCB.14.5.3115
   HEINO J, 1989, J BIOL CHEM, V264, P21806
   HEINO J, 1989, J BIOL CHEM, V264, P380
   HIERCK BP, 1993, CELL ADHES COMMUN, V1, P33, DOI 10.3109/15419069309095680
   HOGERVORST F, 1991, EUR J BIOCHEM, V199, P425, DOI 10.1111/j.1432-1033.1991.tb16140.x
   HOOPER M, 1987, NATURE, V326, P292, DOI 10.1038/326292a0
   HORWITZ KB, 1978, J BIOL CHEM, V253, P2223
   HUANG S, 1994, INT J CANCER, V57, P742, DOI 10.1002/ijc.2910570522
   HYNES RO, 1994, CURR OPIN GENET DEV, V4, P569, DOI 10.1016/0959-437X(94)90074-D
   JIANG RL, 1995, EXP CELL RES, V217, P195, DOI 10.1006/excr.1995.1079
   Kagami S, 1996, EXP CELL RES, V229, P1, DOI 10.1006/excr.1996.0336
   KELLY D, 1989, DIFFERENTIATION, V41, P34, DOI 10.1111/j.1432-0436.1989.tb00729.x
   KEMLER R, 1981, J EMBRYOL EXP MORPH, V64, P45
   Kim LT, 1997, P SOC EXP BIOL MED, V214, P123
   KUHL U, 1982, DEV BIOL, V93, P344, DOI 10.1016/0012-1606(82)90122-1
   LIN CQ, 1993, FASEB J, V7, P737, DOI 10.1096/fasebj.7.9.8330681
   Lin Herbert Y., 1993, Trends in Cell Biology, V3, P14, DOI 10.1016/0962-8924(93)90195-7
   Lyons GE., 1992, SEMIN DEV BIOL, V3, P243
   MALTSEV VA, 1993, MECH DEVELOP, V44, P41, DOI 10.1016/0925-4773(93)90015-P
   MILLERHANCE WC, 1993, J BIOL CHEM, V268, P25244
   Morini M, 1997, EXP CELL RES, V232, P304, DOI 10.1006/excr.1997.3528
   MUMMERY CL, 1990, CELL DIFFER DEV, V30, P195, DOI 10.1016/0922-3371(90)90139-N
   MUMMERY CL, 1991, DIFFERENTIATION, V46, P51, DOI 10.1111/j.1432-0436.1991.tb00865.x
   MUMMERY CL, 1989, NATO ASI SERIES H, V26, P231
   OBRIEN TX, 1993, P NATL ACAD SCI USA, V90, P5157, DOI 10.1073/pnas.90.11.5157
   ROBBINS J, 1990, J BIOL CHEM, V265, P11905
   ROBERTS CJ, 1988, J BIOL CHEM, V263, P4586
   ROELEN BAJ, 1994, DEV BIOL, V166, P716, DOI 10.1006/dbio.1994.1350
   Roelen BAJ, 1998, DIFFERENTIATION, V64, P19, DOI 10.1046/j.1432-0436.1998.6410019.x
   ROHWEDEL J, 1994, DEV BIOL, V164, P87, DOI 10.1006/dbio.1994.1182
   Sastry SK, 1993, CURR OPIN CELL BIOL, V5, P819, DOI 10.1016/0955-0674(93)90031-K
   Sastry SK, 1996, J CELL BIOL, V133, P169, DOI 10.1083/jcb.133.1.169
   SHEPPARD D, 1992, J BIOL CHEM, V267, P17409
   SLAGER HG, 1993, DEV GENET, V14, P212, DOI 10.1002/dvg.1020140308
   SMITH AG, 1987, DEV BIOL, V121, P1, DOI 10.1016/0012-1606(87)90132-1
   SONNENBERG A, 1990, J CELL BIOL, V110, P2145, DOI 10.1083/jcb.110.6.2145
   SOUDAIS C, 1995, DEVELOPMENT, V121, P3877
   SUTHERLAND AE, 1993, DEVELOPMENT, V119, P1175
   TAMURA RN, 1991, P NATL ACAD SCI USA, V88, P10183, DOI 10.1073/pnas.88.22.10183
   THORSTEINSDOTTIR S, 1995, DEV DYNAM, V204, P240, DOI 10.1002/aja.1002040304
   TOKUNAGA K, 1986, NUCLEIC ACIDS RES, V14, P2829
   Tryggvason K, 1993, CURR OPIN CELL BIOL, V5, P877, DOI 10.1016/0955-0674(93)90038-R
   TSUCHIDA K, 1993, BIOCHEM BIOPH RES CO, V191, P790, DOI 10.1006/bbrc.1993.1286
   VANDENEIJNDENVANRAAIJ AJM, 1988, BIOCHEM BIOPH RES CO, V157, P16, DOI 10.1016/S0006-291X(88)80004-4
   WANG DH, 1995, J BIOL CHEM, V270, P14154, DOI 10.1074/jbc.270.23.14154
   Williams Michael J., 1994, Trends in Cell Biology, V4, P109, DOI 10.1016/0962-8924(94)90059-0
   WOBUS AM, 1994, ROUX ARCH DEV BIOL, V204, P36, DOI 10.1007/BF00189066
   ZAMBRUNO G, 1995, J CELL BIOL, V129, P853, DOI 10.1083/jcb.129.3.853
NR 61
TC 20
Z9 20
U1 0
U2 1
PU SPRINGER VERLAG
PI NEW YORK
PA 175 FIFTH AVE, NEW YORK, NY 10010 USA
SN 0301-4681
J9 DIFFERENTIATION
JI Differentiation
PD MAR
PY 1999
VL 64
IS 3
BP 173
EP 184
DI 10.1007/s002580050272
PG 12
WC Cell Biology; Developmental Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Developmental Biology
GA 181EB
UT WOS:000079426900005
PM 10234814
DA 2025-04-10
ER

PT J
AU Salvatorelli, L
   Calabrese, G
   Parenti, R
   Vecchio, GM
   Puzzo, L
   Caltabiano, R
   Musumeci, G
   Magro, G
AF Salvatorelli, Lucia
   Calabrese, Giovanna
   Parenti, Rosalba
   Vecchio, Giada Maria
   Puzzo, Lidia
   Caltabiano, Rosario
   Musumeci, Giuseppe
   Magro, Gaetano
TI Immunohistochemical Expression of Wilms' Tumor 1 Protein in Human
   Tissues: From Ontogenesis to Neoplastic Tissues
SO APPLIED SCIENCES-BASEL
LA English
DT Review
DE immunohistochemistry; WT1; human embryonal; fetal tissues; neoplastic
   tissue; differential diagnosis
ID ROUND-CELL TUMOR; CORD-STROMAL TUMORS; MALIGNANT RHABDOID TUMORS;
   MESSENGER-RNA EXPRESSION; TRANSCRIPTION FACTOR-I; SUPPRESSOR GENE WT1;
   SOFT-TISSUE; DIAGNOSTIC UTILITY; DIFFERENTIAL-DIAGNOSIS; SEROUS
   CARCINOMAS
AB The human Wilms' tumor gene (WT1) was originally isolated in a Wilms' tumor of the kidney as a tumor suppressor gene. Numerous isoforms of WT1, by combination of alternative translational start sites, alternative RNA splicing and RNA editing, have been well documented. During human ontogenesis, according to the antibodies used, anti-C or N-terminus WT1 protein, nuclear expression can be frequently obtained in numerous tissues, including metanephric and mesonephric glomeruli, and mesothelial and sub-mesothelial cells, while cytoplasmic staining is usually found in developing smooth and skeletal cells, myocardium, glial cells, neuroblasts, adrenal cortical cells and the endothelial cells of blood vessels. WT1 has been originally described as a tumor suppressor gene in renal Wilms' tumor, but more recent studies emphasized its potential oncogenic role in several neoplasia with a variable immunostaining pattern that can be exclusively nuclear, cytoplasmic or both, according to the antibodies used (anti-C or N-terminus WT1 protein). With the present review we focus on the immunohistochemical expression of WT1 in some tumors, emphasizing its potential diagnostic role and usefulness in differential diagnosis. In addition, we analyze the WT1 protein expression profile in human embryonal/fetal tissues in order to suggest a possible role in the development of organs and tissues and to establish whether expression in some tumors replicates that observed during the development of tissues from which these tumors arise.
C1 [Salvatorelli, Lucia; Vecchio, Giada Maria; Puzzo, Lidia; Caltabiano, Rosario; Magro, Gaetano] Univ Catania, Dept Med & Surg Sci & Adv Technol GF Ingrassia, Azienda Osped Univ Policlin Vittorio Emanue, Anat Pathol Sect,Sch Med, I-95123 Catania, Italy.
   [Calabrese, Giovanna; Parenti, Rosalba] Univ Catania, Dept Biomed & Biotechnol Sci, Physiol Sect, I-95123 Catania, Italy.
   [Musumeci, Giuseppe] Univ Catania, Dept Biomed & Biotechnol Sci, Human Anat & Histol Sect, Sch Med, I-95123 Catania, Italy.
C3 University of Catania; University of Catania; University of Catania
RP Salvatorelli, L (corresponding author), Univ Catania, Dept Med & Surg Sci & Adv Technol GF Ingrassia, Azienda Osped Univ Policlin Vittorio Emanue, Anat Pathol Sect,Sch Med, I-95123 Catania, Italy.
EM lucia.salvatorelli@unict.it; giovanna.calabrese@unict.it;
   parenti@unict.it; giadamariavecchio@gmail.com; lipuzzo@unict.it;
   rosario.caltabiano@unict.it; g.musumeci@unict.it; g.magro@unict.it
RI Caltabiano, Rosario/I-7583-2019; Vecchio, Giada/AAC-6686-2022; Parenti,
   Rosalba/AAS-5489-2020; Musumeci, Giuseppe/K-9955-2016
OI Caltabiano, Rosario/0000-0001-8591-8010; Calabrese,
   Giovanna/0000-0003-1937-5403; Musumeci, Giuseppe/0000-0002-8260-8890;
   Parenti, Rosalba/0000-0002-1614-4696; Salvatorelli,
   Lucia/0000-0001-9648-4545
CR Acs G, 2004, INT J GYNECOL PATHOL, V23, P110, DOI 10.1097/00004347-200404000-00004
   Al Dhaybi R, 2010, J AM ACAD DERMATOL, V63, P1052, DOI 10.1016/j.jaad.2009.12.017
   Al-Hussain T, 2014, ADV ANAT PATHOL, V21, P166, DOI 10.1097/PAP.0000000000000017
   Al-Hussaini M, 2004, HISTOPATHOLOGY, V44, P109, DOI 10.1111/j.1365-2559.2004.01787.x
   Alaggio R, 2012, PEDIATR DEVEL PATHOL, V15, P267, DOI 10.2350/11-08-1079-PB.1
   Amin EM, 2011, CANCER CELL, V20, P768, DOI 10.1016/j.ccr.2011.10.016
   Andersson C, 2014, CANCER MED-US, V3, P909, DOI 10.1002/cam4.244
   [Anonymous], 2007, GENOME BIOL, DOI [10.1186/gb-2007-8-1-401, DOI 10.1186/gb-2007-8-1-401, DOI 10.1186/GB-2007-8-1-401]
   [Anonymous], WHO CLASSIFICATION T
   [Anonymous], SURG PATHOL
   [Anonymous], PATHOLOGICA
   ARMSTRONG JF, 1993, MECH DEVELOP, V40, P85, DOI 10.1016/0925-4773(93)90090-K
   Arora DS, 1997, J PATHOL, V181, P413, DOI 10.1002/(SICI)1096-9896(199704)181:4<413::AID-PATH789>3.0.CO;2-U
   Artibani M, 2017, SCI REP-UK, V7, DOI 10.1038/srep45255
   Aslan A, 2019, MED SCI MONITOR, V25, P5510, DOI 10.12659/MSM.915335
   Athale UH, 2001, J PEDIAT HEMATOL ONC, V23, P99, DOI 10.1097/00043426-200102000-00006
   Attanoos RL, 1997, HISTOPATHOLOGY, V30, P403, DOI 10.1046/j.1365-2559.1997.5460776.x
   Barnoud R, 2000, AM J SURG PATHOL, V24, P830, DOI 10.1097/00000478-200006000-00008
   BECKWITH JB, 1983, HUM PATHOL, V14, P481, DOI 10.1016/S0046-8177(83)80003-3
   Bisceglia M, 2011, PATHOLOGICA, V103, P4
   Bisceglia M, 2011, INT J SURG PATHOL, V19, P831, DOI 10.1177/1066896910395585
   Bourgeois JM, 2000, AM J SURG PATHOL, V24, P937, DOI 10.1097/00000478-200007000-00005
   Bruening W, 1996, J BIOL CHEM, V271, P8646, DOI 10.1074/jbc.271.15.8646
   CALL KM, 1990, CELL, V60, P509, DOI 10.1016/0092-8674(90)90601-A
   Carpentieri DF, 2002, MODERN PATHOL, V15, P1080, DOI 10.1097/01.MP.0000028646.03760.6B
   Cathro HP, 2005, HUM PATHOL, V36, P195, DOI 10.1016/j.humpath.2004.11.011
   Charles AK, 1998, AM J PATHOL, V153, P991, DOI 10.1016/S0002-9440(10)65641-6
   Charles AK, 1997, J CLIN PATHOL-MOL PA, V50, P138, DOI 10.1136/mp.50.3.138
   Chau YY, 2012, TRENDS GENET, V28, P515, DOI 10.1016/j.tig.2012.04.004
   Choi EJ, 2013, WORLD J SURG ONCOL, V11, DOI 10.1186/1477-7819-11-314
   Clark AJ, 2010, J NEUROSURG, V112, P18, DOI 10.3171/2008.11.JNS08368
   Coffin CM, 2012, PEDIATR DEVEL PATHOL, V15, P127, DOI 10.2350/10-12-0944-PB.1
   Garrido MC, 2014, AM J DERMATOPATH, V36, P238, DOI 10.1097/DAD.0b013e3182987441
   Davies JA, 2004, HUM MOL GENET, V13, P235, DOI 10.1093/hmg/ddh015
   Davies R, 1999, CANCER RES, V59, p1747S
   Deavers MT, 2003, MODERN PATHOL, V16, P584, DOI 10.1097/01.MP.0000073133.79591.A1
   Domfeh AB, 2008, MODERN PATHOL, V21, P1217, DOI 10.1038/modpathol.2008.69
   DUCATMAN BS, 1984, CANCER-AM CANCER SOC, V54, P1049, DOI 10.1002/1097-0142(19840915)54:6<1049::AID-CNCR2820540620>3.0.CO;2-1
   Gaffey MJ, 1996, MODERN PATHOL, V9, P308
   Galfione SK, 2014, INT J CLIN EXP PATHO, V7, P2536
   Garrido-Ruiz MC, 2010, J CUTAN PATHOL, V37, P542, DOI 10.1111/j.1600-0560.2009.01379.x
   GARVIN AJ, 1985, AM J PATHOL, V121, P298
   GESSLER M, 1990, NATURE, V343, P774, DOI 10.1038/343774a0
   Gilks CB, 2004, INT J GYNECOL PATHOL, V23, P200, DOI 10.1097/01.pgp.0000130446.84670.93
   Goldstein NS, 2002, AM J CLIN PATHOL, V117, P541
   Goldstein NS, 2001, AM J CLIN PATHOL, V116, P246
   HABER DA, 1990, CELL, V61, P1257, DOI 10.1016/0092-8674(90)90690-G
   HABER DA, 1991, P NATL ACAD SCI USA, V88, P9618, DOI 10.1073/pnas.88.21.9618
   HARWOOD TR, 1976, AM J CLIN PATHOL, V65, P159
   Hashi A, 2003, INT J GYNECOL PATHOL, V22, P374, DOI 10.1097/01.pgp.0000092130.10100.88
   Hashiba T, 2007, NEUROL MED-CHIR, V47, P165, DOI 10.2176/nmc.47.165
   Hastie ND, 2001, CELL, V106, P391, DOI 10.1016/S0092-8674(01)00469-X
   He HY, 2008, AM J SURG PATHOL, V32A, P884, DOI 10.1097/PAS.0b013e3181609d59
   Hecht JL, 2002, CANCER CYTOPATHOL, V96, P1
   Hill DA, 2000, AM J CLIN PATHOL, V114, P345, DOI 10.1093/ajcp/114.3.345
   Hoehner JC, 1998, LAB INVEST, V78, P29
   Hohenstein P, 2006, HUM MOL GENET, V15, pR196, DOI 10.1093/hmg/ddl196
   Hoot AC, 2004, AM J SURG PATHOL, V28, P1485, DOI 10.1097/01.pas.0000141390.14548.34
   Hwang H, 2004, APPL IMMUNOHISTO M M, V12, P122
   Jemal A, 2007, CA-CANCER J CLIN, V57, P43, DOI 10.3322/canjclin.57.1.43
   Johannessen CM, 2005, P NATL ACAD SCI USA, V102, P8573, DOI 10.1073/pnas.0503224102
   Judkins AR, 2007, ADV ANAT PATHOL, V14, P335, DOI 10.1097/PAP.0b013e3180ca8b08
   Kim A, 2014, WORLD J SURG ONCOL, V12, DOI 10.1186/1477-7819-12-214
   Klebe S, 2010, MODERN PATHOL, V23, P470, DOI 10.1038/modpathol.2009.180
   Koesters R, 2004, INT J CANCER, V109, P385, DOI 10.1002/ijc.11721
   KREIDBERG JA, 1993, CELL, V74, P679, DOI 10.1016/0092-8674(93)90515-R
   Kushitani K, 2008, PATHOL INT, V58, P75, DOI 10.1111/j.1440-1827.2007.02193.x
   Lee AHS, 2007, HISTOPATHOLOGY, V51, P824, DOI 10.1111/j.1365-2559.2007.02884.x
   Lee BH, 2002, AM J CLIN PATHOL, V117, P745, DOI 10.1309/QLV6-HH0H-UCTF-WEF6
   Lee SB, 2001, EXP CELL RES, V264, P74, DOI 10.1006/excr.2000.5131
   Li BQ, 2017, ONCOL LETT, V13, P2531, DOI 10.3892/ol.2017.5784
   Little M, 1999, BIOESSAYS, V21, P191, DOI 10.1002/(SICI)1521-1878(199903)21:3<191::AID-BIES3>3.0.CO;2-8
   Loeb DM, 2001, CANCER RES, V61, P921
   Logani S, 2003, AM J SURG PATHOL, V27, P1434, DOI 10.1097/00000478-200311000-00005
   Machado I, 2010, APPL IMMUNOHISTO M M, V18, P150, DOI 10.1097/PAI.0b013e3181b91a51
   Magro G, 2002, VIRCHOWS ARCH, V440, P249, DOI 10.1007/s00428-001-0572-y
   Magro G, 2000, VIRCHOWS ARCH, V437, P406, DOI 10.1007/s004280000250
   Magro G, 2003, HISTOPATHOLOGY, V42, P233, DOI 10.1046/j.1365-2559.2003.01549.x
   Magro G, 1997, HISTOCHEM J, V29, P293, DOI 10.1023/A:1026422514221
   MAGRO G, 1995, HISTOCHEM J, V27, P694
   Magro G., 2001, Pathologica (Genoa), V93, P505
   Magro G, 2007, PATHOL RES PRACT, V203, P827, DOI 10.1016/j.prp.2007.08.005
   Magro G, 2015, ACTA HISTOCHEM, V117, P397, DOI 10.1016/j.acthis.2015.03.011
   Magro G, 2015, ACTA HISTOCHEM, V117, P492, DOI 10.1016/j.acthis.2015.02.012
   Magro G, 2014, ACTA HISTOCHEM, V116, P1134, DOI 10.1016/j.acthis.2014.05.010
   Magro G, 2014, ACTA HISTOCHEM, V116, P905, DOI 10.1016/j.acthis.2014.03.001
   Magro G, 2012, HUM PATHOL, V43, P243, DOI 10.1016/j.humpath.2011.04.027
   Magro G, 2008, PATHOL RES PRACT, V204, P837, DOI 10.1016/j.prp.2008.05.007
   MARSDEN HB, 1983, VIRCHOWS ARCH A, V399, P1
   Martínez-Estrada OM, 2010, NAT GENET, V42, P89, DOI 10.1038/ng.494
   MCCAUGHEY WTE, 1986, PATHOL ANNU, V21, P271
   Menssen HD, 2000, J CANCER RES CLIN, V126, P226, DOI 10.1007/s004320050037
   Michiels JF, 2010, PFLUG ARCH EUR J PHY, V459, P689, DOI 10.1007/s00424-009-0776-6
   Miller-Hodges E, 2012, J PATHOL, V226, P229, DOI 10.1002/path.2977
   MIWA H, 1992, LEUKEMIA, V6, P405
   Miyata Y, 2015, CANCER BIOMARK, V15, P789, DOI 10.3233/CBM-150521
   Moore AW, 1999, DEVELOPMENT, V126, P1845
   Mrowka C, 2000, J AM SOC NEPHROL, V11, pS106
   MUNDLOS S, 1993, DEVELOPMENT, V119, P1329
   Murphy AJ, 2008, HUM PATHOL, V39, P1763, DOI 10.1016/j.humpath.2008.04.019
   Musumeci G, 2015, ACTA HISTOCHEM, V117, P313, DOI 10.1016/j.acthis.2015.02.011
   Nakahara Yukiko, 2004, Brain Tumor Pathol, V21, P113, DOI 10.1007/BF02482185
   Nakatsuka S, 2006, MODERN PATHOL, V19, P804, DOI 10.1038/modpathol.3800588
   Nasomyon T, 2014, ANTICANCER RES, V34, P1333
   Nik SA, 2005, INT J CANCER, V114, P202, DOI 10.1002/ijc.20717
   Niksic M, 2004, HUM MOL GENET, V13, P463, DOI 10.1093/hmg/ddh040
   NORRIS HJ, 1968, CANCER-AM CANCER SOC, V21, P255, DOI 10.1002/1097-0142(196802)21:2<255::AID-CNCR2820210214>3.0.CO;2-5
   Oates J, 2000, HISTOPATHOLOGY, V36, P341
   Oh EJ, 2014, PATHOL RES PRACT, V210, P953, DOI 10.1016/j.prp.2014.06.026
   Oji Y, 1999, JPN J CANCER RES, V90, P194, DOI 10.1111/j.1349-7006.1999.tb00733.x
   Oji Y, 2002, INT J CANCER, V100, P297, DOI 10.1002/ijc.10476
   Oji Y, 2004, CANCER SCI, V95, P822, DOI 10.1111/j.1349-7006.2004.tb02188.x
   Oji Y, 2004, CANCER SCI, V95, P583, DOI 10.1111/j.1349-7006.2004.tb02490.x
   Oji Y, 2003, CANCER SCI, V94, P712, DOI 10.1111/j.1349-7006.2003.tb01507.x
   Ordóñez NG, 2004, HUM PATHOL, V35, P697, DOI 10.1016/j.humpath.2003.11.013
   Ordóñez NG, 2003, AM J SURG PATHOL, V27, P1031, DOI 10.1097/00000478-200308000-00001
   Ordóñez NG, 2000, AM J SURG PATHOL, V24, P598, DOI 10.1097/00000478-200004000-00016
   Oue T, 2011, J PEDIATR SURG, V46, P2233, DOI 10.1016/j.jpedsurg.2011.09.004
   Parenti R, 2015, ACTA HISTOCHEM, V117, P386, DOI 10.1016/j.acthis.2015.03.009
   Parenti R, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0114333
   Parenti R, 2014, ACTA HISTOCHEM, V116, P48, DOI 10.1016/j.acthis.2013.05.003
   Parenti R, 2013, ACTA HISTOCHEM, V115, P70, DOI 10.1016/j.acthis.2012.04.006
   Parham DM, 2012, PEDIATR DEVEL PATHOL, V15, P211, DOI 10.2350/10-12-0953-PB.1
   Plaza JA, 2016, J CUTAN PATHOL, V43, P313, DOI 10.1111/cup.12654
   PRITCHARDJONES K, 1990, NATURE, V346, P194, DOI 10.1038/346194a0
   Ramani P, 1996, J PATHOL, V179, P162, DOI 10.1002/(SICI)1096-9896(199606)179:2<162::AID-PATH545>3.0.CO;2-0
   Rauscher J, 2014, J CLIN PATHOL, V67, P556, DOI 10.1136/jclinpath-2013-202114
   Roberts SGE, 2005, CURR OPIN GENET DEV, V15, P542, DOI 10.1016/j.gde.2005.08.004
   RODECK U, 1994, INT J CANCER, V59, P78, DOI 10.1002/ijc.2910590116
   Rosai Juan., 2011, Rosai and Ackerman's Surgical Pathology 10e
   Salvatorelli L, 2015, ACTA HISTOCHEM, V117, P367, DOI 10.1016/j.acthis.2015.03.010
   Scharnhorst V, 1999, J BIOL CHEM, V274, P23456, DOI 10.1074/jbc.274.33.23456
   Schittenhelm J, 2008, BRAIN PATHOL, V18, P344, DOI 10.1111/j.1750-3639.2008.00127.x
   Schittenhelm J, 2010, CANCER BIOMARK, V7, P73, DOI 10.3233/CBM-2010-0149
   Scholz H, 2005, PHYSIOLOGY, V20, P54, DOI 10.1152/physiol.00048.2004
   Sebire NJ, 2005, APPL IMMUNOHISTO M M, V13, P1, DOI 10.1097/00129039-200503000-00001
   SHARMA PM, 1994, GENE DEV, V8, P720, DOI 10.1101/gad.8.6.720
   SHARMA PM, 1992, CANCER RES, V52, P6407
   Sheng WQ, 2001, AM J CLIN PATHOL, V115, P348
   Shimizu M, 2000, INT J GYNECOL PATHOL, V19, P158, DOI 10.1097/00004347-200004000-00010
   Sigauke E, 2006, MODERN PATHOL, V19, P717, DOI 10.1038/modpathol.3800581
   Singh A, 2012, PATHOL ONCOL RES, V18, P383, DOI 10.1007/s12253-011-9456-x
   Sotobori T, 2006, CANCER-AM CANCER SOC, V106, P2233, DOI 10.1002/cncr.21861
   Taube ET, 2016, GYNECOL ONCOL, V140, P494, DOI 10.1016/j.ygyno.2015.12.018
   Timár J, 2005, HISTOPATHOLOGY, V47, P67, DOI 10.1111/j.1365-2559.2005.02169.x
   Tsuta K, 2009, APPL IMMUNOHISTO M M, V17, P126, DOI 10.1097/PAI.0b013e318187dd26
   Tuna M, 2005, ONCOGENE, V24, P1648, DOI 10.1038/sj.onc.1208345
   Ueda T, 2003, CANCER SCI, V94, P271, DOI 10.1111/j.1349-7006.2003.tb01432.x
   Wagner KD, 2019, CELLS-BASEL, V8, DOI 10.3390/cells8010041
   Wagner KD, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms6852
   Wagner KD, 2002, EMBO J, V21, P1398, DOI 10.1093/emboj/21.6.1398
   Wagner N, 2008, ONCOGENE, V27, P3662, DOI 10.1038/sj.onc.1211044
   Wagner N, 2005, GENE DEV, V19, P2631, DOI 10.1101/gad.346405
   Wagner N, 2008, PFLUG ARCH EUR J PHY, V455, P839, DOI 10.1007/s00424-007-0340-1
   Wagner N, 2006, AM J PHYSIOL-REG I, V291, pR779, DOI 10.1152/ajpregu.00219.2006
   Waldstrom M, 2005, ARCH PATHOL LAB MED, V129, P85
   Wang LL, 2007, AM J SURG PATHOL, V31, P576, DOI 10.1097/01.pas.0000213432.14740.14
   Weiss S., 2008, Enzinger Weiss's Soft Tissue Tumors, V5th
   WICK MR, 1987, AM J CLIN PATHOL, V87, P425, DOI 10.1093/ajcp/87.4.425
   WIGGER HJ, 1976, HUM PATHOL, V7, P613
   Wilsher M, 2007, HISTOPATHOLOGY, V51, P605, DOI 10.1111/j.1365-2559.2007.02843.x
   Young RH, 2005, MODERN PATHOL, V18, pS81, DOI 10.1038/modpathol.3800311
   YOUNG RH, 1983, INT J GYNECOL PATHOL, V1, P325, DOI 10.1097/00004347-198301040-00002
   Zhao CQ, 2007, AM J SURG PATHOL, V31, P1378, DOI 10.1097/PAS.0b013e3180339961
   Zhao CQ, 2009, AM J SURG PATHOL, V33, P354, DOI 10.1097/PAS.0b013e318188373d
NR 165
TC 7
Z9 7
U1 0
U2 5
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
EI 2076-3417
J9 APPL SCI-BASEL
JI Appl. Sci.-Basel
PD JAN
PY 2020
VL 10
IS 1
AR 40
DI 10.3390/app10010040
PG 27
WC Chemistry, Multidisciplinary; Engineering, Multidisciplinary; Materials
   Science, Multidisciplinary; Physics, Applied
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Chemistry; Engineering; Materials Science; Physics
GA KF7DC
UT WOS:000509398900040
OA gold
DA 2025-04-10
ER

PT J
AU Tanabe, Y
   Hirano, A
   Iwasato, T
   Itohara, S
   Araki, K
   Yamaguchi, T
   Ichikawa, T
   Kumanishi, T
   Aizawa, Y
   Takahashi, H
   Kakita, A
   Nawa, H
AF Tanabe, Yasutaka
   Hirano, Akiko
   Iwasato, Takuji
   Itohara, Shigeyoshi
   Araki, Kazuaki
   Yamaguchi, Tsuyoshi
   Ichikawa, Tomio
   Kumanishi, Toshiro
   Aizawa, Yoshifusa
   Takahashi, Hitoshi
   Kakita, Akiyoshi
   Nawa, Hiroyuki
TI Molecular characterization and gene disruption of a novel zinc-finger
   protein, HIT-4, expressed in rodent brain
SO JOURNAL OF NEUROCHEMISTRY
LA English
DT Article
DE alternative splicing; degeneration; gene targeting; seizure;
   vacuolization; zinc-finger protein
ID MESSENGER-RNA; STEM-CELLS; NEURONS; FAMILY; TESTIS; KRAB
AB To identify a novel regulatory factor involved in brain development or synaptic plasticity, we applied the differential display PCR method to mRNA samples from NMDA-stimulated and un-stimulated neocortical cultures. Among 64 cDNA clones isolated, eight clones were novel genes and one of them encodes a novel zinc-finger protein, HIT-4, which is 317 amino acid residues (36-38 kDa) in length and contains seven C2H2 zinc-finger motifs. Rat HIT-4 cDNA exhibits strong homology to human ZNF597 (57% amino acid identity and 72% homology) and identity to rat ZNF597 at the carboxyl region. Furthermore, genomic alignment of HIT-4 cDNA indicates that the alternative use of distinct promoters and exons produces HIT-4 and ZNF597 mRNAs. Northern blotting revealed that HIT-4 mRNA (similar to 6 kb) is expressed in various tissues such as the lung, heart, and liver, but enriched in the brain, while ZNF597 mRNA (similar to 1.5kb) is found only in the testis. To evaluate biological roles of HIT-4/ZNF597, targeted mutagenesis of this gene was performed in mice. Homozygous (-/-) mutation was embryonic lethal, ceasing embryonic organization before cardiogenesis at embryonic day 7.5. Heterozygous (+/-) mice were able to survive but showing cell degeneration and vacuolization of the striatum, cingulate cortex, and their surrounding white matter. These results reveal novel biological and pathological roles of HIT-4 in brain development and/or maintenance.
C1 [Tanabe, Yasutaka; Hirano, Akiko; Araki, Kazuaki; Yamaguchi, Tsuyoshi; Nawa, Hiroyuki] Niigata Univ, Dept Mol Neurobiol, Brain Res Inst, Niigata 9518585, Japan.
   [Tanabe, Yasutaka; Aizawa, Yoshifusa] Niigata Univ, Div Cardiol, Grad Sch Med & Dent Sci, Niigata 9518585, Japan.
   [Iwasato, Takuji; Itohara, Shigeyoshi] RIKEN, Brain Sci Inst, Lab Behav Genet, Saitama, Japan.
   [Ichikawa, Tomio; Kumanishi, Toshiro] Niigata Univ, Dept Mol Neuropathol, Brain Res Inst, Niigata 9518585, Japan.
   [Takahashi, Hitoshi; Kakita, Akiyoshi] Niigata Univ, Dept Pathol, Brain Res Inst, Niigata 9518585, Japan.
C3 Niigata University; Niigata University; RIKEN; Niigata University;
   Niigata University
RP Nawa, H (corresponding author), Niigata Univ, Dept Mol Neurobiol, Brain Res Inst, 1-757 Asahimachi Dori, Niigata 9518585, Japan.
EM hnawa@bri.niigata-u.ac.jp
RI YAMAGUCHI, Tsuyoshi/AAF-1933-2020; Itohara, Shigeyoshi/I-8769-2012
OI YAMAGUCHI, TSUYOSHI/0000-0002-0058-9244
FU Scientific Research in Priority Areas (Comparative Genome); Promotion of
   Niigata University Research Projects
FX We thank Yoshitaka Maeda, Hiroyuki Aoki, and Kyoko Ishii for technical
   assistance. This work was supported by grant-in-aids for Scientific
   Research in Priority Areas (Comparative Genome) and grants for Promotion
   of Niigata University Research Projects.
CR Abe Y, 2009, NEUROSCIENCE, V161, P95, DOI 10.1016/j.neuroscience.2009.03.022
   AFFARA NA, 1994, GENOMICS, V22, P205, DOI 10.1006/geno.1994.1363
   Amada N, 2003, J BIOCHEM, V133, P615, DOI 10.1093/jb/mvg079
   Barbe L, 2008, MOL CELL PROTEOMICS, V7, P499, DOI 10.1074/mcp.M700325-MCP200
   BECKER KG, 1995, HUM MOL GENET, V4, P685, DOI 10.1093/hmg/4.4.685
   BRAY P, 1991, P NATL ACAD SCI USA, V88, P9563, DOI 10.1073/pnas.88.21.9563
   Collins T, 2001, MOL CELL BIOL, V21, P3609, DOI 10.1128/MCB.21.11.3609-3615.2001
   Cox EH, 2000, CURR OPIN CHEM BIOL, V4, P162, DOI 10.1016/S1367-5931(99)00070-8
   Inoue T, 2007, DEV BIOL, V306, P669, DOI 10.1016/j.ydbio.2007.04.003
   Iuchi S, 2001, CELL MOL LIFE SCI, V58, P625, DOI 10.1007/PL00000885
   Iwasato T, 2007, CELL, V130, P742, DOI 10.1016/j.cell.2007.07.022
   Kowalski K, 2002, J BIOL CHEM, V277, P35720, DOI 10.1074/jbc.M204663200
   Krishna SS, 2003, NUCLEIC ACIDS RES, V31, P532, DOI 10.1093/nar/gkg161
   Leon O, 2000, BIOL RES, V33, P21
   Li N, 2007, J BIOCHEM MOL BIOL, V40, P270
   LIANG P, 1992, SCIENCE, V257, P967, DOI 10.1126/science.1354393
   Nam K, 2004, PROTEINS, V56, P685, DOI 10.1002/prot.20170
   Narisawa-Saito M, 1999, NEUROSCIENCE, V88, P1009, DOI 10.1016/S0306-4522(98)00496-5
   Oteiza Patricia I., 2005, Molecular Aspects of Medicine, V26, P245, DOI 10.1016/j.mam.2005.07.012
   PERROTTI D, 1995, MOL CELL BIOL, V15, P6075
   Tascou S, 2001, INT J ONCOL, V18, P567
   Thomas JH, 2009, BMC EVOL BIOL, V9, DOI 10.1186/1471-2148-9-51
   Urrutia R, 2003, GENOME BIOL, V4, DOI 10.1186/gb-2003-4-10-231
   VRANA KE, 1988, MOL CELL BIOL, V8, P1684, DOI 10.1128/MCB.8.4.1684
   Watakabe A, 2007, CEREB CORTEX, V17, P1918, DOI 10.1093/cercor/bhl102
   UNIGENE HOMEPAGE ORG
NR 26
TC 5
Z9 5
U1 0
U2 4
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0022-3042
EI 1471-4159
J9 J NEUROCHEM
JI J. Neurochem.
PD FEB
PY 2010
VL 112
IS 4
BP 1035
EP 1044
DI 10.1111/j.1471-4159.2009.06525.x
PG 10
WC Biochemistry & Molecular Biology; Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Neurosciences & Neurology
GA 546PH
UT WOS:000273822200017
PM 19968752
OA Bronze
DA 2025-04-10
ER

PT J
AU Kohjitani, A
   Fuda, H
   Hanyu, O
   Strott, CA
AF Kohjitani, A
   Fuda, H
   Hanyu, O
   Strott, CA
TI Cloning, characterization and tissue expression of rat SULT2B1a and
   SULT2B1b steroid/sterol sulfotransferase isoforms:: Divergence of the
   rat SULT2B1 gene structure from orthologous human and mouse genes
SO GENE
LA English
DT Article
DE sulfonation; sulfotransferase; gene structure; cholesterol; pregnenolone
ID HUMAN HYDROXYSTEROID SULFOTRANSFERASE; CRYSTAL-STRUCTURE; CHOLESTEROL
   SULFOTRANSFERASE; NEUROSTEROIDS
AB cDNAs for rat SULT2B1 steroid/sterol sulfotransferase isoforms were cloned, and the encoded proteins overexpressed, purified and characterized. The rat SULT2B1a isoform avidly sulfonates pregnenolone but poorly utilizes cholesterol as a substrate, whereas cholesterol is more efficiently sulfonated than pregnenolone by the SULT2B1b isoform; on the other hand, neither isoform sulfonates dehydroepiandrosterone to any significant degree. Real-time PCR revealed that SULT2B1a was only expressed in brain and testis, whereas SULT2B1b was mainly expressed in skin, intestine and kidney. The SULT2B1 gene is unique among steroid/sterol sulfotransferase genes in that it encodes for two isoforms as a result of an alternative exon 1. Interestingly, whereas the orthologous human and mouse SULT2B1 gene structures are identical, the rat SULT2B1 gene structure diverges. Similar to human and mouse SULT2B1 genes the rat SULT2B1 gene consists of an alternative exon 1; however, as a result of exonic rearrangement, the genic locations of exons IA and IB are reversed in the rat gene. Where exon IA is located downstream of exon IB in the human and mouse SULT2B1 genes, in the rat SULT2B1 gene exon IA is located upstream of exon IB. Furthermore, unlike the case with human and mouse SULT2B1 genes where differential splicing is necessitated since a portion of exon IA is fused with exon IB to complete the SULT2B1b mRNA, this step is not required with the rat gene. Published by Elsevier B.V.
C1 NICHHD, Sect Steroid Regulat, Endocrinol & Reprod Res Branch, NIH, Bethesda, MD 20892 USA.
C3 National Institutes of Health (NIH) - USA; NIH Eunice Kennedy Shriver
   National Institute of Child Health & Human Development (NICHD)
RP NICHHD, Sect Steroid Regulat, Endocrinol & Reprod Res Branch, NIH, Bethesda, MD 20892 USA.
EM chastro@mail.nih.gov
CR Alomary AA, 2001, INT REV NEUROBIOL, V46, P97
   Baulieu EE, 2001, INT REV NEUROBIOL, V46, P1
   Baulieu EE, 1998, PSYCHONEUROENDOCRINO, V23, P963, DOI 10.1016/S0306-4530(98)00071-7
   Engel SR, 2001, INT REV NEUROBIOL, V46, P321
   Fuda H, 2002, J BIOL CHEM, V277, P36161, DOI 10.1074/jbc.M207165200
   Geese WJ, 2001, BIOCHEM BIOPH RES CO, V288, P280, DOI 10.1006/bbrc.2001.5746
   Her C, 1998, GENOMICS, V53, P284, DOI 10.1006/geno.1998.5518
   Higashi Y, 2004, J INVEST DERMATOL, V122, P1207, DOI 10.1111/j.0022-202X.2004.22416.x
   IWAMORI M, 1976, BIOCHIM BIOPHYS ACTA, V441, P268, DOI 10.1016/0005-2760(76)90170-3
   Javitt NB, 2001, ENDOCRINOLOGY, V142, P2978, DOI 10.1210/en.142.7.2978
   Kakuta Y, 1997, NAT STRUCT BIOL, V4, P904, DOI 10.1038/nsb1197-904
   MOUNT SM, 1982, NUCLEIC ACIDS RES, V10, P459, DOI 10.1093/nar/10.2.459
   Nagata K, 2000, ANNU REV PHARMACOL, V40, P159, DOI 10.1146/annurev.pharmtox.40.1.159
   Pedersen LC, 2000, FEBS LETT, V475, P61, DOI 10.1016/S0014-5793(00)01479-4
   Pedersen LC, 2002, J BIOL CHEM, V277, P17928, DOI 10.1074/jbc.M111651200
   Plassart-Schiess E, 2001, BRAIN RES REV, V37, P133, DOI 10.1016/S0165-0173(01)00113-8
   Shimizu C, 2003, ENDOCRINOLOGY, V144, P1186, DOI 10.1210/en.2002-221011
   Strott CA, 2003, J LIPID RES, V44, P1268, DOI 10.1194/jlr.R300005-JLR200
   Strott CA, 2002, ENDOCR REV, V23, P703, DOI 10.1210/er.2001-0040
   THOMPSON JD, 1994, NUCLEIC ACIDS RES, V22, P4673, DOI 10.1093/nar/22.22.4673
NR 20
TC 27
Z9 32
U1 0
U2 5
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
SN 0378-1119
EI 1879-0038
J9 GENE
JI Gene
PD FEB 15
PY 2006
VL 367
BP 66
EP 73
DI 10.1016/j.gene.2005.09.009
PG 8
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA 026BZ
UT WOS:000236313000006
PM 16368200
DA 2025-04-10
ER

PT J
AU Zhao, LQ
   O'Neill, K
   Brinton, RD
AF Zhao, LQ
   O'Neill, K
   Brinton, RD
TI Selective estrogen receptor modulators (SERMs) for the brain: Current
   status and remaining challenges for developing NeuroSERMs
SO BRAIN RESEARCH REVIEWS
LA English
DT Review
DE estrogen; ET; SERM; cognition; neuroprotection; Alzheimer's disease
ID ACTIVATED PROTEIN-KINASE; HORMONE REPLACEMENT THERAPY; HUMAN
   BREAST-CANCER; RANDOMIZED CONTROLLED-TRIAL; HEALTH INITIATIVE MEMORY;
   CHOLINE-ACETYLTRANSFERASE ACTIVITY; CULTURED HIPPOCAMPAL-NEURONS;
   CONJUGATED EQUINE ESTROGENS; MILD COGNITIVE IMPAIRMENT; BONE-MINERAL
   DENSITY
AB Multiple issues regarding the efficacy of estrogen action in the brain remain unresolved. These include the timing, formulation and duration of the therapy intervention. Moreover, issues of thrombotic and neoplastic risks must be factored into the design of estrogen alternatives developed to prevent age-associated neurodegenerative disorders, as well as other climacteric symptoms such as hot flush and sleep dysfunction. One strategy to address these issues is to develop molecules that selectively target and activate estrogen mechanisms of action in the brain while avoiding activation of estrogen receptors peripheral to the brain, particularly in reproductive organs. An overview of recent advances in our understanding of the molecular mechanisms of estrogen action is discussed in the context of designing an efficacious NeuroSERM that will activate cellular, biochemical and genomic events required for the promotion of memory function and neuronal survival. Pharmacological analyses of estrogen receptor subtypes and the case for a membrane-associated estrogen receptor splice variant in mediating these mechanisms are provided along with a summary of the activation profiles of existing clinically relevant estrogen alternatives or SERMs in neurons. Results of these endeavors have yielded insights into strategies for developing novel molecules with NeuroSERM potential in order to prevent brain related climacteric symptoms and neurodegenerative diseases. (c) 2005 Elsevier B.V. All rights reserved.
C1 Univ So Calif, Dept Mol Pharmacol & Toxciol, Pharmaceut Sci Ctr, Sch Pharm, Los Angeles, CA 90089 USA.
   Univ So Calif, Program Neurosci, Pharmaceut Sci Ctr, Sch Pharm, Los Angeles, CA 90089 USA.
C3 University of Southern California; University of Southern California
RP Univ So Calif, Dept Mol Pharmacol & Toxciol, Pharmaceut Sci Ctr, Sch Pharm, Los Angeles, CA 90089 USA.
EM rbrinton@hsc.usc.edu
OI Brinton, Roberta/0000-0001-8450-772X
FU NIA NIH HHS [P01 AG1475] Funding Source: Medline; NIMH NIH HHS [R01
   MH67159] Funding Source: Medline
CR Adams MM, 2002, J NEUROSCI, V22, P3608
   ARONICA SM, 1993, MOL ENDOCRINOL, V7, P743, DOI 10.1210/me.7.6.743
   Baker VL, 1998, J CLIN ENDOCR METAB, V83, P6, DOI 10.1210/jc.83.1.6
   Balabhadrapathruni S, 2000, ONCOL REP, V7, P3
   Beato M, 2000, HUM REPROD UPDATE, V6, P225, DOI 10.1093/humupd/6.3.225
   Beyer C, 2003, ANN NY ACAD SCI, V1007, P17, DOI 10.1196/annals.1286.002
   Beyer C, 2003, J NEUROCHEM, V87, P545, DOI 10.1046/j.1471-4159.2003.02042.x
   Biskobing DM, 2003, EXPERT OPIN INV DRUG, V12, P611, DOI 10.1517/13543784.12.4.611
   Bowers JL, 2000, ENDOCRINOLOGY, V141, P3657, DOI 10.1210/en.141.10.3657
   Brinton R.D, 2004, ESTROGEN THERAPY PRE
   BRINTON RD, 1993, MOL CELL NEUROSCI, V4, P36, DOI 10.1006/mcne.1993.1005
   Brinton RD, 2000, NEUROBIOL AGING, V21, P475, DOI 10.1016/S0197-4580(00)00109-3
   Brinton RD, 2004, CNS DRUGS, V18, P405, DOI 10.2165/00023210-200418070-00001
   Brinton RD, 1997, EXP NEUROL, V147, P211, DOI 10.1006/exnr.1997.6619
   Brinton RD, 2003, JAMA-J AM MED ASSOC, V290, P1706, DOI 10.1001/jama.290.13.1706-a
   Brinton RD, 2002, DRUG DEVELOP RES, V56, P380, DOI 10.1002/ddr.10090
   Brinton RD, 1999, INT J FERTIL WOMEN M, V44, P174
   Brinton RD, 2001, LEARN MEMORY, V8, P121, DOI 10.1101/lm.39601
   BRINTON RD, 2004, Patent No. 60562787
   BRINTON RD, 2001, ABSTR SOC NEUR
   BRINTON RD, 2001, INT ENCY SOC BEHAV S, V21, P13946
   BRINTON RD, 2002, ABSTR SOC NEUR
   Brookmeyer R, 1998, AM J PUBLIC HEALTH, V88, P1337, DOI 10.2105/AJPH.88.9.1337
   BRUNING PF, 1992, EUR J CANCER, V28A, P1404, DOI 10.1016/0959-8049(92)90530-F
   Brzozowski AM, 1997, NATURE, V389, P753, DOI 10.1038/39645
   Carlson MC, 2001, NEUROLOGY, V57, P2210, DOI 10.1212/WNL.57.12.2210
   COEZY E, 1982, CANCER RES, V42, P317
   Cohen FJ, 2000, MATURITAS, V34, P65, DOI 10.1016/S0378-5122(99)00090-0
   COLE MP, 1971, BRIT J CANCER, V25, P270, DOI 10.1038/bjc.1971.33
   Cordey M, 2003, J NEUROCHEM, V84, P1340, DOI 10.1046/j.1471-4159.2003.01631.x
   Datta SR, 1997, CELL, V91, P231, DOI 10.1016/S0092-8674(00)80405-5
   DAUVOIS S, 1993, J CELL SCI, V106, P1377
   DAUVOIS S, 1992, P NATL ACAD SCI USA, V89, P4037, DOI 10.1073/pnas.89.9.4037
   Delmas PD, 1997, NEW ENGL J MED, V337, P1641, DOI 10.1056/NEJM199712043372301
   DENG J, 2004, ABSTR SOC NEUROSCI
   Dixon-Shanies D, 1999, ONCOL REP, V6, P1383
   Dubal DB, 1999, J NEUROSCI, V19, P6385
   Dubal DB, 2001, P NATL ACAD SCI USA, V98, P1952, DOI 10.1073/pnas.98.4.1952
   Dykens JA, 2003, EXP GERONTOL, V38, P101, DOI 10.1016/S0531-5565(02)00162-6
   Ellis PA, 1997, INT J CANCER, V72, P608, DOI 10.1002/(SICI)1097-0215(19970807)72:4<608::AID-IJC10>3.0.CO;2-7
   EPPENBERGER U, 1991, AM J CLIN ONCOL-CANC, V14, pS5
   Espeland MA, 2004, JAMA-J AM MED ASSOC, V291, P2959, DOI 10.1001/jama.291.24.2959
   FAWELL SE, 1990, P NATL ACAD SCI USA, V87, P6883, DOI 10.1073/pnas.87.17.6883
   Fillit H, 2002, FAM MED, V34, P528
   Fillit H, 2002, DRUG DISCOV TODAY, V7, P785, DOI 10.1016/S1359-6446(02)02379-6
   Fillit HM, 2002, J MOL NEUROSCI, V19, P249, DOI 10.1007/s12031-002-0001-y
   Fillit HM, 2002, ARCH INTERN MED, V162, P1934, DOI 10.1001/archinte.162.17.1934
   Fillit HM, 2000, AM J MANAG CARE, V6, pS1139
   Fitzpatrick JL, 2002, J NEUROCHEM, V82, P674, DOI 10.1046/j.1471-4159.2002.01000.x
   Foster TC, 2002, NEUROSCIENTIST, V8, P297, DOI 10.1177/107385840200800404
   Foy MR, 1999, J NEUROPHYSIOL, V81, P925, DOI 10.1152/jn.1999.81.2.925
   Gao S, 1998, ARCH GEN PSYCHIAT, V55, P809, DOI 10.1001/archpsyc.55.9.809
   Genazzani AR, 1999, GYNECOL ENDOCRINOL, V13, P249, DOI 10.3109/09513599909167563
   Gerber B, 1999, Gynakol Geburtshilfliche Rundsch, V39, P136, DOI 10.1159/000022295
   Grandbois M, 2000, NEUROREPORT, V11, P343, DOI 10.1097/00001756-200002070-00024
   Green P S, 2000, Novartis Found Symp, V230, P202, DOI 10.1002/0470870818.ch15
   Green PS, 2001, ENDOCRINOLOGY, V142, P400, DOI 10.1210/en.142.1.400
   Green PS, 2000, INT J DEV NEUROSCI, V18, P347, DOI 10.1016/S0736-5748(00)00017-4
   GRILL HJ, 1991, AM J CLIN ONCOL-CANC, V14, pS21
   Guo J, 2004, NEUROSCI LETT, V355, P177, DOI 10.1016/j.neulet.2003.10.076
   Gustaftson JÅ, 2003, TRENDS PHARMACOL SCI, V24, P479, DOI 10.1016/S0165-6147(03)00229-3
   HAMMOND CB, 1994, FERTIL STERIL, V62, pS157
   Harris HA, 2002, ENDOCRINOLOGY, V143, P4172, DOI 10.1210/en.2002-220403
   Henderson V W, 2000, Novartis Found Symp, V230, P254, DOI 10.1002/0470870818.ch18
   Henderson V.W., 2000, Hormone therapy and the brain: a clinical perspective on the role of estrogen
   Henderson VW, 2000, NEUROLOGY, V54, P295, DOI 10.1212/WNL.54.2.295
   Henderson VW, 1997, NEUROLOGY, V48, pS27, DOI 10.1212/WNL.48.5_Suppl_7.27S
   Hirata S, 2003, TRENDS ENDOCRIN MET, V14, P124, DOI 10.1016/S1043-2760(03)00028-6
   Howell A, 2000, CANCER-AM CANCER SOC, V89, P817, DOI 10.1002/1097-0142(20000815)89:4<817::AID-CNCR14>3.0.CO;2-6
   IGNARTROWBRIDGE DM, 1993, MOL ENDOCRINOL, V7, P992, DOI 10.1210/me.7.8.992
   Jakacka M, 2001, J BIOL CHEM, V276, P13615, DOI 10.1074/jbc.M008384200
   JORDAN VC, 1977, J ENDOCRINOL, V75, P305, DOI 10.1677/joe.0.0750305
   JORDAN VC, 1975, EUR J CANCER, V11, P205, DOI 10.1016/0014-2964(75)90119-X
   KAWAMURA I, 1991, JPN J PHARMACOL, V57, P215, DOI 10.1254/jjp.57.215
   Kawas C, 1997, NEUROLOGY, V48, P1517, DOI 10.1212/WNL.48.6.1517
   Kreijkamp-Kaspers S, 2004, JAMA-J AM MED ASSOC, V292, P65, DOI 10.1001/jama.292.1.65
   KUMAR V, 1988, CELL, V55, P145, DOI 10.1016/0092-8674(88)90017-7
   LaFerla FM, 2002, NAT REV NEUROSCI, V3, P862, DOI 10.1038/nrn960
   LANDFIELD PW, 1994, ANN NY ACAD SCI, V747, P351
   LeBlanc ES, 2001, JAMA-J AM MED ASSOC, V285, P1489, DOI 10.1001/jama.285.11.1489
   LEE J, 2003, ABSTR SOC NEUROSCI
   Lee SJ, 2004, NEUROSCIENCE, V124, P549, DOI 10.1016/j.neuroscience.2003.11.035
   Lewandowski S, 2002, FEBS LETT, V524, P1, DOI 10.1016/S0014-5793(02)03015-6
   Li L, 2003, P NATL ACAD SCI USA, V100, P4807, DOI 10.1073/PNAS.0831079100
   LIPPMAN ME, 1975, NATURE, V256, P592, DOI 10.1038/256592a0
   Liu R, 2002, STROKE, V33, P2485, DOI 10.1161/01.STR.0000030317.43597.C8
   LUINE VN, 1985, EXP NEUROL, V89, P484, DOI 10.1016/0014-4886(85)90108-6
   MAKELA S, 1995, ENVIRON HEALTH PERSP, V103, P123, DOI 10.2307/3432520
   Mäkelä S, 1999, P NATL ACAD SCI USA, V96, P7077, DOI 10.1073/pnas.96.12.7077
   Maki PM, 2001, AM J PSYCHIAT, V158, P227, DOI 10.1176/appi.ajp.158.2.227
   Manson JE, 2003, NEW ENGL J MED, V349, P523, DOI 10.1056/NEJMoa030808
   MASRI R, 2004, ABSTR SOC NEUROSCI
   MATTSON MP, 1993, TRENDS NEUROSCI, V16, P409, DOI 10.1016/0166-2236(93)90009-B
   Mattson MP, 2000, TRENDS NEUROSCI, V23, P222, DOI 10.1016/S0166-2236(00)01548-4
   McEwen B, 2002, RECENT PROG HORM RES, V57, P357, DOI 10.1210/rp.57.1.357
   Meyers MJ, 2001, J MED CHEM, V44, P4230, DOI 10.1021/jm010254a
   Migliaccio A, 1996, EMBO J, V15, P1292, DOI 10.1002/j.1460-2075.1996.tb00471.x
   Miller MM, 2001, ANN NY ACAD SCI, V949, P223
   Mitlak BH, 1997, HORM RES, V48, P155, DOI 10.1159/000185507
   Mitra SW, 2003, ENDOCRINOLOGY, V144, P2055, DOI 10.1210/en.2002-221069
   Mize AL, 2003, ENDOCRINOLOGY, V144, P306, DOI 10.1210/en.2002-220698
   Mosselman S, 1996, FEBS LETT, V392, P49, DOI 10.1016/0014-5793(96)00782-X
   Mulnard RI, 2000, JAMA-J AM MED ASSOC, V283, P1007, DOI 10.1001/jama.283.8.1007
   Murphy LC, 1997, J STEROID BIOCHEM, V62, P363, DOI 10.1016/S0960-0760(97)00084-8
   *NAM SOC, 2003, MEN COR CURR STUD GU
   Nethrapalli IS, 2001, ENDOCRINOLOGY, V142, P5145, DOI 10.1210/en.142.12.5145
   NEURGARTEN BL, 1965, PSYCHOSOM MED, V27, P266
   Nicholson RI, 1996, ANN NY ACAD SCI, V784, P325, DOI 10.1111/j.1749-6632.1996.tb16247.x
   Nilsen J, 2003, P NATL ACAD SCI USA, V100, P10506, DOI 10.1073/pnas.1334098100
   Nilsen J, 1998, MENOPAUSE, V5, P211
   Nilsen J, 2002, BRAIN RES, V930, P216, DOI 10.1016/S0006-8993(02)02254-0
   Nilsen J, 2003, P NATL ACAD SCI USA, V100, P2842, DOI 10.1073/pnas.0438041100
   Nilsen J, 2002, NEUROREPORT, V13, P825, DOI 10.1097/00001756-200205070-00018
   Nilsen J, 2002, ENDOCRINOLOGY, V143, P205, DOI 10.1210/en.143.1.205
   Nilsen J, 2004, CNS NEUROL DISORD-DR, V3, P297, DOI 10.2174/1568007043337193
   Nilsson S, 2001, PHYSIOL REV, V81, P1535, DOI 10.1152/physrev.2001.81.4.1535
   O'Neill K, 2004, EXP NEUROL, V188, P268, DOI 10.1016/j.expneurol.2004.01.014
   O'Neill K, 2004, EXP NEUROL, V185, P63, DOI 10.1016/j.expneurol.2003.09.005
   ONEILL K, 2002, ABSTR SOC NEUR
   ONEILL K, 2004, ABSTR SOC NEUROSCI
   Österlund MK, 2000, NEUROSCIENCE, V95, P333
   Österlund MK, 2000, J CLIN ENDOCR METAB, V85, P3840, DOI 10.1210/jc.85.10.3840
   Paganini-Hill A, 2000, BREAST CANCER RES TR, V64, P165, DOI 10.1023/A:1006426132338
   Pan YL, 2000, MENOPAUSE, V7, P230, DOI 10.1097/00042192-200007040-00004
   Pasqualini C, 2001, MOL ENDOCRINOL, V15, P894, DOI 10.1210/me.15.6.894
   Petersen DN, 1998, ENDOCRINOLOGY, V139, P1082, DOI 10.1210/en.139.3.1082
   Pike ACW, 2001, STRUCTURE, V9, P145, DOI 10.1016/S0969-2126(01)00568-8
   Pike CJ, 1999, J NEUROCHEM, V72, P1552, DOI 10.1046/j.1471-4159.1999.721552.x
   Poola I, 2002, FEBS LETT, V516, P133, DOI 10.1016/S0014-5793(02)02521-8
   Poola I, 2000, J STEROID BIOCHEM, V72, P249, DOI 10.1016/S0960-0760(00)00033-9
   POSNER MI, 1988, SCIENCE, V240, P1627, DOI 10.1126/science.3289116
   Price RH, 2001, ENDOCRINOLOGY, V142, P2039, DOI 10.1210/en.142.5.2039
   Price RH, 2000, MOL BRAIN RES, V80, P260, DOI 10.1016/S0169-328X(00)00135-2
   Price RH, 2000, NEUROSCI LETT, V288, P115, DOI 10.1016/S0304-3940(00)01221-0
   Prokai L, 2003, P NATL ACAD SCI USA, V100, P11741, DOI 10.1073/pnas.2032621100
   Purdie DW, 1999, BRIT J CLIN PHARMACO, V48, P785
   Razandi M, 2003, MOL CELL BIOL, V23, P1633, DOI 10.1128/MCB.23.5.1633-1646.2003
   Razandi M, 1999, MOL ENDOCRINOL, V13, P307, DOI 10.1210/me.13.2.307
   Resnick SM, 1997, NEUROLOGY, V49, P1491, DOI 10.1212/WNL.49.6.1491
   Rice M., 1995, GERONTOLOGIST, V35, P169
   Rissman EF, 2002, P NATL ACAD SCI USA, V99, P3996, DOI 10.1073/pnas.012032699
   Sato M, 1996, FASEB J, V10, P905, DOI 10.1096/fasebj.10.8.8666168
   Savaskan E, 2001, BRAIN RES, V908, P113, DOI 10.1016/S0006-8993(01)02610-5
   Sawada H, 2000, NEUROSCI BIOBEHAV R, V24, P143, DOI 10.1016/S0149-7634(99)00059-7
   SCHWABE JW, 2004, SCI STKE, pPE4
   Shang YF, 2002, SCIENCE, V295, P2465, DOI 10.1126/science.1068537
   SHERWIN BB, 1988, PSYCHONEUROENDOCRINO, V13, P345, DOI 10.1016/0306-4530(88)90060-1
   SHERWIN BB, 1999, TREATMENT POSTMENOPA, P179
   SHIMPKINS JW, 2002, Patent No. 6319914
   Shughrue PJ, 1997, J COMP NEUROL, V388, P507, DOI 10.1002/(SICI)1096-9861(19971201)388:4<507::AID-CNE1>3.0.CO;2-6
   Shughrue PJ, 2000, FRONT NEUROENDOCRIN, V21, P95, DOI 10.1006/frne.1999.0190
   Shumaker SA, 2004, JAMA-J AM MED ASSOC, V291, P2947, DOI 10.1001/jama.291.24.2947
   Shumaker SA, 2003, JAMA-J AM MED ASSOC, V289, P2651, DOI 10.1001/jama.289.20.2651
   Sibonga JD, 1998, ENDOCRINOLOGY, V139, P3736, DOI 10.1210/en.139.9.3736
   Simoncini T, 2000, NATURE, V407, P538, DOI 10.1038/35035131
   SIMPKINS JW, 2002, Patent No. 6339078
   Singh M, 1999, J NEUROSCI, V19, P1179
   Singh M, 2001, ENDOCRINE, V14, P407, DOI 10.1385/ENDO:14:3:407
   SMITH CL, 1993, P NATL ACAD SCI USA, V90, P6120, DOI 10.1073/pnas.90.13.6120
   Stahl S, 1998, TOXICOL APPL PHARM, V152, P41, DOI 10.1006/taap.1998.8500
   Stauffer SR, 2000, J MED CHEM, V43, P4934, DOI 10.1021/jm000170m
   Suh N, 2001, CANCER RES, V61, P8412
   Sun J, 2003, MOL ENDOCRINOL, V17, P247, DOI 10.1210/me.2002-0341
   Tang MX, 1996, LANCET, V348, P429, DOI 10.1016/S0140-6736(96)03356-9
   Taylor AH, 2000, J MOL ENDOCRINOL, V24, P145, DOI 10.1677/jme.0.0240145
   Thibault O, 1998, CELL CALCIUM, V24, P417, DOI 10.1016/S0143-4160(98)90064-1
   Thomas SM, 1997, ANNU REV CELL DEV BI, V13, P513, DOI 10.1146/annurev.cellbio.13.1.513
   TORA L, 1989, CELL, V59, P477, DOI 10.1016/0092-8674(89)90031-7
   Toran-Allerand C D, 2000, Novartis Found Symp, V230, P56, DOI 10.1002/0470870818.ch6
   Toran-Allerand CD, 2002, J NEUROSCI, V22, P8391
   Toran-Allerand CD, 2004, ENDOCRINOLOGY, V145, P1069, DOI 10.1210/en.2003-1462
   WAKELING AE, 1991, CANCER RES, V51, P3867
   WAKELING AE, 1988, J STEROID BIOCHEM, V31, P645, DOI 10.1016/0022-4731(88)90014-3
   Wang CF, 1997, NUTR CANCER, V28, P236, DOI 10.1080/01635589709514582
   Wang L, 2003, P NATL ACAD SCI USA, V100, P703, DOI 10.1073/pnas.242735799
   Wang L, 2001, P NATL ACAD SCI USA, V98, P2792, DOI 10.1073/pnas.041617498
   Wassertheil-Smoller S, 2003, JAMA-J AM MED ASSOC, V289, P2673, DOI 10.1001/jama.289.20.2673
   Watson CS, 2002, STEROIDS, V67, P429, DOI 10.1016/S0039-128X(01)00172-6
   WATSON CS, 1995, ENVIRON HEALTH PERSP, V103, P41, DOI 10.2307/3432507
   Watters JJ, 1997, ENDOCRINOLOGY, V138, P4030, DOI 10.1210/en.138.9.4030
   WEBB P, 1995, MOL ENDOCRINOL, V9, P443, DOI 10.1210/me.9.4.443
   Wijayaratne AL, 1999, ENDOCRINOLOGY, V140, P5828, DOI 10.1210/en.140.12.5828
   Wilson ME, 2002, MECH AGEING DEV, V123, P593, DOI 10.1016/S0047-6374(01)00406-7
   Wise PM, 2001, BRAIN RES REV, V37, P313, DOI 10.1016/S0165-0173(01)00136-9
   WOOLLEY CS, 1994, J NEUROSCI, V14, P7680
   WU TW, 2003, ABSTR SOC NEUROSCI
   WU TW, IN PRESS NEUROSCIENC
   WU TW, 2004, ABSTR SOC NEUROSCI
   Wu X, 1999, BRAIN RES, V847, P98, DOI 10.1016/S0006-8993(99)02062-4
   Wymann MP, 1998, BBA-MOL CELL BIOL L, V1436, P127, DOI 10.1016/S0005-2760(98)00139-8
   Yaffe K, 1998, JAMA-J AM MED ASSOC, V279, P688, DOI 10.1001/jama.279.9.688
   Yaffe K, 2001, NEW ENGL J MED, V344, P1207, DOI 10.1056/NEJM200104193441604
   Yang NN, 1996, ENDOCRINOLOGY, V137, P2075, DOI 10.1210/en.137.5.2075
   Yang SH, 2004, P NATL ACAD SCI USA, V101, P4130, DOI 10.1073/pnas.0306948101
   Yang SH, 2003, ANN NY ACAD SCI, V1007, P101, DOI 10.1196/annals.1286.010
   Zandi PP, 2002, JAMA-J AM MED ASSOC, V288, P2123, DOI 10.1001/jama.288.17.2123
   Zandi PP, 2002, NEUROLOGY, V59, P880, DOI 10.1212/WNL.59.6.880
   Zhang JQ, 2002, BRAIN RES, V935, P73, DOI 10.1016/S0006-8993(02)02460-5
   Zhang WH, 2003, FEBS LETT, V546, P17, DOI 10.1016/S0014-5793(03)00436-8
   ZHAO L, IN PRESS NEUROSCIENC
   ZHAO L, 2004, ABSTR SOC NEUROSCI
   ZHAO L, 1997, NUTR CANC, V27, P31
   ZHAO L, 2004, TRANSLATING BASIC SC
   Zhao LQ, 2004, BRAIN RES, V1010, P22, DOI 10.1016/j.brainres.2004.02.066
   Zhao LX, 2003, EXP BIOL MED, V228, P823, DOI 10.1177/15353702-0322807-08
   Zhao LX, 2002, EXP BIOL MED, V227, P509, DOI 10.1177/153537020222700716
   Znamensky V, 2003, J NEUROSCI, V23, P2340
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TC 86
Z9 98
U1 0
U2 22
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 0165-0173
EI 1872-6321
J9 BRAIN RES REV
JI Brain Res. Rev.
PD NOV
PY 2005
VL 49
IS 3
BP 472
EP 493
DI 10.1016/j.brainresrev.2005.01.009
PG 22
WC Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA 987KH
UT WOS:000233516300003
PM 16269315
DA 2025-04-10
ER

PT J
AU Wimalawansa, SJ
AF Wimalawansa, SJ
TI Amylin, calcitonin gene-related peptide, calcitonin, and adrenomedullin:
   A peptide superfamily
SO CRITICAL REVIEWS IN NEUROBIOLOGY
LA English
DT Review
DE molecular genetics; peptide receptors; molecular modeling; gene cloning;
   new drug development; therapeutic options; diabetes
ID ISLET-AMYLOID POLYPEPTIDE; CENTRAL-NERVOUS-SYSTEM;
   MEDULLARY-THYROID-CARCINOMA; DEPENDENT DIABETES-MELLITUS;
   CONGESTIVE-HEART-FAILURE; CALCIUM-REGULATING HORMONES; CYCLIC-AMP
   FORMATION; AMINO-ACID-SEQUENCE; CIRCULAR-DICHROISM SPECTROSCOPY;
   SPONTANEOUSLY HYPERTENSIVE RAT
AB The calcitonin gene peptide superfamily consists of calcitonin (CT), calcitonin gene-related peptide (CGRP), and amylin. CT and CGRP derive from the CT/CGRP gene, which is encoded on chromosome 11. Alternative splicing of the primary RNA transcript leads to the translation of CGRP and CT. peptides in a tissue-specific manner. CGRP (a 37-amino-acid neuropeptide) and its receptors are widely distributed in the body, and it is the most potent endogenous vasodilatory peptide discovered so far. CT (a 32-amino-acid peptide) is, however, a hormone primarily involved in protecting the skeleton during periods of ''calcium stress'' such as growth, pregnancy, and lactation. CT derives from the C cells of the thyroid gland and is the most potent peptide inhibitor of osteoclast-mediated bone resorption. Therefore, treatment with CT is highly effective for conditions associated with increased bone turnover such as Pager's disease, osteoporosis, Sudeck's atrophy, and hypercalcemia. Amylin (a 37-amino-acid peptide) is generated from a gene located on chromosome 12 (thought to be an evolutionary duplication of chromosome 11) and shares 46% amino acid sequence homology with CGRP and 20% with human CT. Amylin is predominantly located in the beta cells of the islets of the pancreas and may be involved in the pathogenesis of type IT diabetes by deposition as amyloid within the pancreas, leading to beta cell destruction. Adrenomedullin, a recently discovered 52-amino-acid vasoactive peptide from adrenal tissue, shares 24% homology with CGRP and is also a member of this superfamily of peptides. A portion of the B-chain of insulin is strongly homologous to these four peptides. Not only does adrenomedullin (13-52) show 24% amino acid homology with CGRP, it also has a biological activity profile similar to that of CGRP. CGRP, CT, and amylin are related to the insulin gene superfamily of peptides, which may all have diverged from a common ancestral gene during evolution. When the crystallographic and nuclear magnetic resonance-based molecular modeling of the three-dimensional structure of CGRP, CT, amylin, and adrenomedullin peptides and their receptors is available, it will lead to a greater understanding of the involvement of this family of peptides in pathophysiology. Together, CGRP, CT, amylin and adrenomedullin have overlapping biological effects owing to their structures and cross-reactivity between receptors. I propose that CT, CGRP, adrenomedullin, and amylin belong to a family of G-protein-coupled receptors (an ''insulin superfamily'' of peptides) and therefore share some of the characteristics of insulin, such as growth factor-like effects, and possible interaction at insulin receptor sites as an antagonist.
C1 UNIV TEXAS, MED BRANCH, DIV ENDOCRINOL, DEPT INTERNAL MED, GALVESTON, TX 77555 USA.
C3 University of Texas System; University of Texas Medical Branch Galveston
RP UNIV TEXAS, MED BRANCH,DEPT INTERNAL MED,DIV GEN MED, 301 UNIV BLVD, 8-104 MED RES BLDG, GALVESTON, TX 77555 USA.
OI Wimalawansa, Prof. Sunil/0000-0003-1096-8595
CR ABDELRAHMAN A, 1992, BRIT J PHARMACOL, V106, P45, DOI 10.1111/j.1476-5381.1992.tb14290.x
   Aiyar N, 1996, J BIOL CHEM, V271, P11325, DOI 10.1074/jbc.271.19.11325
   AKIMOTO K, 1993, ACTA PAEDIATR, V82, P310, DOI 10.1111/j.1651-2227.1993.tb12669.x
   ALAM ASMT, 1991, BIOCHEM BIOPH RES CO, V179, P134
   ALBRANDT K, 1992, BIOCHIM BIOPHYS ACTA, V1130, P97, DOI 10.1016/0167-4781(92)90470-K
   ALEVIZAKI M, 1986, FEBS LETT, V206, P47, DOI 10.1016/0014-5793(86)81338-2
   ALLAN E, 1983, PHARMATHERAPEUTICA, V3, P482
   ALLISON J, 1981, BIOCHEM J, V199, P725, DOI 10.1042/bj1990725
   AMARA SG, 1980, P NATL ACAD SCI-BIOL, V77, P4444, DOI 10.1073/pnas.77.8.4444
   AMARA SG, 1982, NATURE, V298, P240, DOI 10.1038/298240a0
   AMARA SG, 1985, SCIENCE, V229, P1094, DOI 10.1126/science.2994212
   ANAND IS, 1991, J AM COLL CARDIOL, V17, P208, DOI 10.1016/0735-1097(91)90729-S
   ANDRUS L, 1988, J BIOL CHEM, V263, P6183
   [Anonymous], 1987, BRIT MED J, V295, P914
   ARDEN WA, 1994, CIRC SHOCK, V42, P147
   ARIENTA C, 1991, BRAIN RES BULL, V27, P605, DOI 10.1016/0361-9230(91)90034-H
   AYACHI S, 1979, METABOLISM, V28, P1234, DOI 10.1016/0026-0495(79)90136-7
   Azria M., 1989, Calcitonins: Physiology and Pharmacology
   BAILEY IC, 1992, LANCET, V339, P831
   BALASUBRAMANIAM A, 1991, PEPTIDES, V12, P919, DOI 10.1016/0196-9781(91)90038-Q
   BEAUMONT K, 1995, BRIT J PHARMACOL, V115, P713, DOI 10.1111/j.1476-5381.1995.tb14991.x
   BECKER KL, 1980, ARCH PATHOL LAB MED, V104, P196
   BEHN AR, 1977, BMJ-BRIT MED J, V1, P755, DOI 10.1136/bmj.1.6063.755
   BELL GL, CIBA F S, V130, P167
   BENDTSEN F, 1991, J HEPATOL, V12, P118, DOI 10.1016/0168-8278(91)90920-7
   BENSCH KG, 1965, CANCER-AM CANCER SOC, V18, P592, DOI 10.1002/1097-0142(196505)18:5<592::AID-CNCR2820180508>3.0.CO;2-6
   BERGMAN ASF, 1994, RENAL FAILURE, V16, P351, DOI 10.3109/08860229409044875
   BETSHOLTZ C, 1990, DIABETES, V39, P118, DOI 10.2337/diabetes.39.1.118
   BHOGAL R, 1992, ENDOCRINOLOGY, V130, P906, DOI 10.1210/en.130.2.906
   BIJVOET OLM, 1980, ARTHRITIS RHEUM, V23, P1193, DOI 10.1002/art.1780231018
   BIJVOET OLM, 1968, LANCET, V1, P876
   BINSTOCK ML, 1980, ANN INTERN MED, V93, P269, DOI 10.7326/0003-4819-93-2-269
   Blundell T L, 1971, Recent Prog Horm Res, V27, P1
   BLUNDELL TL, 1972, DIABETES, V21, P492, DOI 10.2337/diab.21.2.S492
   BOOJ S, 1989, NEUROSCIENCE, V30, P479, DOI 10.1016/0306-4522(89)90267-4
   BOORMAN GA, 1972, ARCH PATHOL, V94, P35
   BOUALI SM, 1995, REGUL PEPTIDES, V56, P167, DOI 10.1016/0167-0115(95)00009-Z
   BOUILLON R, 1995, J CLIN ENDOCR METAB, V80, P1194, DOI 10.1210/jc.80.4.1194
   BOUILLON R, 1991, INT CONGR SER, V1000, P1271
   BOYCE BF, 1984, LANCET, V1, P821
   BRAGA P, 1978, LIFE SCI, V22, P971, DOI 10.1016/0024-3205(78)90362-4
   BRAIN SD, 1990, EUR J PHARMACOL, V183, P2221, DOI 10.1016/0014-2999(90)93755-F
   BRAIN SD, 1988, NATURE, V335, P73, DOI 10.1038/335073a0
   BRAIN SD, 1986, J INVEST DERMATOL, V87, P533, DOI 10.1111/1523-1747.ep12455620
   BRAIN SD, 1990, AM J PATHOL, V136, P487
   BRAIN SD, 1986, EUR J PHARMACOL, V124, P349, DOI 10.1016/0014-2999(86)90238-4
   BRAIN SD, 1990, BRIT J CLIN PHARMACO, V30, P853, DOI 10.1111/j.1365-2125.1990.tb05451.x
   BRAIN SD, 1985, NATURE, V313, P54, DOI 10.1038/313054a0
   BRAUND WJ, 1987, LANCET, V1, P237
   BREEZE AL, 1991, BIOCHEMISTRY-US, V30, P575, DOI 10.1021/bi00216a036
   BREIMER LH, 1988, BIOCHEM J, V255, P377, DOI 10.1042/bj2550377
   BRETHERTONWATT D, 1992, ANN NY ACAD SCI, V657, P299, DOI 10.1111/j.1749-6632.1992.tb22777.x
   BRETHERTONWATT D, 1990, DIABETOLOGIA, V33, P115, DOI 10.1007/BF00401050
   BRODERICK CL, 1991, BIOCHEM BIOPH RES CO, V177, P932, DOI 10.1016/0006-291X(91)90628-K
   BROWN P, 1970, Scottish Medical Journal, V15, P207
   BRYERASH M, 1995, METABOLISM, V44, P705, DOI 10.1016/0026-0495(95)90181-7
   BUDAYR AA, 1989, P NATL ACAD SCI USA, V86, P7183, DOI 10.1073/pnas.86.18.7183
   BUTLER PC, 1990, DIABETES, V39, P752, DOI 10.2337/diabetes.39.6.752
   CAMBRIDGE H, 1992, BRIT J PHARMACOL, V106, P746, DOI 10.1111/j.1476-5381.1992.tb14404.x
   CANTALAMESSA L, 1978, METABOLISM, V27, P987, DOI 10.1016/0026-0495(78)90143-9
   CAREY DE, 1985, ARCH PHYS MED REHAB, V66, P640
   CARSTENS JH, 1991, CALCIFIED TISSUE INT, V49, pS2, DOI 10.1007/BF02561368
   CHABRE O, 1992, MOL ENDOCRINOL, V6, P551, DOI 10.1210/me.6.4.551
   CHAKDER S, 1990, J PHARMACOL EXP THER, V253, P200
   CHAMBERS TJ, 1982, J PATHOL, V136, P27, DOI 10.1002/path.1711360104
   CHAMBERS TJ, 1983, J CLIN ENDOCR METAB, V57, P819, DOI 10.1210/jcem-57-4-819
   CHAMBERS TJ, 1984, J ENDOCRINOL, V102, P281, DOI 10.1677/joe.0.1020281
   CHAMBERS TJ, 1985, J PATHOL, V145, P297, DOI 10.1002/path.1711450403
   CHANCE WT, 1991, BRAIN RES, V539, P352, DOI 10.1016/0006-8993(91)91644-G
   CHANTRY A, 1991, BIOCHEM J, V277, P139, DOI 10.1042/bj2770139
   CHATTERJEE TK, 1991, MOL PHARMACOL, V39, P798
   CHATTERJEE TK, 1991, ENDOCRINOLOGY, V128, P2731, DOI 10.1210/endo-128-6-2731
   CHIBA T, 1989, AM J PHYSIOL, V256, pE331, DOI 10.1152/ajpendo.1989.256.2.E331
   CHIN SY, 1994, J PHARMACOL EXP THER, V269, P989
   CHOU PY, 1978, ANNU REV BIOCHEM, V47, P251, DOI 10.1146/annurev.bi.47.070178.001343
   CHOU PY, 1977, J MOL BIOL, V115, P135, DOI 10.1016/0022-2836(77)90094-8
   CHRISTMANSON L, 1990, FEBS LETT, V267, P160, DOI 10.1016/0014-5793(90)80314-9
   CLARK A, 1990, DIABETOLOGIA, V33, P285, DOI 10.1007/BF00403322
   CLEMENTI G, 1985, EUR J PHARMACOL, V108, P71, DOI 10.1016/0014-2999(85)90284-5
   COHN SH, 1971, J CLIN ENDOCR METAB, V33, P719, DOI 10.1210/jcem-33-5-719
   COLLIN E, 1993, PAIN, V54, P203, DOI 10.1016/0304-3959(93)90210-G
   COLLYEAR K, 1991, J MOL ENDOCRINOL, V6, P147, DOI 10.1677/jme.0.0060147
   COLUCCI WS, 1986, NEW ENGL J MED, V314, P290, DOI 10.1056/NEJM198601303140506
   CONLON JM, 1993, PEPTIDES, V14, P581
   CONLON JM, 1989, PEPTIDES, V10, P327, DOI 10.1016/0196-9781(89)90038-7
   COOPER CW, 1967, ENDOCRINOLOGY, V81, P610, DOI 10.1210/endo-81-3-610
   COOPER CW, 1972, CALCIUM PARATHYROID, P128
   COOPER GJS, 1988, P NATL ACAD SCI USA, V85, P7763, DOI 10.1073/pnas.85.20.7763
   COOPER GJS, 1994, ENDOCR REV, V15, P163, DOI 10.1210/er.15.2.163
   COOPER GJS, 1987, P NATL ACAD SCI USA, V84, P8628, DOI 10.1073/pnas.84.23.8628
   COOPER GJS, 1991, MED HYPOTHESES, V36, P284, DOI 10.1016/0306-9877(91)90150-W
   COOPER GJS, 1991, DIABETES, V40, P497
   COPP DH, 1962, ENDOCRINOLOGY, V70, P638, DOI 10.1210/endo-70-5-638
   CRAIG RK, 1982, NATURE, V295, P345, DOI 10.1038/295345a0
   DATTA H, 1990, BIOCHEM SOC T, V18, P1276, DOI 10.1042/bst0181276
   DATTA HK, 1989, BIOCHEM BIOPH RES CO, V162, P876, DOI 10.1016/0006-291X(89)92391-7
   DAVIES D, 1992, BIOCHEM PHARMACOL, V43, P1753, DOI 10.1016/0006-2952(92)90706-O
   DEDEUXCHAISNES CN, 1977, MOL ENDOCRINOL, P405
   DEEMS RO, 1991, BIOCHEM BIOPH RES CO, V174, P716, DOI 10.1016/0006-291X(91)91476-S
   DEEMS RO, 1991, BIOCHEM BIOPH RES CO, V181, P116, DOI 10.1016/S0006-291X(05)81389-0
   DELOSSANTOS ET, 1991, J CLIN ENDOCR METAB, V72, P1031, DOI 10.1210/jcem-72-5-1031
   DENISDONINI S, 1989, NATURE, V339, P701, DOI 10.1038/339701a0
   DENNIS T, 1991, BRAIN RES, V539, P59, DOI 10.1016/0006-8993(91)90686-P
   DENNIS T, 1989, J PHARMACOL EXP THER, V251, P718
   DENNIS T, 1990, J PHARMACOL EXP THER, V254, P123
   DEROSE J, 1974, AM J MED, V56, P858, DOI 10.1016/0002-9343(74)90815-8
   DEWITT BJ, 1994, EUR J PHARMACOL, V257, P303, DOI 10.1016/0014-2999(94)90143-0
   DICK IM, 1991, ACTA ENDOCRINOL-COP, V125, P241, DOI 10.1530/acta.0.1250241
   DIPETTE DJ, 1988, NEUROSCI LETT, V95, P335, DOI 10.1016/0304-3940(88)90681-7
   DIPETTE DJ, 1989, HYPERTENSION, V13, P77, DOI 10.1161/01.HYP.13.1.77
   DIPETTE DJ, 1989, AM J MED SCI, V297, P65, DOI 10.1097/00000441-198902000-00001
   DIPETTE DJ, 1994, CALCIUM REGULATING H, P239
   DSANTOS CS, 1992, MOL PHARMACOL, V41, P894
   DUBE WJ, 1973, MAYO CLIN PROC, V48, P43
   DYMLING JF, 1976, ACTA ENDOCRINOL-COP, V82, P500
   EDBROOKE MR, 1985, EMBO J, V4, P715, DOI 10.1002/j.1460-2075.1985.tb03688.x
   EDVINSSON L, 1989, J HUM HYPERTENS, V3, P267
   EDVINSSON L, 1990, J CEREBR BLOOD F MET, V10, P602, DOI 10.1038/jcbfm.1990.111
   EDVINSSON L, 1985, NEUROSCI LETT, V58, P213, DOI 10.1016/0304-3940(85)90166-1
   EDWARDS BJ, 1992, CLIN RES, V40, pA197
   EDWARDS BJA, 1992, LIFE SCI, V51, P1899, DOI 10.1016/0024-3205(92)90106-Y
   EDWARDS RM, 1990, AM J PHYSIOL, V258, pF121, DOI 10.1152/ajprenal.1990.258.1.F121
   ELIARD PH, 1989, ASSESSMENT NEW 2 SIT
   ELOMAA I, 1983, LANCET, V1, P146
   ERIKSSON J, 1992, DIABETOLOGIA, V35, P291, DOI 10.1007/BF00400933
   ETTINGER B, 1985, ANN INTERN MED, V102, P319, DOI 10.7326/0003-4819-102-3-319
   EVANS IMA, 1979, HUMAN CALCITONIN PAG, P111
   EZRA D, 1987, EUR J PHARMACOL, V137, P101, DOI 10.1016/0014-2999(87)90187-7
   FABBRI A, 1981, INT J CLIN PHARM TH, V19, P509
   FAGIN JA, 1992, J CLIN ENDOCR METAB, V75, P1398, DOI 10.1210/jc.75.6.1398
   FAHIM A, 1990, NEUROENDOCRINOLOGY, V51, P688, DOI 10.1159/000125411
   FANCHESCHINI R, 1984, CURR THER RES, V34, P795
   FEHMANN HC, 1990, FEBS LETT, V262, P279, DOI 10.1016/0014-5793(90)80210-A
   FERRARI R, 1991, LANCET, V338, P1084, DOI 10.1016/0140-6736(91)91944-P
   FERRIER GJM, 1989, J MOL ENDOCRINOL, V3, pR1, DOI 10.1677/jme.0.003R001
   FIORETTI P, 1992, MATURITAS, V15, P225, DOI 10.1016/0378-5122(92)90206-J
   FISCHER JA, 1987, BONE MINER, V2, P347
   FISCHER JA, 1983, J CLIN ENDOCR METAB, V57, P1314, DOI 10.1210/jcem-57-6-1314
   FISHER LA, 1983, NATURE, V305, P534, DOI 10.1038/305534a0
   Fleisch H, 1983, BONE MINERAL RES ANN, P319
   FLEISHC H, 1983, HANDS PHARM, V83, P441
   FLETCHER CD, 1991, ACTA ENDOCRINOL-COP, V124, P353, DOI 10.1530/acta.0.1240353
   FLOOD JF, 1989, PEPTIDES, V10, P809, DOI 10.1016/0196-9781(89)90118-6
   FLOOD JF, 1987, SCIENCE, V236, P832, DOI 10.1126/science.3576201
   FLOOD JF, 1992, PEPTIDES, V13, P577, DOI 10.1016/0196-9781(92)90092-H
   FONTAINE B, 1987, J CELL BIOL, V105, P1337, DOI 10.1083/jcb.105.3.1337
   FONTAINE B, 1986, NEUROSCI LETT, V71, P59, DOI 10.1016/0304-3940(86)90257-0
   FOORD SM, 1987, EUR J BIOCHEM, V170, P373, DOI 10.1111/j.1432-1033.1987.tb13710.x
   FORCE T, 1992, AM J PHYSIOL, V262, pF1110, DOI 10.1152/ajprenal.1992.262.6.F1110
   FOREMAN JC, 1987, INT ARCH ALLER A IMM, V82, P366, DOI 10.1159/000234229
   FOSTER GV, 1966, LANCET, V1, P107
   FOSTER GV, 1964, NATURE, V203, P1029, DOI 10.1038/2031029a0
   FOULKES R, 1989, REGUL PEPTIDES, V25, P25
   FOX N, 1993, FEBS LETT, V323, P40, DOI 10.1016/0014-5793(93)81444-5
   FRANCOCERECEDA A, 1987, ACTA PHYSIOL SCAND, V131, P159
   FRANCOCERECEDA A, 1988, ACTA PHYSIOL SCAND, V133, P1
   FRANCOCERECEDA A, 1987, EUR J PHARMACOL, V134, P69, DOI 10.1016/0014-2999(87)90132-4
   FRANCOCERECEDA A, 1987, EUR J PHARMACOL, V142, P235, DOI 10.1016/0014-2999(87)90112-9
   FRANCOCERECEDA A, 1991, BRIT J PHARMACOL, V102, P506, DOI 10.1111/j.1476-5381.1991.tb12201.x
   FRONTONI S, 1991, DIABETES, V40, P568, DOI 10.2337/diabetes.40.5.568
   FUKUHARA M, 1995, AM J PHYSIOL-REG I, V269, pR1289, DOI 10.1152/ajpregu.1995.269.5.R1289
   GALEAZZA MT, 1991, PEPTIDES, V12, P585, DOI 10.1016/0196-9781(91)90106-Y
   GANGULA RR, 1997, AM J OBSTET GYNECOL, V176, P1
   GARDINER SM, 1991, DIABETES, V40, P948, DOI 10.2337/diabetes.40.8.948
   GARDINER SM, 1991, BRIT J PHARMACOL, V103, P1256, DOI 10.1111/j.1476-5381.1991.tb12333.x
   GARDINER SM, 1991, EUR J PHARMACOL, V199, P375, DOI 10.1016/0014-2999(91)90504-J
   GEARY N, 1983, PHYSIOL BEHAV, V31, P391, DOI 10.1016/0031-9384(83)90207-X
   GEDULIN B, 1993, DIABETES, V42, pA229
   GEDULIN B, 1991, BIOCHEM BIOPH RES CO, V180, P782, DOI 10.1016/S0006-291X(05)81133-7
   GENNARI C, 1991, CALCIFIED TISSUE INT, V49, pS9, DOI 10.1007/BF02561370
   GENNARI C, 1990, CARDIOVASC RES, V24, P239, DOI 10.1093/cvr/24.3.239
   GENNARI C, 1985, CALCIFIED TISSUE INT, V37, P581, DOI 10.1007/BF02554909
   GHATEI MA, 1990, J ENDOCRINOL, V124, pR9, DOI 10.1677/joe.0.124R009
   GIBSON SJ, 1988, NEUROSCI LETT, V91, P283, DOI 10.1016/0304-3940(88)90694-5
   GIBSON SJ, 1984, J NEUROSCI, V4, P3101, DOI 10.1523/jneurosci.04-12-03101.1984
   GILBEY S, 1991, J BONE MINER RES, V6, pS293
   GILBEY SG, 1991, CLIN SCI, V81, P803, DOI 10.1042/cs0810803
   GILL AM, 1991, LIFE SCI, V48, P703, DOI 10.1016/0024-3205(91)90546-N
   Girgis S I, 1987, Henry Ford Hosp Med J, V35, P118
   GIRGIS SI, 1985, LANCET, V2, P14
   GIULIANI S, 1992, BRIT J PHARMACOL, V107, P510, DOI 10.1111/j.1476-5381.1992.tb12775.x
   GKONOS PJ, 1986, J BIOL CHEM, V261, P4386
   GLENNER GG, 1980, NEW ENGL J MED, V302, P1283, DOI 10.1056/NEJM198006053022305
   GLENNER GG, 1988, BIOCHEM BIOPH RES CO, V155, P608, DOI 10.1016/S0006-291X(88)80538-2
   GNAEDINGER MP, 1989, AM J PHYSIOL, V257, pE848, DOI 10.1152/ajpendo.1989.257.6.E848
   GOFF JP, 1991, ENDOCRINOLOGY, V129, P2815, DOI 10.1210/endo-129-6-2815
   GOLDRING SR, 1993, HORM METAB RES, V25, P477, DOI 10.1055/s-2007-1002153
   GOLDRING SR, 1992, CALCIUM REGULATING H, V2, P142
   GOLTZMAN D, 1985, SCIENCE, V227, P1343, DOI 10.1126/science.2983422
   GOMEZFOIX AM, 1991, BIOCHEM J, V276, P607, DOI 10.1042/bj2760607
   GORN AH, 1992, J CLIN INVEST, V90, P1726, DOI 10.1172/JCI116046
   GOTTLEIB A, 1994, CLIN RES, V42, P87
   GRACE GC, 1987, BRIT J PHARMACOL, V91, P729, DOI 10.1111/j.1476-5381.1987.tb11270.x
   GRAY GW, 1991, BRIT J PHARMACOL, V102, pP189
   GRAY TK, 1973, J CLIN INVEST, V52, P3084, DOI 10.1172/JCI107507
   GREENBERG B, 1987, BRIT J PHARMACOL, V92, P789, DOI 10.1111/j.1476-5381.1987.tb11382.x
   GRIFFIN EC, 1992, CIRC SHOCK, V38, P50
   GRUBER HE, 1984, METABOLISM, V33, P295, DOI 10.1016/0026-0495(84)90187-2
   GRUNDITZ T, 1986, ENDOCRINOLOGY, V119, P2313, DOI 10.1210/endo-119-5-2313
   HADDAD JG, 1972, J CLIN INVEST, V51, P3133, DOI 10.1172/JCI107140
   HAEGERSTRAND A, 1990, P NATL ACAD SCI USA, V87, P3299, DOI 10.1073/pnas.87.9.3299
   HAN SP, 1990, BIOCHEM BIOPH RES CO, V168, P786, DOI 10.1016/0006-291X(90)92390-L
   HAO QZ, 1994, LIFE SCI, V54, pPL265, DOI 10.1016/0024-3205(94)00844-2
   HARRIS ST, 1993, AM J MED, V95, P557, DOI 10.1016/0002-9343(93)90350-X
   HARRISON JK, 1993, FEBS LETT, V318, P17, DOI 10.1016/0014-5793(93)81318-T
   HARTTER E, 1991, DIABETOLOGIA, V34, P52, DOI 10.1007/BF00404025
   HAZARD JB, 1959, J CLIN ENDOCR METAB, V19, P152, DOI 10.1210/jcem-19-1-152
   HEATH H, 1979, J LAB CLIN MED, V93, P390
   HELLMAN U, 1990, BIOCHEM BIOPH RES CO, V169, P571, DOI 10.1016/0006-291X(90)90369-X
   HENDRY IA, 1992, J NEUROSCI, V12, P3427
   HENNESSY JF, 1974, J CLIN ENDOCR METAB, V39, P487, DOI 10.1210/jcem-39-3-487
   HILLYARD CJ, 1978, LANCET, V1, P961
   HIRATA Y, 1988, BIOCHEM BIOPH RES CO, V151, P1113, DOI 10.1016/S0006-291X(88)80481-9
   HIROSHIMA O, 1988, J NEUROCHEM, V50, P480, DOI 10.1111/j.1471-4159.1988.tb02936.x
   HOFLE G, 1991, REGUL PEPTIDES, V32, P321, DOI 10.1016/0167-0115(91)90025-C
   HOKFELT T, 1986, PROG BRAIN RES, V68, P33, DOI 10.1016/S0079-6123(08)60230-7
   HOLMAN JJ, 1986, PEPTIDES, V7, P231, DOI 10.1016/0196-9781(86)90218-4
   HOLTROP ME, 1974, J CELL BIOL, V60, P346, DOI 10.1083/jcb.60.2.346
   HOLZER P, 1988, NEUROSCIENCE, V24, P739, DOI 10.1016/0306-4522(88)90064-4
   HOLZER P, 1995, CAN J PHYSIOL PHARM, V73, P991, DOI 10.1139/y95-138
   HONGO K, 1989, STROKE, V20, P100, DOI 10.1161/01.STR.20.1.100
   HOPENER JWM, 1992, BIOCH T, V21, P285
   HOPPENER JWM, 1987, J CLIN ENDOCR METAB, V64, P809
   HOPPENER JWM, 1985, HUM GENET, V70, P259
   HOTHERSALL JS, 1990, BIOCHEM BIOPH RES CO, V169, P451, DOI 10.1016/0006-291X(90)90352-N
   HOUSSAMI S, 1993, J BONE MINER RES, V8, pS129
   HUANG HJS, 1992, HYPERTENSION, V19, pI101, DOI 10.1161/01.HYP.19.1_Suppl.I101
   HUBBARD JAM, 1991, BIOCHEM J, V275, P785, DOI 10.1042/bj2750785
   HUGHES JJ, 1984, PEPTIDES, V5, P665, DOI 10.1016/0196-9781(84)90003-2
   HUGHES SR, 1991, BRIT J PHARMACOL, V104, P738, DOI 10.1111/j.1476-5381.1991.tb12497.x
   HUI SL, 1985, J CLIN ENDOCR METAB, V60, P74, DOI 10.1210/jcem-60-1-74
   HURLEY DL, 1989, J BONE MINER RES, V4, P89
   HUTTEMEIER PC, 1993, AM J PHYSIOL, V265, pH767, DOI 10.1152/ajpheart.1993.265.2.H767
   ICHIKI Y, 1994, FEBS LETT, V338, P6, DOI 10.1016/0014-5793(94)80106-1
   IKEGAME M, 1995, J BONE MINER RES, V10, P59
   INOUE K, 1992, HORM METAB RES, V24, P251, DOI 10.1055/s-2007-1003306
   ISHIHARA T, 1991, EMBO J, V10, P1635, DOI 10.1002/j.1460-2075.1991.tb07686.x
   ISHIKAWA T, 1988, CIRC RES, V63, P726, DOI 10.1161/01.RES.63.4.726
   ISHIMITSU T, 1994, BIOCHEM BIOPH RES CO, V203, P631, DOI 10.1006/bbrc.1994.2229
   ISHIYAMA Y, 1993, EUR J PHARMACOL, V241, P271, DOI 10.1016/0014-2999(93)90214-3
   ISHIZAKA Y, 1994, BIOCHEM BIOPH RES CO, V200, P642, DOI 10.1006/bbrc.1994.1496
   IZUMI H, 1993, AM J OBSTET GYNECOL, V169, P1327, DOI 10.1016/0002-9378(93)90301-X
   JACOBS JW, 1982, ENDOCRINOLOGY, V111, P2014, DOI 10.1210/endo-111-6-2014
   JACOBS JW, 1981, SCIENCE, V213, P457, DOI 10.1126/science.6264603
   JAEGER P, 1986, J CLIN INVEST, V78, P456, DOI 10.1172/JCI112597
   JAGER K, 1990, EUR J CLIN PHARMACOL, V39, P491
   Jakob W, 1970, Zentralbl Veterinarmed A, V17, P818
   JIANFENG Z, 1991, INT J CARDIOL, V33, P43
   JINNAI K, 1989, NEUROSCI LETT, V103, P64, DOI 10.1016/0304-3940(89)90486-2
   JOHNSON KH, 1988, AM J PATHOL, V130, P1
   JOHNSON KH, 1992, LAB INVEST, V66, P522
   JOHNSON KH, 1991, DIABETES, V40, P310, DOI 10.2337/diabetes.40.3.310
   JOHNSON NE, 1985, AM J CLIN NUTR, V42, P12, DOI 10.1093/ajcn/42.1.12
   JOHNSTON FG, 1990, LANCET, V335, P869, DOI 10.1016/0140-6736(90)90473-I
   JONAS V, 1985, P NATL ACAD SCI USA, V82, P1994, DOI 10.1073/pnas.82.7.1994
   JORDAN K, 1990, BIOCHEM BIOPH RES CO, V169, P502, DOI 10.1016/0006-291X(90)90359-U
   JOYCE CD, 1990, SURGERY, V108, P1097
   JUDD AM, 1990, ENDOCRINOLOGY, V127, P191, DOI 10.1210/endo-127-1-191
   JUNG A, 1980, P NATL ACAD SCI-BIOL, V77, P5759, DOI 10.1073/pnas.77.10.5759
   JUPPNER H, 1991, SCIENCE, V254, P1024, DOI 10.1126/science.1658941
   KAISER ET, 1983, P NATL ACAD SCI USA, V80, P1137, DOI 10.1073/pnas.80.4.1137
   KAISER ET, 1984, SCIENCE, V223, P249, DOI 10.1126/science.6322295
   KANATSUKA A, 1989, FEBS LETT, V259, P199, DOI 10.1016/0014-5793(89)81527-3
   KANIS JA, 1986, LANCET, V1, P615
   Kapas S, 1995, BIOCHEM BIOPH RES CO, V217, P832, DOI 10.1006/bbrc.1995.2847
   KAPAS S, 1995, J BIOL CHEM, V270, P25344, DOI 10.1074/jbc.270.43.25344
   KASHIHARA Y, 1989, J NEUROSCI, V9, P3796
   KASSIR AA, 1991, DIABETES, V40, P998, DOI 10.2337/diabetes.40.8.998
   KAWASAKI H, 1988, NATURE, V335, P164, DOI 10.1038/335164a0
   KEITH IM, 1991, HISTOCHEMISTRY, V96, P311, DOI 10.1007/BF00271351
   KEITH IM, 1992, EXP LUNG RES, V18, P205, DOI 10.3109/01902149209031681
   KIMURA S, 1987, NEUROPEPTIDES, V9, P75, DOI 10.1016/0143-4179(87)90034-5
   KITAMURA K, 1994, FEBS LETT, V338, P306, DOI 10.1016/0014-5793(94)80289-0
   KITAMURA K, 1993, BIOCHEM BIOPH RES CO, V192, P553, DOI 10.1006/bbrc.1993.1451
   KITAMURA K, 1993, BIOCHEM BIOPH RES CO, V194, P720, DOI 10.1006/bbrc.1993.1881
   KITTUR SD, 1985, P NATL ACAD SCI USA, V82, P5064, DOI 10.1073/pnas.82.15.5064
   KJARTANSSON J, 1987, EUR J PHARMACOL, V142, P355, DOI 10.1016/0014-2999(87)90073-2
   KNIGHT KB, 1992, AM J CLIN NUTR, V55, P891, DOI 10.1093/ajcn/55.4.891
   KODA JE, 1992, LANCET, V339, P1179, DOI 10.1016/0140-6736(92)90785-2
   KOOPMANS SJ, 1991, DIABETOLOGIA, V34, P218, DOI 10.1007/BF00405079
   KRAHN DD, 1984, PEPTIDES, V5, P861, DOI 10.1016/0196-9781(84)90107-4
   KREAM BE, 1985, ENDOCRINOLOGY, V116, P296, DOI 10.1210/endo-116-1-296
   KREUTTER D, 1990, DIABETES S, V39
   KREUTTER DK, 1993, AM J PHYSIOL, V264, pE606, DOI 10.1152/ajpendo.1993.264.4.E606
   KRUGER L, 1988, BRAIN RES, V463, P223, DOI 10.1016/0006-8993(88)90395-2
   KUBOTA M, 1985, BIOCHEM BIOPH RES CO, V132, P88, DOI 10.1016/0006-291X(85)90992-1
   KURAMOTO H, 1987, CELL TISSUE RES, V247, P309
   KURTZ A, 1989, KIDNEY INT, V36, P222, DOI 10.1038/ki.1989.183
   KURTZ A, 1988, J CLIN INVEST, V82, P538, DOI 10.1172/JCI113629
   KURTZ A, 1989, KLIN WOCHENSCHR, V67, P870, DOI 10.1007/BF01717342
   LAUFER R, 1989, J BIOL CHEM, V264, P2683
   LAUFER R, 1987, EMBO J, V6, P901, DOI 10.1002/j.1460-2075.1987.tb04836.x
   LEE Y, 1985, NEUROSCIENCE, V15, P1227, DOI 10.1016/0306-4522(85)90265-9
   LEFF SE, 1987, CELL, V48, P517, DOI 10.1016/0092-8674(87)90202-9
   LEFFERT JD, 1989, P NATL ACAD SCI USA, V86, P3127, DOI 10.1073/pnas.86.9.3127
   LEIGHTON B, 1990, TRENDS BIOCHEM SCI, V15, P295, DOI 10.1016/0968-0004(90)90015-4
   LEIGHTON B, 1988, NATURE, V335, P632, DOI 10.1038/335632a0
   LEIGHTON B, 1989, FEBS LETT, V249, P357, DOI 10.1016/0014-5793(89)80658-1
   LEMOULLEC JM, 1984, FEBS LETT, V167, P93, DOI 10.1016/0014-5793(84)80839-X
   LENZ HJ, 1985, GASTROENTEROLOGY, V88, P539, DOI 10.1016/0016-5085(85)90518-9
   LEVINE AS, 1982, PHARMACOL BIOCHEM BE, V16, P897, DOI 10.1016/0091-3057(82)90041-7
   LI JZ, 1992, RENAL FAILURE, V14, P11, DOI 10.3109/08860229209039111
   LIBERT F, 1989, SCIENCE, V244, P569, DOI 10.1126/science.2541503
   LIN HY, 1991, SCIENCE, V254, P1022, DOI 10.1126/science.1658940
   LINDSAY RM, 1989, NATURE, V337, P362, DOI 10.1038/337362a0
   LUDVIK B, 1991, DIABETES, V40, P1615, DOI 10.2337/diabetes.40.12.1615
   Luebke AE, 1996, P NATL ACAD SCI USA, V93, P3455, DOI 10.1073/pnas.93.8.3455
   LUKINIUS A, 1989, DIABETOLOGIA, V32, P240, DOI 10.1007/BF00285291
   LUTZ TA, 1995, VET CLIN N AM-SMALL, V25, P527, DOI 10.1016/S0195-5616(95)50051-8
   LYNCH B, 1988, BIOCHEMISTRY-US, V27, P7600, DOI 10.1021/bi00420a005
   LYRITIS GP, 1991, CALCIFIED TISSUE INT, V49, P369, DOI 10.1007/BF02555844
   MACINTYRE I, 1988, LANCET, V1, P900
   MACINTYRE I, 1984, NATURE, V308, P84, DOI 10.1038/308084a0
   MACINTYRE I, 1993, MOL ENDOCRINOL, P193
   MAGGI CA, 1990, EUR J PHARMACOL, V179, P217, DOI 10.1016/0014-2999(90)90422-3
   MAGGI CA, 1991, EUR J PHARMACOL, V192, P85, DOI 10.1016/0014-2999(91)90072-X
   MAHADEVAN D, UNPUB  P NATL ACAD S
   MANLEY HC, 1989, NEUROPEPTIDES, V13, P29, DOI 10.1016/0143-4179(89)90018-8
   MANNING MC, 1989, BIOCHEM BIOPH RES CO, V160, P388, DOI 10.1016/0006-291X(89)91668-9
   MARESCA V, 1985, J INT MED RES, V13, P311, DOI 10.1177/030006058501300602
   MARSHALL I, 1986, EUR J PHARMACOL, V123, P207, DOI 10.1016/0014-2999(86)90661-8
   MARSHALL I, 1986, EUR J PHARMACOL, V123, P217, DOI 10.1016/0014-2999(86)90662-X
   MARTIN TJ, 1991, CRIT REV BIOCHEM MOL, V26, P377, DOI 10.3109/10409239109114073
   MARX SJ, 1972, SCIENCE, V178, P999, DOI 10.1126/science.178.4064.999
   MARX SJ, 1973, J BIOL CHEM, V248, P4797
   MASSRY SG, 1968, J LAB CLIN MED, V71, P212
   MASUDA A, 1992, J HYPERTENS, V10, P1499, DOI 10.1097/00004872-199210120-00010
   MATSUO K, 1991, MOL ENDOCRINOL, V5, P1873, DOI 10.1210/mend-5-12-1873
   MATTSON MP, 1995, BRAIN RES, V676, P219, DOI 10.1016/0006-8993(95)00148-J
   MAUBRAS L, 1993, PEPTIDES, V14, P977, DOI 10.1016/0196-9781(93)90074-Q
   MAZZUOLI GF, 1986, CALCIFIED TISSUE INT, V38, P3, DOI 10.1007/BF02556587
   MCCARRON DA, 1986, AM J NEPHROL, V6, P3, DOI 10.1159/000167206
   MCCARTHY MI, 1992, DIABETES RES CLIN PR, V18, P31, DOI 10.1016/0168-8227(92)90052-S
   MCCORMACK DG, 1989, J APPL PHYSIOL, V67, P1265, DOI 10.1152/jappl.1989.67.3.1265
   MCDOWELL EM, 1976, LAB INVEST, V34, P202
   MCEWAN J, 1985, BRIT HEART J, V54, P643
   MCEWAN J, 1986, CIRCULATION, V74, P1243, DOI 10.1161/01.CIR.74.6.1243
   MCEWAN J, 1989, 71 ANN M AM END SOC
   MCEWAN J, 1989, ENDOCRINE MECHANISMS, P287
   MICHELANGELI VP, 1986, CALCIFIED TISSUE INT, V39, P44, DOI 10.1007/BF02555739
   MILHAUD G, 1975, BIOMEDICINE, V22, P223
   MILHAUD G, 1978, BIOMEDICINE, V29, P271
   MIMEAULT M, 1993, EUR J BIOCHEM, V213, P927, DOI 10.1111/j.1432-1033.1993.tb17837.x
   MIMEAULT M, 1992, J MED CHEM, V35, P2163, DOI 10.1021/jm00090a003
   MINVIELLE S, 1986, FEBS LETT, V203, P7, DOI 10.1016/0014-5793(86)81425-9
   MINVIELLE S, 1987, FEBS LETT, V223, P63, DOI 10.1016/0014-5793(87)80510-0
   MITSUKAWA T, 1992, DIABETES RES CLIN PR, V15, P131, DOI 10.1016/0168-8227(92)90016-K
   MITSUKAWA T, 1990, DIABETES, V39, P639, DOI 10.2337/diabetes.39.5.639
   MITSUMA T, 1984, EUR J PHARMACOL, V102, P123, DOI 10.1016/0014-2999(84)90344-3
   MIYAUCHI T, 1987, J CARDIOVASC PHARM, V10, P675, DOI 10.1097/00005344-198712000-00011
   MIYAUCHI T, 1988, BIOCHEM BIOPH RES CO, V155, P289, DOI 10.1016/S0006-291X(88)81082-9
   MIYAZATO M, 1991, BIOCHEM BIOPH RES CO, V181, P293, DOI 10.1016/S0006-291X(05)81416-0
   MOLINA JM, 1990, DIABETES, V39, P260, DOI 10.2337/diabetes.39.2.260
   MOLNAR M, 1992, AM J OBSTET GYNECOL, V166, P1560, DOI 10.1016/0002-9378(92)91634-M
   MONIZ C, 1990, J MOL ENDOCRINOL, V5, P259, DOI 10.1677/jme.0.0050259
   MOORADIAN AD, 1988, ARCH INTERN MED, V148, P2369, DOI 10.1001/archinte.148.11.2369
   MOORE CX, 1991, BIOCHEM BIOPH RES CO, V179, P1, DOI 10.1016/0006-291X(91)91325-7
   MORA M, 1989, BRAIN RES, V492, P404, DOI 10.1016/0006-8993(89)90930-X
   MORIMOTO S, 1980, CLIN ENDOCRINOL, V13, P135, DOI 10.1111/j.1365-2265.1980.tb01034.x
   MORISHITA T, 1992, DIABETES RES CLIN PR, V15, P63, DOI 10.1016/0168-8227(92)90069-4
   MORLEY JE, 1993, PHARMACOL BIOCHEM BE, V44, P577, DOI 10.1016/0091-3057(93)90169-T
   MORLEY JE, 1990, J AM GERIATR SOC, V38, P605, DOI 10.1111/j.1532-5415.1990.tb02417.x
   MORLEY JE, 1987, ENDOCR REV, V8, P256, DOI 10.1210/edrv-8-3-256
   MORLEY JE, 1991, PEPTIDES, V12, P865, DOI 10.1016/0196-9781(91)90148-I
   MORLEY JE, 1992, PSYCHONEUROENDOCRINO, V17, P391, DOI 10.1016/0306-4530(92)90044-8
   MORRIS HR, 1984, NATURE, V308, P746, DOI 10.1038/308746a0
   MORTON AR, 1988, BRIT MED J, V297, P772, DOI 10.1136/bmj.297.6651.772
   MOSELEY JM, 1995, CRIT REV CL LAB SCI, V32, P299, DOI 10.3109/10408369509084687
   MOSSELMAN S, 1988, FEBS LETT, V239, P227, DOI 10.1016/0014-5793(88)80922-0
   MOTTE P, 1988, CLIN CHIM ACTA, V174, P35, DOI 10.1016/0009-8981(88)90365-8
   MULDERRY PK, 1994, NEUROSCIENCE, V59, P673, DOI 10.1016/0306-4522(94)90186-4
   MULDERRY PK, 1985, NEUROSCIENCE, V14, P947, DOI 10.1016/0306-4522(85)90156-3
   MULLE C, 1988, P NATL ACAD SCI USA, V85, P5728, DOI 10.1073/pnas.85.15.5728
   MUNDY GR, 1982, METABOLISM, V31, P1247, DOI 10.1016/0026-0495(82)90012-9
   NAKAGAWA SH, 1987, J BIOL CHEM, V262, P12054
   NAKAGAWA SH, 1986, J BIOL CHEM, V261, P7332
   NAKAMUTA H, 1986, JPN J PHARMACOL, V42, P175, DOI 10.1254/jjp.42.175
   NAKAZATO M, 1990, REGUL PEPTIDES, V31, P179, DOI 10.1016/0167-0115(90)90004-G
   NAKAZATO M, 1989, BIOCHEM BIOPH RES CO, V164, P394, DOI 10.1016/0006-291X(89)91732-4
   NEHER R, 1968, NATURE, V220, P984, DOI 10.1038/220984a0
   NELKIN BD, 1984, BIOCHEM BIOPH RES CO, V123, P648, DOI 10.1016/0006-291X(84)90278-X
   NELSON SH, 1993, AM J OBSTET GYNECOL, V168, P605, DOI 10.1016/0002-9378(93)90503-B
   NEW HV, 1986, NATURE, V323, P809, DOI 10.1038/323809a0
   NEWBOLD P, 1993, BRIT J PHARMACOL, V108, P705, DOI 10.1111/j.1476-5381.1993.tb12865.x
   NICHOLL CG, 1992, J MOL ENDOCRINOL, V9, P157, DOI 10.1677/jme.0.0090157
   NICHOLSON GC, 1986, J CLIN INVEST, V78, P355, DOI 10.1172/JCI112584
   NISHI M, 1990, J BIOL CHEM, V265, P4173
   NISHI M, 1989, P NATL ACAD SCI USA, V86, P5738, DOI 10.1073/pnas.86.15.5738
   NISHI M, 1989, MOL ENDOCRINOL, V3, P1775, DOI 10.1210/mend-3-11-1775
   NOHR D, 1991, NEUROSCI LETT, V134, P17, DOI 10.1016/0304-3940(91)90498-I
   NOUSPIKEL T, 1992, FEBS LETT, V301, P115, DOI 10.1016/0014-5793(92)80222-3
   NUKI C, 1993, BIOCHEM BIOPH RES CO, V196, P245, DOI 10.1006/bbrc.1993.2241
   NUTI R, 1987, CLIN ORTHOP RELAT R, P217
   OBIE JF, 1979, J PHARMACOL EXP THER, V209, P422
   OBRIEN TD, 1991, DIABETES, V40, P1701, DOI 10.2337/diabetes.40.12.1701
   OGAWA A, 1990, J CLIN INVEST, V85, P973, DOI 10.1172/JCI114528
   OHHASHI T, 1988, PEPTIDES, V9, P613, DOI 10.1016/0196-9781(88)90172-6
   OHMURA T, 1990, BRIT J PHARMACOL, V100, P27, DOI 10.1111/j.1476-5381.1990.tb12046.x
   OHSAWA H, 1989, BIOCHEM BIOPH RES CO, V160, P961, DOI 10.1016/0006-291X(89)92529-1
   OKIMURA Y, 1986, ENDOCRINOL JAPON, V33, P273
   Olefsky JM., 1989, Endocrinology, V2nd, P1369
   ONO K, 1989, NATURE, V340, P721, DOI 10.1038/340721a0
   ORIMO H, 1979, CLIN ENDOCRINOL TOKY, V27, P897
   OVERGAARD K, 1989, CLIN ENDOCRINOL, V30, P435, DOI 10.1111/j.1365-2265.1989.tb00443.x
   OWERBACH D, 1981, DIABETES, V30, P267, DOI 10.2337/diabetes.30.3.267
   PAPAPOULOS SE, 1992, BONE, V13, pS41, DOI 10.1016/S8756-3282(09)80009-4
   PEARSE AGE, 1971, HISTOCHEMISTRY, V27, P96, DOI 10.1007/BF00284951
   PEARSE AGE, 1969, CALCITONIN, P125
   PECK WA, 1993, AM J MED, V94, P646
   PERDRISOT R, 1990, CLIN CHEM, V36, P381
   PERNOW J, 1989, BRIT J PHARMACOL, V97, P983, DOI 10.1111/j.1476-5381.1989.tb12040.x
   PERRET M, 1993, LIFE SCI, V53, pPL377, DOI 10.1016/0024-3205(93)90213-M
   PETERMANN JB, 1987, J BIOL CHEM, V262, P542
   PETTERSSON M, 1986, ENDOCRINOLOGY, V119, P865, DOI 10.1210/endo-119-2-865
   POPPER P, 1989, BRAIN RES, V496, P180, DOI 10.1016/0006-8993(89)91064-0
   PORTALUPPI F, 1992, J HYPERTENS, V10, P1227, DOI 10.1097/00004872-199210000-00017
   POSTON GJ, 1987, SURGERY, V102, P1049
   PRIETO D, 1991, BRIT J PHARMACOL, V103, P1764, DOI 10.1111/j.1476-5381.1991.tb09860.x
   PROUDFOOT NJ, 1976, NATURE, V263, P211, DOI 10.1038/263211a0
   PRZEPIORKA D, 1984, BIOCHEM BIOPH RES CO, V120, P493, DOI 10.1016/0006-291X(84)91281-6
   QUIRION R, 1992, ANN NY ACAD SCI, V657, P88, DOI 10.1111/j.1749-6632.1992.tb22759.x
   RAIVICH G, 1991, NEURON, V7, P151, DOI 10.1016/0896-6273(91)90083-C
   RALSTON SH, 1989, LANCET, V2, P1180
   RASMUSSEN H, 1980, METAB BONE DIS RELAT, V2, P107, DOI 10.1016/0221-8747(80)90006-5
   RAVAZZOLA M, 1981, CELL BIOL INT REP, V5, P937, DOI 10.1016/0309-1651(81)90209-5
   REDDINGTON M, 1995, CAN J PHYSIOL PHARM, V73, P1047, DOI 10.1139/y95-148
   REGINSTER JY, 1990, SCAND J RHEUMATOL, V19, P83, DOI 10.3109/03009749009092626
   REGINSTER JY, 1987, LANCET, V2, P1481
   Resnick L. M., 1989, SALT HYPERTENSION, P190
   RESNICK LM, 1986, ANN INTERN MED, V105, P649, DOI 10.7326/0003-4819-105-5-649
   REYNOLDS J J, 1970, Calcified Tissue Research, V4, P339
   RIGGS BL, 1986, NEW ENGL J MED, V314, P1676, DOI 10.1056/NEJM198606263142605
   RINK TJ, 1993, TRENDS PHARMACOL SCI, V14, P113, DOI 10.1016/0165-6147(93)90081-T
   ROBINSON CJ, 1966, LANCET, V2, P83
   RODEN M, 1992, DIABETOLOGIA, V35, P116, DOI 10.1007/BF00402542
   ROOS BA, 1978, ENDOCRINOLOGY, V103, P2180, DOI 10.1210/endo-103-6-2180
   ROSENFELD MG, 1981, NATURE, V290, P63, DOI 10.1038/290063a0
   ROSENFELD MG, 1983, NATURE, V304, P129, DOI 10.1038/304129a0
   RUSSELL RGG, 1979, P INT S THYR C TELLS, P297
   SABATE MI, 1985, J BIOL CHEM, V260, P2589
   SAGGESE G, 1990, HORM RES, V34, P240, DOI 10.1159/000181833
   SAKAGUCHI M, 1991, J PHYSIOL-LONDON, V434, P257, DOI 10.1113/jphysiol.1991.sp018468
   SAKATA J, 1993, BIOCHEM BIOPH RES CO, V195, P921, DOI 10.1006/bbrc.1993.2132
   SALDANHA J, 1991, PROTEIN ENG, V4, P539, DOI 10.1093/protein/4.5.539
   SALDANHA J, UNPUB FEBS LETT
   SAMAAN NA, 1975, AM J OBSTET GYNECOL, V121, P622, DOI 10.1016/0002-9378(75)90462-7
   SANKE T, 1988, J BIOL CHEM, V263, P17243
   SANKE T, 1991, DIABETOLOGIA, V34, P129, DOI 10.1007/BF00500385
   SANO Y, 1989, J NEUROCHEM, V52, P1919, DOI 10.1111/j.1471-4159.1989.tb07277.x
   SCHIFTER S, 1991, AM J HYPERTENS, V4, P565, DOI 10.1093/ajh/4.7.565
   SCHUBERT D, 1989, P NATL ACAD SCI USA, V92, P1995
   SEIFERT H, 1985, AM J PHYSIOL, V249, pG147, DOI 10.1152/ajpgi.1985.249.1.G147
   SELF CH, 1985, PEPTIDES, V6, P627, DOI 10.1016/0196-9781(85)90164-0
   Seth R, 1989, Horm Metab Res Suppl, V21, P3
   SEXTON PM, 1986, NEUROSCIENCE, V19, P1235, DOI 10.1016/0306-4522(86)90137-5
   SEXTON PM, 1992, BRAIN RES, V596, P279, DOI 10.1016/0006-8993(92)91558-V
   SEXTON PM, 1988, NEUROCHEM INT, V12, P323, DOI 10.1016/0197-0186(88)90171-4
   SHAH GV, 1992, PROSTATE, V21, P87, DOI 10.1002/pros.2990210202
   SHAH GV, 1993, ENDOCRINOLOGY, V132, P1367, DOI 10.1210/en.132.3.1367
   SHEKHAR YC, 1991, AM J CARDIOL, V67, P732, DOI 10.1016/0002-9149(91)90531-O
   SHERIFF S, 1992, PEPTIDES, V13, P1193, DOI 10.1016/0196-9781(92)90028-2
   SHOJI T, 1987, N-S ARCH PHARMACOL, V336, P438, DOI 10.1007/BF00164880
   SIGRIST S, 1986, ENDOCRINOLOGY, V119, P381, DOI 10.1210/endo-119-1-381
   SILVA OL, 1973, ARCH INTERN MED, V132, P337, DOI 10.1001/archinte.132.3.337
   SILVESTRE RA, 1990, REGUL PEPTIDES, V31, P23, DOI 10.1016/0167-0115(90)90192-Y
   SINGER FR, 1972, J CLIN INVEST, V51, P2331, DOI 10.1172/JCI107044
   SINGER FR, 1980, ARTHRITIS RHEUM, V23, P1148, DOI 10.1002/art.1780231012
   SIRGRIST SA, 1988, BIOCHEM BIOPH RES CO, V151, P1081
   SKOFITSCH G, 1995, CAN J PHYSIOL PHARM, V73, P945, DOI 10.1139/y95-131
   SKOFITSCH G, 1985, PEPTIDES, V6, P721, DOI 10.1016/0196-9781(85)90178-0
   SKOFITSCH G, 1985, PEPTIDES, V6, P1069, DOI 10.1016/0196-9781(85)90429-2
   SKOFITSCH G, 1994, CAN J PHYSL PHARM, V72, P28
   SMITH DM, 1994, REGUL PEPTIDES, V51, P293, DOI 10.1016/0167-0115(94)90110-4
   STANGL D, 1991, BIOCHEMISTRY-US, V30, P8605, DOI 10.1021/bi00099a016
   STEENBERGH PH, 1985, FEBS LETT, V183, P408, DOI 10.1016/0014-5793(85)80820-6
   STEENBERGH PH, 1984, J CLIN ENDOCR METAB, V59, P358, DOI 10.1210/jcem-59-2-358
   STEINER DF, 1991, DIABETES, V40, P305, DOI 10.2337/diabetes.40.3.305
   STEPHENS TW, 1991, DIABETES, V40, P395, DOI 10.2337/diabetes.40.3.395
   STEVENSON JC, 1986, BMJ-BRIT MED J, V293, P1329, DOI 10.1136/bmj.293.6558.1329
   STEVENSON JC, 1981, LANCET, V1, P693
   STEVENSON JC, 1983, EUR J CLIN INVEST, V13, P481, DOI 10.1111/j.1365-2362.1983.tb00133.x
   STEVENSON JC, 1982, CALCIF TISSUE INT S1, V34, P821
   STRIDSBERG M, 1992, SCAND J GASTROENTERO, V27, P381, DOI 10.3109/00365529209000092
   STRUTHERS AD, 1986, CLIN SCI, V70, P389, DOI 10.1042/cs0700389
   SUGIYAMA A, 1989, JPN J PHARMACOL, V50, P421, DOI 10.1254/jjp.50.421
   SUGO S, 1994, BIOCHEM BIOPH RES CO, V201, P1160, DOI 10.1006/bbrc.1994.1827
   SUPOWIT SC, 1995, BRAIN RES, V686, P77, DOI 10.1016/0006-8993(95)00461-X
   SUZUKI S, 1992, DIABETES RES CLIN PR, V15, P77, DOI 10.1016/0168-8227(92)90071-X
   TABATA H, 1992, DIABETES RES CLIN PR, V15, P57, DOI 10.1016/0168-8227(92)90068-3
   TAGGART HM, 1982, LANCET, V1, P475
   TAKAMI K, 1985, NEUROSCI LETT, V60, P227, DOI 10.1016/0304-3940(85)90248-4
   TAKAMI K, 1986, JPN J PHARMACOL, V42, P345, DOI 10.1254/jjp.42.345
   TAKAMI K, 1985, BRAIN RES, V328, P386, DOI 10.1016/0006-8993(85)91055-8
   TANG J, 1989, CHINESE MED J-PEKING, V102, P897
   Tashjian A H Jr, 1978, Recent Prog Horm Res, V34, P285
   TASHJIAN AH, 1970, NEW ENGL J MED, V283, P890, DOI 10.1056/NEJM197010222831702
   TJENALOOI S, 1992, AM J PHYSIOL, V263, pH681, DOI 10.1152/ajpheart.1992.263.3.H681
   TJENALOOI S, 1994, 2 INT CGRP S MONTR
   TORRING O, 1991, BONE, V12, P311, DOI 10.1016/8756-3282(91)90016-C
   TORRING O, OSTEOPOROSIS, P393
   TOSHIMORI H, 1990, CELL TISSUE RES, V262, P401, DOI 10.1007/BF00305236
   TSCHOPP FA, 1985, P NATL ACAD SCI USA, V82, P248, DOI 10.1073/pnas.82.1.248
   TSUJIMOTO T, 1988, J NEUROSCI, V8, P3951
   TWERY MJ, 1984, PEPTIDES, V5, P665
   UCHIDA S, 1990, J NEUROCHEM, V54, P1000, DOI 10.1111/j.1471-4159.1990.tb02349.x
   UMEDA Y, 1989, JPN J PHARMACOL, V51, P377, DOI 10.1254/jjp.51.377
   URBAN L, 1985, J AUTONOM NERV SYST, V12, P321, DOI 10.1016/0165-1838(85)90047-5
   UREN NG, 1993, CARDIOVASC RES, V27, P1477, DOI 10.1093/cvr/27.8.1477
   VANJAARSVELD BC, 1990, LANCET, V335, P60, DOI 10.1016/0140-6736(90)90197-D
   VATTIMO A, 1982, HUMAN CALCITONIN, P127
   VERGE VMK, 1995, J NEUROSCI, V15, P2081, DOI 10.1523/JNEUROSCI.15-03-02081.1995
   VILLARREAL D, 1988, PEPTIDES, V9, P1129, DOI 10.1016/0196-9781(88)90100-3
   WAGONER PK, 1993, P NATL ACAD SCI USA, V90, P9145, DOI 10.1073/pnas.90.19.9145
   WALLACH S, 1977, CURR THER RES CLIN E, V22, P556
   WANG MW, 1991, BIOCHEM BIOPH RES CO, V181, P1288, DOI 10.1016/0006-291X(91)92078-X
   WANG MW, 1991, FEBS LETT, V291, P195, DOI 10.1016/0014-5793(91)81282-D
   WANG X, 1992, ANN NY ACAD SCI, V657, P502, DOI 10.1111/j.1749-6632.1992.tb22813.x
   WANG X, 1991, CIRC SHOCK, V34, P217
   WESTERMARK P, 1987, AM J PATHOL, V127, P414
   WESTERMARK P, 1987, P NATL ACAD SCI USA, V84, P3881, DOI 10.1073/pnas.84.11.3881
   WESTERMARK P, 1987, DIABETOLOGIA, V30, P887
   WESTERMARK P, 1990, P NATL ACAD SCI USA, V87, P5036, DOI 10.1073/pnas.87.13.5036
   WESTERMARK P, 1986, BIOCHEM BIOPH RES CO, V140, P827, DOI 10.1016/0006-291X(86)90708-4
   WESTLUND KN, 1991, NEUROSCI LETT, V131, P183, DOI 10.1016/0304-3940(91)90609-W
   WIESENFELDHALLIN Z, 1984, NEUROSCI LETT, V52, P199, DOI 10.1016/0304-3940(84)90374-4
   WILLIAMS ED, 1966, J CLIN PATHOL, V19, P103, DOI 10.1136/jcp.19.2.103
   WIMALAWANSA SJ, 1990, MOL CELL ENDOCRINOL, V71, P13, DOI 10.1016/0303-7207(90)90069-K
   WIMALAWANSA SJ, 1989, J NEUROENDOCRINOL, V1, P15, DOI 10.1111/j.1365-2826.1989.tb00071.x
   WIMALAWANSA SJ, 1988, PEPTIDES, V9, P407, DOI 10.1016/0196-9781(88)90276-8
   WIMALAWANSA SJ, 1992, ANN NY ACAD SCI, V657, P70, DOI 10.1111/j.1749-6632.1992.tb22758.x
   WIMALAWANSA SJ, 1993, PEPTIDES, V14, P247, DOI 10.1016/0196-9781(93)90037-H
   WIMALAWANSA SJ, 1995, PEPTIDES, V16, P307, DOI 10.1016/0196-9781(94)00177-4
   WIMALAWANSA SJ, 1993, PEPTIDES, V14, P691, DOI 10.1016/0196-9781(93)90099-3
   Wimalawansa SJ, 1996, ENDOCR REV, V17, P533, DOI 10.1210/er.17.5.533
   WIMALAWANSA SJ, 1987, BRAIN, V110, P1647, DOI 10.1093/brain/110.6.1647
   WIMALAWANSA SJ, 1991, PEPTIDES, V12, P1143, DOI 10.1016/0196-9781(91)90071-V
   WIMALAWANSA SJ, 1988, INT J CARDIOL, V20, P29, DOI 10.1016/0167-5273(88)90313-0
   WIMALAWANSA SJ, 1989, J MOL ENDOCRINOL, V3, P247, DOI 10.1677/jme.0.0030247
   WIMALAWANSA SJ, 1993, NEUROSCIENCE, V54, P513, DOI 10.1016/0306-4522(93)90270-P
   WIMALAWANSA SJ, 1992, AGING-CLIN EXP RES, V4, P211, DOI 10.1007/BF03324093
   WIMALAWANSA SJ, 1992, J BONE MINER RES, V7, P1113
   WIMALAWANSA SJ, 1993, J BONE MINER RES, V8, P467
   WIMALAWANSA SJ, 1993, AM J HYPERTENS, V6, P996, DOI 10.1093/ajh/6.12.996
   WIMALAWANSA SJ, 1987, NEUROENDOCRINOLOGY, V46, P131, DOI 10.1159/000124809
   WIMALAWANSA SJ, 1995, AM J MED, V99, P36, DOI 10.1016/S0002-9343(99)80102-8
   WIMALAWANSA SJ, 1993, CALCIFIED TISSUE INT, V53, P237, DOI 10.1007/BF01320908
   WIMALAWANSA SJ, 1995, CAN J PHYSIOL PHARM, V73, P981, DOI 10.1139/y95-136
   WIMALAWANSA SJ, 1993, CALCIFIED TISSUE INT, V52, P90, DOI 10.1007/BF00308314
   WIMALAWANSA SJ, 1991, J NEUROENDOCRINOL, V3, P319, DOI 10.1111/j.1365-2826.1991.tb00281.x
   WIMALAWANSA SJ, 1994, CAN J PHYSL PHARM S2, V72, P29
   Wimalawansa SJ., 1993, REV ENDOCRINE RELATE, V45, P5
   WIMALAWANSA SJ, 1984, 76 ANN M END SOC AN
   WIMALAWANSA SJ, 1995, MED INTELLIGENCE UNI
   WIMALAWANSA SJ, 1989, ADV BONE REGULATORY, P121
   WIMALAWANSA SJ, 1989, ISOLATION PURIFICATI
   WIMALAWANSA SJ, 1997, IN PRESS J BONE MIN
   WIMALAWANSA SJ, 1988, RECENT RES GYNECOLOG, V2, P239
   WIMALAWANSA SJ, 1993, EXP CLIN ENDOCRINOL, V12, P1
   WIMALAWANSA SJ, UNPUB ENDOCRINE CLIN
   WIMALAWANSA SJ, 1991, INNOVATION PERSPECTI, P111
   WIMALAWANSA SJ, 1988, BONE, V5, P4
   WIMALAWANSA SJ, 1991, THERAPEUTIC DRUGS CL, pC18
   WOHLWEND A, 1985, BIOCHEM BIOPH RES CO, V131, P537, DOI 10.1016/0006-291X(85)91269-0
   WOODHOUSE NJ, 1971, LANCET, V1, P1139
   WYN AU, 1975, ARCH INTERN MED, V134, P1594
   XUEZHANG Q, 1995, ENDOCRINE, V3, P445, DOI 10.1007/BF02935651
   YAGUI K, 1995, EUR J ENDOCRINOL, V132, P487, DOI 10.1530/eje.0.1320487
   Yallampalli C, 1996, HUM REPROD, V11, P895
   YALLAMPALLI C, 1994, ENDOCRINOLOGY, V134, P1971, DOI 10.1210/en.134.4.1971
   YALLAMPALLI C, 1994, AM J OBSTET GYNECOL, V170, P175
   YALLAMPALLI C, 1993, AM J OBSTET GYNECOL, V169, P1316, DOI 10.1016/0002-9378(93)90299-X
   YAMAGUCHI A, 1990, DIABETES, V39, P168, DOI 10.2337/diabetes.39.2.168
   YAMAMOTO M, 1992, ENDOCRINOLOGY, V130, P741, DOI 10.1210/en.130.2.741
   YOSHIZAKI H, 1987, BIOCHEM BIOPH RES CO, V146, P443, DOI 10.1016/0006-291X(87)90549-3
   YOUNG AA, 1992, AM J PHYSIOL, V263, pE274, DOI 10.1152/ajpendo.1992.263.2.E274
   YOUNG AA, 1991, FEBS LETT, V287, P203, DOI 10.1016/0014-5793(91)80051-4
   YOUNG AA, 1992, MOL CELL ENDOCRINOL, V84, pR1, DOI 10.1016/0303-7207(92)90084-J
   YOUNG AA, 1991, FEBS LETT, V291, P101, DOI 10.1016/0014-5793(91)81113-M
   YOUNG AA, 1991, FEBS LETT, V281, P149, DOI 10.1016/0014-5793(91)80380-L
   YOUNG DA, 1990, AM J PHYSIOL, V259, pE457, DOI 10.1152/ajpendo.1990.259.3.E457
   ZAIDI M, 1986, J ENDOCRINOL, V110, P185, DOI 10.1677/joe.0.1100185
   ZAIDI M, 1987, CALCIFIED TISSUE INT, V40, P149, DOI 10.1007/BF02555699
   ZAIDI M, 1985, EUR J PHARMACOL, V117, P283, DOI 10.1016/0014-2999(85)90616-8
   ZAIDI M, 1990, EXP PHYSIOL, V75, P529, DOI 10.1113/expphysiol.1990.sp003429
   ZANELLI JM, 1984, CALCITONIN CHEM PHYS, P223
   ZHOU ZC, 1986, AM J PHYSIOL, V251, pG391, DOI 10.1152/ajpgi.1986.251.3.G391
   ZHU GC, 1991, BIOCHEM BIOPH RES CO, V177, P771, DOI 10.1016/0006-291X(91)91855-7
   ZIEGLER R, 1976, HUMAN CALCITONIN PAG, P167
   ZIERATH JR, 1992, DIABETOLOGIA, V35, P26, DOI 10.1007/BF00400848
   ZIMMERMANN U, 1995, PEPTIDES, V16, P421, DOI 10.1016/0196-9781(94)00195-C
   ZOCCALI C, 1994, J HYPERTENS, V12, P1249
   ZWEERS EJK, 1992, DIABETOLOGIA, V35, pA179
NR 592
TC 367
Z9 423
U1 0
U2 37
PU BEGELL HOUSE INC
PI DANBURY
PA 50 NORTH ST, DANBURY, CT 06810 USA
SN 0892-0915
J9 CRIT REV NEUROBIOL
JI Crit. Rev. Neurobiol.
PY 1997
VL 11
IS 2-3
BP 167
EP 239
DI 10.1615/CritRevNeurobiol.v11.i2-3.40
PG 73
WC Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA XG213
UT WOS:A1997XG21300004
PM 9209829
DA 2025-04-10
ER

PT J
AU Holzenbein, TJ
   Pomposelli, FB
   Miller, A
   Contreras, MA
   Gibbons, GW
   Campbell, DR
   Freeman, DV
   LoGerfo, FW
AF Holzenbein, TJ
   Pomposelli, FB
   Miller, A
   Contreras, MA
   Gibbons, GW
   Campbell, DR
   Freeman, DV
   LoGerfo, FW
TI Results of a policy with arm veins used as the first alternative to an
   unavailable ipsilateral greater saphenous vein for infrainguinal bypass
SO JOURNAL OF VASCULAR SURGERY
LA English
DT Article
ID LOWER-EXTREMITY REVASCULARIZATION; AUTOGENOUS TISSUE; LIMB SALVAGE;
   GRAFTS; RECONSTRUCTIONS; DISEASE; EXPERIENCE; ANGIOSCOPY
AB Purpose: Aggressive policies for distal bypass and coronary revascularization increase the need to identify alternatives to autologous saphenous vein grafts. We examined the performance of arm vein as the primary alternative to contralateral saphenous vein when the ipsilateral saphenous vein was not available.
   Methods: A total of 250 arm vein grafts were studied retrospectively in 224 patients (143 men, 81 women, 82.6% with diabetes, mean age 68.3 years) from February 1989 to April 1994. Intraoperative angioscopy was carried out to observe valve lysis, remove abnormalities, and select optimal vein segments.
   Results: A total of 85 primary, 103 repeat, and 62 graft revision procedures were done for limb salvage in 99.2% of the patients. A total of 41 femoropopliteal, 114 femorotibial-pedal, 33 popliteodistal, and 62 jump or interposition grafts were constructed. A total of 199 grafts were single vein, and 51 were composite vein. The source was cephalic vein alone in 50.4%, cephalic and basilic vein in 35.6%, and basilic vein only in 14%. The contralateral saphenous vein as an alternative conduit was available in 97 (38.8%) instances. Interventions guided by angioscopy to ''upgrade'' the graft were necessary in 51.6%. Overall early patency (less than or equal to 30 days) was 94.8% (n = 13 occlusions). The cumulative primary patency rate at 1 year was 70.6%, the secondary patency rate was 76.9%, and the limb salvage rate was 88.2%. The 3-year patency rate (limb salvage) was 51.9% (92.4%) for primary grafts, 56.7% (67.1%) in revision grafts, and 42.4% (79.9%) in repeat grafts. In 22.7% (22 of 97) the available contralateral saphenous vein was used for distal revascularization within the follow-up period.
   Conclusions: Arm veins are an easily accessible autologous conduit of sufficient length to reach the midtibial level. Excellent patency rates allow durable limb salvage in otherwise difficult circumstances. Vein configuration and splicing do not affect patency rates, but vein quality and repeat operations do. Angioscopy is a valuable adjunct to upgrade graft quality. The contralateral saphenous should be saved for subsequent contralateral revascularization or coronary artery bypass grafting.
C1 HARVARD UNIV, NEW ENGLAND DEACONESS HOSP,SCH MED,DIV VASC SURG, HARVARD DEACONESS SURG SERV, BOSTON, MA 02215 USA.
C3 Harvard University; Harvard Medical School; Harvard University Medical
   Affiliates; Beth Israel Deaconess Medical Center
CR ANDROS G, 1986, J VASC SURG, V4, P416, DOI 10.1067/mva.1986.avs0040416
   BALSHI JD, 1989, ARCH SURG-CHICAGO, V124, P1078
   CAMPBELL DR, 1979, ANN SURG, V190, P740, DOI 10.1097/00000658-197912000-00012
   CHANG BB, 1992, J VASC SURG, V15, P152, DOI 10.1016/0741-5214(92)70023-E
   DARDIK H, 1988, J VASC SURG, V7, P336, DOI 10.1067/mva.1988.avs0070336
   DONALDSON MC, 1993, J VASC SURG, V18, P41, DOI 10.1067/mva.1993.41958
   ELMASSRY S, 1994, J VASC SURG, V19, P487, DOI 10.1016/S0741-5214(94)70076-1
   Grigg M J, 1988, Eur J Vasc Surg, V2, P49, DOI 10.1016/S0950-821X(88)80108-7
   HARRIS RW, 1984, ANN SURG, V200, P785, DOI 10.1097/00000658-198412000-00019
   HARRIS RW, 1993, J VASC SURG, V18, P553, DOI 10.1016/0741-5214(93)90064-S
   HOLZENBEIN T, 1995, IN PRESS J VASC SURG
   KAKKAR VV, 1969, SURG GYNECOL OBSTETR, V128, P551
   KAPLAN EL, 1958, J AM STAT ASSOC, V53, P457, DOI 10.2307/2281868
   LOGERFO FW, 1987, J VASC SURG, V5, P889, DOI 10.1067/mva.1987.avs0050889
   LOGERFO FW, 1983, CIRCULATION, V68, P117
   LONDREY GL, 1994, J VASC SURG, V20, P451, DOI 10.1016/0741-5214(94)90145-7
   MARCACCIO EJ, 1993, J VASC SURG, V17, P994, DOI 10.1016/0741-5214(93)90669-D
   MILLER A, 1989, ARCH SURG-CHICAGO, V124, P604
   MILLER A, 1991, J VASC SURG, V13, P813
   PANETTA TF, 1992, J VASC SURG, V15, P102, DOI 10.1016/0741-5214(92)70018-G
   RUTHERFORD RB, 1990, J VASC SURG, V12, P422, DOI 10.1067/mva.1990.23532
   RUTHERFORD RB, 1986, J VASC SURG, V4, P80
   SALES CM, 1993, J VASC SURG, V18, P198, DOI 10.1016/0741-5214(93)90599-H
   SCHULMAN ML, 1986, ARCH SURG-CHICAGO, V121, P1010
   SCHWEIGER H, 1993, J VASC SURG, V18, P867, DOI 10.1016/0741-5214(93)90343-K
   SESTO ME, 1992, J VASC SURG, V15, P543, DOI 10.1016/0741-5214(92)90194-D
   STONEBRIDGE PA, 1991, ANN VASC SURG, V5, P171
   TAYLOR LM, 1987, AM J SURG, V153, P505, DOI 10.1016/0002-9610(87)90803-8
   TAYLOR LM, 1990, J VASC SURG, V11, P193, DOI 10.1067/mva.1990.17235
   VANDERHEIJDEN FHWM, 1993, J VASC SURG, V18, P271, DOI 10.1016/0741-5214(93)90608-O
   VEITH FJ, 1986, J VASC SURG, V3, P104
   VERMASSEN F, 1992, J CARDIOVASC SURG, V33, P641
   WEAVER FA, 1987, J VASC SURG, V5, P687, DOI 10.1067/mva.1987.avs0050687
   YANG PM, 1991, J VASC SURG, V14, P292, DOI 10.1016/0741-5214(91)90079-A
NR 34
TC 87
Z9 87
U1 0
U2 1
PU MOSBY-ELSEVIER
PI NEW YORK
PA 360 PARK AVENUE SOUTH, NEW YORK, NY 10010-1710 USA
SN 0741-5214
J9 J VASC SURG
JI J. Vasc. Surg.
PD JAN
PY 1996
VL 23
IS 1
BP 130
EP 140
DI 10.1016/S0741-5214(05)80043-6
PG 11
WC Surgery; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Surgery; Cardiovascular System & Cardiology
GA TT545
UT WOS:A1996TT54500014
PM 8558728
OA Bronze
DA 2025-04-10
ER

PT J
AU Eto, K
   Eda, K
   Kanemoto, S
   Abe, S
AF Eto, Ko
   Eda, Kazufumi
   Kanemoto, Shintaro
   Abe, Shin-ichi
TI The immunoglobulin-like domain is involved in interaction of Neuregulin1
   with ErbB
SO BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
LA English
DT Article
DE Neuregulin1; immunoglobulin-like domain; epidermal growth factor-like
   domain; ErbB receptor; isoform; signaling
ID NEU DIFFERENTIATION FACTOR; RECEPTOR GENE-EXPRESSION; GLIAL
   GROWTH-FACTOR; CARDIAC DEVELOPMENT; XENOPUS NEUREGULIN; CULTURED
   MYOTUBES; HEREGULIN; SURVIVAL; MUSCLE; ARIA
AB Neuregulin I (NRG 1) is a growth factor that signals through the interaction of the epidermal growth factor (EGF)-like domain with ErbB receptors. An immunoglobulin (1g)-like domain is contained together with EGF-like domain in the ectodomain of some isoforms generated by alternative splicing, but its role in NRGI signaling remained unclear. In the present study, we identified a novel isoform of NRGI containing an Ig-like domain conserved among species from adult Xenopus laevis, which is predominantly expressed in the testis and brain. We generated recombinant proteins for the whole ectodomain and EGF-like domain alone of the isoform to compare their effects on cell proliferation, and phosphorylation of and their association with ErbB receptor, demonstrating that the ectodomain had similar to 10(3)- fold higher abilities than the EGF-like domain. Therefore, the Ig-like domain is probably essential for efficient interaction of an EGF-like domain with ErbB receptors. (c) 2006 Elsevier Inc. All rights reserved.
C1 Kumamoto Univ, Grad Sch Sci & Technol, Dept Biol Sci, Kumamoto 8608555, Japan.
C3 Kumamoto University
RP Eto, K (corresponding author), Kumamoto Univ, Grad Sch Sci & Technol, Dept Biol Sci, 2-39-1 Kurokami, Kumamoto 8608555, Japan.
EM etoko@gpo.kumamoto-u.ac.jp
CR ALTIOK N, 1995, EMBO J, V14, P4258, DOI 10.1002/j.1460-2075.1995.tb00100.x
   Altiok N, 1997, EMBO J, V16, P717, DOI 10.1093/emboj/16.4.717
   ANTON EM, UNPUB
   BerminghamMcDonogh O, 1996, DEVELOPMENT, V122, P1427
   Buonanno A, 2001, CURR OPIN NEUROBIOL, V11, P287, DOI 10.1016/S0959-4388(00)00210-5
   Burden S, 1997, NEURON, V18, P847, DOI 10.1016/S0896-6273(00)80324-4
   BURGESS TL, 1995, J BIOL CHEM, V270, P19188, DOI 10.1074/jbc.270.32.19188
   Canoll PD, 1996, NEURON, V17, P229, DOI 10.1016/S0896-6273(00)80155-5
   CARRAWAY KL, 1995, CURR OPIN NEUROBIOL, V5, P606, DOI 10.1016/0959-4388(95)80065-4
   Chung HG, 1999, MOL CELLS, V9, P497
   DONG Z, 1995, NEURON, V15, P585, DOI 10.1016/0896-6273(95)90147-7
   Escher P, 2005, SCIENCE, V308, P1920, DOI 10.1126/science.1108258
   Falls DL, 2003, EXP CELL RES, V284, P14, DOI 10.1016/S0014-4827(02)00102-7
   FALLS DL, 1993, CELL, V72, P801, DOI 10.1016/0092-8674(93)90407-H
   Florini JR, 1996, J BIOL CHEM, V271, P12699, DOI 10.1074/jbc.271.22.12699
   GASSMANN M, 1995, NATURE, V378, P390, DOI 10.1038/378390a0
   GOODEARL ADJ, 1995, J CELL BIOL, V130, P1423, DOI 10.1083/jcb.130.6.1423
   Han B, 1999, J BIOL CHEM, V274, P26407, DOI 10.1074/jbc.274.37.26407
   HO WH, 1995, J BIOL CHEM, V270, P14523, DOI 10.1074/jbc.270.24.14523
   HOLMES WE, 1992, SCIENCE, V256, P1205, DOI 10.1126/science.256.5060.1205
   Jones JT, 1999, FEBS LETT, V447, P227, DOI 10.1016/S0014-5793(99)00283-5
   Kramer R, 1996, P NATL ACAD SCI USA, V93, P4833, DOI 10.1073/pnas.93.10.4833
   LEE KF, 1995, NATURE, V378, P394, DOI 10.1038/378394a0
   LEVI ADO, 1995, J NEUROSCI, V15, P1329
   LOEB JA, 1995, J CELL BIOL, V130, P127, DOI 10.1083/jcb.130.1.127
   MARCHIONNI MA, 1995, NATURE, V378, P334, DOI 10.1038/378334a0
   MEYER D, 1995, NATURE, V378, P386, DOI 10.1038/378386a0
   Montero JC, 2000, MOL CELL NEUROSCI, V16, P631, DOI 10.1006/mcne.2000.0896
   PELES E, 1992, CELL, V69, P205, DOI 10.1016/0092-8674(92)90131-U
   Pinkas-Kramarski R, 1998, MOL CELL BIOL, V18, P6090, DOI 10.1128/MCB.18.10.6090
   Pun S, 1997, FEBS LETT, V418, P275, DOI 10.1016/S0014-5793(97)01369-0
   Rimer M, 2003, J NEUROCYTOL, V32, P665, DOI 10.1023/B:NEUR.0000020615.79831.51
   Trachtenberg JT, 1996, NATURE, V379, P174, DOI 10.1038/379174a0
   WEN DZ, 1994, MOL CELL BIOL, V14, P1909, DOI 10.1128/MCB.14.3.1909
   WEN DZ, 1992, CELL, V69, P559, DOI 10.1016/0092-8674(92)90456-M
   Yang JF, 1999, MOL CELL NEUROSCI, V13, P415, DOI 10.1006/mcne.1999.0759
   Yang JF, 1998, MOL BRAIN RES, V58, P59, DOI 10.1016/S0169-328X(98)00085-0
   Zhao YY, 1998, J BIOL CHEM, V273, P10261, DOI 10.1074/jbc.273.17.10261
NR 38
TC 17
Z9 17
U1 0
U2 3
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0006-291X
EI 1090-2104
J9 BIOCHEM BIOPH RES CO
JI Biochem. Biophys. Res. Commun.
PD NOV 17
PY 2006
VL 350
IS 2
BP 263
EP 271
DI 10.1016/j.bbrc.2006.09.028
PG 9
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA 096PS
UT WOS:000241389900003
PM 17007820
DA 2025-04-10
ER

PT J
AU DeHaven, WI
   Cuevas, J
AF DeHaven, WI
   Cuevas, J
TI Heterogeneity of pituitary adenylate cyclase-activating polypeptide and
   vasoactive intestinal polypeptide receptors in rat intrinsic cardiac
   neurons
SO NEUROSCIENCE LETTERS
LA English
DT Article
DE pituitary adenylate cyclase-activating polypeptide; vasoactive
   intestinal polypeptide; pituitary adenylate cyclase-activating;
   polypeptide type 1 receptor; vasoactive intestinal polypeptide receptor;
   single-cell reverse transcription-polymerase chain, reaction;
   intracardiac ganglia; alternative splicing; parasympathetic neurons
ID PARASYMPATHETIC NEURONS; PACAP RECEPTOR; MODULATION; BLOCKADE; HEART;
   NEUROPEPTIDE; STIMULATION; EXPRESSION; GANGLIA; INSITU
AB The expression of receptors for pituitary adenylate cyclase-activating polypeptide (PACAP) and vasoactive intestinal polypeptide (VIP) was investigated in isolated parasympathetic neurons of neonatal rat intracardiac ganglia using single-cell reverse transcription-polymerase chain reaction. Individual neurons were shown to express multiple isoforms of the PACAP receptor, PAC1, including PAC1-short, -HOP1 and -HOP2 variants, which differ in the region encoding the G protein-binding domain. The PAC1-HOP1 isoform was the predominant species, being expressed at higher levels and in a greater number of cells than other PAC1 variants. In addition to PAC1, intrinsic cardiac neurons express transcripts for the VIP receptors, VPAC1 and VPAC2, with VPAC2 being found in a greater proportion of the neurons. These findings may explain the complex effects of PACAP and VIP on neuroexcitability in mammalian intracardiac ganglia. (C) 2002 Elsevier Science Ireland Ltd. All rights reserved.
C1 Univ S Florida, Coll Med, Dept Pharmacol & Therapeut, Tampa, FL 33612 USA.
C3 State University System of Florida; University of South Florida
RP Cuevas, J (corresponding author), Univ S Florida, Coll Med, Dept Pharmacol & Therapeut, 12901 Bruce B Downs Blvd,MDC 9, Tampa, FL 33612 USA.
RI Cuevas, Javier/I-4941-2012
FU NHLBI NIH HHS [HL63247] Funding Source: Medline
CR Ardell JL., 1994, NEUROCARDIOLOGY, P95
   ARMOUR JA, 1993, PEPTIDES, V14, P191, DOI 10.1016/0196-9781(93)90029-G
   Braas KM, 1999, J BIOL CHEM, V274, P27702, DOI 10.1074/jbc.274.39.27702
   Braas KM, 1998, J NEUROSCI, V18, P9766
   Cuevas J, 1996, J PHYSIOL-LONDON, V493, P503, DOI 10.1113/jphysiol.1996.sp021399
   Cuevas J, 1998, J NEUROSCI, V18, P10335
   Feliciano L, 1998, J AUTONOM NERV SYST, V68, P78, DOI 10.1016/S0165-1838(97)00109-4
   GOURLET P, 1995, EUR J PHARMACOL, V287, P7, DOI 10.1016/0014-2999(95)00467-5
   HENNING RJ, 1992, J AUTONOM NERV SYST, V40, P121, DOI 10.1016/0165-1838(92)90023-A
   Hirose M, 1997, J PHARMACOL EXP THER, V283, P478
   KARASAWA Y, 1990, EUR J PHARMACOL, V187, P9
   Liu DM, 2000, EUR J NEUROSCI, V12, P2243, DOI 10.1046/j.1460-9568.2000.00116.x
   McCulloch DA, 2001, MOL PHARMACOL, V59, P1523, DOI 10.1124/mol.59.6.1523
   Pantaloni C, 1996, J BIOL CHEM, V271, P22146, DOI 10.1074/jbc.271.36.22146
   Poth K, 1997, J NEUROSCI, V17, P586
   ROSSASCUITTO NT, 1993, PEDIATR RES, V34, P323, DOI 10.1203/00006450-199309000-00017
   SEABROOK GR, 1990, AM J PHYSIOL, V259, pH997, DOI 10.1152/ajpheart.1990.259.4.H997
   SPENGLER D, 1993, NATURE, V365, P170, DOI 10.1038/365170a0
   WARREN JB, 1991, EUR J PHARMACOL, V197, P131, DOI 10.1016/0014-2999(91)90511-N
   WEIHE E, 1984, CELL TISSUE RES, V236, P527
NR 20
TC 18
Z9 21
U1 0
U2 0
PU ELSEVIER SCI IRELAND LTD
PI CLARE
PA CUSTOMER RELATIONS MANAGER, BAY 15, SHANNON INDUSTRIAL ESTATE CO, CLARE,
   IRELAND
SN 0304-3940
J9 NEUROSCI LETT
JI Neurosci. Lett.
PD AUG 2
PY 2002
VL 328
IS 1
BP 45
EP 49
AR PII S0304-3940(02)00445-7
DI 10.1016/S0304-3940(02)00445-7
PG 5
WC Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA 584AH
UT WOS:000177444700012
PM 12123856
DA 2025-04-10
ER

PT J
AU Lee, H
   Yoon, Y
AF Lee, Hakjoo
   Yoon, Yisang
TI Mitochondrial Membrane Dynamics-Functional Positioning of OPA1
SO ANTIOXIDANTS
LA English
DT Review
DE mitochondria; mitochondrial dynamics; fission; fusion; Oxidative
   phosphorylation (OXPHOS); OPA1; cristae; Overlapping activity with m-AAA
   protease 1 (OMA1); cardiolipin
ID DOMINANT OPTIC ATROPHY; CYTOCHROME-C RELEASE; INNER MEMBRANE; CRISTAE
   MORPHOGENESIS; PROTEOLYTIC CLEAVAGE; PHOSPHATIDIC-ACID; DRP1
   RECRUITMENT; LIPID DROPLETS; OMA1 PROTEASE; FISSION
AB The maintenance of mitochondrial energetics requires the proper regulation of mitochondrial morphology, and vice versa. Mitochondrial dynamins control mitochondrial morphology by mediating fission and fusion. One of them, optic atrophy 1 (OPA1), is the mitochondrial inner membrane remodeling protein. OPA1 has a dual role in maintaining mitochondrial morphology and energetics through mediating inner membrane fusion and maintaining the cristae structure. OPA1 is expressed in multiple variant forms through alternative splicing and post-translational proteolytic cleavage, but the functional differences between these variants have not been completely understood. Recent studies generated new information regarding the role of OPA1 cleavage. In this review, we will first provide a brief overview of mitochondrial membrane dynamics by describing fission and fusion that are mediated by mitochondrial dynamins. The second part describes OPA1-mediated fusion and energetic maintenance, the role of OPA1 cleavage, and a new development in OPA1 function, in which we will provide new insight for what OPA1 does and what proteolytic cleavage of OPA1 is for.
C1 [Lee, Hakjoo; Yoon, Yisang] Augusta Univ, Dept Physiol, Med Coll Georgia, Augusta, GA 30912 USA.
C3 University System of Georgia; Augusta University
RP Yoon, Y (corresponding author), Augusta Univ, Dept Physiol, Med Coll Georgia, Augusta, GA 30912 USA.
EM haklee@augusta.edu; yyoon@augusta.edu
RI Yoon, Yisang/AAJ-7910-2020
OI Yoon, Yisang/0000-0002-1618-5439
FU American Heart Association (AHA) [16GRNT31170032]; American Heart
   Association (AHA) [16GRNT31170032] Funding Source: American Heart
   Association (AHA)
FX This work was supported by American Heart Association (AHA)
   16GRNT31170032.
CR Acin-Perez R, 2018, SCI TRANSL MED, V10, DOI 10.1126/scitranslmed.aan4935
   Acin-Perez R, 2014, BBA-BIOENERGETICS, V1837, P444, DOI 10.1016/j.bbabio.2013.12.009
   Adachi Y, 2016, MOL CELL, V63, P1034, DOI 10.1016/j.molcel.2016.08.013
   Alexander C, 2000, NAT GENET, V26, P211, DOI 10.1038/79944
   Anand R, 2014, J CELL BIOL, V204, P919, DOI 10.1083/jcb.201308006
   [Anonymous], 1992, BIOENERGETICS
   ARDAIL D, 1990, J BIOL CHEM, V265, P18797
   Baker BM, 2011, TRENDS BIOCHEM SCI, V36, P254, DOI 10.1016/j.tibs.2011.01.004
   Baker MJ, 2014, EMBO J, V33, P578, DOI 10.1002/embj.201386474
   Ban T, 2018, BBA-BIOENERGETICS, V1859, P951, DOI 10.1016/j.bbabio.2018.05.016
   Ban T, 2017, NAT CELL BIOL, V19, P856, DOI 10.1038/ncb3560
   Ban T, 2010, HUM MOL GENET, V19, P2113, DOI 10.1093/hmg/ddq088
   Barrera M, 2016, FEBS LETT, V590, P3309, DOI 10.1002/1873-3468.12384
   Bavelloni A, 2015, IUBMB LIFE, V67, P239, DOI 10.1002/iub.1366
   Belenguer P, 2013, BBA-MOL CELL RES, V1833, P176, DOI 10.1016/j.bbamcr.2012.08.004
   Benador IY, 2018, CELL METAB, V27, P869, DOI 10.1016/j.cmet.2018.03.003
   Bohovych I, 2015, SCI REP-UK, V5, DOI 10.1038/srep13989
   Boissan M, 2014, SCIENCE, V344, P1510, DOI 10.1126/science.1253768
   Boutant M, 2017, EMBO J, V36, P1543, DOI 10.15252/embj.201694914
   Brandt T, 2016, ELIFE, V5, DOI 10.7554/eLife.14618
   Bustillo-Zabalbeitia I, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0102738
   Cao YL, 2017, NATURE, V542, P372, DOI 10.1038/nature21077
   Chen HC, 2005, J BIOL CHEM, V280, P26185, DOI 10.1074/jbc.M503062200
   Chen HC, 2003, J CELL BIOL, V160, P189, DOI 10.1083/jcb.200211046
   Chen HC, 2010, CELL, V141, P280, DOI 10.1016/j.cell.2010.02.026
   Choi SY, 2006, NAT CELL BIOL, V8, P1255, DOI 10.1038/ncb1487
   Civiletto G, 2015, CELL METAB, V21, P845, DOI 10.1016/j.cmet.2015.04.016
   Cogliati S, 2013, CELL, V155, P160, DOI 10.1016/j.cell.2013.08.032
   Davies KM, 2012, P NATL ACAD SCI USA, V109, P13602, DOI 10.1073/pnas.1204593109
   Del Dotto V, 2017, CELL REP, V19, P2557, DOI 10.1016/j.celrep.2017.05.073
   Delettre C, 2000, NAT GENET, V26, P207, DOI 10.1038/79936
   Delettre C, 2001, HUM GENET, V109, P584, DOI 10.1007/s00439-001-0633-y
   Desmurs M, 2015, MOL CELL BIOL, V35, P1139, DOI 10.1128/MCB.01047-14
   Dudek J, 2017, FRONT CELL DEV BIOL, V5, DOI 10.3389/fcell.2017.00090
   Ehses S, 2009, J CELL BIOL, V187, P1023, DOI 10.1083/jcb.200906084
   Fish KN, 2000, J CELL BIOL, V150, P145, DOI 10.1083/jcb.150.1.145
   Francy CA, 2015, J BIOL CHEM, V290, P11692, DOI 10.1074/jbc.M114.610881
   Frank S, 2001, DEV CELL, V1, P515, DOI 10.1016/S1534-5807(01)00055-7
   Frezza C, 2006, CELL, V126, P177, DOI 10.1016/j.cell.2006.06.025
   Friedman JR, 2011, SCIENCE, V334, P358, DOI 10.1126/science.1207385
   Gandre-Babbe S, 2008, MOL BIOL CELL, V19, P2402, DOI 10.1091/mbc.E07-12-1287
   Genova ML, 2014, BBA-BIOENERGETICS, V1837, P427, DOI 10.1016/j.bbabio.2013.11.002
   Gomes LC, 2011, NAT CELL BIOL, V13, P589, DOI 10.1038/ncb2220
   Gonzalvez F, 2005, CELL DEATH DIFFER, V12, P614, DOI 10.1038/sj.cdd.4401571
   Griparic L, 2004, J BIOL CHEM, V279, P18792, DOI 10.1074/jbc.M400920200
   Griparic L, 2007, J CELL BIOL, V178, P757, DOI 10.1083/jcb.200704112
   Head B, 2009, J CELL BIOL, V187, P959, DOI 10.1083/jcb.200906083
   Hoppel CL, 2009, INT J BIOCHEM CELL B, V41, P1949, DOI 10.1016/j.biocel.2009.05.004
   Horvath SE, 2013, PROG LIPID RES, V52, P590, DOI 10.1016/j.plipres.2013.07.002
   Ishihara N, 2006, EMBO J, V25, P2966, DOI 10.1038/sj.emboj.7601184
   James DI, 2003, J BIOL CHEM, V278, P36373, DOI 10.1074/jbc.M303758200
   Jiang X, 2014, P NATL ACAD SCI USA, V111, P14782, DOI 10.1073/pnas.1417253111
   Kagan VE, 2016, CELL DEATH DIFFER, V23, P1140, DOI 10.1038/cdd.2015.160
   Kagan VE, 2005, NAT CHEM BIOL, V1, P223, DOI 10.1038/nchembio727
   Kameoka S, 2018, TRENDS CELL BIOL, V28, P67, DOI 10.1016/j.tcb.2017.08.011
   Kasashima K, 2006, J BIOL CHEM, V281, P36401, DOI 10.1074/jbc.M605260200
   Käser M, 2003, J BIOL CHEM, V278, P46414, DOI 10.1074/jbc.M305584200
   Khalifat N, 2011, BBA-BIOMEMBRANES, V1808, P2724, DOI 10.1016/j.bbamem.2011.07.013
   Khalimonchuk O, 2012, J BIOL CHEM, V287, P7289, DOI 10.1074/jbc.M111.313148
   Koirala S, 2013, P NATL ACAD SCI USA, V110, pE1342, DOI 10.1073/pnas.1300855110
   Korobova F, 2014, CURR BIOL, V24, P409, DOI 10.1016/j.cub.2013.12.032
   Korobova F, 2013, SCIENCE, V339, P464, DOI 10.1126/science.1228360
   Korwitz A, 2016, J CELL BIOL, V212, P157, DOI 10.1083/jcb.201507022
   Koshiba T, 2004, SCIENCE, V305, P858, DOI 10.1126/science.1099793
   Kushnareva YE, 2013, CELL DEATH DIFFER, V20, P353, DOI 10.1038/cdd.2012.128
   Landes T, 2010, SEMIN CELL DEV BIOL, V21, P593, DOI 10.1016/j.semcdb.2009.12.012
   Langer T, 2001, BIOCHEM SOC T, V29, P431, DOI 10.1042/BST0290431
   Lapuente-Brun E, 2013, SCIENCE, V340, P1567, DOI 10.1126/science.1230381
   Lee H, 2017, J BIOL CHEM, V292, P7115, DOI 10.1074/jbc.M116.762567
   Lee H, 2016, BIOCHEM SOC T, V44, P1725, DOI 10.1042/BST20160129
   Lee JE, 2016, NATURE, V540, P139, DOI 10.1038/nature20555
   Lee YJ, 2004, MOL BIOL CELL, V15, P5001, DOI 10.1091/mbc.E04-04-0294
   Liu XG, 2009, EMBO J, V28, P3074, DOI 10.1038/emboj.2009.255
   Losón OC, 2013, MOL BIOL CELL, V24, P659, DOI 10.1091/mbc.E12-10-0721
   Macdonald PJ, 2016, J BIOL CHEM, V291, P493, DOI 10.1074/jbc.M115.680181
   Macdonald PJ, 2014, MOL BIOL CELL, V25, P1905, DOI 10.1091/mbc.E14-02-0728
   MacVicar TDB, 2014, J CELL SCI, V127, P2313, DOI 10.1242/jcs.144337
   Mannella CA, 2013, J MOL CELL CARDIOL, V62, P51, DOI 10.1016/j.yjmcc.2013.05.001
   Manor U, 2015, ELIFE, V4, DOI 10.7554/eLife.08828
   Mears JA, 2011, NAT STRUCT MOL BIOL, V18, P20, DOI 10.1038/nsmb.1949
   Merkwirth C, 2008, GENE DEV, V22, P476, DOI 10.1101/gad.460708
   Mishra P, 2016, J CELL BIOL, V212, P379, DOI 10.1083/jcb.201511036
   Mishra P, 2014, CELL METAB, V19, P630, DOI 10.1016/j.cmet.2014.03.011
   Mishra S, 2006, J CELL MOL MED, V10, P353, DOI 10.1111/j.1582-4934.2006.tb00404.x
   MITCHELL P, 1961, NATURE, V191, P144, DOI 10.1038/191144a0
   Mottie S, 2018, J CELL BIOL, V217, P507, DOI 10.1083/jcb.201611194
   Olichon A, 2007, CELL DEATH DIFFER, V14, P682, DOI 10.1038/sj.cdd.4402048
   Olichon A, 2003, J BIOL CHEM, V278, P7743, DOI 10.1074/jbc.C200677200
   Olichon A, 2002, FEBS LETT, V523, P171, DOI 10.1016/S0014-5793(02)02985-X
   Osellame LD, 2016, J CELL SCI, V129, P2170, DOI 10.1242/jcs.185165
   Osman C, 2009, J CELL SCI, V122, P3823, DOI 10.1242/jcs.037655
   Otera H, 2016, J CELL BIOL, V212, P531, DOI 10.1083/jcb.201508099
   Otera H, 2010, J CELL BIOL, V191, P1141, DOI 10.1083/jcb.201007152
   Palmer CS, 2013, J BIOL CHEM, V288, P27584, DOI 10.1074/jbc.M113.479873
   Palmer CS, 2011, EMBO REP, V12, P565, DOI 10.1038/embor.2011.54
   Patten DA, 2014, EMBO J, V33, P2676, DOI 10.15252/embj.201488349
   Peng YT, 2015, APOPTOSIS, V20, P1135, DOI 10.1007/s10495-015-1143-z
   Perkins GA, 2001, J NEUROSCI RES, V66, P857, DOI 10.1002/jnr.10050
   Perkins G, 2009, EXP NEUROL, V218, P183, DOI 10.1016/j.expneurol.2009.05.021
   Pernas L, 2016, ANNU REV PHYSIOL, V78, P505, DOI 10.1146/annurev-physiol-021115-105011
   Pidoux G, 2011, EMBO J, V30, P4371, DOI 10.1038/emboj.2011.365
   Qi YB, 2016, J CELL BIOL, V215, P621, DOI 10.1083/jcb.201609019
   Rainbolt TK, 2016, CELL REP, V14, P2041, DOI 10.1016/j.celrep.2016.02.011
   Rainbolt TK, 2013, CELL METAB, V18, P908, DOI 10.1016/j.cmet.2013.11.006
   Renner LD, 2011, P NATL ACAD SCI USA, V108, P6264, DOI 10.1073/pnas.1015757108
   Riva A, 2005, AM J PHYSIOL-HEART C, V289, pH868, DOI 10.1152/ajpheart.00866.2004
   Rogne M, 2018, MOL BIOL CELL, V29, P1487, DOI 10.1091/mbc.E17-09-0538
   Rujiviphat J, 2009, J BIOL CHEM, V284, P28682, DOI 10.1074/jbc.M109.044933
   Schägger H, 2000, EMBO J, V19, P1777, DOI 10.1093/emboj/19.8.1777
   Schägger H, 2001, J BIOL CHEM, V276, P37861
   SCHLAME M, 1993, J BIOL CHEM, V268, P74
   Schlattner U, 2018, LAB INVEST, V98, P228, DOI 10.1038/labinvest.2017.113
   Schlattner U, 2013, J BIOL CHEM, V288, P111, DOI 10.1074/jbc.M112.408633
   Schlattner U, 2009, BBA-BIOMEMBRANES, V1788, P2032, DOI 10.1016/j.bbamem.2009.04.018
   Scorrano L, 2003, CELL DEATH DIFFER, V10, P1287, DOI 10.1038/sj.cdd.4401310
   Sebastián D, 2017, TRENDS MOL MED, V23, P201, DOI 10.1016/j.molmed.2017.01.003
   SEDDON JM, 1990, BIOCHIM BIOPHYS ACTA, V1031, P1, DOI 10.1016/0304-4157(90)90002-T
   Sever S, 1999, NATURE, V398, P481, DOI 10.1038/19024
   Shen QF, 2014, MOL BIOL CELL, V25, P145, DOI 10.1091/mbc.E13-09-0525
   Song ZY, 2007, J CELL BIOL, V178, P749, DOI 10.1083/jcb.200704110
   Song ZY, 2009, MOL BIOL CELL, V20, P3525, DOI 10.1091/mbc.E09-03-0252
   Sood A, 2014, P NATL ACAD SCI USA, V111, P16017, DOI 10.1073/pnas.1408061111
   Stepanyants N, 2015, MOL BIOL CELL, V26, P3104, DOI 10.1091/mbc.E15-06-0330
   Stiburek L, 2012, MOL BIOL CELL, V23, P1010, DOI 10.1091/mbc.E11-08-0674
   Stojanovski D, 2004, J CELL SCI, V117, P1201, DOI 10.1242/jcs.01058
   Strauss M, 2008, EMBO J, V27, P1154, DOI 10.1038/emboj.2008.35
   Sun MG, 2007, NAT CELL BIOL, V9, P1057, DOI 10.1038/ncb1630
   Szabadkai G, 2004, MOL CELL, V16, P59, DOI 10.1016/j.molcel.2004.09.026
   Tokarska-Schlattner M, 2008, J BIOL CHEM, V283, P26198, DOI 10.1074/jbc.M803132200
   Tondera D, 2009, EMBO J, V28, P1589, DOI 10.1038/emboj.2009.89
   Twig G, 2008, EMBO J, V27, P433, DOI 10.1038/sj.emboj.7601963
   Varanita T, 2015, CELL METAB, V21, P834, DOI 10.1016/j.cmet.2015.05.007
   Vonck J, 2009, BBA-MOL CELL RES, V1793, P117, DOI 10.1016/j.bbamcr.2008.05.019
   Wai T, 2016, TRENDS ENDOCRIN MET, V27, P105, DOI 10.1016/j.tem.2015.12.001
   Wai T, 2015, SCIENCE, V350, DOI 10.1126/science.aad0116
   Wang H, 2011, J LIPID RES, V52, P2159, DOI 10.1194/jlr.M017939
   Xiao X, 2014, AM J PHYSIOL-RENAL, V306, pF1318, DOI 10.1152/ajprenal.00036.2014
   Yamaguchi R, 2008, MOL CELL, V31, P557, DOI 10.1016/j.molcel.2008.07.010
   Yamaguchi R, 2009, BBA-BIOENERGETICS, V1787, P963, DOI 10.1016/j.bbabio.2009.02.005
   Yoon Y, 2001, MOL BIOL CELL, V12, P2894, DOI 10.1091/mbc.12.9.2894
   Yoon Y, 2003, MOL CELL BIOL, V23, P5409, DOI 10.1128/MCB.23.15.5409-5420.2003
   Zhao J, 2011, EMBO J, V30, P2762, DOI 10.1038/emboj.2011.198
NR 142
TC 49
Z9 55
U1 3
U2 18
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
EI 2076-3921
J9 ANTIOXIDANTS-BASEL
JI Antioxidants
PD DEC
PY 2018
VL 7
IS 12
AR 186
DI 10.3390/antiox7120186
PG 21
WC Biochemistry & Molecular Biology; Chemistry, Medicinal; Food Science &
   Technology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Pharmacology & Pharmacy; Food Science
   & Technology
GA HG1JF
UT WOS:000454709200017
PM 30544804
OA gold, Green Published, Green Submitted
DA 2025-04-10
ER

PT J
AU Hong, SE
   Nho, KJ
   Song, HK
   Kim, DH
AF Hong, Seong-Eui
   Nho, Kyoung Jin
   Song, Hong Ki
   Kim, Do Han
TI Deep sequencing-generated modules demonstrate coherent expression
   patterns for various cardiac diseases
SO GENE
LA English
DT Article
DE Heart-enriched gene; Gene module; Next-generation sequencing; Cardiac
   function
ID SERUM RESPONSE FACTOR; TISSUE-SPECIFIC GENES; MOUSE HEART; TBX20;
   DATABASE; PHOSPHORYLATION; DIFFERENTIATION; IDENTIFICATION; REPRESSION;
   EVOLUTION
AB As sequencing technology rapidly develops, gene annotations have also become increasingly sophisticated with incorporation of information regarding the temporal-spatial context of alternative splicing patterns, developmental stages, and tissue specificity. The present study aimed to identify the heart-enriched genes based on next-generation sequencing data and to investigate the gene modules demonstrating coherent expression patterns for various cardiac disease-related perturbations. Seven gene modules, including 382 heart-enriched genes, were identified. At least two modules containing differentially expressed genes were experimentally confirmed to be highly sensitive to various cardiac diseases. Transcription factors regulating the gene modules were then analyzed based on knowledgebase information; the expression of eight transcription factors changed significantly during pressure-overload cardiac hypertrophy, suggesting possible regulation of the modules by the identified transcription factors. Collectively, our results contribute to the classification of heart-enriched genes and their modules and would aid in identification of the transcription factors involved in cardiac pathogenesis in the future. (C) 2015 Elsevier B.V. All rights reserved.
C1 [Kim, Do Han] Gwangju Inst Sci & Technol, Coll Life Sci, Gwangju 500712, South Korea.
   Gwangju Inst Sci & Technol, Syst Biol Res Ctr, Gwangju 500712, South Korea.
C3 Gwangju Institute of Science & Technology (GIST); Gwangju Institute of
   Science & Technology (GIST)
RP Kim, DH (corresponding author), Gwangju Inst Sci & Technol, Coll Life Sci, 123 Cheomdangwagi Ro, Gwangju 500712, South Korea.
OI Nho, Kyoung Jin/0000-0003-4478-4647
FU GIST Systems Biology Infrastructure Establishment Grant; NRF grant -
   Korean Ministry of Science, ICT & Future Planning [NRF-2013M3A9A7046297]
FX This work was supported by the 2015 GIST Systems Biology Infrastructure
   Establishment Grant and the NRF grant funded by the Korean Ministry of
   Science, ICT & Future Planning (NRF-2013M3A9A7046297). We thank Mrs. Eun
   Hee Park for technical involvement in preparing the animal models.
CR Anders S, 2013, NAT PROTOC, V8, P1765, DOI 10.1038/nprot.2013.099
   Ashcroft M, 1999, MOL CELL BIOL, V19, P1751
   Balza RO, 2006, J BIOL CHEM, V281, P6498, DOI 10.1074/jbc.M509487200
   Barshir R, 2013, NUCLEIC ACIDS RES, V41, pD841, DOI 10.1093/nar/gks1198
   Brawand D, 2011, NATURE, V478, P343, DOI 10.1038/nature10532
   Burns KA, 2007, BBA-MOL CELL BIOL L, V1771, P952, DOI 10.1016/j.bbalip.2007.04.018
   Cai CL, 2005, DEVELOPMENT, V132, P2475, DOI 10.1242/dev.01832
   Chen G, 2013, HUM GENET, V132, P899, DOI 10.1007/s00439-013-1300-9
   Chen HY, 1998, J BIOL CHEM, V273, P13165, DOI 10.1074/jbc.273.21.13165
   Cotney J, 2012, GENOME RES, V22, P1069, DOI 10.1101/gr.129817.111
   DeLaughter DM, 2013, J MOL CELL CARDIOL, V59, P196, DOI 10.1016/j.yjmcc.2013.03.016
   Delgado-Olguín P, 2012, NAT GENET, V44, P343, DOI 10.1038/ng.1068
   Derrien T, 2012, GENOME RES, V22, P1775, DOI 10.1101/gr.132159.111
   Flynn JM, 2013, AGING CELL, V12, P851, DOI 10.1111/acel.12109
   Hong SE, 2006, BIOINFORMATICS, V22, P2053, DOI 10.1093/bioinformatics/btl331
   Hong SE, 2014, BMC GENOMICS, V15, DOI 10.1186/1471-2164-15-592
   Hou XJ, 2012, BMC GENOMICS, V13, DOI 10.1186/1471-2164-13-495
   Howald C, 2012, GENOME RES, V22, P1698, DOI 10.1101/gr.134478.111
   Hünten S, 2013, ADV EXP MED BIOL, V774, P77, DOI 10.1007/978-94-007-5590-1_5
   Johnson DS, 2005, GENOME RES, V15, P1315, DOI 10.1101/gr.4062605
   Karamboulas Christina, 2006, J Cell Sci, V119, P4315, DOI 10.1242/jcs.03186
   Kim D, 2013, GENOME BIOL, V14, DOI 10.1186/gb-2013-14-4-r36
   Kim SY, 2005, BMC BIOINFORMATICS, V6, DOI 10.1186/1471-2105-6-144
   Le MTN, 2009, GENE DEV, V23, P862, DOI 10.1101/gad.1767609
   Lee JH, 2011, CIRC RES, V109, P1332, DOI 10.1161/CIRCRESAHA.111.249433
   Li H, 2009, BIOINFORMATICS, V25, P1754, DOI [10.1093/bioinformatics/btp698, 10.1093/bioinformatics/btp324, 10.1093/bioinformatics/btp352]
   Liu ZQ, 2005, MOL CELL BIOL, V25, P2819, DOI 10.1128/MCB.25.7.2819-2831.2005
   Mitchell S, 2006, PHYSIOL GENOMICS, V25, P50, DOI 10.1152/physiolgenomics.00224.2005
   Murray AJ, 2007, CURR OPIN CLIN NUTR, V10, P704, DOI 10.1097/MCO.0b013e3282f0ecbe
   Pruitt KD, 2014, NUCLEIC ACIDS RES, V42, pD756, DOI 10.1093/nar/gkt1114
   Qian J, 2005, NUCLEIC ACIDS RES, V33, P3479, DOI 10.1093/nar/gki658
   Qian L, 2008, P NATL ACAD SCI USA, V105, P19833, DOI 10.1073/pnas.0808705105
   Sakabe NJ, 2012, HUM MOL GENET, V21, P2194, DOI 10.1093/hmg/dds034
   Searcy RD, 1998, DEVELOPMENT, V125, P4461
   Sharan R, 2003, BIOINFORMATICS, V19, P1787, DOI 10.1093/bioinformatics/btg232
   Sharan R, 2000, Proc Int Conf Intell Syst Mol Biol, V8, P307
   Singh MK, 2005, DEVELOPMENT, V132, P2697, DOI 10.1242/dev.01854
   Solovei I, 2013, CELL, V152, P584, DOI 10.1016/j.cell.2013.01.009
   Song HK, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0035552
   Song Y, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0064483
   Spencer JA, 1996, J BIOL CHEM, V271, P16535, DOI 10.1074/jbc.271.28.16535
   Stanley WC, 2000, CARDIOVASC RES, V45, P805, DOI 10.1016/S0008-6363(99)00419-8
   Stennard FA, 2005, DEVELOPMENT, V132, P2451, DOI 10.1242/dev.01799
   Sun GH, 2013, ENDOCRINOLOGY, V154, P4396, DOI 10.1210/en.2013-1432
   Takeuchi JK, 2005, DEVELOPMENT, V132, P2463, DOI 10.1242/dev.01827
   Tong JL, 2011, FEBS LETT, V585, P3560, DOI 10.1016/j.febslet.2011.10.021
   Ulitsky I, 2010, NAT PROTOC, V5, P303, DOI 10.1038/nprot.2009.230
   Wang ET, 2012, CELL, V150, P710, DOI 10.1016/j.cell.2012.06.041
   Werner T, 2010, BRIEF BIOINFORM, V11, P499, DOI 10.1093/bib/bbq018
   Xiao SJ, 2010, BIOINFORMATICS, V26, P1273, DOI 10.1093/bioinformatics/btq109
   Zhou J, 2011, P NATL ACAD SCI USA, V108, P10355, DOI 10.1073/pnas.1107052108
NR 51
TC 1
Z9 1
U1 0
U2 6
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 0378-1119
EI 1879-0038
J9 GENE
JI Gene
PD DEC 10
PY 2015
VL 574
IS 1
BP 53
EP 60
DI 10.1016/j.gene.2015.07.080
PG 8
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA CV4OR
UT WOS:000364246900008
PM 26232333
DA 2025-04-10
ER

PT J
AU Tan, XG
   Rotllant, J
   Li, HQ
   DeDeyne, P
   Du, SJ
AF Tan, XG
   Rotllant, J
   Li, HQ
   DeDeyne, P
   Du, SJ
TI SmyD1, a histone methyltransferase, is required for myofibril
   organization and muscle contraction in zebrafish embryos
SO PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF
   AMERICA
LA English
DT Article
DE skeletal muscle; sarcomere; myofiber maturation; cardiac muscle;
   transgenic fish
ID ZINC-FINGER PROTEINS; GENE-EXPRESSION; HP1 PROTEINS; HETEROCHROMATIN
   PROTEIN-1; TRANSCRIPTION REGULATION; LYSINE METHYLATION; POTENTIAL ROLE;
   MOUSE CD8B; CHROMATIN; BOP
AB Histone modification has emerged as a fundamental mechanism for control of gene expression and cell differentiation. Recent studies suggest that SmyD1, a novo SET domain-containing protein, may play a critical role in cardiac muscle differentiation. However, its role in skeletal muscle development and its mechanism of actions remains elusive. Here we report that SmyD1a and SmyD1b, generated by alternative splicing of SmyD1 gene, are histone methyltransferases that play a key role in skeletal and cardiac muscle contraction. SmyDla and SmyD1b are specifically expressed in skeletal and cardiac muscles of zebrafish embryos. Knockdown of SmyDla and SmyD1b expression by morpholino antisense oligos resulted in malfunction of skeletal and cardiac muscles. The SmyD1 morphant embryos (embryos injected with morpholino oligos) could not swim and had no heartbeat. Myofibrii organization in the morphant embryos was severely disrupted. The affected myofibers appeared as immature fibers with centrally located nuclei. Together, these data indicate that SmyD1a and SmyD1b are histone methyltransferases and play a critical role in myofibril organization during myofiber maturation.
C1 Univ Maryland, Ctr Marine Biotechnol, Inst Biotechnol, Baltimore, MD 21202 USA.
   Univ Maryland, Sch Med, Dept Phys Therapy & Rehabil Sci, Baltimore, MD 21201 USA.
C3 University System of Maryland; University of Maryland Baltimore;
   University System of Maryland; University of Maryland Baltimore
RP Univ Maryland, Ctr Marine Biotechnol, Inst Biotechnol, 701 E Pratt St, Baltimore, MD 21202 USA.
EM dus@umbi.umd.edu
RI ROTLLANT, JOSEP/K-1146-2014
OI du, Jim/0000-0001-9227-4153; Rotllant, Josep/0000-0001-5331-807X
FU NIGMS NIH HHS [R01GM58537, R01 GM058537] Funding Source: Medline
CR Bannister AJ, 2001, NATURE, V410, P120, DOI 10.1038/35065138
   Baxendale S, 2004, NAT GENET, V36, P88, DOI 10.1038/ng1280
   Blais A, 2005, GENE DEV, V19, P553, DOI 10.1101/gad.1281105
   Buckingham M, 2001, CURR OPIN GENET DEV, V11, P440, DOI 10.1016/S0959-437X(00)00215-X
   Caretti G, 2004, GENE DEV, V18, P2627, DOI 10.1101/gad.1241904
   CATELLI MG, 1985, EMBO J, V4, P3131, DOI 10.1002/j.1460-2075.1985.tb04055.x
   Cheng XD, 2005, ANNU REV BIOPH BIOM, V34, P267, DOI 10.1146/annurev.biophys.34.040204.144452
   Cirillo L, 2004, SCIENCE, V304, P1607, DOI 10.1126/science.1099577
   Du SJ, 2001, DEV DYNAM, V222, P655, DOI 10.1002/dvdy.1219
   Ekker SC, 2001, GENESIS, V30, P89, DOI 10.1002/gene.1038
   FELSENFELD AL, 1990, DEVELOPMENT, V108, P443
   Gottlieb PD, 2002, NAT GENET, V31, P25, DOI 10.1038/ng866
   Granato M, 1996, DEVELOPMENT, V123, P399
   Hamamoto R, 2004, NAT CELL BIOL, V6, P731, DOI 10.1038/ncb1151
   Hwang I, 1997, J IMMUNOL, V158, P1165
   HWANG I, 1995, IMMUNOGENETICS, V42, P353, DOI 10.1007/BF00179396
   Karachentsev D, 2005, GENE DEV, V19, P431, DOI 10.1101/gad.1263005
   Kubicek S, 2004, CELL, V119, P903, DOI 10.1016/j.cell.2004.12.006
   Lachner M, 2002, CURR OPIN CELL BIOL, V14, P286, DOI 10.1016/S0955-0674(02)00335-6
   Lachner M, 2001, NATURE, V410, P116, DOI 10.1038/35065132
   Lechner MS, 2000, MOL CELL BIOL, V20, P6449, DOI 10.1128/MCB.20.17.6449-6465.2000
   Lee H, 2004, SCIENCE, V304, P1675, DOI 10.1126/science.1098096
   Lele Z, 1999, DEV BIOL, V210, P56, DOI 10.1006/dbio.1999.9262
   McKinsey TA, 2002, CURR OPIN CELL BIOL, V14, P763, DOI 10.1016/S0955-0674(02)00389-7
   McKinsey TA, 2001, CURR OPIN GENET DEV, V11, P497, DOI 10.1016/S0959-437X(00)00224-0
   MIYATA Y, 1995, BIOCHEMISTRY-US, V34, P8123, DOI 10.1021/bi00025a019
   Munz B, 1999, J BIOL CHEM, V274, P13305, DOI 10.1074/jbc.274.19.13305
   Nielsen AL, 1999, EMBO J, V18, P6385, DOI 10.1093/emboj/18.22.6385
   Nielsen AL, 2001, MOL CELL, V7, P729, DOI 10.1016/S1097-2765(01)00218-0
   Nishioka K, 2002, MOL CELL, V9, P1201, DOI 10.1016/S1097-2765(02)00548-8
   Parker MH, 2003, NAT REV GENET, V4, P497, DOI 10.1038/nrg1109
   Phan D, 2005, DEVELOPMENT, V132, P2669, DOI 10.1242/dev.01849
   Pownall ME, 2002, ANNU REV CELL DEV BI, V18, P747, DOI 10.1146/annurev.cellbio.18.012502.105758
   PRATT WB, 1992, BIOESSAYS, V14, P841, DOI 10.1002/bies.950141209
   Rea S, 2000, NATURE, V406, P593, DOI 10.1038/35020506
   Rice JC, 2001, NATURE, V414, P258, DOI 10.1038/35104721
   Roy S, 2001, GENE DEV, V15, P1563, DOI 10.1101/gad.195801
   Rupp RAW, 2002, EUR J BIOCHEM, V269, P2294, DOI 10.1046/j.1432-1033.2002.02885.x
   Ryan RF, 1999, MOL CELL BIOL, V19, P4366
   Santos-Rosa H, 2002, NATURE, V419, P407, DOI 10.1038/nature01080
   Sass JB, 1996, MECH DEVELOP, V54, P195, DOI 10.1016/0925-4773(95)00476-9
   Sass JB, 1999, INT J DEV BIOL, V43, P835
   Sass JB, 1997, EXP CELL RES, V233, P391, DOI 10.1006/excr.1997.3572
   SHAKNOVICH R, 1992, MOL CELL BIOL, V12, P5059, DOI 10.1128/MCB.12.11.5059
   SHUE GL, 1994, J BIOL CHEM, V269, P2707
   Sims RJ, 2002, J BIOL CHEM, V277, P26524, DOI 10.1074/jbc.M204121200
   Sims RJ, 2004, NAT CELL BIOL, V6, P685, DOI 10.1038/ncb0804-685
   Strahl BD, 1999, P NATL ACAD SCI USA, V96, P14967, DOI 10.1073/pnas.96.26.14967
   van Holde K.E., 1988, Chromatin
   Yin YL, 2005, J BIOL CHEM, V280, P30025, DOI 10.1074/jbc.M501691200
   Yotov WV, 1996, GENE DEV, V10, P1763, DOI 10.1101/gad.10.14.1763
   Zhang CL, 2002, MOL CELL BIOL, V22, P7302, DOI 10.1128/MCB.22.20.7302-7312.2002
   Zhang Y, 2001, GENE DEV, V15, P2343, DOI 10.1101/gad.927301
NR 53
TC 176
Z9 217
U1 0
U2 17
PU NATL ACAD SCIENCES
PI WASHINGTON
PA 2101 CONSTITUTION AVE NW, WASHINGTON, DC 20418 USA
SN 0027-8424
J9 P NATL ACAD SCI USA
JI Proc. Natl. Acad. Sci. U. S. A.
PD FEB 21
PY 2006
VL 103
IS 8
BP 2713
EP 2718
DI 10.1073/pnas.0509503103
PG 6
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA 015MG
UT WOS:000235554900043
PM 16477022
OA Green Published
DA 2025-04-10
ER

PT J
AU Lartey, J
   Taggart, J
   Robson, S
   Taggart, M
AF Lartey, Jon
   Taggart, Julie
   Robson, Stephen
   Taggart, Michael
TI Altered Expression of Human Smooth Muscle Myosin Phosphatase Targeting
   (MYPT) Isovariants with Pregnancy and Labor
SO PLOS ONE
LA English
DT Article
ID LIGHT-CHAIN PHOSPHATASE; CONTRACTILE RESPONSE; HUMAN MYOMETRIUM;
   URINARY-BLADDER; SUBUNIT; ISOFORM; PHOSPHORYLATION; HYPERTENSION;
   SENSITIVITY; RELAXATION
AB Background
   Myosin light-chain phosphatase is a trimeric protein that hydrolyses phosphorylated myosin II light chains (MYLII) to cause relaxation in smooth muscle cells including those of the uterus. A major component of the phosphatase is the myosin targeting subunit (MYPT), which directs a catalytic subunit to dephosphorylate MYLII. There are 5 main MYPT family members (MYPT1 (PPP1R12A), MYPT2 (PPP1R12B), MYPT3 (PPP1R16A), myosin binding subunit 85 MBS85 (PPP1R12C) and TIMAP (TGF-beta-inhibited membrane-associated protein (PPP1R16B)). Nitric oxide (NO)-mediated smooth muscle relaxation has in part been attributed to activation of the phosphatase by PKG binding to a leucine zipper (LZ) dimerization domain located at the carboxyl-terminus of PPP1R12A. In animal studies, alternative splicing of PPP1R12A can lead to the inclusion of a 31-nucleotide exonic segment that generates a LZ negative (LZ-) isovariant rendering the phosphatase less sensitive to NO vasodilators and alterations in PPP1R12ALZ-and LZ+ expression have been linked to phenotypic changes in smooth muscle function. Moreover, PPP1R12B and PPP1R12C, but not PPP1R16A or PPP1R16B, have the potential for LZ+/LZ-alternative splicing. Yet, by comparison to animal studies, the information on human MYPT genomic sequences/mRNA expressions is scant. As uterine smooth muscle undergoes substantial remodeling during pregnancy we were interested in establishing the patterns of expression of human MYPT isovariants during this process and also following labor onset as this could have important implications for determining successful pregnancy outcome.
   Objectives
   We used cross-species genome alignment, to infer putative human sequences not available in the public domain, and isovariant-specific quantitative PCR, to analyse the expression of mRNA encoding putative LZ+ and LZ-forms of PPP1R12A, PPP1R12B and PPP1R12C as well as canonical PPP1R16A and PPP1R16B genes in human uterine smooth muscle from non-pregnant, pregnant and in-labor donors. Results We found a reduction in the expression of PPP1R12A, PPP1R12BLZ+, PPP1R16A and PPP1R16B mRNA in late pregnancy (not-in-labor) relative to non-pregnancy. PPP1R12ALZ+ and PPP1R12ALZ- mRNA levels were similar in the non-pregnant and pregnant not in labor groups. There was a further reduction in the uterine expression of PPP1R12ALZ+, PPP1R12CLZ+ and PPP1R12ALZ- mRNA with labor relative to the pregnant not-in-labor group. PPP1R12A, PPP1R12BLZ+, PPP1R16A and PPP1R16B mRNA levels were invariant between the not in labor and in-labor groups.
   Conclusions
   MYPT proteins are crucial determinants of smooth muscle function. Therefore, these alterations in human uterine smooth muscle MYPT isovariant expression during pregnancy and labor may be part of the important molecular physiological transition between uterine quiescence and activation.
C1 [Lartey, Jon; Robson, Stephen] Newcastle Univ, Sch Med, Inst Cellular Med, William Leech Bldg,Framlington Pl, Newcastle Upon Tyne NE2 4HH, Tyne & Wear, England.
   [Taggart, Julie; Taggart, Michael] Newcastle Univ, Inst Med Genet, Int Ctr Life, Newcastle Upon Tyne NE1 3BZ, Tyne & Wear, England.
C3 Newcastle University - UK; Newcastle University - UK
RP Lartey, J (corresponding author), Newcastle Univ, Sch Med, Inst Cellular Med, William Leech Bldg,Framlington Pl, Newcastle Upon Tyne NE2 4HH, Tyne & Wear, England.
EM jon.lartey@newcastle.ac.uk
RI Taggart, Michael/A-1288-2012
OI Robson, Stephen/0000-0001-7897-7987
FU National Institute for Health Research Academic Clinical Lecturership
   [NTH/040/601/A]; Academy of Medical Sciences/ Wellcome Trust Award
   (Starter Grant Clinical Lecturer Round2 Lartey)
FX This work was supported by external funder-National Institute for Health
   Research Academic Clinical Lecturership (NTH/040/601/A) Award to JL, and
   external funder-Academy of Medical Sciences/ Wellcome Trust Award
   (Starter Grant Clinical Lecturer Round2 Lartey) to JL. The funders had
   no role in study design, data collection and analysis, decision to
   publish, or preparation of the manuscript.
CR ALESSI D, 1992, EUR J BIOCHEM, V210, P1023, DOI 10.1111/j.1432-1033.1992.tb17508.x
   Arimura T, 2001, J BIOL CHEM, V276, P6073, DOI 10.1074/jbc.M008566200
   Borman MA FT, 2011, MOL CELL BIOCHEM, V327, P93
   Buxton ILO, 2004, MOL PHARMACOL, V65, P1051, DOI 10.1124/mol.65.5.1051
   CHEN YH, 1994, FEBS LETT, V356, P51, DOI 10.1016/0014-5793(94)01231-8
   Cheng JC, 2013, LAB INVEST, V93, P422, DOI 10.1038/labinvest.2013.40
   Dippold RP, 2014, AM J PHYSIOL-REG I, V307, pR256, DOI 10.1152/ajpregu.00145.2014
   Dirksen WP, 2000, AM J PHYSIOL-CELL PH, V278, pC589, DOI 10.1152/ajpcell.2000.278.3.C589
   Dordea AC, 2013, MOL HUM REPROD, V19, P727, DOI 10.1093/molehr/gat045
   Ekman M, 2005, J GEN PHYSIOL, V125, P187, DOI 10.1085/jgp.200409212
   Fisher SA, 2010, PHYSIOL GENOMICS, V42A, P169, DOI 10.1152/physiolgenomics.00111.2010
   Fujioka M, 1998, GENOMICS, V49, P59, DOI 10.1006/geno.1998.5222
   Gomez-Pinilla PJ, 2008, J PINEAL RES, V44, P416, DOI 10.1111/j.1600-079X.2007.00544.x
   Hudson CA, 2012, MOL HUM REPROD, V18, P265, DOI 10.1093/molehr/gar078
   Khatri JJ, 2001, J BIOL CHEM, V276, P37250, DOI 10.1074/jbc.M105275200
   KITAZAWA T, 1989, J BIOL CHEM, V264, P5339
   Lartey J, 2006, BIOL REPROD, V75, P452, DOI 10.1095/biolreprod.105.049130
   Lee MR, 1997, J BIOL CHEM, V272, P5063, DOI 10.1074/jbc.272.8.5063
   Lontay B, 2010, J BIOL CHEM, V285, P29357, DOI 10.1074/jbc.M110.143966
   Lu Y, 2008, AM J PHYSIOL-CELL PH, V294, pC564, DOI 10.1152/ajpcell.00285.2007
   Okamoto R, 2006, CELL SIGNAL, V18, P1408, DOI 10.1016/j.cellsig.2005.11.001
   Payne MC, 2006, J MOL CELL CARDIOL, V40, P274, DOI 10.1016/j.yjmcc.2005.07.009
   Payne MC, 2004, AM J PHYSIOL-HEART C, V286, pH1801, DOI 10.1152/ajpheart.00696.2003
   Surks HK, 1999, SCIENCE, V286, P1583, DOI 10.1126/science.286.5444.1583
   Trujillo M, 2001, J PHARMACOL EXP THER, V296, P841
   Wu XQ, 1996, BIOCHEM BIOPH RES CO, V220, P658, DOI 10.1006/bbrc.1996.0460
   Yong J, 2006, J BIOL CHEM, V281, P31202, DOI 10.1074/jbc.M607287200
   Zhang HY, 2007, CIRC RES, V100, P730, DOI 10.1161/01.RES.0000260189.38975.35
NR 28
TC 9
Z9 10
U1 0
U2 6
PU PUBLIC LIBRARY SCIENCE
PI SAN FRANCISCO
PA 1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA
SN 1932-6203
J9 PLOS ONE
JI PLoS One
PD OCT 31
PY 2016
VL 11
IS 10
AR e0164352
DI 10.1371/journal.pone.0164352
PG 16
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA EA6BX
UT WOS:000386711100008
PM 27798640
OA Green Published, Green Submitted, gold
DA 2025-04-10
ER

PT J
AU Zhang, LW
   Khattar, N
   Kemenes, I
   Kemenes, G
   Zrinyi, Z
   Pirger, Z
   Vertes, A
AF Zhang, Linwen
   Khattar, Nikkita
   Kemenes, Ildiko
   Kemenes, Gyorgy
   Zrinyi, Zita
   Pirger, Zsolt
   Vertes, Akos
TI Subcellular Peptide Localization in Single Identified Neurons by
   Capillary Microsampling Mass Spectrometry
SO SCIENTIFIC REPORTS
LA English
DT Article
ID CENTRAL-NERVOUS-SYSTEM; LYMNAEA-STAGNALIS; NEUROPEPTIDE-Y; FMRFAMIDE
   GENE; MALDI-MS; CELL; PROTEIN; RESOLUTION; EXPRESSION; NUCLEAR
AB Single cell mass spectrometry (MS) is uniquely positioned for the sequencing and identification of peptides in rare cells. Small peptides can take on different roles in subcellular compartments. Whereas some peptides serve as neurotransmitters in the cytoplasm, they can also function as transcription factors in the nucleus. Thus, there is a need to analyze the subcellular peptide compositions in identified single cells. Here, we apply capillary microsampling MS with ion mobility separation for the sequencing of peptides in single neurons of the mollusk Lymnaea stagnalis, and the analysis of peptide distributions between the cytoplasm and nucleus of identified single neurons that are known to express cardioactive Phe-Met-Arg-Phe amide-like (FMRFamide-like) neuropeptides. Nuclei and cytoplasm of Type 1 and Type 2 F group (Fgp) neurons were analyzed for neuropeptides cleaved from the protein precursors encoded by alternative splicing products of the FMRFamide gene. Relative abundances of nine neuropeptides were determined in the cytoplasm. The nuclei contained six of these peptides at different abundances. Enabled by its relative enrichment in Fgp neurons, a new 28-residue neuropeptide was sequenced by tandem MS.
C1 [Zhang, Linwen; Khattar, Nikkita; Vertes, Akos] George Washington Univ, Dept Chem, Washington, DC 20052 USA.
   [Kemenes, Ildiko; Kemenes, Gyorgy] Univ Sussex, Sch Life Sci, Sussex Neurosci, Brighton BN1 9QG, E Sussex, England.
   [Zrinyi, Zita; Pirger, Zsolt] MTA Ctr Ecol Res, Balaton Limnol Inst, Dept Expt Zool, H-8237 Tihany, Hungary.
C3 George Washington University; University of Sussex; HUN-REN; HUN-REN
   Centre for Ecological Research; HUN-REN Balaton Limnological Research
   Institute
RP Vertes, A (corresponding author), George Washington Univ, Dept Chem, Washington, DC 20052 USA.
EM vertes@gwu.edu
RI PIRGER, Zsolt/AAH-4045-2020; Kemenes, Ildiko/A-5339-2015; Zrinyi,
   Zita/HPH-1433-2023; Kemenes, George/L-4910-2019; Vertes,
   Akos/B-7159-2008
OI PIRGER, Zsolt/0000-0001-9039-6966; Kemenes, Ildiko/0000-0002-8722-8766;
   Vertes, Akos/0000-0001-5186-5352; Zhang, Linwen/0000-0002-5728-8813;
   Khattar, Nikkita/0000-0003-3484-2452; Kemenes,
   George/0000-0003-2004-8725
FU U.S. Army Research Office; Defense Advanced Research Projects Agency;
   Hungarian Brain Research Project [2017-1.2.1-NKP-2017-00002]; 
   [W911NF-14-2-0020]; BBSRC [BB/K018515/1, BB/P00766X/1] Funding Source:
   UKRI
FX Research was sponsored by the U.S. Army Research Office and the Defense
   Advanced Research Projects Agency and was accomplished under cooperative
   agreement number W911NF-14-2-0020. The views and conclusions contained
   in this document are those of the authors and should not be interpreted
   as representing the official policies, either expressed or implied, of
   the Army Research Office, DARPA, or the U.S. Government. The U.S.
   Government is authorized to reproduce and distribute reprints for
   Government purposes notwithstanding any copyright notation hereon. IHC
   experiments were supported by Hungarian Brain Research Project
   (2017-1.2.1-NKP-2017-00002). The authors thank John Young in the Tabin
   Lab at Harvard Medical School, Department of Genetics, for providing the
   initial cohort of experimental animals.
CR BENJAMIN PR, 1994, BIOESSAYS, V16, P335, DOI 10.1002/bies.950160508
   BENJAMIN PR, 1981, COMP BIOCHEM PHYS A, V70, P293, DOI 10.1016/0300-9629(81)90182-1
   Bergquist J, 2002, MASS SPECTROMETRY HY
   Bordeaux J, 2010, BIOTECHNIQUES, V48, P197, DOI 10.2144/000113382
   BRIGHT K, 1993, J NEUROSCI, V13, P2719, DOI 10.1523/JNEUROSCI.13-06-02719.1993
   Buchberger A, 2015, ANN REV ANAL CHEM, V8
   Burns TJ, 2017, CYTOM PART A, V91A, P180, DOI 10.1002/cyto.a.23054
   Chen RB, 2009, J AM SOC MASS SPECTR, V20, P708, DOI 10.1016/j.jasms.2008.12.007
   Chen WW, 2016, CELL, V166, P1324, DOI 10.1016/j.cell.2016.07.040
   Comi TJ, 2017, J AM CHEM SOC, V139, P3920, DOI 10.1021/jacs.6b12822
   COTTRELL GA, 1983, NATURE, V304, P638, DOI 10.1038/304638a0
   Cox B, 2006, NAT PROTOC, V1, P1872, DOI 10.1038/nprot.2006.273
   Date S, 2012, ANAL SCI, V28, P201, DOI 10.2116/analsci.28.201
   Diekmann Y, 2013, BIOCHEM J, V449, P319, DOI 10.1042/BJ20120957
   Duenas M. E, 2018, MAIZE METHODS PROTOC
   Ekman R, 2001, PEPTIDES, V22, P67, DOI 10.1016/S0196-9781(00)00357-0
   Fehr M, 2005, BIOCHEM SOC T, V33, P287, DOI 10.1042/BST0330287
   FERGUSON GP, 1991, J EXP BIOL, V158, P63
   Giesen C, 2014, NAT METHODS, V11, P417, DOI [10.1038/nmeth.2869, 10.1038/NMETH.2869]
   Glory E, 2007, DEV CELL, V12, P7, DOI 10.1016/j.devcel.2006.12.007
   Gohar AV, 2013, BIOMED OPT EXPRESS, V4, P1390, DOI 10.1364/BOE.4.001390
   Hobro AJ, 2017, VIB SPECTROSC, V91, P31, DOI 10.1016/j.vibspec.2016.10.012
   Horn PJ, 2011, J BIOL CHEM, V286, P3298, DOI 10.1074/jbc.M110.186353
   Hua JYY, 2004, NAT NEUROSCI, V7, P327, DOI 10.1038/nn1218
   Jacques D, 2003, CAN J PHYSIOL PHARM, V81, P288, DOI 10.1139/Y02-165
   Janes TA, 2015, EUR J NEUROSCI, V42, P1858, DOI 10.1111/ejn.12940
   KELLETT E, 1994, J NEUROSCI, V14, P6564
   Kiss T, 2014, PHYSIOL BEHAV, V131, P93, DOI 10.1016/j.physbeh.2014.04.026
   Korte AR, 2015, ANAL BIOANAL CHEM, V407, P2301, DOI 10.1007/s00216-015-8460-5
   KREINER T, 1986, J CELL BIOL, V102, P769, DOI 10.1083/jcb.102.3.769
   Lagercrantz H, 2001, ACTA PAEDIATR, V90, P707
   LINACRE A, 1990, J NEUROSCI, V10, P412
   Mao SP, 2016, FRONT NEUROANAT, V10, DOI 10.3389/fnana.2016.00054
   Martin W, 2010, PHILOS T R SOC B, V365, P847, DOI 10.1098/rstb.2009.0252
   Masujima T, 2009, ANAL SCI, V25, P953, DOI 10.2116/analsci.25.953
   MCCROHAN CR, 1980, J EXP BIOL, V85, P169
   Miao H, 2005, ANAL CHEM, V77, P7190, DOI 10.1021/ac0511694
   Mizuno H, 2008, J MASS SPECTROM, V43, P1692, DOI 10.1002/jms.1460
   Nassel DR, 1996, CURR OPIN NEUROBIOL, V6, P842, DOI 10.1016/S0959-4388(96)80036-5
   Passarelli MK, 2015, ANAL CHEM, V87, P6696, DOI 10.1021/acs.analchem.5b00842
   PEZZELLA F, 1990, AM J PATHOL, V137, P225
   Phelps MS, 2016, J AM SOC MASS SPECTR, V27, P187, DOI 10.1007/s13361-015-1232-9
   Qi M, 2018, ACS CHEM NEUROSCI, V9, P40, DOI 10.1021/acschemneuro.7b00304
   Ramamoorthy P, 2008, J NEUROSCI, V28, P13815, DOI 10.1523/JNEUROSCI.5361-07.2008
   Reits E, 2003, IMMUNITY, V18, P97, DOI 10.1016/S1074-7613(02)00511-3
   Rizk A, 2014, NAT PROTOC, V9, P586, DOI 10.1038/nprot.2014.037
   Rubakhin SS, 2003, ANAL CHEM, V75, P5374, DOI 10.1021/ac034498+
   Rubakhin SS, 2000, NAT BIOTECHNOL, V18, P172, DOI 10.1038/72622
   Ruotolo BT, 2008, NAT PROTOC, V3, P1139, DOI 10.1038/nprot.2008.78
   Santama N, 2000, MICROSC RES TECHNIQ, V49, P547, DOI 10.1002/1097-0029(20000615)49:6<547::AID-JEMT5>3.0.CO;2-Y
   SAUNDERS SE, 1992, J NEUROSCI, V12, P1033
   Stadler C, 2013, NAT METHODS, V10, P315, DOI [10.1038/NMETH.2377, 10.1038/nmeth.2377]
   Stolee JA, 2012, ANGEW CHEM INT EDIT, V51, P10386, DOI 10.1002/anie.201205436
   Strohalm M, 2008, RAPID COMMUN MASS SP, V22, P905, DOI 10.1002/rcm.3444
   Tian H, 2017, ANAL CHEM, V89, P5050, DOI 10.1021/acs.analchem.7b00466
   Xia JG, 2015, NUCLEIC ACIDS RES, V43, pW251, DOI 10.1093/nar/gkv380
   Zavalin A, 2012, J MASS SPECTROM, V47, P1473, DOI 10.1002/jms.3108
   Zenobi R, 2013, SCIENCE, V342, P1201, DOI 10.1126/science.1243259
   Zhang LW, 2018, ANGEW CHEM INT EDIT, V57, P4466, DOI 10.1002/anie.201709719
   Zhang LW, 2018, ANAL CHEM, V90, P4626, DOI 10.1021/acs.analchem.7b05126
   Zhang LW, 2015, ANAL CHEM, V87, P10397, DOI 10.1021/acs.analchem.5b02502
   Zhang LW, 2014, ANALYST, V139, P5079, DOI [10.1039/C4AN01018C, 10.1039/c4an01018c]
NR 62
TC 27
Z9 30
U1 0
U2 30
PU NATURE PORTFOLIO
PI BERLIN
PA HEIDELBERGER PLATZ 3, BERLIN, 14197, GERMANY
SN 2045-2322
J9 SCI REP-UK
JI Sci Rep
PD AUG 15
PY 2018
VL 8
AR 12227
DI 10.1038/s41598-018-29704-z
PG 10
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA GQ4GJ
UT WOS:000441627700001
PM 30111831
OA Green Accepted, Green Published, gold
DA 2025-04-10
ER

PT J
AU Meirhaeghe, A
   Fajas, L
   Gouilleux, F
   Cottel, D
   Helbecque, N
   Auwerx, J
   Amouyel, P
AF Meirhaeghe, A
   Fajas, L
   Gouilleux, F
   Cottel, D
   Helbecque, N
   Auwerx, J
   Amouyel, P
TI A functional polymorphism in a STAT5B site of the human
   PPARγ3 gene promoter affects height and lipid metabolism
   in a French population
SO ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY
LA English
DT Article
DE obesity; cholesterol; PPAR; growth hormone; STAT
ID ACTIVATED RECEPTOR-GAMMA; PPAR-GAMMA; ADIPOCYTE DIFFERENTIATION;
   OSTEOBLAST DIFFERENTIATION; SIGNAL TRANSDUCERS; TYROSINE KINASE;
   MESSENGER-RNA; DNA-BINDING; IN-VITRO; EXPRESSION
AB Objective-The peroxisome proliferator-activated receptor-gamma(PPARgamma) plays a role in adipocyte differentiation and insulin sensitization. It has been shown that genetic variation in the PPARgamma gene alters body weight control, lipid and insulin homeostasis, and the susceptibility to type 2 diabetes. Four PPARgamma isoforms are generated by alternative splicing and promoter usage. PPARgamma3 is only expressed in adipose tissue, colon, and macrophages and therefore seems to be a good candidate gene for metabolic and cardiovascular-associated diseases. In the present study, we looked for genetic variation in the PPARgamma3 promoter.
   Methods and Results-The proximal PPARgamma3 promoter was sequenced in 20 individuals. We detected a C/G polymorphism at position -681 from exon A2. Interestingly, it was located in a signal transducer and activator of transcription 5B (STAT5B) binding consensus site. In a French population (n=836), the -681G allele was associated with increased height and plasma low-density lipoprotein cholesterol concentrations. In vitro, we showed that the -681G allele completely abolished the binding of STAT5B to the cognate promoter element as well as the transactivation of the PPARgamma3 promoter by the growth hormone/STAT5B pathway.
   Conclusions-Our results suggest that PPARgamma3 may regulate the control of height and lipid homeostasis via the STAT5B pathway.
C1 Inst Pasteur, Serv Epidemiol & Sante Publ, INSERM, U508, F-59019 Lille, France.
   IGBMC, Illkirch Graffenstaden, France.
   CHU Amiens, Fac Med, Amiens, France.
   Ctr Hosp Reg & Univ Lille, F-59037 Lille, France.
C3 Pasteur Network; Universite de Lille; Institut Pasteur Lille; Institut
   National de la Sante et de la Recherche Medicale (Inserm); Institut
   National de la Sante et de la Recherche Medicale (Inserm); Universite de
   Picardie Jules Verne (UPJV); CHU Amiens; Universite de Lille; CHU Lille
RP Amouyel, P (corresponding author), Inst Pasteur, Serv Epidemiol & Sante Publ, INSERM, U508, 1 Rue Calmette,BP 245, F-59019 Lille, France.
RI Auwerx, Johan/ABE-9307-2021; Amouyel, Philippe/D-3662-2018; Coll,
   Lluis/C-8567-2014; Meirhaeghe, Aline/E-4663-2015
OI Meirhaeghe, Aline/0000-0001-6983-2364; Gouilleux,
   Fabrice/0000-0001-6047-1718; Auwerx, Johan/0000-0002-5065-5393; Fajas,
   Lluis/0000-0002-1283-9503; Amouyel, Philippe/0000-0001-9088-234X
CR Altshuler D, 2000, NAT GENET, V26, P76, DOI 10.1038/79216
   ARGETSINGER LS, 1993, CELL, V74, P237, DOI 10.1016/0092-8674(93)90415-M
   Barak Y, 1999, MOL CELL, V4, P585, DOI 10.1016/S1097-2765(00)80209-9
   Barroso I, 1999, NATURE, V402, P880, DOI 10.1038/47254
   Boucheron C, 1998, J BIOL CHEM, V273, P33936, DOI 10.1074/jbc.273.51.33936
   Chawla A, 2001, NAT MED, V7, P48, DOI 10.1038/83336
   Clarke SD, 1999, AM J CLIN NUTR, V70, P566
   DARNELL JE, 1994, SCIENCE, V264, P1415, DOI 10.1126/science.8197455
   Darnell JE, 1997, SCIENCE, V277, P1630, DOI 10.1126/science.277.5332.1630
   Day C, 1999, DIABETIC MED, V16, P179, DOI 10.1046/j.1464-5491.1999.00023.x
   Fajas L, 1998, FEBS LETT, V438, P55, DOI 10.1016/S0014-5793(98)01273-3
   Fajas L, 1997, J BIOL CHEM, V272, P18779, DOI 10.1074/jbc.272.30.18779
   Fajas L, 2001, J MOL ENDOCRINOL, V27, P1, DOI 10.1677/jme.0.0270001
   FORMAN BM, 1995, CELL, V83, P803, DOI 10.1016/0092-8674(95)90193-0
   Harp JB, 2001, BIOCHEM BIOPH RES CO, V281, P907, DOI 10.1006/bbrc.2001.4460
   Hogan JC, 2001, BIOCHEM BIOPH RES CO, V287, P484, DOI 10.1006/bbrc.2001.5606
   Ihle JN, 1996, CELL, V84, P331, DOI 10.1016/S0092-8674(00)81277-5
   Jackson SM, 2000, FEBS LETT, V471, P119, DOI 10.1016/S0014-5793(00)01372-7
   Kitamura S, 1999, JPN J CANCER RES, V90, P75, DOI 10.1111/j.1349-7006.1999.tb00668.x
   Kliewer SA, 1997, P NATL ACAD SCI USA, V94, P4318, DOI 10.1073/pnas.94.9.4318
   KLIEWER SA, 1995, CELL, V83, P813, DOI 10.1016/0092-8674(95)90194-9
   Kliewer SA, 1999, SCIENCE, V284, P757, DOI 10.1126/science.284.5415.757
   Lecka-Czernik B, 2002, ENDOCRINOLOGY, V143, P2376, DOI 10.1210/en.143.6.2376
   Lecka-Czernik B, 1999, J CELL BIOCHEM, V74, P357, DOI 10.1002/(SICI)1097-4644(19990901)74:3<357::AID-JCB5>3.0.CO;2-7
   LEHMANN JM, 1995, J BIOL CHEM, V270, P12953, DOI 10.1074/jbc.270.22.12953
   LIU XW, 1995, P NATL ACAD SCI USA, V92, P8831, DOI 10.1073/pnas.92.19.8831
   Mbalaviele G, 2000, J BIOL CHEM, V275, P14388, DOI 10.1074/jbc.275.19.14388
   Meirhaeghe A, 1998, HUM MOL GENET, V7, P435, DOI 10.1093/hmg/7.3.435
   Moriggl R, 1996, MOL CELL BIOL, V16, P5691
   Mueller E, 1998, MOL CELL, V1, P465, DOI 10.1016/S1097-2765(00)80047-7
   Nanbu-Wakao R, 2000, MOL ENDOCRINOL, V14, P307, DOI 10.1210/me.14.2.307
   Ogawa S, 1999, BIOCHEM BIOPH RES CO, V260, P122, DOI 10.1006/bbrc.1999.0896
   Okazaki R, 1999, ENDOCRINOLOGY, V140, P5060, DOI 10.1210/en.140.11.5060
   Ricote M, 1998, P NATL ACAD SCI USA, V95, P7614, DOI 10.1073/pnas.95.13.7614
   Ricote M, 1998, NATURE, V391, P79, DOI 10.1038/34178
   Ristow M, 1998, NEW ENGL J MED, V339, P953, DOI 10.1056/NEJM199810013391403
   Rosen ED, 1999, MOL CELL, V4, P611, DOI 10.1016/S1097-2765(00)80211-7
   Spiegelman BM, 1996, CELL, V87, P377, DOI 10.1016/S0092-8674(00)81359-8
   Stephens JM, 1999, BIOCHEM BIOPH RES CO, V262, P216, DOI 10.1006/bbrc.1999.0889
   Stephens JM, 1996, J BIOL CHEM, V271, P10441, DOI 10.1074/jbc.271.18.10441
   STRED SE, 1992, ENDOCRINOLOGY, V130, P1626, DOI 10.1210/en.130.3.1626
   Sundvold H, 2001, BIOCHEM BIOPH RES CO, V287, P383, DOI 10.1006/bbrc.2001.5602
   Teglund S, 1998, CELL, V93, P841, DOI 10.1016/S0092-8674(00)81444-0
   TONTONOZ P, 1994, GENE DEV, V8, P1224, DOI 10.1101/gad.8.10.1224
   Udy GB, 1997, P NATL ACAD SCI USA, V94, P7239, DOI 10.1073/pnas.94.14.7239
NR 45
TC 82
Z9 94
U1 0
U2 3
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA 530 WALNUT ST, PHILADELPHIA, PA 19106-3621 USA
SN 1079-5642
J9 ARTERIOSCL THROM VAS
JI Arterioscler. Thromb. Vasc. Biol.
PD FEB
PY 2003
VL 23
IS 2
BP 289
EP 294
DI 10.1161/01.ATV.0000051382.28752.FE
PG 6
WC Hematology; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Hematology; Cardiovascular System & Cardiology
GA 648TD
UT WOS:000181165900024
PM 12588773
OA Bronze, Green Published
DA 2025-04-10
ER

PT J
AU Wen, XD
   Wang, JH
   Wang, Q
   Liu, PL
   Zhao, HM
AF Wen, Xiaodong
   Wang, Junhu
   Wang, Qiong
   Liu, Peilong
   Zhao, Hongmou
TI Interaction between N6-methyladenosine and autophagy in the regulation
   of bone and tissue degeneration
SO FRONTIERS IN BIOENGINEERING AND BIOTECHNOLOGY
LA English
DT Review
DE degenerative; disease; M6A; autophagy; mRNA; osteoporosis
AB Bone and tissue degeneration are the most common skeletal disorders that seriously affect people's quality of life. N6-methyladenosine (m6A) is one of the most common RNA modifications in eukaryotic cells, affecting the alternative splicing, translation, stability and degradation of mRNA. Interestingly, increasing number of evidences have indicated that m6A modification could modulate the expression of autophagy-related (ATG) genes and promote autophagy in the cells. Autophagy is an important process regulating intracellular turnover and is evolutionarily conserved in eukaryotes. Abnormal autophagy results in a variety of diseases, including cardiomyopathy, degenerative disorders, and inflammation. Thus, the interaction between m6A modification and autophagy plays a prominent role in the onset and progression of bone and tissue degeneration. In this review, we summarize the current knowledge related to the effect of m6A modification on autophagy, and introduce the role of the crosstalk between m6A modification and autophagy in bone and tissue degeneration. An in-depth knowledge of the above crosstalk may help to improve our understanding of their effects on bone and tissue degeneration and provide novel insights for the future therapeutics.
C1 [Wen, Xiaodong; Wang, Junhu; Wang, Qiong; Liu, Peilong; Zhao, Hongmou] Xi An Jiao Tong Univ, Dept Foot & Ankle Surg, Honghui Hosp, Xian, Peoples R China.
C3 Xi'an Jiaotong University
RP Zhao, HM (corresponding author), Xi An Jiao Tong Univ, Dept Foot & Ankle Surg, Honghui Hosp, Xian, Peoples R China.
EM zhaohongmou@xiyi.edu.cn
FU Key R & D plan of Shaanxi Province; Free exploration project of Xi'an
   Jiaotong University [2021SF-025, xzy012022130];  [2022SF-532]
FX HZ, Key R & D plan of Shaanxi Province (No. 2021SF-025), Free
   exploration project of Xi'an Jiaotong University (No. xzy012022130); XW,
   Key R & D plan of Shaanxi Province (No. 2022SF-532)
CR Affortit C, 2022, SCI SIGNAL, V15, DOI 10.1126/scisignal.abj4583
   Arumugam P, 2021, AM J CANCER RES, V11, P3688
   Chen LS, 2022, ACTA PHARMACOL SIN, V43, P1311, DOI 10.1038/s41401-021-00756-8
   Chen PB, 2022, OXID MED CELL LONGEV, V2022, DOI 10.1155/2022/4036274
   Chen XC, 2021, CELL BIOSCI, V11, DOI 10.1186/s13578-021-00661-x
   Chen YB, 2021, AUTOPHAGY, V17, P457, DOI 10.1080/15548627.2020.1720431
   Chen Y, 2022, FRONT IMMUNOL, V13, DOI 10.3389/fimmu.2022.897487
   Dai YZ, 2022, CELL MOL BIOL LETT, V27, DOI 10.1186/s11658-022-00342-8
   Deretic V, 2022, J CELL BIOL, V221, DOI 10.1083/jcb.202203083
   Du AS, 2022, MOL CANCER, V21, DOI 10.1186/s12943-022-01575-z
   Grenov A, 2022, CELL REP, V39, DOI 10.1016/j.celrep.2022.110778
   Han L, 2022, FRONT MOL BIOSCI, V8, DOI 10.3389/fmolb.2021.780089
   He Y, 2022, BONE, V154, DOI 10.1016/j.bone.2021.116182
   Huang CS, 2022, CLIN TRANSL MED, V12, DOI 10.1002/ctm2.848
   Li GC, 2022, CLIN TRANSL MED, V12, DOI 10.1002/ctm2.765
   Li GC, 2022, NAT COMMUN, V13, DOI 10.1038/s41467-022-28990-6
   Li GC, 2020, CELL DEATH DIS, V11, DOI 10.1038/s41419-020-2284-8
   Li HF, 2022, INT J BIOL SCI, V18, P3223, DOI 10.7150/ijbs.70335
   Li Q, 2021, SIGNAL TRANSDUCT TAR, V6, DOI 10.1038/s41392-020-00453-8
   Li S., 2022, CEREB CORTEX
   Li ZJ, 2017, CANCER CELL, V31, P127, DOI 10.1016/j.ccell.2016.11.017
   Lin RR, 2020, ONCOGENE, V39, P4983, DOI 10.1038/s41388-020-1349-6
   Lin ZY, 2020, EMBO J, V39, DOI 10.15252/embj.2019103181
   Liu JZ, 2014, NAT CHEM BIOL, V10, P93, DOI 10.1038/nchembio.1432
   Liu J, 2022, J CELL MOL MED, V26, P2505, DOI 10.1111/jcmm.16845
   Mi BB, 2020, MOL THER-NUCL ACIDS, V21, P814, DOI 10.1016/j.omtn.2020.07.023
   Mi BB, 2020, J CELL MOL MED, V24, P6385, DOI 10.1111/jcmm.15284
   Oerum S, 2021, NUCLEIC ACIDS RES, V49, P7239, DOI 10.1093/nar/gkab378
   Pan HL, 2021, BMC CANCER, V21, DOI 10.1186/s12885-021-08961-8
   Peng J, 2022, CELL TISSUE RES, V388, P301, DOI 10.1007/s00441-022-03588-y
   Qi S, 2022, ELIFE, V11, DOI [10.7554/eLife.67150, 10.7554/eLife.67150.sa0, 10.7554/eLife.67150.sa1, 10.7554/eLife.67150.sa2]
   Ren JD, 2022, CELL DEATH DISCOV, V8, DOI 10.1038/s41420-022-00890-0
   Ruszkowska A, 2021, INT J MOL SCI, V22, DOI 10.3390/ijms22042176
   Shen DD, 2022, ACTA PHARM SIN B, V12, P2193, DOI 10.1016/j.apsb.2022.01.003
   Shen M, 2022, FREE RADICAL BIO MED, V182, P246, DOI 10.1016/j.freeradbiomed.2022.02.028
   Shen WW, 2022, RNA BIOL, V19, P751, DOI 10.1080/15476286.2022.2079889
   Sun S, 2022, CELL BIOSCI, V12, DOI 10.1186/s13578-022-00788-5
   Tang FJ, 2022, FRONT CELL DEV BIOL, V10, DOI 10.3389/fcell.2022.817112
   Wang J, 2021, AGING-US, V13, P21134, DOI 10.18632/aging.203377
   Wang X, 2016, NATURE, V534, P575, DOI 10.1038/nature18298
   Wang XX, 2020, AUTOPHAGY, V16, P1221, DOI 10.1080/15548627.2019.1659617
   Wang ZW, 2022, CELL REP, V39, DOI 10.1016/j.celrep.2022.110813
   Wilkinson E, 2022, FRONT CELL DEV BIOL, V10, DOI 10.3389/fcell.2022.828683
   Wu XB, 2021, AM J TRANSL RES, V13, P11209
   Xiong Y, 2019, MOL THER-NUCL ACIDS, V17, P223, DOI 10.1016/j.omtn.2019.06.001
   Xiong Y, 2019, MED SCI MONITOR, V25, P2246, DOI 10.12659/MSM.915451
   Xu P, 2022, CANCER CELL INT, V22, DOI 10.1186/s12935-021-02368-y
   Yan RC, 2022, CANCER LETT, V534, DOI 10.1016/j.canlet.2022.215615
   Yang ZC, 2022, EBIOMEDICINE, V80, DOI 10.1016/j.ebiom.2022.104019
   Yao JY, 2018, AUTOPHAGY, V14, P1226, DOI 10.1080/15548627.2018.1463121
   Yao YJ, 2022, BIOCHEM PHARMACOL, V202, DOI 10.1016/j.bcp.2022.115139
   Yu Dan, 2021, Nucleic Acids Res, V49, P11629, DOI 10.1093/nar/gkab460
   Yu T, 2020, AGING-US, V12, P10359, DOI 10.18632/aging.103262
   Yu TT, 2022, INT J BIOL SCI, V18, P2235, DOI 10.7150/ijbs.64943
   Zhang L, 2022, CELL ONCOL, V45, P355, DOI 10.1007/s13402-022-00666-9
   Zhang N, 2022, MOL NEUROBIOL, V59, P1925, DOI 10.1007/s12035-022-02739-0
   Zhang W, 2023, BIOACT MATER, V19, P429, DOI 10.1016/j.bioactmat.2022.04.017
   Zhang ZH, 2022, AUTOPHAGY, V18, P1483, DOI 10.1080/15548627.2022.2083305
   Zheng QQ, 2021, THERANOSTICS, V11, P147, DOI 10.7150/thno.47723
   Zheng Y, 2022, CELL MOL LIFE SCI, V79, DOI 10.1007/s00018-022-04331-0
   Zhong H, 2022, OSTEOARTHR CARTILAGE, V30, P341, DOI 10.1016/j.joca.2021.11.005
NR 61
TC 1
Z9 1
U1 0
U2 13
PU FRONTIERS MEDIA SA
PI LAUSANNE
PA AVENUE DU TRIBUNAL FEDERAL 34, LAUSANNE, CH-1015, SWITZERLAND
SN 2296-4185
J9 FRONT BIOENG BIOTECH
JI Front. Bioeng. Biotechnol.
PD AUG 22
PY 2022
VL 10
AR 978283
DI 10.3389/fbioe.2022.978283
PG 8
WC Biotechnology & Applied Microbiology; Engineering, Biomedical
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biotechnology & Applied Microbiology; Engineering
GA 5Q6ZH
UT WOS:000873976500001
PM 36072293
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Wang, HV
   Moser, M
AF Wang, Hao-Ven
   Moser, Markus
TI Comparative Expression Analysis of the Murine Palladin Isoforms
SO DEVELOPMENTAL DYNAMICS
LA English
DT Article
DE palladin; actin cytoskeleton; Z-disc; muscle development
ID GIRDLE MUSCULAR-DYSTROPHY; BINDING PARTNER; ACTIN CYTOSKELETON;
   SARCOMERIC PROTEIN; ALPHA-ACTININ; CELL; MYOTILIN; DOMAINS; KINASE;
   FAMILY
AB Palladin fulfils a crucial function as a molecular scaffold in organizing and stabilizing the actin cytoskeleton. At least four major palladin isoforms exist due to different promoter usage and alternative splicing: a 200-kDa isoform, a 140-kDa isoform, and two isoforms with a size of 90-92 kDa. Here, we describe their expression during mouse development and in adult tissues. The 200-kDa isoform is predominantly expressed in developing heart and skeletal muscle. The 140-kDa isoform is expressed in various mesenchymal tissues, and also represents the major isoform of the brain. The 90-92-kDa isoforms are almost ubiquitously expressed with the highest levels in smooth muscle-rich tissues. Immunohistochemical and immunofluorecence staining with an anti-200-kDa isoform-specific antiserum localizes the large isoform to the Z-discs of cardiac and skeletal muscle cells. Interestingly, the expression of this isoform is initiated and increasing during in vitro differentiation and fusion of C2C12 myoblasts, suggesting that the 200-kDa palladin isoform may play a scaffolding role during sarcomeric organization. Developmental Dynamics 237:3342-3351, 2008. (C) 2008 Wiley-Liss, Inc.
C1 [Wang, Hao-Ven; Moser, Markus] Max Planck Inst Biochem, Dept Mol Med, D-82152 Martinsried, Germany.
C3 Max Planck Society
RP Moser, M (corresponding author), Max Planck Inst Biochem, Dept Mol Med, Klopferspitz 18, D-82152 Martinsried, Germany.
EM moser@biochem.mpg.de
OI Wang, Hao-Ven/0000-0001-7523-087X
CR Bang ML, 2001, J CELL BIOL, V153, P413, DOI 10.1083/jcb.153.2.413
   Boukhelifa M, 2006, FEBS J, V273, P26, DOI 10.1111/j.1742-4658.2005.05036.x
   Boukhelifa M, 2004, CELL MOTIL CYTOSKEL, V58, P17, DOI 10.1002/cm.10173
   Dixon RDS, 2008, J BIOL CHEM, V283, P6222, DOI 10.1074/jbc.M707694200
   Goicoechea S, 2006, J CELL SCI, V119, P3316, DOI 10.1242/jcs.03076
   Hauser MA, 2000, HUM MOL GENET, V9, P2141, DOI 10.1093/hmg/9.14.2141
   Jin L, 2007, CIRC RES, V100, P817, DOI 10.1161/01.RES.0000261351.54147.de
   Liu XS, 2007, J CELL BIOCHEM, V100, P1288, DOI 10.1002/jcb.21126
   Luo HJ, 2005, MOL CELL NEUROSCI, V29, P507, DOI 10.1016/j.mcn.2004.12.002
   MOSER M, 1995, DEVELOPMENT, V121, P2779
   Mykkänen OM, 2001, MOL BIOL CELL, V12, P3060, DOI 10.1091/mbc.12.10.3060
   Otey CA, 2005, INT REV CYTOL, V246, P31, DOI 10.1016/S0074-7696(05)46002-7
   Parast MM, 2000, J CELL BIOL, V150, P643, DOI 10.1083/jcb.150.3.643
   Rachlin AS, 2006, J CELL SCI, V119, P995, DOI 10.1242/jcs.02825
   RANDO TA, 1994, J CELL BIOL, V125, P1275, DOI 10.1083/jcb.125.6.1275
   Rönty M, 2005, EXP CELL RES, V310, P88, DOI 10.1016/j.yexcr.2005.06.026
   Rönty M, 2004, FEBS LETT, V566, P30, DOI 10.1061/j.febslet.2004.04.006
   Rönty M, 2007, EXP CELL RES, V313, P2575, DOI 10.1016/j.yexcr.2007.04.030
   Salmikangas P, 1999, HUM MOL GENET, V8, P1329, DOI 10.1093/hmg/8.7.1329
   Selcen D, 2004, NEUROLOGY, V62, P1363, DOI 10.1212/01.WNL.0000123576.74801.75
   Wilkinson DG, 1993, SITU HYBRIDIZATION P, P75
NR 21
TC 27
Z9 29
U1 0
U2 2
PU WILEY-LISS
PI HOBOKEN
PA DIV JOHN WILEY & SONS INC, 111 RIVER ST, HOBOKEN, NJ 07030 USA
SN 1058-8388
J9 DEV DYNAM
JI Dev. Dyn.
PD NOV
PY 2008
VL 237
IS 11
BP 3342
EP 3351
DI 10.1002/dvdy.21755
PG 10
WC Anatomy & Morphology; Developmental Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Anatomy & Morphology; Developmental Biology
GA 372VP
UT WOS:000260930400024
PM 18924229
OA Bronze
DA 2025-04-10
ER

PT J
AU Horie, M
   Kobayashi, K
   Takeda, S
   Nakamura, Y
   Lyons, GE
   Toda, T
AF Horie, M
   Kobayashi, K
   Takeda, S
   Nakamura, Y
   Lyons, GE
   Toda, T
TI Isolation and characterization of the mouse ortholog of the
   fukuyama-type congenital muscular dystrophy gene
SO GENOMICS
LA English
DT Article
DE fukuyama-type congenital muscular dystrophy; FCMD; fukutin; mouse; cDNA;
   neuronal migration; brain development; alternative splicing
ID ALPHA-DYSTROGLYCAN; LINKAGE-DISEQUILIBRIUM; GLIA LIMITANS; FCMD;
   GLYCOSYLATION; DEFICIENCY; FETUS
AB Fukuyama-type congenital muscular dystrophy (FCMD) is a severe autosomal-recessive muscular dystrophy accompanied by brain malformation. Previously, we identified the gene responsible for FCMD through positional cloning. Here we report the isolation of its murine ortholog, Fcmd. The predicted amino acid sequence of murine fukutin protein encoded by Fcmd is 90% identical to that of its human counterpart. Radiation hybrid mapping localized the gene to 2.02 cR telomeric to D4Mit272 on chromosome 4. Northern blot analysis revealed ubiquitous expression of Fcmd in adult mouse tissues. Through in situ hybridization, we observed a wide distribution of Fcmd expression throughout embryonic development, most predominantly in the central and peripheral nervous systems. We also detected high Fcmd expression in the ventricular zone of proliferating neurons at 13.5 days post-coitum. Brain malformation in FCMD patients is thought to result from defective neuronal migration. Our data suggest that neuronally expressed Fcmd is likely to be important in the development of normal brain structure.
C1 Otsuka Pharmaceut Co Ltd, Otsuka GEN Res Inst, Tokushima 7710192, Japan.
   Osaka Univ, Grad Sch Med, Dept Post Genom & Dis, Div Funct Genom, Suita, Osaka 5650871, Japan.
   Univ Tokyo, Ctr Human Genome, Inst Med Sci, Mol Med Lab,Minato Ku, Tokyo 1088639, Japan.
   Univ Wisconsin, Sch Med, Dept Anat, Madison, WI 53706 USA.
C3 Otsuka Pharmaceutical; The University of Osaka; University of Tokyo;
   University of Wisconsin System; University of Wisconsin Madison
RP Toda, T (corresponding author), Otsuka Pharmaceut Co Ltd, Otsuka GEN Res Inst, 463-10 Kagasuno,Kawauchi Cho, Tokushima 7710192, Japan.
RI Kobayashi, Kazuhiro/AAH-8638-2021
OI Kobayashi, Kazuhiro/0000-0001-7801-147X
CR Aravind L, 1999, CURR BIOL, V9, pR836, DOI 10.1016/S0960-9822(00)80039-1
   Brockington M, 2001, AM J HUM GENET, V69, P1198, DOI 10.1086/324412
   FUKUYAMA Y, 1981, BRAIN DEV-JPN, V3, P1
   Grewal PK, 2001, NAT GENET, V28, P151, DOI 10.1038/88865
   Hayashi YK, 2001, NEUROLOGY, V57, P115, DOI 10.1212/WNL.57.1.115
   IZUMI T, 1995, BRAIN DEV-JPN, V17, P33, DOI 10.1016/0387-7604(94)00114-D
   Kobayashi K, 1998, NATURE, V394, P388, DOI 10.1038/28653
   LYONS GE, 1995, J NEUROSCI, V15, P5727, DOI 10.1523/jneurosci.15-08-05727.1995
   Nakano I, 1996, ACTA NEUROPATHOL, V91, P313, DOI 10.1007/s004010050431
   Saito Y, 1999, ACTA NEUROPATHOL, V98, P330, DOI 10.1007/s004010051089
   TAKADA K, 1987, ACTA NEUROPATHOL, V74, P300, DOI 10.1007/BF00688196
   TODA T, 1993, NAT GENET, V5, P283, DOI 10.1038/ng1193-283
   Toda T, 1996, AM J HUM GENET, V59, P1313
   TODA T, 1994, AM J HUM GENET, V55, P946
   Yamamoto T, 1997, BRAIN DEV-JPN, V19, P35, DOI 10.1016/S0387-7604(96)00056-3
   Yoshida A, 2001, DEV CELL, V1, P717, DOI 10.1016/S1534-5807(01)00070-3
NR 16
TC 8
Z9 9
U1 0
U2 1
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0888-7543
J9 GENOMICS
JI Genomics
PD NOV
PY 2002
VL 80
IS 5
BP 482
EP 486
DI 10.1006/geno.2002.6853
PG 5
WC Biotechnology & Applied Microbiology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biotechnology & Applied Microbiology; Genetics & Heredity
GA 611AM
UT WOS:000178994300006
PM 12408965
DA 2025-04-10
ER

PT J
AU Kashyap, M
   Sharma, A
   Bhavesh, NS
AF Kashyap, Maruthi
   Sharma, Ashwani
   Bhavesh, Neel Sarovar
TI Purification, crystallization and preliminary crystallographic studies
   of C-terminal RNA recognition motif (RRM-3) of human ELAV-type
   RNA-binding protein 3 (ETR-3)
SO ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
LA English
DT Article
ID MYOTONIC-DYSTROPHY; MESSENGER-RNA; FAMILY
AB Human embryonically lethal abnormal vision (ELAV)-type RNA-binding protein 3 (ETR-3) has been implicated in many aspects of RNA-processing events including alternative splicing, stability, editing and translation. RNA recognition motif 3 (RRM-3) is an independent C-terminal RNA-binding domain of ETR-3 that preferentially binds to UG-rich repeats of the nuclear or cytoplasmic pre-mRNA, and along with the other domains mediates the inclusion of cardiac troponin T (c-TNT) exon 5 in embryonic muscle, which is otherwise excluded in the adult. In the present study, RRM-3 was cloned, overexpressed, purified and crystallized by the hanging-drop vapour-diffusion method. The crystals diffracted to 3 angstrom resolution at the home source and belonged to space group P2(1)3, with unit-cell parameters a = b = c = 118.5 angstrom, alpha = beta = gamma = 90 degrees. There were two molecules of RRM-3 in the asymmetric unit and the calculated Matthews coefficient (V-M) was 6.35 angstrom(3) Da(-1), with a solvent content of 80.62%. Initial phases were determined by molecular replacement.
C1 [Kashyap, Maruthi; Sharma, Ashwani; Bhavesh, Neel Sarovar] ICGEB, Struct & Computat Biol Grp, New Delhi 110067, India.
C3 Department of Biotechnology (DBT) India; International Center for
   Genetic Engineering & Biotechnology (ICGEB); International Center for
   Genetic Engineering & Biotechnology (ICGEB), New Delhi
RP Bhavesh, NS (corresponding author), ICGEB, Struct & Computat Biol Grp, Aruna Asaf Ali Marg, New Delhi 110067, India.
EM neelsb@icgeb.res.in
RI ; Bhavesh, Neel Sarovar/F-3127-2015
OI Maruthi, Kashyap/0000-0001-5290-4413; Bhavesh, Neel
   Sarovar/0000-0002-7248-4978
FU Department of Science and Technology, Government of India under the SERC
   FAST Track Scheme [SR/FT/L-011/2009]; Indian Council for Medical
   Research (ICMR)
FX The work is funded by the Department of Science and Technology,
   Government of India under the SERC FAST Track Scheme No.
   SR/FT/L-011/2009. X-ray diffraction data were collected at the home
   source at ICGEB, New Delhi. We thank Dr Manickam Yogavel for the use of
   the X-ray diffraction facility and useful discussion. MK is the
   recipient of an Indian Council for Medical Research (ICMR) senior
   research fellowship.
CR Barreau C, 2006, BIOCHIMIE, V88, P515, DOI 10.1016/j.biochi.2005.10.011
   CAMPOS AR, 1985, J NEUROGENET, V2, P197, DOI 10.3109/01677068509100150
   Dasgupta T, 2012, WIRES RNA, V3, P104, DOI 10.1002/wrna.107
   Faustino NA, 2005, MOL CELL BIOL, V25, P879, DOI 10.1128/MCB.25.3.879-887.2005
   Handa N, 1999, NATURE, V398, P579, DOI 10.1038/19242
   JIMENEZ F, 1987, J NEUROGENET, V4, P179, DOI 10.3109/01677068709102340
   Ladd AN, 2001, MOL CELL BIOL, V21, P1285, DOI 10.1128/MCB.21.4.1285-1296.2001
   Mankodi A, 2002, MOL CELL, V10, P35, DOI 10.1016/S1097-2765(02)00563-4
   MATTHEWS BW, 1968, J MOL BIOL, V33, P491, DOI 10.1016/0022-2836(68)90205-2
   Modrek B, 2002, NAT GENET, V30, P13, DOI 10.1038/ng0102-13
   Otwinowski Z, 1997, METHOD ENZYMOL, V276, P307, DOI 10.1016/S0076-6879(97)76066-X
   Philips AV, 1998, SCIENCE, V280, P737, DOI 10.1126/science.280.5364.737
   Vagin A, 2010, ACTA CRYSTALLOGR D, V66, P22, DOI 10.1107/S0907444909042589
NR 13
TC 0
Z9 1
U1 0
U2 5
PU INT UNION CRYSTALLOGRAPHY
PI CHESTER
PA 2 ABBEY SQ, CHESTER, CH1 2HU, ENGLAND
EI 2053-230X
J9 ACTA CRYSTALLOGR F
JI Acta Crystallogr. F-Struct. Biol. Commun.
PD OCT
PY 2013
VL 69
BP 1107
EP 1109
DI 10.1107/S1744309113023439
PN 10
PG 3
WC Biochemical Research Methods; Biochemistry & Molecular Biology;
   Biophysics; Crystallography
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics; Crystallography
GA 231GD
UT WOS:000325402900009
PM 24100559
OA Green Published
DA 2025-04-10
ER

PT J
AU Toramoto, T
   Ikeda, D
   Ochiai, Y
   Minoshima, S
   Shimizu, N
   Watabe, S
AF Toramoto, T
   Ikeda, D
   Ochiai, Y
   Minoshima, S
   Shimizu, N
   Watabe, S
TI Multiple gene organization of pufferfish Fugu rubripes
   tropomyosin isoforms and tissue distribution of their transcripts
SO GENE
LA English
DT Article
DE alternative splicing; genome duplication; Fugu; TPM
ID ALPHA-TROPOMYOSIN; MESSENGER-RNA; NONMUSCLE TROPOMYOSIN; CARDIAC
   TROPOMYOSIN; ACTIN-BINDING; EVOLUTION; GENOME; MUSCLE; IDENTIFICATION;
   EXPRESSION
AB The Japanese pufferfish, torafugu (Fugu rubripes), has a haploid genome of about 400 Mb in size, which has been sequenced to approximately 90% coverage. Here we identified six Fugu tropomyosin (TPM) gene sequences by using the BLASTN program and the sequence of the white croaker TPM1 gene in our collection against the draft assembly of the Fugu genomic sequence database. TPM2, TPM3 and TPM4 genes were identified together with a set of two potentially duplicated genes of TPM1 (TPM1-1 and TPM1-2) as described in our previous report and TPM4 (TPM4-1 and TPM4-2) newly found in this study. The expression patterns of these Fugu TPM genes were determined by reverse transcription polymerase chain reaction (RT-PCR). A phylogenetic tree was constructed using the deduced amino acid sequences, which were encoded by the exons common to all vertebrate TPM genes. This indicated that the Fugu TPM1 and TPM4 genes had resulted from a gene duplication in the fish evolutionary lineage. (C) 2004 Elsevier B.V. All rights reserved.
C1 Univ Tokyo, Grad Sch Agr & Life Sci, Lab Aquat Mol Biol & Biotechnol, Tokyo 1138657, Japan.
   Keio Univ, Sch Med, Dept Mol Biol, Tokyo 1608582, Japan.
C3 University of Tokyo; Keio University
RP Univ Tokyo, Grad Sch Agr & Life Sci, Lab Aquat Mol Biol & Biotechnol, Tokyo 1138657, Japan.
EM awatabe@mail.ece.u-tokyo.ac.jp
OI Ikeda, Daisuke/0000-0002-5666-7387
CR [Anonymous], 2012, Molecular cloning: a laboratory manual
   Aparicio S, 2002, SCIENCE, V297, P1301, DOI 10.1126/science.1072104
   Aparicio S, 2000, TRENDS GENET, V16, P54, DOI 10.1016/S0168-9525(99)01934-4
   BEISEL KW, 1994, GENE, V143, P251, DOI 10.1016/0378-1119(94)90105-8
   Blanchard EM, 1997, CIRC RES, V81, P1005
   BRENNER S, 1993, NATURE, V366, P265, DOI 10.1038/366265a0
   CLAYTON L, 1988, J MOL BIOL, V201, P507, DOI 10.1016/0022-2836(88)90633-X
   Cooley BC, 2001, ARCH BIOCHEM BIOPHYS, V390, P71, DOI 10.1006/abbi.2001.2347
   Dufour C, 1998, J BIOL CHEM, V273, P18547, DOI 10.1074/jbc.273.29.18547
   Force A, 1999, GENETICS, V151, P1531
   FORRYSCHAUDIES S, 1990, CELL GROWTH DIFFER, V1, P473
   GOODWIN LO, 1991, J BIOL CHEM, V266, P8408
   Hammell RL, 1997, J BIOL CHEM, V272, P22409, DOI 10.1074/jbc.272.36.22409
   HANKE PD, 1988, MOL CELL BIOL, V8, P3591, DOI 10.1128/MCB.8.9.3591
   HARDY S, 1995, GENE, V156, P265, DOI 10.1016/0378-1119(94)00929-M
   Hitchcock-DeGregori SE, 2001, BIOCHEMISTRY-US, V40, P2104, DOI 10.1021/bi002421z
   Ikeda D, 2003, MOL BIOL REP, V30, P83, DOI 10.1023/A:1023995208279
   KAGAWA H, 1995, J MOL BIOL, V251, P603, DOI 10.1006/jmbi.1995.0459
   Kehrer-Sawatzki H, 1998, GENE, V222, P145, DOI 10.1016/S0378-1119(98)00495-8
   Kumar S, 2001, BIOINFORMATICS, V17, P1244, DOI 10.1093/bioinformatics/17.12.1244
   LEESMILLER JP, 1991, BIOESSAYS, V13, P429, DOI 10.1002/bies.950130902
   LEESMILLER JP, 1990, MOL CELL BIOL, V10, P1729, DOI 10.1128/MCB.10.4.1729
   LEMONNIER M, 1991, GENE, V107, P229, DOI 10.1016/0378-1119(91)90323-4
   Meyer A, 1999, CURR OPIN CELL BIOL, V11, P699, DOI 10.1016/S0955-0674(99)00039-3
   Naito T, 1998, P NATL ACAD SCI USA, V95, P5178, DOI 10.1073/pnas.95.9.5178
   Ochiai Y, 2001, FISHERIES SCI, V67, P556, DOI 10.1046/j.1444-2906.2001.00272.x
   Peixoto BR, 2000, GENE, V246, P275, DOI 10.1016/S0378-1119(00)00091-3
   Perry SV, 2001, J MUSCLE RES CELL M, V22, P5, DOI 10.1023/A:1010303732441
   Pieples K, 2000, BIOCHEMISTRY-US, V39, P8291, DOI 10.1021/bi000047x
   REESE G, 1999, INT ARCH ALLERGY IMM, V32, P198
   Rethinasamy P, 1998, CIRC RES, V82, P116
   Robinson-Rechavi M, 2001, CURR BIOL, V11, pR458, DOI 10.1016/S0960-9822(01)00280-9
   SAITOU N, 1987, MOL BIOL EVOL, V4, P406, DOI 10.1093/oxfordjournals.molbev.a040454
   Spinner BJ, 2002, J CELL BIOCHEM, V85, P747, DOI 10.1002/jcb.10178
   Thompson JD, 1997, NUCLEIC ACIDS RES, V25, P4876, DOI 10.1093/nar/25.24.4876
   Venkatesh B, 1996, J MOL BIOL, V259, P655, DOI 10.1006/jmbi.1996.0347
   Venkatesh B, 2000, FEBS LETT, V476, P3, DOI 10.1016/S0014-5793(00)01659-8
   Villard L, 1998, GENE, V210, P17, DOI 10.1016/S0378-1119(98)00032-8
   Wheelan SJ, 2001, GENOME RES, V11, P1952, DOI 10.1101/gr.195301
   Yu WP, 2001, ONCOGENE, V20, P5554, DOI 10.1038/sj.onc.1204679
NR 40
TC 23
Z9 25
U1 0
U2 5
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
SN 0378-1119
EI 1879-0038
J9 GENE
JI Gene
PD APR 28
PY 2004
VL 331
BP 41
EP 51
DI 10.1016/j.gene.2004.01.013
PG 11
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA 821XA
UT WOS:000221495400005
PM 15094190
DA 2025-04-10
ER

PT J
AU Zhang, SY
   Yang, XH
   Jiang, M
   Ma, LH
   Hu, J
   Zhang, HH
AF Zhang, Shiyu
   Yang, Xiaohua
   Jiang, Miao
   Ma, Lianhua
   Hu, Ji
   Zhang, Hong-Hong
TI Post-transcriptional control by RNA-binding proteins in diabetes and its
   related complications
SO FRONTIERS IN PHYSIOLOGY
LA English
DT Review
DE RNA-binding proteins; RNA-protein interaction; chronic complications;
   post-transcriptional gene regulation; diabetes mellitus
ID ANGIOTENSINOGEN GENE-EXPRESSION; GROWTH-FACTOR EXPRESSION;
   MESSENGER-RNA; POSTTRANSLATIONAL MODIFICATIONS; INSULIN SENSITIVITY;
   ENDOTHELIAL-CELLS; GLUCOSE; HYPERGLYCEMIA; HUD; TRANSLATION
AB Diabetes mellitus (DM) is a fast-growing chronic metabolic disorder that leads to significant health, social, and economic problems worldwide. Chronic hyperglycemia caused by DM leads to multiple devastating complications, including macrovascular complications and microvascular complications, such as diabetic cardiovascular disease, diabetic nephropathy, diabetic neuropathy, and diabetic retinopathy. Numerous studies provide growing evidence that aberrant expression of and mutations in RNA-binding proteins (RBPs) genes are linked to the pathogenesis of diabetes and associated complications. RBPs are involved in RNA processing and metabolism by directing a variety of post-transcriptional events, such as alternative splicing, stability, localization, and translation, all of which have a significant impact on RNA fate, altering their function. Here, we purposed to summarize the current progression and underlying regulatory mechanisms of RBPs in the progression of diabetes and its complications. We expected that this review will open the door for RBPs and their RNA networks as novel therapeutic targets for diabetes and its related complications.
C1 [Zhang, Shiyu; Jiang, Miao; Ma, Lianhua; Hu, Ji; Zhang, Hong-Hong] Soochow Univ, Affiliated Hosp 2, Dept Endocrinol, Suzhou, Peoples R China.
   [Yang, Xiaohua] Nantong Univ, Affiliated Haian Hosp, Nantong, Peoples R China.
C3 Soochow University - China; Nantong University
RP Hu, J; Zhang, HH (corresponding author), Soochow Univ, Affiliated Hosp 2, Dept Endocrinol, Suzhou, Peoples R China.
EM huji@suda.edu.cn; zhh55022@sina.com
RI Yang, Xiaohua/H-5053-2011; HU, JI/LWI-5934-2024
FU National Natural Science Foundation of China; Jiangsu Youth Medical
   Talents Project;  [82071234];  [82170836];  [QNRC2016874]
FX Funding This work was supported by grant from the National Natural
   Science Foundation of China (82071234 to H-HZ, 82170836 to JH) and from
   the Jiangsu Youth Medical Talents Project (QNRC2016874 to H-HZ).
CR Amadio M, 2012, MOL VIS, V18, P2153
   Amadio M, 2010, BIOCHEM PHARMACOL, V80, P1230, DOI 10.1016/j.bcp.2010.06.033
   Amadio M, 2016, PHARMACOL RES, V111, P713, DOI 10.1016/j.phrs.2016.07.042
   Ambrosio FA, 2021, J MED CHEM, V64, P9989, DOI 10.1021/acs.jmedchem.1c00191
   Feldman Eva L, 2019, Nat Rev Dis Primers, V5, P41, DOI [10.1038/s41572-019-0097-9, 10.1038/s41572-019-0092-1]
   Araki K, 2019, J CLIN INVEST, V129, P3578, DOI 10.1172/JCI124481
   Atkinson MA, 2014, LANCET, V383, P69, DOI 10.1016/S0140-6736(13)60591-7
   Belanger K, 2019, BIOCHEM BIOPH RES CO, V509, P384, DOI 10.1016/j.bbrc.2018.12.150
   Belanger K, 2018, BIOCHEM BIOPH RES CO, V503, P3205, DOI 10.1016/j.bbrc.2018.08.126
   Blackshear PJ, 2002, BIOCHEM SOC T, V30, P945, DOI 10.1042/BST0300945
   Blech-Hermoni Y, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0149061
   Bucolo C, 2021, FRONT PHARMACOL, V12, DOI 10.3389/fphar.2021.707909
   Caines R, 2019, J CELL SCI, V132, DOI 10.1242/jcs.230276
   Calcutt NA, 2020, PAIN, V161, pS65, DOI 10.1097/j.pain.0000000000001922
   Campbell JE, 2021, NAT REV MOL CELL BIO, V22, P142, DOI 10.1038/s41580-020-00317-7
   Cao HP, 2008, OBESITY, V16, P1208, DOI 10.1038/oby.2008.65
   Cao JG, 2021, J CLIN ENDOCR METAB, V106, P2807, DOI 10.1210/clinem/dgab391
   Caracciolo V, 2018, AM J PHYSIOL-ENDOC M, V315, pE676, DOI 10.1152/ajpendo.00224.2017
   Chang SH, 2013, J BIOL CHEM, V288, P4908, DOI 10.1074/jbc.M112.423871
   Chi X, 2017, DRUG DISCOV TODAY, V22, P823, DOI 10.1016/j.drudis.2017.01.013
   Cho NH, 2018, DIABETES RES CLIN PR, V138, P271, DOI 10.1016/j.diabres.2018.02.023
   Ciafrè SA, 2013, RNA BIOL, V10, P935, DOI 10.4161/rna.24641
   Cole JB, 2020, NAT REV NEPHROL, V16, P377, DOI 10.1038/s41581-020-0278-5
   Connerty P, 2016, INT J MOL SCI, V17, DOI 10.3390/ijms17010031
   Corley M, 2020, MOL CELL, V78, P9, DOI 10.1016/j.molcel.2020.03.011
   Demir S, 2021, ADV SCI, V8, DOI 10.1002/advs.202100275
   Dennis MD, 2015, J BIOL CHEM, V290, P3865, DOI 10.1074/jbc.M114.623058
   Deribe YL, 2010, NAT STRUCT MOL BIOL, V17, P666, DOI 10.1038/nsmb.1842
   Dierschke SK, 2020, J BIOL CHEM, V295, P10831, DOI 10.1074/jbc.RA120.013711
   Dierschke SK, 2019, J BIOL CHEM, V294, P5508, DOI 10.1074/jbc.RA119.007494
   Dillmann WH, 2019, CIRC RES, V124, P1160, DOI 10.1161/CIRCRESAHA.118.314665
   Eizirik DL, 2020, NAT REV ENDOCRINOL, V16, P349, DOI 10.1038/s41574-020-0355-7
   Fred RG, 2011, BIOCHEM BIOPH RES CO, V412, P693, DOI 10.1016/j.bbrc.2011.08.030
   Fu XL, 2020, J CELL BIOCHEM, V121, P954, DOI 10.1002/jcb.28978
   Fukao A, 2015, RNA BIOL, V12, P922, DOI 10.1080/15476286.2015.1073436
   Gazzara MR, 2017, GENOME RES, V27, P1360, DOI 10.1101/gr.220517.117
   Gerstberger S, 2014, NAT REV GENET, V15, P829, DOI 10.1038/nrg3813
   Gokulakrishnan K, 2012, METABOLISM, V61, P43, DOI 10.1016/j.metabol.2011.05.014
   Gomes C, 2017, J CELL SCI, V130, P3650, DOI 10.1242/jcs.201244
   Good AL, 2020, DIABETES, V69, P499, DOI 10.2337/dbi18-0068
   Good AL, 2019, MOL METAB, V26, P45, DOI 10.1016/j.molmet.2019.05.009
   Grammatikakis I, 2017, WIRES RNA, V8, DOI 10.1002/wrna.1372
   Gu Y, 2021, BIOCHEM BIOPH RES CO, V557, P280, DOI 10.1016/j.bbrc.2021.04.035
   Guo J, 2020, CELL DEATH DIS, V11, DOI 10.1038/s41419-020-2630-x
   Guo WG, 2014, J MOL CELL CARDIOL, V75, P131, DOI 10.1016/j.yjmcc.2014.07.010
   Hammes HP, 2018, DIABETOLOGIA, V61, P29, DOI 10.1007/s00125-017-4435-8
   Harding JL, 2019, DIABETOLOGIA, V62, P3, DOI 10.1007/s00125-018-4711-2
   Haywood NJ, 2017, DIABETES, V66, P287, DOI 10.2337/db16-0997
   Hentze MW, 2018, NAT REV MOL CELL BIO, V19, P327, DOI 10.1038/nrm.2017.130
   Ho JJD, 2021, WIRES RNA, V12, DOI 10.1002/wrna.1647
   Ho JJD, 2016, TRENDS BIOCHEM SCI, V41, P821, DOI 10.1016/j.tibs.2016.05.009
   Hong Y, 2020, CELL DEATH DIFFER, V27, P1633, DOI 10.1038/s41418-019-0447-x
   Issad T, 2010, DIABETES METAB, V36, P423, DOI 10.1016/j.diabet.2010.09.001
   Jeong DE, 2018, MOL CELLS, V41, P909, DOI 10.14348/molcells.2018.0147
   Jia GH, 2018, DIABETOLOGIA, V61, P21, DOI 10.1007/s00125-017-4390-4
   Jones JI, 2021, FRONT MOL NEUROSCI, V14, DOI 10.3389/fnmol.2021.728163
   Kang QZ, 2020, REDOX BIOL, V37, DOI 10.1016/j.redox.2020.101799
   Kanwar YS, 2011, ANNU REV PATHOL-MECH, V6, P395, DOI 10.1146/annurev.pathol.4.110807.092150
   Kelaini S, 2021, BIOLOGY-BASEL, V10, DOI 10.3390/biology10050366
   Khalaj K, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-06081-7
   Klim JR, 2021, TRENDS NEUROSCI, V44, P424, DOI 10.1016/j.tins.2021.02.008
   Knoch KP, 2014, MOL METAB, V3, P518, DOI 10.1016/j.molmet.2014.05.002
   Knoch KP, 2004, NAT CELL BIOL, V6, P207, DOI 10.1038/ncb1099
   Kulkarni SD, 2011, J BIOL CHEM, V286, P14146, DOI 10.1074/jbc.M110.190553
   Lay AC, 2021, DIABETOLOGIA, V64, P1690, DOI 10.1007/s00125-021-05427-1
   LAZARISKARATZAS A, 1990, NATURE, V345, P544, DOI 10.1038/345544a0
   Lee EK, 2012, MOL CELL, V45, P826, DOI 10.1016/j.molcel.2012.01.016
   Li ZH, 2018, NUCLEIC ACIDS RES, V46, P12052, DOI 10.1093/nar/gky867
   Liu FX, 2021, J CELL PHYSIOL, V236, P6607, DOI 10.1002/jcp.30238
   Lo CS, 2012, DIABETES, V61, P2597, DOI 10.2337/db11-1349
   Long YX, 2019, J BIOL CHEM, V294, P1312, DOI 10.1074/jbc.RA118.003392
   Lovci MT, 2016, ADV EXP MED BIOL, V907, P297, DOI 10.1007/978-3-319-29073-7_12
   Lujan DA, 2018, WIRES RNA, V9, DOI 10.1002/wrna.1462
   Magro MG, 2013, MOL METAB, V2, P348, DOI 10.1016/j.molmet.2013.09.003
   Makita S, 2021, FRONT IMMUNOL, V12, DOI 10.3389/fimmu.2021.711633
   Masaki N, 2020, J AM HEART ASSOC, V9, DOI 10.1161/JAHA.119.014046
   Mayr C, 2019, CSH PERSPECT BIOL, V11, DOI 10.1101/cshperspect.a034728
   Mayr F, 2013, INT J MOL SCI, V14, P16532, DOI 10.3390/ijms140816532
   Mellor KM, 2015, LIFE SCI, V129, P48, DOI 10.1016/j.lfs.2014.03.020
   Miller WP, 2016, INVEST OPHTH VIS SCI, V57, P1327, DOI 10.1167/iovs.15-18719
   Mohibi S, 2019, PHARMACOL THERAPEUT, V203, DOI 10.1016/j.pharmthera.2019.07.001
   Mustaciosu CC, 2019, INT J MOL SCI, V20, DOI 10.3390/ijms20081965
   Nutter CA, 2018, WIRES RNA, V9, DOI 10.1002/wrna.1459
   Nutter CA, 2016, CELL REP, V15, P2200, DOI 10.1016/j.celrep.2016.05.002
   Osborne MJ, 2015, IMMUNOL REV, V263, P210, DOI 10.1111/imr.12240
   Park JT, 2014, AM J PHYSIOL-RENAL, V307, pF1390, DOI 10.1152/ajprenal.00458.2014
   Pereira B, 2017, TRENDS CANCER, V3, P506, DOI 10.1016/j.trecan.2017.05.003
   Pérez-Ortín JE, 2013, J MOL BIOL, V425, P3750, DOI 10.1016/j.jmb.2013.02.029
   Petersmann A, 2019, EXP CLIN ENDOCR DIAB, V127, pS1, DOI 10.1055/a-1018-9078
   Peterson SB, 2016, CRIT REV BIOCHEM MOL, V51, P150, DOI 10.3109/10409238.2015.1135102
   Platania CBM, 2020, BIOCHEM PHARMACOL, V175, DOI 10.1016/j.bcp.2020.113908
   Pope SD, 2018, MOL CELL, V71, P389, DOI 10.1016/j.molcel.2018.07.017
   Rajwani A, 2012, DIABETES, V61, P915, DOI 10.2337/db11-0963
   Ross EA, 2017, ANN RHEUM DIS, V76, P612, DOI 10.1136/annrheumdis-2016-209424
   Salem ESB, 2019, FRONT CARDIOVASC MED, V6, DOI 10.3389/fcvm.2019.00106
   Sanna MD, 2015, EXP NEUROL, V267, P53, DOI 10.1016/j.expneurol.2015.02.036
   Sanna MD, 2014, PHARMACOL RES, V81, P44, DOI 10.1016/j.phrs.2014.02.004
   Sanna MD, 2017, BRAIN RES, V1659, P55, DOI 10.1016/j.brainres.2017.01.019
   Sawicki KT, 2018, JCI INSIGHT, V3, DOI 10.1172/jci.insight.95948
   Schaeffer V, 2012, AM J PHYSIOL-RENAL, V303, pF75, DOI 10.1152/ajprenal.00185.2012
   Schrufer TL, 2010, DIABETES, V59, P2107, DOI 10.2337/db10-0148
   Shang J, 2015, FREE RADICAL BIO MED, V79, P217, DOI 10.1016/j.freeradbiomed.2014.12.013
   Shi Q, 2020, MOL METAB, V36, DOI 10.1016/j.molmet.2020.02.011
   Shinoda G, 2013, STEM CELLS, V31, P1563, DOI 10.1002/stem.1423
   Si R, 2021, JCI INSIGHT, V6, DOI 10.1172/jci.insight.147982
   Sidali A, 2022, INT J MOL SCI, V23, DOI 10.3390/ijms23010096
   Simó R, 2018, DIABETOLOGIA, V61, P1902, DOI 10.1007/s00125-018-4692-1
   Sperling R, 2017, WIRES RNA, V8, DOI 10.1002/wrna.1377
   Stitt AW, 2013, CLIN SCI, V125, P1, DOI 10.1042/CS20120588
   Stoll L, 2020, NAT COMMUN, V11, DOI 10.1038/s41467-020-19381-w
   Sun SH, 2016, BIOCHEM BIOPH RES CO, V469, P29, DOI 10.1016/j.bbrc.2015.11.065
   Sung Y, 2019, CELL BIOCHEM FUNCT, V37, P139, DOI 10.1002/cbf.3376
   Tao LL, 2021, LIFE SCI, V268, DOI 10.1016/j.lfs.2020.119015
   Van Nostrand EL, 2020, NATURE, V583, P711, DOI 10.1038/s41586-020-2077-3
   Velázquez-Cruz A, 2021, FRONT MOL BIOSCI, V8, DOI 10.3389/fmolb.2021.658852
   Verma SK, 2022, NUCLEIC ACIDS RES, V50, P2270, DOI 10.1093/nar/gkac055
   Verma SK, 2013, J BIOL CHEM, V288, P35372, DOI 10.1074/jbc.M113.507426
   Wan XX, 2020, BBA-MOL BASIS DIS, V1866, DOI 10.1016/j.bbadis.2019.165620
   Wang FF, 2015, P NATL ACAD SCI USA, V112, pE4995, DOI 10.1073/pnas.1513780112
   Wang W, 2018, INT J MOL SCI, V19, DOI 10.3390/ijms19061816
   Wei CC, 2005, J AM SOC NEPHROL, V16, P616, DOI 10.1681/ASN.2004080715
   Weir GC, 2020, LANCET DIABETES ENDO, V8, P249, DOI 10.1016/S2213-8587(20)30022-X
   Weisse J, 2020, INT J MOL SCI, V21, DOI 10.3390/ijms21186835
   Wu TF, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0083869
   Wu YL, 2022, INT J MOL SCI, V23, DOI 10.3390/ijms23031032
   Xing XD, 2019, BIOCHEM BIOPH RES CO, V512, P552, DOI 10.1016/j.bbrc.2019.03.135
   Xu YJ, 2019, OPEN BIOL, V9, DOI 10.1098/rsob.180239
   Yang CB, 2020, NAT COMMUN, V11, DOI 10.1038/s41467-020-17468-y
   Yang CB, 2018, FRONT PHYSIOL, V9, DOI 10.3389/fphys.2018.01310
   Yao ZT, 2022, CANCER COMMUN, V42, P117, DOI 10.1002/cac2.12254
   You PH, 2020, J CELL PHYSIOL, V235, P4455, DOI 10.1002/jcp.29321
   Zhai K, 2016, DIABETOLOGIA, V59, P1959, DOI 10.1007/s00125-016-4005-5
   Zhang CY, 2020, THERANOSTICS, V10, P10908, DOI 10.7150/thno.48264
   Zhao MX, 2020, J MOL CELL BIOL, V12, P277, DOI 10.1093/jmcb/mjz050
   Zhu H, 2011, CELL, V147, P81, DOI 10.1016/j.cell.2011.08.033
   Zhu Y, 2021, MOL ASPECTS MED, V79, DOI 10.1016/j.mam.2020.100885
   Zoja C, 2020, FRONT PHARMACOL, V11, DOI 10.3389/fphar.2020.586892
NR 137
TC 4
Z9 4
U1 1
U2 18
PU FRONTIERS MEDIA SA
PI LAUSANNE
PA AVENUE DU TRIBUNAL FEDERAL 34, LAUSANNE, CH-1015, SWITZERLAND
EI 1664-042X
J9 FRONT PHYSIOL
JI Front. Physiol.
PD OCT 6
PY 2022
VL 13
AR 953880
DI 10.3389/fphys.2022.953880
PG 13
WC Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Physiology
GA 5Q7WA
UT WOS:000874035800001
PM 36277184
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Higashiyama, S
   Horikawa, M
   Yamada, K
   Ichino, N
   Nakano, N
   Nakagawa, T
   Miyagawa, J
   Matsushita, N
   Nagatsu, T
   Taniguchi, N
   Ishiguro, H
AF Higashiyama, S
   Horikawa, M
   Yamada, K
   Ichino, N
   Nakano, N
   Nakagawa, T
   Miyagawa, J
   Matsushita, N
   Nagatsu, T
   Taniguchi, N
   Ishiguro, H
TI A novel brain-derived member of the epidermal growth factor family that
   interacts with ErbB3 and ErbB4
SO JOURNAL OF BIOCHEMISTRY
LA English
DT Article
DE EGF; ErbB; neuregulin; NTAK; PC-12
ID FACTOR RECEPTOR; EGF RECEPTOR; MICE LACKING; NEUREGULIN RECEPTOR;
   CARDIAC DEVELOPMENT; EXPRESSION; RAT; GENE; AMPLIFICATION; CARCINOMA
AB A novel member of the epidermal growth factor (EGF) family, the neural-and thymus-derived activator for ErbB kinases (NTAK), has been purified and cloned. Five alternative spliced isoforms have been detected in the rat adrenal pheochromocytoma cell line, PC-12 cells. The rat NTAK alpha 2a isoform exhibits 94% identity in its primary sequence with the human NTAK alpha isoform. In vivo, NTAK is only expressed in the brain of rat E11.5 embryos, and in the brain and thymus of adult rats. The soluble 46 kDa form binds directly to ErbB3 and B4, but not to ErbB1 or B2. NTAK, however, transactivates ErbB1 and B2 via heterodimerization with ErbB3 or E4. NTAK stimulates the differentiation of MDA-MB-453 cells and competitively inhibits the binding of [I-125] neuregulin to these cells. In addition to these neuregulin-like properties, NTAK exhibits limited structural homology to neuregulins in the immunoglobulin (Ig)-like, EGF-like, and hydrophobic domains. Thus, NTAK appears to be a new member of the EGF family displaying neuregulin properties.
C1 OSAKA UNIV,SCH MED,DEPT INTERNAL MED,SUITA,OSAKA 565,JAPAN.
   FUJITA HLTH UNIV,SCH MED,INST COMPREHENS MED SCI,TOYOAKE,AICHI 47011,JAPAN.
C3 The University of Osaka; Fujita Health University
RP Higashiyama, S (corresponding author), OSAKA UNIV,SCH MED,DEPT BIOCHEM,2-2 YAMADAOKA,SUITA,OSAKA 565,JAPAN.
RI Taniguchi, Naoyuki/I-4182-2014
OI Taniguchi, Naoyuki/0000-0001-5889-5968
CR ABRAHAM JA, 1993, BIOCHEM BIOPH RES CO, V190, P125, DOI 10.1006/bbrc.1993.1020
   Carraway KL, 1997, NATURE, V387, P512, DOI 10.1038/387512a0
   Chang H, 1997, NATURE, V387, P509, DOI 10.1038/387509a0
   COHEN STANLEY, 1964, NAT CANCER INST MONOGR, V13, P13
   COUSSENS L, 1985, SCIENCE, V230, P1132, DOI 10.1126/science.2999974
   DERYNCK R, 1984, CELL, V38, P287, DOI 10.1016/0092-8674(84)90550-6
   GASSMANN M, 1995, NATURE, V378, P390, DOI 10.1038/378390a0
   HIGASHIYAMA S, 1991, SCIENCE, V251, P936, DOI 10.1126/science.1840698
   HIGASHIYAMA S, 1992, J BIOL CHEM, V267, P6205
   HOLMES WE, 1992, SCIENCE, V256, P1205, DOI 10.1126/science.256.5060.1205
   KIMURA H, 1990, NATURE, V348, P257, DOI 10.1038/348257a0
   KING CR, 1985, SCIENCE, V229, P974, DOI 10.1126/science.2992089
   LEE KF, 1995, NATURE, V378, P394, DOI 10.1038/378394a0
   MALMQVIST M, 1993, NATURE, V361, P186, DOI 10.1038/361186a0
   MARQUARDT H, 1984, SCIENCE, V223, P1079, DOI 10.1126/science.6320373
   MEYER D, 1995, NATURE, V378, P386, DOI 10.1038/378386a0
   MIETTINEN PJ, 1995, NATURE, V376, P337, DOI 10.1038/376337a0
   PinkasKramarski R, 1996, EMBO J, V15, P2452, DOI 10.1002/j.1460-2075.1996.tb00603.x
   PLOWMAN GD, 1993, P NATL ACAD SCI USA, V90, P1746, DOI 10.1073/pnas.90.5.1746
   PLOWMAN GD, 1990, P NATL ACAD SCI USA, V87, P4905, DOI 10.1073/pnas.87.13.4905
   RIESE DJ, 1995, MOL CELL BIOL, V15, P5770
   SAIKI RK, 1988, SCIENCE, V239, P487, DOI 10.1126/science.2448875
   SHING Y, 1993, SCIENCE, V259, P1604, DOI 10.1126/science.8456283
   SHOYAB M, 1989, SCIENCE, V243, P1074, DOI 10.1126/science.2466334
   SIBILIA M, 1995, SCIENCE, V269, P234, DOI 10.1126/science.7618085
   SIMPSON RJ, 1985, EUR J BIOCHEM, V153, P629, DOI 10.1111/j.1432-1033.1985.tb09346.x
   THREADGILL DW, 1995, SCIENCE, V269, P230, DOI 10.1126/science.7618084
   TOYODA H, 1995, J BIOL CHEM, V270, P7495, DOI 10.1074/jbc.270.13.7495
   ULLRICH A, 1984, NATURE, V309, P418, DOI 10.1038/309418a0
   WEN DZ, 1994, MOL CELL BIOL, V14, P1909, DOI 10.1128/MCB.14.3.1909
   WEN DZ, 1992, CELL, V69, P559, DOI 10.1016/0092-8674(92)90456-M
NR 31
TC 65
Z9 97
U1 0
U2 0
PU JAPANESE BIOCHEMICAL SOC
PI TOKYO
PA ISHIKAWA BLDG-3F, 25-16 HONGO-5-CHOME, BUNKYO-KU, TOKYO 113, JAPAN
SN 0021-924X
J9 J BIOCHEM-TOKYO
JI J. Biochem. (Tokyo)
PD SEP
PY 1997
VL 122
IS 3
BP 675
EP 680
PG 6
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA XU612
UT WOS:A1997XU61200030
PM 9348101
DA 2025-04-10
ER

PT J
AU Hou, L
   Jiang, F
   Yang, PC
   Wang, XH
   Kang, L
AF Hou, Li
   Jiang, Feng
   Yang, Pengcheng
   Wang, Xianhui
   Kang, Le
TI Molecular characterization and expression profiles of neuropeptide
   precursors in the migratory locust
SO INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY
LA English
DT Article
DE Migratory locust; Polyphenism; Peptides; Expression pattern
ID INSULIN-LIKE PEPTIDES; RED FLOUR BEETLE; ADIPOKINETIC HORMONE;
   PHASE-CHANGES; FUNCTIONAL-ANALYSIS; CORPORA CARDIACA; DESERT LOCUST;
   DROSOPHILA; PEPTIDOMICS; RECEPTOR
AB Neuropeptides serve as the most important regulatory signals in insects. Many neuropeptides and their precursors have been identified in terms of the contig sequences of whole genome information of the migratory locust (Locusta migratoria), which exhibits a typical phenotypic plasticity in morphology, behavior and physiology. However, functions of these locust neuropeptides are largely unknown. In this study, we first revised the 23 reported neuropeptide precursor genes and identified almost all the neuropeptide precursors and corresponding products in L migratoria. We further revealed the significant expansion profiles (such as AKH) and alternative splicing of neuropeptide genes (Lom-ITP, Lom-OK and Lom-NPF1). Transcriptomic analysis indicated that several neuropeptides, such as Lom-ACP and Lom-OK, displayed development-specific expression patterns. qRT-PCR data confirmed that most neuropeptide precursors were strongly expressed in the central nervous system. Fifteen neuropeptide genes displayed different expression levels between solitarious and gregarious locusts. These findings provide valuable clues to understand neuropeptide evolution and their functional roles in basic biology and phase transition in locusts. (C) 2015 Elsevier Ltd. All rights reserved.
C1 [Hou, Li; Wang, Xianhui; Kang, Le] Chinese Acad Sci, State Key Lab Integrated Management Pest Insects, Inst Zool, Beijing 100101, Peoples R China.
   [Jiang, Feng; Yang, Pengcheng; Kang, Le] Chinese Acad Sci, Beijing Inst Life Sci, Beijing 100101, Peoples R China.
C3 Chinese Academy of Sciences; Institute of Zoology, CAS; Chinese Academy
   of Sciences
RP Kang, L (corresponding author), Chinese Acad Sci, Inst Zool, 1 Beichen West Rd, Beijing 100101, Peoples R China.
EM wangxh@ioz.ac.cn; lkang@ioz.ac.cn
RI Kang, Le/ABD-1116-2022; Jiang, Feng/AHC-5102-2022; Yang,
   Pengcheng/Q-5597-2019; Yang, Pengcheng/N-1037-2014; Hou,
   Li/HLX-0405-2023
OI Jiang, Feng/0000-0002-7407-7604; Kang, Le/0000-0003-4262-2329; Yang,
   Pengcheng/0000-0001-5496-8357; Hou, Li/0000-0001-6727-7053
FU China Postdoctoral Science Foundation [2012M520379, 2013T60171];
   National Natural Science Foundation of China [31472047]
FX This work was supported by the China Postdoctoral Science Foundation
   (Grant Nos. 2012M520379 and 2013T60171) and the National Natural Science
   Foundation of China (No. 31472047).
CR [Anonymous], 1977, Grasshoppers and locusts. 2: behaviour, ecology
   Apone Fabio, 2014, J Insect Sci, V14, P87, DOI 10.1093/jis/14.1.87
   Arakane Y, 2008, MECH DEVELOP, V125, P984, DOI 10.1016/j.mod.2008.09.002
   Audsley N, 2013, PEPTIDES, V41, P74, DOI 10.1016/j.peptides.2012.11.001
   Ayali A, 1996, PHYSIOL ENTOMOL, V21, P167, DOI 10.1111/j.1365-3032.1996.tb00851.x
   Ayali A, 1996, ARCH INSECT BIOCHEM, V31, P439, DOI 10.1002/(SICI)1520-6327(1996)31:4<439::AID-ARCH6>3.0.CO;2-Q
   Badisco L, 2011, PEPTIDES, V32, P573, DOI 10.1016/j.peptides.2010.11.008
   Baggerman G, 2002, J BIOL CHEM, V277, P40368, DOI 10.1074/jbc.M206257200
   Begum K, 2009, INSECT BIOCHEM MOLEC, V39, P717, DOI 10.1016/j.ibmb.2009.08.005
   Broeck JV, 2001, PEPTIDES, V22, P241, DOI 10.1016/S0196-9781(00)00376-4
   Brogiolo W, 2001, CURR BIOL, V11, P213, DOI 10.1016/S0960-9822(01)00068-9
   Chen QQ, 2015, INSECT BIOCHEM MOLEC, V56, P1, DOI 10.1016/j.ibmb.2014.11.001
   Chen SA, 2010, PLOS ONE, V5, DOI 10.1371/journal.pone.0015633
   Clynen E, 2006, BMC GENOMICS, V7, DOI 10.1186/1471-2164-7-201
   Clynen E, 2009, INSECT BIOCHEM MOLEC, V39, P491, DOI 10.1016/j.ibmb.2009.06.001
   Cornils A, 2011, DEVELOPMENT, V138, P1183, DOI 10.1242/dev.060905
   Dircksen H, 2011, J PROTEOME RES, V10, P4478, DOI 10.1021/pr200284e
   Ernst UR, 2015, J EXP BIOL, V218, P88, DOI 10.1242/jeb.107078
   Fontana JR, 2012, DEV BIOL, V372, P131, DOI 10.1016/j.ydbio.2012.09.010
   Guo XJ, 2013, FRONT BEHAV NEUROSCI, V7, DOI 10.3389/fnbeh.2013.00129
   Hansen KK, 2010, J BIOL CHEM, V285, P10736, DOI 10.1074/jbc.M109.045369
   Herbert Z, 2010, J MORPHOL, V271, P1509, DOI 10.1002/jmor.10895
   Hewes RS, 2001, GENOME RES, V11, P1126, DOI 10.1101/gr.169901
   Hofer S, 2006, J EXP BIOL, V209, P2794, DOI 10.1242/jeb.02307
   Homberg U, 2002, MICROSC RES TECHNIQ, V56, P189, DOI 10.1002/jemt.10024
   Hummon AB, 2006, SCIENCE, V314, P647, DOI 10.1126/science.1124128
   Janssen T, 2001, INSECT MOL BIOL, V10, P183, DOI 10.1046/j.1365-2583.2001.00257.x
   Kang L, 2004, P NATL ACAD SCI USA, V101, P17611, DOI 10.1073/pnas.0407753101
   Lee KS, 2004, J BIOL CHEM, V279, P50781, DOI 10.1074/jbc.M407842200
   Li B, 2008, GENOME RES, V18, P113, DOI 10.1101/gr.6714008
   Ma Z., 2015, SCI REP, V5
   Ma ZY, 2011, P NATL ACAD SCI USA, V108, P3882, DOI 10.1073/pnas.1015098108
   Maeno K., 2007, B ENTOMOL RES, V94
   Nässel DR, 2002, PROG NEUROBIOL, V68, P1, DOI 10.1016/S0301-0082(02)00057-6
   Pascual N, 2004, INSECT BIOCHEM MOLEC, V34, P1141, DOI 10.1016/j.ibmb.2004.07.005
   Patel H, 2014, GEN COMP ENDOCR, V195, P1, DOI 10.1016/j.ygcen.2013.10.012
   Predel R, 2005, FEBS J, V272, P3365, DOI 10.1111/j.1742-4658.2005.04752.x
   Predel R, 2010, J PROTEOME RES, V9, P2006, DOI 10.1021/pr901187p
   Riehle MA, 2006, PEPTIDES, V27, P2547, DOI 10.1016/j.peptides.2006.07.016
   Roller L, 2008, INSECT BIOCHEM MOLEC, V38, P1147, DOI 10.1016/j.ibmb.2008.04.009
   Sajwan S, 2015, INSECT BIOCHEM MOLEC, V61, P79, DOI 10.1016/j.ibmb.2015.01.011
   SCHOOFS L, 1991, REGUL PEPTIDES, V36, P111, DOI 10.1016/0167-0115(91)90199-Q
   Schoofs L, 1997, PEPTIDES, V18, P145, DOI 10.1016/S0196-9781(96)00236-7
   Sim C, 2013, FRONT PHYSIOL, V4, DOI 10.3389/fphys.2013.00189
   Tawfik AI, 1999, P NATL ACAD SCI USA, V96, P7083, DOI 10.1073/pnas.96.12.7083
   Van Wielendaele P, 2013, INSECT BIOCHEM MOLEC, V43, P102, DOI 10.1016/j.ibmb.2012.10.002
   Veenstra JA, 2000, ARCH INSECT BIOCHEM, V43, P49, DOI 10.1002/(SICI)1520-6327(200002)43:2<49::AID-ARCH1>3.0.CO;2-M
   Veenstra JA, 2014, FRONT PHYSIOL, V5, DOI 10.3389/fphys.2014.00454
   Veenstra JA, 2014, CELL TISSUE RES, V357, P607, DOI 10.1007/s00441-014-1880-2
   Veenstra JA, 2009, INSECT BIOCHEM MOLEC, V39, P161, DOI 10.1016/j.ibmb.2008.10.014
   Verlinden H, 2009, GEN COMP ENDOCR, V162, P79, DOI 10.1016/j.ygcen.2008.11.016
   Wang XH, 2014, NAT COMMUN, V5, P1, DOI 10.1038/ncomms3957
   Wang XH, 2014, ANNU REV ENTOMOL, V59, P225, DOI 10.1146/annurev-ento-011613-162019
   Xu J, 2010, J NEUROSCI, V30, P2504, DOI 10.1523/JNEUROSCI.3262-09.2010
   Yamanaka N, 2011, J COMP NEUROL, V519, P238, DOI 10.1002/cne.22517
   Zandawala M, 2012, INSECT BIOCHEM MOLEC, V42, P816, DOI 10.1016/j.ibmb.2012.06.006
NR 56
TC 27
Z9 31
U1 1
U2 69
PU PERGAMON-ELSEVIER SCIENCE LTD
PI OXFORD
PA THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND
SN 0965-1748
EI 1879-0240
J9 INSECT BIOCHEM MOLEC
JI Insect Biochem. Mol. Biol.
PD AUG
PY 2015
VL 63
BP 63
EP 71
DI 10.1016/j.ibmb.2015.05.014
PG 9
WC Biochemistry & Molecular Biology; Entomology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Entomology
GA CO4YM
UT WOS:000359166800008
PM 26036749
DA 2025-04-10
ER

PT J
AU Jennions, E
   Hedberg-Oldfors, C
   Berglund, AK
   Kollberg, G
   Törnhage, CJ
   Eklund, EA
   Oldfors, A
   Verloo, P
   Vanlander, AV
   De Meirleir, L
   Seneca, S
   Sterky, FH
   Darin, N
AF Jennions, Elizabeth
   Hedberg-Oldfors, Carola
   Berglund, Anna-Karin
   Kollberg, Gittan
   Tornhage, Carl-Johan
   Eklund, Erik A.
   Oldfors, Anders
   Verloo, Patrick
   Vanlander, Arnaud V.
   De Meirleir, Linda
   Seneca, Sara
   Sterky, Fredrik H.
   Darin, Niklas
TI TANGO2 deficiency as a cause of neurodevelopmental delay with
   indirect effects on mitochondrial energy metabolism
SO JOURNAL OF INHERITED METABOLIC DISEASE
LA English
DT Article
DE copy-number variation; developmental delay; FAD; rare disease; succinate
   dehydrogenase
ID CRISES
AB Exome sequencing has recently identified mutations in the gene TANGO2 (transport and Golgi organization 2) as a cause of developmental delay associated with recurrent crises involving rhabdomyolysis, cardiac arrhythmias, and metabolic derangements. The disease is not well understood, in part as the cellular function and subcellular localization of the TANGO2 protein remain unknown. Furthermore, the clinical syndrome with its heterogeneity of symptoms, signs, and laboratory findings is still being defined. Here, we describe 11 new cases of TANGO2-related disease, confirming and further expanding the previously described clinical phenotype. Patients were homozygous or compound heterozygous for previously described exonic deletions or new frameshift, splice site, and missense mutations. All patients showed developmental delay with ataxia, dysarthria, intellectual disability, or signs of spastic diplegia. Of importance, we identify two subjects (aged 12 and 17 years) who have never experienced any overt episode of the catabolism-induced metabolic crises typical for the disease. Mitochondrial complex II activity was mildly reduced in patients investigated in association with crises but normal in other patients. In one deceased patient, post-mortem autopsy revealed heterotopic neurons in the cerebral white matter, indicating a possible role for TANGO2 in neuronal migration. Furthermore, we have addressed the subcellular localization of several alternative isoforms of TANGO2, none of which were mitochondrial but instead appeared to have a primarily cytoplasmic localization. Previously described aberrations in Golgi morphology were not observed in cultured skin fibroblasts.
C1 [Jennions, Elizabeth; Tornhage, Carl-Johan; Darin, Niklas] Univ Gothenburg, Sahlgrenska Acad, Inst Clin Sci, Dept Pediat, Gothenburg, Sweden.
   [Hedberg-Oldfors, Carola; Oldfors, Anders] Univ Gothenburg, Inst Biomed, Dept Pathol & Genet, Gothenburg, Sweden.
   [Berglund, Anna-Karin; Kollberg, Gittan; Sterky, Fredrik H.] Univ Gothenburg, Inst Biomed, Dept Clin Chem & Transfus Med, Gothenburg, Sweden.
   [Berglund, Anna-Karin; Sterky, Fredrik H.] Univ Gothenburg, Wallenberg Ctr Mol & Translat Med, Gothenburg, Sweden.
   [Tornhage, Carl-Johan] Skaraborg Hosp, Dept Paediat, Skovde, Sweden.
   [Eklund, Erik A.] Lund Univ, Paediat Sect, Dept Clin Sci, Lund, Sweden.
   [Verloo, Patrick; Vanlander, Arnaud V.] Ghent Univ Hosp, Div Paediat Neurol & Metab, Dept Internal Med & Paediat, Ghent, Belgium.
   [De Meirleir, Linda] UZ Brussel, Dept Paediat Neurol & Metab Dis, Brussels, Belgium.
   [Seneca, Sara] Vrije Univ Brussel, Ctr Med Genet, Univ Hosp Brussels, Brussels, Belgium.
   [Seneca, Sara] Vrije Univ Brussel, Res Unit Genet & Fertil, Brussels, Belgium.
C3 University of Gothenburg; University of Gothenburg; University of
   Gothenburg; University of Gothenburg; Lund University; Ghent University;
   Ghent University Hospital; University Hospital Brussels; Vrije
   Universiteit Brussel; University Hospital Brussels; Vrije Universiteit
   Brussel
RP Sterky, FH (corresponding author), Univ Gothenburg, Inst Biomed, Dept Clin Chem & Transfus Med, Gothenburg, Sweden.; Jennions, E (corresponding author), Queen Silvias Childrens Hosp, Dept Paediat Neurol, Rondvagen 10, S-41650 Gothenburg, Sweden.
EM elizabeth.jennions@vgregion.se; fredrik.sterky@gu.se
RI Darin, Niklas/AAL-6345-2020; Sterky, Fredrik/ABZ-7879-2022; Arnaud,
   Vanlander/ABB-5978-2021
OI Oldfors, Anders/0000-0002-5758-7397; Vanlander,
   Arnaud/0000-0002-9520-5564; Eklund, Erik/0000-0003-1902-4865; Jennions,
   Elizabeth/0000-0001-6235-0469; Verloo, Patrick/0000-0003-2077-0275
FU Vastra Gotalandsregionen (SE) [ALFGBG-76200]; Vastra Gotalandsregionen
   [ALFGBG-797811, ALFGBG-716821]; Vetenskapsradet; Goteborgs Universitet;
   Knut och Alice Wallenbergs Stiftelse; Swedish Research Council
   [ALFGBG76200]
FX Vastra Gotalandsregionen (SE), Grant/Award Number: ALFGBG-76200; Vastra
   Gotalandsregionen, Grant/Award Numbers: ALFGBG-797811, ALFGBG-716821;
   Vetenskapsradet, Grant/Award Number: None; Goteborgs Universitet; Knut
   och Alice Wallenbergs Stiftelse; Swedish Research Council, Grant/Award
   Number: ALFGBG76200
CR Bard F, 2006, NATURE, V439, P604, DOI 10.1038/nature04377
   Calvo SE, 2016, NUCLEIC ACIDS RES, V44, pD1251, DOI 10.1093/nar/gkv1003
   Coe BP, 2014, NAT GENET, V46, P1063, DOI 10.1038/ng.3092
   Dines JN, 2019, GENET MED, V21, P601, DOI 10.1038/s41436-018-0137-y
   Dubowitz V, 2013, MUSCLE BIOPSY PRACTI
   Kremer LS, 2016, AM J HUM GENET, V98, P358, DOI 10.1016/j.ajhg.2015.12.009
   Lalani SR, 2016, AM J HUM GENET, V98, P347, DOI 10.1016/j.ajhg.2015.12.008
   Maynard TM, 2008, MOL CELL NEUROSCI, V39, P439, DOI 10.1016/j.mcn.2008.07.027
   Shaikh TH, 2009, GENOME RES, V19, P1682, DOI 10.1101/gr.083501.108
   Sterky FH, 2017, P NATL ACAD SCI USA, V114, pE1253, DOI 10.1073/pnas.1621321114
   Wiedemann N, 2017, ANNU REV BIOCHEM, V86, P685, DOI 10.1146/annurev-biochem-060815-014352
NR 11
TC 36
Z9 37
U1 0
U2 7
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0141-8955
EI 1573-2665
J9 J INHERIT METAB DIS
JI J. Inherit. Metab. Dis.
PD SEP
PY 2019
VL 42
IS 5
BP 898
EP 908
DI 10.1002/jimd.12149
PG 11
WC Endocrinology & Metabolism; Genetics & Heredity; Medicine, Research &
   Experimental
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism; Genetics & Heredity; Research & Experimental
   Medicine
GA IX9US
UT WOS:000486036500017
PM 31276219
DA 2025-04-10
ER

PT J
AU Northrup, V
   Perez, LJ
   Edgett, BA
   Karakach, T
   Simpson, JA
   Brunt, KR
AF Northrup, Victoria
   Perez, Lester J.
   Edgett, Brittany A.
   Karakach, Tobias
   Simpson, Jeremy A.
   Brunt, Keith R.
TI Intron retention is a mechanism of erythropoietin regulation in brain
   cell models
SO GENE
LA English
DT Article
DE Transcription regulation; Alternative splicing; Oxidaditive metabolism;
   Oxygen; Erythropoietin
ID GENE-REGULATION; PROGRAM; TRANSCRIPTS
AB Intron retention is a mechanism of post-transcriptional gene regulation, including genes involved in erythropoiesis. Erythropoietin (EPO) is a hormone without evidence of intracellular vesicle storage that regulates erythropoiesis. We hypothesize that EPO uses intron retention as a mechanism of post-transcriptional regulation in response to hypoxia and ischemia. Cell models of hypoxia and ischemia for kidney, liver, and brain cells were examined for intron retention by real time quantitative PCR. EPO expression increased in most cells except for blood brain barrier and liver cells. The intron retained transcript ratio decreased in brain cells, except for Astrocytes, but showed no change in kidney or liver after 24 h of ischemia. The shift in intron ratio was maintained when using poly (A) enriched cDNA, suggesting that intron retention is not due to immature transcripts. The expression of EPO was elevated at variable time points amongst cell models with the intron ratio also changing over a time course of 2 to 16 h after ischemia. We conclude that intron retention is a mechanism regulating EPO expression in response to ischemia in a tissue specific manner.
C1 [Northrup, Victoria; Perez, Lester J.; Karakach, Tobias; Brunt, Keith R.] Dalhousie Univ, Dept Pharmacol, Halifax, NS, Canada.
   [Northrup, Victoria; Perez, Lester J.; Brunt, Keith R.] Dalhousie Med New Brunswick, St John, NB, Canada.
   [Simpson, Jeremy A.] Univ Guelph, Dept Human & Nutr Sci, Guelph, ON, Canada.
   [Edgett, Brittany A.] Univ Calgary, Dept Kinesiol, Calgary, AB, Canada.
   [Northrup, Victoria; Perez, Lester J.; Edgett, Brittany A.; Karakach, Tobias; Simpson, Jeremy A.; Brunt, Keith R.] IMPART investigator team Canada, St John, NB, Canada.
C3 Dalhousie University; University of Guelph; University of Calgary
RP Brunt, KR (corresponding author), Dalhousie Univ, Dept Pharmacol, Halifax, NS, Canada.
EM Keith.brunt@dal.ca
RI Brunt, Keith/J-1052-2019; Perez, Lester J/A-1339-2016
OI Edgett, Brittany/0000-0002-8232-0432; Karakach,
   Tobias/0000-0003-2460-3781; Perez, Lester J/0000-0002-5717-5181;
   Northrup, Victoria/0000-0002-0254-5456
FU Natural Sciences and Engineering Research Council (NSERC)
   [RGPIN-(2020)-04878]; Killam Foundation Fellowship; NSERC Alexander
   Graham Bell Canada Graduate Scholarship-Doctoral (CGS D); New Brunswick
   Health Research Foundation; Beatrice Hunter Cancer Research Training
   Program Award
FX This study was supported by Natural Sciences and Engineering Research
   Council (NSERC) [grant #RGPIN-(2020)-04878] , (JAS & KRB) and Killam
   Foundation Fellowship (BAE) . VN was supported by the NSERC Alexander
   Graham Bell Canada Graduate Scholarship-Doctoral (CGS D) & the New
   Brunswick Health Research Foundation; Beatrice Hunter Cancer Research
   Training Program Award.
CR Adusumalli S, 2019, AGING CELL, V18, DOI 10.1111/acel.12928
   BARRON C, 1994, GENE, V147, P263, DOI 10.1016/0378-1119(94)90078-7
   Bonnas C, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-03167-0
   Braunschweig U, 2014, GENOME RES, V24, P1774, DOI 10.1101/gr.177790.114
   Buckley PT, 2011, NEURON, V69, P877, DOI 10.1016/j.neuron.2011.02.028
   Chen Zhilin, 2017, Front Biosci (Schol Ed), V9, P46
   De Conti L, 2013, WIRES RNA, V4, P49, DOI 10.1002/wrna.1140
   Edwards CR, 2016, BLOOD, V127, pE24, DOI 10.1182/blood-2016-01-692764
   Felkin LE, 2011, CIRCULATION, V123, P2838, DOI 10.1161/CIRCULATIONAHA.110.012211
   Furuichi Y, 2000, ADV VIRUS RES, V55, P135, DOI 10.1016/S0065-3527(00)55003-9
   Gontijo AM, 2011, NAT COMMUN, V2, DOI 10.1038/ncomms1328
   Grabski DF, 2021, WIRES RNA, V12, DOI 10.1002/wrna.1631
   Gudipati RK, 2012, MOL CELL, V48, P409, DOI 10.1016/j.molcel.2012.08.018
   Gunga HC, 1996, EUR J APPL PHYSIOL, V73, P11, DOI 10.1007/BF00262804
   GUY AL, 1978, P NATL ACAD SCI USA, V75, P6088, DOI 10.1073/pnas.75.12.6088
   Häsler R, 2011, EUR J CELL BIOL, V90, P603, DOI 10.1016/j.ejcb.2010.11.010
   Hall TA., 1999, NUCL ACIDS S SER, V41, P95, DOI [DOI 10.1021/BK-1999-0734.CH008, DOI 10.14344/IOC.ML.11.1]
   Hernando S, 2018, CURR DRUG DELIV, V15, P1218, DOI 10.2174/1567201815666180510103747
   Huynh JL, 2014, NAT NEUROSCI, V17, P121, DOI 10.1038/nn.3588
   Inoue D, 2021, NAT GENET, V53, P707, DOI 10.1038/s41588-021-00828-9
   Iommarini L, 2017, FRONT ONCOL, V7, DOI 10.3389/fonc.2017.00286
   Jaillon O, 2008, NATURE, V451, P359, DOI 10.1038/nature06495
   Korzeniewski S.J., 2017, Endogenous Erythropoietin, V1st, DOI [10.1016/bs.vh.2017.03.003, DOI 10.1016/BS.VH.2017.03.003]
   Lai WS, 2019, METHODS, V155, P77, DOI 10.1016/j.ymeth.2019.01.003
   Lee ST, 2012, J NEUROCHEM, V120, P115, DOI 10.1111/j.1471-4159.2011.07534.x
   Li HD, 2021, ALZHEIMERS DEMENT, V17, P984, DOI 10.1002/alz.12254
   Ma YY, 2022, FRONT PHARMACOL, V13, DOI 10.3389/fphar.2022.743926
   Mauger O, 2016, NEURON, V92, P1266, DOI 10.1016/j.neuron.2016.11.032
   Memon D, 2016, NPJ GENOM MED, V1, DOI 10.1038/npjgenmed.2016.20
   Middleton R, 2017, GENOME BIOL, V18, DOI 10.1186/s13059-017-1184-4
   Miyamoto O, 2000, NEUROLOGY, V54, P362, DOI 10.1212/WNL.54.2.362
   Monteuuis G, 2019, NUCLEIC ACIDS RES, V47, P11497, DOI 10.1093/nar/gkz1068
   Moyon S, 2016, CELL REP, V15, P748, DOI 10.1016/j.celrep.2016.03.060
   Naro C, 2017, DEV CELL, V41, P82, DOI 10.1016/j.devcel.2017.03.003
   Ngian ZK, 2022, P NATL ACAD SCI USA, V119, DOI 10.1073/pnas.2204179119
   Ni T, 2016, NUCLEIC ACIDS RES, V44, P6817, DOI 10.1093/nar/gkw591
   Ong CT, 2020, NEURAL REGEN RES, V15, P259, DOI 10.4103/1673-5374.265549
   Parenteau J, 2019, NATURE, V565, P612, DOI 10.1038/s41586-018-0859-7
   Passmore LA, 2022, NAT REV MOL CELL BIO, V23, P93, DOI 10.1038/s41580-021-00417-y
   Perrone B, 2020, CELL MOL NEUROBIOL, V40, P1, DOI 10.1007/s10571-019-00717-0
   Pimentel H, 2016, NUCLEIC ACIDS RES, V44, P838, DOI 10.1093/nar/gkv1168
   Rychlik W., 2007, OLIGO 7 Primer Analysis Software, DOI [10.1007/978-1-59745-528-2_2/FIGURES/2_14_978-1-59745-528-2, DOI 10.1007/978-1-59745-528-2_2/FIGURES/2_14_978-1-59745-528-2]
   Sakabe NJ, 2007, BMC GENOMICS, V8, DOI 10.1186/1471-2164-8-59
   Sun JH, 2019, NEUROMOL MED, V21, P12, DOI 10.1007/s12017-019-08524-y
   Vanichkina DP, 2018, SEMIN CELL DEV BIOL, V75, P40, DOI 10.1016/j.semcdb.2017.07.030
   Wong JJL, 2016, BIOESSAYS, V38, P41, DOI 10.1002/bies.201500117
   Wong JJL, 2013, CELL, V154, P583, DOI 10.1016/j.cell.2013.06.052
NR 47
TC 0
Z9 0
U1 0
U2 2
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
SN 0378-1119
EI 1879-0038
J9 GENE
JI Gene
PD MAR 10
PY 2024
VL 898
AR 148099
DI 10.1016/j.gene.2023.148099
EA DEC 2023
PG 9
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA FC1F0
UT WOS:001143451500001
PM 38128788
DA 2025-04-10
ER

PT J
AU He, DN
   Frost, AR
   Falany, CN
AF He, DN
   Frost, AR
   Falany, CN
TI Identification and immunohistochemical localization of Sulfotransferase
   2B1b (SULT2B1b) in human lung
SO BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
LA English
DT Article
DE sulfotransferase; lung; SULT2B1b; sulfation; immunohistochemical
   localization
ID DEHYDROEPIANDROSTERONE-SULFOTRANSFERASE; HUMAN LIVER; PHENOL
   SULFOTRANSFERASE; CYTOSOLIC SULFOTRANSFERASE; ESTROGEN ACTIVITY; HUMAN
   FETAL; EXPRESSION; SULFATION; PURIFICATION; METABOLISM
AB Sulfotransferase 2B1b (SULT2B1b) is a member of SULT 2 gene family. SUMB1a and SULT2B1b are transcribed from the same gene using different transcriptional start sites and contain different first exons as the result of alternative splicing. SULT2B1 a and SULT2B1b are 350 and 365 AA in length, respectively. Northern blot analysis and SULT2B1 isoform specific RT-PCR detected only SULT2B1 message in human lung tissue. Immunoblot analysis of human lung tissue with a specific rabbit anti-SUMB1 polyclonal antibody detected only SULT2B1b immunoreactive protein in human lung cytosol. Immunoprecipitation and MALDI mass spectroscopic analysis verified that the immunoreactive protein was SULT2B1b. Immunohistochemical localization of SULT2B1b in human tissues showed expression in the cytoplasm of ciliated columnar or cuboidal epithelial cells in terminal bronchia. No staining was observed in alveolar cells. SULT2B1b is selective for the sulfation of 3 beta-hydroxysteroids such as dehydroepiandrosterone and pregnenolone as well as cholesterol. The presence of SULT2B1b in lung tissues suggests a role in the regulation of local steroid hormone synthesis and metabolism. (c) 2005 Elsevier B.V All rights reserved.
C1 Univ Alabama Birmingham, Dept Pharmacol & Toxicol, Birmingham, AL 35249 USA.
   Univ Alabama Birmingham, Dept Pathol, Birmingham, AL 35249 USA.
C3 University of Alabama System; University of Alabama Birmingham;
   University of Alabama System; University of Alabama Birmingham
RP Univ Alabama Birmingham, Dept Pharmacol & Toxicol, 1670 Univ Blvd,Volker Hall,Room G133M, Birmingham, AL 35249 USA.
EM Charles.Falany@ccc.uab.edu
RI He, Dong/LBH-8540-2024
CR Adjei AA, 2003, BRIT J PHARMACOL, V139, P1373, DOI 10.1038/sj.bjp.0705369
   BECKMANN JD, 1994, J CELL PHYSIOL, V160, P603, DOI 10.1002/jcp.1041600324
   BECKMANN JD, 1993, CELL TISSUE RES, V274, P475, DOI 10.1007/BF00314544
   Beckmann JD, 1996, J CELL PHYSIOL, V166, P281, DOI 10.1002/(SICI)1097-4652(199602)166:2<281::AID-JCP5>3.0.CO;2-L
   COMER KA, 1992, MOL PHARMACOL, V41, P645
   Coughtrie M. W. H., 2002, Pharmacogenomics Journal, V2, P297
   Degano B, 2001, AM J RESP CRIT CARE, V164, P1849, DOI 10.1164/ajrccm.164.10.2102009
   Falany CN, 1995, ANN NY ACAD SCI, V774, P59, DOI 10.1111/j.1749-6632.1995.tb17372.x
   FALANY CN, 1995, J STEROID BIOCHEM, V52, P529, DOI 10.1016/0960-0760(95)00015-R
   Falany CN, 2005, METHOD PHARMACOL TOX, P341
   Falany CN, 2004, DRUG METAB REV, V36, P166
   FALANY CN, 1990, ARCH BIOCHEM BIOPHYS, V278, P312, DOI 10.1016/0003-9861(90)90265-Z
   Falany CN, 1997, FASEB J, V11, P206, DOI 10.1096/fasebj.11.4.9068609
   FALANY CN, 1994, J STEROID BIOCHEM, V48, P369, DOI 10.1016/0960-0760(94)90077-9
   Falany CN, 2000, BIOCHEM J, V346, P857, DOI 10.1042/0264-6021:3460857
   Falany JL, 1997, ONCOL RES, V9, P589
   Falany JL, 2004, J STEROID BIOCHEM, V88, P383, DOI 10.1016/j.jsbmb.2004.01.005
   Falany JL, 1998, CHEM-BIOL INTERACT, V109, P329, DOI 10.1016/S0009-2797(97)00143-9
   Falany JL, 2002, BREAST CANCER RES TR, V74, P167, DOI 10.1023/A:1016147004188
   Frost AR, 2000, APPL IMMUNOHISTO M M, V8, P236, DOI 10.1097/00022744-200009000-00011
   Geese WJ, 2001, BIOCHEM BIOPH RES CO, V288, P280, DOI 10.1006/bbrc.2001.5746
   HARLOW E, 1988, ANTIBODIES LABORATOR, P421
   Hartman AP, 1998, CHIRALITY, V10, P800, DOI 10.1002/(SICI)1520-636X(1998)10:9<800::AID-CHIR4>3.3.CO;2-M
   He DN, 2004, DRUG METAB REV, V36, P167
   He DN, 2004, BIOCHEM J, V379, P533, DOI 10.1042/BJ20031524
   Her C, 1998, GENOMICS, V53, P284, DOI 10.1006/geno.1998.5518
   Higashi Y, 2004, J INVEST DERMATOL, V122, P1207, DOI 10.1111/j.0022-202X.2004.22416.x
   Hume R, 2001, BIOL NEONATE, V80, P18, DOI 10.1159/000047172
   KINOSHITA T, 1992, ANAL BIOCHEM, V206, P231, DOI 10.1016/0003-2697(92)90358-E
   Kotov A, 1999, J STEROID BIOCHEM, V68, P137, DOI 10.1016/S0960-0760(99)00022-9
   LuuThe V, 1996, J ENDOCRINOL, V150, pS87
   Meloche CA, 2002, DRUG METAB DISPOS, V30, P582, DOI 10.1124/dmd.30.5.582
   Meloche CA, 2001, J STEROID BIOCHEM, V77, P261, DOI 10.1016/S0960-0760(01)00064-4
   Pacifici GM, 1997, EUR J DRUG METAB PH, V22, P253, DOI 10.1007/BF03189815
   Pacifici GM, 1997, XENOBIOTICA, V27, P279, DOI 10.1080/004982597240604
   Provost PR, 2000, ENDOCRINOLOGY, V141, P2786, DOI 10.1210/en.141.8.2786
   Rehman KS, 2003, J SOC GYNECOL INVEST, V10, P372, DOI 10.1016/S1071-5576(03)00118-7
   SCHAUSS SJ, 1995, BIOCHEM J, V311, P209, DOI 10.1042/bj3110209
   SHARP S, 1993, EUR J BIOCHEM, V211, P539, DOI 10.1111/j.1432-1033.1993.tb17580.x
   Tashiro A, 2000, J STEROID BIOCHEM, V72, P149, DOI 10.1016/S0960-0760(00)00020-0
   TORDAY JS, 1990, ENDOCRINOLOGY, V126, P3240, DOI 10.1210/endo-126-6-3240
   WALLE T, 1993, DRUG METAB DISPOS, V21, P76
   Wang J, 1998, MOL PHARMACOL, V53, P274, DOI 10.1124/mol.53.2.274
   Yanai H, 2004, CIRCULATION, V109, P92, DOI 10.1161/01.CIR.0000108925.95658.8D
   Yu Chun-Keung, 2002, Journal of Microbiology Immunology and Infection, V35, P199
NR 45
TC 26
Z9 37
U1 0
U2 2
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
SN 0304-4165
EI 1872-8006
J9 BBA-GEN SUBJECTS
JI Biochim. Biophys. Acta-Gen. Subj.
PD JUN 20
PY 2005
VL 1724
IS 1-2
BP 119
EP 126
DI 10.1016/j.bbagen.2005.03.018
PG 8
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA 940YS
UT WOS:000230182400013
PM 15878639
DA 2025-04-10
ER

PT J
AU Dube, DK
   Dube, S
   Shi, HY
   Benz, P
   Randhawa, S
   Fan, YL
   Wang, JS
   Ma, Z
   Sanger, JW
   Sanger, JM
   Poiesz, BJ
AF Dube, Dipak K.
   Dube, Syamalima
   Shi, Huaiyu
   Benz, Patricia
   Randhawa, Samender
   Fan, Yingli
   Wang, Jusuo
   Ma, Zhen
   Sanger, Joseph W.
   Sanger, Jean M.
   Poiesz, Bernard J.
TI Sarcomeric tropomyosin expression during human iPSC differentiation into
   cardiomyocytes
SO CYTOSKELETON
LA English
DT Article
DE hiPSC-derived cardiomyocytes; LC-MS/MS; qRT-PCR; TPM1 alpha; TPM1 mu
ID NEBULIN FAMILY; HEART; PROTEINS; ISOFORMS; BINDING; ROLES; CELLS
AB Tropomyosin (TPM) is an essential sarcomeric component, stabilizing the thin filament and facilitating actin's interaction with myosin. In mammals, including humans, there are four TPM genes (TPM1, TPM2, TPM3, and TPM4) each of which generates a multitude of TPM isoforms via alternative splicing and using different promoters. In this study, we have examined the expression of transcripts as well as proteins of various sarcomeric TPM isoforms during human inducible pluripotent stem cell differentiation into cardiomyocytes. During the differentiation time course, we harvested cells on Days 0, 5, 10, 15, and 20 to analyze for various sarcomeric TPM transcripts by qRT-PCR and for sarcomeric TPM proteins using two-dimensional Western blot with sarcomeric TPM-specific CH1 monoclonal antibody followed by mass spectra analyses. Our results show increasing levels of total TPM transcripts and proteins during the period of differentiation, but varying levels of specific TPM isoforms during the same period. By Day 20, the rank order of TPM transcripts was TPM1 alpha > TPM1 kappa > TPM2 alpha > TPM1 mu > TPM3 alpha > TPM4 alpha. TPM1 alpha was the dominant protein produced with some TPM2 and much less TPM1 kappa and mu. Interestingly, small amounts of two lower molecular weight TPM3 isoforms were detected on Day 15. To the best of our knowledge this is the first demonstration of TPM1 mu non-muscle isoform protein expression before and during cardiac differentiation.
C1 [Dube, Dipak K.; Dube, Syamalima; Benz, Patricia; Randhawa, Samender; Poiesz, Bernard J.] SUNY Upstate Med Univ, Dept Med, 750 East Adams St, Syracuse, NY 13210 USA.
   [Shi, Huaiyu; Ma, Zhen] Syracuse Univ, Dept Biomed & Chem Engn, Syracuse, NY USA.
   [Fan, Yingli; Wang, Jusuo; Sanger, Joseph W.; Sanger, Jean M.] SUNY Upstate Med Univ, Dept Cell & Dev Biol, Syracuse, NY 13210 USA.
C3 State University of New York (SUNY) System; State University of New York
   (SUNY) Upstate Medical Center; Syracuse University; State University of
   New York (SUNY) System; State University of New York (SUNY) Upstate
   Medical Center
RP Dube, DK (corresponding author), SUNY Upstate Med Univ, Dept Med, 750 East Adams St, Syracuse, NY 13210 USA.
EM dubed@upstate.edu
OI Sanger, Joesph/0000-0002-2281-8490
FU NIAMS grant [R01 AR-57063]; NIAMS; Hendricks Fund; SUNY Upstate Medical
   University [NSF CMMI-2130192]; SUNY Upstate Medical University Cancer
   Center
FX The work was supported by a NIAMS grant (R01 AR-57063) awarded to Jean
   M. Sanger and Joseph W. Sanger. Joseph W. Sanger was also supported by
   the Hendricks Fund, SUNY Upstate Medical University. Grant support from
   the SUNY Upstate Medical University Cancer Center Fund was essential for
   experiments undertaken for this report (Jusuo Wang, Bernard J. Poiesz,
   Dipak K. Dube, Jean M. Sanger, and Joseph W. Sanger). This work was also
   supported by the following grants: NSF CMMI-2130192 to Zhen Ma; Barbara
   Kopp Cancer Research Fund to Bernard J. Poiesz. We are grateful to Lori
   Spicer for help with manuscript preparation and revisions.
CR [Anonymous], 2020, ACS APPL MAT, V12
   [Anonymous], 2009, CARDIOVASC TOXICOL, V9
   Bang ML, 2015, CIRC J, V79, P2081, DOI 10.1253/circj.CJ-15-0854
   Bonzo JR, 2008, EXP CELL RES, V314, P3519, DOI 10.1016/j.yexcr.2008.09.001
   Darie CC, 2011, PROTEOMICS, V11, P4514, DOI 10.1002/pmic.201000819
   Dube DK, 2023, BIOCHEM RES INT, V2023, DOI 10.1155/2023/1303500
   Dube DK, 2020, CYTOSKELETON, V77, P313, DOI 10.1002/cm.21629
   Dube DK, 2018, CYTOSKELETON, V75, P437, DOI 10.1002/cm.21495
   Dube DK, 2017, CYTOSKELETON, V74, P125, DOI 10.1002/cm.21352
   Dube DK., 2016, MOL BIOL INT, V2016, P3105478, DOI [DOI 10.1155/2016/3105478, 10.1155/2016/3105478]
   Dube S, 2015, INT J BREAST CANCER, V2015, DOI 10.1155/2015/859427
   England J, 2017, J MOL CELL CARDIOL, V106, P1, DOI 10.1016/j.yjmcc.2017.03.006
   Geeves MA, 2015, J MUSCLE RES CELL M, V36, P147, DOI 10.1007/s10974-014-9389-6
   Gunning P, 2008, PHYSIOL REV, V88, P1, DOI 10.1152/physrev.00001.2007
   Hammell RL, 1997, J BIOL CHEM, V272, P22409, DOI 10.1074/jbc.272.36.22409
   Han ELY, 2019, CELL REP, V29, P3751, DOI 10.1016/j.celrep.2019.11.026
   Helfman DM, 1999, J CELL SCI, V112, P371
   Kuo CT, 1997, GENE DEV, V11, P1048, DOI 10.1101/gad.11.8.1048
   LEESMILLER JP, 1991, BIOESSAYS, V13, P429, DOI 10.1002/bies.950130902
   Lian XJ, 2012, P NATL ACAD SCI USA, V109, pE1848, DOI 10.1073/pnas.1200250109
   LINTS TJ, 1993, DEVELOPMENT, V119, P419
   MANN HB, 1947, ANN MATH STAT, V18, P50, DOI 10.1214/aoms/1177730491
   Nefedova VV, 2019, BIOCHEM BIOPH RES CO, V514, P613, DOI 10.1016/j.bbrc.2019.05.008
   Pappas CT, 2011, TRENDS CELL BIOL, V21, P29, DOI 10.1016/j.tcb.2010.09.005
   Rajan S, 2010, CIRCULATION, V121, P410, DOI 10.1161/CIRCULATIONAHA.109.889725
   Schevzov Galina, 2011, Bioarchitecture, V1, P135
   Shevchenko A, 1996, ANAL CHEM, V68, P850, DOI 10.1021/ac950914h
   Sokolowska I, 2012, PROTEOME SCI, V10, DOI 10.1186/1477-5956-10-47
   Strausberg RL, 2001, P NATL ACAD SCI USA, V98, P11837, DOI 10.1073/pnas.221463598
   Thomas A, 2010, J CELL BIOCHEM, V110, P875, DOI 10.1002/jcb.22599
   Wang JS, 2021, CYTOSKELETON, V78, P461, DOI 10.1002/cm.21697
   Wang JS, 2012, CYTOSKELETON, V69, P1021, DOI 10.1002/cm.21058
NR 32
TC 0
Z9 0
U1 3
U2 3
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 1949-3584
EI 1949-3592
J9 CYTOSKELETON
JI Cytoskeleton
PD SEP
PY 2024
VL 81
IS 9-10
BP 448
EP 472
DI 10.1002/cm.21850
EA MAR 2024
PG 25
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA K0W5J
UT WOS:001182591400001
PM 38470291
DA 2025-04-10
ER

PT J
AU Quade-Lyssy, P
   Kanarek, AM
   Baiersdörfer, M
   Postina, R
   Kojro, E
AF Quade-Lyssy, Patricia
   Kanarek, Anna Maria
   Baiersdoerfer, Markus
   Postina, Rolf
   Kojro, Elzbieta
TI Statins stimulate the production of a soluble form of the receptor for
   advanced glycation end products
SO JOURNAL OF LIPID RESEARCH
LA English
DT Article
DE hypercholesterolemia; diabetic complications; atherosclerosis; ADAM 10
ID CARDIOVASCULAR-DISEASE; CHOLESTEROL DEPLETION; ALZHEIMER-DISEASE;
   PRIMARY PREVENTION; PLASMA-MEMBRANE; RAGE RECEPTOR; ATORVASTATIN; RISK;
   ATHEROSCLEROSIS; PHARMACOKINETICS
AB The beneficial effects of statin therapy in the reduction of cardiovascular pathogenesis, atherosclerosis, and diabetic complications are well known. The receptor for advanced glycation end products (RAGE) plays an important role in the progression of these diseases. In contrast, soluble forms of RAGE act as decoys for RAGE ligands and may prevent the development of RAGE-mediated disorders. Soluble forms of RAGE are either produced by alternative splicing [endogenous secretory RAGE (esRAGE)] or by proteolytic shedding mediated by metalloproteinases [shed RAGE (sRAGE)]. Therefore we analyzed whether statins influence the production of soluble RAGE. Lovastatin treatment of either mouse alveolar epithelial cells endogenously expressing RAGE or HEK cells overexpressing RAGE caused induction of RAGE shedding, but did not influence secretion of esRAGE from HEK cells overexpressing esRAGE. Lovastatin-induced secretion of sRAGE was also evident after restoration of the isoprenylation pathway, demonstrating a correlation of sterol biosynthesis and activation of RAGE shedding. Lovastatin-stimulated induction of RAGE shedding was completely abolished by a metalloproteinase ADAM10 inhibitor. We also demonstrate that statins stimulate RAGE shedding at low physiologically relevant concentrations. Our results show that statins, due to their cholesterol-lowering effects, increase the soluble RAGE level by inducing RAGE shedding, and by doing this, might prevent the development of RAGE-mediated pathogenesis
C1 [Quade-Lyssy, Patricia; Kanarek, Anna Maria; Baiersdoerfer, Markus; Postina, Rolf; Kojro, Elzbieta] Johannes Gutenberg Univ Mainz, Inst Pharm & Biochem, D-55128 Mainz, Germany.
C3 Johannes Gutenberg University of Mainz
RP Kojro, E (corresponding author), Johannes Gutenberg Univ Mainz, Inst Pharm & Biochem, D-55128 Mainz, Germany.
EM kojro@uni-mainz.de
FU Alzheimer Forschung Initiative e.V. (Dusseldorf, Germany) [07807]
FX This work was supported by grant 07807 to E. K. from the Alzheimer
   Forschung Initiative e.V. (Dusseldorf, Germany).
CR Abbas A, 2012, CLIN MED INSIGHTS-EN, V5, P13, DOI 10.4137/CMED.S7591
   Barlovic Drazenka P., 2010, Cardiovascular & Hematological Disorders - Drug Targets, V10, P7
   Bierhaus A, 2005, J MOL MED, V83, P876, DOI 10.1007/s00109-005-0688-7
   Bucciarelli LG, 2002, CELL MOL LIFE SCI, V59, P1117, DOI 10.1007/s00018-002-8491-x
   Bucciarelli LG, 2002, CIRCULATION, V106, P2827, DOI 10.1161/01.CIR.0000039325.03698.36
   Butterfield DA, 2011, PHARMACOL RES, V64, P180, DOI 10.1016/j.phrs.2011.04.007
   Colhoun HM, 2011, DIABETES, V60, P2379, DOI 10.2337/db11-0291
   Colhoun HM, 2004, LANCET, V364, P685, DOI 10.1016/S0140-6736(04)16895-5
   Corsini A, 1999, PHARMACOL THERAPEUT, V84, P413, DOI 10.1016/S0163-7258(99)00045-5
   Cuccurullo C, 2006, ARTERIOSCL THROM VAS, V26, P2716, DOI 10.1161/01.ATV.0000249630.02085.12
   CUTTS JL, 1988, BIOCHIM BIOPHYS ACTA, V961, P65, DOI 10.1016/0005-2760(88)90131-2
   Deane R, 2003, NAT MED, V9, P907, DOI 10.1038/nm890
   Feng B, 2011, BBA-MOL BASIS DIS, V1812, P1130, DOI 10.1016/j.bbadis.2011.05.007
   Fujisawa K, 2013, ATHEROSCLEROSIS, V227, P425, DOI 10.1016/j.atherosclerosis.2013.01.016
   Galichet A, 2008, BIOCHEM BIOPH RES CO, V370, P1, DOI 10.1016/j.bbrc.2008.02.163
   Goova MT, 2001, AM J PATHOL, V159, P513, DOI 10.1016/S0002-9440(10)61723-3
   Haag MDM, 2009, J NEUROL NEUROSUR PS, V80, P13, DOI 10.1136/jnnp.2008.150433
   Hoettecke N, 2010, NEURODEGENER DIS, V7, P232, DOI 10.1159/000267865
   Hudson BI, 2011, ATHEROSCLEROSIS, V216, P192, DOI 10.1016/j.atherosclerosis.2011.01.024
   Ilangumaran S, 1998, BIOCHEM J, V335, P433, DOI 10.1042/bj3350433
   Jick H, 2000, LANCET, V356, P1627, DOI 10.1016/S0140-6736(00)03155-X
   Jinnouchi Y, 2006, CLIN EXP MED, V6, P191, DOI 10.1007/s10238-006-0115-6
   Kojro E, 2001, P NATL ACAD SCI USA, V98, P5815, DOI 10.1073/pnas.081612998
   Kojro E, 2010, J ALZHEIMERS DIS, V20, P1215, DOI 10.3233/JAD-2010-091621
   Li JF, 1997, J BIOL CHEM, V272, P16498, DOI 10.1074/jbc.272.26.16498
   Lindsey JB, 2009, DIABETES CARE, V32, P1218, DOI 10.2337/dc09-0053
   Lu L, 2011, J ZHEJIANG UNIV-SC B, V12, P652, DOI 10.1631/jzus.B1101004
   Matthews V, 2003, J BIOL CHEM, V278, P38829, DOI 10.1074/jbc.M210584200
   Metz VV, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0041823
   PAN HY, 1990, J CLIN PHARMACOL, V30, P1128, DOI 10.1002/j.1552-4604.1990.tb01856.x
   Park' L, 1998, NAT MED, V4, P1025, DOI 10.1038/2012
   Posvar EL, 1996, J CLIN PHARMACOL, V36, P728, DOI 10.1002/j.1552-4604.1996.tb04242.x
   Raucci A, 2008, FASEB J, V22, P3716, DOI 10.1096/fj.08-109033
   Ridker PM, 2012, LANCET, V380, P565, DOI 10.1016/S0140-6736(12)61190-8
   Santilli F, 2007, FREE RADICAL BIO MED, V43, P1255, DOI 10.1016/j.freeradbiomed.2007.06.017
   Schlueter C, 2003, BBA-GENE STRUCT EXPR, V1630, P1, DOI 10.1016/j.bbaexp.2003.08.008
   Selvin E, 2013, DIABETES, V62, P2116, DOI 10.2337/db12-1528
   Soro-Paavonen A, 2008, DIABETES, V57, P2461, DOI 10.2337/db07-1808
   Tam HL, 2010, ATHEROSCLEROSIS, V209, P173, DOI 10.1016/j.atherosclerosis.2009.08.031
   TARABOULOS A, 1995, J CELL BIOL, V129, P121, DOI 10.1083/jcb.129.1.121
   TSE FLS, 1992, J CLIN PHARMACOL, V32, P630, DOI 10.1002/j.1552-4604.1992.tb05773.x
   Ueno H, 2010, ATHEROSCLEROSIS, V211, P431, DOI 10.1016/j.atherosclerosis.2010.04.006
   Wautier JL, 1996, J CLIN INVEST, V97, P238, DOI 10.1172/JCI118397
   Wolozin B, 2000, ARCH NEUROL-CHICAGO, V57, P1439, DOI 10.1001/archneur.57.10.1439
   Yonekura H, 2003, BIOCHEM J, V370, P1097, DOI 10.1042/BJ20021371
   Zhang L, 2008, J BIOL CHEM, V283, P35507, DOI 10.1074/jbc.M806948200
   Zimina EP, 2005, J BIOL CHEM, V280, P34019, DOI 10.1074/jbc.M503751200
NR 47
TC 53
Z9 54
U1 0
U2 9
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
SN 0022-2275
EI 1539-7262
J9 J LIPID RES
JI J. Lipid Res.
PD NOV
PY 2013
VL 54
IS 11
BP 3052
EP 3061
DI 10.1194/jlr.M038968
PG 10
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 301LS
UT WOS:000330534400012
PM 23966666
OA Green Published, hybrid
DA 2025-04-10
ER

PT J
AU Sun, LH
   Bai, KH
   Wu, GY
   Tian, XP
   Zou, ZQ
   Wang, DW
   Dai, YJ
   Chen, SL
AF Sun, Li-Hua
   Bai, Kun-Hao
   Wu, Guo-Yan
   Tian, Xiao-Peng
   Zou, Zhi-Qing
   Wang, Da-Wei
   Dai, Yu-Jun
   Chen, Si-Liang
TI Mechanism of Abnormal Coagulation Induced by Tigecycline in Cancer
   Patients
SO FRONTIERS IN PHARMACOLOGY
LA English
DT Article
DE tigecycline; abnormal coagulation; cancer; RNA-Seq; CHO
ID ACUTE MYELOID-LEUKEMIA; MULTICENTER; INHIBITION; THROMBOSIS; CHILDREN
AB Tigecycline is a broad-spectrum active intravenous antibiotic that is active against methicillin-resistant staphylococcus aureus. In Phase 3 and 4 clinical trials, increased all-cause mortality was observed in patients treated with tigecycline compared to patients in the control group. The reason for the increase is unclear. In this study, we found that tigecycline cause abnormal coagulation in tumor patients, especially in patients with hematological malignancies. The main manifestations were decreased fibrinogen and prolonged activated prothrombin time (APTT), thrombin time (TT), and D-dimer. In addition, through functional studies, we found that tigecycline inhibit platelet adhesion and aggregation, and the coagulation function of patients gradually recover after discontinuation. Gene sequencing results suggested that tigecycline significantly regulate the expression of genes related to platelet function pathways and increase the incidence of single nucleotide polymorphisms and the number of alternative splices in the Chinese hamster ovary (CHO) cells treated with tigecycline. An abnormal function and low numbers of platelets are common in patients with hematological malignancies. Our study can explain the mechanism of abnormal coagulation caused by tigecycline. Additionally, doctors who apply tigecycline to cure infections in tumor patients should be warned.
C1 [Sun, Li-Hua; Chen, Si-Liang] Peking Univ, Shenzhen Hosp, Dept Hematol, Shenzhen, Peoples R China.
   [Bai, Kun-Hao; Zou, Zhi-Qing; Dai, Yu-Jun] Collaborat Innovat Ctr Canc Med, State Key Lab Oncol South China, Guangzhou, Peoples R China.
   [Bai, Kun-Hao] Sun Yat Sen Univ, Canc Ctr, Dept Endoscopy, Guangzhou, Peoples R China.
   [Wu, Guo-Yan] Shanghai Jiao Tong Univ, Shanghai Gen Hosp, Dept Crit Care Med, Sch Med, Shanghai, Peoples R China.
   [Tian, Xiao-Peng] Soochow Univ, Affiliated Hosp 1, Jiangsu Inst Hematol, Suzhou, Peoples R China.
   [Wang, Da-Wei] Shanghai Jiao Tong Univ, Ruijin Hosp, Natl Res Ctr Translat Med Shanghai, Shanghai Inst Hematol,State Key Lab Med Genom,Sch, Shanghai, Peoples R China.
   [Dai, Yu-Jun] Sun Yat Sen Univ, Canc Ctr, Dept Hematol Oncol, Guangzhou, Peoples R China.
C3 Peking University; State Key Lab Oncology South China; Sun Yat Sen
   University; Shanghai Jiao Tong University; Soochow University - China;
   Shanghai Jiao Tong University; Chinese Academy of Sciences; Sun Yat Sen
   University
RP Chen, SL (corresponding author), Peking Univ, Shenzhen Hosp, Dept Hematol, Shenzhen, Peoples R China.; Dai, YJ (corresponding author), Collaborat Innovat Ctr Canc Med, State Key Lab Oncol South China, Guangzhou, Peoples R China.; Dai, YJ (corresponding author), Sun Yat Sen Univ, Canc Ctr, Dept Hematol Oncol, Guangzhou, Peoples R China.
EM daiyj@sysucc.org.cn; chensiliang@tom.com
OI Bai, Kunhao/0000-0003-1184-7576
FU National Natural Science Foundation of China [82000144]
FX Funding This work was supported by the National Natural Science
   Foundation of China (82000144).
CR Alsaad N, 2014, EUR RESPIR J, V43, P884, DOI 10.1183/09031936.00113713
   Bochennek K, 2016, BLOOD CANCER J, V6, DOI 10.1038/bcj.2015.110
   Brandtner A, 2020, ANTIBIOTICS-BASEL, V9, DOI 10.3390/antibiotics9020084
   Bucaneve G, 2014, J CLIN ONCOL, V32, P1463, DOI 10.1200/JCO.2013.51.6963
   Cai Y, 2011, LANCET INFECT DIS, V11, P804, DOI 10.1016/S1473-3099(11)70183-9
   Chatzidimitriou C, 2021, AM J HEMATOL, V96, P632, DOI 10.1002/ajh.26145
   Chen SL, 2020, DNA CELL BIOL, V39, P2040, DOI 10.1089/dna.2020.5392
   Cui NN, 2019, INT J CLIN PHARM-NET, V41, P1408, DOI 10.1007/s11096-019-00912-5
   Erman M, 2004, ANN ONCOL, V15, P1622, DOI 10.1093/annonc/mdh437
   Grant MA, 2017, BLOOD, V130, P2548, DOI 10.1182/blood-2017-02-770792
   Guo MX, 2022, THROMB J, V20, DOI 10.1186/s12959-022-00369-z
   Guo YP, 2021, FRONT NEUROL, V12, DOI 10.3389/fneur.2021.712024
   Halim TY, 2007, ANN ONCOL, V18, P1246, DOI 10.1093/annonc/mdm112
   Huang JS, 2015, J HEMATOL ONCOL, V8, DOI 10.1186/s13045-015-0159-8
   Ji SD, 2017, J HEMATOL ONCOL, V10, DOI 10.1186/s13045-017-0475-2
   Karlström C, 2022, BRIT J HAEMATOL, V196, P224, DOI 10.1111/bjh.17820
   Kumarasamy KK, 2010, LANCET INFECT DIS, V10, P597, DOI 10.1016/S1473-3099(10)70143-2
   Leng B, 2019, CHEM PHARM BULL, V67, P258, DOI 10.1248/cpb.c18-00844
   Libourel EJ, 2016, BLOOD, V128, P1854, DOI 10.1182/blood-2016-02-701094
   Miles MVP, 2022, J TRAUMA ACUTE CARE, V92, P701, DOI 10.1097/TA.0000000000003516
   Montravers P, 2014, INTENS CARE MED, V40, P988, DOI 10.1007/s00134-014-3323-7
   Ahmad JAN, 2022, CLIN NUCL MED, V47, P409, DOI 10.1097/RLU.0000000000004130
   Provinciali M, 2011, J MED MICROBIOL, V60, P1806, DOI 10.1099/jmm.0.032516-0
   Röllig C, 2015, BLOOD, V125, P3246, DOI 10.1182/blood-2014-10-551507
   Sekar PK, 2022, BIOSENS BIOELECTRON, V197, DOI 10.1016/j.bios.2021.113786
   Senior K, 2005, LANCET INFECT DIS, V5, P474, DOI 10.1016/S1473-3099(05)70179-1
   Skrtic M, 2011, CANCER CELL, V20, P674, DOI 10.1016/j.ccr.2011.10.015
   TESTA JR, 1978, BLOOD, V52, P272
   Tramsen L, 2016, J CLIN ONCOL, V34, P2776, DOI 10.1200/JCO.2016.66.7881
   Vinholt PJ, 2019, AM J HEMATOL, V94, P891, DOI 10.1002/ajh.25512
   Wang YM, 2014, J CLIN INVEST, V124, P4281, DOI 10.1172/JCI74630
   Wu JM, 2006, NUCLEIC ACIDS RES, V34, pW720, DOI 10.1093/nar/gkl167
   Zheng Z, 2020, J CLIN INVEST, V130, P4348, DOI 10.1172/JCI135919
   Zimdahl H, 2004, SCIENCE, V303, P807, DOI 10.1126/science.1092427
NR 34
TC 2
Z9 2
U1 1
U2 8
PU FRONTIERS MEDIA SA
PI LAUSANNE
PA AVENUE DU TRIBUNAL FEDERAL 34, LAUSANNE, CH-1015, SWITZERLAND
EI 1663-9812
J9 FRONT PHARMACOL
JI Front. Pharmacol.
PD JUL 5
PY 2022
VL 13
AR 891952
DI 10.3389/fphar.2022.891952
PG 10
WC Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Pharmacology & Pharmacy
GA 3C4ZQ
UT WOS:000828633000001
PM 35865948
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Estrada, FJ
   Mornet, D
   Rosas-Vargas, H
   Angulo, A
   Hernández, M
   Becker, V
   Rendón, A
   Ramos-Kuri, M
   Coral-Vázquez, RM
AF Estrada, FJ
   Mornet, D
   Rosas-Vargas, H
   Angulo, A
   Hernández, M
   Becker, V
   Rendón, A
   Ramos-Kuri, M
   Coral-Vázquez, RM
TI A novel isoform of δ-sarcoglycan is localized at the sarcoplasmic
   reticulum of mouse skeletal muscle
SO BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
LA English
DT Article
DE sarcoglycan-sarcospan complex; delta-sarcoglycan isoform; sarcoplasmic
   reticulum; skeletal muscle
ID DYSTROPHIN-GLYCOPROTEIN COMPLEX; GIRDLE MUSCULAR-DYSTROPHY;
   EPSILON-SARCOGLYCAN; SMOOTH-MUSCLE; ALPHA-SARCOGLYCAN; GENE; COMPONENT;
   MUTATIONS; SARCOSPAN; 2D
AB The sarcoglycan-sarcospan complex (alpha-, beta-, gamma-, delta-, epsilon-, and zeta-SG-SSPN), a component of the dystrophin-associated glycoprotein complex (DAGC), is located at the sarcolemma Of Muscle fibers where it contributes to maintain cell integrity during contraction-relaxation cycles; gamma- and delta-SG are also expressed in the sarcoplasmic reticulum (SR). In this study, we report the identification of a novel isoform of murine delta-SG produced by alternative splicing that we named delta-SG3. This isoform is present at transcript level in several tissues, with its highest expression in skeletal and cardiac muscle. The delta-SG3 protein lacks the last 122 amino acids at the C-terminal, which are replaced by 10 new amino acids (EGFLNMQLAG). Interestingly, double immunofluorescence analysis for delta-SG3 and the dihydropyridine receptor (DHPR) shows a close localization of these two proteins. We propose the subcellular distribution of this novel delta-SG3 isoform at the SR and its involvement in intracellular calcium concentration regulation. (c) 2005 Elsevier Inc. All rights reserved.
C1 Ctr Med Nacl Siglo, XXI, IMSS, Hosp Pediat,Unidad Invest Med Genet Humana, Mexico City 06725, DF, Mexico.
   Univ Panamericana, Escuela Med, Mol Biol Lab, Mexico City, DF, Mexico.
   IPN, Escuela Nacl Ciencias Biol, Mexico City, DF, Mexico.
   Inst Biol, Dept Physiol Interact EA 701, F-34060 Montpellier, France.
   Hop St Antoine, Lab Physiopathol Cellulaire & Mol Retine, INSERM U592, F-75571 Paris, France.
C3 Instituto Mexicano del Seguro Social; Universidad Panamericana - Ciudad
   de Mexico; Instituto Politecnico Nacional - Mexico; Institut National de
   la Sante et de la Recherche Medicale (Inserm); Assistance Publique
   Hopitaux Paris (APHP); Sorbonne Universite; Hopital Universitaire
   Saint-Antoine - APHP
RP Ctr Med Nacl Siglo, XXI, IMSS, Hosp Pediat,Unidad Invest Med Genet Humana, Av Cuauhtemoc 330, Mexico City 06725, DF, Mexico.
EM rmcoralv@prodigy.net.mx
RI Rosas-Vargas, Haydee/ISS-9640-2023; Estrada-Mena,
   Francisco/AAI-2437-2020; Rendon, Alvaro/A-1127-2012; Coral,
   RamÃ³n/HLQ-1611-2023
OI Hernandez-Hernandez, Jose Manuel/0000-0001-7624-9986; Estrada, Francisco
   Javier/0000-0002-0833-3630; Rosas-Vargas, Haydee/0000-0003-0635-8284;
   Coral-Vazquez, Ramon Mauricio/0000-0001-6126-2002
CR Anastasi G, 2005, INT J MOL MED, V16, P367
   Angelini C, 2002, Basic Appl Myol, P17
   BEAM KG, 1989, ANN NY ACAD SCI, V560, P127, DOI 10.1111/j.1749-6632.1989.tb24090.x
   Chan YM, 1998, J CELL BIOL, V143, P2033, DOI 10.1083/jcb.143.7.2033
   Coral-Vazquez R, 1999, CELL, V98, P465, DOI 10.1016/S0092-8674(00)81975-3
   Crosbie RH, 1997, J BIOL CHEM, V272, P31221, DOI 10.1074/jbc.272.50.31221
   Ettinger AJ, 1997, J BIOL CHEM, V272, P32534, DOI 10.1074/jbc.272.51.32534
   Hack AA, 2000, MICROSC RES TECHNIQ, V48, P167, DOI 10.1002/(SICI)1097-0029(20000201/15)48:3/4<167::AID-JEMT5>3.0.CO;2-T
   Holt KH, 1998, J BIOL CHEM, V273, P34667, DOI 10.1074/jbc.273.52.34667
   Iwata Y, 2005, BIOCHEM PHARMACOL, V70, P740, DOI 10.1016/j.bcp.2005.05.034
   Jung D, 1996, J BIOL CHEM, V271, P32321, DOI 10.1074/jbc.271.50.32321
   MANTTARI S, 2005, DIHIDROPYRIDINE RECE
   Manttari Satu, 2005, BMC Physiol, V5, P4, DOI 10.1186/1472-6793-5-4
   McNally EM, 1996, HUM MOL GENET, V5, P1841, DOI 10.1093/hmg/5.11.1841
   McNally EM, 1998, FEBS LETT, V422, P27, DOI 10.1016/S0014-5793(97)01593-7
   Nigro V, 1996, HUM MOL GENET, V5, P1179, DOI 10.1093/hmg/5.8.1179
   Rivier F, 1999, J MUSCLE RES CELL M, V20, P305, DOI 10.1023/A:1005426920070
   Sakamoto A, 1999, FEBS LETT, V447, P124, DOI 10.1016/S0014-5793(99)00267-7
   Sciandra Francesca, 2003, Ann Ist Super Sanita, V39, P173
   Shi WX, 2004, MUSCLE NERVE, V29, P409, DOI 10.1002/mus.10566
   Straub V, 1999, J BIOL CHEM, V274, P27989, DOI 10.1074/jbc.274.39.27989
   Straub V, 1997, CURR OPIN NEUROL, V10, P168, DOI 10.1097/00019052-199704000-00016
   Ueda H, 2001, J HISTOCHEM CYTOCHEM, V49, P529, DOI 10.1177/002215540104900413
   UEYAMA T, 1998, AM J PHYSIOL, V274, P1
   Wheeler MT, 2002, HUM MOL GENET, V11, P2147, DOI 10.1093/hmg/11.18.2147
   Zimprich A, 2001, NAT GENET, V29, P66, DOI 10.1038/ng709
NR 26
TC 11
Z9 11
U1 0
U2 5
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0006-291X
EI 1090-2104
J9 BIOCHEM BIOPH RES CO
JI Biochem. Biophys. Res. Commun.
PD FEB 17
PY 2006
VL 340
IS 3
BP 865
EP 871
DI 10.1016/j.bbrc.2005.12.083
PG 7
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA 009DR
UT WOS:000235092000019
PM 16403451
OA Green Submitted, Green Accepted
DA 2025-04-10
ER

PT J
AU Ivanova, A
   Agochiya, M
   Amoyel, M
   Richardson, WD
AF Ivanova, A
   Agochiya, M
   Amoyel, M
   Richardson, WD
TI Receptor tyrosine phosphatase zeta/beta in astrocyte progenitors in the
   developing chick spinal cord
SO GENE EXPRESSION PATTERNS
LA English
DT Article
DE astrocyte; central nervous system; chick; development; FGFR3; glial
   cell; glutamine synthetase; in situ hybridization; neural precursor;
   oligodendrocyte; PDGFRalpha; phosphacan; spinal cord; tyrosine
   phosphatase
ID CHONDROITIN SULFATE PROTEOGLYCAN; CELL-ADHESION MOLECULES; RPTP-BETA;
   NERVOUS-SYSTEM; PTP-ZETA; BRAIN; EXPRESSION; DOMAIN; NEUROCAN; GLIA
AB We cloned a cDNA encoding the receptor-type protein tyrosine phosphatase zeta/beta (RPTPZ/beta) from embryonic chick spinal cord. RPTPZ/beta was expressed throughout the ventricular zone (VZ) of the developing spinal cord and in scattered cells outside the VZ. Platelet-derived growth factor receptor alpha (PDGFRa)-positive oligodendrocyte progenitors co-expressed RPTPZ/beta within the VZ but down-regulated RPTPZ/beta after leaving the VZ. Most RPTPZ/beta-positive Cells Outside the VZ co-expressed glutamine synthetase and fibroblast growth factor receptor-3, indicating that they are astrocyte progenitors. Northern blot analysis revealed a single similar to9 kbp RPTPZ/beta transcript expressed in the embryonic chick spinal cord, indicating that the shorter alternative-splice products of RPTPZ/beta found in rodent spinal cord and brain-including the abundant extracellular proteoglycan known as phosphacan-are not present in the embryonic chick spinal cord. (C) 2003 Elsevier B.V. All rights reserved.
C1 UCL, Wolfson Inst Biomed Res, London WC1E 6BT, England.
   UCL, Dept Biol, London WC1E 6BT, England.
C3 University of London; University College London; University of London;
   University College London
RP Richardson, WD (corresponding author), UCL, Wolfson Inst Biomed Res, Gower St, London WC1E 6BT, England.
EM w.richardson@ucl.ac.uk
RI Amoyel, Marc/GLR-0962-2022; Richardson FMedSci FRS, William
   D/C-1762-2008
OI Richardson FMedSci FRS, William D/0000-0001-7261-2485; Amoyel,
   Marc/0000-0002-2691-2097
CR Adamsky K, 2001, ONCOGENE, V20, P609, DOI 10.1038/sj.onc.1204119
   Canoll PD, 1996, J NEUROSCI RES, V44, P199, DOI 10.1002/(SICI)1097-4547(19960501)44:3<199::AID-JNR1>3.0.CO;2-B
   CHORNCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156
   Hall A, 1996, DEVELOPMENT, V122, P4085
   HAMBURGER V, 1992, DEV DYNAM, V195, P231, DOI 10.1002/dvdy.1001950404
   Harroch S, 2000, MOL CELL BIOL, V20, P7706, DOI 10.1128/MCB.20.20.7706-7715.2000
   Harroch S, 2002, NAT GENET, V32, P411, DOI 10.1038/ng1004
   KRUEGER NX, 1992, P NATL ACAD SCI USA, V89, P7417, DOI 10.1073/pnas.89.16.7417
   LEVY JB, 1993, J BIOL CHEM, V268, P10573
   MAEDA N, 1995, NEUROSCIENCE, V67, P23, DOI 10.1016/0306-4522(94)00069-H
   Malatesta P, 2003, NEURON, V37, P751, DOI 10.1016/S0896-6273(03)00116-8
   Margolis RK, 1996, PERSPECT DEV NEUROBI, V3, P273
   MAUREL P, 1994, P NATL ACAD SCI USA, V91, P2512, DOI 10.1073/pnas.91.7.2512
   McKeon RJ, 1999, J NEUROSCI, V19, P10778, DOI 10.1523/JNEUROSCI.19-24-10778.1999
   MILEV P, 1994, J CELL BIOL, V127, P1703, DOI 10.1083/jcb.127.6.1703
   Nishiwaki T, 1998, J BIOCHEM-TOKYO, V123, P458
   Pringle NP, 2003, DEVELOPMENT, V130, P93, DOI 10.1242/dev.00184
   ROWLEY RB, 1993, CELL MOL BIOL RES, V39, P209
   Sakurai T, 1996, J NEUROSCI RES, V43, P694, DOI 10.1002/(SICI)1097-4547(19960315)43:6<694::AID-JNR6>3.0.CO;2-9
   SHITARA K, 1994, J BIOL CHEM, V269, P20189
   Snyder SE, 1996, MOL BRAIN RES, V40, P79
   van Heyningen P, 2001, CURR BIOL, V11, P232, DOI 10.1016/S0960-9822(01)00075-6
NR 22
TC 9
Z9 10
U1 0
U2 1
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 1567-133X
J9 GENE EXPR PATTERNS
JI Gene Expr. Patterns
PD MAR
PY 2004
VL 4
IS 2
BP 161
EP 166
DI 10.1016/j.modgep.2003.09.003
PG 6
WC Developmental Biology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Developmental Biology; Genetics & Heredity
GA 800IH
UT WOS:000220021500005
PM 15161096
DA 2025-04-10
ER

PT J
AU Eisenreich, A
   Bolbrinker, J
   Leppert, U
AF Eisenreich, Andreas
   Bolbrinker, Juliane
   Leppert, Ulrike
TI Tissue Factor: A Conventional or Alternative Target in Cancer Therapy
SO CLINICAL CHEMISTRY
LA English
DT Review
ID FACTOR PATHWAY INHIBITOR; HUMAN ENDOTHELIAL-CELLS; DNA TOPOISOMERASE-I;
   FACTOR EXPRESSION; TUMOR-GROWTH; LUNG-CANCER; COAGULATION ACTIVATION;
   PROMOTES; ANGIOGENESIS; METASTASIS
AB BACKGROUND: Tissue factor (TF) is an evolutionary conserved glycoprotein that plays an important role in the pathogenesis of cancer. TF is expressed in 2 naturally occurring protein isoforms, membrane-bound full-length (fl)TF and soluble alternatively spliced (as)TF. Both isoforms have been shown to affect a variety of pathophysiologically relevant functions, such as tumor-associated angiogenesis, thrombogenicity, tumor growth, and metastasis. Therefore, targeting TF either by direct inhibition or indirectly, i.e., on a posttranscriptional level, offers a novel therapeutic option for cancer treatment.
   CONTENT: In this review we summarize the latest findings regarding the role of TF and its isoforms in cancer biology. Moreover, we briefly depict and discuss the therapeutic potential of direct and/or indirect inhibition of TF activity and expression for the treatment of cancer.
   SUMMARY: asTF and flTF play important and often distinct roles in cancer biology, i.e., in thrombogenicity and angiogenesis, which is mediated by isoform-specific signal transduction pathways. Therefore, both TF isoforms and downstream signaling are promising novel therapeutic targets in malignant diseases. (C) 2016 American Association for Clinical Chemistry
C1 [Eisenreich, Andreas; Bolbrinker, Juliane] Charite, Inst Klin Pharmakol & Toxikol, CC04,Charitepl 1, D-10117 Berlin, Germany.
   [Leppert, Ulrike] Charite, Inst Physiol, CC02, D-10117 Berlin, Germany.
C3 Berlin Institute of Health; Free University of Berlin; Humboldt
   University of Berlin; Charite Universitatsmedizin Berlin; Berlin
   Institute of Health; Free University of Berlin; Humboldt University of
   Berlin; Charite Universitatsmedizin Berlin
RP Eisenreich, A (corresponding author), Charite, Inst Klin Pharmakol & Toxikol, CC04,Charitepl 1, D-10117 Berlin, Germany.
EM andreas.eisenreich@charite.de
OI Bolbrinker, Juliane/0000-0002-0812-8549; Eisenreich,
   Andreas/0000-0002-0615-7901; Eisenreich, Andreas/0000-0001-7169-3615
CR Abraham E, 2001, CRIT CARE MED, V29, P2081, DOI 10.1097/00003246-200111000-00007
   [Anonymous], CARDIO VASC SYST
   [Anonymous], 2013, Cell Biol. Res. Ther, DOI 10.4172/2324-9293.1000101
   [Anonymous], 2013, THROMBOSIS
   Badimon JJ, 1999, CIRCULATION, V99, P1780, DOI 10.1161/01.CIR.99.14.1780
   Bogdanov VY, 2003, NAT MED, V9, P458, DOI 10.1038/nm841
   Boltzen U, 2012, J MOL CELL CARDIOL, V52, P1056, DOI 10.1016/j.yjmcc.2012.01.015
   Breij ECW, 2014, CANCER RES, V74, P1214, DOI 10.1158/0008-5472.CAN-13-2440
   Chand HS, 2006, INT J CANCER, V118, P1713, DOI 10.1002/ijc.21550
   Chandradas S, 2010, J LEUKOCYTE BIOL, V87, P147, DOI 10.1189/jlb.0409252
   Davila M, 2008, J THROMB HAEMOST, V6, P1517, DOI 10.1111/j.1538-7836.2008.02987.x
   Davila M, 2014, J THROMB HAEMOST, V12, P186, DOI 10.1111/jth.12475
   Dorfleutner A, 2004, MOL BIOL CELL, V15, P4416, DOI 10.1091/mbc.E03-09-0640
   Eisenreich A, 2008, BIOL CHEM, V389, P1333, DOI 10.1515/BC.2008.152
   Eisenreich A, 2011, CIRC J, V75, P1235, DOI 10.1253/circj.CJ-10-0783
   Eisenreich A, 2009, CIRC RES, V104, P589, DOI 10.1161/CIRCRESAHA.108.183905
   Eisenreichi A, 2013, ONCOL REP, V30, P462, DOI 10.3892/or.2013.2413
   Geddings JE, 2014, THROMB HAEMOSTASIS, V111, P570, DOI 10.1160/TH13-10-0812
   Goldin-Lang P, 2008, ONCOL REP, V20, P123
   Hembrough TA, 2003, CANCER RES, V63, P2997
   Hobbs JE, 2007, THROMB RES, V120, pS13, DOI 10.1016/S0049-3848(07)70126-3
   Hu LC, 2013, TUMOR BIOL, V34, P2573, DOI 10.1007/s13277-013-0803-2
   Hu ZW, 1999, P NATL ACAD SCI USA, V96, P8161, DOI 10.1073/pnas.96.14.8161
   Kocatürk B, 2013, P NATL ACAD SCI USA, V110, P11517, DOI 10.1073/pnas.1307100110
   Bauça JM, 2014, CLIN CHEM, V60, P1052, DOI 10.1373/clinchem.2013.211714
   Morrow DA, 2005, EUR HEART J, V26, P682, DOI 10.1093/eurheartj/ehi094
   MUELLER BM, 1992, P NATL ACAD SCI USA, V89, P11832, DOI 10.1073/pnas.89.24.11832
   Nakchbandi W, 2006, SCAND J GASTROENTERO, V41, P1095, DOI 10.1080/00365520600575720
   Palumbo JS, 2000, J PEDIAT HEMATOL ONC, V22, P281, DOI 10.1097/00043426-200005000-00019
   Pengo V, 2011, BLOOD, V117, P1707, DOI 10.1182/blood-2010-08-304758
   Regina S, 2009, CLIN CHEM, V55, P1834, DOI 10.1373/clinchem.2009.123695
   Ruf W, 2011, J THROMB HAEMOST, V9, P306, DOI 10.1111/j.1538-7836.2011.04318.x
   Ruf W, 1996, Curr Opin Hematol, V3, P379
   Schaffner F, 2008, SEMIN THROMB HEMOST, V34, P147, DOI 10.1055/s-2008-1079254
   Sun L, 2013, ACTA ONCOL, V52, P842, DOI 10.3109/0284186X.2013.705890
   Unruh D, 2014, INT J CANCER, V134, P9, DOI 10.1002/ijc.28327
   van den Berg YW, 2009, P NATL ACAD SCI USA, V106, P19497, DOI 10.1073/pnas.0905325106
   Versteeg HH, 2008, CANCER RES, V68, P7219, DOI 10.1158/0008-5472.CAN-08-0419
   Versteeg HH, 2008, BLOOD, V111, P190, DOI 10.1182/blood-2007-07-101048
   Versteeg HH, 2004, SEMIN HEMATOL, V41, P168, DOI 10.1053/j.seminhematol.2003.11.028
   Yu JL, 2005, BLOOD, V105, P1734, DOI 10.1182/blood-2004-05-2042
   Yu JL, 2004, J THROMB HAEMOST, V2, P2065, DOI 10.1111/j.1538-7836.2004.00972.x
   Zhang XX, 2011, J BIOL CHEM, V286, P1429, DOI 10.1074/jbc.M110.146530
   Zoldhelyi P, 2001, P NATL ACAD SCI USA, V98, P4078, DOI 10.1073/pnas.061004098
   Zwicker JI, 2009, CLIN CANCER RES, V15, P6830, DOI 10.1158/1078-0432.CCR-09-0371
NR 45
TC 23
Z9 27
U1 0
U2 8
PU AMER ASSOC CLINICAL CHEMISTRY
PI WASHINGTON
PA 2101 L STREET NW, SUITE 202, WASHINGTON, DC 20037-1526 USA
SN 0009-9147
EI 1530-8561
J9 CLIN CHEM
JI Clin. Chem.
PD APR
PY 2016
VL 62
IS 4
BP 563
EP 570
DI 10.1373/clinchem.2015.241521
PG 8
WC Medical Laboratory Technology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Medical Laboratory Technology
GA DH9DR
UT WOS:000373097100007
PM 26896447
OA Bronze
DA 2025-04-10
ER

PT J
AU Lorca, RA
   Prabagaran, M
   England, SK
AF Lorca, Ramon A.
   Prabagaran, Monali
   England, Sarah K.
TI Functional insights into modulation of BKCa channel activity
   to alter myometrial contractility
SO FRONTIERS IN PHYSIOLOGY
LA English
DT Review
DE BKCa channel; ion channel modulation; myometrium; pregnancy; uterine
   contraction
ID CA2+-ACTIVATED K+ CHANNEL; PROTEIN-KINASE-C; ACTIVATED POTASSIUM
   CHANNELS; CORONARY SMOOTH-MUSCLE; RAT UTERINE MYOCYTES;
   LARGE-CONDUCTANCE; PREGNANT MYOMETRIUM; VOLTAGE; EXPRESSION; ESTROGEN
AB The large-conductance voltage-and Ca2+-activated K+ channel (BKCa) is an important regulator of membrane excitability in a wide variety of cells and tissues. In myometrial smooth muscle, activation of BKCa plays essential roles in buffering contractility to maintain uterine quiescence during pregnancy and in the transition to a more contractile state at the onset of labor. Multiple mechanisms of modulation have been described to alter BKCa channel activity, expression, and cellular localization. In the myometrium, BKCa is regulated by alternative splicing, protein targeting to the plasma membrane, compartmentation in membrane microdomains, and posttranslational modifications. In addition, interaction with auxiliary proteins (i.e., beta 1- and beta 2-subunits), association with G-protein coupled receptor signaling pathways, such as those activated by adrenergic and oxytocin receptors, and hormonal regulation provide further mechanisms of variable modulation of BKCa channel function in myometrial smooth muscle. Here, we provide an overview of these mechanisms of BKCa channel modulation and provide a context for them in relation to myometrial function.
C1 [Lorca, Ramon A.; Prabagaran, Monali; England, Sarah K.] Washington Univ, Dept Obstet & Gynaecol, Sch Med, St Louis, MO 63110 USA.
C3 Washington University (WUSTL)
RP Lorca, RA (corresponding author), Washington Univ, Dept Obstet & Gynaecol, 425 S Euclid Ave, St Louis, MO 63110 USA.
EM lorcar@wustl.edu
FU National Institutes of Health [5R01HD037831]
FX We thank Dr. Deborah J. Frank for critical reading of the manuscript.
   Funded by the National Institutes of Health (5R01HD037831 grant to Sarah
   K. England).
CR Aaronson PI, 2006, BRIT J PHARMACOL, V147, P815, DOI 10.1038/sj.bjp.0706644
   ADELMAN JP, 1992, NEURON, V9, P209, DOI 10.1016/0896-6273(92)90160-F
   Alioua A, 1998, J BIOL CHEM, V273, P32950, DOI 10.1074/jbc.273.49.32950
   Alioua A, 2008, J BIOL CHEM, V283, P4808, DOI 10.1074/jbc.M709802200
   Almassy J, 2012, MOL PHARMACOL, V81, P21, DOI 10.1124/mol.111.075234
   ANWER K, 1992, AM J PHYSIOL, V263, pC1049, DOI 10.1152/ajpcell.1992.263.5.C1049
   ANWER K, 1993, AM J PHYSIOL, V265, pC976, DOI 10.1152/ajpcell.1993.265.4.C976
   ARCHER SL, 1994, P NATL ACAD SCI USA, V91, P7583, DOI 10.1073/pnas.91.16.7583
   Arendt J, 2005, SLEEP MED REV, V9, P25, DOI 10.1016/j.smrv.2004.05.002
   ATKINSON NS, 1991, SCIENCE, V253, P551, DOI 10.1126/science.1857984
   Babiychuk EB, 2004, J MEMBRANE BIOL, V198, P95, DOI 10.1007/s00232-004-0663-1
   Bednarczyk P, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0068125
   Behrens R, 2000, FEBS LETT, V474, P99, DOI 10.1016/S0014-5793(00)01584-2
   Benkusky NA, 2002, FEBS LETT, V524, P97, DOI 10.1016/S0014-5793(02)03011-9
   Benkusky NA, 2000, J BIOL CHEM, V275, P27712
   Berkman ND, 2003, AM J OBSTET GYNECOL, V188, P1648, DOI 10.1067/mob.2003.356
   Bernal AL, 2007, SEMIN CELL DEV BIOL, V18, P340, DOI 10.1016/j.semcdb.2007.05.002
   Bonev AD, 1997, AM J PHYSIOL-CELL PH, V273, pC2090, DOI 10.1152/ajpcell.1997.273.6.C2090
   BORODITSKY RS, 1978, OBSTET GYNECOL, V51, P686
   Brainard AM, 2009, REPROD BIOL ENDOCRIN, V7, DOI 10.1186/1477-7827-7-131
   Brainard AM, 2005, AM J PHYSIOL-CELL PH, V289, pC49, DOI 10.1152/ajpcell.00399.2004
   Bravo-Zehnder M, 2000, P NATL ACAD SCI USA, V97, P13114, DOI 10.1073/pnas.240455697
   Brenner R, 2000, J BIOL CHEM, V275, P6453, DOI 10.1074/jbc.275.9.6453
   Breuiller-Fouché M, 1998, BIOL REPROD, V59, P153, DOI 10.1095/biolreprod59.1.153
   Brodt-Eppley J, 1999, OBSTET GYNECOL, V93, P89, DOI 10.1016/S0029-7844(98)00378-0
   Bru-Mercier G, 2012, J CELL MOL MED, V16, P2990, DOI 10.1111/j.1582-4934.2012.01626.x
   BULBRING E, 1987, PHARMACOL REV, V39, P49
   BUSTER JE, 1979, J CLIN ENDOCR METAB, V48, P139, DOI 10.1210/jcem-48-1-139
   BUTLER A, 1993, SCIENCE, V261, P221, DOI 10.1126/science.7687074
   CAMPBELL EA, 1987, J CLIN ENDOCR METAB, V64, P1054, DOI 10.1210/jcem-64-5-1054
   Carvajal JA, 2003, AM J OBSTET GYNECOL, V188, P84, DOI 10.1067/mob.2003.102
   Chan YW, 2014, EXP PHYSIOL, V99, P510, DOI 10.1113/expphysiol.2013.072868
   Chanrachakul B, 2004, AM J PHYSIOL-CELL PH, V287, pC1747, DOI 10.1152/ajpcell.00236.2004
   Chen L, 2010, J BIOL CHEM, V285, P23263, DOI 10.1074/jbc.M110.139758
   Choi J. W., 2002, ANN CLIN LAB SCI, V32, P357
   Choudhury S, 2011, ANIM REPROD SCI, V126, P173, DOI 10.1016/j.anireprosci.2011.05.014
   CRANKSHAW DJ, 1994, CAN J PHYSIOL PHARM, V72, P870, DOI 10.1139/y94-123
   Curley Michael, 2004, Reprod Biol Endocrinol, V2, P67, DOI 10.1186/1477-7827-2-67
   Danesh SM, 2011, J BIOL CHEM, V286, P31064, DOI 10.1074/jbc.M111.235457
   De Wet H, 2006, MOL MEMBR BIOL, V23, P420, DOI 10.1080/09687860600802803
   Deák BH, 2013, EUR J PHARMACOL, V714, P96, DOI 10.1016/j.ejphar.2013.05.037
   Doheny HC, 2005, J CLIN ENDOCR METAB, V90, P5786, DOI 10.1210/jc.2005-0574
   Doheny HC, 2003, J CLIN ENDOCR METAB, V88, P4310, DOI 10.1210/jc.2003-030221
   Doheny HC, 2007, REPROD BIOL ENDOCRIN, V5, DOI 10.1186/1477-7827-5-10
   Dolan J, 2007, BMC GENOMICS, V8, DOI 10.1186/1471-2164-8-320
   DRAY F, 1976, AM J OBSTET GYNECOL, V126, P13, DOI 10.1016/0002-9378(76)90457-9
   Eude I, 2000, BIOL REPROD, V63, P1567, DOI 10.1095/biolreprod63.5.1567
   Feinberg-Zadek PL, 2007, ALCOHOL CLIN EXP RES, V31, P737, DOI 10.1111/j.1530-0277.2007.00371.x
   Gao L, 2009, REPROD BIOL ENDOCRIN, V7, DOI 10.1186/1477-7827-7-27
   Giangiacomo KM, 2000, BIOCHEMISTRY-US, V39, P6115, DOI 10.1021/bi992865z
   GOLAND RS, 1986, J CLIN ENDOCR METAB, V63, P1199, DOI 10.1210/jcem-63-5-1199
   Gonzalez-Perez V, 2014, P NATL ACAD SCI USA, V111, P4868, DOI 10.1073/pnas.1322123111
   Grammatopoulos DK, 2007, FRONT BIOSCI-LANDMRK, V12, P561, DOI 10.2741/2082
   Gravina FS, 2010, BRIT J PHARMACOL, V161, P1375, DOI 10.1111/j.1476-5381.2010.00949.x
   Gu XQ, 2014, GLIA, V62, P504, DOI 10.1002/glia.22620
   Gülmezoglu AM, 2006, COCHRANE DB SYST REV, DOI 10.1002/14651858.CD004945
   Hawkins JS, 2012, EXPERT OPIN PHARMACO, V13, P2005, DOI 10.1517/14656566.2012.722622
   HILLHOUSE EW, 1993, J CLIN ENDOCR METAB, V76, P736, DOI 10.1210/jc.76.3.736
   Hristov KL, 2014, AM J PHYSIOL-CELL PH, V306, pC460, DOI 10.1152/ajpcell.00325.2013
   Hu XQ, 2011, HYPERTENSION, V58, P1132, DOI 10.1161/HYPERTENSIONAHA.111.179952
   INOUE Y, 1992, CAN J PHYSIOL PHARM, V70, P1597, DOI 10.1139/y92-229
   Jeyabalan A, 2002, CLIN OBSTET GYNECOL, V45, P99, DOI 10.1097/00003081-200203000-00011
   Khan RN, 1998, HUM REPROD, V13, P208, DOI 10.1093/humrep/13.1.208
   KHAN RN, 1993, P ROY SOC B-BIOL SCI, V251, P9, DOI 10.1098/rspb.1993.0002
   Kim EY, 2007, NEUROSCIENCE, V146, P1652, DOI 10.1016/j.neuroscience.2007.03.038
   Kim EY, 2007, J NEUROPHYSIOL, V97, P3508, DOI 10.1152/jn.00009.2007
   Klukovits A, 2010, BIOL REPROD, V83, P36, DOI 10.1095/biolreprod.109.082222
   Knaus H. G., 1994, J BIOL CHEM, V269
   KNAUS HG, 1994, J BIOL CHEM, V269, P3921
   Korovkina VP, 2006, J PHYSIOL-LONDON, V573, P329, DOI 10.1113/jphysiol.2006.106922
   Korovkina VP, 2004, J BIOL CHEM, V279, P1217, DOI 10.1074/jbc.M309158200
   Korovkina VP, 2001, AM J PHYSIOL-CELL PH, V281, pC361, DOI 10.1152/ajpcell.2001.281.1.C361
   Ku CY, 2005, J SOC GYNECOL INVEST, V12, P421, DOI 10.1016/j.jsgi.2005.04.002
   Ku CY, 2002, BIOL REPROD, V67, P605, DOI 10.1095/biolreprod67.2.605
   Kundu P, 2007, J BIOL CHEM, V282, P27478, DOI 10.1074/jbc.M704777200
   Kyle BD, 2013, FASEB J, V27, P2027, DOI 10.1096/fj.12-223669
   Lee JH, 2009, BIOPHYS J, V97, P730, DOI 10.1016/j.bpj.2009.04.058
   Lee US, 2010, J NEUROSCI, V30, P16170, DOI 10.1523/JNEUROSCI.2323-10.2010
   Levitan I, 2010, SUBCELL BIOCHEM, V51, P509, DOI 10.1007/978-90-481-8622-8_19
   Liu GX, 2004, EMBO J, V23, P2196, DOI 10.1038/sj.emboj.7600228
   Lorca RA, 2014, J BIOL CHEM, V289, P10095, DOI 10.1074/jbc.M113.521526
   Lu R, 2006, J PHYSIOL-LONDON, V570, P65, DOI 10.1113/jphysiol.2005.098913
   Lu T, 2010, CIRC RES, V106, P1164, DOI 10.1161/CIRCRESAHA.109.209767
   Ma DH, 2007, FEBS LETT, V581, P1000, DOI 10.1016/j.febslet.2007.01.077
   Mannowetz N, 2013, ELIFE, V2, DOI 10.7554/eLife.01009
   Marijic J, 2001, CIRC RES, V88, P210
   Martin JA, 2013, MMWR-MORBID MORTAL W, V62, P136
   Matharoo-Ball B, 2003, BIOL REPROD, V68, P2135, DOI 10.1095/biolreprod.102.010454
   McKillen K, 1999, AM J PHYSIOL-ENDOC M, V276, pE345
   MCMANUS OB, 1995, NEURON, V14, P645, DOI 10.1016/0896-6273(95)90321-6
   Meera P, 1997, P NATL ACAD SCI USA, V94, P14066, DOI 10.1073/pnas.94.25.14066
   Meredith AL, 2004, J BIOL CHEM, V279, P36746, DOI 10.1074/jbc.M405621200
   Meredith AL, 2006, NAT NEUROSCI, V9, P1041, DOI 10.1038/nn1740
   Mesiano S, 2007, SEMIN CELL DEV BIOL, V18, P321, DOI 10.1016/j.semcdb.2007.05.003
   MONTELONGO A, 1992, DIABETES, V41, P1651, DOI 10.2337/diabetes.41.12.1651
   Morrison JJ, 1996, HUM REPROD, V11, P2285
   Nishimura I, 2008, ENDOCRINOLOGY, V149, P774, DOI 10.1210/en.2007-0759
   Olcese J, 2013, REPROD SCI, V20, P168, DOI 10.1177/1933719112442244
   Orio P, 2005, J GEN PHYSIOL, V125, P395, DOI 10.1085/jgp.200409236
   Pearson T, 2009, AM J PHYSIOL-ENDOC M, V297, pE647, DOI 10.1152/ajpendo.00227.2009
   PEREZ G, 1994, AM J PHYSIOL, V266, pC1459, DOI 10.1152/ajpcell.1994.266.5.C1459
   PEREZ GJ, 1993, AM J OBSTET GYNECOL, V168, P652, DOI 10.1016/0002-9378(93)90513-I
   Peri KG, 2002, SEMIN PERINATOL, V26, P389, DOI 10.1053/sper.2002.37307
   PHILLIPPE M, 1994, BIOL REPROD, V50, P855, DOI 10.1095/biolreprod50.4.855
   Razani B, 2002, PHARMACOL REV, V54, P431, DOI 10.1124/pr.54.3.431
   Renthal NE, 2010, P NATL ACAD SCI USA, V107, P20828, DOI 10.1073/pnas.1008301107
   Ricciotti E, 2011, ARTERIOSCL THROM VAS, V31, P986, DOI 10.1161/ATVBAHA.110.207449
   ROBERTSON BE, 1993, AM J PHYSIOL, V265, pC299
   Sadlonova V, 2011, J OBSTET GYNAECOL RE, V37, P215, DOI 10.1111/j.1447-0756.2010.01340.x
   Saito M, 1997, J BIOL CHEM, V272, P11710, DOI 10.1074/jbc.272.18.11710
   Sanborn BM, 2000, J SOC GYNECOL INVEST, V7, P4, DOI 10.1016/S1071-5576(99)00051-9
   Sato T, 2005, CIRCULATION, V111, P198, DOI 10.1161/01.CIR.0000151099.15706.B1
   Schlabritz-Loutsevitch N, 2003, J CLIN ENDOCR METAB, V88, P908, DOI 10.1210/jc.2002-020449
   Schubert R, 2001, TRENDS PHARMACOL SCI, V22, P505, DOI 10.1016/S0165-6147(00)01775-2
   Sharkey JT, 2009, J CLIN ENDOCR METAB, V94, P421, DOI 10.1210/jc.2008-1723
   Shimano M, 2000, GYNECOL OBSTET INVES, V49, P249, DOI 10.1159/000010254
   Shmygol A, 2007, J PHYSIOL-LONDON, V581, P445, DOI 10.1113/jphysiol.2007.129452
   Shmygol A, 2007, ANN NY ACAD SCI, V1101, P97, DOI 10.1196/annals.1389.031
   Shruti S, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0033429
   Siemen D, 1999, BIOCHEM BIOPH RES CO, V257, P549, DOI 10.1006/bbrc.1999.0496
   Simpkin JC, 1999, BRIT J OBSTET GYNAEC, V106, P439, DOI 10.1111/j.1471-0528.1999.tb08297.x
   Singh H, 2013, P NATL ACAD SCI USA, V110, P10836, DOI 10.1073/pnas.1302028110
   Smith RD, 2005, AM J PHYSIOL-CELL PH, V288, pC982, DOI 10.1152/ajpcell.00120.2004
   Smith RC, 2007, REPROD BIOL ENDOCRIN, V5, DOI 10.1186/1477-7827-5-41
   Soloff MS, 2011, REPROD SCI, V18, P781, DOI 10.1177/1933719111398150
   Song M, 1999, FEBS LETT, V460, P427, DOI 10.1016/S0014-5793(99)01394-0
   Sorensen MV, 2008, J PHYSIOL-LONDON, V586, P4251, DOI 10.1113/jphysiol.2008.156968
   Steffens F, 2003, MOL ENDOCRINOL, V17, P2103, DOI 10.1210/me.2003-0047
   Tanaka Y, 1997, J PHYSIOL-LONDON, V502, P545, DOI 10.1111/j.1469-7793.1997.545bj.x
   Tian LJ, 2001, J BIOL CHEM, V276, P7717, DOI 10.1074/jbc.C000741200
   Toro B, 2006, NEUROSCIENCE, V142, P661, DOI 10.1016/j.neuroscience.2006.06.061
   Toro L, 1998, NEWS PHYSIOL SCI, V13, P112
   TORO L, 1990, J GEN PHYSIOL, V96, P373, DOI 10.1085/jgp.96.2.373
   TRITTHART HA, 1991, Z KARDIOL, V80, P29
   TSENGCRANK J, 1994, NEURON, V13, P1315, DOI 10.1016/0896-6273(94)90418-9
   Turi A, 2001, CELL BIOL INT, V25, P785, DOI 10.1006/cbir.2001.0769
   Tyson EK, 2008, ENDOCRINOLOGY, V149, P6157, DOI 10.1210/en.2008-0593
   Uebele VN, 2000, J BIOL CHEM, V275, P23211, DOI 10.1074/jbc.M910187199
   Valverde MA, 1999, SCIENCE, V285, P1929, DOI 10.1126/science.285.5435.1929
   Vassort G., 1975, J PHYSL, V252, P313
   Wallner M, 1999, P NATL ACAD SCI USA, V96, P4137, DOI 10.1073/pnas.96.7.4137
   Wallner M, 1996, P NATL ACAD SCI USA, V93, P14922, DOI 10.1073/pnas.93.25.14922
   Wallner M, 1995, RECEPTOR CHANNEL, V3, P185
   WARREN WB, 1995, PLACENTA, V16, P147, DOI 10.1016/0143-4004(95)90003-9
   Welsh T, 2012, J ENDOCRINOL, V212, P227, DOI 10.1530/JOE-11-0358
   Willets JM, 2009, MOL ENDOCRINOL, V23, P1272, DOI 10.1210/me.2009-0047
   Williams KC, 2012, MOL ENDOCRINOL, V26, P1857, DOI 10.1210/me.2012-1199
   Witt-Enderby PA, 2003, LIFE SCI, V72, P2183, DOI 10.1016/S0024-3205(03)00098-5
   Wong CM, 2008, STEROIDS, V73, P272, DOI 10.1016/j.steroids.2007.10.010
   Wong MSK, 2010, ACTA PHARMACOL SIN, V31, P1095, DOI 10.1038/aps.2010.127
   WRAY S, 1993, AM J PHYSIOL, V264, pC1, DOI 10.1152/ajpcell.1993.264.1.C1
   Wu JJ, 2000, EUR J ENDOCRINOL, V142, P92, DOI 10.1530/eje.0.1420092
   Xia XM, 2003, J GEN PHYSIOL, V121, P125, DOI 10.1085/jgp.20028667
   Xie JY, 1998, SCIENCE, V280, P443, DOI 10.1126/science.280.5362.443
   Xu C, 2013, J CLIN ENDOCR METAB, V98, P2975, DOI 10.1210/jc.2012-2829
   Xu C, 2011, ENDOCRINOLOGY, V152, P4406, DOI 10.1210/en.2011-0262
   Xu WH, 2002, SCIENCE, V298, P1029, DOI 10.1126/science.1074360
   Yamamura H, 2012, AM J PHYSIOL-CELL PH, V302, pC1257, DOI 10.1152/ajpcell.00191.2011
   Yan JS, 2012, P NATL ACAD SCI USA, V109, P7917, DOI 10.1073/pnas.1205435109
   Yan JS, 2010, NATURE, V466, P513, DOI 10.1038/nature09162
   Yang CT, 2011, P NATL ACAD SCI USA, V108, P19419, DOI 10.1073/pnas.1111104108
   Yang HH, 2008, BIOPHYS J, V94, P4678, DOI 10.1529/biophysj.107.121590
   Yu X, 2011, AM J PHYSIOL-ENDOC M, V301, pE882, DOI 10.1152/ajpendo.00037.2011
   Zarei MM, 2004, P NATL ACAD SCI USA, V101, P10072, DOI 10.1073/pnas.0302919101
   Zarei MM, 2001, J BIOL CHEM, V276, P16232, DOI 10.1074/jbc.M008852200
   Zhang JH, 2007, ANAL BIOCHEM, V365, P40, DOI 10.1016/j.ab.2007.03.001
   Zhou XB, 2000, J PHYSIOL-LONDON, V524, P339, DOI 10.1111/j.1469-7793.2000.t01-1-00339.x
   Zhou XB, 1998, PFLUG ARCH EUR J PHY, V436, P725, DOI 10.1007/s004240050695
   Zhou XB, 1996, J BIOL CHEM, V271, P19760, DOI 10.1074/jbc.271.33.19760
   Zhou XB, 2001, J BIOL CHEM, V276, P43239, DOI 10.1074/jbc.M104202200
   Zhou XB, 2008, J BIOL CHEM, V283, P21036, DOI 10.1074/jbc.M800447200
   Zhou XB, 2007, MOL ENDOCRINOL, V21, P740, DOI 10.1210/me.2006-0220
   Zhou XB, 2010, P NATL ACAD SCI USA, V107, P8005, DOI 10.1073/pnas.0912029107
   Zhou XX, 2000, REFR SCI T, V2000, P279
   Zhu N, 2005, FEBS LETT, V579, P4856, DOI 10.1016/j.febslet.2005.07.069
   Zou SW, 2008, MOL PHARMACOL, V73, P359, DOI 10.1124/mol.107.039743
NR 176
TC 34
Z9 36
U1 0
U2 8
PU FRONTIERS MEDIA SA
PI LAUSANNE
PA AVENUE DU TRIBUNAL FEDERAL 34, LAUSANNE, CH-1015, SWITZERLAND
SN 1664-042X
J9 FRONT PHYSIOL
JI Front. Physiol.
PD JUL 31
PY 2014
VL 5
AR 289
DI 10.3389/fphys.2014.00289
PG 12
WC Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Physiology
GA AX7DJ
UT WOS:000347076800001
PM 25132821
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Hong, SE
   Song, HK
   Kim, DH
AF Hong, Seong-Eui
   Song, Hong Ki
   Kim, Do Han
TI Identification of tissue-enriched novel transcripts and novel exons in
   mice
SO BMC GENOMICS
LA English
DT Article
DE Next generation sequencing; Novel transcript; Novel exon;
   Tissue-specificity
ID RNA-SEQ; GENE-EXPRESSION; MOUSE; PROTEIN; PREDICTION; CLONING;
   TRANSLATION; ELEMENTS; PROLINE; REVEALS
AB Background: RNA sequencing (RNA-seq) has revolutionized the detection of transcriptomic signatures due to its high-throughput sequencing ability. Therefore, genomic annotations on different animal species have been rapidly updated using information from tissue-enriched novel transcripts and novel exons.
   Results: 34 putative novel transcripts and 236 putative tissue-enriched exons were identified using RNA-Seq datasets representing six tissues available in mouse databases. RT-PCR results indicated that expression of 21 and 2 novel transcripts were enriched in testes and liver, respectively, while 31 of the 39 selected novel exons were detected in the testes or heart. The novel isoforms containing the identified novel exons exhibited more dominant expression than the known isoforms in heart and testes. We also identified an example of pathology-associated exclusion of heart-enriched novel exons such as Sorbs1 and Cluh during pressure-overload cardiac hypertrophy.
   Conclusion: The present study depicted tissue-enriched novel transcripts, a tissue-specific isoform switch, and pathology-associated alternative splicing in a mouse model, suggesting tissue-specific genomic diversity and plasticity.
C1 [Kim, Do Han] GIST, Sch Life Sci, Kwangju 500712, South Korea.
   GIST, Syst Biol Res Ctr, Kwangju 500712, South Korea.
C3 Gwangju Institute of Science & Technology (GIST); Gwangju Institute of
   Science & Technology (GIST)
RP Kim, DH (corresponding author), GIST, Sch Life Sci, 123 Cheomdangwagi Ro Oryong Dong, Kwangju 500712, South Korea.
EM dhkim@gist.ac.kr
FU Bio & Medical Technology Development Program of the National Research
   Foundation (NRF) - Ministry of Science, ICT & Future Planning
   [NRF-2013M3A9A7046297]; GIST Systems Biology Infrastructure
   Establishment Grant;  [NRF-2012R1A1A2043217]
FX This research was supported by the Bio & Medical Technology Development
   Program of the National Research Foundation (NRF) funded by the Ministry
   of Science, ICT & Future Planning (NRF-2013M3A9A7046297),
   NRF-2012R1A1A2043217, and the 2014 GIST Systems Biology Infrastructure
   Establishment Grant.
CR Alcazar O, 2004, BIOCHEM BIOPH RES CO, V317, P285, DOI 10.1016/j.bbrc.2004.03.038
   Anders S, 2010, GENOME BIOL, V11, DOI 10.1186/gb-2010-11-10-r106
   Anders S, 2012, GENOME RES, V22, P2008, DOI 10.1101/gr.133744.111
   Beltran M, 2008, GENE DEV, V22, P756, DOI 10.1101/gad.455708
   Blom N, 2004, PROTEOMICS, V4, P1633, DOI 10.1002/pmic.200300771
   Brawand D, 2011, NATURE, V478, P343, DOI 10.1038/nature10532
   Bugaut A, 2012, NUCLEIC ACIDS RES, V40, P4727, DOI 10.1093/nar/gks068
   Cabili MN, 2011, GENE DEV, V25, P1915, DOI 10.1101/gad.17446611
   Chen FC, 2006, BMC BIOINFORMATICS, V7, DOI 10.1186/1471-2105-7-136
   Chen G, 2011, BMC GENOMICS, V12, DOI 10.1186/1471-2164-12-590
   Da Ros V, 2007, Soc Reprod Fertil Suppl, V65, P353
   Eswaran J, 2013, SCI REP-UK, V3, DOI 10.1038/srep01689
   Forster SC, 2013, BIOINFORMATICS, V29, P810, DOI 10.1093/bioinformatics/btt034
   Gasteiger E, 2003, NUCLEIC ACIDS RES, V31, P3784, DOI 10.1093/nar/gkg563
   Goodrich JA, 2006, NAT REV MOL CELL BIO, V7, P612, DOI 10.1038/nrm1946
   Hong CS, 2001, GENE, V278, P193, DOI 10.1016/S0378-1119(01)00718-1
   Howald C, 2012, GENOME RES, V22, P1698, DOI 10.1101/gr.134478.111
   Huang CJ, 2009, BMC MOL BIOL, V10, DOI 10.1186/1471-2199-10-74
   Hulett MD, 2001, BIOCHEM BIOPH RES CO, V280, P374, DOI 10.1006/bbrc.2000.4088
   Jakhesara SJ, 2013, J BIOTECHNOL, V165, P37, DOI 10.1016/j.jbiotec.2013.02.015
   Kämper N, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0035972
   Kay BK, 2000, FASEB J, V14, P231, DOI 10.1096/fasebj.14.2.231
   Kim D, 2013, GENOME BIOL, V14, DOI 10.1186/gb-2013-14-4-r36
   Kosugi S, 2009, P NATL ACAD SCI USA, V106, P10171, DOI 10.1073/pnas.0900604106
   Lagacé M, 2001, GENOMICS, V77, P181, DOI 10.1006/geno.2001.6635
   Lee JH, 2011, CIRC RES, V109, P1332, DOI 10.1161/CIRCRESAHA.111.249433
   Mandai K, 1999, J CELL BIOL, V144, P1001, DOI 10.1083/jcb.144.5.1001
   Martianov I, 2007, NATURE, V445, P666, DOI 10.1038/nature05519
   Mochizuki Y, 2013, J BIOL CHEM, V288, P1009, DOI 10.1074/jbc.M112.395087
   Pan YX, 2005, MOL PHARMACOL, V68, P866, DOI 10.1124/mol.105.011858
   Roberts A, 2011, BIOINFORMATICS, V27, P2325, DOI 10.1093/bioinformatics/btr355
   Skehel PA, 2000, P NATL ACAD SCI USA, V97, P1101, DOI 10.1073/pnas.97.3.1101
   Song HK, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0035552
   Sparks AB, 1996, NAT BIOTECHNOL, V14, P741, DOI 10.1038/nbt0696-741
   Steel LF, 1996, CELL GROWTH DIFFER, V7, P1415
   Sun L, 2012, BMC BIOINFORMATICS, V13, DOI 10.1186/1471-2105-13-331
   VONHEIJNE G, 1992, J MOL BIOL, V225, P487, DOI 10.1016/0022-2836(92)90934-C
   Wang HD, 2005, J CELL BIOL, V171, P811, DOI 10.1083/jcb.200506006
   YU HT, 1994, CELL, V76, P933, DOI 10.1016/0092-8674(94)90367-0
NR 39
TC 11
Z9 11
U1 0
U2 11
PU BMC
PI LONDON
PA CAMPUS, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
SN 1471-2164
J9 BMC GENOMICS
JI BMC Genomics
PD JUL 13
PY 2014
VL 15
AR 592
DI 10.1186/1471-2164-15-592
PG 11
WC Biotechnology & Applied Microbiology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biotechnology & Applied Microbiology; Genetics & Heredity
GA AL7DY
UT WOS:000339294500001
PM 25017872
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Passier, R
   Richardson, JA
   Olson, EN
AF Passier, R
   Richardson, JA
   Olson, EN
TI Oracle, a novel PDZ-LIM domain protein expressed in heart and skeletal
   muscle
SO MECHANISMS OF DEVELOPMENT
LA English
DT Article
DE heart muscle; skeletal muscle; PDZ-LIM domain protein
ID GENE; DIFFERENTIATION; HOMEODOMAIN; ELEGANS
AB In order to identify novel genes enriched in adult heart, we performed a subtractive hybridization for genes expressed in mouse heart but not in skeletal muscle. We identified two alternative splicing variants of a novel PDZ-LIM domain protein, which we named Oracle. Both variants contain a PDZ domain at the amino-terminus and three LIM domains at the carboxy-terminus. Highest homology of Oracle was found with the human and rat enigma proteins in the PDZ domain (62 and 61% respectively) and in the LIM domains (60 and 69%, respectively). By Northern hybridization analysis, we showed that expression is highest in adult mouse heart, low in skeletal muscle and undetectable in other adult mouse tissues. In situ hybridization in mouse embryos confirmed and extended these data by showing high expression of Oracle mRNA in atrial and ventricular rmyocardial cells from E8.5. From E9.5 low expression of Oracle mRNA was detectable in myotomes. These data suggest a role for Oracle in the early development and function of heart and skeletal muscle. (C) 2000 Elsevier Science Ireland Ltd. All rights reserved.
C1 Univ Texas, SW Med Ctr Dallas, Dept Biol Mol, Hamon Ctr Basic Canc Res, Dallas, TX 75235 USA.
   Univ Texas, SW Med Ctr, Dept Pathol, Dallas, TX 75235 USA.
C3 University of Texas System; University of Texas Dallas; University of
   Texas Southwestern Medical Center Dallas; University of Texas System;
   University of Texas Southwestern Medical Center Dallas; University of
   Texas Dallas
RP Olson, EN (corresponding author), Univ Texas, SW Med Ctr Dallas, Dept Biol Mol, Hamon Ctr Basic Canc Res, 5323 Harry Hines Blvd, Dallas, TX 75235 USA.
RI Olson, Eric/B-4391-2013; Richardson, James/MEO-1254-2025
OI Olson, Eric N./0000-0003-1151-8262
CR ABER S, 1997, CELL, V88, P393
   ARBER S, 1994, CELL, V79, P221, DOI 10.1016/0092-8674(94)90192-9
   Boden SD, 1998, ENDOCRINOLOGY, V139, P5125, DOI 10.1210/en.139.12.5125
   Fanning AS, 1996, CURR BIOL, V6, P1385, DOI 10.1016/S0960-9822(96)00737-3
   FREYD G, 1990, NATURE, V344, P876, DOI 10.1038/344876a0
   FROHMAN MA, 1990, DEVELOPMENT, V110, P589
   Guy PM, 1999, MOL BIOL CELL, V10, P1973, DOI 10.1091/mbc.10.6.1973
   HUBANK M, 1994, NUCLEIC ACIDS RES, V22, P5640, DOI 10.1093/nar/22.25.5640
   KARLSSON O, 1990, NATURE, V344, P879, DOI 10.1038/344879a0
   KIESS M, 1995, ONCOGENE, V10, P61
   Kuroda S, 1996, J BIOL CHEM, V271, P31029, DOI 10.1074/jbc.271.49.31029
   Nakagawa O, 1999, DEV BIOL, V216, P72, DOI 10.1006/dbio.1999.9454
   SADLER L, 1992, J CELL BIOL, V6, P1573
   SCHMEICHEL KL, 1994, CELL, V79, P211, DOI 10.1016/0092-8674(94)90191-0
   WANG H, 1995, GENE, P267
   WAY JC, 1988, CELL, V54, P5, DOI 10.1016/0092-8674(88)90174-2
   WILKINSON DG, 1987, DEVELOPMENT, V99, P493
   WU RY, 1994, J BIOL CHEM, V269, P25085
   Wu RY, 1996, J BIOL CHEM, V271, P15934, DOI 10.1074/jbc.271.27.15934
   Xia HH, 1997, J CELL BIOL, V139, P507, DOI 10.1083/jcb.139.2.507
NR 20
TC 59
Z9 67
U1 0
U2 3
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 0925-4773
J9 MECH DEVELOP
JI Mech. Dev.
PD APR
PY 2000
VL 92
IS 2
BP 277
EP 284
DI 10.1016/S0925-4773(99)00330-5
PG 8
WC Developmental Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Developmental Biology
GA 303BA
UT WOS:000086399900016
PM 10727866
OA Bronze
DA 2025-04-10
ER

PT J
AU Liu, XY
   Ali, MK
   Zhao, L
   Dua, K
   Mao, YQ
AF Liu, Xiaoying
   Ali, Md Khadem
   Zhao, Lan
   Dua, Kamal
   Mao, Yuqiang
TI The emerging diagnostic and therapeutic roles of small nucleolar RNAs in
   lung diseases
SO BIOMEDICINE & PHARMACOTHERAPY
LA English
DT Review
DE snoRNAs; Lung cancer; Asthma; COPD; Pulmonary hypertension; COVID-19
ID PRE-MESSENGER-RNA; NONCODING RNAS; CANCER; H/ACA; MECHANISMS;
   EXPRESSION; SNORNAS; NUCLEAR; GENE; RAS
AB Small nucleolar RNAs (snoRNAs) are non-coding RNA molecules that range from 60 to 300 nucleotides in length and are primarily located in the nucleoli of cells. They play a critical role in modifying ribosomal RNA and can also regulate alternative splicing and posttranscriptional modification of mRNA. Alterations in snoRNA expression can affect numerous cellular processes, including cell proliferation, apoptosis, angiogenesis, fibrosis, and inflammation, making them a promising target for diagnostics and treatment of various human pathologies. Recent evidence suggests that abnormal snoRNA expression is strongly associated with the development and progression of several lung diseases, such as lung cancer, asthma, chronic obstructive pulmonary disease, and pulmonary hypertension, as well as COVID-19. While few studies have shown a causal relationship between snoRNA expression and disease onset, this research field presents exciting opportunities for identifying new biomarkers and therapeutic targets in lung disease. This review discusses the emerging role and molecular mechanisms of snoRNAs in the pathogenesis of lung diseases, focusing on research opportunities, clinical studies, biomarkers, and therapeutic potential.
C1 [Liu, Xiaoying] China Med Univ, Dept Breast Surg, Affiliated Hosp 1, Shenyang, Peoples R China.
   [Ali, Md Khadem; Zhao, Lan] Stanford Univ, Dept Med, Div Pulm & Crit Care Med, Stanford, CA USA.
   [Ali, Md Khadem] Stanford Univ, Vera Moulton Wall Ctr Pulm Vasc Dis, Stanford, CA USA.
   [Dua, Kamal] Univ Technol Sydney, Grad Sch Hlth, Discipline Pharm, Sydney, NSW 2007, Australia.
   [Mao, Yuqiang] China Med Univ, Dept Thorac Surg, Shengjing Hosp, Shenyang 110022, Liaoning, Peoples R China.
C3 China Medical University; Stanford University; Stanford University;
   University of Technology Sydney; China Medical University
RP Mao, YQ (corresponding author), China Med Univ, Dept Thorac Surg, Shengjing Hosp, Shenyang 110022, Liaoning, Peoples R China.
EM maoyq@sj-hospital.org
RI Ali, Khadem/R-2746-2018; Zhao, Lan/HSH-5158-2023
OI Zhao, Lan/0000-0003-2681-7695
CR Alexandrova E, 2016, J ALLERGY CLIN IMMUN, V137, P58, DOI 10.1016/j.jaci.2015.05.031
   Aw JGA, 2016, MOL CELL, V62, P603, DOI 10.1016/j.molcel.2016.04.028
   Bagheri A, 2019, J CELL BIOCHEM, V120, P8280, DOI 10.1002/jcb.28111
   Balsara BR, 2002, ONCOGENE, V21, P6877, DOI 10.1038/sj.onc.1205836
   Bergeron D, 2023, NUCLEIC ACIDS RES, V51, pD291, DOI 10.1093/nar/gkac835
   Bergeron D, 2020, BIOCHEM SOC T, V48, P645, DOI 10.1042/BST20191046
   Bouchard-Bourelle P, 2020, NUCLEIC ACIDS RES, V48, pD220, DOI 10.1093/nar/gkz884
   Bratkovic T, 2020, NUCLEIC ACIDS RES, V48, P1627, DOI 10.1093/nar/gkz1140
   Bratkovic T, 2018, SCI REP-UK, V8, DOI 10.1038/s41598-018-23293-7
   Brown JWS, 2008, TRENDS PLANT SCI, V13, P335, DOI 10.1016/j.tplants.2008.04.010
   Bryant HE, 2005, NATURE, V434, P913, DOI 10.1038/nature03443
   Butler Merlin G, 2015, Adv Genomics Genet, V2015, P53
   Cech TR, 2014, CELL, V157, P77, DOI 10.1016/j.cell.2014.03.008
   Chen NS, 2020, LANCET, V395, P507, DOI 10.1016/S0140-6736(20)30211-7
   Chen S, 2022, J CELL MOL MED, V26, P5150, DOI 10.1111/jcmm.17540
   Cui CH, 2021, ONCOGENE, V40, P909, DOI 10.1038/s41388-020-01570-y
   Davanian H, 2017, ONCOTARGET, V8, P4530, DOI 10.18632/oncotarget.13889
   Dong XH, 2021, THORAC CANCER, V12, P659, DOI 10.1111/1759-7714.13823
   Eblen ST, 2018, ADV CANCER RES, V138, P99, DOI 10.1016/bs.acr.2018.02.004
   Elliott BA, 2019, NAT COMMUN, V10, DOI 10.1038/s41467-019-11375-7
   Falaleeva M, 2016, P NATL ACAD SCI USA, V113, pE1625, DOI 10.1073/pnas.1519292113
   Falaleeva M, 2013, BIOESSAYS, V35, P46, DOI 10.1002/bies.201200117
   Gao L, 2015, INT J CANCER, V136, pE623, DOI 10.1002/ijc.29169
   Girard A, 2006, NATURE, V442, P199, DOI 10.1038/nature04917
   Gong J, 2017, CELL REP, V21, P1968, DOI 10.1016/j.celrep.2017.10.070
   He XX, 2015, NUCLEIC ACIDS RES, V43, P3712, DOI 10.1093/nar/gkv214
   Henras A, 1998, EMBO J, V17, P7078, DOI 10.1093/emboj/17.23.7078
   Hirose T, 2001, P NATL ACAD SCI USA, V98, P12914, DOI 10.1073/pnas.231490998
   Hombach S, 2016, ADV EXP MED BIOL, V937, P3, DOI 10.1007/978-3-319-42059-2_1
   Huang CL, 2020, LANCET, V395, P497, DOI [10.1016/S0140-6736(20)30183-5, 10.1016/S0140-6736(20)30211-7]
   Jorjani H, 2016, NUCLEIC ACIDS RES, V44, P5068, DOI 10.1093/nar/gkw386
   Kim RY, 2021, SCI TRANSL MED, V13, DOI 10.1126/scitranslmed.aav7223
   Kishore S, 2006, SCIENCE, V311, P230, DOI 10.1126/science.1118265
   Kiss T, 2010, MOL CELL, V37, P597, DOI 10.1016/j.molcel.2010.01.032
   Labaki WW, 2020, ANN INTERN MED, V173, pITC17, DOI 10.7326/AITC202008040
   Langhendries JL, 2016, ONCOTARGET, V7, P59519, DOI 10.18632/oncotarget.11148
   Lestrade L, 2006, NUCLEIC ACIDS RES, V34, pD158, DOI 10.1093/nar/gkj002
   Liao JP, 2010, MOL CANCER, V9, DOI 10.1186/1476-4598-9-198
   Lu SH, 2019, NUCLEIC ACIDS RES, V47, P8111, DOI 10.1093/nar/gkz646
   Lu ZP, 2016, CELL, V165, P1267, DOI 10.1016/j.cell.2016.04.028
   Lykke-Andersen S, 2018, MOL CELL, V72, P99, DOI 10.1016/j.molcel.2018.08.017
   Mannoor K, 2014, MOL CANCER, V13, DOI 10.1186/1476-4598-13-104
   Matera AG, 2007, NAT REV MOL CELL BIO, V8, P209, DOI 10.1038/nrm2124
   Mattick JS, 2006, HUM MOL GENET, V15, pR17, DOI 10.1093/hmg/ddl046
   McErlean P, 2014, BMC MED GENOMICS, V7, DOI 10.1186/1755-8794-7-37
   Mei YP, 2012, ONCOGENE, V31, P2794, DOI 10.1038/onc.2011.449
   Mourksi N.E., 2020, CELLS-BASEL, V9, P3
   Mourksi NEH, 2020, CELLS-BASEL, V9, DOI 10.3390/cells9030541
   Murakami K, 2015, CURR HYPERTENS REV, V11, P80, DOI 10.2174/1573402111666150401105317
   Naito A, 2019, PLOS ONE, V14, DOI 10.1371/journal.pone.0211377
   Jorge NAN, 2017, PLOS ONE, V12, DOI 10.1371/journal.pone.0183410
   Ohara T, 2007, NAT STRUCT MOL BIOL, V14, P349, DOI 10.1038/nsmb1220
   Palazzo AF, 2015, FRONT GENET, V6, DOI 10.3389/fgene.2015.00002
   Parray A., 2021, Vaccines (Basel), P9
   Parray A, 2021, VACCINES-BASEL, V9, DOI 10.3390/vaccines9101056
   Raabe CA, 2019, SCI REP-UK, V9, DOI 10.1038/s41598-019-39940-6
   Reichow SL, 2007, NUCLEIC ACIDS RES, V35, P1452, DOI 10.1093/nar/gkl1172
   Schabath MB, 2019, CANCER EPIDEM BIOMAR, V28, P1563, DOI 10.1158/1055-9965.EPI-19-0221
   Schon P., 2018, SEM CELL DEV BIOL
   Scott MS, 2012, NUCLEIC ACIDS RES, V40, P3676, DOI 10.1093/nar/gkr1233
   Sharma E, 2016, MOL CELL, V62, P618, DOI 10.1016/j.molcel.2016.04.030
   Sharma S, 2017, PLOS GENET, V13, DOI [10.1371/journal.pgen.1007019, 10.1371/journal.pgen.1006804]
   Siprashvili Z, 2016, NAT GENET, V48, P53, DOI 10.1038/ng.3452
   Smith CM, 1997, CELL, V89, P669, DOI 10.1016/S0092-8674(00)80247-0
   Su H, 2014, ONCOGENE, V33, P1348, DOI 10.1038/onc.2013.89
   Su J, 2016, ONCOTARGET, V7, P5131, DOI 10.18632/oncotarget.4219
   Taft RJ, 2009, RNA, V15, P1233, DOI 10.1261/rna.1528909
   Tang GL, 2019, J CANCER, V10, P2261, DOI 10.7150/jca.31077
   van der Werf J., 2021, BIOLOGY-BASEL, P10
   Vitali P, 2019, GENE DEV, V33, P741, DOI 10.1101/gad.326363.119
   Wajahat M, 2021, INT J MOL SCI, V22, DOI 10.3390/ijms221910193
   Wang C, 2004, EMBO J, V23, P1857, DOI 10.1038/sj.emboj.7600181
   Wang H, 2022, SIGNAL TRANSDUCT TAR, V7, DOI 10.1038/s41392-022-01210-9
   Wang K., 2022, RESP RES
   Wang K., 2022, J CLIN LAB ANAL, V36
   Wang KY, 2023, CELL DEATH DIFFER, V30, P341, DOI 10.1038/s41418-022-01087-9
   Wang KY, 2022, FUTURE ONCOL, V18, P821, DOI 10.2217/fon-2021-1278
   Wang W., 2021, FRONT CELL DEV BIOL, P9
   Wang W, 2021, FRONT CELL DEV BIOL, V9, DOI 10.3389/fcell.2021.672159
   Wang XN, 2019, FRONT ONCOL, V9, DOI 10.3389/fonc.2019.00788
   Wu H, 2016, MOL CELL, V64, P534, DOI 10.1016/j.molcel.2016.10.007
   Yoshihama Maki, 2013, BMC Res Notes, V6, P426, DOI 10.1186/1756-0500-6-426
   Yu HQ, 2021, FRONT ONCOL, V11, DOI 10.3389/fonc.2021.620213
   Zhao YL, 2021, BIOMED RES INT-UK, V2021, DOI 10.1155/2021/9921012
   Zheng D, 2015, J EXP CLIN CANC RES, V34, DOI 10.1186/s13046-015-0170-5
   Zhong FD, 2015, NUCLEIC ACIDS RES, V43, P10474, DOI 10.1093/nar/gkv954
   Zhou FB, 2017, NAT CELL BIOL, V19, P844, DOI 10.1038/ncb3563
   Zhou HW, 2022, BIOMED RES INT, V2022, DOI 10.1155/2022/5501171
   Zhu N, 2020, NEW ENGL J MED, V382, P727, DOI [10.1056/NEJMoa2001017, 10.1172/JCI89857]
   Zhuo Y., 2022, J IMMUNOTHER CANCER, V10, P5
NR 90
TC 11
Z9 11
U1 1
U2 12
PU ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
PI ISSY-LES-MOULINEAUX
PA 65 RUE CAMILLE DESMOULINS, CS50083, 92442 ISSY-LES-MOULINEAUX, FRANCE
SN 0753-3322
EI 1950-6007
J9 BIOMED PHARMACOTHER
JI Biomed. Pharmacother.
PD MAY
PY 2023
VL 161
AR 114519
DI 10.1016/j.biopha.2023.114519
EA MAR 2023
PG 7
WC Medicine, Research & Experimental; Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Research & Experimental Medicine; Pharmacology & Pharmacy
GA D8OX2
UT WOS:000971276700001
PM 36906975
OA gold
DA 2025-04-10
ER

PT J
AU Zhang, DX
   Sliwkowski, MX
   Mark, M
   Frantz, G
   Akita, R
   Sun, Y
   Hillan, K
   Crowley, C
   Brush, J
   Godowski, PJ
AF Zhang, DX
   Sliwkowski, MX
   Mark, M
   Frantz, G
   Akita, R
   Sun, Y
   Hillan, K
   Crowley, C
   Brush, J
   Godowski, PJ
TI Neuregulin-3 (NRG3): A novel neural tissue-enriched protein that binds
   and activates ErbB4
SO PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF
   AMERICA
LA English
DT Article
ID EPIDERMAL GROWTH-FACTOR; DIFFERENTIATION FACTOR; CARDIAC DEVELOPMENT;
   RECEPTOR FAMILY; NERVOUS-SYSTEM; HEREGULIN; EXPRESSION; MEMBER; GENE;
   EGF
AB We describe the identification of Neuregulin-3 (NRG3), a novel protein that is structurally related to the neuregulins (NRG1). The NRG1/neuregulins are a diverse family of proteins that arise by alternative splicing from a single gene. These proteins play an important role in controlling the growth and differentiation of glial, epithelial, and muscle cells. The biological effects of NRG1 are mediated by receptor tyrosine kinases ErbB2, ErbB3, and ErbB4. However, genetic studies have suggested that the activity of ErbB4 may also be regulated in the central nervous system by a ligand distinct from NRG1. NRG3 is predicted to contain an extracellular domain with an epidermal growth factor (EGF) motif, a transmembrane domain, and a large cytoplasmic domain. We show that the EGF-like domain of NRG3 binds to the extracellular domain of ErbB4 in vitro. Moreover, NRG3 binds to ErbB4 expressed on cells and stimulates tyrosine phosphorylation of this receptor. The expression of NRG3 is highly restricted to the developing and adult nervous system. These data suggest that NRG3 is a novel, neural-enriched ligand for ErbB4.
C1 GENENTECH INC, DEPT MOL BIOL, San Francisco, CA 94080 USA.
   GENENTECH INC, DEPT PROT CHEM, San Francisco, CA 94080 USA.
   GENENTECH INC, DEPT PATHOL, San Francisco, CA 94080 USA.
C3 Roche Holding; Genentech; Roche Holding USA; Roche Holding; Roche
   Holding USA; Genentech; Roche Holding; Roche Holding USA; Genentech
CR BARBACCI EG, 1995, J BIOL CHEM, V270, P9585, DOI 10.1074/jbc.270.16.9585
   Beerli RR, 1996, J BIOL CHEM, V271, P6071, DOI 10.1074/jbc.271.11.6071
   BerminghamMcDonogh O, 1996, DEVELOPMENT, V122, P1427
   BLOBEL G, 1980, P NATL ACAD SCI-BIOL, V77, P1496, DOI 10.1073/pnas.77.3.1496
   CARRAWAY KL, 1994, J BIOL CHEM, V269, P14303
   CARRAWAY KL, 1994, CELL, V78, P5, DOI 10.1016/0092-8674(94)90564-9
   Carraway KL, 1997, NATURE, V387, P512, DOI 10.1038/387512a0
   CARTER P, 1992, P NATL ACAD SCI USA, V89, P4285, DOI 10.1073/pnas.89.10.4285
   Chang H, 1997, NATURE, V387, P509, DOI 10.1038/387509a0
   DERYNCK R, 1984, CELL, V38, P287, DOI 10.1016/0092-8674(84)90550-6
   FALLS DL, 1993, CELL, V72, P801, DOI 10.1016/0092-8674(93)90407-H
   FRANCOEUR JR, 1995, J NEUROSCI RES, V41, P836, DOI 10.1002/jnr.490410614
   GASSMANN M, 1995, NATURE, V378, P390, DOI 10.1038/378390a0
   GODOWSKI PJ, 1989, P NATL ACAD SCI USA, V86, P8083, DOI 10.1073/pnas.86.20.8083
   Grinspan JB, 1996, J NEUROSCI, V16, P6107
   HIGASHIYAMA S, 1991, SCIENCE, V251, P936, DOI 10.1126/science.1840698
   HO WH, 1995, J BIOL CHEM, V270, P14523, DOI 10.1074/jbc.270.24.14523
   HOLMES WE, 1992, SCIENCE, V256, P1205, DOI 10.1126/science.256.5060.1205
   Karunagaran D, 1996, EMBO J, V15, P254, DOI 10.1002/j.1460-2075.1996.tb00356.x
   KITA YA, 1994, FEBS LETT, V349, P139, DOI 10.1016/0014-5793(94)00644-X
   LEE J, 1993, GENOMICS, V16, P790, DOI 10.1006/geno.1993.1272
   LEE KF, 1995, NATURE, V378, P394, DOI 10.1038/378394a0
   Lemke G, 1996, MOL CELL NEUROSCI, V7, P247, DOI 10.1006/mcne.1996.0019
   LEVI ADO, 1995, J NEUROSCI, V15, P1329
   LU LH, 1994, CELL VISION, V1, P169
   MARCHIONNI MA, 1993, NATURE, V362, P312, DOI 10.1038/362312a0
   MARK MR, 1994, J BIOL CHEM, V269, P10720
   MEYER D, 1995, NATURE, V378, P386, DOI 10.1038/378386a0
   NAGAI M, 1985, GENE, V36, P183
   ORRURTREGER A, 1993, P NATL ACAD SCI USA, V90, P1867, DOI 10.1073/pnas.90.5.1867
   PLOWMAN GD, 1990, MOL CELL BIOL, V10, P1969, DOI 10.1128/MCB.10.5.1969
   PLOWMAN GD, 1993, P NATL ACAD SCI USA, V90, P1746, DOI 10.1073/pnas.90.5.1746
   PLOWMAN GD, 1993, NATURE, V366, P473, DOI 10.1038/366473a0
   RIESE DJ, 1995, MOL CELL BIOL, V15, P5770
   SABATINI DD, 1982, J CELL BIOL, V92, P1, DOI 10.1083/jcb.92.1.1
   SASADA R, 1993, BIOCHEM BIOPH RES CO, V190, P1173, DOI 10.1006/bbrc.1993.1173
   SHING Y, 1993, SCIENCE, V259, P1604, DOI 10.1126/science.8456283
   SLIWKOWSKI MX, 1994, J BIOL CHEM, V269, P14661
   Toyoda H, 1995, FEBS LETT, V377, P403, DOI 10.1016/0014-5793(95)01403-9
   TZAHAR E, 1994, J BIOL CHEM, V269, P25226
   Weber J., 1996, Society for Neuroscience Abstracts, V22, P1579
   WEN DZ, 1992, CELL, V69, P559, DOI 10.1016/0092-8674(92)90456-M
   WICKNER WT, 1985, SCIENCE, V230, P400, DOI 10.1126/science.4048938
   ZHU XJ, 1995, EMBO J, V14, P5842, DOI 10.1002/j.1460-2075.1995.tb00272.x
NR 44
TC 308
Z9 397
U1 0
U2 4
PU NATL ACAD SCIENCES
PI WASHINGTON
PA 2101 CONSTITUTION AVE NW, WASHINGTON, DC 20418 USA
SN 0027-8424
J9 P NATL ACAD SCI USA
JI Proc. Natl. Acad. Sci. U. S. A.
PD SEP 2
PY 1997
VL 94
IS 18
BP 9562
EP 9567
DI 10.1073/pnas.94.18.9562
PG 6
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA XU455
UT WOS:A1997XU45500010
PM 9275162
OA Green Published
DA 2025-04-10
ER

PT J
AU Nishio, T
   Adachi, H
   Nakagomi, R
   Tokui, T
   Sato, E
   Tanemoto, M
   Fujiwara, K
   Okabe, M
   Onogawa, T
   Suzuki, T
   Nakai, D
   Shiiba, K
   Suzuki, M
   Ohtani, H
   Kondo, Y
   Unno, M
   Ito, S
   Iinuma, K
   Nunoki, K
   Matsuno, S
   Abe, T
AF Nishio, T
   Adachi, H
   Nakagomi, R
   Tokui, T
   Sato, E
   Tanemoto, M
   Fujiwara, K
   Okabe, M
   Onogawa, T
   Suzuki, T
   Nakai, D
   Shiiba, K
   Suzuki, M
   Ohtani, H
   Kondo, Y
   Unno, M
   Ito, S
   Iinuma, K
   Nunoki, K
   Matsuno, S
   Abe, T
TI Molecular identification of a rat novel organic anion transporter moat1,
   which transports prostaglandin D2, leuko-triene
   C4, and taurocholate
SO BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
LA English
DT Article
ID FUNCTIONAL-CHARACTERIZATION; MESSENGER-RNA; HUMAN LIVER; DOMINANT
   EXPRESSION; TISSUE DISTRIBUTION; D RECEPTOR; BRAIN; CLONING; PROTEIN;
   LEPTOMENINGES
AB We have isolated a rat novel multispecific organic anion transporter, moat1, The isolated clones were originated by alternative splicing of the moat1 mRNA. The nucleotide sequences predict a protein of 682 amino acids with moderate sequence similarity to LST-1, the oatp family, and the prostaglandin transporter. Northern blot analysis of rat moat1 identified a predominant transcript of 4.4 kilonucleotides in all tissues. Northern blot and in situ hybridization analyses of rat brain further indicated that moat1 mRNA is widely distributed in neuronal cells of the central nervous system, especially in the hippocampus and cerebellum. moat1 transports prostaglandin D-2 (K-m; 35.5 nM), leukotriene C-4 (K-m; 3.2 mu M) and taurocholate (K-m; 17.6 mu M) in a sodium-independent manner, moat1 also transports prostaglandin E-1, E-2, thromboxane B-2, and iloprost but not dehydroepiandrosterone sulfate and digoxin, of which the substrate specificity is similar, but definitively different from those of any other organic anion transporters, (C) 2000 Academic Press.
C1 Tohoku Univ, Sch Med, Dept Neurophysiol, Aoba Ku, Sendai, Miyagi 9808575, Japan.
   Tohoku Univ, Sch Med, Dept Pediat, Sendai, Miyagi 9808575, Japan.
   Tohoku Univ, Sch Med, Dept Surg 1, Sendai, Miyagi 9808575, Japan.
   Tohoku Univ, Sch Med, Dept Pathol, Sendai, Miyagi 9808575, Japan.
   Tohoku Univ, Sch Med, Dept Internal Med 2, Sendai, Miyagi 9808575, Japan.
   Tohoku Univ, Sch Med, Dept Mol Pharmacol, Sendai, Miyagi 9808575, Japan.
   Sankyo Co Ltd, Analyt & Metab Res Labs, Tokyo 1408710, Japan.
   Univ Tokyo, Fac Med, Dept Nephrol, Tokyo 1138655, Japan.
C3 Tohoku University; Tohoku University; Tohoku University; Tohoku
   University; Tohoku University; Tohoku University; Daiichi Sankyo Company
   Limited; University of Tokyo
RP Abe, T (corresponding author), Tohoku Univ, Sch Med, Dept Neurophysiol, Aoba Ku, 2-1 Seiryo Cho, Sendai, Miyagi 9808575, Japan.
RI Ito, Sadayoshi/A-3933-2015; Unno, Michiaki/AAX-5246-2020
OI Ito, Sadayoshi/0000-0002-5092-3626; Nakai, Daisuke/0009-0009-3678-2976
CR Abe T, 1999, J BIOL CHEM, V274, P17159, DOI 10.1074/jbc.274.24.17159
   ABE T, 1992, J BIOL CHEM, V267, P13361
   Abe T, 1998, J BIOL CHEM, V273, P22395, DOI 10.1074/jbc.273.35.22395
   ANDERSON MW, 1976, PROSTAG OTH LIPID M, V11, P645, DOI 10.1016/0090-6980(76)90067-8
   BAROODY RA, 1981, PROSTAG OTH LIPID M, V21, P133, DOI 10.1016/0090-6980(81)90203-3
   BIOE Y, 1995, J BIOL CHEM, V270, P18910
   BITO LZ, 1972, COMP BIOCHEM PHYSIOL, V43, P65, DOI 10.1016/0300-9629(72)90470-7
   Chan BS, 1998, J BIOL CHEM, V273, P6689, DOI 10.1074/jbc.273.12.6689
   DENZLINGER C, 1985, SCIENCE, V230, P330, DOI 10.1126/science.4048937
   EGUCHI N, 1992, J PHARMACOL EXP THER, V262, P1110
   Gerashchenko D, 1998, J NEUROCHEM, V71, P937
   HAYAISHI O, 1988, J BIOL CHEM, V263, P14593
   HIRATA M, 1994, P NATL ACAD SCI USA, V91, P11192, DOI 10.1073/pnas.91.23.11192
   HORIGUCHI S, 1986, EUR J PHARMACOL, V122, P173, DOI 10.1016/0014-2999(86)90100-7
   IRISH JM, 1979, AM J PHYSIOL, V237, pF268, DOI 10.1152/ajprenal.1979.237.4.F268
   JACQUEMIN E, 1994, P NATL ACAD SCI USA, V91, P133, DOI 10.1073/pnas.91.1.133
   KANAI N, 1995, SCIENCE, V268, P866, DOI 10.1126/science.7754369
   KEMP BE, 1990, TRENDS BIOCHEM SCI, V15, P342, DOI 10.1016/0968-0004(90)90073-K
   KENNELLY PJ, 1991, J BIOL CHEM, V266, P15555
   Kullak-Ublick GA, 1998, FEBS LETT, V424, P173, DOI 10.1016/S0014-5793(98)00168-9
   KULLAKUBLICK GA, 1995, GASTROENTEROLOGY, V109, P1274, DOI 10.1016/0016-5085(95)90588-X
   KYTE J, 1982, J MOL BIOL, V157, P105, DOI 10.1016/0022-2836(82)90515-0
   Li LQ, 1998, J BIOL CHEM, V273, P16184, DOI 10.1074/jbc.273.26.16184
   Lu R, 1996, J CLIN INVEST, V98, P1142, DOI 10.1172/JCI118897
   Masuda S, 1999, MOL PHARMACOL, V55, P743
   MATSUMURA H, 1994, P NATL ACAD SCI USA, V91, P11998, DOI 10.1073/pnas.91.25.11998
   Muller M, 1997, AM J PHYSIOL-GASTR L, V272, pG1285, DOI 10.1152/ajpgi.1997.272.6.G1285
   NARUMIYA S, 1982, LIFE SCI, V31, P2093, DOI 10.1016/0024-3205(82)90101-1
   Noe B, 1997, P NATL ACAD SCI USA, V94, P10346, DOI 10.1073/pnas.94.19.10346
   Oida H, 1997, FEBS LETT, V417, P53, DOI 10.1016/S0014-5793(97)01253-2
   Page RDM, 1996, COMPUT APPL BIOSCI, V12, P357
   PETRIC R, 1994, KIDNEY INT, V46, P1322, DOI 10.1038/ki.1994.401
   Saito H, 1996, J BIOL CHEM, V271, P20719, DOI 10.1074/jbc.271.34.20719
   Schuster VL, 1998, ANNU REV PHYSIOL, V60, P221, DOI 10.1146/annurev.physiol.60.1.221
   Tamai I, 2000, BIOCHEM BIOPH RES CO, V273, P251, DOI 10.1006/bbrc.2000.2922
   THOMPSON JD, 1994, NUCLEIC ACIDS RES, V22, P4673, DOI 10.1093/nar/22.22.4673
   UENO R, 1982, P NATL ACAD SCI-BIOL, V79, P6093, DOI 10.1073/pnas.79.19.6093
   UJIHARA M, 1988, ARCH BIOCHEM BIOPHYS, V260, P521, DOI 10.1016/0003-9861(88)90477-8
   URADE Y, 1993, P NATL ACAD SCI USA, V90, P9070, DOI 10.1073/pnas.90.19.9070
   WATANABE Y, 1986, BRAIN RES, V378, P216, DOI 10.1016/0006-8993(86)90924-8
   WETTSTEIN M, 1990, EUR J BIOCHEM, V191, P251, DOI 10.1111/j.1432-1033.1990.tb19117.x
   YAMASHITA A, 1983, P NATL ACAD SCI-BIOL, V80, P6114, DOI 10.1073/pnas.80.19.6114
NR 42
TC 59
Z9 64
U1 0
U2 1
PU ACADEMIC PRESS INC
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0006-291X
J9 BIOCHEM BIOPH RES CO
JI Biochem. Biophys. Res. Commun.
PD SEP 7
PY 2000
VL 275
IS 3
BP 831
EP 838
DI 10.1006/bbrc.2000.3377
PG 8
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA 353FV
UT WOS:000089264900020
PM 10973807
DA 2025-04-10
ER

PT J
AU Yamashita, T
   Ohneda, O
   Nagano, M
   Iemitsu, M
   Makino, Y
   Tanaka, H
   Miyauchi, T
   Goto, K
   Ohneda, K
   Fujii-Kuriyama, Y
   Poellinger, L
   Yamamoto, M
AF Yamashita, Toshiharu
   Ohneda, Osamu
   Nagano, Masumi
   Iemitsu, Motoyuki
   Makino, Yuichi
   Tanaka, Hirotoshi
   Miyauchi, Takashi
   Goto, Katsutoshi
   Ohneda, Kinuko
   Fujii-Kuriyama, Yoshiaki
   Poellinger, Lorenz
   Yamamoto, Masayuki
TI Abnormal heart development and lung remodeling in mice lacking the
   hypoxia-inducible factor-related basic helix-loop-helix PAS protein
   NEPAS
SO MOLECULAR AND CELLULAR BIOLOGY
LA English
DT Article
ID PERSISTENT PULMONARY-HYPERTENSION; GENE-EXPRESSION; DOMAIN PROTEIN;
   FACTOR 1-ALPHA; ENDOTHELIN-1; VEGF; DEGRADATION; HIF-1-ALPHA;
   HOMEOSTASIS; DEFICIENCY
AB Hypoxia-inducible factors (HIFs) are crucial for oxygen homeostasis during both embryonic development and postnatal life. Here we show that a novel HIF family basic helix-loop-helix (bHLH) PAS (Per-Arnt-Sim) protein, which is expressed predominantly during embryonic and neonatal stages and thereby designated NEPAS (neonatal and embryonic PAS), acts as a negative regulator of HIF-mediated gene expression. NEPAS mRNA is derived from the HIF-3 alpha gene by alternative splicing, replacing the first exon of HIF-3 alpha with that of inhibitory PAS. NEPAS can dimerize with Arnt and exhibits only low levels of transcriptional activity, similar to that of HIF-3a. NEPAS suppressed reporter gene expression driven by HIF-1 alpha and HIF-2 alpha. By generating mice with a targeted disruption of the NEPAS/HIF-3 alpha locus, we found that homozygous mutant mice (NEPAS/ HIF-3 alpha(-/-)) were viable but displayed enlargement of the right ventricle and impaired lung remodeling. The expression of endothelin I and platelet-derived growth factor beta was increased in the lung endothelial cells of NEPAS/HIF-3 alpha-null mice. These results demonstrate a novel regulatory mechanism in which the activities of HIF-1 alpha and HIF-2 alpha are negatively regulated by NEPAS in endothelial cells, which is pertinent to lung and heart development during the embryonic and neonatal stages.
C1 [Yamashita, Toshiharu; Ohneda, Osamu; Nagano, Masumi] Univ Tsukuba, Inst Basic Med Sci, Dept Regenerat Med, Tsukuba, Ibaraki 3058575, Japan.
   [Goto, Katsutoshi] Univ Tsukuba, Inst Basic Med Sci, Dept Regenerat Med, Tsukuba, Ibaraki 3058575, Japan.
   [Iemitsu, Motoyuki] Univ Tsukuba, Dept Mol Pharmacol, Tsukuba, Ibaraki 3058575, Japan.
   [Goto, Katsutoshi] Univ Tsukuba, Inst Basic Med Sci, Inst Hlth & Sport Sci, Tsukuba, Ibaraki 3058575, Japan.
   [Makino, Yuichi; Tanaka, Hirotoshi] Univ Tsukuba, Inst Clin Med, Dept Internal Med, Div Cardiovasc, Tsukuba, Ibaraki 3058575, Japan.
   [Makino, Yuichi; Tanaka, Hirotoshi] Univ Tokyo, Div Clin Immunol, Minato Ku, Tokyo 1088639, Japan.
   [Ohneda, Kinuko] Takasaki Univ Hlth & Welfare, Fac Pharm, Mol Pathophysiol Lab, Takasaki, Gunma 3700033, Japan.
   [Fujii-Kuriyama, Yoshiaki] Univ Tsukuba, Ctr TARA, Tsukuba, Ibaraki 3058575, Japan.
   [Fujii-Kuriyama, Yoshiaki] Univ Tsukuba, JST SORST Project, Tsukuba, Ibaraki 3058575, Japan.
   [Poellinger, Lorenz] Karolinska Inst, Dept Cell & Mol Biol, Med Nobel Inst, S-17177 Stockholm, Sweden.
   [Yamamoto, Masayuki] ERATO, JST, Tsukuba, Ibaraki 3058575, Japan.
   [Yamamoto, Masayuki] Ctr TARA, Tsukuba, Ibaraki 3058575, Japan.
   [Yamamoto, Masayuki] Tohoku Univ, Grad Sch Med, Aoba Ku, Sendai, Miyagi 9808575, Japan.
C3 University of Tsukuba; University of Tsukuba; University of Tsukuba;
   University of Tsukuba; University of Tsukuba; University of Tokyo;
   University of Tsukuba; University of Tsukuba; Karolinska Institutet;
   Japan Science & Technology Agency (JST); University of Tsukuba; Tohoku
   University
RP Ohneda, O (corresponding author), Univ Tsukuba, Inst Basic Med Sci, Dept Regenerat Med, 1-1-1 Tennoudai, Tsukuba, Ibaraki 3058575, Japan.
EM oohneda@md.tsukuba.ac.jp; masi@mail.tains.tohoku.ac.jp
RI Yamamoto, Masayuki/A-4873-2010; Ohneda, Kinuko/AAC-8822-2019; Iemitsu,
   Motoyuki/LOQ-9172-2024
CR Asikainen TM, 2005, FREE RADICAL BIO MED, V38, P1002, DOI 10.1016/j.freeradbiomed.2004.12.004
   Brusselmans K, 2003, J CLIN INVEST, V111, P1519, DOI 10.1172/JCI200315496
   BURRI PH, 1984, ANNU REV PHYSIOL, V46, P617, DOI 10.1146/annurev.ph.46.030184.003153
   Compernolle V, 2002, NAT MED, V8, P702, DOI 10.1038/nm721
   Edelberg JM, 1998, J CLIN INVEST, V102, P837, DOI 10.1172/JCI3058
   Ema M, 1997, P NATL ACAD SCI USA, V94, P4273, DOI 10.1073/pnas.94.9.4273
   Endo A, 2001, EUR J PEDIATR, V160, P217, DOI 10.1007/PL00008431
   Epstein ACR, 2001, CELL, V107, P43, DOI 10.1016/S0092-8674(01)00507-4
   Genbacev O, 2001, DEV BIOL, V233, P526, DOI 10.1006/dbio.2001.0231
   Gu YZ, 1998, GENE EXPRESSION, V7, P205
   Hara S, 2001, BIOCHEM BIOPH RES CO, V287, P808, DOI 10.1006/bbrc.2001.5659
   Huang LE, 1998, P NATL ACAD SCI USA, V95, P7987, DOI 10.1073/pnas.95.14.7987
   Iyer NV, 1998, GENE DEV, V12, P149, DOI 10.1101/gad.12.2.149
   Kakinuma Y, 2001, CIRCULATION, V103, P2387
   Kumar P, 1996, AM J PERINAT, V13, P335, DOI 10.1055/s-2007-994352
   KUWABARA K, 1995, P NATL ACAD SCI USA, V92, P4606, DOI 10.1073/pnas.92.10.4606
   Lee YM, 2001, DEV DYNAM, V220, P175, DOI 10.1002/1097-0177(20010201)220:2<175::AID-DVDY1101>3.0.CO;2-F
   Makino Y, 2002, J BIOL CHEM, V277, P32405, DOI 10.1074/jbc.C200328200
   Makino Y, 2001, NATURE, V414, P550, DOI 10.1038/35107085
   Maulik N, 2002, J CELL MOL MED, V6, P13, DOI 10.1111/j.1582-4934.2002.tb00308.x
   Maxwell PH, 1999, NATURE, V399, P271, DOI 10.1038/20459
   Maynard MA, 2003, J BIOL CHEM, V278, P11032, DOI 10.1074/jbc.M208681200
   Morita M, 2003, EMBO J, V22, P1134, DOI 10.1093/emboj/cdg117
   Ohneda O, 1998, BLOOD, V92, P908
   Peng J, 2000, P NATL ACAD SCI USA, V97, P8386, DOI 10.1073/pnas.140087397
   Rose F, 2002, FASEB J, V16, P1660, DOI 10.1096/fj.02-0420fje
   ROSENBERG AA, 1993, J PEDIATR-US, V123, P109, DOI 10.1016/S0022-3476(05)81552-5
   Schiffrin EL, 2005, VASC PHARMACOL, V43, P19, DOI 10.1016/j.vph.2005.03.004
   Semenza GL, 2004, J APPL PHYSIOL, V96, P1173, DOI 10.1152/japplphysiol.00770.2003
   Shimoda LA, 2001, AM J PHYSIOL-LUNG C, V281, pL202, DOI 10.1152/ajplung.2001.281.1.L202
   SUGIHARA C, 2001, J PEDIATR, V77, pS17
   Tanaka Y, 2004, HYPERTENS RES, V27, P865, DOI 10.1291/hypres.27.865
   Tian H, 1998, GENE DEV, V12, P3320, DOI 10.1101/gad.12.21.3320
   WANG GL, 1995, P NATL ACAD SCI USA, V92, P5510, DOI 10.1073/pnas.92.12.5510
   Wang XJ, 2001, CIRCULATION, V103, P2402, DOI 10.1161/01.cir.103.19.2402
   Weinberger B, 2001, PHARMACOL THERAPEUT, V89, P67, DOI 10.1016/S0163-7258(00)00104-2
   Wenger RH, 1997, BIOL CHEM, V378, P609
   Zheng XW, 2006, MOL CELL BIOL, V26, P4628, DOI 10.1128/MCB.02236-05
NR 38
TC 96
Z9 111
U1 0
U2 6
PU AMER SOC MICROBIOLOGY
PI WASHINGTON
PA 1752 N ST NW, WASHINGTON, DC 20036-2904 USA
SN 0270-7306
EI 1098-5549
J9 MOL CELL BIOL
JI Mol. Cell. Biol.
PD FEB
PY 2008
VL 28
IS 4
BP 1285
EP 1297
DI 10.1128/MCB.01332-07
PG 13
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA 260SD
UT WOS:000253029800009
PM 18070924
OA Green Published
DA 2025-04-10
ER

PT J
AU Kanaji, T
   Vo, MN
   Kanaji, S
   Zarpellon, A
   Shapiro, R
   Morodomi, Y
   Yuzuriha, A
   Eto, K
   Belani, R
   Do, MH
   Yang, XL
   Ruggeri, ZM
   Schimmel, P
AF Kanaji, Taisuke
   Vo, My-Nuong
   Kanaji, Sachiko
   Zarpellon, Alessandro
   Shapiro, Ryan
   Morodomi, Yosuke
   Yuzuriha, Akinori
   Eto, Koji
   Belani, Rajesh
   Do, Minh-Ha
   Yang, Xiang-Lei
   Ruggeri, Zaverio M.
   Schimmel, Paul
TI Tyrosyl-tRNA synthetase stimulates thrombopoietin-independent
   hematopoiesis accelerating recovery from thrombocytopenia
SO PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF
   AMERICA
LA English
DT Article
DE tyrosyl-tRNA synthetase; megakaryopoiesis; thrombocytopenia
ID RECOMBINANT HUMAN INTERLEUKIN-6; HUMAN MEGAKARYOCYTE GROWTH; STEM-CELLS;
   DOUBLE-BLIND; PLATELET PRODUCTION; CRYSTAL-STRUCTURE; EVOLVING ROLE;
   KAPPA-B; EXPRESSION; ERYTHROPOIESIS
AB New mechanisms behind blood cell formation continue to be uncovered, with therapeutic approaches for hematological diseases being of great interest. Here we report an enzyme in protein synthesis, known for cell-based activities beyond translation, is a factor inducing megakaryocyte-biased hematopoiesis, most likely under stress conditions. We show an activated form of tyrosylt-RNA synthetase (YRSACT), prepared either by rationally designed mutagenesis or alternative splicing, induces expansion of a previously unrecognized high-ploidy Sca-1(+) megakaryocyte population capable of accelerating platelet replenishment after depletion. Moreover, YRSACT targets monocytic cells to induce secretion of transacting cytokines that enhance megakaryocyte expansion stimulating the Toll-like receptor/MyD88 pathway. Platelet replenishment by YRSACT is independent of thrombopoietin (TPO), as evidenced by expansion of the megakaryocytes from induced pluripotent stem cell-derived hematopoietic stem cells from a patient deficient in TPO signaling. We suggest megakaryocyte-biased hematopoiesis induced by YRSACT offers new approaches for treating thrombocytopenia, boosting yields from cell-culture production of platelet concentrates for transfusion, and bridging therapy for hematopoietic stem cell transplantation.
C1 [Kanaji, Taisuke; Vo, My-Nuong; Kanaji, Sachiko; Zarpellon, Alessandro; Shapiro, Ryan; Morodomi, Yosuke; Belani, Rajesh; Yang, Xiang-Lei; Ruggeri, Zaverio M.; Schimmel, Paul] Scripps Res Inst, Dept Mol Med, La Jolla, CA 92037 USA.
   [Kanaji, Taisuke; Kanaji, Sachiko; Zarpellon, Alessandro; Morodomi, Yosuke; Ruggeri, Zaverio M.] Scripps Res Inst, MERU Roon Res Ctr Vasc Biol & Thrombosis, La Jolla, CA 92037 USA.
   [Vo, My-Nuong; Kanaji, Sachiko; Shapiro, Ryan; Belani, Rajesh; Yang, Xiang-Lei; Schimmel, Paul] Scripps Res Inst, Scripps Labs TRNA Synthetase Res, La Jolla, CA 92037 USA.
   [Yuzuriha, Akinori; Eto, Koji] Kyoto Univ, Ctr iPS Cell Res & Applicat, Dept Clin Applicat Res, Kyoto 6068507, Japan.
   [Do, Minh-Ha] ATyr Pharma, San Diego, CA 92121 USA.
   [Schimmel, Paul] Scripps Res Inst, Dept Mol Med, Jupiter, FL 33458 USA.
   [Do, Minh-Ha] Lumos Pharma, Austin, TX 78756 USA.
C3 Scripps Research Institute; Scripps Research Institute; Scripps Research
   Institute; Kyoto University; State University System of Florida;
   University of Florida; Herbert Wertheim UF Scripps Institute for
   Biomedical Innovation & Technology
RP Ruggeri, ZM; Schimmel, P (corresponding author), Scripps Res Inst, Dept Mol Med, La Jolla, CA 92037 USA.; Ruggeri, ZM (corresponding author), Scripps Res Inst, MERU Roon Res Ctr Vasc Biol & Thrombosis, La Jolla, CA 92037 USA.; Schimmel, P (corresponding author), Scripps Res Inst, Scripps Labs TRNA Synthetase Res, La Jolla, CA 92037 USA.; Schimmel, P (corresponding author), Scripps Res Inst, Dept Mol Med, Jupiter, FL 33458 USA.
EM ruggeri@scripps.edu; schimmel@scripps.edu
RI Kanaji, Taisuke/AAN-1458-2021; Yang, Xiang-Lei/AAR-7107-2020
OI Morodomi, Yosuke/0000-0002-8882-0833; Yang,
   Xiang-Lei/0000-0003-2554-084X; Kanaji, Taisuke/0000-0002-3588-6038; Do,
   Minh-Ha T./0000-0003-0851-8472
FU aTyr Pharma; NIH [HL117722, HL135294, CA92577, HL129011]; National
   Foundation for Cancer Research; MERU Foundation, Italy
FX We thank L. De Marco and M. Mazzucato (Department of Translational
   Research, National Cancer Center, IRCCS CRO) for providing human
   peripheral blood stem cells. This work was supported by aTyr Pharma, NIH
   Grants HL117722 and HL135294 (to Z.M.R.), CA92577 (to P.S.), and
   HL129011 (to T.K.), and a fellowship from the National Foundation for
   Cancer Research (to P.S.). T.K. is a past recipient, and S.K. and A.Z.
   are current recipients, of Junior Faculty Transition Awards from the
   MERU Foundation, Italy.
CR Abbruzzese L, 2010, VOX SANG, V98, P172, DOI 10.1111/j.1423-0410.2009.01239.x
   Aquino VM, 1998, J PEDIAT HEMATOL ONC, V20, P474, DOI 10.1097/00043426-199809000-00013
   Archimbaud E, 1999, BLOOD, V94, P3694, DOI 10.1182/blood.V94.11.3694.423k18_3694_3701
   Arif A, 2017, NATURE, V542, P357, DOI 10.1038/nature21380
   ASANO S, 1990, BLOOD, V75, P1602
   Ballmaier M, 2011, SEMIN THROMB HEMOST, V37, P673, DOI 10.1055/s-0031-1291377
   Beaulieu LM, 2011, BLOOD, V117, P5963, DOI 10.1182/blood-2010-09-304949
   Beck G, 1996, CYTOKINE, V8, P507, DOI 10.1006/cyto.1996.0069
   Buchmann K, 2014, FRONT IMMUNOL, V5, DOI 10.3389/fimmu.2014.00459
   Chen Q, 2016, NAT REV GENET, V17, P733, DOI 10.1038/nrg.2016.106
   Chow A, 2013, NAT MED, V19, P429, DOI 10.1038/nm.3057
   Debili N, 1996, BLOOD, V88, P1284, DOI 10.1182/blood.V88.4.1284.bloodjournal8841284
   do O PP, 2002, BLOOD, V99, P3939, DOI 10.1182/blood.V99.11.3939
   Erridge C, 2010, J LEUKOCYTE BIOL, V87, P989, DOI 10.1189/jlb.1209775
   Fu GS, 2012, J BIOL CHEM, V287, P9330, DOI 10.1074/jbc.C111.325902
   Torres AG, 2014, TRENDS MOL MED, V20, P306, DOI 10.1016/j.molmed.2014.01.008
   Gekas C, 2013, BLOOD, V121, P4463, DOI 10.1182/blood-2012-09-457929
   Gernsheimer Terry B, 2008, Hematology Am Soc Hematol Educ Program, P219, DOI 10.1182/asheducation-2008.1.219
   GORDON MS, 1995, BLOOD, V85, P3066, DOI 10.1182/blood.V85.11.3066.bloodjournal85113066
   Guo M, 2013, NAT CHEM BIOL, V9, P145, DOI [10.1038/nchembio.1158, 10.1038/NCHEMBIO.1158]
   Guo M, 2010, NAT REV MOL CELL BIO, V11, P668, DOI 10.1038/nrm2956
   Haas S, 2015, CELL STEM CELL, V17, P422, DOI 10.1016/j.stem.2015.07.007
   Han JM, 2012, CELL, V149, P410, DOI 10.1016/j.cell.2012.02.044
   He WW, 2015, NATURE, V526, P710, DOI 10.1038/nature15510
   Hirata S, 2013, J CLIN INVEST, V123, P3802, DOI 10.1172/JCI64721
   Holmes C, 2007, STEM CELLS, V25, P1339, DOI 10.1634/stemcells.2006-0644
   ISHIBASHI T, 1989, BLOOD, V74, P1241
   Kawai T, 2006, CELL DEATH DIFFER, V13, P816, DOI 10.1038/sj.cdd.4401850
   Kawai T, 2007, TRENDS MOL MED, V13, P460, DOI 10.1016/j.molmed.2007.09.002
   Kellum A, 2010, CURR MED RES OPIN, V26, P2339, DOI 10.1185/03007995.2010.510051
   Kim S, 2011, NAT REV CANCER, V11, P708, DOI 10.1038/nrc3124
   Kirchner S, 2015, NAT REV GENET, V16, P98, DOI 10.1038/nrg3861
   Kitajima K, 2011, BLOOD, V117, P3748, DOI 10.1182/blood-2010-07-298596
   Kuter DJ, 2014, BRIT J HAEMATOL, V165, P248, DOI 10.1111/bjh.12781
   Lo WS, 2014, SCIENCE, V345, P328, DOI 10.1126/science.1252943
   Marcus K, 2000, ELECTROPHORESIS, V21, P2622, DOI 10.1002/1522-2683(20000701)21:13<2622::AID-ELPS2622>3.3.CO;2-V
   Mirando AC, 2014, INT J MOL SCI, V15, P23725, DOI 10.3390/ijms151223725
   Motzik A, 2013, TRENDS MOL MED, V19, P726, DOI 10.1016/j.molmed.2013.07.011
   Müller-Newen G, 2017, J LEUKOCYTE BIOL, V101, P1109, DOI 10.1189/jlb.1RU0916-391RR
   Mukhopadhyay R, 2009, TRENDS BIOCHEM SCI, V34, P324, DOI 10.1016/j.tibs.2009.03.004
   Nagai Y, 2006, IMMUNITY, V24, P801, DOI 10.1016/j.immuni.2006.04.008
   National Research Council, 2011, GUIDE CARE USE LAB A
   Nishikii H, 2015, STEM CELLS, V33, P2196, DOI 10.1002/stem.1985
   Nishimura S, 2015, J CELL BIOL, V209, P453, DOI 10.1083/jcb.201410052
   Oshima Y, 2013, INTERNAL MED, V52, P2193, DOI 10.2169/internalmedicine.52.0324
   Pahl HL, 1999, ONCOGENE, V18, P6853, DOI 10.1038/sj.onc.1203239
   Park MC, 2012, P NATL ACAD SCI USA, V109, pE640, DOI 10.1073/pnas.1200194109
   Piccinini AM, 2010, MEDIAT INFLAMM, V2010, DOI 10.1155/2010/672395
   Pitchford SC, 2012, BLOOD, V120, P2787, DOI 10.1182/blood-2011-09-378174
   Ramos P, 2013, NAT MED, V19, P437, DOI 10.1038/nm.3126
   Rodeghiero F, 2017, ANN HEMATOL, V96, P1421, DOI 10.1007/s00277-017-2953-6
   Sajish M, 2015, NATURE, V519, P370, DOI 10.1038/nature14028
   Sampath P, 2004, CELL, V119, P195, DOI 10.1016/j.cell.2004.09.030
   Sanjuan-Pla A, 2013, NATURE, V502, P232, DOI 10.1038/nature12495
   Schiffer CA, 2000, BLOOD, V95, P2530, DOI 10.1182/blood.V95.8.2530.008k31_2530_2535
   Schimmel P, 2018, NAT REV MOL CELL BIO, V19, P45, DOI 10.1038/nrm.2017.77
   Shi Y, 2014, ELIFE, V3, DOI 10.7554/eLife.02349
   Shin JY, 2014, J EXP MED, V211, P217, DOI 10.1084/jem.20131128
   Sim X, 2016, BLOOD, V127, P1227, DOI 10.1182/blood-2015-08-607929
   Son SH, 2014, TOP CURR CHEM, V344, P145, DOI 10.1007/128_2013_476
   Takashima Y, 2014, CELL, V158, P1254, DOI 10.1016/j.cell.2014.08.029
   Takayama N, 2012, METHODS MOL BIOL, V788, P205, DOI 10.1007/978-1-61779-307-3_15
   Tzima E, 2005, J BIOL CHEM, V280, P2405, DOI 10.1074/jbc.C400431200
   Vo MN, 2011, J BIOL CHEM, V286, P11563, DOI 10.1074/jbc.C110.213876
   Wakasugi K, 1998, EMBO J, V17, P297, DOI 10.1093/emboj/17.1.297
   Wakasugi K, 2002, J BIOL CHEM, V277, P20124, DOI 10.1074/jbc.C200126200
   Wakasugi K, 1999, SCIENCE, V284, P147, DOI 10.1126/science.284.5411.147
   Wei N, 2014, MOL CELL, V56, P323, DOI 10.1016/j.molcel.2014.09.006
   Weisser SB, 2012, JOVE-J VIS EXP, DOI 10.3791/4105
   Weyrich AS, 2009, J THROMB HAEMOST, V7, P241, DOI 10.1111/j.1538-7836.2008.03211.x
   Weyrich AS, 2003, J THROMB HAEMOST, V1, P1897, DOI 10.1046/j.1538-7836.2003.00304.x
   Xu XL, 2012, NAT COMMUN, V3, DOI 10.1038/ncomms1686
   Yang XL, 2007, CHEM BIOL, V14, P1323, DOI 10.1016/j.chembiol.2007.10.016
   Yang XL, 2003, HELV CHIM ACTA, V86, P1246, DOI 10.1002/hlca.200390107
   Yang XL, 2002, P NATL ACAD SCI USA, V99, P15369, DOI 10.1073/pnas.242611799
   Yannay-Cohen N, 2009, MOL CELL, V34, P603, DOI 10.1016/j.molcel.2009.05.019
   Yao P, 2014, TOP CURR CHEM, V344, P167, DOI 10.1007/128_2013_422
   Zhou QS, 2010, NAT STRUCT MOL BIOL, V17, P57, DOI 10.1038/nsmb.1706
NR 78
TC 35
Z9 35
U1 1
U2 2
PU NATL ACAD SCIENCES
PI WASHINGTON
PA 2101 CONSTITUTION AVE NW, WASHINGTON, DC 20418 USA
SN 0027-8424
J9 P NATL ACAD SCI USA
JI Proc. Natl. Acad. Sci. U. S. A.
PD AUG 28
PY 2018
VL 115
IS 35
BP EB228
EP EB235
DI 10.1073/pnas.1807000115
PG 8
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA GR7ID
UT WOS:000442861600019
PM 30104364
OA Green Published, hybrid
DA 2025-04-10
ER

PT J
AU Niederländer, N
   Fayein, NA
   Auffray, C
   Pomiès, P
AF Niederländer, N
   Fayein, NA
   Auffray, C
   Pomiès, P
TI Characterization of a new human isoform of the enigma homolog family
   specifically expressed in skeletal muscle
SO BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
LA English
DT Article
DE enigma homolog; skeletal muscle; Z-disk; PDZ domain; alpha-actinin;
   alternative splicing; human isoforms
ID PROTEIN-KINASE-C; LIM DOMAINS; PDZ; GENE; ENH; RECOGNITION; COMPLEX;
   HEART; RIL
AB We have identified a fourth member of the enigma homolog (ENH) family within a pool of human transcripts specifically expressed in skeletal muscle tissue. This new ENH isoform of 215 amino acids is the shorter of the family, it lacks the C-terminal LIM domains present in ENH1 but contains the N-terminal PDZ domain. Northern blot analysis confirmed the muscle specificity of ENH4. Western blot studies of muscle tissues using a non-isoform-specific anti-ENH antibody revealed that ENH4 is present only in skeletal muscle and that there is a specific distribution of ENH members between skeletal and cardiac muscles, which is different in human and mouse. ENH4 was found to co-localize in the sarcomeric Z-band and to interact with alpha-actinin like the other members of the ENH family. Two additional new ENH4 partners of about 34 and 54 kDa were also identified. These results bring new lights on the ENH protein family members. (C) 2004 Elsevier Inc. All rights reserved.
C1 CNRS, Ctr Rech Biochim Macromol, FRE 2593, Montpellier, France.
   CNRS, FRE 2571, Villejuif, France.
C3 Universite de Montpellier; Centre National de la Recherche Scientifique
   (CNRS); Centre National de la Recherche Scientifique (CNRS)
RP CNRS, Ctr Rech Biochim Macromol, FRE 2593, Montpellier, France.
EM pascal.pomies@crbm.cnrs.fr
RI ; Pomies, Pascal/AAC-8037-2020
OI Niederlander, Nicolas/0000-0003-1323-8387; Pomies,
   Pascal/0000-0002-5301-6087
CR Bogoyevitch MA, 1996, INT J BIOCHEM CELL B, V28, P1, DOI 10.1016/1357-2725(95)00142-5
   Brown S, 2001, IUBMB LIFE, V51, P359
   Faulkner G, 1999, J CELL BIOL, V146, P465, DOI 10.1083/jcb.146.2.465
   Khurana T, 2002, PROTOPLASMA, V219, P1, DOI 10.1007/s007090200000
   KIESS M, 1995, ONCOGENE, V10, P61
   Kuroda S, 1996, J BIOL CHEM, V271, P31029, DOI 10.1074/jbc.271.49.31029
   LAU YT, UNPUB
   Maeno-Hikichi Y, 2003, NAT NEUROSCI, V6, P468, DOI 10.1038/nn1041
   Nakagawa N, 2000, BIOCHEM BIOPH RES CO, V272, P505, DOI 10.1006/bbrc.2000.2787
   NOURRY C, 2003, SCI STKE, V22, pRE7
   Perez-Terzic C, 1999, CIRC RES, V84, P1292, DOI 10.1161/01.RES.84.11.1292
   Pietu G, 1996, GENOME RES, V6, P492, DOI 10.1101/gr.6.6.492
   Puceat M, 1996, MOL CELL BIOCHEM, V157, P65
   SANDERMANN H, 1977, EUR J BIOCHEM, V80, P507, DOI 10.1111/j.1432-1033.1977.tb11906.x
   TOWBIN H, 1979, P NATL ACAD SCI USA, V76, P4350, DOI 10.1073/pnas.76.9.4350
   Ueki N, 1999, J HUM GENET, V44, P256, DOI 10.1007/s100380050155
   van Ham M, 2003, MOL BIOL REP, V30, P69, DOI 10.1023/A:1023941703493
   WANG HC, 1995, GENE, V165, P267, DOI 10.1016/0378-1119(95)00542-E
   WU RY, 1994, J BIOL CHEM, V269, P25085
   Xia HH, 1997, J CELL BIOL, V139, P507, DOI 10.1083/jcb.139.2.507
   Zhou Q, 1999, J BIOL CHEM, V274, P19807, DOI 10.1074/jbc.274.28.19807
NR 21
TC 29
Z9 31
U1 0
U2 7
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0006-291X
EI 1090-2104
J9 BIOCHEM BIOPH RES CO
JI Biochem. Biophys. Res. Commun.
PD DEC 24
PY 2004
VL 325
IS 4
BP 1304
EP 1311
DI 10.1016/j.bbrc.2004.10.178
PG 8
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA 877HB
UT WOS:000225557500027
PM 15555569
DA 2025-04-10
ER

PT J
AU Khurana, S
   Peng, SY
   McDonald, E
   Yates, W
   Venkataraman, K
   Tai, TC
AF Khurana, Sandhya
   Peng, Siyuan
   McDonald, Erika
   Yates, William
   Venkataraman, Krishnan
   Tai, T. C.
TI Phenylethanolamine N-methyltransferase gene expression in PC12 cells
   exposed to intermittent hypoxia
SO NEUROSCIENCE LETTERS
LA English
DT Article
DE Catecholamines; OSA; Intermittent hypoxia; PNMT; Hypertension
ID OBSTRUCTIVE SLEEP-APNEA; HYDROXYLASE MESSENGER-RNA; PYRIMIDINE-RICH
   SEQUENCE; TYROSINE-HYDROXYLASE; GLUCOCORTICOID-RECEPTOR; RESISTANT
   HYPERTENSION; ADRENAL-MEDULLA; BLOOD-PRESSURE; STRESS; CATECHOLAMINES
AB Epidemiological studies show a strong correlation between Obstructive Sleep Apnea (OSA) and cardiovascular disorders. OSA patients experience intermittent hypoxia (IH), characterized by brief, but recurring episodes of cessation in breathing. These patients have higher levels of circulating catecholamines and an increased incidence of hypertension; however the mechanisms defining this association are not clearly established. Genetic linkage studies have associated the phenylethanolamine N-methyltransferase (PNMT) gene to the development of hypertension. PNMT, the terminal enzyme in the catecholamine biosynthetic pathway, directly responsible for adrenaline synthesis, is elevated in hypertensive animals. Recent studies utilizing PC12 cells show an increase in the expression of PNMT and its regulatory transcription factors when exposed to continuous hypoxia. The current study examined the regulation of PNMT under conditions of IH. The mRNA of PNMT was analyzed to assess if the regulation of PNMT expression entails alternative splicing. The mRNA and protein of transcription factors HIF1 alpha, Egr-1, GR, and Sp1, were analyzed to assess the cellular pathways involved in regulating PNMT expression. A PNMT promoter-driven luciferase assay was performed to evaluate promoter activity under IH. Preliminary results lay an antecedent for the regulation of PNMT by IH conceivably via an altered regulation of its transcription factors and establish a possible role for PNMT in IH mediated hypertension in OSA patients.
C1 [Khurana, Sandhya; Yates, William; Tai, T. C.] Northern Ontario Sch Med, Med Sci Div, Sudbury, ON, Canada.
   [Peng, Siyuan; Tai, T. C.] Laurentian Univ, Dept Chem & Biochem, Sudbury, ON, Canada.
   [McDonald, Erika] Laurentian Univ, Dept Psychol, Sudbury, ON, Canada.
   [Tai, T. C.] Laurentian Univ, Dept Biol, Sudbury, ON, Canada.
   [Tai, T. C.] Laurentian Univ, Biomol Sci, Sudbury, ON, Canada.
   [Venkataraman, Krishnan] Huntington Univ, Gerontol Dept, Sudbury, ON, Canada.
C3 NOSM University; Laurentian University; Laurentian University;
   Laurentian University; Laurentian University; Laurentian University
RP Tai, TC (corresponding author), Northern Ontario Sch Med, 935 Ramsey Lake Rd, Sudbury, ON P3E 2C6, Canada.
RI Venkataraman, Krishnan/ABB-1062-2020
OI Khurana, Sandhya/0000-0002-3263-9840
FU Natural Sciences and Engineering Research Council of Canada (NSERC);
   Northern Ontario School of Medicine (NOSM) Research Development Fund
FX The Natural Sciences and Engineering Research Council of Canada (NSERC),
   and the Northern Ontario School of Medicine (NOSM) Research Development
   Fund supported this study.
CR [Anonymous], 2011, WHO I Global atlas on cardiovascular disease prevention and control
   Bao G, 1997, J APPL PHYSIOL, V83, P95, DOI 10.1152/jappl.1997.83.1.95
   BOUSSIF O, 1995, P NATL ACAD SCI USA, V92, P7297, DOI 10.1073/pnas.92.16.7297
   BUHLER FR, 1982, J CARDIOVASC PHARM, V4, pS134
   Carretero O. A., 1998, CLIN CARDIOLOGY NEW, P2079
   Coffman TM, 2011, NAT MED, V17, P1402, DOI 10.1038/nm.2541
   Crispo JAG, 2011, OXID MED CELL LONGEV, V2011, DOI 10.1155/2011/756938
   CZYZYKKRZESKA MF, 1994, J BIOL CHEM, V269, P760
   CZYZYKRZESKA MF, 1994, J BIOL CHEM, V269, P9940
   Eisele HJ, 2015, OXID MED CELL LONGEV, V2015, DOI 10.1155/2015/608438
   García-Río F, 2000, CHEST, V117, P1417, DOI 10.1378/chest.117.5.1417
   GOLDSTEIN DS, 1983, HYPERTENSION, V5, P86, DOI 10.1161/01.HYP.5.1.86
   Goodfriend TL, 2004, HYPERTENSION, V43, P518, DOI 10.1161/01.HYP.0000116223.97436.e5
   Gozal E, 2005, J APPL PHYSIOL, V99, P642, DOI 10.1152/japplphysiol.00880.2004
   Grandbois J, 2016, NEUROSCI LETT, V635, P103, DOI 10.1016/j.neulet.2016.10.028
   Kodama T, 2003, J BIOL CHEM, V278, P33384, DOI 10.1074/jbc.M302581200
   KOIKE G, 1995, HYPERTENSION, V26, P595, DOI 10.1161/01.HYP.26.4.595
   Konecny T, 2014, HYPERTENSION, V63, P203, DOI 10.1161/HYPERTENSIONAHA.113.00613
   Kumar GK, 2015, ADV EXP MED BIOL, V860, P195, DOI 10.1007/978-3-319-18440-1_21
   Kumar GK, 2015, RESP PHYSIOL NEUROBI, V209, P115, DOI 10.1016/j.resp.2015.01.001
   Kumar GK, 2003, J APPL PHYSIOL, V95, P536, DOI 10.1152/japplphysiol.00186.2003
   Leonard MO, 2005, J IMMUNOL, V174, P2250, DOI 10.4049/jimmunol.174.4.2250
   Leung AA, 2017, CAN J CARDIOL, V33, P557, DOI 10.1016/j.cjca.2017.03.005
   MARRONE O, 1993, CHEST, V103, P722, DOI 10.1378/chest.103.3.722
   Paulding WR, 1999, J BIOL CHEM, V274, P2532, DOI 10.1074/jbc.274.4.2532
   Pedrosa RP, 2011, HYPERTENSION, V58, P811, DOI 10.1161/HYPERTENSIONAHA.111.179788
   Peng YJ, 2014, P NATL ACAD SCI USA, V111, P1174, DOI 10.1073/pnas.1322172111
   Peppard PE, 2000, NEW ENGL J MED, V342, P1378, DOI 10.1056/NEJM200005113421901
   Prabhakar NR, 2012, J APPL PHYSIOL, V113, P1304, DOI 10.1152/japplphysiol.00444.2012
   Shamsuzzaman ASM, 2003, JAMA-J AM MED ASSOC, V290, P1906, DOI 10.1001/jama.290.14.1906
   Souvannakitti D, 2009, J NEUROPHYSIOL, V101, P2837, DOI 10.1152/jn.00036.2009
   Tai TC, 2010, BRAIN RES, V1353, P14, DOI 10.1016/j.brainres.2010.07.036
   Tai TC, 2009, J NEUROCHEM, V109, P513, DOI 10.1111/j.1471-4159.2009.05978.x
   Unsworth BR, 1999, INT J DEV NEUROSCI, V17, P45, DOI 10.1016/S0736-5748(98)00058-6
   Vardhan Vasu, 2012, Med J Armed Forces India, V68, P33, DOI 10.1016/S0377-1237(11)60128-7
   Wong DL, 2006, CELL MOL NEUROBIOL, V26, P891, DOI 10.1007/s10571-006-9056-6
   Wong DL, 2012, CELL MOL NEUROBIOL, V32, P737, DOI 10.1007/s10571-011-9768-0
   Wong DL, 2010, CELL MOL NEUROBIOL, V30, P1451, DOI 10.1007/s10571-010-9567-z
   Yuan G, 2008, J CELL PHYSIOL, V217, P674, DOI 10.1002/jcp.21537
NR 39
TC 6
Z9 7
U1 0
U2 8
PU ELSEVIER IRELAND LTD
PI CLARE
PA ELSEVIER HOUSE, BROOKVALE PLAZA, EAST PARK SHANNON, CO, CLARE, 00000,
   IRELAND
SN 0304-3940
EI 1872-7972
J9 NEUROSCI LETT
JI Neurosci. Lett.
PD FEB 14
PY 2018
VL 666
BP 169
EP 174
DI 10.1016/j.neulet.2017.12.056
PG 6
WC Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA FX6ZB
UT WOS:000426234700029
PM 29288726
DA 2025-04-10
ER

PT J
AU Houtman, MJC
   Takanari, H
   Kok, BGJM
   van Eck, M
   Montagne, DR
   Vos, MA
   de Boer, TP
   van der Heyden, MAG
AF Houtman, Marien J. C.
   Takanari, Hiroki
   Kok, Bart G. J. M.
   van Eck, Margot
   Montagne, Denise R.
   Vos, Marc A.
   de Boer, Teun P.
   van der Heyden, Marcel A. G.
TI Experimental mapping of the canine KCNJ2 and KCNJ12 gene
   structures and functional analysis of the canine KIR2.2 ion
   channel
SO FRONTIERS IN PHYSIOLOGY
LA English
DT Article
DE inward rectifier current; Canis farniliaris; KCNJ2; KCNJ12; K.2.1;
   K.2.2; genes
ID INWARD RECTIFIER CURRENT; TO-BEAT VARIABILITY; K+ CURRENT I-K1;
   POTASSIUM CHANNEL; KIR2.1; BLOCK; IDENTIFICATION; REPOLARIZATION;
   EXPRESSION; MUTATION
AB For many model organisms traditionally in use for cardiac electrophysiological studies, characterization of ion channel genes is lacking. We focused here on two genes encoding the inward rectifier current, KCNJ2 and KCNJ12, in the dog heart. A combination of RT-PCR, 5'RACE, and 3'-RACE demonstrated the status of KCNJ2 as a two exon gene. The complete open reading frame (ORE) was located on the second exon. One transcription initiation site was mapped. Four differential transcription termination sites were found downstream of two consensus polyadenylation signals. The canine KCNJ12 gene was found to consist of three exons, with its ORE located on the third exon. One transcription initiation and one termination site were found. No alternative splicing was observed in right ventricle or brain cortex. The gene structure of canine KCNJ2 and KCNJ12 was conserved amongst other vertebrates, while current Gen Bank gene annotation was determined as incomplete. In silico translation of KCN12 revealed a non-conserved glycine rich stretch located near the carboxy-terminus of the KIR 2.2 protein. However, no differences were observed when comparing dog with human K1R2.2 protein upon ectopic expression in COS-7 or HEK293 cells with respect to subcellular localization or electrophysiological properties.
C1 [Houtman, Marien J. C.; Takanari, Hiroki; Kok, Bart G. J. M.; van Eck, Margot; Montagne, Denise R.; Vos, Marc A.; de Boer, Teun P.; van der Heyden, Marcel A. G.] Univ Med Ctr Utrecht, Dept Med Physiol, Div Heart & Lungs, NL-3584 CM Utrecht, Netherlands.
C3 Utrecht University; Utrecht University Medical Center
RP van der Heyden, MAG (corresponding author), Univ Med Ctr Utrecht, Dept Med Physiol, Div Heart & Lungs, Yalelaan 50, NL-3584 CM Utrecht, Netherlands.
EM m.a.g.vanderheyden@umcutrecht.nl
RI de Boer, Teun/A-5577-2010
OI de Boer, Teun/0000-0002-0561-6491; van der Heyden,
   Marcel/0000-0002-4225-7942
FU SENSHIN Medical Research Foundation
FX Dr. H. Takanari was supported during this work through the SENSHIN
   Medical Research Foundation.
CR Anumonwo JMB, 2010, J MOL CELL CARDIOL, V48, P45, DOI 10.1016/j.yjmcc.2009.08.013
   Coronel R, 2010, FRONT PHYSIOL, V1, DOI [10.3389/fphys.2010.00008is, 10.3389/fphys.2010.00008]
   de Boer TP, 2010, ACTA PHYSIOL, V199, P243, DOI 10.1111/j.1748-1716.2010.02108.x
   de Boer TP, 2010, BRIT J PHARMACOL, V159, P1532, DOI 10.1111/j.1476-5381.2010.00658.x
   Dhamoon AS, 2005, HEART RHYTHM, V2, P316, DOI 10.1016/j.hrthm.2004.11.012
   Flicek P, 2007, GENOME BIOL, V8, DOI 10.1186/gb-2007-8-12-233
   Gaborit N, 2007, J PHYSIOL-LONDON, V582, P675, DOI 10.1113/jphysiol.2006.126714
   Hugnot JP, 1997, GENOMICS, V39, P113, DOI 10.1006/geno.1996.4450
   Ishihara K, 2004, J PHYSIOL-LONDON, V556, P61, DOI 10.1113/jphysiol.2003.055434
   Ishihara K, 2007, J PHYSIOL-LONDON, V583, P891, DOI 10.1113/jphysiol.2007.136028
   Jansen JA, 2008, BIOCHEM BIOPH RES CO, V367, P687, DOI 10.1016/j.bbrc.2007.12.168
   Kaibara M, 2002, FEBS LETT, V531, P250, DOI 10.1016/S0014-5793(02)03512-3
   Li JD, 2004, AM J PHYSIOL-HEART C, V287, pH2790, DOI 10.1152/ajpheart.00114.2004
   Lindblad-Toh K, 2005, NATURE, V438, P803, DOI 10.1038/nature04338
   Michael G, 2009, CARDIOVASC RES, V81, P491, DOI 10.1093/cvr/cvn266
   Mutai H, 2004, BMC GENOMICS, V5, DOI 10.1186/1471-2164-5-90
   Ojaimi C, 2007, PHYSIOL GENOMICS, V29, P76, DOI 10.1152/physiolgenomics.00159.2006
   Oros A, 2008, PHARMACOL THERAPEUT, V119, P168, DOI 10.1016/j.pharmthera.2008.03.006
   Priori SG, 2005, CIRC RES, V96, P800, DOI 10.1161/01.RES.0000162101.76263.8c
   Redell JB, 1998, J BIOL CHEM, V273, P22807, DOI 10.1074/jbc.273.35.22807
   Roden DM, 1998, PACE, V21, P1029, DOI 10.1111/j.1540-8159.1998.tb00148.x
   Rodriguez-Menchaca AA, 2008, P NATL ACAD SCI USA, V105, P1364, DOI 10.1073/pnas.0708153105
   Ryan DP, 2010, CELL, V140, P88, DOI 10.1016/j.cell.2009.12.024
   Thomsen MB, 2007, CARDIOVASC RES, V73, P521, DOI 10.1016/j.cardiores.2006.11.025
   Thomsen MB, 2006, J AM COLL CARDIOL, V48, P1268, DOI 10.1016/j.jacc.2006.05.048
   Thomsen MB, 2006, PHARMACOL THERAPEUT, V112, P150, DOI 10.1016/j.pharmthera.2005.04.009
   Tian B, 2005, NUCLEIC ACIDS RES, V33, P201, DOI 10.1093/nar/gki158
   Tristani-Firouzi M, 2010, PFLUG ARCH EUR J PHY, V460, P289, DOI 10.1007/s00424-010-0820-6
   Vega AL, 2009, CIRC-ARRHYTHMIA ELEC, V2, P540, DOI 10.1161/CIRCEP.109.872309
   Xia M, 2005, BIOCHEM BIOPH RES CO, V332, P1012, DOI 10.1016/j.bbrc.2005.05.054
   Yan DH, 2005, J PHYSIOL-LONDON, V563, P713, DOI 10.1113/jphysiol.2004.077677
   Yang BF, 2007, NAT MED, V13, P486, DOI 10.1038/nm1569
   Zaritsky JJ, 2001, J PHYSIOL-LONDON, V533, P697, DOI 10.1111/j.1469-7793.2001.t01-1-00697.x
   Zhao J, 1999, MICROBIOL MOL BIOL R, V63, P405, DOI 10.1128/MMBR.63.2.405-445.1999
   Zobel C, 2003, J PHYSIOL-LONDON, V550, P365, DOI 10.1113/jphysiol.2002.036400
NR 35
TC 9
Z9 10
U1 0
U2 4
PU FRONTIERS MEDIA SA
PI LAUSANNE
PA AVENUE DU TRIBUNAL FEDERAL 34, LAUSANNE, CH-1015, SWITZERLAND
SN 1664-042X
J9 FRONT PHYSIOL
JI Front. Physiol.
PY 2012
VL 3
AR 9
DI 10.3389/fphys.2012.00009
PG 9
WC Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Physiology
GA V35UH
UT WOS:000209173000009
PM 22363290
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Pande, J
   Grover, AK
AF Pande, J
   Grover, AK
TI Plasma membrane calcium pumps in smooth muscle: from fictional molecules
   to novel inhibitors
SO CANADIAN JOURNAL OF PHYSIOLOGY AND PHARMACOLOGY
LA English
DT Review
DE ATPases; hypertension; caloxin; protein kinase A; protein kinase C;
   calmodulin
ID SPONTANEOUSLY HYPERTENSIVE-RATS; AORTIC ENDOTHELIAL-CELLS; LACRIMAL
   ACINAR-CELLS; RETICULUM CA2+ PUMP; RED-BLOOD-CELLS;
   SARCOPLASMIC-RETICULUM; CORONARY-ARTERY; CA-2+ PUMP; CA-2&-TRANSPORT
   ATPASE; ABNORMAL BIOCHEMISTRY
AB Plasma membrane Ca2+ pumps (PMCA pumps) are Ca2+-Mg2+ ATPases that expel Ca2+ from the cytosol to extracellular space and are pivotal to cell survival and function. PMCA pumps are encoded by the genes PMCA1, -2, -3, and -4. Alternative splicing results in a large number of isoforms that differ in their kinetics and activation by calmodulin and protein kinases A and C. Expression by 4 genes and a multifactorial regulation provide redundancy to allow for animal survival despite genetic defects. Heterozygous mice with ablation of any of the PMCA genes survive and only the homozygous mice with PMCA1 ablation are embryolethal. Some PMCA isoforms may also be involved in other cell functions. Biochemical and biophysical studies of PMCA pumps have been limited by their low levels of expression. Delineation of the exact physiological roles of PMCA pumps has been difficult since most cells also express sarco/endoplasmic reticulum Ca2+ pumps and a Na+-Ca2+-exchanger, both of which can lower cytosolic Ca2+. A major limitation in the field has been the lack of specific inhibitors of PMCA pumps. More recently, a class of inhibitors named caloxins have emerged, and these may aid in delineating the roles of PMCA pumps.
C1 McMaster Univ, Dept Med, Hamilton, ON L8N 3Z5, Canada.
   McMaster Univ, Dept Biol, Hamilton, ON L8N 3Z5, Canada.
C3 McMaster University; McMaster University
RP McMaster Univ, Dept Med, 1200 Main St W, Hamilton, ON L8N 3Z5, Canada.
EM groverak@mcmaster.ca
CR Afroze T, 2000, J BIOL CHEM, V275, P9062, DOI 10.1074/jbc.275.12.9062
   Antoine S, 2001, J MEMBRANE BIOL, V179, P37, DOI 10.1007/s002320010035
   Armesilla AL, 2004, J BIOL CHEM, V279, P31318, DOI 10.1074/jbc.M307557200
   CANTLEY LC, 1977, J BIOL CHEM, V252, P7421
   Carafoli E, 1997, BASIC RES CARDIOL, V92, P59, DOI 10.1007/BF00794069
   Carafoli E, 2002, P NATL ACAD SCI USA, V99, P1115, DOI 10.1073/pnas.032427999
   Caride AJ, 2001, CELL CALCIUM, V30, P49, DOI 10.1054/ceca.2001.0212
   Chaudhary J, 2001, AM J PHYSIOL-CELL PH, V280, pC1027, DOI 10.1152/ajpcell.2001.280.4.C1027
   Cho WJ, 2005, AM J PHYSIOL-GASTR L, V288, pG571, DOI 10.1152/ajpgi.00222.2004
   Chuhma N, 2002, J NEUROPHYSIOL, V87, P222, DOI 10.1152/jn.00235.2001
   DANIEL EE, 1982, FED PROC, V41, P2898
   Daniels Norman, 2001, American Journal of Bioethics, V1, P2, DOI 10.1162/152651601300168834
   Darby PJ, 2000, AM J PHYSIOL-LUNG C, V279, pL1226, DOI 10.1152/ajplung.2000.279.6.L1226
   De Luisi A, 2003, J CELL SCI, V116, P1527, DOI 10.1242/jcs.00368
   DELASIERRA A, 1990, J HYPERTENS, V8, P285
   DEVINE CE, 1972, J CELL BIOL, V52, P690, DOI 10.1083/jcb.52.3.690
   Goellner GM, 2003, ANN NY ACAD SCI, V986, P461, DOI 10.1111/j.1749-6632.2003.tb07230.x
   Gros R, 2003, CIRC RES, V93, P614, DOI 10.1161/01.RES.0000092142.19896.D9
   GROVER AK, 1983, AM J PHYSIOL, V244, pC158, DOI 10.1152/ajpcell.1983.244.3.C158
   GROVER AK, 1985, AM J PHYSIOL, V248, pC449, DOI 10.1152/ajpcell.1985.248.5.C449
   GROVER AK, 1986, AM J PHYSIOL, V251, pC529, DOI 10.1152/ajpcell.1986.251.4.C529
   Grover AK, 1996, AM J PHYSIOL-CELL PH, V271, pC181, DOI 10.1152/ajpcell.1996.271.1.C181
   GROVER AK, 1985, LIFE SCI, V37, P2193, DOI 10.1016/0024-3205(85)90571-5
   GROVER AK, 1988, J BIOL CHEM, V263, P19510
   GROVER AK, 1992, CELL CALCIUM, V13, P9, DOI 10.1016/0143-4160(92)90025-N
   GROVER AK, 1985, CELL CALCIUM, V6, P227, DOI 10.1016/0143-4160(85)90008-9
   GROVER AK, 1988, AM J PHYSIOL, V255, pC297, DOI 10.1152/ajpcell.1988.255.3.C297
   GROVER AK, 1982, AM J PHYSIOL, V242, pC278, DOI 10.1152/ajpcell.1982.242.5.C278
   Guerini D, 1998, ACTA PHYSIOL SCAND, V163, P265
   Guerini D, 1996, BIOCHEMISTRY-US, V35, P3290, DOI 10.1021/bi952572f
   Hammes A, 1998, CIRC RES, V83, P877
   HASSELBACH W, 1962, BIOCHEM BIOPH RES CO, V7, P132, DOI 10.1016/0006-291X(62)90161-4
   Holmes ME, 2003, CELL CALCIUM, V33, P241, DOI 10.1016/S0143-4160(02)00207-5
   Husain M, 1997, AM J PHYSIOL-CELL PH, V272, pC1947, DOI 10.1152/ajpcell.1997.272.6.C1947
   Iwamoto T, 2004, J PHARMACOL SCI, V96, P27, DOI 10.1254/jphs.FMJ04002X6
   JAMES P, 1988, J BIOL CHEM, V263, P2905
   KATZ S, 1975, BIOCHIM BIOPHYS ACTA, V389, P314, DOI 10.1016/0005-2736(75)90324-7
   Kawano S, 2003, CELL CALCIUM, V34, P145, DOI 10.1016/S0143-4160(03)00069-1
   KHAN I, 1991, BIOCHEM J, V277, P345, DOI 10.1042/bj2770345
   KLAVEN NB, 1983, ARCH BIOCHEM BIOPHYS, V226, P618, DOI 10.1016/0003-9861(83)90331-4
   Kozel PJ, 1998, J BIOL CHEM, V273, P18693, DOI 10.1074/jbc.273.30.18693
   Krizaj D, 2002, J COMP NEUROL, V451, P1, DOI 10.1002/cne.10281
   Krizaj D, 1998, NEURON, V21, P249, DOI 10.1016/S0896-6273(00)80531-0
   KWAN CY, 1990, J BIOL CHEM, V265, P678
   KWAN CY, 1980, BLOOD VESSELS, V17, P131
   KWAN CY, 1980, MOL PHARMACOL, V17, P137
   KWAN CY, 1979, BLOOD VESSELS, V16, P259
   KWAN CY, 1990, AM J PHYSIOL, V258, pC1006, DOI 10.1152/ajpcell.1990.258.6.C1006
   KWAN CY, 1983, PREP BIOCHEM, V13, P275, DOI 10.1080/00327488308068175
   Lehotsky J, 2002, FRONT BIOSCI-LANDMRK, V7, pD53, DOI 10.2741/lehotsky
   LEVITSKY DO, 1993, J BIOL CHEM, V268, P8325
   Liang W, 2004, CELL CALCIUM, V36, P431, DOI 10.1016/j.ceca.2004.04.003
   MATLIB MA, 1979, J BIOL CHEM, V254, P1834
   Misquitta CM, 1999, CELL CALCIUM, V25, P277, DOI 10.1054/ceca.1999.0032
   MISSIAEN L, 1991, PHARMACOL THERAPEUT, V50, P191, DOI 10.1016/0163-7258(91)90014-D
   MISSIAEN L, 1992, PHARMACOL THERAPEUT, V56, P191, DOI 10.1016/0163-7258(92)90017-T
   Monteith GR, 1997, BIOCHEM BIOPH RES CO, V230, P344, DOI 10.1006/bbrc.1996.5956
   Moreau R, 2003, MOL REPROD DEV, V64, P189, DOI 10.1002/mrd.10247
   Morgans CW, 1998, J NEUROSCI, V18, P2467
   Nazer MA, 1998, AM J PHYSIOL-HEART C, V274, pH123, DOI 10.1152/ajpheart.1998.274.1.H123
   NIGGLI V, 1981, J BIOL CHEM, V256, P395
   Okunande GW, 2004, J BIOL CHEM, V279, P33742, DOI 10.1074/jbc.M404628200
   Palacios J, 2003, BBA-BIOMEMBRANES, V1611, P197, DOI 10.1016/S0005-2736(03)00057-9
   Pande I, 2005, EUR J PHARMACOL, V508, P1, DOI 10.1016/j.ejphar.2004.11.057
   Pande J, 2005, CELL CALCIUM, V37, P245, DOI 10.1016/j.ceca.2004.10.004
   Penniston JT, 1998, J MEMBRANE BIOL, V165, P101, DOI 10.1007/s002329900424
   Philipson KD, 2002, ANN NY ACAD SCI, V976, P1
   Pinet C, 2002, J MEMBRANE BIOL, V187, P185, DOI 10.1007/s00232-001-0163-5
   Postnov Y V, 1983, J Hypertens Suppl, V1, P9
   Schuh K, 2004, J BIOL CHEM, V279, P28220, DOI 10.1074/jbc.M312599200
   Schuh K, 2003, J BIOL CHEM, V278, P41246, DOI 10.1074/jbc.M307606200
   Shmigol A, 1998, PFLUG ARCH EUR J PHY, V437, P158, DOI 10.1007/s004240050761
   Shull GE, 2003, ANN NY ACAD SCI, V986, P453, DOI 10.1111/j.1749-6632.2003.tb07229.x
   SKOU JC, 1981, BIOCHIM BIOPHYS ACTA, V647, P232, DOI 10.1016/0005-2736(81)90251-0
   Slinchenko NN, 1998, BIOCHEMISTRY-MOSCOW+, V63, P685
   SOMLYO AP, 1971, J CELL BIOL, V51, P722, DOI 10.1083/jcb.51.3.722
   SPENCER GG, 1991, BIOCHIM BIOPHYS ACTA, V1063, P15, DOI 10.1016/0005-2736(91)90347-B
   Storozhevykh TP, 2003, B EXP BIOL MED+, V135, P139, DOI 10.1023/A:1023811613109
   Strehler EE, 2004, CURR MOL MED, V4, P323, DOI 10.2174/1566524043360735
   STREHLER EE, 1991, ADV EXP MED BIOL, V307, P251
   Strehler EE, 2001, PHYSIOL REV, V81, P21, DOI 10.1152/physrev.2001.81.1.21
   Suzuki S, 2002, J NEUROPHYSIOL, V87, P1816, DOI 10.1152/jn.00456.2001
   Toyoshima C, 2000, NATURE, V405, P647, DOI 10.1038/35015017
   VERBIST J, 1986, BIOCHEM J, V240, P633, DOI 10.1042/bj2400633
   VINCENZI FF, 1986, HYPERTENSION, V8, P1058, DOI 10.1161/01.HYP.8.11.1058
   Wang K K, 1992, Trends Cell Biol, V2, P46, DOI 10.1016/0962-8924(92)90162-G
   Wang X, 2002, CELL CALCIUM, V31, P265, DOI 10.1016/S0143-4160(02)00075-1
   Wood JD, 2004, JARO-J ASSOC RES OTO, V5, P99, DOI 10.1007/s10162-003-4022-1
   WUYTACK F, 1989, BIOCHEM J, V257, P117, DOI 10.1042/bj2570117
   WUYTACK F, 1983, FEBS LETT, V154, P191, DOI 10.1016/0014-5793(83)80901-6
   WUYTACK F, 1978, BIOCHIM BIOPHYS ACTA, V540, P253, DOI 10.1016/0304-4165(78)90138-1
   WUYTACK F, 1984, BIOCHEM J, V224, P445, DOI 10.1042/bj2240445
   Young HS, 2004, J MEMBRANE BIOL, V198, P55, DOI 10.1007/s00232-004-0666-y
   Zylinska L, 2000, ACTA BIOCHIM POL, V47, P529
NR 94
TC 17
Z9 19
U1 0
U2 1
PU CANADIAN SCIENCE PUBLISHING, NRC RESEARCH PRESS
PI OTTAWA
PA 65 AURIGA DR, SUITE 203, OTTAWA, ON K2E 7W6, CANADA
SN 0008-4212
EI 1205-7541
J9 CAN J PHYSIOL PHARM
JI Can. J. Physiol. Pharmacol.
PD AUG-SEP
PY 2005
VL 83
IS 8-9
BP 743
EP 754
DI 10.1139/Y05-075
PG 12
WC Pharmacology & Pharmacy; Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Pharmacology & Pharmacy; Physiology
GA 987RO
UT WOS:000233535200011
PM 16333376
DA 2025-04-10
ER

PT J
AU Price, DA
   Doble, KE
   Lesser, W
   Greenberg, MJ
   Swiderek, KM
   Lee, TD
   Lutz, EM
   Sommerville, J
   Falconer, S
   Cottrell, GA
AF Price, DA
   Doble, KE
   Lesser, W
   Greenberg, MJ
   Swiderek, KM
   Lee, TD
   Lutz, EM
   Sommerville, J
   Falconer, S
   Cottrell, GA
TI The peptide pQFYRFamide is encoded on the FMRFamide precursor of the
   snail Helix aspersa but does not activate the FMRFamide-gated sodium
   current
SO BIOLOGICAL BULLETIN
LA English
DT Article
ID NEUROPEPTIDE PHE-MET-ARG-PHE-NH2 FMRFAMIDE; MOLLUSCAN CARDIOEXCITATORY
   NEUROPEPTIDE; MUTUALLY EXCLUSIVE EXPRESSION; CARDIOACTIVE PEPTIDES;
   LYMNAEA-STAGNALIS; NEURONS; GENE; APLYSIA; CHANNEL; FAMILY
AB The complete sequence of the FMRFamide precursor cDNA from Helix aspersa is reported here. Since the 5' end of this cDNA is identical to that of the precursor that encodes the heptapeptide analogs of FLRFamide, the two transcripts are probably derived by alternative RNA splicing. A novel pentapeptide, Glp-Phe-Tyr-Arg-Phe-NH2 (pQFYRFamide), predicted from the cDNA sequence, was purified from extracts of H. aspersa ganglia and identified by mass spectroscopy, Partial gene sequences for the FMRFamide precursors of two closely related pulmonate species-Cepaea nemoralis and Polydontes acutangula-were also determined and compared with the cDNA sequence of H. aspersa and a partial gene sequence previously determined from H. pomatia. Not only are the FMRFamide-related sequences and proteolytic processing sites conserved, but the linear arrangement of these landmarks is also retained. Synthetic pQFYRFamide has some effects on the isolated heart and on neuronal potassium currents in H. aspersa that are similar to those of FMRFamide, but it does not activate the neuronal FMRFamide-gated sodium channel.
C1 CITY HOPE NATL MED CTR,BECKMAN RES INST,DUARTE,CA 91010.
   UNIV ST ANDREWS,SCH BIOL & MED SCI,ST ANDREWS KY16 9TS,FIFE,SCOTLAND.
C3 City of Hope; Beckman Research Institute of City of Hope; University of
   St Andrews
RP Price, DA (corresponding author), UNIV FLORIDA,WHITNEY LAB,9505 OCEAN SHORE BLVD,ST AUGUSTINE,FL 32086, USA.
FU NHLBI NIH HHS [HL 28440] Funding Source: Medline
CR ALVAREZLEEFMANS FJ, 1982, SOC NEUR ABSTR, V8, P684
   BENJAMIN PR, 1994, BIOESSAYS, V16, P335, DOI 10.1002/bies.950160508
   BRIGHT K, 1993, J NEUROSCI, V13, P2719, DOI 10.1523/JNEUROSCI.13-06-02719.1993
   Burke J. F., 1993, Society for Neuroscience Abstracts, V19, P1274
   COLOMBAIONI L, 1985, J NEUROSCI, V5, P2533
   COTTRELL GA, 1987, J PHYSIOL-LONDON, V382, P51, DOI 10.1113/jphysiol.1987.sp016355
   COTTRELL GA, 1984, J PHYSIOL-LONDON, V356, P315, DOI 10.1113/jphysiol.1984.sp015467
   COTTRELL GA, 1992, BIOL BULL, V183, P113, DOI 10.2307/1542412
   COTTRELL GA, 1994, MOL CELL NEUROSCI, V5, P632, DOI 10.1006/mcne.1994.1077
   COTTRELL GA, 1990, PFLUG ARCH EUR J PHY, V416, P612, DOI 10.1007/BF00382698
   COTTRELL GA, 1987, J PHYSIOL-LONDON, V392, pP33
   Davis M. T., 1994, Methods (Orlando), V6, P304, DOI 10.1006/meth.1994.1031
   DAVIS MT, 1995, J AM SOC MASS SPECTR, V6, P571, DOI 10.1016/1044-0305(95)00192-G
   FISHER JM, 1988, CELL, V54, P813, DOI 10.1016/S0092-8674(88)91131-2
   GREEN KA, 1994, PFLUG ARCH EUR J PHY, V428, P232, DOI 10.1007/BF00724502
   GREENBERG MJ, 1992, PROG BRAIN RES, V92, P25, DOI 10.1016/S0079-6123(08)61162-0
   HOSAKA M, 1991, J BIOL CHEM, V266, P12127
   Kellett E, 1996, J NEUROSCI, V16, P4949
   LEHMAN HK, 1987, J EXP BIOL, V131, P55
   LESSER W, 1993, J EXP BIOL, V178, P205
   LINACRE A, 1990, J NEUROSCI, V10, P412
   LINGUEGLIA E, 1995, NATURE, V378, P730, DOI 10.1038/378730a0
   LUTZ EM, 1992, MOL CELL NEUROSCI, V3, P373, DOI 10.1016/1044-7431(92)90049-8
   MILLER MW, 1993, J NEUROSCI, V13, P3358
   NEWCOMB R, 1988, J BIOL CHEM, V263, P12514
   PAYZA K, 1987, PEPTIDES, V8, P1065, DOI 10.1016/0196-9781(87)90138-0
   PRICE DA, 1977, SCIENCE, V197, P670, DOI 10.1126/science.877582
   PRICE DA, 1990, J EXP BIOL, V154, P421
   SAUNDERS SE, 1991, J NEUROSCI, V11, P740
   SAUNDERS SE, 1992, J NEUROSCI, V12, P1033
   SCHAEFER M, 1985, CELL, V41, P457, DOI 10.1016/S0092-8674(85)80019-2
   Swiderek KM, 1996, METHOD ENZYMOL, V271, P68
   TAUSSIG R, 1986, DNA-J MOLEC CELL BIO, V5, P453, DOI 10.1089/dna.1.1986.5.453
   WHITEHOUSE EH, 1991, BIOTECHNIQUES, V11, P617
NR 34
TC 18
Z9 18
U1 0
U2 1
PU MARINE BIOLOGICAL LABORATORY
PI WOODS HOLE
PA 7 MBL ST, WOODS HOLE, MA 02543
SN 0006-3185
J9 BIOL BULL
JI Biol. Bull.
PD DEC
PY 1996
VL 191
IS 3
BP 341
EP 352
DI 10.2307/1543007
PG 12
WC Biology; Marine & Freshwater Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Life Sciences & Biomedicine - Other Topics; Marine & Freshwater Biology
GA WA834
UT WOS:A1996WA83400002
PM 8976594
OA Green Submitted
DA 2025-04-10
ER

PT J
AU Liu, L
   O'Hara, DS
   Cala, SE
   Poornima, I
   Hines, RN
   Marsh, JD
AF Liu, L
   O'Hara, DS
   Cala, SE
   Poornima, I
   Hines, RN
   Marsh, JD
TI Developmental regulation of the L-type calcium channel α1C
   subunit expression in heart
SO MOLECULAR AND CELLULAR BIOCHEMISTRY
LA English
DT Article
DE dihydropyridine receptor; development; heart; calcium channel; rat
ID ADULT CARDIAC MYOCYTES; CA2+ CHANNEL; SKELETAL-MUSCLE; ALPHA-1 SUBUNIT;
   RAT-HEART; VENTRICULAR MYOCYTES; CALSEQUESTRIN GENES; CARBOXYL-TERMINUS;
   PHOSPHORYLATION; NEURONS
AB We used Northern analyses, RNase protection assays and immunoblot analyses to examine the relationship among developmental age of the heart, abundance of mRNA and L-type calcium channel alpha(1C) subunit protein, and to establish the size of the native protein in heart. Northern analysis, RNase protection assays, and immunoblots were used to study RNA and protein from rat heart of various ages. In fetal and adult ventricles there was a predominant 8.3-kb transcript for the alpha(1C) subunit with no change in transcript size during development. RNase protection assays demonstrated a 2-fold increase in abundance of the DHP receptor message during postnatal development. Immunoblots identified a 240 kD protein, corresponding to the predicted molecular mass of the full length alpha(1C) subunit. No change in size of protein for the alpha(1C) subunit was observed at any developmental stage and there was no evidence for a truncated isoform. There was an approximate 2-fold increase in alpha(1C) subunit protein in ventricular homogenates during postnatal development. Thus, in the developing rat heart, alterations in calcium channel properties during development appear to result neither from alternative splicing that produces a smaller transcript for the alpha(1C) subunit nor from expression of a truncated protein, but at least in part from transcriptionally-regulated expression of the 240 kDa polypeptide.
C1 Wayne State Univ, Sch Med, Program Mol & Cellular Biol, Dept Internal Med, Detroit, MI 48201 USA.
   Brigham & Womens Hosp, Div Cardiovasc, Boston, MA 02115 USA.
   Wayne State Univ, Sch Med, Dept Pharmacol, Detroit, MI 48201 USA.
C3 Wayne State University; Harvard University; Harvard University Medical
   Affiliates; Brigham & Women's Hospital; Wayne State University
RP Marsh, JD (corresponding author), Wayne State Univ, Sch Med, Program Mol & Cellular Biol, Dept Internal Med, 421 E Canfield Ave, Detroit, MI 48201 USA.
OI Hines, Ronald/0000-0002-3094-4200
FU NHLBI NIH HHS [HL54086, HL35781] Funding Source: Medline
CR AIBA S, 1993, CIRC RES, V72, P396, DOI 10.1161/01.RES.72.2.396
   ARTMAN M, 1992, AM J PHYSIOL, V263, pH1506, DOI 10.1152/ajpheart.1992.263.5.H1506
   BRILLANTES AMB, 1994, CIRC RES, V75, P503, DOI 10.1161/01.RES.75.3.503
   CALA SE, 1992, BIOCHIM BIOPHYS ACTA, V1118, P277, DOI 10.1016/0167-4838(92)90285-L
   CHANG FC, 1988, J BIOL CHEM, V263, P929
   CHIEN AJ, 1995, J BIOL CHEM, V270, P30036
   CHURCH GM, 1984, P NATL ACAD SCI-BIOL, V81, P1991, DOI 10.1073/pnas.81.7.1991
   COHEN NM, 1988, J PHYSIOL-LONDON, V406, P115, DOI 10.1113/jphysiol.1988.sp017372
   Davidoff AJ, 1997, J MOL CELL CARDIOL, V29, P1791, DOI 10.1006/jmcc.1997.0406
   DeJongh KS, 1996, BIOCHEMISTRY-US, V35, P10392, DOI 10.1021/bi953023c
   DEJONGH KS, 1991, P NATL ACAD SCI USA, V88, P10778, DOI 10.1073/pnas.88.23.10778
   DIEBOLD RJ, 1992, P NATL ACAD SCI USA, V89, P1497, DOI 10.1073/pnas.89.4.1497
   FARRELL R, 1993, RNA METHODOLOGIES LA
   Haase H, 1996, J MOL MED-JMM, V74, P99
   HELL JW, 1993, J BIOL CHEM, V268, P1945
   HOSEY MM, 1989, ANN NY ACAD SCI, V560, P27, DOI 10.1111/j.1749-6632.1989.tb24076.x
   HUYNH TV, 1992, CIRC RES, V70, P508, DOI 10.1161/01.RES.70.3.508
   KIM D, 1987, J CLIN INVEST, V80, P88, DOI 10.1172/JCI113068
   LIU L, 1995, CIRCULATION, V92, P372
   LOMPRE AM, 1991, CIRC RES, V69, P1380, DOI 10.1161/01.RES.69.5.1380
   MARSH JD, 1989, AM J PHYSIOL, V256, pH179, DOI 10.1152/ajpheart.1989.256.1.H179
   MARSH JD, 1989, J CLIN INVEST, V84, P817, DOI 10.1172/JCI114241
   MIKAMI A, 1989, NATURE, V340, P230, DOI 10.1038/340230a0
   Mitterdorfer J, 1996, BIOCHEMISTRY-US, V35, P9400, DOI 10.1021/bi960683o
   OGAWA S, 1992, J CLIN INVEST, V89, P1085, DOI 10.1172/JCI115688
   SANGER F, 1977, P NATL ACAD SCI USA, V74, P5463, DOI 10.1073/pnas.74.12.5463
   SCHMIDT JW, 1986, CELL, V46, P437, DOI 10.1016/0092-8674(86)90664-1
   SOLDATOV NM, 1995, J BIOL CHEM, V270, P10540, DOI 10.1074/jbc.270.18.10540
   SOLDATOV NM, 1994, GENOMICS, V22, P77, DOI 10.1006/geno.1994.1347
   TAKAHASHI T, 1992, J CLIN INVEST, V90, P927, DOI 10.1172/JCI115969
   TOHSE N, 1992, J PHYSIOL-LONDON, V451, P295, DOI 10.1113/jphysiol.1992.sp019165
   WEI XY, 1994, J BIOL CHEM, V269, P1635
   WETZEL GT, 1991, PEDIATR RES, V30, P89, DOI 10.1203/00006450-199107000-00018
   Wyatt CN, 1997, J PHYSIOL-LONDON, V502, P307, DOI 10.1111/j.1469-7793.1997.307bk.x
   YANEY GC, 1992, MOL ENDOCRINOL, V6, P2143, DOI 10.1210/me.6.12.2143
   YOSHIDA A, 1992, FEBS LETT, V309, P343, DOI 10.1016/0014-5793(92)80804-P
NR 36
TC 18
Z9 18
U1 0
U2 0
PU KLUWER ACADEMIC PUBL
PI DORDRECHT
PA SPUIBOULEVARD 50, PO BOX 17, 3300 AA DORDRECHT, NETHERLANDS
SN 0300-8177
J9 MOL CELL BIOCHEM
JI Mol. Cell. Biochem.
PD FEB
PY 2000
VL 205
IS 1-2
BP 101
EP 109
PG 9
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA 288QU
UT WOS:000085575400011
PM 10821427
DA 2025-04-10
ER

PT J
AU Cabral, RM
   Liu, L
   Hogan, C
   Dopping-Hepenstal, PJC
   Winik, BC
   Asial, RA
   Dobson, R
   Mein, CA
   Baselaga, PA
   Mellerio, JE
   Nanda, A
   Boente, MD
   Kelsell, DP
   McGrath, JA
   South, AP
AF Cabral, Rita M.
   Liu, Lu
   Hogan, Carol
   Dopping-Hepenstal, Patricia J. C.
   Winik, Beatriz C.
   Asial, Raul A.
   Dobson, Richard
   Mein, Charles A.
   Baselaga, Patricia A.
   Mellerio, Jemima E.
   Nanda, Arti
   del Carmen Boente, Maria
   Kelsell, David P.
   McGrath, John A.
   South, Andrew P.
TI Homozygous Mutations in the 5′ Region of the JUP Gene Result in
   Cutaneous Disease but Normal Heart Development in Children
SO JOURNAL OF INVESTIGATIVE DERMATOLOGY
LA English
DT Article
ID RIGHT-VENTRICULAR CARDIOMYOPATHY; GROWTH-FACTOR RECEPTOR; BETA-CATENIN;
   HUMAN PLAKOGLOBIN; EMBRYONIC HEART; NAXOS-DISEASE; CADHERIN; DOMAINS;
   PROTEIN; IDENTIFICATION
AB Desmosomes are intercellular adhesive junctions and attachment sites for the intermediate filament (IF) cytoskeleton, prominent in tissues subject to high levels of mechanical stress such as the epidermis and heart. The obligate desmosomal constituent, plakoglobin (PG), is involved in coupling transmembrane desmosomal components with IFs. PG also contributes to intercellular adhesion through adherens junctions and has additional signaling roles. To date, two mutations in the gene encoding PG, JUP, have been described, and in both instances, patients harboring pathogenic mutations suffered from arrhythmogenic right ventricular cardiomyopathy with or without skin abnormalities. We describe homozygous nonsense mutation, p.S24X, and homozygous splice site mutation, c.468G>A, in the JUP gene that results in skin fragility, diffuse palmoplantar keratoderma, and woolly hair with no symptoms of cardiomyopathy. We show barely detectable levels of PG immunostaining in skin sections from patients harboring these mutations and show that an alternative AUG codon in p.S24X mRNA translates a 42-amino-acid N-terminal truncation. We conclude that PG is required for correct maintenance of skin integrity, and the absence of heart phenotype in patients suggests that aberrant PG expression does not compromise normal human heart development in children. Our findings provide new insight into the distinct roles that PG has in the epidermis and heart.
C1 [Hogan, Carol; South, Andrew P.] Univ Dundee, Ninewells Hosp & Med Sch, Dept Surg & Mol Oncol, Dundee DD1 9SY, Scotland.
   [Cabral, Rita M.; Kelsell, David P.; South, Andrew P.] Univ London, Ctr Cutaneous Res, Inst Cell & Mol Sci, Barts & London Sch Med & Dent, London, England.
   [Liu, Lu; Dopping-Hepenstal, Patricia J. C.] St Thomas Hosp, Natl Diagnost Epidermolysis Bullosa Lab, GSTS Pathol, London, England.
   [Winik, Beatriz C.] Univ Nacl Tucuman, CONICET, INSIBIO, Serv Microscopia Elect, San Miguel De Tucuman, Argentina.
   [Asial, Raul A.] Univ Nacl Tucuman, Fac Med, San Miguel De Tucuman, Argentina.
   [Dobson, Richard; Mein, Charles A.] Univ London, Genome Ctr, Queen Marys Sch Med & Dent, London, England.
   [Baselaga, Patricia A.] Hosp Nino Jesus, Dept Cardiol, San Miguel De Tucuman, Argentina.
   [Mellerio, Jemima E.; McGrath, John A.] Kings Coll London, Genet Skin Dis Grp, St Johns Inst Dermatol, London WC2R 2LS, England.
   [Mellerio, Jemima E.; McGrath, John A.] St Thomas Sch Med, London WC2R 2LS, England.
   [Nanda, Arti] Asad Al Hamad Dermatol Ctr, Kuwait, Kuwait.
   [del Carmen Boente, Maria] Hosp Nino Jesus, Dept Dermatol, San Miguel De Tucuman, Argentina.
C3 University of Dundee; University of London; Queen Mary University
   London; Guy's & St Thomas' NHS Foundation Trust; Consejo Nacional de
   Investigaciones Cientificas y Tecnicas (CONICET); Universidad Nacional
   de Tucuman; Universidad Nacional de Tucuman; University of London; Queen
   Mary University London; University of London; King's College London;
   University of London; King's College London
RP South, AP (corresponding author), Univ Dundee, Ninewells Hosp & Med Sch, Dept Surg & Mol Oncol, Dundee DD1 9SY, Scotland.
EM a.p.south@dundee.ac.uk
RI Kelsell, David/F-8767-2011; McGrath, John/N-3529-2019; Cabral,
   Rita/G-5706-2013; Nanda, Arti/H-8565-2019; dobson, richard/C-9269-2011;
   Mellerio, Jemima/G-3681-2012; McGrath, John/D-6824-2012
OI dobson, richard/0000-0003-4224-9245; Cabral, Rita/0000-0003-2741-8100;
   Mellerio, Jemima/0000-0002-2670-8117; Mein, Charles/0000-0003-0811-9658;
   McGrath, John/0000-0002-3708-9964; Nanda, Arti/0000-0002-1223-3181;
   Kelsell, David/0000-0002-9910-7144
FU Barts and the London Charity; Medical Research Council; Dystrophic
   Epidermolysis Research Association UK; European Commission
   [LSHM-CT-2005-512117]
FX This work was supported by Barts and the London Charity, the Medical
   Research Council, the Dystrophic Epidermolysis Research Association UK,
   and by the European Commission (no. LSHM-CT-2005-512117).
CR Aberle H, 1997, EMBO J, V16, P3797, DOI 10.1093/emboj/16.13.3797
   Asimaki A, 2007, AM J HUM GENET, V81, P964, DOI 10.1086/521633
   Asimaki A, 2009, NEW ENGL J MED, V360, P1075, DOI 10.1056/NEJMoa0808138
   Bierkamp C, 1996, DEV BIOL, V180, P780, DOI 10.1006/dbio.1996.0346
   COWIN P, 1986, CELL, V46, P1063, DOI 10.1016/0092-8674(86)90706-3
   FRANKE WW, 1989, P NATL ACAD SCI USA, V86, P4027, DOI 10.1073/pnas.86.11.4027
   Garcia-Gras E, 2006, J CLIN INVEST, V116, P2012, DOI 10.1172/JCI27751
   Gaudry CA, 2001, J BIOL CHEM, V276, P24871, DOI 10.1074/jbc.M102731200
   Green KJ, 2000, NAT REV MOL CELL BIO, V1, P208, DOI 10.1038/35043032
   Kowalczyk AP, 1997, J CELL BIOL, V139, P773, DOI 10.1083/jcb.139.3.773
   Lai-Cheong JE, 2007, J INVEST DERMATOL, V127, P2713, DOI 10.1038/sj.jid.5700727
   McKoy G, 2000, LANCET, V355, P2119, DOI 10.1016/S0140-6736(00)02379-5
   North AJ, 1999, J CELL SCI, V112, P4325
   Palka HL, 1997, J CELL SCI, V110, P2359
   PARRISH EP, 1987, J PATHOL, V153, P265, DOI 10.1002/path.1711530311
   Protonotarios N, 2001, J AM COLL CARDIOL, V38, P1477, DOI 10.1016/S0735-1097(01)01568-6
   Purcell S, 2007, AM J HUM GENET, V81, P559, DOI 10.1086/519795
   Rogan PK, 1998, HUM MUTAT, V12, P153, DOI 10.1002/(SICI)1098-1004(1998)12:3<153::AID-HUMU3>3.0.CO;2-I
   Ruiz P, 1996, J CELL BIOL, V135, P215, DOI 10.1083/jcb.135.1.215
   SACCO PA, 1995, J BIOL CHEM, V270, P20201, DOI 10.1074/jbc.270.34.20201
   Sadot E, 2000, ONCOGENE, V19, P1992, DOI 10.1038/sj.onc.1203519
   Seldin MF, 2007, AM J PHYS ANTHROPOL, V132, P455, DOI 10.1002/ajpa.20534
   South AP, 2003, J CELL SCI, V116, P3303, DOI 10.1242/jcs.00636
   Whittock NV, 2000, EXP DERMATOL, V9, P323, DOI 10.1034/j.1600-0625.2000.009005323.x
   Winik BC, 2009, BRIT J DERMATOL, V160, P868, DOI 10.1111/j.1365-2133.2008.08946.x
   Witcher LL, 1996, J BIOL CHEM, V271, P10904, DOI 10.1074/jbc.271.18.10904
   Yin TF, 2005, J BIOL CHEM, V280, P40355, DOI 10.1074/jbc.M506692200
   Yin TF, 2004, SEMIN CELL DEV BIOL, V15, P665, DOI 10.1016/j.semcdb.2004.09.005
   Zhurinsky J, 2000, J CELL SCI, V113, P3127
NR 29
TC 41
Z9 44
U1 0
U2 2
PU NATURE PUBLISHING GROUP
PI NEW YORK
PA 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA
SN 0022-202X
J9 J INVEST DERMATOL
JI J. Invest. Dermatol.
PD JUN
PY 2010
VL 130
IS 6
BP 1543
EP 1550
DI 10.1038/jid.2010.7
PG 8
WC Dermatology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Dermatology
GA 596DS
UT WOS:000277665200012
PM 20130592
OA Bronze
DA 2025-04-10
ER

PT J
AU Morini, E
   Rizzacasa, B
   Pucci, S
   Polidoro, C
   Ferrè, F
   Caporossi, D
   Citterich, MH
   Novelli, G
   Amati, F
AF Morini, Elena
   Rizzacasa, Barbara
   Pucci, Sabina
   Polidoro, Chiara
   Ferre, Fabrizio
   Caporossi, Daniela
   Citterich, Manuela Helmer
   Novelli, Giuseppe
   Amati, Francesca
TI The human rs1050286 polymorphism alters LOX-1 expression through
   modifying miR-24 binding
SO JOURNAL OF CELLULAR AND MOLECULAR MEDICINE
LA English
DT Article
DE Hsa-mir-24; OLR1 gene; acute myocardial infarction; Atherosclerosis;
   alternative splicing
ID OLR1 GENE; RECEPTOR; ATHEROSCLEROSIS; CELLS; MIRNA
AB The up-regulation of lectin-like oxidized low-density lipoprotein receptor-1 (LOX-1), encoded by the OLR1 gene, plays a fundamental role in the pathogenesis of atherosclerosis. Moreover, OLR1 polymorphisms were associated with increased susceptibility to acute myocardial infarction (AMI) and coronary artery diseases (CAD). In these pathologies, the identification of therapeutic approaches that can inhibit or reduce LOX-1 overexpression is crucial. Predictive analysis showed a putative hsa-miR-24 binding site in the 3'UTR of OLR1, 'naturally' mutated by the presence of the rs1050286 single nucleotide polymorphism (SNP). Luciferase assays revealed that miR-24 targets OLR1 3'UTR-G, but not 3'UTR-A (P < 0.0005). The functional relevance of miR-24 in regulating the expression of OLR1 was established by overexpressing miR-24 in human cell lines heterozygous (A/G, HeLa) and homozygous (A/A, HepG2) for rs1050286 SNP. Accordingly, HeLa (A/G), but not HepG2 (A/A), showed a significant down-regulation of OLR1 both at RNA and protein level. Our results indicate that rs1050286 SNP significantly affects miR-24 binding affinity to the 3'UTR of OLR1, causing a more efficient post-transcriptional gene repression in the presence of the G allele. On this basis, we considered that OLR1 rs1050286 SNP may contribute to modify OLR1 susceptibility to AMI and CAD, so ORL1 SNPs screening could help to stratify patients risk.
C1 [Morini, Elena; Caporossi, Daniela] Foro Italico Univ, Dept Movement Human & Hlth Sci, Rome, Italy.
   [Morini, Elena; Rizzacasa, Barbara; Pucci, Sabina; Polidoro, Chiara; Novelli, Giuseppe; Amati, Francesca] Univ Roma Tor Vergata, Dept Biomed & Prevent, Rome, Italy.
   [Ferre, Fabrizio; Citterich, Manuela Helmer] Univ Roma Tor Vergata, Dept Biol, I-00173 Rome, Italy.
C3 Foro Italico University of Rome; University of Rome Tor Vergata;
   University of Rome Tor Vergata
RP Amati, F (corresponding author), Univ Roma Tor Vergata, Dept Biomed & Prevent, Rome, Italy.
EM amati@med.uniroma2.it
RI Ferrè, Fabrizio/IAQ-1674-2023; Novelli, Giuseppe/A-5195-2013; Caporossi,
   Daniela/D-7434-2011; Amati, Francesca/J-8439-2012
OI FERRE', FABRIZIO/0000-0003-2768-5305; Amati,
   Francesca/0000-0003-2209-2156; Helmer-Citterich,
   Manuela/0000-0001-9530-7504; Caporossi, Daniela/0000-0001-9628-0665;
   Novelli, Giuseppe/0000-0002-7781-602X
FU Fondazione Roma; Lazio Regional Municipality [7 12650/2010]
FX This work was supported by a grant from Fondazione Roma (Non
   Communicable Diseases, NCDs: Development of a integrated protocol based
   on environmental and genetic/epigenetic data for the risk prediction of
   AMI in patients with coronary atherosclerosis) to G.N. and by the Lazio
   Regional Municipality (Agreement CRUL-Lazio n. 7 12650/2010) PhD
   scholarship to E.M. We are grateful to Dr. Li Qian for kindly supporting
   pEFDEST51 premiR-24-2 vector.
CR [Anonymous], J CELL MOL MED
   Biocca S, 2008, J MOL CELL CARDIOL, V44, P561, DOI 10.1016/j.yjmcc.2007.11.017
   Ding ZF, 2013, INT J CARDIOL, V168, P1378, DOI 10.1016/j.ijcard.2012.12.045
   Hirsch HA, 2010, CANCER CELL, V17, P348, DOI 10.1016/j.ccr.2010.01.022
   Katoh M, 2014, FRONT CELL DEV BIOL, V2, DOI 10.3389/fcell.2014.00061
   Khaidakov M, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0046973
   Mango R, 2005, CIRC RES, V97, P152, DOI 10.1161/01.RES.0000174563.62625.8e
   Mango R, 2003, J MED GENET, V40, P933, DOI 10.1136/jmg.40.12.933
   Novelli G, 2007, Clin Ter, V158, P239
   Pirillo A, 2013, MEDIAT INFLAMM, V2013, DOI 10.1155/2013/152786
   Qian L, 2011, J EXP MED, V208, P549, DOI 10.1084/jem.20101547
   Sawamura T, 1997, NATURE, V386, P73, DOI 10.1038/386073a0
   Ulrich-Merzenich G, 2013, EXPERT OPIN THER TAR, V17, P905, DOI 10.1517/14728222.2013.805748
   White SJ, 2011, CARDIOVASC PATHOL, V20, P369, DOI 10.1016/j.carpath.2010.08.007
   Ying SY, 2008, MOL BIOTECHNOL, V38, P257, DOI 10.1007/s12033-007-9013-8
NR 15
TC 21
Z9 21
U1 2
U2 6
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 1582-1838
EI 1582-4934
J9 J CELL MOL MED
JI J. Cell. Mol. Med.
PD JAN
PY 2016
VL 20
IS 1
BP 181
EP 187
DI 10.1111/jcmm.12716
PG 7
WC Cell Biology; Medicine, Research & Experimental
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Research & Experimental Medicine
GA DB1NA
UT WOS:000368273700018
PM 26542080
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Davenport, AP
   Bonner, TI
   Foord, SM
   Harmar, AJ
   Neubig, RR
   Pin, JP
   Spedding, M
   Kojima, M
   Kangawa, K
AF Davenport, AP
   Bonner, TI
   Foord, SM
   Harmar, AJ
   Neubig, RR
   Pin, JP
   Spedding, M
   Kojima, M
   Kangawa, K
TI International Union of Pharmacology. LVI. Ghrelin receptor nomenclature,
   distribution, and function
SO PHARMACOLOGICAL REVIEWS
LA English
DT Review
ID HORMONE-RELEASING PEPTIDE; LEFT-VENTRICULAR DYSFUNCTION; DES-ACYL
   GHRELIN; CIRCULATING GHRELIN; CARDIAC CACHEXIA; GROWTH; PITUITARY; CELL;
   HYPOTHALAMUS; IDENTIFICATION
AB Ghrelin is a 28-amino acid peptide originally isolated from rat stomach and is cleaved from a 117-amino acid precursor. The sequence of the mature peptide from rats and mice differs by two amino acids from that of human ghrelin. Alternative splicing of the ghrelin gene transcript can result in the translation of a second biologically active peptide, des-Gln(14)-ghrelin. Both peptides have a unique post-translational modification, octanoylation of Ser(3), which is essential for the binding to receptors in hypothalamus and pituitary and stimulating the release of growth hormone from the pituitary. The growth hormone secretagogue receptor (GHS-R1a, Swiss-Prot code Q92847, LocusLink ID 2693), a rhodopsin-like seven transmembrane spanning G protein-coupled receptors belonging to Family A, was cloned in 1996 from the pituitary and hypothalamus and shown to be the target of growth hormone secretagogues (GHS), a class of synthetic peptide and non-peptide compounds causing growth hormone release from the anterior pituitary. In 1999, ghrelin was identified as the endogenous cognate ligand for this receptor. The purpose of this review is to propose an official International Union of Pharmacology Committee on Receptor Nomenclature and Drug Classification (NC-IUPHAR) nomenclature designating GHS-R1a as the ghrelin receptor to follow the convention of naming receptors after the endogenous agonist, abbreviated where necessary to GRLN.
C1 Univ Cambridge, Clin Pharmacol Unit, Cambridge, England.
   NIMH, Genet Lab, Bethesda, MD 20892 USA.
   GlaxoSmithKline Res & Dev Ltd, Stevenage, Herts, England.
   Univ Edinburgh, Div Neurosci, Edinburgh, Midlothian, Scotland.
   Univ Edinburgh, Neurosci Res Ctr, Edinburgh, Midlothian, Scotland.
   Univ Michigan, Dept Pharmacol, Ann Arbor, MI 48109 USA.
   CNRS, Montpellier, France.
   IRIS, Neuilly Sur Seine, France.
   Natl Cardiovasc Ctr, Res Inst, Osaka, Japan.
C3 University of Cambridge; National Institutes of Health (NIH) - USA; NIH
   National Institute of Mental Health (NIMH); GlaxoSmithKline;
   Glaxosmithkline United Kingdom; University of Edinburgh; University of
   Edinburgh; University of Michigan System; University of Michigan; Centre
   National de la Recherche Scientifique (CNRS); Institut National de la
   Sante et de la Recherche Medicale (Inserm); National Cerebral &
   Cardiovascular Center - Japan
RP Univ Cambridge, Addenbrookes Hosp, Clin Pharmacol Unit, NC IUPHAR Emerging Pharmacol Grp, Cambridge CB2 2QQ, England.
EM apd10@medschl.cam.ac.uk
RI Pin, Jean-Philippe/Y-6668-2019; Spedding, Michael/AAE-7342-2019;
   Davenport, Anthony Peter/A-5773-2008
OI Neubig, Richard/0000-0003-0501-0008; Pin,
   Jean-Philippe/0000-0002-1423-345X; Davenport, Anthony
   Peter/0000-0002-2096-3117; Spedding, Michael/0000-0002-1248-8221;
   Harmar, Anthony/0000-0002-3838-9264
CR Ariyasu H, 2001, J CLIN ENDOCR METAB, V86, P4753, DOI 10.1210/jc.86.10.4753
   Asakawa A, 2003, GUT, V52, P947, DOI 10.1136/gut.52.7.947
   Bagnasco M, 2003, REGUL PEPTIDES, V111, P161, DOI 10.1016/S0167-0115(02)00283-5
   Baldanzi G, 2002, J CELL BIOL, V159, P1029, DOI 10.1083/jcb.200207165
   Bedendi I, 2003, EUR J PHARMACOL, V476, P87, DOI 10.1016/S0014-2999(03)02083-1
   Bednarek MA, 2000, J MED CHEM, V43, P4370, DOI 10.1021/jm0001727
   Cassoni P, 2001, J CLIN ENDOCR METAB, V86, P1738, DOI 10.1210/jc.86.4.1738
   Cowley MA, 2003, NEURON, V37, P649, DOI 10.1016/S0896-6273(03)00063-1
   Date Y, 2000, ENDOCRINOLOGY, V141, P4255, DOI 10.1210/en.141.11.4255
   Foord SM, 2005, PHARMACOL REV, V57, P279, DOI 10.1124/pr.57.2.5
   Gualillo O, 2001, ENDOCRINOLOGY, V142, P788, DOI 10.1210/en.142.2.788
   Haqq AM, 2003, J CLIN ENDOCR METAB, V88, P3573, DOI 10.1210/jc.2003-030205
   Hosoda H, 2000, BIOCHEM BIOPH RES CO, V279, P909, DOI 10.1006/bbrc.2000.4039
   Howard AD, 1996, SCIENCE, V273, P974, DOI 10.1126/science.273.5277.974
   Inui A, 2001, NAT REV NEUROSCI, V2, P551, DOI 10.1038/35086018
   Katugampola SD, 2001, BRIT J PHARMACOL, V134, P143, DOI 10.1038/sj.bjp.0704228
   Kleinz M, 2003, ATHEROSCLEROSIS, V170, pS9
   Kojima M, 1999, NATURE, V402, P656, DOI 10.1038/45230
   Kojima M, 2001, TRENDS ENDOCRIN MET, V12, P118, DOI 10.1016/S1043-2760(00)00362-3
   Korbonits M, 2001, J CLIN ENDOCR METAB, V86, P881, DOI 10.1210/jc.86.2.881
   Korbonits M, 2004, FRONT NEUROENDOCRIN, V25, P27, DOI 10.1016/j.yfrne.2004.03.002
   Matsumoto M, 2001, BIOCHEM BIOPH RES CO, V287, P142, DOI 10.1006/bbrc.2001.5553
   McKee KK, 1997, MOL ENDOCRINOL, V11, P415, DOI 10.1210/me.11.4.415
   Muccioli G, 2001, J ENDOCRINOL INVEST, V24, pRC7, DOI 10.1007/BF03343831
   Nagaya N, 2003, REGUL PEPTIDES, V114, P71, DOI 10.1016/S0167-0115(03)00117-4
   Nagaya N, 2003, CURR OPIN PHARMACOL, V3, P146, DOI 10.1016/S1471-4892(03)00013-4
   Nagaya N, 2001, J CLIN ENDOCR METAB, V86, P5854, DOI 10.1210/jc.86.12.5854
   Nagaya N, 2001, CIRCULATION, V104, P1430, DOI 10.1161/hc3601.095575
   Nagaya N, 2001, AM J PHYSIOL-REG I, V280, pR1483, DOI 10.1152/ajpregu.2001.280.5.R1483
   Okumura H, 2002, J CARDIOVASC PHARM, V39, P779, DOI 10.1097/00005344-200206000-00001
   Pöykkö SM, 2003, DIABETES, V52, P2546, DOI 10.2337/diabetes.52.10.2546
   Shuto YJ, 2001, LIFE SCI, V68, P991, DOI 10.1016/S0024-3205(00)01001-8
   Sugino T, 2002, BIOCHEM BIOPH RES CO, V295, P255, DOI 10.1016/S0006-291X(02)00654-X
   Sun YX, 2003, MOL CELL BIOL, V23, P7973, DOI 10.1128/MCB.23.22.7973-7981.2003
   Sun YX, 2004, P NATL ACAD SCI USA, V101, P4679, DOI 10.1073/pnas.0305930101
   Tanaka M, 2003, PSYCHONEUROENDOCRINO, V28, P829, DOI 10.1016/S0306-4530(02)00066-5
   Tomasetto C, 2000, GASTROENTEROLOGY, V119, P395, DOI 10.1053/gast.2000.9371
   van der Lely AJ, 2004, ENDOCR REV, V25, P426, DOI 10.1210/er.2002-0029
   Wierup N, 2002, REGUL PEPTIDES, V107, P63, DOI 10.1016/S0167-0115(02)00067-8
   Wiley KE, 2002, BRIT J PHARMACOL, V136, P1146, DOI 10.1038/sj.bjp.0704815
   Yokote R, 1998, PEPTIDES, V19, P15, DOI 10.1016/S0196-9781(97)00263-5
NR 41
TC 191
Z9 211
U1 0
U2 10
PU AMER SOC PHARMACOLOGY EXPERIMENTAL THERAPEUTICS
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3995 USA
SN 0031-6997
EI 1521-0081
J9 PHARMACOL REV
JI Pharmacol. Rev.
PD DEC
PY 2005
VL 57
IS 4
BP 541
EP 546
DI 10.1124/pr.57.4.1
PG 6
WC Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Pharmacology & Pharmacy
GA 997TG
UT WOS:000234270300012
PM 16382107
DA 2025-04-10
ER

PT J
AU Kelly, MI
   Albahrani, M
   Castro, C
   Poon, E
   Yan, B
   Littrell, J
   Waas, M
   Boheler, KR
   Gundry, RL
AF Kelly, Maia I.
   Albahrani, Mustafa
   Castro, Chase
   Poon, Ellen
   Yan, Bin
   Littrell, Jack
   Waas, Matthew
   Boheler, Kenneth R.
   Gundry, Rebekah L.
TI Importance of evaluating protein glycosylation in pluripotent stem
   cell-derived cardiomyocytes for research and clinical applications
SO PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY
LA English
DT Review
DE Stem cell-derived cardiomyocytes; Protein glycosylation; Mass
   spectrometry
AB Proper protein glycosylation is critical to normal cardiomyocyte physiology. Aberrant glycosylation can alter protein localization, structure, drug interactions, and cellular function. The in vitro differentiation of human pluripotent stem cells into cardiomyocytes (hPSC-CM) has become increasingly important to the study of protein function and to the fields of cardiac disease modeling, drug testing, drug discovery, and regenerative medicine. Here, we offer our perspective on the importance of protein glycosylation in hPSC-CM. Protein glycosylation is dynamic in hPSC-CM, but the timing and extent of glycosylation are still poorly defined. We provide new data highlighting how observed changes in hPSC-CM glycosylation may be caused by underlying differences in the protein or transcript abundance of enzymes involved in building and trimming the glycan structures or glycoprotein gene products. We also provide evidence that alternative splicing results in altered sites of glycosylation within the protein sequence. Our findings suggest the need to precisely define protein glycosylation events that may have a critical impact on the function and maturation state of hPSC-CM. Finally, we provide an overview of analytical strategies available for studying protein glycosylation and identify opportunities for the development of new bioinformatic approaches to integrate diverse protein glycosylation data types. We predict that these tools will promote the accurate assessment of protein glycosylation in future studies of hPSC-CM that will ultimately be of significant experimental and clinical benefit.
C1 [Kelly, Maia I.; Albahrani, Mustafa; Castro, Chase; Littrell, Jack; Waas, Matthew; Gundry, Rebekah L.] Univ Nebraska Med Ctr, Dept Cellular & Integrat Physiol, Div Cardiovasc Med, CardiOm Program,Ctr Heart & Vasc Res, Omaha, NE 68198 USA.
   [Poon, Ellen] Chinese Univ Hong Kong, Ctr Cardiovasc Genom & Med, Lui Che Woo Inst Innovat Med, Dept Med & Therapeut,Hong Kong Hub Pediat Excelle, Hong Kong, Peoples R China.
   [Yan, Bin] Univ Hong Kong, Dept Comp Sci, Hong Kong, Peoples R China.
   [Yan, Bin] Wenzhou Med Univ, Affiliated Hosp 2, Wenzhou, Zhejiang, Peoples R China.
   [Yan, Bin] Wenzhou Med Univ, Yuying Childrens Hosp, Wenzhou, Zhejiang, Peoples R China.
   [Waas, Matthew] Univ Hlth Network, Princess Margaret Canc Ctr, Toronto, ON M5G 0A3, Canada.
   [Boheler, Kenneth R.] Johns Hopkins Univ, Dept Biomed Engn, Whiting Sch Engn, Traylor Bldg, Baltimore, MD 21205 USA.
C3 University of Nebraska System; University of Nebraska Medical Center;
   Chinese University of Hong Kong; University of Hong Kong; Wenzhou
   Medical University; Wenzhou Medical University; University of Toronto;
   University Health Network Toronto; Princess Margaret Cancer Centre;
   Johns Hopkins University
RP Gundry, RL (corresponding author), Univ Nebraska Med Ctr, Dept Cellular & Integrat Physiol, Div Cardiovasc Med, CardiOm Program,Ctr Heart & Vasc Res, Omaha, NE 68198 USA.
EM rebekah.gundry@unmc.edu
RI Waas, Matthew/AAY-4364-2020; Gundry, Rebekah/K-6080-2019; Poon,
   Ellen/ABD-6962-2020
OI Castro, Chase S/0000-0002-4692-4888; Gundry, Rebekah
   L./0000-0002-9263-833X; Littrell, John/0000-0003-1264-894X; Boheler,
   Kenneth Richard/0000-0002-4016-6932; Poon, Ellen/0000-0002-9280-3681;
   Kelly, Maia/0000-0002-9383-1107; /0000-0002-2168-3379; Waas,
   Matthew/0000-0003-4537-1502
FU Hong Kong Research Grant Council Theme-based Research Scheme
   [T13-706/11]; Huey Foundation; Chinese University of Hong Kong; Hong
   Kong Research Grant Council General Research Fund [17117918]; National
   Institutes of Health [R01-HL134010, R01-HL126785, R33-HL154123,
   R35-HL155460, F31-HL140914]; Juvenile Diabetes Research Foundation
   [2-SRA-2019-829-S-B]; Improvement on competitiveness in hiring new
   faculties funding scheme; National Heart Lung and Blood Institute
   [R33HL154123] Funding Source: NIH RePORTER
FX This work was supported by a Hong Kong Research Grant Council
   Theme-based Research Scheme [T13-706/11], funding from the Huey
   Foundation, and by a gift from EntopsisAsia to K.R.B.; by funding from
   the Improvement on competitiveness in hiring new faculties funding
   scheme and the direct grant from the Chinese University of Hong Kong to
   E.N.P.; by the Hong Kong Research Grant Council General Research Fund
   [17117918] to B. Y.; and by the National Institutes of Health
   [R01-HL134010, R01-HL126785, R33-HL154123, R35-HL155460 to R.L.G.,
   F31-HL140914 to M.W.], Juvenile Diabetes Research Foundation
   [2-SRA-2019-829-S-B to R.L.G.]. Funding sources were not involved in
   study design, data collection, interpretation, analysis or publication.
CR Abeln M, 2017, CHEMBIOCHEM, V18, P1305, DOI 10.1002/cbic.201700083
   Alavi A, 2008, RHEUMATOLOGY, V47, P760, DOI 10.1093/rheumatology/ken081
   Alocci D, 2019, J PROTEOME RES, V18, P664, DOI 10.1021/acs.jproteome.8b00766
   Aoki-Kinoshita K, 2016, NUCLEIC ACIDS RES, V44, pD1237, DOI 10.1093/nar/gkv1041
   Aoki-Kinoshita KF, 2020, GLYCOBIOLOGY, V30, P70, DOI 10.1093/glycob/cwz078
   Ashwood C, 2020, J MOL CELL CARDIOL, V139, P33, DOI 10.1016/j.yjmcc.2019.12.012
   Banazadeh A, 2017, ELECTROPHORESIS, V38, P162, DOI 10.1002/elps.201600357
   Baroni D, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-10645-y
   BAUSE E, 1979, FEBS LETT, V108, P341, DOI 10.1016/0014-5793(79)80559-1
   Berg Luecke Linda, 2019, Curr Protoc Stem Cell Biol, V50, pe94, DOI 10.1002/cpsc.94
   Berger RP, 2016, BIOESSAYS, V38, P1255, DOI 10.1002/bies.201600138
   Braam SR, 2010, STEM CELL RES, V4, P107, DOI 10.1016/j.scr.2009.11.004
   Cao WQ, 2021, MOL CELL PROTEOMICS, V20, DOI 10.1074/mcp.R120.002090
   Carvajal-Vergara X, 2010, NATURE, V465, P808, DOI 10.1038/nature09005
   Ceroni A, 2007, SOURCE CODE BIOL MED, V2, DOI 10.1186/1751-0473-2-3
   Chong JJH, 2014, NATURE, V510, P273, DOI 10.1038/nature13233
   Churko JM, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-07333-4
   Contessotto P, 2020, MATRIX BIOL, V85-86, P173, DOI 10.1016/j.matbio.2019.05.001
   Cortada E, 2019, J BIOL CHEM, V294, P16123, DOI 10.1074/jbc.RA119.007903
   Cotarelo RP, 2008, CLIN GENET, V73, P139, DOI 10.1111/j.1399-0004.2007.00936.x
   de Haan N, 2015, ANAL CHEM, V87, P8284, DOI 10.1021/acs.analchem.5b02426
   Dobin A, 2013, BIOINFORMATICS, V29, P15, DOI 10.1093/bioinformatics/bts635
   Doherty M, 2018, SCI REP-UK, V8, DOI 10.1038/s41598-018-26805-7
   DRYSDALE RG, 1968, VOX SANG, V15, P194, DOI 10.1111/j.1423-0410.1968.tb01749.x
   Ednie AR, 2013, J MOL CELL CARDIOL, V59, P117, DOI 10.1016/j.yjmcc.2013.02.013
   EDWARDS K, 1991, NUCLEIC ACIDS RES, V19, P1349, DOI 10.1093/nar/19.6.1349
   Fonoudi H, 2021, J THROMB THROMBOLYS, V51, P890, DOI 10.1007/s11239-020-02299-x
   Freeze HH., 2015, Essentials of Glycobiology, V3rd
   Fujinaka CM, 2018, METHODS MOL BIOL, V1722, P57, DOI 10.1007/978-1-4939-7553-2_4
   Furukawa J, 2017, GLYCOCONJUGATE J, V34, P807, DOI 10.1007/s10719-017-9800-9
   Furukawa J, 2016, GLYCOCONJUGATE J, V33, P707, DOI 10.1007/s10719-016-9701-3
   Gabius HJ, 2011, TRENDS BIOCHEM SCI, V36, P298, DOI 10.1016/j.tibs.2011.01.005
   Giudice J, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms4603
   Han ELY, 2019, CELL REP, V29, P3751, DOI 10.1016/j.celrep.2019.11.026
   HARRIS RJ, 1993, GLYCOBIOLOGY, V3, P219, DOI 10.1093/glycob/3.3.219
   Hayes CA, 2011, BIOINFORMATICS, V27, P1343, DOI 10.1093/bioinformatics/btr137
   Hinneburg H, 2016, J AM SOC MASS SPECTR, V27, P507, DOI 10.1007/s13361-015-1308-6
   Hoosdally SJ, 2009, J BIOL CHEM, V284, P16277, DOI 10.1074/jbc.M109.007849
   Jensen PH, 2012, NAT PROTOC, V7, P1299, DOI 10.1038/nprot.2012.063
   Kapusta L, 2013, HEART FAIL REV, V18, P187, DOI 10.1007/s10741-012-9302-6
   Karakikes I, 2015, CIRC RES, V117, P80, DOI 10.1161/CIRCRESAHA.117.305365
   Kawamura T, 2015, STEM CELL TRANSL MED, V4, P1258, DOI 10.5966/sctm.2015-0029
   Kawamura T, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0111064
   Kelly MI, 2020, J AM SOC MASS SPECTR, V31, P624, DOI 10.1021/jasms.9b00065
   Kolarich D, 2012, NAT PROTOC, V7, P1285, DOI 10.1038/nprot.2012.062
   Konze SA, 2017, CHEMBIOCHEM, V18, P1317, DOI 10.1002/cbic.201700100
   KORNFELD R, 1985, ANNU REV BIOCHEM, V54, P631, DOI 10.1146/annurev.bi.54.070185.003215
   Lauc G, 2016, BBA-GEN SUBJECTS, V1860, P1574, DOI 10.1016/j.bbagen.2015.10.016
   Lee-Sundlov MM, 2017, GLYCOBIOLOGY, V27, P188, DOI 10.1093/glycob/cww108
   Li M, 2015, BIOCHEM J, V466, P77, DOI 10.1042/BJ20140692
   Li QY, 2020, NAT PROTOC, V15, P2668, DOI 10.1038/s41596-020-0350-4
   Li QY, 2019, CELLS-BASEL, V8, DOI 10.3390/cells8080882
   Li QY, 2019, ANAL CHEM, V91, P5433, DOI 10.1021/acs.analchem.9b00776
   Lindahl U., 2015, PROTEOGLYCANS SULFAT
   Lombard V, 2014, NUCLEIC ACIDS RES, V42, pD490, DOI 10.1093/nar/gkt1178
   LOTAN R, 1975, J BIOL CHEM, V250, P8518
   Lu Q, 2020, ANAL CHEM, V92, P6269, DOI 10.1021/acs.analchem.9b02643
   Luiken JJFP, 2016, BBA-MOL BASIS DIS, V1862, P2253, DOI 10.1016/j.bbadis.2016.09.004
   Ma JF, 2021, GLYCOBIOLOGY, V31, P719, DOI 10.1093/glycob/cwab003
   Mannhardt I, 2020, STEM CELL REP, V15, P983, DOI 10.1016/j.stemcr.2020.09.002
   Margeta M, 2009, MUSCLE NERVE, V40, P883, DOI 10.1002/mus.21432
   Mariño K, 2010, NAT CHEM BIOL, V6, P713, DOI [10.1038/NCHEMBIO.437, 10.1038/nchembio.437]
   Marques-da-Silva D, 2017, J INHERIT METAB DIS, V40, P657, DOI 10.1007/s10545-017-0066-y
   Marshall R D, 1974, Biochem Soc Symp, P17
   Marth JD, 2008, NAT REV IMMUNOL, V8, P874, DOI 10.1038/nri2417
   Matsa E, 2014, SCI TRANSL MED, V6, DOI 10.1126/scitranslmed.3008921
   Matsa E, 2014, EUR HEART J, V35, P1078, DOI 10.1093/eurheartj/eht067
   McDonald CA, 2009, MOL CELL PROTEOMICS, V8, P287, DOI 10.1074/mcp.M800272-MCP200
   McKitrick TR, 2020, BIOCHEMISTRY-US, V59, P3111, DOI 10.1021/acs.biochem.9b01015
   Mehta AY, 2020, BIOINFORMATICS, V36, P3613, DOI 10.1093/bioinformatics/btaa190
   Mehta A, 2014, CARDIOVASC RES, V102, P497, DOI 10.1093/cvr/cvu060
   Mills RJ, 2017, P NATL ACAD SCI USA, V114, pE8372, DOI 10.1073/pnas.1707316114
   MIURA K, 1987, ACTA PATHOL JAPON, V37, P1823
   Montpetit ML, 2009, P NATL ACAD SCI USA, V106, P16517, DOI 10.1073/pnas.0905414106
   Moretti A, 2010, NEW ENGL J MED, V363, P1397, DOI 10.1056/NEJMoa0908679
   Much B, 2003, J BIOL CHEM, V278, P43781, DOI 10.1074/jbc.M306958200
   Mummery CL, 2012, CIRC RES, V111, P344, DOI 10.1161/CIRCRESAHA.110.227512
   Murakami T, 2006, ANN NEUROL, V60, P597, DOI 10.1002/ana.20973
   Nishihara S, 2018, FEBS LETT, V592, P3773, DOI 10.1002/1873-3468.13167
   Omasits U, 2014, BIOINFORMATICS, V30, P884, DOI 10.1093/bioinformatics/btt607
   Park Ki-Ho, 2003, FASEB Journal, V17, P2308
   Park M, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-06607-z
   Pesl M, 2017, J MOL RECOGNIT, V30, DOI 10.1002/jmr.2602
   Poon ENY, 2020, CELL RES, V30, P626, DOI 10.1038/s41422-020-0292-y
   Ramya TNC, 2013, GLYCOBIOLOGY, V23, P211, DOI 10.1093/glycob/cws144
   Raval KK, 2015, J BIOL CHEM, V290, P3121, DOI 10.1074/jbc.M114.628628
   Riley NM, 2020, J PROTEOME RES, V19, P3286, DOI 10.1021/acs.jproteome.0c00218
   RINDERLE SJ, 1989, J BIOL CHEM, V264, P16123
   Rossdam C, 2019, ANAL CHEM, V91, P6413, DOI 10.1021/acs.analchem.9b01114
   Ruiz-Canada C, 2009, CELL, V136, P272, DOI 10.1016/j.cell.2008.11.047
   Schjoldager KT, 2020, NAT REV MOL CELL BIO, V21, P729, DOI 10.1038/s41580-020-00294-x
   SchulzeBahr E, 1997, NAT GENET, V17, P267, DOI 10.1038/ng1197-267
   Sesti F, 2000, P NATL ACAD SCI USA, V97, P10613, DOI 10.1073/pnas.180223197
   Shen SH, 2014, P NATL ACAD SCI USA, V111, pE5593, DOI 10.1073/pnas.1419161111
   Steentoft C, 2013, EMBO J, V32, P1478, DOI 10.1038/emboj.2013.79
   Stocker PJ, 2006, J GEN PHYSIOL, V127, P253, DOI 10.1085/jgp.200509423
   Tétreault MP, 2016, J BIOL CHEM, V291, P4826, DOI 10.1074/jbc.M115.692178
   Thaysen-Andersen M, 2014, BBA-PROTEINS PROTEOM, V1844, P1437, DOI 10.1016/j.bbapap.2014.05.002
   Tokhtaeva E, 2016, J CELL SCI, V129, P2394, DOI 10.1242/jcs.186148
   Tress ML, 2007, P NATL ACAD SCI USA, V104, P5495, DOI 10.1073/pnas.0700800104
   van de Kamp JM, 2007, J MED GENET, V44, P277, DOI 10.1136/jmg.2006.044735
   Van den Steen P, 1998, CRIT REV BIOCHEM MOL, V33, P151
   van Laake LW, 2008, CIRC RES, V102, P1008, DOI 10.1161/CIRCRESAHA.108.175505
   van Meer BJ, 2016, STEM CELLS, V34, P2008, DOI 10.1002/stem.2403
   Veillon L, 2017, ELECTROPHORESIS, V38, P2100, DOI 10.1002/elps.201700042
   Waas M, 2020, BIOINFORMATICS, V36, P3447, DOI 10.1093/bioinformatics/btaa092
   Waas M, 2020, J AM SOC MASS SPECTR, V31, P1389, DOI 10.1021/jasms.0c00021
   Waas M, 2019, STEM CELL REP, V12, P395, DOI 10.1016/j.stemcr.2018.12.016
   Wan HH, 2020, ANAL BIOANAL CHEM, V412, P1497, DOI 10.1007/s00216-020-02415-z
   Wang H, 2016, SCI REP-UK, V6, DOI 10.1038/srep35520
   Wang L, 2012, J PROTEOME RES, V11, P143, DOI 10.1021/pr200916k
   Wang YC, 2015, EXPERT OPIN BIOL TH, V15, P679, DOI 10.1517/14712598.2015.1021329
   Watanabe Y, 2021, NUCLEIC ACIDS RES, V49, pD1523, DOI 10.1093/nar/gkaa1012
   Weng YJ, 2014, ANAL CHIM ACTA, V833, P1, DOI 10.1016/j.aca.2014.04.037
   Wiedmann F, 2019, INT J MOL SCI, V20, DOI 10.3390/ijms20205193
   Wollscheid B, 2009, NAT BIOTECHNOL, V27, P378, DOI 10.1038/nbt.1532
   Wu AM, 2003, LIFE SCI, V72, P2285, DOI 10.1016/S0024-3205(03)00116-4
   Wulff-Fuentes E, 2021, SCI DATA, V8, DOI 10.1038/s41597-021-00810-4
   Xiao HP, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-04081-3
   Yamada I, 2020, NAT METHODS, V17, P649, DOI 10.1038/s41592-020-0879-8
   Yang GL, 2018, ANAL CHEM, V90, P14294, DOI 10.1021/acs.analchem.8b03520
   YEE HF, 1991, J MOL CELL CARDIOL, V23, P175, DOI 10.1016/0022-2828(91)90104-T
   York WS, 2020, GLYCOBIOLOGY, V30, P72, DOI 10.1093/glycob/cwz080
   Zacchi LF, 2016, GLYCOCONJUGATE J, V33, P359, DOI 10.1007/s10719-015-9641-3
   Zeng Y, 2009, NAT METHODS, V6, P207, DOI [10.1038/NMETH.1305, 10.1038/nmeth.1305]
   Zielinska DF, 2010, CELL, V141, P897, DOI 10.1016/j.cell.2010.04.012
NR 126
TC 10
Z9 11
U1 1
U2 17
PU SPRINGER HEIDELBERG
PI HEIDELBERG
PA TIERGARTENSTRASSE 17, D-69121 HEIDELBERG, GERMANY
SN 0031-6768
EI 1432-2013
J9 PFLUG ARCH EUR J PHY
JI Pflugers Arch.
PD JUL
PY 2021
VL 473
IS 7
SI SI
BP 1041
EP 1059
DI 10.1007/s00424-021-02554-x
EA APR 2021
PG 19
WC Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Physiology
GA TC3RX
UT WOS:000638059900001
PM 33830329
OA hybrid, Green Published
DA 2025-04-10
ER

PT J
AU Pasquet, S
   Thiebaud, P
   Faucheux, C
   Olive, M
   Fourcade, S
   Lalevee, N
   Lamaziere, JMD
   Theze, N
AF Pasquet, S
   Thiebaud, P
   Faucheux, C
   Olive, M
   Fourcade, S
   Lalevee, N
   Lamaziere, JMD
   Theze, N
TI Characterization of a mammalian smooth muscle cell line that has
   retained transcriptional and posttranscriptional potencies
SO IN VITRO CELLULAR & DEVELOPMENTAL BIOLOGY-ANIMAL
LA English
DT Article
DE gene expression; transcription; splicing
ID SERUM RESPONSE FACTOR; GENE-EXPRESSION; ALPHA-TROPOMYOSIN; PHENOTYPIC
   MODULATION; CALPONIN GENE; PROMOTER; DIFFERENTIATION; ACTIVATION;
   MYOCARDIN; ASSOCIATION
AB Unlike skeletal and cardiac muscle cells that differentiate irreversibly, smooth muscle cells (SMCs) retain a high degree of plasticity. During the so-called phenotypic modulation, SMCs can undergo transition between a contractile phenotype and a highly proliferative synthetic phenotype, as apparent from the extinction of numerous smooth muscle (SM) markers when they are passaged in culture. It would be very useful to have an SMC line that can be indefinitely propagated for the cellular and molecular analysis of the mechanisms that underlie the control of SM differentiation. This report describes an immortalized rabbit aorta SMC-derived cell line (U8A4) that has conserved differentiated properties through multiple subcultures. U8A4 cells can grow in the absence of serum and express the SMC markers studied, including SM alpha-actin, SM calponin, SM22alpha, SM alpha-tropomyosin (alpha-TM), SM myosin heavy chain (SM-MHC), and myocardin. U8A4 cells can activate SMC-restricted promoters like those of SM22alpha, SM calponin, and SM-MHC genes as efficiently as described previously for rat SMC lines (PAC1, A7r5, and A10). These cells can also process exogenous alpha-TM transcripts according to an SM-specific pattern. These results demonstrate that the U8A4 cell line constitutes a good alternative model to existing SMC lines that could facilitate the Study of the transcriptional and posttranscriptional regulatory mechanisms underlying SMC differentiation.
C1 Univ Bordeaux 2, INSERM, Unite 441, F-33600 Pessac, France.
C3 Universite de Bordeaux; Institut National de la Sante et de la Recherche
   Medicale (Inserm)
RP Univ Bordeaux 2, INSERM, Unite 441, Ave Haut Leveque, F-33600 Pessac, France.
EM nadine.theze@bordeaux.inserm.fr
RI ; LALEVEE, Nathalie/M-4636-2016; Fourcade, Stephane/N-4508-2014
OI , Maurice Olive/0009-0001-7522-9497; LALEVEE,
   Nathalie/0000-0003-1924-1667; THIEBAUD, Pierre/0000-0003-1174-1616;
   Fourcade, Stephane/0000-0002-8031-5007
CR Bhalla SS, 2001, J BIOL CHEM, V276, P11439, DOI 10.1074/jbc.M100208200
   BochatonPiallat ML, 1996, ARTERIOSCL THROM VAS, V16, P815, DOI 10.1161/01.ATV.16.6.815
   Camoretti-Mercado B, 2000, J BIOL CHEM, V275, P30387, DOI 10.1074/jbc.M000840200
   Casco VH, 2002, J HISTOCHEM CYTOCHEM, V50, P799, DOI 10.1177/002215540205000606
   Chen JY, 2002, J MOL CELL CARDIOL, V34, P1345, DOI 10.1006/jmcc.2002.2086
   Dulin NO, 2001, BIOCHEM J, V357, P587, DOI 10.1042/0264-6021:3570587
   Firulli AB, 1998, IN VITRO CELL DEV-AN, V34, P217
   Gaillard C, 1998, DEV GENES EVOL, V207, P435, DOI 10.1007/s004270050134
   GIMONA M, 1995, P NATL ACAD SCI USA, V92, P9776, DOI 10.1073/pnas.92.21.9776
   GOODING C, 1994, EMBO J, V13, P3861, DOI 10.1002/j.1460-2075.1994.tb06697.x
   Kashiwada K, 1997, J BIOL CHEM, V272, P15396, DOI 10.1074/jbc.272.24.15396
   Kumar MS, 2003, ARTERIOSCL THROM VAS, V23, P737, DOI 10.1161/01.ATV.0000065197.07635.BA
   LEESMILLER JP, 1991, BIOESSAYS, V13, P429, DOI 10.1002/bies.950130902
   Li L, 1996, J CELL BIOL, V132, P849, DOI 10.1083/jcb.132.5.849
   Miano JM, 2002, RES PRO CEL, V38, P39
   Miano JM, 2000, J BIOL CHEM, V275, P9814, DOI 10.1074/jbc.275.13.9814
   OLSON EN, 1990, GENE DEV, V4, P1454, DOI 10.1101/gad.4.9.1454
   OWENS GK, 1995, PHYSIOL REV, V75, P487
   PINCONRAYMOND M, 1991, DEV BIOL, V148, P517, DOI 10.1016/0012-1606(91)90270-D
   SMITH CWJ, 1989, CELL, V56, P749, DOI 10.1016/0092-8674(89)90678-8
   Sobue K, 1999, MOL CELL BIOCHEM, V190, P105, DOI 10.1023/A:1006941621170
   Wang DZ, 2001, CELL, V105, P851, DOI 10.1016/S0092-8674(01)00404-4
   Yoshida T, 2003, CIRC RES, V92, P856, DOI 10.1161/01.RES.0000068405.49081.09
NR 23
TC 8
Z9 8
U1 0
U2 0
PU SPRINGER
PI NEW YORK
PA 233 SPRING ST, NEW YORK, NY 10013 USA
SN 1071-2690
EI 1543-706X
J9 IN VITRO CELL DEV-AN
JI In Vitro Cell. Dev. Biol.-Anim.
PD MAY-JUN
PY 2004
VL 40
IS 5-6
BP 133
EP 137
PG 5
WC Cell Biology; Developmental Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Developmental Biology
GA 863FE
UT WOS:000224545500003
PM 15479116
DA 2025-04-10
ER

PT J
AU Lin, HCH
   Paul, CR
   Kuo, CH
   Chang, YH
   Chen, WST
   Ho, TJ
   Day, CH
   Viswanadha, VP
   Tsai, Y
   Huang, CY
AF Lin, Henry Cherng-Han
   Paul, Catherine Reena
   Kuo, Chia-Hua
   Chang, Yung-Hsien
   Chen, William Shao-Tsu
   Ho, Tsung-Jung
   Day, Cecilia Hsuan
   Viswanadha, Vijaya Padma
   Tsai, Yuhsin
   Huang, Chih-Yang
TI IGF 11Rα-triggered pathological manifestations in the heart aggravate
   renal inflammation in STZ-induced type-I diabetes rats
SO AGING-US
LA English
DT Article
DE diabetes; renal fibrosis; cardiac stress; embryonic gene; cardiorenal
   syndrome; insulin receptor
ID JAK/STAT SIGNALING PATHWAY; CHRONIC KIDNEY-DISEASE; FIBRONECTIN
   SYNTHESIS; HYPERTROPHY; INHIBITION; EXPRESSION; ALDOSTERONE; ACTIVATION;
   PREVENTS; FIBROSIS
AB Pathological manifestations in either heart or kidney impact the function of the other and form the basis for the development of cardiorenal syndrome. However, the mechanism or factors involved in such scenario are not completely elucidated. In our study, to find the correlation between late fetal gene expression in diabetic hearts and their influence on diabetic nephropathy, we created a rat model with cardiac specific overexpression of IGF-IIR alpha, which is an alternative splicing variant of IGFIIR, expressed in pathological hearts. In this study, transgenic rats over expressing cardiac specific IGF-IIR alpha and non-transgenic animal models established in SD rats were administered with single dose of streptozotocin (STZ, 55 mg/Kg) to induce Type I diabetes. The correlation between IGF-IIR alpha and kidney damages were further determined based on their intensity of damage in the kidneys. The results show that cardiac specific overexpression of IGF-IIR alpha elevates the diabetes associated inflammation and morphological changes in the kidneys. The diabetic transgenic rats showed advancement in the pathological features such a renal tubular damage, collagen accumulation and enhancement in STAT3 associated mechanism of renal fibrosis. The results therefore show that that IGF-IIR alpha expression in the heart during pathological condition may worsen symptoms of diabetic nephropathy in rats.
C1 [Lin, Henry Cherng-Han] China Med Univ, Grad Inst Chinese Med, Taichung 404, Taiwan.
   [Paul, Catherine Reena; Huang, Chih-Yang] Buddhist Tzu Chi Med Fdn, Hualien Tzu Chi Hosp, Cardiovasc & Mitochondrial Related Dis Res Ctr, Hualien 97004, Taiwan.
   [Kuo, Chia-Hua] Univ Taipei, Lab Exercise Biochem, Taipei 11153, Taiwan.
   [Chang, Yung-Hsien] China Med Univ, China Med Univ Hosp, Dept Chinese Med, Taichung 404, Taiwan.
   [Chen, William Shao-Tsu] Tzu Chi Gen Hosp, Dept Psychiat, Hualien 97004, Taiwan.
   [Chen, William Shao-Tsu] Tzu Chi Univ, Sch Med, Hualien 97004, Taiwan.
   [Ho, Tsung-Jung] Tzu Chi Univ, Hualien Tzu Chi Hosp, Buddhist Tzu Chi Med Fdn, Dept Chinese Med, Hualien 97004, Taiwan.
   [Ho, Tsung-Jung] Buddhist Tzu Chi Med Fdn, Hualien Tzu Chi Hosp, Integrat Ctr Tradit Chinese & Modern Med, Hualien 97004, Taiwan.
   [Ho, Tsung-Jung] Tzu Chi Univ, Coll Med, Sch Postbaccalaureate Chinese Med, Hualien 97004, Taiwan.
   [Day, Cecilia Hsuan] MeiHo Univ, Dept Nursing, Pingtung 912, Taiwan.
   [Viswanadha, Vijaya Padma] Bharathiar Univ, Dept Biotechnol, Coimbatore 641046, Tamil Nadu, India.
   [Tsai, Yuhsin] China Med Univ, Grad Inst Chinese Med, Taichung 41354, Taiwan.
   [Huang, Chih-Yang] China Med Univ, Grad Inst Biomed Sci, Taichung 404, Taiwan.
   [Huang, Chih-Yang] Tzu Chi Univ Sci & Technol, Buddhist Tzu Chi Med Fdn, Ctr Gen Educ, Hualien 970, Taiwan.
   [Huang, Chih-Yang] China Med Univ, China Med Univ Hosp, Dept Med Res, Taichung 404, Taiwan.
   [Huang, Chih-Yang] Asia Univ, Dept Biotechnol, Taichung 413, Taiwan.
C3 China Medical University Taiwan; Buddhist Tzu Chi General Hospital;
   Hualien Tzu Chi Hospital; University of Taipei; China Medical University
   Taiwan; China Medical University Hospital - Taiwan; Buddhist Tzu Chi
   General Hospital; Hualien Tzu Chi Hospital; Tzu Chi University; Buddhist
   Tzu Chi General Hospital; Hualien Tzu Chi Hospital; Tzu Chi University;
   Buddhist Tzu Chi General Hospital; Hualien Tzu Chi Hospital; Tzu Chi
   University; Bharathiar University; China Medical University Taiwan;
   China Medical University Taiwan; Tzu Chi University of Science &
   Technology; China Medical University Taiwan; China Medical University
   Hospital - Taiwan; Asia University Taiwan
RP Huang, CY (corresponding author), Buddhist Tzu Chi Med Fdn, Hualien Tzu Chi Hosp, Cardiovasc & Mitochondrial Related Dis Res Ctr, Hualien 97004, Taiwan.; Tsai, Y (corresponding author), China Med Univ, Grad Inst Chinese Med, Taichung 41354, Taiwan.; Huang, CY (corresponding author), China Med Univ, Grad Inst Biomed Sci, Taichung 404, Taiwan.; Huang, CY (corresponding author), Tzu Chi Univ Sci & Technol, Buddhist Tzu Chi Med Fdn, Ctr Gen Educ, Hualien 970, Taiwan.; Huang, CY (corresponding author), China Med Univ, China Med Univ Hosp, Dept Med Res, Taichung 404, Taiwan.; Huang, CY (corresponding author), Asia Univ, Dept Biotechnol, Taichung 413, Taiwan.
EM yhtsai@mail.cmu.edu.tw; cyhuang@mail.cmu.edu.tw
RI Hu, Luna/KOC-2661-2024; Viswanadha, Vijaya/ABG-4936-2020; Kuo,
   Chin-Sung/JCE-4770-2023; Yuang, Chih-Yang/O-5111-2015
OI Huang, Chih-Yang/0000-0003-2347-0411
FU China medical University, Taiwan [CMU102-AISA-04-08]; Asia University,
   Taiwan [SIA-107-CMUH-01]; Tzu Chi hospital, Taiwan [IMART110-01-15]
FX This study was supported by a joint grant from China medical University,
   Taiwan (CMU102-AISA-04-08), Asia University, Taiwan (SIA-107-CMUH-01)
   and Tzu Chi hospital, Taiwan (IMART110-01-15).
CR Alsaied T, 2017, PEDIATR RES, V81, P919, DOI 10.1038/pr.2017.18
   Animaw W, 2017, PLOS ONE, V12, DOI 10.1371/journal.pone.0187670
   Banerjee S, 2017, HELL J CARDIOL, V58, P342, DOI 10.1016/j.hjc.2017.01.003
   Amenós AC, 2010, REV ESP CARDIOL, V63, P225, DOI 10.1016/S0300-8932(10)70041-5
   Chang MH, 2008, J MOL ENDOCRINOL, V41, P65, DOI 10.1677/JME-08-0051
   Chang RL, 2019, PLOS ONE, V14, DOI 10.1371/journal.pone.0216285
   Chang RL, 2019, ENVIRON TOXICOL, V34, P210, DOI 10.1002/tox.22676
   Chen CH, 2020, J CELL PHYSIOL, V235, P3539, DOI 10.1002/jcp.29242
   Chen W, 2019, THERANOSTICS, V9, P3980, DOI 10.7150/thno.32352
   Chu CH, 2008, J ENDOCRINOL, V197, P381, DOI 10.1677/JOE-07-0619
   Di Lullo L, 2017, INDIAN HEART J, V69, P255, DOI 10.1016/j.ihj.2017.01.005
   Dirkx E, 2013, BBA-MOL BASIS DIS, V1832, P2414, DOI 10.1016/j.bbadis.2013.07.023
   Herzog CA, 2011, KIDNEY INT, V80, P572, DOI 10.1038/ki.2011.223
   Huang CY, 2018, INT J CARDIOL, V257, P283, DOI 10.1016/j.ijcard.2017.10.102
   Huang CY, 2016, CELL DEATH DIS, V7, DOI 10.1038/cddis.2016.356
   Ichihara A, 1998, HYPERTENSION, V31, P1255, DOI 10.1161/01.HYP.31.6.1255
   Levey AS, 2015, JAMA-J AM MED ASSOC, V313, P837, DOI 10.1001/jama.2015.0602
   Liu YL, 2018, CARDIORENAL MED, V8, P31, DOI 10.1159/000479010
   Liu YL, 2015, CARDIORENAL MED, V5, P79, DOI 10.1159/000371454
   Marchais SJ, 1999, NEPHROL DIAL TRANSPL, V14, P2178, DOI 10.1093/ndt/14.9.2178
   Marrero MB, 2006, AM J PHYSIOL-RENAL, V290, pF762, DOI 10.1152/ajprenal.00181.2005
   Matsui F, 2012, J SURG RES, V178, P339, DOI 10.1016/j.jss.2012.06.050
   Nandi Shyam Sundar, 2015, J Nat Sci, V1
   Nesarhosseini V, 2019, CASP J INTERN MED, V10, P36, DOI 10.22088/cjim.10.1.36
   Pace J, 2019, AM J PHYSIOL-RENAL, V316, pF1151, DOI 10.1152/ajprenal.00034.2019
   Pandey S, 2019, AM J PHYSIOL-CELL PH, V317, pC235, DOI 10.1152/ajpcell.00079.2019
   Pandey S, 2019, J CELL BIOCHEM, V120, P16956, DOI 10.1002/jcb.28957
   Raizada V, 2012, J INVEST MED, V60, P785, DOI 10.2310/JIM.0b013e318250b101
   Ronco C, 2012, J AM COLL CARDIOL, V60, P1031, DOI 10.1016/j.jacc.2012.01.077
   Segall L, 2014, BIOMED RES INT, V2014, DOI 10.1155/2014/937398
   Sheu ML, 2017, ONCOTARGET, V8, P16925, DOI 10.18632/oncotarget.14808
   Shi YH, 2008, FEBS LETT, V582, P3484, DOI 10.1016/j.febslet.2008.09.014
   Steigerwalt S, 2007, AM J NEPHROL, V27, P159, DOI 10.1159/000100106
   The diagnosis of diabetes, 1969, GP, V39, P133
   Wang XD, 2002, DIABETES, V51, P3505, DOI 10.2337/diabetes.51.12.3505
   Wang Yunfei, 2021, Aging (Albany NY), V13, DOI 10.18632/aging.202599
   Zheng C, 2019, CELL DEATH DIS, V10, DOI 10.1038/s41419-019-2085-0
NR 37
TC 1
Z9 1
U1 0
U2 4
PU IMPACT JOURNALS LLC
PI ORCHARD PARK
PA 6666 E QUAKER ST, STE 1, ORCHARD PARK, NY 14127 USA
SN 1945-4589
J9 AGING-US
JI Aging-US
PD JUL 15
PY 2021
VL 13
IS 13
BP 17536
EP 17547
PG 12
WC Cell Biology; Geriatrics & Gerontology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Geriatrics & Gerontology
GA TU8LU
UT WOS:000681283300010
PM 34233296
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Zhang, JJ
   Cao, J
   Qian, JN
   Gu, XS
   Zhang, W
   Chen, XF
AF Zhang, Jingjing
   Cao, Ji
   Qian, Jianan
   Gu, Xiaosong
   Zhang, Wei
   Chen, Xianfan
TI Regulatory mechanism of CaMKII 8 mediated by RIPK3 on myocardial
   fibrosis and reversal effects of RIPK3 inhibitor GSK'872
SO BIOMEDICINE & PHARMACOTHERAPY
LA English
DT Article
DE Receptor-interacting protein kinase3 (RIPK3); CaMKII; Necroptosis;
   Oxidative stress; RIPK3 inhibitor GSK'872; Myocardial fibrosis
ID CARDIOMYOPATHY; BIOMARKERS
AB Background: Myocardial fibrosis (MF) remains a prominent challenge in heart disease. The role of receptorinteracting protein kinase 3 (RIPK3)-mediated necroptosis is evident in the pathogenesis of numerous heart diseases. Concurrently, the activation of Ca2+/calmodulin-dependent protein kinase (CaMKII) is pivotal in cardiovascular disease (CVD). This study aimed to evaluate the impact and underlying mechanisms of RIPK3 on myocardial injury in MF and to elucidate the potential involvement of CaMKII. Methods: Building upon our previous research methods [1], wild-type (WT) mice and RIPK3 knockout (RIPK3 -/-) mice underwent random assignment for transverse aortic constriction (TAC) in vivo. Four weeks post-procedure, the MF model was effectively established. Parameters such as the extent of MF, myocardial injury, RIPK3 expression, necroptosis, CaMKII activity, phosphorylation of mixed lineage kinase domain-like protein (MLKL), mitochondrial ultrastructural details, and oxidative stress levels were examined. Cardiomyocyte fibrosis was simulated in vitro using angiotensin II on cardiac fibroblasts. Results: TAC reliably produced MF, myocardial injury, CaMKII activation, and necroptosis in mice. RIPK3 depletion ameliorated these conditions. The RIPK3 inhibitor, GSK'872, suppressed the expression of RIPK3 in myocardial fibroblasts, leading to improved fibrosis and inflammation, diminished CaMKII oxidation and phosphorylation levels, and the rectification of CaMKII8 alternative splicing anomalies. Furthermore, GSK'872 downregulated the expressions of RIPK1, RIPK3, and MLKL phosphorylation, attenuated necroptosis, and bolstered the oxidative stress response. Conclusions: Our data suggested that in MF mice, necroptosis was augmented in a RIPK3-dependent fashion. There seemed to be a positive correlation between CaMKII activation and RIPK3 expression. The adverse effects on myocardial fibrosis mediated by CaMKII 8 through RIPK3 could potentially be mitigated by the RIPK3 inhibitor, GSK'872. This offered a fresh perspective on the amelioration and treatment of MF and myocardial injury.
C1 [Zhang, Jingjing; Cao, Ji; Qian, Jianan; Zhang, Wei] Nantong Univ, Sch Pharm, Nantong 226001, Jiangsu, Peoples R China.
   [Zhang, Jingjing; Gu, Xiaosong; Zhang, Wei] Nantong Univ, Sch Med, Nantong 226001, Jiangsu, Peoples R China.
   [Chen, Xianfan] Nantong Univ, Affiliated Hosp 2, Nantong Peoples Hosp 1, Dept Pharm, Nantong 226001, Jiangsu, Peoples R China.
C3 Nantong University; Nantong University; Nantong University
RP Zhang, W (corresponding author), Nantong Univ, Sch Pharm, Nantong 226001, Jiangsu, Peoples R China.; Chen, XF (corresponding author), Nantong Univ, Affiliated Hosp 2, Nantong Peoples Hosp 1, Dept Pharm, Nantong 226001, Jiangsu, Peoples R China.
EM zhangw@ntu.edu.cn; cxf8448180@163.com
RI Zhang, Wei/JKI-3565-2023; Gu, Xiao-song/ABD-5166-2021
FU National Natural Science Foundation of China [82070418, 81873470]
FX The work was funded by grants 81873470 and 82070418 from the National
   Natural Science Foundation of China.
CR Alonso-Herranz L, 2020, ELIFE, V9, DOI 10.7554/eLife.57920
   Beckendorf J, 2018, BASIC RES CARDIOL, V113, DOI 10.1007/s00395-018-0688-8
   Bers DM, 2008, ANNU REV PHYSIOL, V70, P23, DOI 10.1146/annurev.physiol.70.113006.100455
   Bertheloot D, 2021, CELL MOL IMMUNOL, V18, P1106, DOI 10.1038/s41423-020-00630-3
   Cao J., 2022, Front. Med., V28
   Chaouhan HS, 2022, INT J MOL SCI, V23, DOI 10.3390/ijms232112714
   Das K, 2022, REDOX BIOL, V57, DOI 10.1016/j.redox.2022.102487
   Del Re DP, 2019, PHYSIOL REV, V99, P1763, DOI 10.1152/physrev.00022.2018
   Duan XR, 2020, CELL DEATH DIS, V11, DOI 10.1038/s41419-020-2328-0
   Espeland T, 2018, Tidsskr Nor Laegeforen, V138
   Frangogiannis NG, 2021, CARDIOVASC RES, V117, P1450, DOI 10.1093/cvr/cvaa324
   Gong YN, 2017, CELL, V169, P286, DOI 10.1016/j.cell.2017.03.020
   Guo CH, 2019, J AUTOIMMUN, V103, DOI 10.1016/j.jaut.2019.05.014
   Hegyi B, 2019, J MOL CELL CARDIOL, V127, P246, DOI 10.1016/j.yjmcc.2019.01.001
   Heymans S, 2015, EUR J HEART FAIL, V17, P764, DOI 10.1002/ejhf.312
   Hinderer S, 2019, ADV DRUG DELIVER REV, V146, P77, DOI 10.1016/j.addr.2019.05.011
   Hu XL, 2022, FRONT ENDOCRINOL, V13, DOI 10.3389/fendo.2022.1032614
   Javier Duran, 2021, Front. Cell Dev. Biol., V9
   Jorgensen AN, 2022, EXP MOL PATHOL, V127, DOI 10.1016/j.yexmp.2022.104815
   Khoury MK, 2020, AM J PATHOL, V190, P272, DOI 10.1016/j.ajpath.2019.10.012
   Kremastiotis G, 2021, SCI REP-UK, V11, DOI 10.1038/s41598-021-02508-4
   Kurose H, 2021, CELLS-BASEL, V10, DOI 10.3390/cells10071716
   Liu M, 2022, INT J BIOL SCI, V18, P199, DOI 10.7150/ijbs.65402
   López B, 2021, NAT REV CARDIOL, V18, P479, DOI 10.1038/s41569-020-00504-1
   Ma YX, 2021, INT J MOL SCI, V22, DOI 10.3390/ijms222212341
   Nikolov A, 2022, METABOLITES, V12, DOI 10.3390/metabo12040297
   Nulali J, 2022, BIOMOLECULES, V12, DOI 10.3390/biom12111674
   Patel NJ, 2021, EXPERT OPIN THER TAR, V25, P63, DOI 10.1080/14728222.2021.1849145
   Pichler G, 2020, J HYPERTENS, V38, P2036, DOI 10.1097/HJH.0000000000002504
   Qiao SG, 2022, CELL DEATH DIS, V13, DOI 10.1038/s41419-022-04587-1
   Schimmel K, 2022, FRONT CARDIOVASC MED, V9, DOI 10.3389/fcvm.2022.886553
   Scridon A, 2022, PHARMACEUTICS, V14, DOI 10.3390/pharmaceutics14081599
   Spinale FG, 2014, BIOCHEM PHARMACOL, V90, P7, DOI 10.1016/j.bcp.2014.04.011
   Srivastava A, 2022, MATRIX BIOL, V112, P72, DOI 10.1016/j.matbio.2022.08.005
   Suetomi T, 2018, CIRCULATION, V138, P2530, DOI 10.1161/CIRCULATIONAHA.118.034621
   Ureche C, 2020, BIOMARK MED, V14, P1265, DOI 10.2217/bmm-2020-0298
   Willeford A, 2018, JCI INSIGHT, V3, DOI 10.1172/jci.insight.97054
   Winkle AJ, 2022, EXPERT OPIN THER TAR, V26, P29, DOI 10.1080/14728222.2022.2031974
   Yang YJ, 2021, FRONT MOL BIOSCI, V8, DOI 10.3389/fmolb.2021.668129
   Ying L, 2021, ACTA PHYSIOL, V231, DOI 10.1111/apha.13541
   Zhan QH, 2022, AUTOPHAGY, V18, P726, DOI 10.1080/15548627.2021.1954348
   Zhang JX, 2022, CIRCULATION, V145, P1154, DOI 10.1161/CIRCULATIONAHA.121.055920
   Zhang M, 2019, NAT CELL BIOL, V21, P1152, DOI 10.1038/s41556-019-0380-8
   Zhang T, 2003, CIRC RES, V92, P912, DOI 10.1161/01.RES.0000069686.31472.C5
   Zhang T, 2016, NAT MED, V22, P175, DOI 10.1038/nm.4017
   Zhong P, 2017, J CARDIOVASC PHARM, V70, P245, DOI 10.1097/FJC.0000000000000512
   Zhou T, 2021, CELLS-BASEL, V10, DOI 10.3390/cells10092397
   Zhu PJ, 2021, OXID MED CELL LONGEV, V2021, DOI 10.1155/2021/6635955
   Zi M, 2019, CURR RES PHYSIOL, V1, P1, DOI 10.1016/j.crphys.2019.10.001
NR 49
TC 9
Z9 9
U1 2
U2 15
PU ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
PI ISSY-LES-MOULINEAUX
PA 65 RUE CAMILLE DESMOULINS, CS50083, 92442 ISSY-LES-MOULINEAUX, FRANCE
SN 0753-3322
EI 1950-6007
J9 BIOMED PHARMACOTHER
JI Biomed. Pharmacother.
PD OCT
PY 2023
VL 166
AR 115380
DI 10.1016/j.biopha.2023.115380
EA AUG 2023
PG 15
WC Medicine, Research & Experimental; Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Research & Experimental Medicine; Pharmacology & Pharmacy
GA R0EC6
UT WOS:001061146500001
PM 37639745
OA gold
DA 2025-04-10
ER

PT J
AU Otten, J
   van der Ven, PFM
   Vakeel, P
   Eulitz, S
   Kirfel, G
   Brandau, O
   Boesl, M
   Schrickel, JW
   Linhart, M
   Hayess, K
   Naya, FJ
   Milting, H
   Meyer, R
   Fürst, DO
AF Otten, Julia
   van der Ven, Peter F. M.
   Vakeel, Padmanabhan
   Eulitz, Stefan
   Kirfel, Gregor
   Brandau, Oliver
   Boesl, Michael
   Schrickel, Jan W.
   Linhart, Markus
   Hayess, Katrin
   Naya, Francisco J.
   Milting, Hendrik
   Meyer, Rainer
   Fuerst, Dieter O.
TI Complete loss of murine Xin results in a mild cardiac phenotype with
   altered distribution of intercalated discs
SO CARDIOVASCULAR RESEARCH
LA English
DT Article
DE Cardiac hypertrophy; Intercalated disc; Xin-repeat protein isoforms;
   Alternative splicing; Null mutation
ID IMMUNOELECTRON MICROSCOPY; CONDUCTION DEFECTS; N-CADHERIN; MXIN-ALPHA;
   PROTEIN; HEART; MICE; MUSCLE; GENE; CARDIOMYOPATHY
AB Xin is a striated muscle-specific F-actin binding protein that has been implicated in cardiomyopathies. In cardiomyocytes, Xin is localized at intercalated discs (IDs). Mice lacking only two of the three Xin isoforms (XinAB(-/-) mice) develop severe cardiac hypertrophy. To further investigate the function of Xin variants in the mammalian heart, we generated XinABC(-/-) mice deficient in all Xin isoforms.
   XinABC(-/-) mice showed a very mild phenotype: heart weight, heart weight to tibia length ratios, and cardiac dimensions were not altered. Increased perivascular fibrosis was only observed in hearts of young XinABC(-/-) mice. Striking differences were revealed in isolated cardiomyocytes: XinABC(-/-) cells demonstrated a significantly increased number of non-terminally localized ID-like structures. Furthermore, resting sarcomere length was increased, sarcomere shortening, peak shortening at 0.5-1 Hz, and the duration of shortening were decreased, and shortening and relengthening velocities were accelerated at frequencies above 4 Hz in XinABC(-/-) cardiomyocytes. ECG showed a significantly shorter HV interval and a trend towards shorter QRS interval in XinABC(-/-) mice, suggesting a faster conduction velocity of the ventricular-specific conduction system. In human cardiac tissue, expression of XinC protein was detected solely in samples from patients with cardiac hypertrophy.
   Total Xin deficiency leads to topographical ID alterations, premature fibrosis and subtle changes in contractile behaviour; this is a milder cardiac phenotype than that observed in XinAB(-/-) mice, which still can express XinC. Together with the finding that XinC is detected solely in cardiomyopathic human tissues, this suggests that its expression is responsible for the stronger dominant phenotype in XinAB(-/-) mice. Furthermore, it indicates that XinC may be involved in the development of human cardiac hypertrophy.
C1 [Meyer, Rainer] Univ Bonn, Inst Physiol 2, D-5300 Bonn, Germany.
   [Otten, Julia; van der Ven, Peter F. M.; Vakeel, Padmanabhan; Eulitz, Stefan; Kirfel, Gregor; Fuerst, Dieter O.] Univ Bonn, Inst Cell Biol, Dept Mol & Cell Biol, D-53121 Bonn, Germany.
   [van der Ven, Peter F. M.; Vakeel, Padmanabhan; Hayess, Katrin; Fuerst, Dieter O.] Univ Potsdam, Dept Cell Biol, Potsdam, Germany.
   [Brandau, Oliver; Boesl, Michael] Max Planck Inst Biochem, D-82152 Martinsried, Germany.
   [Schrickel, Jan W.; Linhart, Markus] Univ Bonn, Dept Med Cardiol, D-5300 Bonn, Germany.
   [Naya, Francisco J.] Boston Univ, Dept Biol, Boston, MA 02215 USA.
   [Milting, Hendrik] Erich & Hanna Klessmann Inst Kardiovaskulare Fors, Herz & Diabet Zentrum NRW, Bad Oeynhausen, Germany.
C3 University of Bonn; University of Bonn; University of Potsdam; Max
   Planck Society; University of Bonn; Boston University; Ruhr University
   Bochum
RP Meyer, R (corresponding author), Univ Bonn, Inst Physiol 2, Wilhelmstr 31, D-5300 Bonn, Germany.
EM rainer.meyer@ukb.uni-bonn.de; dfuerst@uni-bonn.de
RI Meyer, Rainer/H-5871-2013; Furst, Dieter O./H-8561-2013
OI Furst, Dieter O./0000-0001-8805-6444; van der Ven,
   Peter/0000-0002-9750-8913
FU Deutsche Forschungsgemeinschaft [FU339/5-1]; German Ministry of
   Education and Research (BMBF, Bonn, Germany)
FX This study was supported by a grant from the Deutsche
   Forschungsgemeinschaft (grant number FU339/5-1 to D. O. F. and R. M.).
   D. O. F. and P. F. M. V. are supported by a grant from the German
   network on muscular dystrophies (MD-NET) funded by the German Ministry
   of Education and Research (BMBF, Bonn, Germany).
CR Awad MM, 2008, NAT CLIN PRACT CARD, V5, P258, DOI 10.1038/ncpcardio1182
   Cherepanova O, 2006, J MOL BIOL, V356, P714, DOI 10.1016/j.jmb.2005.11.082
   Choi SJ, 2007, J BIOL CHEM, V282, P36024, DOI 10.1074/jbc.M707639200
   FASSLER R, 1995, GENE DEV, V9, P1896, DOI 10.1101/gad.9.15.1896
   Franke WW, 2006, EUR J CELL BIOL, V85, P69, DOI 10.1016/j.ejcb.2005.11.003
   FURST DO, 1988, J CELL BIOL, V106, P1563, DOI 10.1083/jcb.106.5.1563
   Grosskurth SE, 2008, PLOS ONE, V3, DOI 10.1371/journal.pone.0002857
   Gustafson-Wagner EA, 2007, AM J PHYSIOL-HEART C, V293, pH2680, DOI 10.1152/ajpheart.00806.2007
   Huang HT, 2006, J BIOL CHEM, V281, P39370, DOI 10.1074/jbc.M603244200
   Kostetskii I, 2005, CIRC RES, V96, P346, DOI 10.1161/01.RES.0000156274.72390.2c
   Kreuzberg MM, 2006, P NATL ACAD SCI USA, V103, P5959, DOI 10.1073/pnas.0508512103
   Mitchell GF, 1998, AM J PHYSIOL-HEART C, V274, pH747, DOI 10.1152/ajpheart.1998.274.3.H747
   Obermann WMJ, 1996, J CELL BIOL, V134, P1441, DOI 10.1083/jcb.134.6.1441
   Pacholsky D, 2004, J CELL SCI, V117, P5257, DOI 10.1242/jcs.01406
   Radice GL, 1997, DEV BIOL, V181, P64, DOI 10.1006/dbio.1996.8443
   Ruiz P, 1996, J CELL BIOL, V135, P215, DOI 10.1083/jcb.135.1.215
   Schrickel JW, 2007, CARDIOVASC RES, V76, P257, DOI 10.1016/j.cardiores.2007.07.001
   Schrickel JW, 2002, BASIC RES CARDIOL, V97, P452, DOI 10.1007/s003950200052
   Sinn HW, 2002, DEV DYNAM, V225, P1, DOI 10.1002/dvdy.10131
   Tiemann K, 2003, AM J PHYSIOL-HEART C, V284, pH464, DOI 10.1152/ajpheart.00540.2002
   van der Ven PFM, 2006, EXP CELL RES, V312, P2154, DOI 10.1016/j.yexcr.2006.03.015
   van der Ven PFM, 2000, CELL MOTIL CYTOSKEL, V45, P149, DOI 10.1002/(SICI)1097-0169(200002)45:2<149::AID-CM6>3.0.CO;2-G
   Walker Michael G., 2001, Mini-Reviews in Medicinal Chemistry, V1, P197, DOI 10.2174/1389557013407034
   Wang Da-Zhi, 1996, Frontiers in Bioscience (online), V1, pA1
   Wang DZ, 1999, DEVELOPMENT, V126, P1281
NR 25
TC 32
Z9 37
U1 0
U2 3
PU OXFORD UNIV PRESS
PI OXFORD
PA GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND
SN 0008-6363
J9 CARDIOVASC RES
JI Cardiovasc. Res.
PD MAR 1
PY 2010
VL 85
IS 4
BP 739
EP 750
DI 10.1093/cvr/cvp345
PG 12
WC Cardiac & Cardiovascular Systems
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology
GA 555DO
UT WOS:000274487900014
PM 19843512
OA Bronze
DA 2025-04-10
ER

PT J
AU Pasipoularides, A
AF Pasipoularides, Ares
TI Linking Genes to Cardiovascular Diseases: Gene Action and
   Gene-Environment Interactions
SO JOURNAL OF CARDIOVASCULAR TRANSLATIONAL RESEARCH
LA English
DT Article
DE Genotype and expressed phenotypes; Exons, introns and alternative
   splicing; Monogenic and polygenic traits and gene networks; Major gene,
   "modifier genes," and pleiotropy; Regulatory DNA "switches" and
   regulation of gene expression; Gene interactions and epistasis; Genetic
   cardiomyopathies; HCM; DCM; Environmental influences and epigenetics;
   Mutations and haplotypes
ID ELECTRONIC HEALTH RECORD; DIASTOLIC VORTEX FORCES; PRE-MESSENGER-RNA;
   FLUID-DYNAMICS; AORTIC-STENOSIS; MECHANOTRANSDUCTION MECHANISMS;
   CLINICAL-ASSESSMENT; VENTRICULAR LOAD; MOLECULAR-BASIS; FILLING VORTEX
AB A unique myocardial characteristic is its ability to grow/remodel in order to adapt; this is determined partly by genes and partly by the environment and the milieu int,rieur. In the "post-genomic" era, a need is emerging to elucidate the physiologic functions of myocardial genes, as well as potential adaptive and maladaptive modulations induced by environmental/epigenetic factors. Genome sequencing and analysis advances have become exponential lately, with escalation of our knowledge concerning sometimes controversial genetic underpinnings of cardiovascular diseases. Current technologies can identify candidate genes variously involved in diverse normal/abnormal morphomechanical phenotypes, and offer insights into multiple genetic factors implicated in complex cardiovascular syndromes. The expression profiles of thousands of genes are regularly ascertained under diverse conditions. Global analyses of gene expression levels are useful for cataloging genes and correlated phenotypes, and for elucidating the role of genes in maladies. Comparative expression of gene networks coupled to complex disorders can contribute insights as to how "modifier genes" influence the expressed phenotypes. Increasingly, a more comprehensive and detailed systematic understanding of genetic abnormalities underlying, for example, various genetic cardiomyopathies is emerging. Implementing genomic findings in cardiology practice may well lead directly to better diagnosing and therapeutics. There is currently evolving a strong appreciation for the value of studying gene anomalies, and doing so in a non-disjointed, cohesive manner. However, it is challenging for many-practitioners and investigators-to comprehend, interpret, and utilize the clinically increasingly accessible and affordable cardiovascular genomics studies. This survey addresses the need for fundamental understanding in this vital area.
C1 [Pasipoularides, Ares] Duke Univ, Sch Med, Durham, NC 27708 USA.
   [Pasipoularides, Ares] Duke NSF Res Ctr Emerging Cardiovasc Technol, Durham, NC USA.
   [Pasipoularides, Ares] Duke Univ, Sch Med, Dept Surg, Durham, NC 27710 USA.
C3 Duke University; Duke University
RP Pasipoularides, A (corresponding author), Duke Univ, Sch Med, Durham, NC 27708 USA.
EM apasipou@duke.edu
FU National Heart, Lung, and Blood Institute [R01 HL 050446]; National
   Science Foundation [CDR 8622201]; North Carolina Supercomputing Center
   and Cray Research
FX Research support, for work from my Laboratory surveyed here, was
   provided by National Heart, Lung, and Blood Institute, Grant R01 HL
   050446; National Science Foundation, Grant CDR 8622201; and North
   Carolina Supercomputing Center and Cray Research.
CR Altshuler D, 2005, NATURE, V437, P1299, DOI 10.1038/nature04226
   [Anonymous], HELLENIC J CARDIOL
   [Anonymous], 2001, Foundations of Systems Biology
   [Anonymous], 2007, Analysis of Biological Data: A Soft Computing Approach
   Antonarakis SE, 2006, NAT REV GENET, V7, P277, DOI 10.1038/nrg1826
   Arnaudo AM, 2013, EPIGENET CHROMATIN, V6, DOI 10.1186/1756-8935-6-24
   Austin ED, 2014, CIRC RES, V115, P189, DOI 10.1161/CIRCRESAHA.115.303404
   BALDI P, 2002, DNA MICROARRAYS GENE
   Baldwin H. Scott, 1999, Current Opinion in Pediatrics, V11, P413, DOI 10.1097/00008480-199910000-00008
   Barabási AL, 2011, NAT REV GENET, V12, P56, DOI 10.1038/nrg2918
   Bartel DP, 2009, CELL, V136, P215, DOI 10.1016/j.cell.2009.01.002
   Bass JIF, 2015, CELL, V161, P661, DOI 10.1016/j.cell.2015.03.003
   Bateman MG, 2013, J CARDIOVASC TRANSL, V6, P155, DOI 10.1007/s12265-012-9437-9
   Beadle GW, 1941, P NATL ACAD SCI USA, V27, P499, DOI 10.1073/pnas.27.11.499
   Berger SI, 2007, BMC BIOINFORMATICS, V8, DOI 10.1186/1471-2105-8-372
   Bernal JA, 2013, J CARDIOVASC TRANSL, V6, P956, DOI 10.1007/s12265-013-9494-8
   Bevilacqua V., 2006, Engineering Letters, V13, P335
   Beyer A, 2007, NAT REV GENET, V8, P699, DOI 10.1038/nrg2144
   BIRD JJ, 1982, CIRCULATION, V66, P835, DOI 10.1161/01.CIR.66.4.835
   Bittner M, 1999, NAT GENET, V22, P213, DOI 10.1038/10265
   Bodi V, 2013, J CARDIOVASC TRANSL, V6, P808, DOI 10.1007/s12265-013-9505-9
   Boley N, 2014, NAT BIOTECHNOL, V32, P341, DOI 10.1038/nbt.2850
   Celniker SE, 2009, NATURE, V459, P927, DOI 10.1038/459927a
   Celotto AM, 2001, GENETICS, V159, P599
   Chen J, 1999, J CLIN INVEST, V103, P1483, DOI 10.1172/JCI7297
   Cheung VG, 2002, NAT GENET, V32, P522, DOI 10.1038/ng1036
   Cohen JC, 2004, SCIENCE, V305, P869, DOI 10.1126/science.1099870
   Collins FS, 2004, NATURE, V431, P931, DOI 10.1038/nature03001
   Cooper DN, 2013, HUM GENET, V132, P1077, DOI 10.1007/s00439-013-1331-2
   Cordeddu V, 2009, NAT GENET, V41, P1022, DOI 10.1038/ng.425
   Craig WE, 1987, DIASTOLIC RELAXATION, P125
   Dalton L, 2009, CURR GENOMICS, V10, P430, DOI 10.2174/138920209789177601
   de Klerk E, 2015, TRENDS GENET, V31, P128, DOI 10.1016/j.tig.2015.01.001
   Deddens JC, 2013, J CARDIOVASC TRANSL, V6, P884, DOI 10.1007/s12265-013-9493-9
   Diez D, 2010, MOL BIOSYST, V6, P289, DOI 10.1039/b912078e
   Douglas PS, 2008, J CARDIOVASC TRANSL, V1, P17, DOI 10.1007/s12265-007-9004-y
   Draghici S., 2003, DATA ANAL TOOLS DNA
   Dudley JT, 2012, GENOME RES, V22, P1383, DOI 10.1101/gr.133702.111
   Enard W, 2002, SCIENCE, V296, P340, DOI 10.1126/science.1068996
   Evans GA, 2000, NAT BIOTECHNOL, V18, P127, DOI 10.1038/72480
   Friede KA, 2015, J CARDIOVASC TRANSL, V8, P339, DOI 10.1007/s12265-015-9640-6
   Gelb BD, 2014, CSH PERSPECT MED, V4, DOI 10.1101/cshperspect.a013953
   Génin E, 2008, HUM GENET, V124, P357, DOI 10.1007/s00439-008-0560-2
   GEORGIADIS JG, 1992, ANN BIOMED ENG, V20, P81, DOI 10.1007/BF02368507
   Gibbs RA, 2003, NATURE, V426, P789, DOI 10.1038/nature02168
   Glass DJ, 2010, CLIN CHEM, V56, P1080, DOI 10.1373/clinchem.2010.144477
   Glotov AS, 2015, CLIN CHIM ACTA, V446, P132, DOI 10.1016/j.cca.2015.04.014
   Goh KI, 2007, P NATL ACAD SCI USA, V104, P8685, DOI 10.1073/pnas.0701361104
   Haldane JBS, 1941, J GENET, V41, P149, DOI 10.1007/BF02983018
   Hall JL, 2008, J CARDIOVASC TRANSL, V1, P283, DOI 10.1007/s12265-008-9068-3
   Harrington ED, 2008, FEBS LETT, V582, P1251, DOI 10.1016/j.febslet.2008.02.033
   Hershberger RE, 2010, CIRC-CARDIOVASC GENE, V3, P155, DOI 10.1161/CIRCGENETICS.109.912345
   Hershberger RE, 2009, J CARD FAIL, V15, P83, DOI 10.1016/j.cardfail.2009.01.006
   Hudson JE, 2013, J CARDIOVASC TRANSL, V6, P909, DOI 10.1007/s12265-013-9486-8
   ISAAZ K, 1991, J AM COLL CARDIOL, V17, P112, DOI 10.1016/0735-1097(91)90712-I
   JACOB F, 1961, J MOL BIOL, V3, P318, DOI 10.1016/S0022-2836(61)80072-7
   Johannsen W., 1909, Elemente der exakten Erblichkeitslehre
   Jones MJ, 2013, GENOME BIOL, V14, DOI 10.1186/gb-2013-14-7-126
   Kamisago M, 2000, NEW ENGL J MED, V343, P1688, DOI 10.1056/NEJM200012073432304
   Kan ZY, 2002, GENOME RES, V12, P1837, DOI 10.1101/gr.764102
   Kassem HS, 2013, J CARDIOVASC TRANSL, V6, P65, DOI 10.1007/s12265-012-9425-0
   KAUFFMAN S, 1969, NATURE, V224, P177, DOI 10.1038/224177a0
   Kimura A, 2010, J HUM GENET, V55, P81, DOI 10.1038/jhg.2009.138
   KING MC, 1975, SCIENCE, V188, P107, DOI 10.1126/science.1090005
   Kitao H, 2011, INT J HEMATOL, V93, P417, DOI 10.1007/s12185-011-0777-z
   Kluger Y, 2003, GENOME RES, V13, P703, DOI 10.1101/gr.648603
   Kraus WE, 2015, J CARDIOVASC TRANSL, V8, P449, DOI 10.1007/s12265-015-9648-y
   Krishnamoorthy P, 2014, J CARDIOVASC TRANSL, V7, P692, DOI 10.1007/s12265-014-9586-0
   Lander ES, 2001, NATURE, V409, P860, DOI 10.1038/35057062
   Lara-Pezzi E, 2013, J CARDIOVASC TRANSL, V6, P945, DOI 10.1007/s12265-013-9482-z
   Larribe F, 2011, STAT SINICA, V21, P43
   Lawrence J., 1994, INTRO NEURAL NETWORK
   Luco RF, 2011, CELL, V144, P16, DOI 10.1016/j.cell.2010.11.056
   Lunkenheimer PP, 2013, J CARDIOVASC TRANSL, V6, P176, DOI 10.1007/s12265-012-9440-1
   Madeira SC, 2004, IEEE ACM T COMPUT BI, V1, P24, DOI 10.1109/TCBB.2004.2
   Marian AJ, 2001, J MOL CELL CARDIOL, V33, P655, DOI 10.1006/jmcc.2001.1340
   Marston SB, 2011, J CARDIOVASC TRANSL, V4, P245, DOI 10.1007/s12265-011-9266-2
   Mason Paul H., 2010, Biology Theory, V5, P277
   Matkovich SJ, 2010, J CLIN INVEST, V120, P280, DOI 10.1172/JCI39085
   Maurano MT, 2012, SCIENCE, V337, P1190, DOI 10.1126/science.1222794
   McKernan KJ, 2009, GENOME RES, V19, P1527, DOI 10.1101/gr.091868.109
   McPherson JD, 2001, NATURE, V409, P934, DOI 10.1038/35057157
   MIRSKY I, 1990, PROG CARDIOVASC DIS, V32, P291, DOI 10.1016/0033-0620(90)90018-W
   MIRSKY I, 1980, FED PROC, V39, P156
   Moffatt JD, 2005, PHARMACOL THERAPEUT, V107, P343, DOI 10.1016/j.pharmthera.2005.03.007
   Moller DV, 2009, EUR J HUM GENET, V17, P1241, DOI 10.1038/ejhg.2009.34
   Moreno-Moral A, 2013, J CARDIOVASC TRANSL, V6, P931, DOI 10.1007/s12265-013-9504-x
   Moss Lenny., 2003, WHAT GENES CANT
   Nadal-Ginard B, 1990, CURR OPIN CELL BIOL, V2, P1058, DOI 10.1016/0955-0674(90)90156-9
   Neph S, 2012, CELL, V150, P1274, DOI 10.1016/j.cell.2012.04.040
   Noble D, 2013, PROG BIOPHYS MOL BIO, V111, P59, DOI 10.1016/j.pbiomolbio.2012.09.004
   Nührenberg TG, 2013, J CARDIOVASC TRANSL, V6, P81, DOI 10.1007/s12265-012-9420-5
   Ooi CH, 2003, BIOINFORMATICS, V19, P37, DOI 10.1093/bioinformatics/19.1.37
   Pan Q, 2008, NAT GENET, V40, P1413, DOI 10.1038/ng.259
   Papait R, 2013, J CARDIOVASC TRANSL, V6, P876, DOI 10.1007/s12265-013-9488-6
   PASIPOULARIDES A, 1987, CIRC RES, V61, P220, DOI 10.1161/01.RES.61.2.220
   PASIPOULARIDES A, 1986, CIRCULATION, V74, P991, DOI 10.1161/01.CIR.74.5.991
   PASIPOULARIDES A, 1984, AM J PHYSIOL, V246, pH542, DOI 10.1152/ajpheart.1984.246.4.H542
   Pasipoularides A, 2003, AM J PHYSIOL-HEART C, V285, pH1956, DOI 10.1152/ajpheart.00372.2003
   Pasipoularides A, 2003, AM J PHYSIOL-HEART C, V284, pH1064, DOI 10.1152/ajpheart.00804.2002
   PASIPOULARIDES A, 1990, J AM COLL CARDIOL, V15, P859, DOI 10.1016/0735-1097(90)90287-Y
   PASIPOULARIDES A, 1992, ANN BIOMED ENG, V20, P3, DOI 10.1007/BF02368503
   Pasipoularides A., 2011, AM SOC ECH 22 ANN SC
   Pasipoularides A, 2007, AM HEART J, V153, P4, DOI 10.1016/j.ahj.2006.10.035
   Pasipoularides A, 2015, J CARDIOVASC TRANSL, V8, P293, DOI 10.1007/s12265-015-9630-8
   Pasipoularides A, 2015, J CARDIOVASC TRANSL, V8, P76, DOI 10.1007/s12265-015-9611-y
   Pasipoularides A, 2015, HELL J CARDIOL, V56, P85
   Pasipoularides A, 2014, INT J CARDIOL, V172, P47, DOI 10.1016/j.ijcard.2013.12.166
   Pasipoularides A, 2014, INT J CARDIOL, V171, P103, DOI 10.1016/j.ijcard.2013.11.133
   Pasipoularides A, 2013, INT J CARDIOL, V168, P3173, DOI 10.1016/j.ijcard.2013.07.253
   Pasipoularides A, 2013, J CARDIOVASC TRANSL, V6, P623, DOI 10.1007/s12265-013-9461-4
   Pasipoularides A, 2013, J APPL PHYSIOL, V114, P1493, DOI 10.1152/japplphysiol.00216.2013
   Pasipoularides A, 2013, REV ESP CARDIOL, V66, P337, DOI 10.1016/j.rec.2012.07.011
   Pasipoularides A, 2013, J CARDIOVASC TRANSL, V6, P239, DOI 10.1007/s12265-012-9424-1
   Pasipoularides A, 2012, HELL J CARDIOL, V53, P458
   Pasipoularides A, 2011, AM HEART J, V162, DOI 10.1016/j.ahj.2011.08.019
   Pasipoularides A, 2011, HELL J CARDIOL, V52, P416
   Pasipoularides Ares., 2010, The Heart's Vortex: Intracardiac Blood Flow Phenomena
   Pennisi E, 2012, SCIENCE, V337, P1159, DOI 10.1126/science.337.6099.1159
   Phillips PC, 2008, NAT REV GENET, V9, P855, DOI 10.1038/nrg2452
   Pontes B, 2015, J BIOMED INFORM, V57, P163, DOI 10.1016/j.jbi.2015.06.028
   Pontes B, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0115497
   Rao DC, 2008, ADV GENET, V60, P3, DOI 10.1016/S0065-2660(07)00401-4
   Rasmussen LV, 2014, J CARDIOVASC TRANSL, V7, P607, DOI 10.1007/s12265-014-9579-z
   Risch NJ, 2000, NATURE, V405, P847, DOI 10.1038/35015718
   Robinson P, 2007, CIRC RES, V101, P1266, DOI 10.1161/CIRCRESAHA.107.156380
   Rosendaal FR, 1999, LANCET, V353, P1167, DOI 10.1016/S0140-6736(98)10266-0
   Sakharkar Meena Kishore, 2004, In Silico Biology, V4, P387
   Schmitt T, 2014, NUCLEIC ACIDS RES, V42, pD380, DOI 10.1093/nar/gkt984
   Shannon P, 2003, GENOME RES, V13, P2498, DOI 10.1101/gr.1239303
   SHIM Y, 1992, CIRC RES, V71, P1174, DOI 10.1161/01.RES.71.5.1174
   Solovieff N, 2013, NAT REV GENET, V14, P483, DOI 10.1038/nrg3461
   Stearns FW, 2010, GENETICS, V186, P767, DOI 10.1534/genetics.110.122549
   Steinberg M., 2001, DISORDERS HEMOGLOBIN
   Sturm Amy Curry, 2013, Curr Heart Fail Rep, V10, P63, DOI 10.1007/s11897-012-0124-6
   Su ZQ, 2011, EXPERT REV MOL DIAGN, V11, P333, DOI [10.1586/erm.11.3, 10.1586/ERM.11.3]
   Tarasov Kirill V, 2007, Methods Mol Biol, V366, P41
   Teekakirikul P, 2013, J MOL DIAGN, V15, P158, DOI 10.1016/j.jmoldx.2012.09.002
   Terwilliger JD, 2006, EUR J HUM GENET, V14, P426, DOI 10.1038/sj.ejhg.5201583
   Thurman RE, 2012, NATURE, V489, P75, DOI 10.1038/nature11232
   van Berlo JH, 2013, J CLIN INVEST, V123, P37, DOI 10.1172/JCI62839
   Venter JC, 2001, SCIENCE, V291, P1304, DOI 10.1126/science.1058040
   Wakabayashi I, 2013, INTERDISCIPLINARY CO, VI
   Wallace Bruce., 1992, SEARCH GENE
   Wang ET, 2008, NATURE, V456, P470, DOI 10.1038/nature07509
   Ware JS, 2013, J CARDIOVASC TRANSL, V6, P94, DOI 10.1007/s12265-012-9401-8
   Watson JamesD., 1992, Recombinant DNA, V9th
   Weeland CJ, 2015, J MOL CELL CARDIOL, V81, P107, DOI 10.1016/j.yjmcc.2015.02.008
   Weiner RB, 2014, EXPERT REV CARDIOVAS, V12, P1243, DOI 10.1586/14779072.2014.970178
   Wheeler MT, 2008, J CARDIOVASC TRANSL, V1, P25, DOI 10.1007/s12265-007-9007-8
NR 150
TC 22
Z9 22
U1 0
U2 15
PU SPRINGER
PI NEW YORK
PA 233 SPRING ST, NEW YORK, NY 10013 USA
SN 1937-5387
EI 1937-5395
J9 J CARDIOVASC TRANSL
JI J. Cardiovasc. Transl. Res.
PD DEC
PY 2015
VL 8
IS 9
BP 506
EP 527
DI 10.1007/s12265-015-9658-9
PG 22
WC Cardiac & Cardiovascular Systems; Medicine, Research & Experimental
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology; Research & Experimental Medicine
GA CY0NH
UT WOS:000366102300002
PM 26545598
OA Green Accepted
DA 2025-04-10
ER

PT J
AU DeKryger, W
   Chroneos, ZC
AF DeKryger, William
   Chroneos, Zissis C.
TI Emerging concepts of myosin 18A isoform mechanobiology in organismal and
   immune system physiology, development, and function
SO FASEB JOURNAL
LA English
DT Review
ID INTERACTING EXCHANGE FACTOR; PDZ-CONTAINING MYOSIN; BETA-PIX; F-ACTIN;
   PROTEIN; MYO18A; IDENTIFICATION; GOLGI; GOLPH3; RECEPTOR
AB Alternative and combinatorial splicing of myosin 18A (MYO18A) gene transcripts results in expression of MYO18A protein isoforms and isoform variants with different membrane and subcellular localizations, and functional properties. MYO18A proteins are members of the myosin superfamily consisting of a myosin-like motor domain, an IQ motif, and a coiled-coil domain. MYO18A isoforms, however, lack the ability to hydrolyze ATP and do not perform ATP-dependent motor activity. MYO18A isoforms are distinguished by different amino- and carboxy-terminal extensions and domains. The domain organization and functions of MYO18A alpha, MYO18A beta, and MYO18A gamma have been studied experimentally. MYO18A alpha and MYO18A beta have a common carboxy-terminal extension but differ by the presence or absence of an amino-terminal KE repeat and PDZ domain, respectively. The amino- and carboxy-terminal extensions of MYO18A gamma contain unique proline and serine-rich domains. Computationally predicted MYO18A epsilon and MYO18A delta isoforms contain the carboxy-terminal serine-rich extension but differ by the presence or absence of the amino-terminal KE/PDZ extension. Additional isoform variants within each category arise by alternative utilization or inclusion/exclusion of small exons. MYO18A alpha variants are expressed in somatic cells and mature immune cells, whereas MYO18A beta variants occur mainly in myeloid and natural killer cells. MYO18A gamma expression is selective to cardiac and skeletal muscle. In the present review perspective, we discuss current and emerging concepts of the functional specialization of MYO18A proteins in membrane and cytoskeletal dynamics, cellular communication and signaling, endocytic and exocytic organelle movement, viral infection, and as the SP-R210 receptor for surfactant protein A.
C1 [DeKryger, William; Chroneos, Zissis C.] Penn State Univ, Coll Med, Dept Pediat, Div Neonatal Perinatal Med Pulm Immunol & Physiol, Hershey, PA 17036 USA.
   [Chroneos, Zissis C.] Penn State Univ, Coll Med, Dept Microbiol & Immunol, Hershey, PA USA.
C3 Pennsylvania Commonwealth System of Higher Education (PCSHE);
   Pennsylvania State University; Penn State Health; Pennsylvania
   Commonwealth System of Higher Education (PCSHE); Pennsylvania State
   University; Penn State Health
RP Chroneos, ZC (corresponding author), Penn State Univ, Coll Med, Dept Pediat, Div Neonatal Perinatal Med Pulm Immunol & Physiol, Hershey, PA 17036 USA.
EM zchroneos@pennstatehealth.psu.edu
RI Chroneos, Zissis/CAA-4884-2022
OI , Zissis/0000-0002-9841-7917; DeKryger, William/0009-0007-0986-4912
FU Children's Miracle Network Hospitals (CMN)
FX None.
CR Alexander CJ, 2021, FASEB J, V35, DOI 10.1096/fj.202001449R
   Aydin B, 2019, FRONT ENDOCRINOL, V10, DOI 10.3389/fendo.2019.00361
   Beach JR, 2014, CURR BIOL, V24, P1160, DOI 10.1016/j.cub.2014.03.071
   Beltran PMJ, 2016, CELL SYST, V3, P361, DOI 10.1016/j.cels.2016.08.012
   Billington N, 2015, CURR BIOL, V25, P942, DOI 10.1016/j.cub.2015.02.012
   Bishé B, 2012, J BIOL CHEM, V287, P27637, DOI 10.1074/jbc.M112.346569
   Borron P, 1998, AM J PHYSIOL-LUNG C, V275, pL679, DOI 10.1152/ajplung.1998.275.4.L679
   Bruun K, 2017, CYTOSKELETON, V74, P205, DOI 10.1002/cm.21364
   Buschman Matthew D., 2018, Advances in Biological Regulation, V67, P84, DOI 10.1016/j.jbior.2017.09.005
   Cao C, 2021, GENES GENOM, V43, P371, DOI 10.1007/s13258-021-01037-8
   Cao JM, 2016, SCI REP-UK, V6, DOI 10.1038/srep36768
   Cao JM, 2014, J GENET GENOMICS, V41, P417, DOI 10.1016/j.jgg.2014.06.008
   Capponi S, 2020, RNA BIOL, V17, P62, DOI 10.1080/15476286.2019.1667214
   Chang JY, 2015, CELL DEATH DISCOV, V1, DOI 10.1038/cddiscovery.2015.3
   Chang JY, 2012, CELL DEATH DIS, V3, DOI 10.1038/cddis.2012.36
   Chang NS, 1998, BIOCHEM BIOPH RES CO, V253, P743, DOI 10.1006/bbrc.1998.9846
   Chatterjee P, 2023, J CELL SCI, V136, DOI 10.1242/jcs.261100
   Cheung MB, 2021, J IMMUNOL, V206, P2521, DOI 10.4049/jimmunol.2100084
   Chiritoiu-Butnaru M, 2022, FRONT CELL DEV BIOL, V10, DOI 10.3389/fcell.2022.1088002
   Chou PY, 2019, CELL COMMUN SIGNAL, V17, DOI 10.1186/s12964-019-0382-y
   Chroneos ZC, 1996, J BIOL CHEM, V271, P16375, DOI 10.1074/jbc.271.27.16375
   CHRONEOS ZC, 1995, ARCH BIOCHEM BIOPHYS, V319, P63, DOI 10.1006/abbi.1995.1267
   Cross M, 2004, BIOCHEM J, V380, P243, DOI 10.1042/BJ20031978
   De Masson A, 2016, ONCOIMMUNOLOGY, V5, DOI 10.1080/2162402X.2015.1127493
   Dippold HC, 2009, CELL, V139, P337, DOI 10.1016/j.cell.2009.07.052
   Dowhan W, 2009, ANNU REV BIOCHEM, V78, P515, DOI 10.1146/annurev.biochem.77.060806.091251
   Farber-Katz SE, 2014, CELL, V156, P413, DOI 10.1016/j.cell.2013.12.023
   Feng SH, 2022, IEEE ACM T COMPUT BI, V19, P795, DOI 10.1109/TCBB.2020.3029274
   Feng SH, 2020, J MOL BIOL, V432, P1279, DOI 10.1016/j.jmb.2019.12.007
   Filaquier A, 2022, CURR OPIN CELL BIOL, V75, DOI 10.1016/j.ceb.2022.02.006
   Fortin J, 2016, NAT MED, V22, P339, DOI 10.1038/nm.4083
   Furusawa T, 2000, BIOCHEM BIOPH RES CO, V270, P67, DOI 10.1006/bbrc.2000.2377
   Garcia-Fojeda B, 2022, FRONT IMMUNOL, V13, DOI 10.3389/fimmu.2022.860262
   Gardel ML, 2010, ANNU REV CELL DEV BI, V26, P315, DOI 10.1146/annurev.cellbio.011209.122036
   Guan ZW, 2024, AM J PHYSIOL-LUNG C, V326, pL508, DOI 10.1152/ajplung.00383.2023
   Guzik-Lendrum S, 2013, J BIOL CHEM, V288, P9532, DOI 10.1074/jbc.M112.441238
   Guzik-Lendrum S, 2011, J BIOL CHEM, V286, P21755, DOI 10.1074/jbc.M111.218669
   Hong Qunying, 2013, Transl Respir Med, V1, P5, DOI 10.1186/2213-0802-1-5
   Horsthemke M, 2019, J BIOL CHEM, V294, P7202, DOI 10.1074/jbc.RA118.004560
   Hsu RM, 2014, BBA-MOL CELL RES, V1843, P2513, DOI 10.1016/j.bbamcr.2014.06.023
   Hsu RM, 2010, MOL BIOL CELL, V21, P287, DOI 10.1091/mbc.E09-03-0232
   Isogawa Y, 2005, BIOCHEMISTRY-US, V44, P6190, DOI 10.1021/bi0475931
   Jenkinson S, 2016, LEUKEMIA, V30, P39, DOI 10.1038/leu.2015.206
   Ji HB, 2000, BIOCHEM BIOPH RES CO, V270, P267, DOI 10.1006/bbrc.2000.2413
   JONES DT, 1994, BIOCHEMISTRY-US, V33, P3038, DOI 10.1021/bi00176a037
   Kaufmann TL, 2020, PLOS COMPUT BIOL, V16, DOI 10.1371/journal.pcbi.1007801
   Koh CG, 2001, J CELL SCI, V114, P4239
   Kuo JC, 2011, NAT CELL BIOL, V13, P383, DOI 10.1038/ncb2216
   Langer W, 2010, BMC GENOMICS, V11, DOI 10.1186/1471-2164-11-676
   Latham SL, 2020, CELL REP, V32, DOI 10.1016/j.celrep.2020.108090
   Lee MH, 2010, CELL DEATH DIS, V1, DOI 10.1038/cddis.2010.83
   Li JT, 2021, BIOLOGY-BASEL, V10, DOI 10.3390/biology10121337
   Lin PC, 2020, FRONT ONCOL, V10, DOI 10.3389/fonc.2020.588557
   Lin YH, 2022, INT J MOL SCI, V23, DOI 10.3390/ijms232314510
   Liu JL, 2022, CELL DEATH DIFFER, V29, P818, DOI 10.1038/s41418-021-00897-7
   López-Sánchez A, 2011, EUR J PHARM BIOPHARM, V77, P384, DOI 10.1016/j.ejpb.2010.12.013
   Ma XF, 2012, P NATL ACAD SCI USA, V109, P4509, DOI 10.1073/pnas.1116268109
   Madar IH, 2021, BIOINFORMATION, V17, P348, DOI 10.6026/97320630017348
   Madeira F, 2022, NUCLEIC ACIDS RES, V50, pW276, DOI 10.1093/nar/gkac240
   Majewska H, 2021, VIRCHOWS ARCH, V478, P933, DOI 10.1007/s00428-020-02971-w
   Makowska KA, 2015, CELL REP, V13, P2118, DOI 10.1016/j.celrep.2015.11.012
   Manabe R, 2002, J CELL SCI, V115, P1497
   Martelli AM, 2019, CANCERS, V11, DOI 10.3390/cancers11050629
   Martin FJ, 2023, NUCLEIC ACIDS RES, V51, pD933, DOI 10.1093/nar/gkac958
   Matsui K, 2011, J PROTEOME RES, V10, P3983, DOI 10.1021/pr200577d
   Minutti CM, 2017, SCIENCE, V356, P1076, DOI 10.1126/science.aaj2067
   Mitsuhashi A, 2013, AM J PATHOL, V182, P1843, DOI 10.1016/j.ajpath.2013.01.030
   Mori K, 2005, BIOCHEM BIOPH RES CO, V326, P491, DOI 10.1016/j.bbrc.2004.11.058
   Mori K, 2003, J BIOCHEM, V133, P405, DOI 10.1093/jb/mvg053
   Morotti A, 2015, HEMATOL REP, V7, P84, DOI 10.4081/hr.2015.6027
   Nalian A, 2019, FRONT IMMUNOL, V10, DOI 10.3389/fimmu.2019.02613
   Newman D, 2023, CELL REP, V42, DOI 10.1016/j.celrep.2023.113554
   Ng MM, 2013, MOL BIOL CELL, V24, P796, DOI 10.1091/mbc.E12-07-0525
   Ouyang ZH, 2021, FRONT CELL DEV BIOL, V9, DOI 10.3389/fcell.2021.632445
   Parada GE, 2021, GENOME BIOL, V22, DOI 10.1186/s13059-020-02246-2
   Rahajeng J, 2019, DEV CELL, V50, P573, DOI 10.1016/j.devcel.2019.05.038
   Ruge CA, 2016, MOL PHARMACEUT, V13, P4168, DOI 10.1021/acs.molpharmaceut.6b00773
   Samten B, 2008, J LEUKOCYTE BIOL, V84, P115, DOI 10.1189/jlb.1207835
   Schultz L, 2004, DNA CELL BIOL, V23, P67, DOI 10.1089/104454904322745943
   Sever-Chroneos Z, 2011, J BIOL CHEM, V286, P4854, DOI 10.1074/jbc.M110.125567
   Sheng GY, 2017, MOL CYTOGENET, V10, DOI 10.1186/s13039-017-0306-8
   Straight AF, 2003, SCIENCE, V299, P1743, DOI 10.1126/science.1081412
   Szeliga J, 2005, ANAL BIOCHEM, V346, P179, DOI 10.1016/j.ab.2005.07.021
   Taft MH, 2020, ADV EXP MED BIOL, V1239, P421, DOI 10.1007/978-3-030-38062-5_19
   Taft MH, 2013, J BIOL CHEM, V288, P30029, DOI 10.1074/jbc.M113.497180
   Tan I, 2008, CELL, V135, P123, DOI 10.1016/j.cell.2008.09.018
   Tibarewal P., 2023, Adv Biol Regul, V2023
   Trost M, 2009, IMMUNITY, V30, P143, DOI 10.1016/j.immuni.2008.11.006
   Ussowicz M, 2012, CANCER GENET-NY, V205, P261, DOI 10.1016/j.cancergen.2012.02.006
   Vicente-Manzanares M, 2009, NAT REV MOL CELL BIO, V10, P778, DOI 10.1038/nrm2786
   Walz C, 2005, LEUKEMIA, V19, P1005, DOI 10.1038/sj.leu.2403712
   Waz C, 2009, GENE CHROMOSOME CANC, V48, P179, DOI 10.1002/gcc.20629
   Weikert LF, 2000, AM J PHYSIOL-LUNG C, V279, pL216, DOI 10.1152/ajplung.2000.279.2.L216
   Weikert LF, 1997, AM J PHYSIOL-LUNG C, V272, pL989, DOI 10.1152/ajplung.1997.272.5.L989
   Xing MK, 2016, MOL BIOL CELL, V27, P3828, DOI 10.1091/mbc.E16-01-0005
   Xu ZH, 2023, CELL REP, V42, DOI 10.1016/j.celrep.2023.112967
   Yang CH, 2005, J BIOL CHEM, V280, P34447, DOI 10.1074/jbc.M505229200
   Yang L, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0126576
   Yang Q., 2023, Biochim Biophys Acta Mol Cell Res, V1871
   Yau E., 2023, Microbes Infect, V26
   Yau E, 2023, FRONT IMMUNOL, V14, DOI 10.3389/fimmu.2023.919800
   Yau E, 2021, IMMUNOBIOLOGY, V226, DOI 10.1016/j.imbio.2021.152150
   Yehia L, 2020, ANNU REV MED, V71, P103, DOI 10.1146/annurev-med-052218-125823
   Zhang HJ, 2018, CSH MOL CASE STUD, V4, DOI 10.1101/mcs.a003079
NR 104
TC 0
Z9 0
U1 0
U2 4
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0892-6638
EI 1530-6860
J9 FASEB J
JI Faseb J.
PD MAY 31
PY 2024
VL 38
IS 10
AR e23649
DI 10.1096/fj.202400350R
PG 13
WC Biochemistry & Molecular Biology; Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Life Sciences & Biomedicine - Other
   Topics; Cell Biology
GA RQ0C2
UT WOS:001228997900001
PM 38776246
OA hybrid
DA 2025-04-10
ER

PT J
AU Feriotto, G
   Finotti, A
   Volpe, P
   Treves, S
   Ferrari, S
   Angelelli, C
   Zorzato, F
   Gambari, R
AF Feriotto, G
   Finotti, A
   Volpe, P
   Treves, S
   Ferrari, S
   Angelelli, C
   Zorzato, F
   Gambari, R
TI Myocyte enhancer factor 2 activates promoter sequences of the human
   AβH-J-J locus, encoding aspartyl-β-hydroxylase, junctin, and junctate
SO MOLECULAR AND CELLULAR BIOLOGY
LA English
DT Article
ID MEF2 TRANSCRIPTION FACTOR; PROTEIN-PROTEIN INTERACTIONS; MUSCLE-SPECIFIC
   ENHANCER; SKELETAL-MUSCLE; BINDING-SITES; MYOGENIC DIFFERENTIATION;
   RHABDOMYOSARCOMA CELLS; SARCOPLASMIC-RETICULUM; ALTERNATIVE PROMOTERS;
   CARDIAC-HYPERTROPHY
AB Alternative splicing of the locus A beta H-J-J generates three functionally distinct proteins: an enzyme, A beta H (aspartyl-beta-hydroxylase), a structural protein of the sarcoplasmic reticulum membrane (junctin), and an integral membrane calcium binding protein (junctate). Junctin and junctate are two important proteins involved in calcium regulation in eukaryotic cells. To understand the regulation of these two proteins, we identified and functionally characterized one of the two promoter sequences of the A beta H-J-J locus. We demonstrate that the P2 promoter of the A beta H-J-J locus contains (i) a minimal sequence localized within a region -159 bp from the transcription initiation site, which is sufficient to activate transcription of both mRNAs; (ii) sequences which bind known transcriptional factors such as those belonging to the myocyte enhancer factor 2 (MEF-2), MEF-3, and NF-kappa B protein families; and (iii) sequences bound by unknown proteins. The functional characterization of the minimal promoter in C2C12 cells and in the rat solleus muscle in vivo model indicates the existence of cis elements having positive and negative effects on transcription. In addition, our data demonstrate that in striated muscle cells the calcium-dependent transcription factor MEF-2 is crucial for the transcription activity directed by the P2 promoter. The transcription directed by the A beta H-J-J P2 promoter is induced by high expression of MEF-2, further stimulated by calcineurin and Ca2(+)/calmodulin-dependent protein kinase I, and inhibited by histone deacetylase 4.
C1 Univ Ferrara, Dept Biochem & Mol Biol, Ctr Biotechnol, Mol Biol Sect, I-44100 Ferrara, Italy.
   Univ Ferrara, Dept Expt & Diagnost Med, Sect Gen Pathol, I-44100 Ferrara, Italy.
   Univ Padua, Dept BIomed Expt Sci, Padua, Italy.
   Univ Modena & Reggio Emilia, Dept Biomed Sci, Modena, Italy.
   Kantonsspital, Dept Anaesthesia, CH-4031 Basel, Switzerland.
   Kantonsspital, Dept Res, CH-4031 Basel, Switzerland.
C3 University of Ferrara; University of Ferrara; University of Padua;
   Universita di Modena e Reggio Emilia; Kantonsspital Aarau AG (KSA);
   University of Basel; Kantonsspital Aarau AG (KSA); University of Basel
RP Univ Ferrara, Dept Biochem & Mol Biol, Ctr Biotechnol, Mol Biol Sect, Via Borsari 46, I-44100 Ferrara, Italy.
EM gam@unife.it
RI Finotti, Alessia/C-6268-2012; Gambari, Roberto/F-9555-2015
OI Finotti, Alessia/0000-0002-7638-515X; Treves, Susan/0000-0002-0007-9631;
   Gambari, Roberto/0000-0001-9205-6033
FU Telethon [GP0210Y01] Funding Source: Medline
CR Alway SE, 2002, AM J PHYSIOL-CELL PH, V283, pC66, DOI 10.1152/ajpcell.00598.2001
   Ayoubi TAY, 1996, FASEB J, V10, P453, DOI 10.1096/fasebj.10.4.8647344
   Berezikov E, 2004, GENOME RES, V14, P170
   BLACK BL, 1995, J BIOL CHEM, V270, P2889, DOI 10.1074/jbc.270.7.2889
   Blanchette M, 2002, GENOME RES, V12, P739, DOI 10.1101/gr.6902
   Blough E, 1999, BIOTECHNIQUES, V26, P202, DOI 10.2144/99262bm05
   Borgatti M, 2003, J BIOL CHEM, V278, P7500, DOI 10.1074/jbc.M206780200
   CAIRNS W, 1991, J BIOL CHEM, V266, P11221
   Chen SL, 2001, MOL ENDOCRINOL, V15, P783, DOI 10.1210/me.15.5.783
   DECHESNE CA, 1994, MOL CELL BIOL, V14, P5474, DOI 10.1128/MCB.14.8.5474
   Dinchuk JE, 2000, J BIOL CHEM, V275, P39543, DOI 10.1074/jbc.M006753200
   EISENBERG BR, 1985, J EXP BIOL, V115, P55
   Engelhardt S, 2001, FASEB J, V15, P2718, DOI 10.1096/fj.01-0107fje
   Esser K, 1999, J BIOL CHEM, V274, P12095, DOI 10.1074/jbc.274.17.12095
   FEO S, 1995, MOL CELL BIOL, V15, P5991
   FERIOTTO G, 1995, NUCLEIC ACIDS RES, V23, P1671, DOI 10.1093/nar/23.10.1671
   Friday BB, 2003, DIFFERENTIATION, V71, P217, DOI 10.1046/j.1432-0436.2003.710303.x
   Glover L, 2002, EUR J BIOCHEM, V269, P4607, DOI 10.1046/j.1432-1033.2002.03160.x
   GOSSETT LA, 1989, MOL CELL BIOL, V9, P5022, DOI 10.1128/MCB.9.11.5022
   Grayson J, 1998, J CELL BIOCHEM, V70, P366, DOI 10.1002/(SICI)1097-4644(19980901)70:3<366::AID-JCB10>3.3.CO;2-T
   Groh S, 1999, J BIOL CHEM, V274, P12278, DOI 10.1074/jbc.274.18.12278
   GUNDERSEN K, 1994, P NATL ACAD SCI USA, V91, P3647, DOI 10.1073/pnas.91.9.3647
   Han AD, 2003, NATURE, V422, P730, DOI 10.1038/nature01555
   Himeda CL, 2004, MOL CELL BIOL, V24, P2132, DOI 10.1128/MCB.24.5.2132-2143.2004
   Hong CS, 2001, BIOCHEM BIOPH RES CO, V289, P882, DOI 10.1006/bbrc.2001.6056
   HORLICK RA, 1989, MOL CELL BIOL, V9, P2396, DOI 10.1128/MCB.9.6.2396
   Hsu DKW, 1996, J BIOL CHEM, V271, P13786, DOI 10.1074/jbc.271.23.13786
   Kageyama K, 2002, J BIOL CHEM, V277, P19255, DOI 10.1074/jbc.M112377200
   Kane CD, 2000, EMBO J, V19, P691, DOI 10.1093/emboj/19.4.691
   KURABAYASHI M, 1993, J BIOL CHEM, V268, P5524
   Landry JR, 2003, TRENDS GENET, V19, P640, DOI 10.1016/j.tig.2003.09.014
   Lim HW, 1999, NAT MED, V5, P246, DOI 10.1038/6430
   Lu JR, 2000, P NATL ACAD SCI USA, V97, P4070, DOI 10.1073/pnas.080064097
   Luo DC, 2002, J BIOL CHEM, V277, P25527, DOI 10.1074/jbc.M202494200
   Mackrill JJ, 1999, BIOCHEM J, V337, P345, DOI 10.1042/0264-6021:3370345
   Mathiesen I, 1999, GENE THER, V6, P508, DOI 10.1038/sj.gt.3300847
   McKinsey TA, 2002, TRENDS BIOCHEM SCI, V27, P40, DOI 10.1016/S0968-0004(01)02031-X
   Meshorer E, 2004, J BIOL CHEM, V279, P29740, DOI 10.1074/jbc.M402752200
   Mickelson JR, 1996, PHYSIOL REV, V76, P537, DOI 10.1152/physrev.1996.76.2.537
   Mir LM, 1999, P NATL ACAD SCI USA, V96, P4262, DOI 10.1073/pnas.96.8.4262
   Mischiati C, 2000, J VIROL, V74, P8989, DOI 10.1128/JVI.74.19.8989-9001.2000
   Mischiati C, 1999, J BIOL CHEM, V274, P33114, DOI 10.1074/jbc.274.46.33114
   Miska EA, 1999, EMBO J, V18, P5099, DOI 10.1093/emboj/18.18.5099
   Mitchell-Felton H, 2000, J BIOL CHEM, V275, P23005, DOI 10.1074/jbc.M003678200
   Molkentin JD, 1998, CELL, V93, P215, DOI 10.1016/S0092-8674(00)81573-1
   Musarò A, 1999, NATURE, V400, P581, DOI 10.1038/23060
   Nagamura-Inoue T, 2001, Int Rev Immunol, V20, P83, DOI 10.3109/08830180109056724
   NORI A, 2003, BIOCHEM J, V370, P373
   Ostrovsky O, 2002, J BIOL CHEM, V277, P40043, DOI 10.1074/jbc.M205494200
   PARMACEK MS, 1994, MOL CELL BIOL, V14, P1870, DOI 10.1128/MCB.14.3.1870
   Passier R, 2000, J CLIN INVEST, V105, P1395, DOI 10.1172/JCI8551
   PINSET C, 1988, DIFFERENTIATION, V38, P28, DOI 10.1111/j.1432-0436.1988.tb00588.x
   Relaix F, 1998, NAT GENET, V18, P287, DOI 10.1038/ng0398-287
   SALVATORI S, 1988, MUSCLE NERVE, V11, P1246, DOI 10.1002/mus.880111209
   Selman C, 2003, AM J PHYSIOL-REG I, V284, pR538, DOI 10.1152/ajpregu.00679.2002
   Spitz F, 1998, P NATL ACAD SCI USA, V95, P14220, DOI 10.1073/pnas.95.24.14220
   SUWANICHKUL A, 1990, J BIOL CHEM, V265, P21185
   Takekura H, 1996, J MUSCLE RES CELL M, V17, P391, DOI 10.1007/BF00123356
   Tasic B, 2002, MOL CELL, V10, P21, DOI 10.1016/S1097-2765(02)00578-6
   Treves S, 2004, J CELL BIOL, V166, P537, DOI 10.1083/jcb.200404079
   Treves S, 2000, J BIOL CHEM, V275, P39555, DOI 10.1074/jbc.M005473200
   Wang JK, 2003, ANAL BIOCHEM, V316, P192, DOI 10.1016/S0003-2697(03)00049-6
   Wang XZ, 2002, GENE DEV, V16, P1890, DOI 10.1101/gad.1004802
   Weng L, 2003, J BIOL CHEM, V278, P19164, DOI 10.1074/jbc.M300653200
   Wu H, 2000, EMBO J, V19, P1963, DOI 10.1093/emboj/19.9.1963
   Xie GX, 2003, J MOL BIOL, V325, P721, DOI 10.1016/S0022-2836(02)01283-4
   Xue LX, 2004, FEBS LETT, V564, P199, DOI 10.1016/S0014-5793(04)00352-7
   YU YT, 1992, GENE DEV, V6, P1783, DOI 10.1101/gad.6.9.1783
   Zhang L, 1997, J BIOL CHEM, V272, P23389, DOI 10.1074/jbc.272.37.23389
   Zhu BM, 2004, MOL CELL BIOL, V24, P8264, DOI 10.1128/MCB.24.18.8264-8275.2004
NR 70
TC 13
Z9 15
U1 0
U2 1
PU AMER SOC MICROBIOLOGY
PI WASHINGTON
PA 1752 N ST NW, WASHINGTON, DC 20036-2904 USA
SN 0270-7306
EI 1098-5549
J9 MOL CELL BIOL
JI Mol. Cell. Biol.
PD APR
PY 2005
VL 25
IS 8
BP 3261
EP 3275
DI 10.1128/MCB.25.8.3261-3275.2005
PG 15
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA 913GB
UT WOS:000228138500033
PM 15798210
OA Green Published, Green Accepted
DA 2025-04-10
ER

PT J
AU Mittmann, C
   Schüler, C
   Chung, CH
   Höppner, G
   Nose, M
   Kehrl, JH
   Wieland, T
AF Mittmann, C
   Schüler, C
   Chung, CH
   Höppner, G
   Nose, M
   Kehrl, JH
   Wieland, T
TI Evidence for a short form of RGS3 preferentially expressed in the human
   heart
SO NAUNYN-SCHMIEDEBERGS ARCHIVES OF PHARMACOLOGY
LA English
DT Article
DE RGS protein; G protein; human heart
ID PROTEIN ALPHA-SUBUNITS; SACCHAROMYCES-CEREVISIAE; ADENYLATE-CYCLASE;
   DILATED CARDIOMYOPATHY; FACTOR PHEROMONES; PHOSPHOLIPASE-C; G1 ARREST;
   A-FACTOR; REGULATORS; MEMBRANE
AB RGS proteins (regulators of G protein signalling) negatively regulate G protein function as GTPase-activating proteins (GAP) for G protein alpha -subunits. The existence of mRNAs of different size for some of the RGS proteins, e.g. RGS3, suggests that these proteins may exist in isoforms due to alternative splicing. We therefore investigated RGS3 mRNA and protein expression in different human tissues. Ribonuclease protection assays and Northern blot analysis showed two specific mRNAs for RGS3 (RGS3L, RGS3S) in human myocardium, suggesting an additional, N-terminally truncated form of approximately 168 aa. When expressed as a recombinant protein RGS3S was recognized at similar to 23 kDa by an antipeptide antiserum originally raised against an RGS2 sequence. In membranes of human tissues this antiserum detected specific signals for RGS3L (similar to 70 kDa), RGS2 (similar to 30 kDa) and a 25-kDa protein, most likely RGS3S. Both RGS3S mRNA and the 25 kDa protein were abundant in human heart, whereas expression in liver, brain and myometrium was much weaker. To characterize RGS3S functionally, single turnover GTPase, adenylyl cyclase (AC) and phospholipase C (PLC) activities were determined. Both recombinant RGS3S and RGS16 increased P-i release from G(alpha i1) by about 150% and increased GTP- and GTP plus isoprenaline-stimulated AC activity by 20-30% in human left ventricular myocardial membranes. Additionally, both RGS proteins reduced basal and endothelin-stimulated PLC activity in these membranes by about 40%.
   We conclude that an additional truncated form of RGS3 is expressed in the human heart. As described for the full-length protein, RGS3S negatively regulates the activity of G(i/o)- and G(q)-, but not G(s)-subfamily members.
C1 Univ Hamburg, Klinikum Eppendorf, Abt Pharmakol, Inst Expt & Klin Pharmakol & Toxikol, D-20246 Hamburg, Germany.
   NIAID, Immunoregulat Lab, NIH, Bethesda, MD 20892 USA.
C3 University of Hamburg; National Institutes of Health (NIH) - USA; NIH
   National Institute of Allergy & Infectious Diseases (NIAID)
RP Mittmann, C (corresponding author), Univ Hamburg, Klinikum Eppendorf, Abt Pharmakol, Inst Expt & Klin Pharmakol & Toxikol, Martinistr 52, D-20246 Hamburg, Germany.
RI Wieland, Thomas/Q-1506-2019; Kehrl, John/AAE-6292-2019
OI Wieland, Thomas/0000-0001-8262-8261; Kehrl, John/0000-0002-6526-159X
CR BOHM M, 1990, AM HEART J, V120, P1381, DOI 10.1016/0002-8703(90)90252-S
   BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
   CHAN RK, 1982, MOL CELL BIOL, V2, P21, DOI 10.1128/MCB.2.1.21
   CHAN RK, 1982, MOL CELL BIOL, V2, P11, DOI 10.1128/MCB.2.1.11
   Chatterjee TK, 1997, GENOMICS, V45, P429, DOI 10.1006/geno.1997.4929
   Chatterjee TK, 1997, J BIOL CHEM, V272, P15481, DOI 10.1074/jbc.272.24.15481
   Chen CK, 1996, P NATL ACAD SCI USA, V93, P12885, DOI 10.1073/pnas.93.23.12885
   CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
   DeVries L, 1996, P NATL ACAD SCI USA, V93, P15203, DOI 10.1073/pnas.93.26.15203
   Druey KM, 1996, NATURE, V379, P742, DOI 10.1038/379742a0
   Druey KM, 1999, J BIOL CHEM, V274, P18836, DOI 10.1074/jbc.274.26.18836
   Dulin NO, 1999, MOL CELL BIOL, V19, P714
   ESCHENHAGEN T, 1995, J MOL CELL CARDIOL, V27, P357, DOI 10.1016/S0022-2828(08)80033-8
   Gsell S, 2000, FASEB J, V14, P17, DOI 10.1096/fasebj.14.1.17
   JAKOBS KH, 1982, J BIOL CHEM, V257, P2829
   Koelle MR, 1996, CELL, V84, P115, DOI 10.1016/S0092-8674(00)80998-8
   MATTERA R, 1985, J BIOL CHEM, V260, P7410
   Mittmann C, 1998, J MOL MED, V76, P133, DOI 10.1007/s001090050201
   Natochin M, 1998, BIOCHEMISTRY-US, V37, P13776, DOI 10.1021/bi981155a
   Neill JD, 1997, ENDOCRINOLOGY, V138, P843, DOI 10.1210/en.138.2.843
   Salomon Y, 1979, Adv Cyclic Nucleotide Res, V10, P35
   Schmidt M, 1996, N-S ARCH PHARMACOL, V354, P87, DOI 10.1007/BF00178707
   Srinivasa SP, 1998, P NATL ACAD SCI USA, V95, P5584, DOI 10.1073/pnas.95.10.5584
   Watson N, 1996, NATURE, V383, P172, DOI 10.1038/383172a0
   Weil J, 1997, J MOL CELL CARDIOL, V29, P743, DOI 10.1006/jmcc.1996.0318
   Wieland T, 2000, J BIOL CHEM, V275, P28500, DOI 10.1074/jbc.M004187200
   Wieland T, 1999, N-S ARCH PHARMACOL, V360, P14, DOI 10.1007/s002109900031
   Xu X, 1999, J BIOL CHEM, V274, P3549, DOI 10.1074/jbc.274.6.3549
   Zeng WZ, 1998, J BIOL CHEM, V273, P34687, DOI 10.1074/jbc.273.52.34687
NR 29
TC 19
Z9 22
U1 0
U2 0
PU SPRINGER-VERLAG
PI NEW YORK
PA 175 FIFTH AVE, NEW YORK, NY 10010 USA
SN 0028-1298
J9 N-S ARCH PHARMACOL
JI Naunyn-Schmiedebergs Arch. Pharmacol.
PD APR
PY 2001
VL 363
IS 4
BP 456
EP 463
PG 8
WC Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Pharmacology & Pharmacy
GA 413XD
UT WOS:000167636100012
PM 11330340
DA 2025-04-10
ER

PT J
AU Mannila, MN
   Lovely, RS
   Kazmierczak, SC
   Eriksson, P
   Samnegård, A
   Farrell, DH
   Hamsten, A
   Silveira, A
AF Mannila, M. N.
   Lovely, R. S.
   Kazmierczak, S. C.
   Eriksson, P.
   Samnegard, A.
   Farrell, D. H.
   Hamsten, A.
   Silveira, A.
TI Elevated plasma fibrinogen γ′ concentration is associated with
   myocardial infarction:: effects of variation in fibrinogen genes and
   environmental factors
SO JOURNAL OF THROMBOSIS AND HAEMOSTASIS
LA English
DT Article
DE fibrinogen gamma '; fibrinogen polymorphisms; interaction; myocardial
   infarction
ID VARIANT GAMMA'; SPLICE VARIANT; CHAIN; RISK; HYPOFIBRINOLYSIS;
   TRANSCRIPTION; FIBRINOLYSIS; ARCHITECTURE; DISEASE
AB Background: Fibrinogen gamma', a fibrinogen gamma-chain variant generated via alternative mRNA processing, has been associated with susceptibility to thrombotic disease. Objective: The present case-control study searched for potential determinants of the plasma fibrinogen gamma' concentration and examined the relationship between this variant and risk of myocardial infarction (MI). Patienst and methods: The Stockholm Coronary Artery Risk Factor study, comprising 387 postinfarction patients and 387 healthy individuals, was employed. The fibrinogen gamma (FGG) 9340T > C [rs1049636], fibrinogen alpha (FGA) 2224G > A [rs2070011] and fibrinogen beta (FGB) 1038G > A [rs1800791] polymorphisms were determined. The plasma fibrinogen gamma' concentration was measured by enzyme-linked immunosorbent assay. The multifactor dimensionality reduction method was used for interaction analyses on risk of MI. Results: The FGG 9340T > C and FGA 2224G > A polymorphisms, total plasma concentrations of fibrinogen, insulin and high-density lipoprotein, and gender appeared to be independent determinants of plasma fibrinogen gamma' concentration in patients, and the corresponding determinants in controls included FGG 9340T > C and FGA 2224G > A polymorphisms and plasma fibrinogen concentration. An elevated plasma fibrinogen gamma' concentration proved to be an independent predictor of MI [adjusted odds ratio (OR) (95% CI): 1.24 (1.01, 1.52)]. The plasma fibrinogen gamma' concentration was involved in a high-order interaction with total plasma fibrinogen and the FGG 9340T > C and FGA 2224G > A polymorphisms, associated with a further increased risk of MI [OR (95% CI): 3.22 (2.35, 4.39)]. Conclusions: Plasma fibrinogen gamma' concentration influences the risk of MI, and this relationship seems to be strengthened by the presence of an elevated total plasma fibrinogen concentration and the FGG 9340T and FGA 2224G alleles.
C1 Karolinska Inst, King Gustaf V Res Inst, Atherosclerosis Res Unit, Dept Med, Solna, Sweden.
   Oregon Hlth & Sci Univ, Dept Pathol, Portland, OR USA.
   Danderyd Hosp, Dept Med, Cardiol Unit, Stockholm, Sweden.
   Karolinska Univ Hosp, Dept Cardiol, Solna, Sweden.
C3 Karolinska Institutet; Oregon Health & Science University; Danderyds
   Hospital; Karolinska Institutet; Karolinska University Hospital
RP Mannila, MN (corresponding author), Karolinska Univ Hosp, King Gustaf V Res Inst, S-17176 Stockholm, Sweden.
EM maria.nastase.mannila@ki.se
RI Kazmierczak, Steven/A-4839-2011
OI Silveira, Angela/0000-0003-2063-4935
FU NHLBI NIH HHS [1 R21 HL75006] Funding Source: Medline
CR Bai YD, 1999, NUCLEIC ACIDS RES, V27, P1126, DOI 10.1093/nar/27.4.1126
   BLAND M, 2000, INTRO MED STAT, P272
   BLOMBACK B, 1994, THROMB RES, V75, P521, DOI 10.1016/0049-3848(94)90227-5
   Carlson K, 1973, J Clin Pathol Suppl (Assoc Clin Pathol), V5, P32
   CHUNG DW, 1984, BIOCHEMISTRY-US, V23, P4232, DOI 10.1021/bi00313a033
   CLAUSS A., 1957, ACTA HAEMATOL, V17, P237
   Collet JP, 2006, ARTERIOSCL THROM VAS, V26, P2567, DOI 10.1161/01.ATV.0000241589.52950.4c
   COLLET JP, 1993, BLOOD, V82, P2462
   Collet JP, 2004, ARTERIOSCL THROM VAS, V24, P382, DOI 10.1161/01.ATV.0000109748.77727.3e
   Cooper AV, 2003, BLOOD, V102, P535, DOI 10.1182/blood-2002-10-3150
   CRABTREE GR, 1982, CELL, V31, P159, DOI 10.1016/0092-8674(82)90415-9
   de Willige SU, 2005, BLOOD, V106, P4176, DOI 10.1182/blood-2005-05-2180
   DROUET L, 1999, BLOOD COAGUL FIBRI S, V10, P35
   Falls LA, 1997, J BIOL CHEM, V272, P14251, DOI 10.1074/jbc.272.22.14251
   FATAH K, 1992, THROMB HAEMOSTASIS, V68, P130
   Fatah K, 1996, THROMB HAEMOSTASIS, V76, P535
   FORNACE AJ, 1984, J BIOL CHEM, V259, P2826
   Hahn LW, 2003, BIOINFORMATICS, V19, P376, DOI 10.1093/bioinformatics/btf869
   Lim BCB, 2003, LANCET, V361, P1424, DOI 10.1016/S0140-6736(03)13135-2
   Lovely RS, 2002, THROMB HAEMOSTASIS, V88, P26
   Mannila MN, 2005, THROMB HAEMOSTASIS, V93, P570, DOI 10.1160/TH04-10-0698
   MIZUGUCHI J, 1995, J BIOL CHEM, V270, P28350
   MOSESSON MW, 1972, J BIOL CHEM, V247, P5223
   OTTO JM, 1987, J CELL BIOL, V105, P1067, DOI 10.1083/jcb.105.3.1067
   Pastinen T, 2004, SCIENCE, V306, P647, DOI 10.1126/science.1101659
   Proudfoot NJ, 2002, CELL, V108, P501, DOI 10.1016/S0092-8674(02)00617-7
   Siebenlist KR, 2005, BLOOD, V106, P2730, DOI 10.1182/blood-2005-01-0240
   WOLFENSTEINTODEL C, 1980, P NATL ACAD SCI-BIOL, V77, P5069, DOI 10.1073/pnas.77.9.5069
NR 28
TC 84
Z9 93
U1 1
U2 6
PU BLACKWELL PUBLISHING
PI OXFORD
PA 9600 GARSINGTON RD, OXFORD OX4 2DQ, OXON, ENGLAND
SN 1538-7933
J9 J THROMB HAEMOST
JI J. Thromb. Haemost.
PD APR
PY 2007
VL 5
IS 4
BP 766
EP 773
DI 10.1111/j.1538-7836.2007.02406.x
PG 8
WC Hematology; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Hematology; Cardiovascular System & Cardiology
GA 153DR
UT WOS:000245412400015
PM 17263791
OA Bronze
DA 2025-04-10
ER

PT J
AU Jaén, C
   Doupnik, CA
AF Jaén, C
   Doupnik, CA
TI Neuronal Kir3.1/Kir302a channels coupled to serotonin 1A and muscarinic
   m2 receptors are differentially modulated by the 'short' RGS3 isoform
SO NEUROPHARMACOLOGY
LA English
DT Article
DE inward rectifier potassium channels; G protein coupled receptors;
   regulators of G protein signaling; acetylcholine; serotonin; patch
   clamp; Chinese hamster ovary cells
ID PROTEIN SIGNALING RGS; RECTIFIER K+ CHANNELS; ADENYLYL-CYCLASE;
   ALPHA-SUBUNITS; SUBCELLULAR-LOCALIZATION; ACUTE DESENSITIZATION;
   POTASSIUM CHANNELS; KINASE ACTIVATION; DISTINCT DOMAINS;
   TRANSITION-STATE
AB 'Regulators of G protein signaling' (RGS proteins) have profound effects on ion channels regulated by G protein-coupled receptor (GPCR) signaling, including the G protein-gated inwardly rectifying K+ (GIRK) channels that inhibit excitability of neuronal, endocrine, and cardiac cells. Here we describe the effects of an alternatively spliced 'short' RGS3 isoform (RGS3s) in comparison to RGS4, on the temporal and steady-state gating properties of neuronal GIRK channels (Kir3.1/Kir3.2a) activated by either serotonin 1A (5-HT1A) receptors or muscarinic m2 receptors expressed in Chinese hamster ovary (CHO-K1) cells. RGS3s is abundantly expressed in brain and contains a unique short N-terminus via alternative splicing that distinguishes it from other RGS3 isoforms as well as other members of the B/R4 RGS gene subfamily. Our results indicate that RGS3s and RGS4 similarly affect the temporal and steady-state gating properties of 5-HT1A receptor-coupled Kir3.1/Kir3.2a channels, but differentially modulate muscarinic m2 receptor-coupled channels. RGS3s caused a significant similar to 45% reduction in the maximal acetylcholine (ACh)-evoked GIRK current amplitude and a marked shift in the steady-state ACh dose-response relation indicative of a reduction in functionally coupled m2 receptor-GIRK channel complexes. Yet RGS3s still accelerated the m2 receptor-dependent GIRK activation, deactivation, and acute desensitization time course consistent with the RGS-enhanced GAP activity that was also observed with RGS4. Several mechanisms that may contribute to the receptor-dependent effects of RGS3s are discussed with particular attention to the role of the distinct N-terminal domain. Our findings highlight the potential impact of selective RGS-GPCR interactions on neuronal GIRK channel function that may affect the properties of inhibitory postsynaptic potentials activated by different GPCR-GIRK channel complexes. (c) 2005 Elsevier Ltd. All rights reserved.
C1 Univ S Florida, Coll Med, Dept Physiol & Biophys, Tampa, FL 33612 USA.
C3 State University System of Florida; University of South Florida
RP Univ S Florida, Coll Med, Dept Physiol & Biophys, 12901 Bruce B Downs Blvd MDCS, Tampa, FL 33612 USA.
EM cdoupnik@hsc.usf.edu
RI Doupnik, Craig/I-3617-2012
OI Doupnik, Craig/0000-0002-7314-0747
CR Berman DM, 1996, J BIOL CHEM, V271, P27209, DOI 10.1074/jbc.271.44.27209
   Bernstein LS, 2004, J BIOL CHEM, V279, P21248, DOI 10.1074/jbc.M312407200
   Bernstein LS, 2000, J BIOL CHEM, V275, P18520, DOI 10.1074/jbc.M000618200
   Blednov YA, 2001, PHYSIOL BEHAV, V74, P109, DOI 10.1016/S0031-9384(01)00555-8
   Blednow YA, 2003, P NATL ACAD SCI USA, V100, P277, DOI 10.1073/pnas.012682399
   BREITWIESER GE, 1988, J GEN PHYSIOL, V91, P469, DOI 10.1085/jgp.91.4.469
   Bünemann M, 1998, J BIOL CHEM, V273, P31186, DOI 10.1074/jbc.273.47.31186
   Chatterjee TK, 1997, J BIOL CHEM, V272, P15481, DOI 10.1074/jbc.272.24.15481
   Chen CH, 1999, J BIOL CHEM, V274, P19799, DOI 10.1074/jbc.274.28.19799
   Chuang HH, 1998, P NATL ACAD SCI USA, V95, P11727, DOI 10.1073/pnas.95.20.11727
   Costigan M, 2003, MOL CELL NEUROSCI, V24, P106, DOI 10.1016/S1044-7431(03)00135-0
   Davydov IV, 2000, J BIOL CHEM, V275, P22931, DOI 10.1074/jbc.M001605200
   DELLACQUA ML, 1993, J BIOL CHEM, V268, P5676
   Doupnik CA, 2004, METHOD ENZYMOL, V389, P131
   Doupnik CA, 2001, BBA-GENE STRUCT EXPR, V1522, P97, DOI 10.1016/S0167-4781(01)00342-6
   Doupnik CA, 1997, P NATL ACAD SCI USA, V94, P10461, DOI 10.1073/pnas.94.19.10461
   Druey KM, 1996, NATURE, V379, P742, DOI 10.1038/379742a0
   Druey KM, 1998, J BIOL CHEM, V273, P18405, DOI 10.1074/jbc.273.29.18405
   Dulin NO, 1999, MOL CELL BIOL, V19, P714
   Ghavami A, 2004, CELL SIGNAL, V16, P711, DOI 10.1016/j.cellsig.2003.11.006
   Gold SJ, 1997, J NEUROSCI, V17, P8024
   HAMILL OP, 1981, PFLUG ARCH EUR J PHY, V391, P85, DOI 10.1007/BF00656997
   Heximer SP, 2001, J BIOL CHEM, V276, P14195, DOI 10.1074/jbc.M009942200
   Hollinger S, 2002, PHARMACOL REV, V54, P527, DOI 10.1124/pr.54.3.527
   Inanobe A, 2001, J PHYSIOL-LONDON, V535, P133, DOI 10.1111/j.1469-7793.2001.t01-1-00133.x
   Jeong SW, 2001, J PHYSIOL-LONDON, V535, P335, DOI 10.1111/j.1469-7793.2001.00335.x
   Kehrl JH, 2002, GENOMICS, V79, P860, DOI 10.1006/geno.2002.6773
   Keren-Raifman T, 2001, FEBS LETT, V492, P20, DOI 10.1016/S0014-5793(01)02220-7
   Koelle MR, 1996, CELL, V84, P115, DOI 10.1016/S0092-8674(00)80998-8
   Lavine N, 2002, J BIOL CHEM, V277, P46010, DOI 10.1074/jbc.M205035200
   Leaney JL, 2004, AM J PHYSIOL-CELL PH, V287, pC182, DOI 10.1152/ajpcell.00540.2003
   Masuho I, 2004, J NEUROCHEM, V88, P161, DOI 10.1046/j.1471-4159.2003.02139.x
   Neill JD, 1997, ENDOCRINOLOGY, V138, P843, DOI 10.1210/en.138.2.843
   RAYMOND JR, 1993, BIOCHEMISTRY-US, V32, P11064, DOI 10.1021/bi00092a016
   Reif K, 2000, J IMMUNOL, V164, P4720, DOI 10.4049/jimmunol.164.9.4720
   Ross EM, 2000, ANNU REV BIOCHEM, V69, P795, DOI 10.1146/annurev.biochem.69.1.795
   Roy AA, 2003, MOL PHARMACOL, V64, P587, DOI 10.1124/mol.64.3.587
   Saitoh O, 2001, J BIOL CHEM, V276, P5052, DOI 10.1074/jbc.M006917200
   Saitoh O, 2002, P NATL ACAD SCI USA, V99, P10138, DOI 10.1073/pnas.152085999
   Saitoh O, 1997, NATURE, V390, P525, DOI 10.1038/37385
   Shea L, 1997, BIOCHEM PHARMACOL, V53, P519, DOI 10.1016/S0006-2952(96)00768-X
   Signorini S, 1997, P NATL ACAD SCI USA, V94, P923, DOI 10.1073/pnas.94.3.923
   Slessareva JE, 2003, J BIOL CHEM, V278, P50530, DOI 10.1074/jbc.M304417200
   Stanfield PR, 2002, REV PHYSIOL BIOCH P, V145, P47, DOI 10.1007/BFb0116431
   Tesmer JJG, 1997, CELL, V89, P251, DOI 10.1016/S0092-8674(00)80204-4
   Tosetti P, 2003, P NATL ACAD SCI USA, V100, P7337, DOI 10.1073/pnas.1231837100
   Tu YP, 2001, J BIOL CHEM, V276, P20160, DOI 10.1074/jbc.M101599200
   Wang Q, 2002, J BIOL CHEM, V277, P24949, DOI 10.1074/jbc.M203802200
   Xu X, 1999, J BIOL CHEM, V274, P3549, DOI 10.1074/jbc.274.6.3549
   Zeng WZ, 1998, J BIOL CHEM, V273, P34687, DOI 10.1074/jbc.273.52.34687
   Zhang QL, 2002, J PHYSIOL-LONDON, V545, P355, DOI 10.1113/jphysiol.2002.032151
NR 51
TC 21
Z9 27
U1 0
U2 4
PU PERGAMON-ELSEVIER SCIENCE LTD
PI OXFORD
PA THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND
SN 0028-3908
EI 1873-7064
J9 NEUROPHARMACOLOGY
JI Neuropharmacology
PD SEP
PY 2005
VL 49
IS 4
BP 465
EP 476
DI 10.1016/j.neuropharm.2005.04.010
PG 12
WC Neurosciences; Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology; Pharmacology & Pharmacy
GA 963BO
UT WOS:000231778000005
PM 15935408
DA 2025-04-10
ER

PT J
AU Miller, BM
   Zhang, SX
   Suggs, JA
   Swank, DM
   Littlefield, KP
   Knowles, AF
   Bernstein, SI
AF Miller, BM
   Zhang, SX
   Suggs, JA
   Swank, DM
   Littlefield, KP
   Knowles, AF
   Bernstein, SI
TI An alternative domain near the nucleotide-binding site of
   Drosophila muscle myosin affects ATPase kinetics
SO JOURNAL OF MOLECULAR BIOLOGY
LA English
DT Article
DE myosin; Drosophila; muscle; ATPase
ID HEAVY-CHAIN GENE; FAMILIAL HYPERTROPHIC CARDIOMYOPATHY; ACTIN SLIDING
   VELOCITY; POWER STROKE STATE; MOTOR DOMAIN; FUNCTIONAL DOMAINS;
   CRYSTAL-STRUCTURE; SKELETAL-MUSCLE; MOLECULAR MOTOR; LIGHT-CHAIN
AB In Drosophila melanogaster expression of muscle myosin heavy chain isoforms occurs by alternative splicing of transcripts from a single gene. The exon 7 domain is one of four variable regions in the catalytic head and is located near the nucleotide-binding site. To ascribe a functional role to this domain, we created two chimeric myosin isoforms (indirect flight isoform-exon 7a and embryonic-exon 7d) that differ from the native indirect flight muscle and embryonic body-wall muscle isoforms only in the exon 7 region. Germline transformation and subsequent expression of the chimeric myosins in the indirect flight muscle of myosin-null Drosophila allowed us to purify the myosin for in vitro studies and to assess in vivo structure and function of transgenic muscles. Intriguingly, in vitro experiments show the exon 7 domain modulates myosin ATPase activity but has no effect on actin filament velocity, a novel result compared to similar studies with other Drosophila variable exons. Transgenic flies expressing the indirect flight isoform-exon 7a. have normal indirect flight muscle structure, and flight and jump ability. However, expression of the embryonic-exon 7d chimeric isoform yields flightless flies that show improvements in both the structural stability of the indirect flight muscle and in locomotor abilities as compared to flies expressing the embryonic isoform. Overall, our results suggest the exon 7 domain participates in the regulation of the attachment of myosin to actin in order to fine-tune the physiological properties of Drosophila myosin isoforms. (c) 2005 Elsevier Ltd. All rights reserved.
C1 San Diego State Univ, Dept Biol, San Diego, CA 92182 USA.
   San Diego State Univ, Inst Mol Biol, San Diego, CA 92182 USA.
   San Diego State Univ, Dept Chem, San Diego, CA 92182 USA.
C3 California State University System; San Diego State University;
   California State University System; San Diego State University;
   California State University System; San Diego State University
RP San Diego State Univ, Dept Biol, San Diego, CA 92182 USA.
EM sbernst@sciences.sdsu.edu
OI Bernstein, Sanford/0000-0001-7094-5390
FU NIGMS NIH HHS [GM32443] Funding Source: Medline
CR Baker JE, 2003, J BIOL CHEM, V278, P28533, DOI 10.1074/jbc.M303583200
   BERNSTEIN SI, 1983, NATURE, V302, P393, DOI 10.1038/302393a0
   Bernstein SI, 1997, J MOL BIOL, V271, P1, DOI 10.1006/jmbi.1997.1160
   Bobkov AA, 1996, P NATL ACAD SCI USA, V93, P2285, DOI 10.1073/pnas.93.6.2285
   COLLIER VL, 1990, GENE DEV, V4, P885, DOI 10.1101/gad.4.6.885
   Conibear PB, 2003, NAT STRUCT BIOL, V10, P831, DOI 10.1038/nsb986
   CRIPPS RM, 1994, J CELL BIOL, V126, P689, DOI 10.1083/jcb.126.3.689
   Cripps RM, 1999, EMBO J, V18, P1793, DOI 10.1093/emboj/18.7.1793
   Dominguez R, 1998, CELL, V94, P559, DOI 10.1016/S0092-8674(00)81598-6
   DRUMMOND DR, 1991, MOL GEN GENET, V226, P70, DOI 10.1007/BF00273589
   FISHER AJ, 1995, BIOCHEMISTRY-US, V34, P8960, DOI 10.1021/bi00028a004
   Geeves MA, 1999, ANNU REV BIOCHEM, V68, P687, DOI 10.1146/annurev.biochem.68.1.687
   GEORGE EL, 1989, MOL CELL BIOL, V9, P2957, DOI 10.1128/MCB.9.7.2957
   Gourinath S, 2003, STRUCTURE, V11, P1621, DOI 10.1016/j.str.2003.10.013
   HARRIS DE, 1993, J BIOL CHEM, V268, P14764
   HASTINGS GA, 1991, J CELL BIOL, V114, P263, DOI 10.1083/jcb.114.2.263
   HESS NK, 1991, DEV BIOL, V146, P339, DOI 10.1016/0012-1606(91)90235-U
   Himmel DM, 2002, P NATL ACAD SCI USA, V99, P12645, DOI 10.1073/pnas.202476799
   Holmes KC, 2003, NATURE, V425, P423, DOI 10.1038/nature02005
   Houdusse A, 1999, CELL, V97, P459, DOI 10.1016/S0092-8674(00)80756-4
   KAZZAZ JA, 1989, DEV BIOL, V133, P550, DOI 10.1016/0012-1606(89)90057-2
   KRON SJ, 1991, METHOD ENZYMOL, V196, P399
   KRONERT WA, 1991, EMBO J, V10, P2479, DOI 10.1002/j.1460-2075.1991.tb07787.x
   Kurzawa-Goertz SE, 1998, BIOCHEMISTRY-US, V37, P7517, DOI 10.1021/bi972844+
   Littlefield KP, 2003, AM J PHYSIOL-CELL PH, V284, pC1031, DOI 10.1152/ajpcell.00474.2002
   LYMN RW, 1971, BIOCHEMISTRY-US, V10, P4617, DOI 10.1021/bi00801a004
   MAHMOOD R, 1989, BIOCHEMISTRY-US, V28, P3989, DOI 10.1021/bi00435a054
   MARGOSSIAN SS, 1982, METHOD ENZYMOL, V85, P55
   Murphy CT, 1998, BIOCHEMISTRY-US, V37, P6738, DOI 10.1021/bi972903j
   ODONNELL PT, 1988, J CELL BIOL, V107, P2601, DOI 10.1083/jcb.107.6.2601
   Okimoto N, 2001, BIOPHYS J, V81, P2786, DOI 10.1016/S0006-3495(01)75921-8
   PARDEE JD, 1982, METHOD ENZYMOL, V85, P164
   Pereira JS, 2001, J BIOL CHEM, V276, P4409, DOI 10.1074/jbc.M006441200
   Pette D, 2000, MICROSC RES TECHNIQ, V50, P500, DOI 10.1002/1097-0029(20000915)50:6<500::AID-JEMT7>3.3.CO;2-Z
   Pirrotta V, 1988, Biotechnology, V10, P437
   RAYMENT I, 1993, SCIENCE, V261, P50, DOI 10.1126/science.8316857
   Razzaq A, 1999, J BIOL CHEM, V274, P28321, DOI 10.1074/jbc.274.40.28321
   Reubold TF, 2003, NAT STRUCT BIOL, V10, P826, DOI 10.1038/nsb987
   Risal D, 2004, P NATL ACAD SCI USA, V101, P8930, DOI 10.1073/pnas.0403002101
   ROBERTS DB, 1998, DROSOPHILA PRACTIAL
   Rovner AS, 1997, J MUSCLE RES CELL M, V18, P103, DOI 10.1023/A:1018689102122
   ROZEK CE, 1983, CELL, V32, P23, DOI 10.1016/0092-8674(83)90493-2
   RUBIN GM, 1982, SCIENCE, V218, P348, DOI 10.1126/science.6289436
   Sasaki N, 2003, BIOCHEMISTRY-US, V42, P90, DOI 10.1021/bi026051l
   Steffen W, 2003, P NATL ACAD SCI USA, V100, P6434, DOI 10.1073/pnas.1231998100
   Swank DM, 2000, MICROSC RES TECHNIQ, V50, P430, DOI 10.1002/1097-0029(20000915)50:6<430::AID-JEMT2>3.0.CO;2-E
   Swank DM, 2003, J BIOL CHEM, V278, P17475, DOI 10.1074/jbc.M212727200
   Swank DM, 2002, NAT CELL BIOL, V4, P312, DOI 10.1038/ncb776
   Swank DM, 2001, J BIOL CHEM, V276, P15117, DOI 10.1074/jbc.M008379200
   Sweeney HL, 1998, J BIOL CHEM, V273, P6262, DOI 10.1074/jbc.273.11.6262
   TOHTONG R, 1995, NATURE, V374, P650, DOI 10.1038/374650a0
   Tyska MJ, 2000, CIRC RES, V86, P737, DOI 10.1161/01.RES.86.7.737
   Tyska MJ, 2002, CELL MOTIL CYTOSKEL, V51, P1, DOI 10.1002/cm.10014
   UYEDA TQP, 1990, J MOL BIOL, V214, P699, DOI 10.1016/0022-2836(90)90287-V
   Volkmann N, 2003, P NATL ACAD SCI USA, V100, P3227, DOI 10.1073/pnas.0536510100
   Volkmann N, 2000, NAT STRUCT BIOL, V7, P1147
   Weiss A, 1996, ANNU REV CELL DEV BI, V12, P417, DOI 10.1146/annurev.cellbio.12.1.417
   Wells L, 1996, EMBO J, V15, P4454, DOI 10.1002/j.1460-2075.1996.tb00822.x
   Xiao M, 2003, NAT STRUCT BIOL, V10, P402, DOI 10.1038/nsb916
   Yamashita H, 2000, J BIOL CHEM, V275, P28045
   Zhang SX, 2001, MECH DEVELOP, V101, P35, DOI 10.1016/S0925-4773(00)00549-9
NR 61
TC 16
Z9 20
U1 0
U2 1
PU ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
PI LONDON
PA 24-28 OVAL RD, LONDON NW1 7DX, ENGLAND
SN 0022-2836
EI 1089-8638
J9 J MOL BIOL
JI J. Mol. Biol.
PD OCT 14
PY 2005
VL 353
IS 1
BP 14
EP 25
DI 10.1016/j.jmb.2005.08.012
PG 12
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 972AT
UT WOS:000232426900002
PM 16154586
DA 2025-04-10
ER

PT J
AU Pereverzev, A
   Klöckner, U
   Henry, M
   Grabsch, H
   Vajna, R
   Olyschläger, S
   Viatchenko-Karpinski, S
   Schröder, R
   Hescheler, J
   Schneider, T
AF Pereverzev, A
   Klöckner, U
   Henry, M
   Grabsch, H
   Vajna, R
   Olyschläger, S
   Viatchenko-Karpinski, S
   Schröder, R
   Hescheler, J
   Schneider, T
TI Structural diversity of the voltage-dependent Ca<SUP>2+</SUP> channel
   α1E-subunit
SO EUROPEAN JOURNAL OF NEUROSCIENCE
LA English
DT Article
DE class E calcium channels; cerebellum; HEK293 cells; isoforms; in vitro
   differentiation; splice variants
ID CARDIAC CALCIUM-CHANNEL; RAT CEREBELLAR NEURONS; FUNCTIONAL EXPRESSION;
   ALPHA(1) SUBUNIT; SKELETAL-MUSCLE; MESSENGER-RNA; MOLECULAR DIVERSITY;
   HEK293 CELLS; INACTIVATION; PHARMACOLOGY
AB Voltage-operated Ca2+ channels are heteromultimeric proteins. Their structural diversity is caused by several genes encoding homologous subunits and by alternative splicing of single transcripts. Isoforms of al subunits, which contain the ion conducting pore, have been deduced from each of the six cDNA sequences cloned so far from different species. The isoforms predicted for the alpha(1E) subunit are structurally related to the primary sequence of the amino terminus, the centre of the subunit (II-III loop), and the carboxy terminus. Mouse and human alpha(1E) transcripts have been analysed by reverse transcription-polymerase chain reaction and by sequencing of amplified fragments. For the II-III loop three different alpha(1E) cDNA fragments are amplified from mouse and human brain, showing that isoforms originally predicted from sequence alignment of different species are expressed in a single one. Both predicted alpha(1E) cDNA fragments of the carboxy terminus are identified in vivo, Two different alpha(1E) constructs, referring to the major structural difference in the carboxy terminus, were stably transfected in HEK293 cells. The biophysical properties of these cells were compared in order to evaluate the importance in vitro of the carboxy terminal insertion found in vivo. The wild-type alpha(1E) subunit showed properties, typical for a high-voltage activated Ca2+ channel. The deletion of 43 amino acid residues at the carboxy terminus does not cause significant differences in the current density and the basic biophysical properties. However, a functional difference is suggested, as in embryonic stem cells, differentiated in vitro to neuronal cells, the pattern of transcripts indicative for different alpha(1E) isoforms changes during development. In human cerebellum the longer alpha(1E) isoform is expressed predominantly. Although, it has not been possible to assign functional differences to the two alpha(1E) constructs tested in vitro, the expression pattern of the structurally related isoforms may have functional importance in vivo.
C1 Univ Cologne, Inst Neurophysiol, D-50931 Cologne, Germany.
   Univ Cologne, Inst Vegetat Physiol, D-50931 Cologne, Germany.
   Univ Cologne, Inst Neuropathol, D-50931 Cologne, Germany.
C3 University of Cologne; University of Cologne; University of Cologne
RP Schneider, T (corresponding author), Univ Cologne, Inst Neurophysiol, Robert Koch Str 39, D-50931 Cologne, Germany.
RI Schröder, Rieke/HTO-0713-2023
CR AUGUSTINE GJ, 1987, ANNU REV NEUROSCI, V10, P633, DOI 10.1146/annurev.ne.10.030187.003221
   BADING H, 1993, SCIENCE, V260, P181, DOI 10.1126/science.8097060
   Berjukow S, 1996, BRIT J PHARMACOL, V118, P748, DOI 10.1111/j.1476-5381.1996.tb15463.x
   BERTOLINO M, 1992, ANNU REV PHARMACOL, V32, P399, DOI 10.1146/annurev.pa.32.040192.002151
   BLEAKMAN D, 1995, NEUROPHARMACOLOGY, V34, P753, DOI 10.1016/0028-3908(95)00078-K
   Bourinet E, 1996, J NEUROSCI, V16, P4983
   CATTERALL WA, 1995, ANNU REV BIOCHEM, V64, P493, DOI 10.1146/annurev.biochem.64.1.493
   CHAUDHARI N, 1993, DEV BIOL, V155, P507, DOI 10.1006/dbio.1993.1048
   CHAUDHARI N, 1994, BIOPHYS J, V66, pA319
   DIEBOLD RJ, 1992, P NATL ACAD SCI USA, V89, P1497, DOI 10.1073/pnas.89.4.1497
   DUNLAP K, 1994, SCIENCE, V266, P828, DOI 10.1126/science.7973643
   Eberst R, 1997, PFLUG ARCH EUR J PHY, V433, P633, DOI 10.1007/s004240050324
   ELLINOR PT, 1993, NATURE, V363, P455, DOI 10.1038/363455a0
   FORTI L, 1994, J NEUROSCI, V14, P5243
   Harlow ED, 1988, ANTIBODIES LAB MANUA
   HO SN, 1989, GENE, V77, P51, DOI 10.1016/0378-1119(89)90358-2
   HOFMANN F, 1994, ANNU REV NEUROSCI, V17, P399, DOI 10.1146/annurev.neuro.17.1.399
   KLOCKNER U, 1995, J BIOL CHEM, V270, P17306, DOI 10.1074/jbc.270.29.17306
   Lievano A, 1996, FEBS LETT, V388, P150, DOI 10.1016/0014-5793(96)00515-7
   Lin ZX, 1997, NEURON, V18, P153, DOI 10.1016/S0896-6273(01)80054-4
   MALOUF NN, 1992, NEURON, V8, P899, DOI 10.1016/0896-6273(92)90204-Q
   Marubio LM, 1996, RECEPTOR CHANNEL, V4, P243
   Mehrke G, 1997, FEBS LETT, V408, P261, DOI 10.1016/S0014-5793(97)00437-7
   MERRIFIELD B, 1986, SCIENCE, V232, P241
   Mochida S, 1996, NEURON, V17, P781, DOI 10.1016/S0896-6273(00)80209-3
   NIIDOME T, 1992, FEBS LETT, V308, P7, DOI 10.1016/0014-5793(92)81038-N
   OLCESE R, 1994, NEURON, V13, P1433, DOI 10.1016/0896-6273(94)90428-6
   PEREZREYES E, 1990, J BIOL CHEM, V265, P20430
   PEREZREYES E, 1995, KIDNEY INT, V48, P1111, DOI 10.1038/ki.1995.395
   Qin N, 1997, P NATL ACAD SCI USA, V94, P8866, DOI 10.1073/pnas.94.16.8866
   RANDALL A, 1995, J NEUROSCI, V15, P2995
   Rettig J, 1996, P NATL ACAD SCI USA, V93, P7363, DOI 10.1073/pnas.93.14.7363
   Schneider T, 1997, TRENDS PHARMACOL SCI, V18, P8, DOI 10.1016/S0165-6147(96)01001-2
   SCHNEIDER T, 1994, RECEPTOR CHANNEL, V2, P255
   SCHNEIDER T, 1996, EUR J NEUROSCI, V9, P10
   SHEARDOWN SA, 1992, TRENDS GENET, V8, P121, DOI 10.1016/0168-9525(92)90360-G
   SOLDATOV NM, 1992, P NATL ACAD SCI USA, V89, P4628, DOI 10.1073/pnas.89.10.4628
   SOLDATOV NM, 1995, J BIOL CHEM, V270, P10540, DOI 10.1074/jbc.270.18.10540
   SOONG TW, 1993, SCIENCE, V260, P1133, DOI 10.1126/science.8388125
   Stea A., 1995, HDB RECEPTORS CHANNE, P113
   Stephens GJ, 1997, PFLUG ARCH EUR J PHY, V433, P523, DOI 10.1007/s004240050308
   STRUBING C, 1995, MECH DEVELOP, V53, P275, DOI 10.1016/0925-4773(95)00446-8
   TANABE T, 1990, NATURE, V346, P567, DOI 10.1038/346567a0
   Tottene A, 1996, J NEUROSCI, V16, P6353
   WAKAMORI M, 1994, RECEPTOR CHANNEL, V2, P303
   WEI XY, 1994, J BIOL CHEM, V269, P1635
   WEI XY, 1995, J BIOL CHEM, V270, P27106, DOI 10.1074/jbc.270.45.27106
   WELLING A, 1993, CIRC RES, V73, P974, DOI 10.1161/01.RES.73.5.974
   WILLIAMS ME, 1994, J BIOL CHEM, V269, P22347
   ZHANG JF, 1993, NEUROPHARMACOLOGY, V32, P1075, DOI 10.1016/0028-3908(93)90003-L
NR 50
TC 42
Z9 44
U1 0
U2 0
PU BLACKWELL SCIENCE LTD
PI OXFORD
PA P O BOX 88, OSNEY MEAD, OXFORD OX2 0NE, OXON, ENGLAND
SN 0953-816X
J9 EUR J NEUROSCI
JI Eur. J. Neurosci.
PD MAR
PY 1998
VL 10
IS 3
BP 916
EP 925
DI 10.1046/j.1460-9568.1998.00099.x
PG 10
WC Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA ZB073
UT WOS:000072432600010
PM 9753159
DA 2025-04-10
ER

PT J
AU Luan, YZ
   Ou, JX
   Kunze, VP
   Qiao, FY
   Wang, Y
   Wei, L
   Li, W
   Xie, Z
AF Luan, Yizhao
   Ou, Jingxing
   Kunze, Vincent P.
   Qiao, Fengyu
   Wang, Yan
   Wei, Lai
   Li, Wei
   Xie, Zhi
TI Integrated transcriptomic and metabolomic analysis reveals adaptive
   changes of hibernating retinas
SO JOURNAL OF CELLULAR PHYSIOLOGY
LA English
DT Article
DE 13-lined ground squirrel; hibernation; metabolome; retina; RNA-seq
ID MAMMALIAN HIBERNATION; GROUND-SQUIRRELS; SUPPRESSION; PLASTICITY; BRAIN;
   ACID; RESPIRATION; EXPRESSION; RESPONSES; SKELETAL
AB Hibernation is a seasonally adaptive strategy that allows hibernators to live through extremely cold conditions. Despite the profound reduction of blood flow to the retinas, hibernation causes no lasting retinal injury. Instead, hibernators show an increased tolerance to ischemic insults during the hibernation period. To understand the molecular changes of the retinas in response to hibernation, we applied an integrative transcriptome and metabolome analysis to explore changes in gene expression and metabolites of 13-lined ground squirrel retinas during hibernation. Metabolomic analysis showed a global decrease of ATP synthesis in hibernating retinas. Decreased glucose and galactose, increased beta-oxidation of carnitine and decreased storage of some amino acids in hibernating retinas indicated a shift of fuel use from carbohydrates to lipids and alternative usage of amino acids. Transcriptomic analysis revealed that the down-regulated genes were enriched in DNA-templated transcription and immune-related functions, while the up-regulated genes were enriched in mitochondrial inner membrane and DNA packaging-related functions. We further showed that a subset of genes underwent active alternative splicing events in response to hibernation. Finally, integrative analysis of the transcriptome and metabolome confirmed the shift of fuel use in the hibernating retina by the regulation of catabolism of amino acids and lipids. Through transcriptomic and metabolomic data, our analysis revealed the altered state of mitochondrial oxidative phosphorylation and the shift of energy source in the hibernating retina, advancing our understanding of the molecular mechanisms employed by hibernators. The data will also serve as a useful resource for the ocular and hibernation research communities.
C1 [Luan, Yizhao; Wang, Yan; Wei, Lai; Li, Wei; Xie, Zhi] Sun Yat Sen Univ, State Key Lab Ophthalmol, Zhongshan Ophthalm Ctr, Guangdong Prov Key Lab Ophthalmol,Visual Sci, 54 South Xianlie South Rd,Bldg 3, Guangzhou, Guangdong, Peoples R China.
   [Luan, Yizhao] Sun Yat Sen Univ, Sch Life Sci, Guangzhou, Guangdong, Peoples R China.
   [Ou, Jingxing; Kunze, Vincent P.; Qiao, Fengyu; Li, Wei] NEI, Retinal Neurobiol Sect, 35 Convent Dr,Bldg 35A,Rm 3F-226, Bethesda, MD 20892 USA.
C3 Sun Yat Sen University; Sun Yat Sen University; National Institutes of
   Health (NIH) - USA; NIH National Eye Institute (NEI)
RP Xie, Z (corresponding author), Sun Yat Sen Univ, State Key Lab Ophthalmol, Zhongshan Ophthalm Ctr, Guangdong Prov Key Lab Ophthalmol,Visual Sci, 54 South Xianlie South Rd,Bldg 3, Guangzhou, Guangdong, Peoples R China.; Li, W (corresponding author), NEI, Retinal Neurobiol Sect, 35 Convent Dr,Bldg 35A,Rm 3F-226, Bethesda, MD 20892 USA.
EM liwei2@nei.nih.gov; xiezhi@gmail.com
RI Xie, Zhi/A-3108-2012; wei, lai/JCO-0672-2023; Luan, Yizhao/JJE-7039-2023
OI Kunze, Vincent/0000-0002-7869-9793; Luan, Yizhao/0000-0003-4396-6078;
   Xie, Zhi/0000-0002-5589-4836; Ou, Jingxing/0000-0002-2777-8176; Wei,
   Lai/0000-0002-3300-8506; Li, Wei/0000-0002-2897-649X
FU Science and Technology Planning Projects of Guangdong Province
   [2014B030301040]; Joint Research Fund for Overseas Natural Science of
   China [3030901001222]; Major Program of Science and Technology of
   Guangzhou [201607020001]; National Natural Science Foundation of China
   [31471232]; National Eye Institute; Center for Precision Medicine, SYSU
FX Science and Technology Planning Projects of Guangdong Province, Grant
   number: 2014B030301040; Joint Research Fund for Overseas Natural Science
   of China, Grant number: 3030901001222; Major Program of Science and
   Technology of Guangzhou, Grant number: 201607020001; National Natural
   Science Foundation of China, Grant number: 31471232; National Eye
   Institute, Grant number: intramural research program; Center for
   Precision Medicine, SYSU
CR Aken BL, 2016, DATABASE-OXFORD, DOI 10.1093/database/baw093
   Anders S, 2012, GENOME RES, V22, P2008, DOI 10.1101/gr.133744.111
   Andrews MT, 2007, BIOESSAYS, V29, P431, DOI 10.1002/bies.20560
   [Anonymous], 2010, GENOME BIOL, DOI DOI 10.1186/gb-2010-11-10-r106
   Arendt T, 2013, AM J PHYSIOL-REG I, V305, pR478, DOI 10.1152/ajpregu.00117.2013
   Arnesen T, 2011, PLOS BIOL, V9, DOI 10.1371/journal.pbio.1001074
   BARNES BM, 1989, SCIENCE, V244, P1593, DOI 10.1126/science.2740905
   BOCHAROVA LS, 1992, COMP BIOCHEM PHYS B, V101, P189, DOI 10.1016/0305-0491(92)90177-S
   Boyer BB, 1999, BIOSCIENCE, V49, P713, DOI 10.2307/1313595
   Brown JCL, 2014, J COMP PHYSIOL B, V184, P401, DOI 10.1007/s00360-013-0799-3
   Brown JCL, 2012, AM J PHYSIOL-REG I, V302, pR15, DOI 10.1152/ajpregu.00230.2011
   BRUSTOVETSKY NN, 1989, COMP BIOCHEM PHYS B, V94, P537, DOI 10.1016/0305-0491(89)90193-4
   Carey HV, 2003, PHYSIOL REV, V83, P1153, DOI 10.1152/physrev.00008.2003
   Chertov AO, 2011, J BIOL CHEM, V286, P34700, DOI 10.1074/jbc.M111.279752
   Cuenca N, 2014, PROG RETIN EYE RES, V43, P17, DOI 10.1016/j.preteyeres.2014.07.001
   Dave KR, 2012, COMP BIOCHEM PHYS B, V162, P1, DOI 10.1016/j.cbpb.2012.01.008
   den Hollander AI, 2007, NAT GENET, V39, P889, DOI 10.1038/ng2066
   Drew KL, 2001, FREE RADICAL BIO MED, V31, P563, DOI 10.1016/S0891-5849(01)00628-1
   Eisenreich A, 2009, CIRC RES, V104, P589, DOI 10.1161/CIRCRESAHA.108.183905
   Fang LQ, 2011, J CHROMATOGR A, V1218, P7316, DOI 10.1016/j.chroma.2011.08.044
   Field KA, 2015, PLOS PATHOG, V11, DOI 10.1371/journal.ppat.1005168
   Florant GL, 2012, J COMP PHYSIOL B, V182, P451, DOI 10.1007/s00360-011-0630-y
   Geiser F, 2004, ANNU REV PHYSIOL, V66, P239, DOI 10.1146/annurev.physiol.66.032102.115105
   Hampton M, 2011, PLOS ONE, V6, DOI 10.1371/journal.pone.0027021
   Hindle AG, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0071627
   Inman DM, 2017, FRONT NEUROSCI-SWITZ, V11, DOI 10.3389/fnins.2017.00146
   Janeway C., 2001, IMMUNOBIOLOGY
   Kabine M, 2003, BIOCHIMIE, V85, P707, DOI 10.1016/S0300-9084(03)00117-2
   Kaden TR, 2013, ASIA-PAC J OPHTHALMO, V2, P341, DOI 10.1097/APO.0b013e31829d3e33
   Kanehisa M, 2016, NUCLEIC ACIDS RES, V44, pD457, DOI 10.1093/nar/gkv1070
   Li CQ, 2013, NUCLEIC ACIDS RES, V41, DOI 10.1093/nar/gkt161
   Li CQ, 2009, NUCLEIC ACIDS RES, V37, DOI 10.1093/nar/gkp667
   Liao Y, 2013, NUCLEIC ACIDS RES, V41, DOI 10.1093/nar/gkt214
   Melvin RG, 2009, TRENDS ENDOCRIN MET, V20, P490, DOI 10.1016/j.tem.2009.09.005
   Merriman DK, 2016, EXP EYE RES, V150, P90, DOI 10.1016/j.exer.2016.01.011
   Mortazavi A, 2008, NAT METHODS, V5, P621, DOI 10.1038/nmeth.1226
   Narayan DS, 2017, CLIN EXP OPHTHALMOL, V45, P730, DOI 10.1111/ceo.12952
   Nelson CJ, 2009, PHYSIOL GENOMICS, V37, P43, DOI 10.1152/physiolgenomics.90323.2008
   Pan YH, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0062039
   Peretti D, 2015, NATURE, V518, P236, DOI 10.1038/nature14142
   POPOV VI, 1992, NEUROSCIENCE, V48, P53, DOI 10.1016/0306-4522(92)90337-2
   POPOV VI, 1992, NEUROSCIENCE, V48, P45, DOI 10.1016/0306-4522(92)90336-Z
   Sirianni AC, 2015, J NEUROCHEM, V134, P956, DOI 10.1111/jnc.13190
   Soga T, 2006, J BIOL CHEM, V281, P16768, DOI 10.1074/jbc.M601876200
   Staples JF, 2016, COMPR PHYSIOL, V6, P737, DOI 10.1002/cphy.c140064
   Staples JF, 2014, J EXP BIOL, V217, P2032, DOI 10.1242/jeb.092973
   Sterling P, 1999, NAT NEUROSCI, V2, P851, DOI 10.1038/13142
   Stieler JT, 2011, PLOS ONE, V6, DOI 10.1371/journal.pone.0014530
   Toien O, 2011, SCIENCE, V331, P906, DOI 10.1126/science.1199435
   Trapnell C, 2009, BIOINFORMATICS, V25, P1105, DOI 10.1093/bioinformatics/btp120
   van Breukelen F, 2002, J COMP PHYSIOL B, V172, P355, DOI 10.1007/s00360-002-0256-1
   Väremo L, 2013, NUCLEIC ACIDS RES, V41, P4378, DOI 10.1093/nar/gkt111
   Vaughan DK, 2006, LAB ANIMAL, V35, P33, DOI 10.1038/laban0406-33
   Vermillion KL, 2015, J PROTEOME RES, V14, P4792, DOI 10.1021/acs.jproteome.5b00575
   von der Ohe CG, 2006, J NEUROSCI, V26, P10590, DOI 10.1523/JNEUROSCI.2874-06.2006
   WATANABE M, 1990, COMP BIOCHEM PHYS B, V97, P605, DOI 10.1016/0305-0491(90)90167-R
   Xu YC, 2013, BMC GENOMICS, V14, DOI 10.1186/1471-2164-14-567
   Yates A, 2016, NUCLEIC ACIDS RES, V44, pD710, DOI 10.1093/nar/gkv1157
   Zhou F, 2001, AM J PATHOL, V158, P2145, DOI 10.1016/S0002-9440(10)64686-X
NR 59
TC 17
Z9 17
U1 2
U2 55
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0021-9541
EI 1097-4652
J9 J CELL PHYSIOL
JI J. Cell. Physiol.
PD FEB
PY 2018
VL 233
IS 2
BP 1434
EP 1445
DI 10.1002/jcp.26030
PG 12
WC Cell Biology; Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Physiology
GA FL9RB
UT WOS:000414593500063
PM 28542832
DA 2025-04-10
ER

PT J
AU Milstein, ML
   McFarland, TP
   Marsh, JD
   Cala, SE
AF Milstein, Michelle L.
   McFarland, Timothy P.
   Marsh, James D.
   Cala, Steven E.
TI Inefficient glycosylation leads to high steady-state levels of actively
   degrading cardiac triadin-1
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID JUNCTIONAL SARCOPLASMIC-RETICULUM; RYANODINE RECEPTOR;
   MOLECULAR-CLONING; SKELETAL-MUSCLE; IMPORTANT DETERMINANT;
   N-GLYCOSYLATION; RELEASE CHANNEL; AMINO-ACID; CALSEQUESTRIN; PROTEIN
AB In junctional sarcoplasmic reticulum, binding to cardiac triadin-1 provides a mechanism by which the Ca2+-release channel/ryanodine receptor may link with calsequestrin to regulate Ca2+ release. Calsequestrin and triadin-1 both contain N-linked glycans, but about half of triadin-1 in the heart remains unglycosylated. To investigate mechanisms for this incomplete glycosylation, we overexpressed triadin-1 as a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors. We showed that the characteristic incomplete glycosylation stemmed from properties of the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane. Although triadin-1 appeared by SDS-PAGE analysis as a 35/40-kDa doublet in all cells, variations occurred in the relative levels of the two glycoforms depending on the cell type and whether overexpression involved a plasmid or adenoviral vector. Treatment of triadin-1 with the proteasome inhibitor MG-132 led to striking changes in the relative levels of triadin-1 that indicated active breakdown of unglycosylated, but not glycosylated, triadin-1. Besides substantial increases in the relative levels of unglycosylated triadin-1, proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75). Effects of tunicamycin and endoglycosidase H confirmed that these novel isoforms represent two alternative N-linked glycosylation sites, indicating that an alternative topology occurs infrequently leading to yet other glycoforms with short half-lives.
C1 [McFarland, Timothy P.; Cala, Steven E.] Wayne State Univ, Sch Med, Dept Physiol, Detroit, MI 48201 USA.
   [Milstein, Michelle L.] Wayne State Univ, Sch Med, Dept Pharmacol, Detroit, MI 48201 USA.
   [Marsh, James D.] Univ Arkansas Med Sci, Dept Internal Med, Little Rock, AR 72205 USA.
C3 Wayne State University; Wayne State University; University of Arkansas
   System; University of Arkansas Medical Sciences
RP Cala, SE (corresponding author), Wayne State Univ, Sch Med, Dept Physiol, Elliman Bldg 421 E Canfield Ave, Detroit, MI 48201 USA.
EM s.cala@wayne.edu
FU NHLBI NIH HHS [HL62586] Funding Source: Medline
CR BAUSE E, 1983, BIOCHEM J, V209, P331, DOI 10.1042/bj2090331
   Bers DM, 2004, J MOL CELL CARDIOL, V37, P417, DOI 10.1016/j.yjmcc.2004.05.026
   BURNETTE WN, 1981, ANAL BIOCHEM, V112, P195, DOI 10.1016/0003-2697(81)90281-5
   CASWELL AH, 1991, BIOCHEMISTRY-US, V30, P7507, DOI 10.1021/bi00244a020
   Guo W, 1996, J BIOL CHEM, V271, P458, DOI 10.1074/jbc.271.1.458
   GUO W, 1995, J BIOL CHEM, V270, P9027, DOI 10.1074/jbc.270.16.9027
   Helenius A, 2001, SCIENCE, V291, P2364, DOI 10.1126/science.291.5512.2364
   Hölscher C, 2001, J BIOL CHEM, V276, P13388, DOI 10.1074/jbc.M007331200
   Hong CS, 2001, GENE, V278, P193, DOI 10.1016/S0378-1119(01)00718-1
   Houle TD, 2006, EXP CELL RES, V312, P4150, DOI 10.1016/j.yexcr.2006.09.010
   INUI M, 1987, J BIOL CHEM, V262, P15637
   Jones LR, 1995, J BIOL CHEM, V270, P30787, DOI 10.1074/jbc.270.51.30787
   KIM KC, 1990, BIOCHEMISTRY-US, V29, P9281, DOI 10.1021/bi00491a025
   Kirchhof P, 2007, J MOL CELL CARDIOL, V42, P962, DOI 10.1016/j.yjmcc.2007.02.012
   KNUDSON CM, 1993, J BIOL CHEM, V268, P12646
   Kobayashi YM, 2000, J BIOL CHEM, V275, P17639, DOI 10.1074/jbc.M002091200
   Kobayashi YM, 1999, J BIOL CHEM, V274, P28660, DOI 10.1074/jbc.274.40.28660
   LAEMMLI UK, 1970, NATURE, V227, P680, DOI 10.1038/227680a0
   Lee JM, 2004, J BIOL CHEM, V279, P6994, DOI 10.1074/jbc.M312446200
   LOWRY OH, 1951, J BIOL CHEM, V193, P265
   Maki T, 1996, J CLIN INVEST, V97, P656, DOI 10.1172/JCI118462
   Mellquist JL, 1998, BIOCHEMISTRY-US, V37, P6833, DOI 10.1021/bi972217k
   NAKAI J, 1990, FEBS LETT, V271, P169, DOI 10.1016/0014-5793(90)80399-4
   O'Brian JJ, 2002, J BIOL CHEM, V277, P37154, DOI 10.1074/jbc.M204370200
   OTSU K, 1990, J BIOL CHEM, V265, P13472
   Popov M, 1997, J BIOL CHEM, V272, P18325, DOI 10.1074/jbc.272.29.18325
   Ram ML, 2004, MOL CELL BIOCHEM, V266, P209, DOI 10.1023/B:MCBI.0000049164.28580.56
   ShakinEshleman SH, 1996, J BIOL CHEM, V271, P6363, DOI 10.1074/jbc.271.11.6363
   Terentyev D, 2005, CIRC RES, V96, P651, DOI 10.1161/01.RES.0000160609.98948.25
   Zhang L, 1997, J BIOL CHEM, V272, P23389, DOI 10.1074/jbc.272.37.23389
NR 30
TC 6
Z9 7
U1 0
U2 3
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD JAN 25
PY 2008
VL 283
IS 4
BP 1929
EP 1935
DI 10.1074/jbc.M704623200
PG 7
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 253EH
UT WOS:000252501000019
PM 18025088
OA hybrid
DA 2025-04-10
ER

PT J
AU Sonnenberg, A
   Liem, RKH
AF Sonnenberg, Arnoud
   Liem, Ronald K. H.
TI Plakins in development and disease
SO EXPERIMENTAL CELL RESEARCH
LA English
DT Review
DE plakin; cytolinker; desmoplakin; plectin; BPAG; MACF; epidermolysis
   bullosa; cardiomyopathy; muscular dystrophy; spectrin; cytoskeleton
ID CYTOSKELETAL LINKER PROTEIN; RIGHT-VENTRICULAR CARDIOMYOPATHY; INTEGRIN
   BETA-4 SUBUNIT; INTERMEDIATE-FILAMENT-BINDING; EPIDERMOLYSIS-BULLOSA
   SIMPLEX; RETROGRADE AXONAL-TRANSPORT; MUSCLE-TENDON JUNCTION; LINKING
   FACTOR MACF; PALMOPLANTAR KERATODERMA; STRATIFIED EPITHELIA
AB Plakins are large multi-domain molecules that have various functions to link cytoskeletal elements together and to connect them to junctional complexes. Plakins were first identified in epithelial cells where they were found to connect the intermediate filaments to desmosomes and hemidesmosomes [Ruhrberg, C., and Watt, F.M. (1997). The plakin family: versatile organizers of cytoskeletal architecture. Curr Opin Genet Dev 7, 392-397.]. They were subsequently found to be important for the integrity of muscle cells. Most recently, they have been found in the nervous system, where their functions appear to be more complex, including cross-linking of microtubules (MTs) and actin filaments [Leung, C. L., Zheng, M., Prater, S.M., and Liem, R.K. (2001). The BPAG1 locus: Alternative splicing produces multiple isoforms with distinct cytoskeletal linker domains, including predominant isoforms in neurons and muscles. J Cell Biol 154, 691-697., Leung, C.L., Sun, D., Zheng, M., Knowles, D.R., and Liem, R.K. (1999). Microtubule actin cross-linking factor (MACF): a hybrid of dystonin and dystrophin that can interact with the actin and microtubule cytoskeletons. J Cell Biol 147, 1275-1286.]. These plakins have also indicated their relationship to the spectrin superfamily of proteins and the plakins appear to be evolutionarily related to the spectrins, but have diverged to perform different specialized functions. in invertebrates, a single plakin is present in both Drosophila melanogaster and Caenorhabditis elegans, which resemble the more complex plakins found in mammals [Roper, K., Gregory, S.L., and Brown, N.H. (2002). The 'spectraplakins': cytoskeletal giants with characteristics of both spectrin and plakin families. J Cell Sci 115, 4215-4225.1. In contrast, there are seven plakins found in mammals and most of them have alternatively spliced forms leading to a very complex group of proteins with potential tissue specific functions [Jefferson, J.J., Leung, C.L., and Liem, R.K. (2004). Plakins: goliaths that link cell junctions and the cytoskeleton. Nat Rev Mol Cell Biol 5, 542-553.]. In this review, we will first describe the plakins, desmoplakin, plectin, envoplakin and periplakin and then describe two other mammalian plakins, Bullous pemphigoid antigen 1 (BPAG1) and microtubule actin cross-linking factor 1 (MACF1), that are expressed in multiple isoforms in different tissues. We will also describe the relationship of these two proteins to the invertebrate plakins, shortstop (shot) in Drosophila and VAB-10 in C. elegans. Finally, we will describe an unusual mammalian plakin, called epiplakin. (c) 2007 Elsevier Inc. All rights reserved.
C1 Netherlands Canc Inst, Div Cell Biol, NL-1066 CX Amsterdam, Netherlands.
   Columbia Univ, Coll Phys & Surg, Dept Pathol & Cell Biol, New York, NY 10032 USA.
C3 Netherlands Cancer Institute; Columbia University
RP Sonnenberg, A (corresponding author), Netherlands Canc Inst, Div Cell Biol, Plesmanlaan 121, NL-1066 CX Amsterdam, Netherlands.
EM a.sonnenberg@nki.nl; rkl2@columbia.edu
CR Abrahamsberg C, 2005, P NATL ACAD SCI USA, V102, P18449, DOI 10.1073/pnas.0505380102
   Aho S, 2004, MOL CELL BIOL, V24, P6410, DOI 10.1128/MCB.24.14.6410-6418.2004
   Alcalai R, 2003, J AM COLL CARDIOL, V42, P319, DOI 10.1016/S0735-1097(03)00628-4
   Andrä K, 1998, GENE DEV, V12, P3442, DOI 10.1101/gad.12.21.3442
   Andra K, 1997, GENE DEV, V11, P3143, DOI 10.1101/gad.11.23.3143
   ANGST BD, 1990, J CELL SCI, V97, P247
   Bennett V, 2001, PHYSIOL REV, V81, P1353, DOI 10.1152/physrev.2001.81.3.1353
   Bernier G, 1995, MOL CELL NEUROSCI, V6, P509, DOI 10.1006/mcne.1995.0003
   Bornslaeger EA, 2001, J CELL SCI, V114, P727
   Borradori L, 1999, J INVEST DERMATOL, V112, P411, DOI 10.1046/j.1523-1747.1999.00546.x
   Bosher JM, 2003, J CELL BIOL, V161, P757, DOI 10.1083/jcb.200302151
   BROWN A, 1995, NAT GENET, V10, P301, DOI 10.1038/ng0795-301
   BYERS TJ, 1995, FEBS LETT, V368, P500, DOI 10.1016/0014-5793(95)00722-L
   Camargo LM, 2007, MOL PSYCHIATR, V12, P74, DOI 10.1038/sj.mp.4001880
   Carmeliet P, 1999, CELL, V98, P147, DOI 10.1016/S0092-8674(00)81010-7
   Charlesworth A, 2003, J INVEST DERMATOL, V121, P1344, DOI 10.1111/j.1523-1747.2003.12639.x
   Chen HJ, 2006, GENE DEV, V20, P1933, DOI 10.1101/gad.1411206
   Choi HJ, 2002, NAT STRUCT BIOL, V9, P612, DOI 10.1038/nsb818
   Claudepierre T, 2005, J COMP NEUROL, V487, P190, DOI 10.1002/cne.20549
   Dalpé G, 1998, MOL CELL NEUROSCI, V10, P243, DOI 10.1006/mcne.1997.0660
   Dalpé G, 1999, DEV BIOL, V210, P367, DOI 10.1006/dbio.1999.9263
   Drabek K, 2006, CURR BIOL, V16, P2259, DOI 10.1016/j.cub.2006.09.065
   DUCHEN LW, 1964, BRAIN, V87, P367, DOI 10.1093/brain/87.2.367
   Eger A, 1997, J CELL SCI, V110, P1307
   Elliott CE, 1997, GENOMICS, V42, P115, DOI 10.1006/geno.1997.4724
   Favre B, 2001, J BIOL CHEM, V276, P32427, DOI 10.1074/jbc.M011005200
   Fontao L, 2003, MOL BIOL CELL, V14, P1978, DOI 10.1091/mbc.E02-08-0548
   Fuchs P, 1999, HUM MOL GENET, V8, P2461, DOI 10.1093/hmg/8.13.2461
   Fujiwara S, 2001, J BIOL CHEM, V276, P13340, DOI 10.1074/jbc.M011386200
   Gache Y, 1996, J CLIN INVEST, V97, P2289, DOI 10.1172/JCI118671
   Gallicano GI, 2001, DEVELOPMENT, V128, P929
   Gallicano GI, 1998, J CELL BIOL, V143, P2009, DOI 10.1083/jcb.143.7.2009
   Geerts D, 1999, J CELL BIOL, V147, P417, DOI 10.1083/jcb.147.2.417
   Gerull B, 2004, NAT GENET, V36, P1162, DOI 10.1038/ng1461
   Getsios S, 2004, NAT REV MOL CELL BIO, V5, P271, DOI 10.1038/nrm1356
   Geuijen CAW, 2002, MOL BIOL CELL, V13, P3845, DOI 10.1091/mbc.02-01-0601
   Giorda R, 2004, J MED GENET, V41, DOI 10.1136/jmg.2003.012260
   Goto M, 2006, MOL CELL BIOL, V26, P548, DOI 10.1128/MCB.26.2.548-558.2006
   GREEN KJ, 1992, INT J BIOL MACROMOL, V14, P145, DOI 10.1016/S0141-8130(05)80004-2
   Gregor M, 2006, J CELL SCI, V119, P1864, DOI 10.1242/jcs.02891
   Gregory SL, 1998, J CELL BIOL, V143, P1271, DOI 10.1083/jcb.143.5.1271
   Groot KR, 2004, J CELL BIOL, V166, P653, DOI 10.1083/jcb.200312123
   Grossmann KS, 2004, J CELL BIOL, V167, P149, DOI 10.1083/jcb.200402096
   GUO LF, 1995, CELL, V81, P233, DOI 10.1016/0092-8674(95)90333-X
   Hämmerling B, 2006, CELL TISSUE RES, V324, P55, DOI 10.1007/s00441-005-0090-3
   Herrmann H, 2004, ANNU REV BIOCHEM, V73, P749, DOI 10.1146/annurev.biochem.73.011303.073823
   Jang SI, 2005, J CELL SCI, V118, P781, DOI 10.1242/jcs.01647
   Jefferson JJ, 2004, NAT REV MOL CELL BIO, V5, P542, DOI 10.1038/nrm1425
   Jefferson JJ, 2007, J MOL BIOL, V366, P244, DOI 10.1016/j.jmb.2006.11.036
   Jefferson JJ, 2006, EXP CELL RES, V312, P2712, DOI 10.1016/j.yexcr.2006.04.025
   Jones JCR, 1998, BIOESSAYS, V20, P488, DOI 10.1002/(SICI)1521-1878(199806)20:6<488::AID-BIES7>3.3.CO;2-9
   Jonkman MF, 2005, AM J HUM GENET, V77, P653, DOI 10.1086/496901
   Karakesisoglou I, 2000, J CELL BIOL, V149, P195, DOI 10.1083/jcb.149.1.195
   Karashima T, 2002, J CELL SCI, V115, P5027, DOI 10.1242/jcs.00191
   Keith D, 1999, HUM MOL GENET, V8, P143, DOI 10.1093/hmg/8.1.143
   Kodama A, 2003, CELL, V115, P343, DOI 10.1016/S0092-8674(03)00813-4
   Koster J, 2004, HANDB EXP PHARM, V165, P243, DOI 10.1007/978-3-540-68170-0_9
   Koster J, 2004, MOL BIOL CELL, V15, P1211, DOI 10.1091/mbc.E03-09-0697
   Koster J, 2003, J CELL SCI, V116, P387, DOI 10.1242/jcs.00241
   Koster J, 2001, J INVEST DERMATOL, V117, P1405, DOI 10.1046/j.0022-202x.2001.01567.x
   Kowalczyk AP, 1997, J CELL BIOL, V139, P773, DOI 10.1083/jcb.139.3.773
   Lapouge K, 2006, J CELL SCI, V119, P4974, DOI 10.1242/jcs.03255
   Lechler T, 2007, J CELL BIOL, V176, P147, DOI 10.1083/jcb.200609109
   Lee S, 2000, J NEUROSCI, V20, P1096, DOI 10.1523/JNEUROSCI.20-03-01096.2000
   Lee S, 2002, DEVELOPMENT, V129, P1195
   Lee S, 2002, DEVELOPMENT, V129, P1509
   Leung CL, 1999, J CELL BIOL, V147, P1275, DOI 10.1083/jcb.147.6.1275
   Leung CL, 2002, TRENDS CELL BIOL, V12, P37, DOI 10.1016/S0962-8924(01)02180-8
   Leung CL, 2001, J CELL BIOL, V154, P691, DOI 10.1083/jcb.200012098
   Lin CM, 2005, J CELL SCI, V118, P3727, DOI 10.1242/jcs.02510
   Litjens SHM, 2006, TRENDS CELL BIOL, V16, P376, DOI 10.1016/j.tcb.2006.05.004
   Litjens SHM, 2003, MOL BIOL CELL, V14, P4039, DOI 10.1091/mbc.E03-05-0268
   Liu JJ, 2007, P NATL ACAD SCI USA, V104, P2223, DOI 10.1073/pnas.0602222104
   Liu JJ, 2003, J CELL BIOL, V163, P223, DOI 10.1083/jcb.200306075
   Lunter PC, 2002, BIOCHEM BIOPH RES CO, V296, P904, DOI 10.1016/S0006-291X(02)02007-7
   Määttä A, 2001, MOL CELL BIOL, V21, P7047, DOI 10.1128/MCB.21.20.7047-7053.2001
   McGrath JA, 1997, NAT GENET, V17, P240, DOI 10.1038/ng1097-240
   McKoy G, 2000, LANCET, V355, P2119, DOI 10.1016/S0140-6736(00)02379-5
   McLean WHI, 1996, GENE DEV, V10, P1724, DOI 10.1101/gad.10.14.1724
   Meng JJ, 1997, J BIOL CHEM, V272, P21495, DOI 10.1074/jbc.272.34.21495
   Nakano A, 2001, PEDIATR RES, V49, P618, DOI 10.1203/00006450-200105000-00003
   Nikolic B, 1996, J CELL BIOL, V134, P1455, DOI 10.1083/jcb.134.6.1455
   Norgett EE, 2000, HUM MOL GENET, V9, P2761, DOI 10.1093/hmg/9.18.2761
   OKEEFE EJ, 1989, J BIOL CHEM, V264, P8310
   Okuda T, 1999, BIOCHEM BIOPH RES CO, V264, P568, DOI 10.1006/bbrc.1999.1538
   Osmanagic-Myers S, 2004, J BIOL CHEM, V279, P18701, DOI 10.1074/jbc.M312382200
   Osmanagic-Myers S, 2006, J CELL BIOL, V174, P557, DOI 10.1083/jcb.200605172
   Prokop A, 1998, J CELL BIOL, V143, P1283, DOI 10.1083/jcb.143.5.1283
   Prout M, 1997, GENETICS, V146, P275
   Pulkkinen L, 1998, AM J HUM GENET, V63, P1376, DOI 10.1086/302116
   Rampazzo A, 2002, AM J HUM GENET, V71, P1200, DOI 10.1086/344208
   Rezniczek GA, 2003, HUM MOL GENET, V12, P3181, DOI 10.1093/hmg/ddg345
   Rezniczek GA, 1998, J CELL BIOL, V141, P209, DOI 10.1083/jcb.141.1.209
   Röper K, 2003, J CELL BIOL, V162, P1305, DOI 10.1083/jcb.200307089
   Röper K, 2002, J CELL SCI, V115, P4215, DOI 10.1242/jcs.00157
   Ruhrberg C, 1997, J CELL BIOL, V139, P1835, DOI 10.1083/jcb.139.7.1835
   Ruhrberg C, 1996, J CELL BIOL, V134, P715, DOI 10.1083/jcb.134.3.715
   Ruhrberg C, 1997, CURR OPIN GENET DEV, V7, P392, DOI 10.1016/S0959-437X(97)80154-2
   Ruiz P, 1996, J CELL BIOL, V135, P215, DOI 10.1083/jcb.135.1.215
   Sjöblom T, 2006, SCIENCE, V314, P268, DOI 10.1126/science.1133427
   Slep KC, 2005, J CELL BIOL, V168, P587, DOI 10.1083/jcb.200410114
   Smith EA, 1998, J CELL BIOL, V141, P1229, DOI 10.1083/jcb.141.5.1229
   Smith FJD, 1996, NAT GENET, V13, P450, DOI 10.1038/ng0896-450
   Sonnenberg A, 2007, J MOL BIOL, V368, P1379, DOI 10.1016/j.jmb.2007.02.090
   Spazierer D, 2006, MOL CELL BIOL, V26, P559, DOI 10.1128/MCB.26.2.559-568.2006
   Spazierer D, 2003, J BIOL CHEM, V278, P31657, DOI 10.1074/jbc.M303055200
   STAPPENBECK TS, 1994, J BIOL CHEM, V269, P29351
   Stegh AH, 2000, MOL CELL BIOL, V20, P5665, DOI 10.1128/MCB.20.15.5665-5679.2000
   Strumpf D, 1998, J CELL BIOL, V143, P1259, DOI 10.1083/jcb.143.5.1259
   Subramanian A, 2003, CURR BIOL, V13, P1086, DOI 10.1016/S0960-9822(03)00416-0
   Sun DM, 2001, J CELL SCI, V114, P161
   Sun YP, 1999, J BIOL CHEM, V274, P33522, DOI 10.1074/jbc.274.47.33522
   Thoma-Uszynski S, 2006, J IMMUNOL, V176, P2015, DOI 10.4049/jimmunol.176.3.2015
   Uitto J, 2007, EXP CELL RES, V313, P1995, DOI 10.1016/j.yexcr.2007.03.029
   VANVACTOR D, 1993, CELL, V73, P1137, DOI 10.1016/0092-8674(93)90643-5
   Vasioukhin V, 2001, NAT CELL BIOL, V3, P1076, DOI 10.1038/ncb1201-1076
   Whittock NV, 1999, J INVEST DERMATOL, V113, P940, DOI 10.1046/j.1523-1747.1999.00783.x
   Whittock NV, 2002, J INVEST DERMATOL, V118, P232, DOI 10.1046/j.0022-202x.2001.01664.x
   Wiche G, 1998, J CELL SCI, V111, P2477
   Wilhelmsen K, 2005, J CELL BIOL, V171, P799, DOI 10.1083/jcb.200506083
   Yang YM, 1999, CELL, V98, P229, DOI 10.1016/S0092-8674(00)81017-X
   Yang YM, 1996, CELL, V86, P655, DOI 10.1016/S0092-8674(00)80138-5
   Yang Z, 2006, CIRC RES, V99, P646, DOI 10.1161/01.RES.0000241482.19382.c6
   Zhou X, 2004, J CELL SCI, V117, P3129, DOI 10.1242/jcs.01132
NR 124
TC 223
Z9 264
U1 1
U2 27
PU ELSEVIER INC
PI SAN DIEGO
PA 525 B STREET, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0014-4827
EI 1090-2422
J9 EXP CELL RES
JI Exp. Cell Res.
PD JUN 10
PY 2007
VL 313
IS 10
BP 2189
EP 2203
DI 10.1016/j.yexcr.2007.03.039
PG 15
WC Oncology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Oncology; Cell Biology
GA 179ZC
UT WOS:000247328300019
PM 17499243
DA 2025-04-10
ER

PT J
AU Stobdan, T
   Jain, PP
   Xiong, MM
   Bafna, V
   Yuan, JXJ
   Haddad, GG
AF Stobdan, Tsering
   Jain, Pritesh P.
   Xiong, Mingmei
   Bafna, Vineet
   Yuan, Jason X-J
   Haddad, Gabriel G.
TI Heterozygous Tropomodulin 3 mice have improved lung
   vascularization after chronic hypoxia
SO HUMAN MOLECULAR GENETICS
LA English
DT Article
ID ALTITUDE PULMONARY-HYPERTENSION; GENETIC-BASIS; POINTED ENDS; ACTIN;
   TROPOMYOSIN; ADAPTATION; MECHANISM; MUSCLE
AB The molecular mechanisms leading to high-altitude pulmonary hypertension (HAPH) remains poorly understood. We previously analyzed the whole genome sequence of Kyrgyz highland population and identified eight genomic intervals having a potential role in HAPH. Tropomodulin 3 gene (TMOD3), which encodes a protein that binds and caps the pointed ends of actin filaments and inhibits cell migration, was one of the top candidates. Here we systematically sought additional evidence to validate the functional role of TMOD3. In-silico analysis reveals that some of the SNPs in HAPH associated genomic intervals were positioned in a regulatory region that could result in alternative splicing of TMOD3. In order to functionally validate the role of TMOD3 in HAPH, we exposed Tmod(-/+) mice to 4 weeks of constant hypoxia, i.e. 10% O-2 and analyzed both functional (hemodynamic measurements) and structural (angiography) parameters related to HAPH. The hemodynamic measurements, such as right ventricular systolic pressure, a surrogate measure for pulmonary arterial systolic pressure, and right ventricular contractility (RV- +/- dP/dt), increases with hypoxia did not separate between Tmod3(-)(/+) and control mice. Remarkably, there was a significant increase in the number of lung vascular branches and total length of pulmonary vascular branches (P < 0.001) in Tmod3(-/+) after 4 weeks of constant hypoxia as compared with controls. Notably, the Tmod3(-)(/+) endothelial cells migration was also significantly higher than that from the wild-type littermates. Our results indicate that, under chronic hypoxia, lower levels of Tmod3 play an important role in the maintenance or neo-vascularization of pulmonary arteries.
C1 [Stobdan, Tsering; Haddad, Gabriel G.] Univ Calif San Diego, Div Resp Med Dept Pediat, La Jolla, CA 92093 USA.
   [Jain, Pritesh P.; Xiong, Mingmei; Yuan, Jason X-J] Univ Calif San Diego, Dept Med, La Jolla, CA 92093 USA.
   [Bafna, Vineet] Univ Calif San Diego, Dept Comp Sci & Engn, La Jolla, CA 92093 USA.
   [Haddad, Gabriel G.] Univ Calif San Diego, Dept Neurosci, La Jolla, CA 92093 USA.
   [Haddad, Gabriel G.] Rady Childrens Hosp, San Diego, CA 92123 USA.
C3 University of California System; University of California San Diego;
   University of California System; University of California San Diego;
   University of California System; University of California San Diego;
   University of California System; University of California San Diego;
   Rady Childrens Hospital San Diego
RP Haddad, GG (corresponding author), Univ Calif San Diego, Dept Pediat, 9500 Gilman Dr MC0735, La Jolla, CA 92093 USA.
EM ghaddad@health.ucsd.edu
RI Bafna, Vineet/LTF-6857-2024
FU National Institutes of Health [R01HL127403, R01GM114362]
FX National Institutes of Health (R01HL127403 to G.G.H., and R01GM114362 to
   V.B.).
CR Aggarwal S, 2010, P NATL ACAD SCI USA, V107, P18961, DOI 10.1073/pnas.1006108107
   Aguet F, 2020, SCIENCE, V369, P1318, DOI 10.1126/science.aaz1776
   Aldashev AA, 2002, AM J RESP CRIT CARE, V166, P1396, DOI 10.1164/rccm.200204-345OC
   Cox PR, 2000, GENOMICS, V63, P97, DOI 10.1006/geno.1999.6061
   Fischer RS, 2003, J CELL BIOL, V161, P371, DOI 10.1083/jcb.200209057
   FOWLER VM, 1993, J CELL BIOL, V120, P411, DOI 10.1083/jcb.120.2.411
   FOWLER VM, 1990, J CELL BIOL, V111, P471, DOI 10.1083/jcb.111.2.471
   Fowler VM, 1997, SOC GEN PHY, V52, P79
   Gokhin DS, 2011, J CELL BIOL, V194, P105, DOI 10.1083/jcb.201011128
   Iranmehr A, 2019, EUR J HUM GENET, V27, P150, DOI 10.1038/s41431-018-0270-8
   Jain PP, 2021, BRIT J PHARMACOL, V178, P3373, DOI 10.1111/bph.15442
   Jain PP, 2020, PULM CIRC, V10, DOI 10.1177/2045894020956592
   Jo YJ, 2016, SCI REP-UK, V6, DOI 10.1038/srep29204
   Kumari R, 2020, CURR BIOL, V30, P767, DOI 10.1016/j.cub.2019.12.049
   Landry JR, 2003, TRENDS GENET, V19, P640, DOI 10.1016/j.tig.2003.09.014
   León-Velarde F, 2005, HIGH ALT MED BIOL, V6, P147, DOI 10.1089/ham.2005.6.147
   Li YI, 2018, NAT GENET, V50, P151, DOI 10.1038/s41588-017-0004-9
   Lim CY, 2015, NAT COMMUN, V6, DOI 10.1038/ncomms6951
   Liu CS, 2019, MOL THER-NUCL ACIDS, V16, P335, DOI 10.1016/j.omtn.2019.03.001
   Lorenzo FR, 2014, NAT GENET, V46, P951, DOI 10.1038/ng.3067
   Maggiorini M, 2003, EUR RESPIR J, V22, P1019, DOI 10.1183/09031936.03.00052403
   MEYRICK B, 1983, CLIN CHEST MED, V4, P199
   Naeije R, 2019, EUR RESPIR J, V53, DOI 10.1183/13993003.00985-2019
   Ongen H, 2016, BIOINFORMATICS, V32, P1479, DOI 10.1093/bioinformatics/btv722
   Pai AA, 2016, PLOS GENET, V12, DOI 10.1371/journal.pgen.1006338
   Pak O, 2007, EUR RESPIR J, V30, P364, DOI 10.1183/09031936.00128706
   Parreno Justin, 2018, Biophys Rev, V10, P1605, DOI 10.1007/s12551-018-0481-9
   Rao JN, 2014, SCIENCE, V345, P463, DOI 10.1126/science.1256159
   Sakao S, 2009, RESP RES, V10, DOI 10.1186/1465-9921-10-95
   Seeger W, 2013, PULM CIRC, V3, P128, DOI 10.4103/2045-8932.109951
   Soria R, 2019, EUR RESPIR J, V53, DOI 10.1183/13993003.02040-2018
   Stobdan T, 2017, MOL BIOL EVOL, V34, P3154, DOI 10.1093/molbev/msx239
   Storey JD, 2003, P NATL ACAD SCI USA, V100, P9440, DOI 10.1073/pnas.1530509100
   Sui ZH, 2014, BLOOD, V123, P758, DOI 10.1182/blood-2013-03-492710
   Sydykov A, 2021, INT J ENV RES PUB HE, V18, DOI 10.3390/ijerph18041692
   Taraseviciene-Stewart L, 2001, FASEB J, V15, P427, DOI 10.1096/fj.00-0343com
   Tofovic P S, 2009, Prilozi, V30, P25
   Udpa N, 2014, GENOME BIOL, V15, DOI 10.1186/gb-2014-15-2-r36
   Wang ET, 2008, NATURE, V456, P470, DOI 10.1038/nature07509
   Wang JP, 2019, SCI REP-UK, V9, DOI 10.1038/s41598-018-37130-4
   WEBER A, 1994, J CELL BIOL, V127, P1627, DOI 10.1083/jcb.127.6.1627
   Witt KE, 2019, PHILOS T R SOC B, V374, DOI 10.1098/rstb.2018.0235
   Xin DD, 2008, PLOS ONE, V3, DOI 10.1371/journal.pone.0002377
   Yamashiro S, 2012, CYTOSKELETON, V69, P337, DOI 10.1002/cm.21031
   Zhou D, 2013, AM J HUM GENET, V93, P452, DOI 10.1016/j.ajhg.2013.07.011
NR 45
TC 2
Z9 2
U1 0
U2 1
PU OXFORD UNIV PRESS
PI OXFORD
PA GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND
SN 0964-6906
EI 1460-2083
J9 HUM MOL GENET
JI Hum. Mol. Genet.
PD APR 1
PY 2022
VL 31
IS 7
BP 1130
EP 1140
DI 10.1093/hmg/ddab291
EA NOV 2021
PG 11
WC Biochemistry & Molecular Biology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Genetics & Heredity
GA 2C1NJ
UT WOS:000790041200001
PM 34718575
OA Green Published
DA 2025-04-10
ER

PT J
AU Mango, R
   Predazzi, IM
   Romeo, F
   Novelli, G
AF Mango, Ruggiero
   Predazzi, Irene Marta
   Romeo, Francesco
   Novelli, Giuseppe
TI LOX-1/LOXIN: The Yin/Yang of Atheroscleorosis
SO CARDIOVASCULAR DRUGS AND THERAPY
LA English
DT Article
DE Atherosclerosis; Genetics; LOX-1; LOXIN; Polymorphisms
ID SMOOTH-MUSCLE-CELLS; DENSITY-LIPOPROTEIN RECEPTOR-1;
   ISCHEMIA-REPERFUSION INJURY; OXIDIZED LDL RECEPTOR-1; MITOCHONDRIAL
   DYSFUNCTION; ENDOTHELIAL RECEPTOR; OLR1 GENE; APOPTOSIS; LOX-1;
   MACROPHAGES
AB Atherosclerosis is the first cause of death in industrialized countries. Together with traditional risk factors (male gender, hypercholesterolemia, hypertension, diabetes, smoking and age), non-traditional risk factors have also been described as predisposing to this disease. Among these, oxidized low density lipoproteins (OxLDL) have been described in correlation to many proatherogenic processes. Many of the effects of OxLDL are mediated by the lectin like oxidized low density lipoprotein receptor 1 (LOX-1), expressed on endothelial cells, macrophages, SMCs and platelets. LOX-1 is encoded by the lectin like oxidized low density lipoprotein receptor 1 (OLR1) gene, located in the p12.3-p13.2 region of human chromosome 12. Variations on this gene have been studied extensively both at the functional and epidemiological level. Despite the fact that functional roles for two variants have been demonstrated, the epidemiological studies have provided inconsistent and inconclusive results. Of particular interest, it has been demonstrated that a linkage disequilibirum block of SNPs located in the intronic sequence of the OLR1 gene modulates the alternative splicing of OLR1 mRNA, leading to different ratios of LOX-1 full receptor and LOXIN, an isoform lacking part of the functional domain. As demonstrated, LOXIN acts by blocking the negative effective of LOX-1 activation. Here we review the state of the art regarding LOX-1, LOXIN, and the functional effects that are associated with the interaction of these molecules.
C1 [Novelli, Giuseppe] Univ Rome, Natl Agcy Evaluat, Rome, Italy.
   [Mango, Ruggiero; Romeo, Francesco] Univ Roma Tor Vergata, Dipartimento Med Interna, Rome, Italy.
   [Mango, Ruggiero; Romeo, Francesco] Univ Roma Tor Vergata, UOC Cardiol Fdn Policlin, Rome, Italy.
   [Predazzi, Irene Marta] Univ Roma Tor Vergata, Dipartimento Biopatol & Diagnost Immagini, Rome, Italy.
   [Novelli, Giuseppe] St Peter Hosp Fatebenefratelli, Rome, Italy.
   [Novelli, Giuseppe] ANVUR, Rome, Italy.
C3 Sapienza University Rome; University of Rome Tor Vergata; University of
   Rome Tor Vergata; University of Rome Tor Vergata
RP Novelli, G (corresponding author), Univ Rome, Natl Agcy Evaluat, Rome, Italy.
EM novelli@med.uniroma2.it
RI Novelli, Giuseppe/A-5195-2013; Romeo, Francesco/IRZ-6637-2023
OI Novelli, Giuseppe/0000-0002-7781-602X
CR Aoyama T, 1999, BIOCHEM J, V339, P177, DOI 10.1042/0264-6021:3390177
   Asmis R, 2003, CIRC RES, V92, pE20, DOI 10.1161/01.RES.0000051886.43510.90
   Bauriedel G, 1999, CARDIOVASC RES, V41, P480, DOI 10.1016/S0008-6363(98)00318-6
   Bennett MR, 1999, CARDIOVASC RES, V41, P361, DOI 10.1016/S0008-6363(98)00212-0
   BENNETT MR, 1995, J CLIN INVEST, V95, P2266, DOI 10.1172/JCI117917
   Binder CJ, 2002, NAT MED, V8, P1218, DOI 10.1038/nm1102-1218
   Biocca S, 2008, J MOL CELL CARDIOL, V44, P561, DOI 10.1016/j.yjmcc.2007.11.017
   Biocca S, 2009, PLOS ONE, V4, DOI 10.1371/journal.pone.0004648
   Brodsky SV, 2004, CIRC RES, V94, P377, DOI 10.1161/01.RES.0000111802.09964.EF
   Chen MJ, 2002, PHARMACOL THERAPEUT, V95, P89, DOI 10.1016/S0163-7258(02)00236-X
   Dhume AS, 2003, ANN VASC SURG, V17, P1, DOI 10.1007/s10016-001-0331-1
   Dhume AS, 2003, J VASC SURG, V38, P155, DOI 10.1016/S0741-5214(02)75463-3
   Ehara S, 2001, CIRCULATION, V103, P1955, DOI 10.1161/01.cir.103.15.1955
   Geng YJ, 2003, BIOCHEM PHARMACOL, V66, P1485, DOI 10.1016/S0006-2952(03)00502-1
   GENG YJ, 1995, AM J PATHOL, V147, P251
   HAN DKM, 1995, AM J PATHOL, V147, P267
   Hardwick SJ, 1996, J PATHOL, V179, P294
   HARRISON GJ, 1995, HEART VESSELS, V10, P249, DOI 10.1007/BF01744904
   Hou XW, 2008, CLIN CHIM ACTA, V388, P200, DOI 10.1016/j.cca.2007.11.016
   Hu C, 2008, J MOL CELL CARDIOL, V44, P76, DOI 10.1016/j.yjmcc.2007.10.009
   ISNER JM, 1995, CIRCULATION, V91, P2703, DOI 10.1161/01.CIR.91.11.2703
   Iwai-Kanai E, 2001, CIRCULATION, V104, P2948, DOI 10.1161/hc4901.100381
   Iwanaga Y, 1998, CIRCULATION, V98, P2065, DOI 10.1161/01.CIR.98.19.2065
   Jaffer FA, 2006, J AM COLL CARDIOL, V47, P1328, DOI 10.1016/j.jacc.2006.01.029
   Kataoka H, 1999, CIRCULATION, V99, P3110, DOI 10.1161/01.CIR.99.24.3110
   Kataoka H, 2001, ARTERIOSCL THROM VAS, V21, P955, DOI 10.1161/01.ATV.21.6.955
   Knowles JW, 2008, BMC MED GENET, V9, DOI 10.1186/1471-2350-9-23
   Kolodgie FD, 2000, AM J PATHOL, V157, P1259, DOI 10.1016/S0002-9440(10)64641-X
   Kume N, 1998, CIRC RES, V83, P322, DOI 10.1161/01.RES.83.3.322
   Lee TS, 2001, AM J PHYSIOL-CELL PH, V280, pC709, DOI 10.1152/ajpcell.2001.280.3.C709
   Li D. Y., 2002, Journal of Cardiovascular Pharmacology and Therapeutics, V7, P147, DOI 10.1177/107424840200700304
   Li DY, 2003, J AM COLL CARDIOL, V41, P1048, DOI 10.1016/S0735-1097(02)02966-2
   Li DY, 2002, AM J PHYSIOL-HEART C, V283, pH1795, DOI 10.1152/ajpheart.00382.2002
   Li DY, 1999, CIRC RES, V84, P1043, DOI 10.1161/01.RES.84.9.1043
   Libby P, 2002, NATURE, V420, P868, DOI [10.1038/nature01323, 10.1161/ATVBAHA.108.179705]
   Lusis AJ, 2000, NATURE, V407, P233, DOI 10.1038/35025203
   Mango R, 2005, CIRC RES, V97, P152, DOI 10.1161/01.RES.0000174563.62625.8e
   Mango R, 2003, J MED GENET, V40, P933, DOI 10.1136/jmg.40.12.933
   Mehta JL, 2004, CARDIOVASC RES, V64, P243, DOI 10.1016/j.cardiores.2004.07.002
   Mehta JL, 2002, J AM COLL CARDIOL, V39, P1429, DOI 10.1016/S0735-1097(02)01803-X
   Murase T, 1998, CIRC RES, V83, P328, DOI 10.1161/01.RES.83.3.328
   Murray CJL, 1997, LANCET, V349, P1498, DOI 10.1016/S0140-6736(96)07492-2
   Napoli C, 2003, ANNU REV PHARMACOL, V43, P97, DOI 10.1146/annurev.pharmtox.43.100901.140226
   Ohmori R, 2004, CLIN CARDIOL, V27, P641, DOI 10.1002/clc.4960271112
   Salvayre R, 2002, BBA-MOL CELL BIOL L, V1585, P213, DOI 10.1016/S1388-1981(02)00343-8
   Sata M, 1998, J CLIN INVEST, V102, P1682, DOI 10.1172/JCI3531
   Sawamura T, 1997, NATURE, V386, P73, DOI 10.1038/386073a0
   Sentinelli F, 2006, NUTR METAB CARDIOVAS, V16, P345, DOI 10.1016/j.numecd.2005.06.002
   Shi XH, 2001, J CELL SCI, V114, P1273
   Steinberg D, 2002, NAT MED, V8, P1211, DOI 10.1038/nm1102-1211
   Stoneman VEA, 2004, CLIN SCI, V107, P343, DOI 10.1042/CS20040086
   Suzuki T, 2002, CLIN BIOCHEM, V35, P347, DOI 10.1016/S0009-9120(02)00326-0
   Tatsuguchi M, 2003, BIOCHEM BIOPH RES CO, V303, P247, DOI 10.1016/S0006-291X(03)00326-7
   Wang LY, 2011, STROKE, V42, P588, DOI 10.1161/STROKEAHA.110.596841
   WHITE SJ, 2010, CARDIOVASC IN PRESS
   Yao PM, 2001, J BIOL CHEM, V276, P42468, DOI 10.1074/jbc.M101419200
NR 56
TC 23
Z9 23
U1 0
U2 7
PU SPRINGER
PI DORDRECHT
PA VAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDS
SN 0920-3206
EI 1573-7241
J9 CARDIOVASC DRUG THER
JI Cardiovasc. Drugs Ther.
PD OCT
PY 2011
VL 25
IS 5
BP 489
EP 494
DI 10.1007/s10557-011-6333-5
PG 6
WC Cardiac & Cardiovascular Systems; Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology; Pharmacology & Pharmacy
GA 839IT
UT WOS:000296359600012
PM 21904818
DA 2025-04-10
ER

PT J
AU Yang, L
   Sakurai, T
   Kamiyoshi, A
   Ichikawa-Shindo, Y
   Kawate, H
   Yoshizawa, T
   Koyama, T
   Iesato, Y
   Uetake, R
   Yamauchi, A
   Tanaka, M
   Toriyama, Y
   Igarashi, K
   Shindo, T
AF Yang, Lei
   Sakurai, Takayuki
   Kamiyoshi, Akiko
   Ichikawa-Shindo, Yuka
   Kawate, Hisaka
   Yoshizawa, Takahiro
   Koyama, Teruhide
   Iesato, Yasuhiro
   Uetake, Ryuichi
   Yamauchi, Akihiro
   Tanaka, Megumu
   Toriyama, Yuichi
   Igarashi, Kyoko
   Shindo, Takayuki
TI Endogenous CGRP protects against neointimal hyperplasia following
   wire-induced vascular injury
SO JOURNAL OF MOLECULAR AND CELLULAR CARDIOLOGY
LA English
DT Article
DE Calcitonin gene-related peptide (CORP); Neointimal hyperplasia; Vascular
   smooth muscle cell (VSMC); Oxidative stress; Inflammation
ID GENE-RELATED PEPTIDE; SMOOTH-MUSCLE-CELLS; RAT PULMONARY-ARTERY;
   CALCITONIN-GENE; ANGIOTENSIN-II; ENDOTHELIAL-CELLS; NAD(P)H OXIDASE;
   GROWTH-FACTOR; PROLIFERATION; MICE
AB Neointimal hyperplasia is the primary lesion underlying atherosclerosis and restenosis after percutaneous coronary intervention. Calcitonin gene-related peptide (CGRP) is produced by alternative splicing of the primary transcript of the calcitonin/CGRP gene. Originally identified as a strongly vasodilatory neuropeptide, CGRP is now known to be a pleiotropic peptide widely distributed in various organs and tissues. Our aim was to investigate the possibility that CGRP acts as an endogenous vasoprotective molecule.
   We compared the effect of CGRP deficiency on neointimal formation after wire-induced vascular injury in wild-type and CGRP knockout (CGRP-/-) mice. We found that neointimal formation after vascular injury was markedly enhanced in CGRP-/- mice, which also showed a higher degree of oxidative stress, as indicated by reduced expression of nitric oxide synthase, increased expression of p47phox, and elevated levels of 4HNE, as well as greater infiltration of macrophages. In addition, CGRP-deficiency led to increased vascular smooth muscle cell (VSMC) proliferation within the neointima. By contrast, bone marrow-derived cells had little or no effect on neointimal formation in CGRP-/- mice. In vitro analysis showed that CGRP-treatment suppressed VSMC proliferation, migration, and ERK1/2 activity.
   These results clearly demonstrate that endogenous CGRP suppresses the oxidative stress and VSMC proliferation induced by vascular injury. As a vasoprotective molecule, CGRP could be an important therapeutic target in cardiovascular disease. (C) 2013 Elsevier Ltd. All rights reserved.
C1 [Yang, Lei; Sakurai, Takayuki; Kamiyoshi, Akiko; Ichikawa-Shindo, Yuka; Kawate, Hisaka; Yoshizawa, Takahiro; Koyama, Teruhide; Iesato, Yasuhiro; Uetake, Ryuichi; Yamauchi, Akihiro; Tanaka, Megumu; Toriyama, Yuichi; Igarashi, Kyoko; Shindo, Takayuki] Shinshu Univ, Grad Sch Med, Dept Cardiovasc Res, Matsumoto, Nagano 3908621, Japan.
   [Yang, Lei] Hebei Med Univ, Sch Publ Hlth, Dept Epidemiol & Stat, Shijiazhuang, Peoples R China.
   [Yoshizawa, Takahiro; Koyama, Teruhide] Japan Soc Promot Sci, Tokyo, Japan.
C3 Shinshu University; Hebei Medical University; Japan Society for the
   Promotion of Science
RP Shindo, T (corresponding author), Shinshu Univ, Grad Sch Med, Dept Cardiovasc Res, Asahi 3-1-1, Matsumoto, Nagano 3908621, Japan.
EM tshindo@shinshu-u.ac.jp
RI 晃英, 小山/AAI-9805-2020
OI Sakurai, Takayuki/0000-0002-7220-5940
FU Funding Program for Next Generation World-Leading Researchers (NEXT
   Program) from the Cabinet Office, Government of Japan; PRESTO of the
   Japan Science and Technology Agency (JST); A-STEP of the JST; Ministry
   of Education, Culture, Sports, Science and Technology (MEXT); Japan
   Society for the Promotion of Science (JSPS); National Cardiovascular
   Center; Mitsui Life Social Welfare Foundation; Takeda Science
   Foundation; Kanzawa Medical Research Foundation; Public Trust Fund;
   Suzuken Memorial Foundation; Japan Heart Foundation; Naito Foundation;
   SENSHIN Medical Research Foundation; NOVARTIS Foundation (Japan) for the
   Promotion of Science; Grants-in-Aid for Scientific Research [23590456,
   25460330, 23790288] Funding Source: KAKEN
FX This study was supported by the Funding Program for Next Generation
   World-Leading Researchers (NEXT Program) from the Cabinet Office,
   Government of Japan, by PRESTO of the Japan Science and Technology
   Agency (JST), A-STEP of the JST, a grant-in-aid for Scientific Research
   from the the Ministry of Education, Culture, Sports, Science and
   Technology (MEXT), a grant-in-aid from the Japan Society for the
   Promotion of Science (JSPS) Fellows, a research grant for cardiovascular
   disease from the National Cardiovascular Center, research grants from
   the Mitsui Life Social Welfare Foundation, Takeda Science Foundation,
   Kanzawa Medical Research Foundation, Public Trust Fund for the Promotion
   of Surgery, Suzuken Memorial Foundation, Japan Heart Foundation, The
   Naito Foundation, SENSHIN Medical Research Foundation, and The NOVARTIS
   Foundation (Japan) for the Promotion of Science.
CR Bennett GS, 1998, BRIT J PHARMACOL, V124, P1573, DOI 10.1038/sj.bjp.0701986
   Bol M, 2012, PFLUG ARCH EUR J PHY, V463, P669, DOI 10.1007/s00424-012-1083-1
   Brain SD, 2004, PHYSIOL REV, V84, P903, DOI 10.1152/physrev.00037.2003
   BUNKER CB, 1993, LANCET, V342, P80, DOI 10.1016/0140-6736(93)91286-U
   Chattergoon NN, 2005, AM J PHYSIOL-LUNG C, V288, pL202, DOI 10.1152/ajplung.00064.2004
   Costa MA, 2005, CIRCULATION, V111, P2257, DOI 10.1161/01.CIR.0000163587.36485.A7
   Das M, 2001, J BIOL CHEM, V276, P15631, DOI 10.1074/jbc.M010690200
   Deng PY, 2005, PEPTIDES, V26, P1676, DOI 10.1016/j.peptides.2005.02.002
   Duckers HJ, 2001, NAT MED, V7, P693, DOI 10.1038/89068
   Dzau VJ, 2002, NAT MED, V8, P1249, DOI 10.1038/nm1102-1249
   GRAY DW, 1992, EUR J PHARMACOL, V212, P37, DOI 10.1016/0014-2999(92)90069-G
   Gulati R, 2003, CIRCULATION, V108, P1520, DOI 10.1161/01.CIR.0000089084.48655.49
   HIRATA Y, 1988, BIOCHEM BIOPH RES CO, V151, P1113, DOI 10.1016/S0006-291X(88)80481-9
   HOLZER P, 1988, NEUROSCIENCE, V24, P739, DOI 10.1016/0306-4522(88)90064-4
   Kainiyoshi A, 2006, BIOCHEM BIOPH RES CO, V343, P152, DOI 10.1016/j.bbrc.2006.02.132
   Kawai J, 2004, CIRCULATION, V109, P1147, DOI 10.1161/01.CIR.0000117231.40057.6D
   Kobayashi M, 2005, J ATHEROSCLER THROMB, V12, P138, DOI 10.5551/jat.12.138
   Kohno M, 1999, J AM SOC NEPHROL, V10, P2495
   Kong DL, 2004, CIRCULATION, V110, P2039, DOI 10.1161/01.CIR.0000143161.01901.BD
   Koundrioukoff S, 2000, J BIOL CHEM, V275, P22882, DOI 10.1074/jbc.M001850200
   Li WJ, 2006, AM J PHYSIOL-CELL PH, V291, pC456, DOI 10.1152/ajpcell.00538.2005
   Li XW, 2012, EUR J PHARMACOL, V679, P117, DOI 10.1016/j.ejphar.2012.01.015
   Marx SO, 2011, CIRC-CARDIOVASC INTE, V4, P104, DOI 10.1161/CIRCINTERVENTIONS.110.957332
   Oh-hashi Y, 2001, CIRC RES, V89, P983, DOI 10.1161/hh2301.100812
   Patterson C, 1999, J BIOL CHEM, V274, P19814, DOI 10.1074/jbc.274.28.19814
   Qin XP, 2004, EUR J PHARMACOL, V488, P45, DOI 10.1016/j.ejphar.2004.02.010
   Ray Jenna Lynn, 2001, Methods in Cell Science, V23, P185
   ROSENFELD MG, 1983, NATURE, V304, P129, DOI 10.1038/304129a0
   Ross R, 1999, NEW ENGL J MED, V340, P115, DOI 10.1056/NEJM199901143400207
   SAITO A, 1989, J PHARMACOL EXP THER, V248, P455
   Sata M, 2000, J MOL CELL CARDIOL, V32, P2097, DOI 10.1006/jmcc.2000.1238
   Sata M, 2002, NAT MED, V8, P403, DOI 10.1038/nm0402-403
   Schneider L, 2009, PANCREATOLOGY, V9, P662, DOI 10.1159/000212099
   Schramm A, 2012, VASC PHARMACOL, V56, P216, DOI 10.1016/j.vph.2012.02.012
   Shi Y, 2001, ARTERIOSCL THROM VAS, V21, P739, DOI 10.1161/01.ATV.21.5.739
   Sueur S, 2005, J MOL CELL CARDIOL, V39, P955, DOI 10.1016/j.yjmcc.2005.09.008
   Supowit SC, 2005, HYPERTENSION, V45, P109, DOI 10.1161/01.HYP.0000151130.34874.fa
   Tanaka K, 2003, CIRC RES, V93, P783, DOI 10.1161/01.RES.0000096651.13001.B4
   Thiévent A, 2005, PEPTIDES, V26, P1567, DOI 10.1016/j.peptides.2005.02.015
   Touyz RM, 1999, J HYPERTENS, V17, P907, DOI 10.1097/00004872-199917070-00006
   Wellman GC, 1998, J PHYSIOL-LONDON, V507, P117, DOI 10.1111/j.1469-7793.1998.117bu.x
   Welt FGP, 2002, ARTERIOSCL THROM VAS, V22, P1769, DOI 10.1161/01.ATV.0000037100.44766.5B
   Wimalawansa SJ, 1996, ENDOCR REV, V17, P533, DOI 10.1210/er.17.5.533
   Wisskirchen FM, 1998, BRIT J PHARMACOL, V123, P1673, DOI 10.1038/sj.bjp.0701783
   Wu L, 2001, CIRCULATION, V104, P2716, DOI 10.1161/hc4601.099404
   Yajima N, 2008, CIRCULATION, V117, P3079, DOI 10.1161/CIRCULATIONAHA.107.746453
   Yoneda M, 2003, EUR J PHARMACOL, V478, P173, DOI 10.1016/j.ejphar.2003.08.040
   Yoshioka T, 2006, CARDIOVASC RES, V70, P61, DOI 10.1016/j.cardiores.2005.12.013
   Zhang XN, 2010, ANN THORAC SURG, V90, P117, DOI 10.1016/j.athoracsur.2010.03.063
   Zheng SA, 2010, AM J PHYSIOL-CELL PH, V299, pC1485, DOI 10.1152/ajpcell.00173.2010
   Zhou Z, 2010, ATHEROSCLEROSIS, V213, P92, DOI 10.1016/j.atherosclerosis.2010.08.050
NR 51
TC 22
Z9 29
U1 0
U2 11
PU ELSEVIER SCI LTD
PI OXFORD
PA THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND
SN 0022-2828
EI 1095-8584
J9 J MOL CELL CARDIOL
JI J. Mol. Cell. Cardiol.
PD JUN
PY 2013
VL 59
BP 55
EP 66
DI 10.1016/j.yjmcc.2013.02.002
PG 12
WC Cardiac & Cardiovascular Systems; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology; Cell Biology
GA 144SF
UT WOS:000318960000006
PM 23416515
OA Green Submitted
DA 2025-04-10
ER

PT J
AU Spinner, BJ
   Zajdel, RW
   McLean, MD
   Denz, CR
   Dube, S
   Mehta, S
   Choudhury, A
   Nakatsugawa, M
   Dobbins, N
   Lemanski, LF
   Dube, DK
AF Spinner, BJ
   Zajdel, RW
   McLean, MD
   Denz, CR
   Dube, S
   Mehta, S
   Choudhury, A
   Nakatsugawa, M
   Dobbins, N
   Lemanski, LF
   Dube, DK
TI Characterization of a TM-4 type Tropomyosin that is essential for
   myofibrillogenesis and contractile activity in embryonic hearts of the
   Mexican axolotl
SO JOURNAL OF CELLULAR BIOCHEMISTRY
LA English
DT Article
DE oligonucleotide; transfection; tropomyosin isoforms; nonmuscle
   tropomyosin; alternative splicing
ID SMOOTH-MUSCLE TROPOMYOSIN; ALPHA-TROPOMYOSIN; AMBYSTOMA-MEXICANUM;
   SKELETAL-MUSCLE; FIBROBLAST TROPOMYOSIN; ISOFORM DIVERSITY;
   GENE-EXPRESSION; CARDIAC MUTANT; NONMUSCLE; MECHANISM
AB A striated muscle isoform of a Tropomyosin (TM-4) gene was characterized and found to be necessary for contractile function in embryonic heart. The full-length clone of this isoform was isolated from the Mexican axolotl (Ambystoma mexicanum) and named 6 Cardiac-3 (ATmC-3). The gene encoded a cardiac-specific, Axolotl Tropomyosin tropomyosin protein with 284 amino acid residues that demonstrated high homology to the Xenopus cardiac TM-4 type tropomyosin. Northern blot analysis indicates a transcript of similar to1.25 kb in size. RT-PCR and in situ hybridization demonstrated that this isoform is predominantly in cardiac tissue. Our laboratory uses an animal model that carries a cardiac lethal mutation (gene c), this mutation results in a greatly diminished level of tropomyosin protein in the ventricle. Transfection of ATmC-3 DNA into mutant hearts increased tropomyosin levels and promoted myofibrillogenesis. ATmC-3 expression was blocked in normal hearts by transfection of exon-specific anti-sense oligonucleotide (AS-ODN). RT-PCR confirmed lower transcript expression of ATmC-3 and in vitro analysis confirmed the specificity of the ATmC-3 exon 2 anti-sense oligonucleotide. These AS-ODN treated hearts also had a disruption of myofibril organization and disruption of synchronous contractions. These results demonstrated that a striated muscle isoform of the TM-4 gene was expressed embryonically and was necessary for normal structure and function of the ventricle.
C1 Upstate Med Univ, Dept Med, Syracuse, NY 13210 USA.
   Upstate Med Univ, Dept Cell & Dev Biol, Syracuse, NY 13210 USA.
   Texas A&M Univ, Dept Med Physiol, College Stn, TX 77843 USA.
C3 State University of New York (SUNY) System; State University of New York
   (SUNY) Upstate Medical Center; State University of New York (SUNY)
   System; State University of New York (SUNY) Upstate Medical Center;
   Texas A&M University System; Texas A&M University College Station
RP Dube, DK (corresponding author), Upstate Med Univ, Dept Med, 750 E Adams St, Syracuse, NY 13210 USA.
FU NHLBI NIH HHS [HL37702, HL32184] Funding Source: Medline; NICHD NIH HHS
   [N0-1HD-6-2915] Funding Source: Medline
CR Blanchard EM, 1997, CIRC RES, V81, P1005
   BORDZILOVSKAYA NP, 1989, DEV BIOL AXOLOTL, P210
   BOYD J, 1995, P NATL ACAD SCI USA, V92, P11534, DOI 10.1073/pnas.92.25.11534
   BROWN HR, 1985, P NATL ACAD SCI USA, V82, P2359, DOI 10.1073/pnas.82.8.2359
   CHO YJ, 1991, P NATL ACAD SCI USA, V88, P10153, DOI 10.1073/pnas.88.22.10153
   DAVIS LA, 1987, DEVELOPMENT, V99, P145
   EPSTEIN HF, 1991, SCIENCE, V251, P1039, DOI 10.1126/science.1998120
   FLEENOR DE, 1992, J MUSCLE RES CELL M, V13, P55, DOI 10.1007/BF01738428
   FORRYSCHAUDIES S, 1990, J MOL BIOL, V211, P321, DOI 10.1016/0022-2836(90)90354-O
   GAUR A, 1995, GENE, V162, P249, DOI 10.1016/0378-1119(95)00348-A
   Gaur A, 1998, BIOCHEM BIOPH RES CO, V245, P746, DOI 10.1006/bbrc.1998.8514
   GOODWIN LO, 1991, J BIOL CHEM, V266, P8408
   GUNNING P, 1990, DEV BIOL, V138, P443, DOI 10.1016/0012-1606(90)90210-A
   HARDY S, 1995, GENE, V156, P265, DOI 10.1016/0378-1119(94)00929-M
   HARDY S, 1991, EUR J BIOCHEM, V202, P431, DOI 10.1111/j.1432-1033.1991.tb16392.x
   HELFMAN DM, 1986, MOL CELL BIOL, V6, P3582, DOI 10.1128/MCB.6.11.3582
   JANCSO A, 1991, J BIOL CHEM, V266, P5891
   LEESMILLER JP, 1991, BIOESSAYS, V13, P429, DOI 10.1002/bies.950130902
   LEESMILLER JP, 1990, J MOL BIOL, V213, P399, DOI 10.1016/S0022-2836(05)80202-5
   LEHRER SS, 1990, J BIOL CHEM, V265, P1134
   LEMANSKI LF, 1973, DEV BIOL, V33, P312, DOI 10.1016/0012-1606(73)90140-1
   Lemanski LF, 1996, BIOCHEM BIOPH RES CO, V229, P974, DOI 10.1006/bbrc.1996.1910
   Lin J J, 1997, Int Rev Cytol, V170, P1, DOI 10.1016/S0074-7696(08)61619-8
   LIN JJC, 1985, J CELL BIOL, V100, P692, DOI 10.1083/jcb.100.3.692
   LUQUE EA, 1994, BIOCHEM BIOPH RES CO, V203, P319, DOI 10.1006/bbrc.1994.2184
   Luque EA, 1997, GENE, V185, P175, DOI 10.1016/S0378-1119(96)00606-3
   MACLEOD AR, 1987, J MOL BIOL, V194, P1, DOI 10.1016/0022-2836(87)90710-8
   MOORE PB, 1982, J MUSCLE RES CELL M, V3, P161, DOI 10.1007/BF00711940
   NEEDLEMAN SB, 1970, J MOL BIOL, V48, P443, DOI 10.1016/0022-2836(70)90057-4
   ORDAHL CP, 1992, CURR TOP DEV BIOL, V26, P145, DOI 10.1016/S0070-2153(08)60444-5
   Pieples K, 2000, BIOCHEMISTRY-US, V39, P8291, DOI 10.1021/bi000047x
   PITTENGER MF, 1994, CURR OPIN CELL BIOL, V6, P96, DOI 10.1016/0955-0674(94)90122-8
   PRASAD GL, 1993, P NATL ACAD SCI USA, V90, P7039, DOI 10.1073/pnas.90.15.7039
   Sambrook J., 1989, Molecular Cloning: A Laboratory Manual, V2nd edn
   SCHEVZOV G, 1993, J CELL BIOL, V121, P811, DOI 10.1083/jcb.121.4.811
   SMILLIE LB, 1979, TRENDS BIOCHEM SCI, V4, P151, DOI 10.1016/0968-0004(79)90003-3
   STARR CM, 1989, J MORPHOL, V201, P1, DOI 10.1002/jmor.1052010102
   Swofford D L., 1991, Phylogenetic analysis using parsimony
   Vize P. D., 1991, METHOD CELL BIOL, V36, P368
   WIECZOREK DF, 1988, MOL CELL BIOL, V8, P679, DOI 10.1128/MCB.8.2.679
   ZACKSON SL, 1986, DEV BIOL, V117, P343
   Zajdel RT, 1998, DEV DYNAM, V213, P412, DOI 10.1002/(SICI)1097-0177(199812)213:4<412::AID-AJA6>3.0.CO;2-C
   Zelphati O, 1996, P NATL ACAD SCI USA, V93, P11493, DOI 10.1073/pnas.93.21.11493
   ZOT AS, 1987, ANNU REV BIOPHYS BIO, V16, P535
NR 44
TC 22
Z9 22
U1 0
U2 3
PU WILEY-LISS
PI NEW YORK
PA DIV JOHN WILEY & SONS INC, 605 THIRD AVE, NEW YORK, NY 10158-0012 USA
SN 0730-2312
J9 J CELL BIOCHEM
JI J. Cell. Biochem.
PY 2002
VL 85
IS 4
BP 747
EP 761
DI 10.1002/jcb.10178
PG 15
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA 548RX
UT WOS:000175404400010
PM 11968015
OA Bronze
DA 2025-04-10
ER

PT J
AU Yan, JM
   Zhang, WK
   Li, F
   Zhou, CM
   Yu, XJ
AF Yan, Jia-min
   Zhang, Wen-kang
   Li, Fei
   Zhou, Chuan-min
   Yu, Xue-jie
TI Integrated transcriptome profiling in THP-1 macrophages infected with
   bunyavirus SFTSV
SO VIRUS RESEARCH
LA English
DT Article
DE SFTSV; RNA-seq; lncRNAs; Transcription factors; Alternative splicing
ID THROMBOCYTOPENIA SYNDROME VIRUS; LONG NONCODING RNAS; SEVERE FEVER;
   GENE; PROTEIN; IDENTIFICATION; SUPPRESSION; EXPRESSION; REGULATORS;
   SCREEN
AB Severe fever with thrombocytopenia syndrome virus (SFTSV) is a tick-borne bunyavirus that causes an emerging hemorrhagic fever termed SFTS with high mortality. However, knowledge of SFTSV-host interactions is largely limited. Here, we performed a global transcriptome analysis of mRNAs and lncRNAs in THP-1 macrophages infected with SFTSV for 24 and 48 h. A total of 2,334 differentially expressed mRNAs and 154 differentially expressed lncRNAs were identified with 577 mRNAs and 31 lncRNAs commonly changed at both time points. Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis revealed that differentially expressed mRNAs were mainly associated with innate immune, cytokine signaling, systemic lupus erythematosus, and alcoholism. Differentially expressed lncRNAs were enriched in systemic lupus erythematosus, alcoholism, and ribosome. Bioinformatic analysis also revealed hub regulatory mRNAs including IL6, TNF, UBA52, SRC, IL10, CXCL10, and CDK1 and core regulatory lncRNAs including XLOC_083027 and XLOC_113317. Transcription factor analysis of the differentially expressed mRNAs revealed that IRF1, SPI1, SPIB, ELF5, and FEV were enriched during SFTSV infection. Taken together, our studies illustrate the complex interaction between THP-1 macrophages and SFTSV.
C1 [Yan, Jia-min; Zhang, Wen-kang; Zhou, Chuan-min; Yu, Xue-jie] Wuhan Univ, Sch Hlth Sci, State Key Lab Virol, Wuhan 430071, Peoples R China.
   [Li, Fei] Shandong Univ, Sch Publ Hlth, Jinan 250012, Shandong, Peoples R China.
   [Zhou, Chuan-min] Wuhan Univ, Zhongnan Hosp, Wuhan 430071, Peoples R China.
C3 Wuhan University; Shandong University; Wuhan University
RP Zhou, CM; Yu, XJ (corresponding author), Wuhan Univ, Sch Hlth Sci, State Key Lab Virol, Wuhan 430071, Peoples R China.
EM 00033465@whu.edu.cn; yuxuejie@whu.edu.cn
RI Yu, Xuejie/AAP-9246-2021; Zhou, Chuan-min/AAQ-5382-2021; Li,
   Fei/I-8918-2019
OI Zhou, Chuan-min/0000-0002-5975-4603
CR Ashraf U, 2019, TRENDS MICROBIOL, V27, P268, DOI 10.1016/j.tim.2018.11.004
   Boudreault S, 2019, WIRES RNA, V10, DOI 10.1002/wrna.1543
   Calle AS, 2018, CANCER SCI, V109, P2093, DOI 10.1111/cas.13642
   Carpinelli MR, 2004, P NATL ACAD SCI USA, V101, P6553, DOI 10.1073/pnas.0401496101
   Chaudhary V, 2015, J GEN VIROL, V96, P3204, DOI 10.1099/jgv.0.000280
   Choi SJ, 2016, PLOS NEGLECT TROP D, V10, DOI 10.1371/journal.pntd.0005264
   Choi YH, 2019, NAT MICROBIOL, V4, P429, DOI 10.1038/s41564-018-0329-x
   De Maio FA, 2016, PLOS PATHOG, V12, DOI 10.1371/journal.ppat.1005841
   Derrien T, 2012, GENOME RES, V22, P1775, DOI 10.1101/gr.132159.111
   Dykes IM, 2017, GENOM PROTEOM BIOINF, V15, P177, DOI 10.1016/j.gpb.2016.12.005
   Fortes P, 2016, VIRUS RES, V212, P1, DOI 10.1016/j.virusres.2015.10.002
   Fulton DL, 2009, GENOME BIOL, V10, DOI 10.1186/gb-2009-10-3-r29
   Gallant S, 2006, ARCH IMMUNOL THER EX, V54, P149, DOI 10.1007/s00005-006-0017-z
   Guttman M, 2009, NATURE, V458, P223, DOI 10.1038/nature07672
   Hadjicharalambous MR, 2018, FRONT IMMUNOL, V9, DOI 10.3389/fimmu.2018.02906
   Havranek KE, 2019, PLOS ONE, V14, DOI 10.1371/journal.pone.0217497
   Hu BX, 2017, VIROL J, V14, DOI 10.1186/s12985-017-0882-6
   Hu BX, 2016, VIROL J, V13, DOI 10.1186/s12985-016-0592-5
   Huang C, 2018, J PROTEOME RES, V17, P1485, DOI 10.1021/acs.jproteome.7b00828
   Jumaa H, 1997, MOL CELL BIOL, V17, P3116, DOI 10.1128/MCB.17.6.3116
   Kambara H, 2014, NUCLEIC ACIDS RES, V42, P10668, DOI 10.1093/nar/gku713
   Kato H, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0165207
   Khalil J, 2021, MOL CELL BIOL, V41, DOI 10.1128/MCB.00542-20
   Kim KH, 2013, EMERG INFECT DIS, V19, P1892, DOI 10.3201/eid1911.130792
   Kornblihtt AR, 2013, NAT REV MOL CELL BIO, V14, P153, DOI 10.1038/nrm3525
   Kwon AT, 2012, G3-GENES GENOM GENET, V2, P987, DOI 10.1534/g3.112.003202
   Langmead B, 2012, NAT METHODS, V9, P357, DOI [10.1038/NMETH.1923, 10.1038/nmeth.1923]
   Li Y, 2018, VIRUSES-BASEL, V10, DOI 10.3390/v10100556
   Liu SH, 2020, J VIROL, V94, DOI 10.1128/JVI.01575-19
   Long JC, 2009, BIOCHEM J, V417, P15, DOI 10.1042/BJ20081501
   Luo LM, 2015, EMERG INFECT DIS, V21, P1770, DOI 10.3201/eid2110.150126
   Meng K, 2015, PARASITOL RES, V114, P4703, DOI 10.1007/s00436-015-4718-2
   Meng XY, 2017, FRONT IMMUNOL, V8, DOI 10.3389/fimmu.2017.01663
   Mor A, 2016, NAT MICROBIOL, V1, DOI [10.1038/NMICROBIOL.2016.69, 10.1038/nmicrobiol.2016.69]
   More S, 2019, RNA BIOL, V16, P340, DOI 10.1080/15476286.2019.1572448
   Nakata Y, 2007, MOL CELL BIOL, V27, P2048, DOI 10.1128/MCB.01100-06
   Oh SS, 2016, VECTOR-BORNE ZOONOT, V16, P408, DOI 10.1089/vbz.2015.1848
   Ouyang J, 2014, CELL HOST MICROBE, V16, P616, DOI 10.1016/j.chom.2014.10.001
   Panda D, 2019, FRONT IMMUNOL, V10, DOI 10.3389/fimmu.2019.01019
   Panda D, 2013, CELL REP, V5, P1737, DOI 10.1016/j.celrep.2013.11.028
   Pertea M, 2016, NAT PROTOC, V11, P1650, DOI 10.1038/nprot.2016.095
   Pinkham C, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-14800-3
   Qiu LP, 2018, FRONT MICROBIOL, V9, DOI 10.3389/fmicb.2018.01621
   Schmitt AM, 2016, CANCER CELL, V29, P452, DOI 10.1016/j.ccell.2016.03.010
   Shultz DB, 2009, J INTERF CYTOK RES, V29, P817, DOI 10.1089/jir.2009.0034
   Song PX, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-06921-6
   Stoilov P, 2004, HUM MOL GENET, V13, P509, DOI 10.1093/hmg/ddh051
   Sun JM, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-08042-6
   Sun YL, 2012, J INFECT DIS, V206, P1085, DOI 10.1093/infdis/jis452
   Takahashi T, 2014, J INFECT DIS, V209, P816, DOI 10.1093/infdis/jit603
   Thompson MG, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-04779-4
   Wang P, 2019, FRONT IMMUNOL, V9, DOI 10.3389/fimmu.2018.03138
   Wang ZQ, 2017, CELL MOL LIFE SCI, V74, P1117, DOI 10.1007/s00018-016-2398-4
   Xie C, 2011, NUCLEIC ACIDS RES, V39, pW316, DOI 10.1093/nar/gkr483
   Young MD, 2010, GENOME BIOL, V11, DOI 10.1186/gb-2010-11-2-r14
   Yu XJ, 2011, NEW ENGL J MED, V364, P1523, DOI 10.1056/NEJMoa1010095
   Zhan JB, 2017, VIROL SIN, V32, P51, DOI 10.1007/s12250-016-3931-1
   Zhang L, 2019, FRONT IMMUNOL, V10, DOI 10.3389/fimmu.2019.01095
   Zhang Q, 2016, GENE, V594, P144, DOI 10.1016/j.gene.2016.09.014
   Zhang Q, 2013, MBIO, V4, DOI 10.1128/mBio.00596-12
   Zheng XY, 2017, FRONT IMMUNOL, V7, DOI 10.3389/fimmu.2016.00535
NR 61
TC 5
Z9 7
U1 4
U2 17
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
SN 0168-1702
EI 1872-7492
J9 VIRUS RES
JI Virus Res.
PD DEC
PY 2021
VL 306
AR 198594
DI 10.1016/j.virusres.2021.198594
EA OCT 2021
PG 13
WC Virology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Virology
GA WP7AI
UT WOS:000713279300003
PM 34637813
DA 2025-04-10
ER

PT J
AU Couzi, L
   Contin-Bordes, C
   Marliot, F
   Sarrat, A
   Grimal, P
   Moreau, JF
   Merville, P
   Fremeaux-Bacchi, V
AF Couzi, Lionel
   Contin-Bordes, Cecile
   Marliot, Florence
   Sarrat, Anne
   Grimal, Pierre
   Moreau, Jean-Francois
   Merville, Pierre
   Fremeaux-Bacchi, Veronique
TI Inherited deficiency of membrane cofactor protein expression and varying
   manifestations of recurrent atypical hemolytic uremic syndrome in a
   sibling pair
SO AMERICAN JOURNAL OF KIDNEY DISEASES
LA English
DT Article
DE complement; atypical hemolytic and uremic syndrome; membrane cofactor
   protein; MCP; CD46; homozygous null mutation
ID COMPLEMENT REGULATOR; MUTATIONS; CD46; PREDISPOSITION; GENES; MCP
AB Atypical hemolytic uremic syndrome (aHUS) is a rare thrombotic microangiopathic disorder that may be familial or sporadic. Complement factor H (CFH), factor I, and membrane cofactor protein (MCP; CD46), 3 regulators of the alternative pathway of the complement system activation, have been implicated in this pathological state. To date, 29 different mutations of CD46 have been reported, with incomplete penetrance and better clinical outcome compared with CFH mutations. Of those mutations, only 6 were found to be homozygous (accounting for 8 patients), and 5 resulted in a lack of or dramatically decreased cell-surface CD46 expression. We report here the seventh patient with a null mutation associated with recurrent aHUS. This mutation, a guanine to cytosine substitution in the first nucleotide of intron 2, disrupts a splice donor site. Interestingly, the patient's disease-free sister showed the same homozygous mutation. Extensive analysis of other complement regulatory protein- and polymorphism-associated risk factors did not uncover a difference between the patient and his sister. In conclusion, we describe for the first time a disease-free individual with complete CD46 deficiency, confirming the extremely variable penetrance and genetic complexity of aHUS.
C1 [Couzi, Lionel; Contin-Bordes, Cecile; Moreau, Jean-Francois; Merville, Pierre] CNRS, UMR 5164, F-33076 Bordeaux, France.
   [Couzi, Lionel; Contin-Bordes, Cecile; Sarrat, Anne; Moreau, Jean-Francois; Merville, Pierre] Hop Pellegrin, CHU Bordeaux, F-33076 Bordeaux, France.
   [Couzi, Lionel; Contin-Bordes, Cecile; Moreau, Jean-Francois; Merville, Pierre] Univ Bordeaux 2, F-33076 Bordeaux, France.
   [Marliot, Florence; Fremeaux-Bacchi, Veronique] Hop Europeen Georges Pompidou, AP HP, Paris, France.
   [Grimal, Pierre] Ctr Hosp Cote Basque, Bayonne, France.
C3 Centre National de la Recherche Scientifique (CNRS); CNRS - National
   Institute for Biology (INSB); Universite de Bordeaux; Universite de
   Bordeaux; CHU Bordeaux; Universite de Bordeaux; Assistance Publique
   Hopitaux Paris (APHP); Universite Paris Cite; Hopital Universitaire
   Europeen Georges-Pompidou - APHP
RP Couzi, L (corresponding author), CNRS, UMR 5164, 146 Rue Leo Saignat, F-33076 Bordeaux, France.
EM lionel.couzi@u-bordeaux2.fr
RI contin-bordes, cecile/KCZ-2603-2024; DEBACK, Claire/GQP-1022-2022
CR Caprioli J, 2006, BLOOD, V108, P1267, DOI 10.1182/blood-2005-10-007252
   de Jorge EG, 2007, P NATL ACAD SCI USA, V104, P240, DOI 10.1073/pnas.0603420103
   Dragon-Durey MA, 2005, SPRINGER SEMIN IMMUN, V27, P359, DOI 10.1007/s00281-005-0003-2
   Dragon-Durey MA, 2004, J AM SOC NEPHROL, V15, P787, DOI 10.1097/01.ASN.0000115702.28859.A7
   Esparza-Gordillo J, 2006, MOL IMMUNOL, V43, P1769, DOI 10.1016/j.molimm.2005.11.008
   Esparza-Gordillo J, 2005, HUM MOL GENET, V14, P703, DOI 10.1093/hmg/ddi066
   Fremeaux-Bacchi V, 2007, AM J KIDNEY DIS, V49, P323, DOI 10.1053/j.ajkd.2006.10.022
   Fremeaux-Bacchi V, 2006, J AM SOC NEPHROL, V17, P2017, DOI 10.1681/ASN.2005101051
   NAKANISHI I, 1994, EUR J IMMUNOL, V24, P1529, DOI 10.1002/eji.1830240711
   Nangaku M, 1998, KIDNEY INT, V54, P1419, DOI 10.1046/j.1523-1755.1998.00130.x
   Richards A, 2003, P NATL ACAD SCI USA, V100, P12966, DOI 10.1073/pnas.2135497100
   Richards A, 2007, MOL IMMUNOL, V44, P111, DOI 10.1016/j.molimm.2006.07.004
   Zipfel PF, 2007, PLOS GENET, V3, P387, DOI 10.1371/journal.pgen.0030041
NR 13
TC 19
Z9 20
U1 0
U2 2
PU W B SAUNDERS CO-ELSEVIER INC
PI PHILADELPHIA
PA 1600 JOHN F KENNEDY BOULEVARD, STE 1800, PHILADELPHIA, PA 19103-2899 USA
SN 0272-6386
J9 AM J KIDNEY DIS
JI Am. J. Kidney Dis.
PD AUG
PY 2008
VL 52
IS 2
BP E5
EP E9
DI 10.1053/j.ajkd.2008.02.359
PG 5
WC Urology & Nephrology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Urology & Nephrology
GA 330LR
UT WOS:000257943400029
PM 18514989
DA 2025-04-10
ER

PT J
AU Novotny, J
   Svoboda, P
AF Novotny, J
   Svoboda, P
TI The long (Gsα-L) and short (Gsα-S) variants of the
   stimulatory guanine nucleotide-binding protein.: Do they behave in an
   identical way?
SO JOURNAL OF MOLECULAR ENDOCRINOLOGY
LA English
DT Review
ID BROWN-ADIPOSE-TISSUE; BETA-ADRENERGIC RECEPTORS; ADENYLYL-CYCLASE
   ACTIVITY; MESSENGER-RIBONUCLEIC-ACID; SPONTANEOUSLY HYPERTENSIVE RATS;
   SIGNAL TRANSDUCTION PROTEIN; ALPHA-SUBUNIT LEVELS; S49 LYMPHOMA-CELLS;
   GS-ALPHA; DOWN-REGULATION
AB The relative proportions and tissue distribution of the long (G(s alpha-L)) and short (G(s alpha-S)) variants of the alpha subunit of the stimulatory G-protein (G,,) change under a wide range of metabolic conditions, such as cellular differentiation, ontogenetic development, ageing and various adaptive processes. Although the two variants of G(s alpha) are generally regarded to be functionally identical, this review summarizes recent experimental support for the non-identical behaviour of these proteins. Similarly, there is no consistent evidence for the functional meaning of these changes as far as regulation of adenylate cyclase activity is concerned. Since it is hard to believe that the complicated scheme of alternative splicing and the energy-consuming synthesis of proteins would be performed for no reason, it is suggested that G(s alpha) variants might be involved in controlling other effector molecules and processes besides adenylate cyclase and cAMP metabolism. Such an idea is indirectly supported by specific alterations in the G(s alpha-L)/G(s alpha-S) ratio under various physiological and pathophysiological conditions.
C1 Acad Sci Czech Republ, Inst Physiol, CR-14220 Prague 4, Czech Republic.
C3 Czech Academy of Sciences; Institute of Physiology of the Czech Academy
   of Sciences
RP Svoboda, P (corresponding author), Acad Sci Czech Republ, Inst Physiol, Videnska 1083, CR-14220 Prague 4, Czech Republic.
RI Svoboda, Petr/C-2619-2012; Novotny, Jiri/B-2163-2012
OI Svoboda, Petr/0000-0002-3076-4672; Novotny, Jiri/0000-0002-6372-0131
CR ADIE EJ, 1994, BIOCHEM J, V300, P709, DOI 10.1042/bj3000709
   ADIE EJ, 1992, BIOCHEM J, V285, P529, DOI 10.1042/bj2850529
   ALI IU, 1992, NUCLEIC ACIDS RES, V20, P4263, DOI 10.1093/nar/20.16.4263
   BEGINHEICK N, 1990, BIOCHEM J, V268, P83, DOI 10.1042/bj2680083
   BeginHeick N, 1996, INT J OBESITY, V20, pS32
   BEGINHEICK N, 1992, AM J PHYSIOL, V263, pC121, DOI 10.1152/ajpcell.1992.263.1.C121
   BIRNBAUMER L, 1990, BIOCHIM BIOPHYS ACTA, V1031, P163, DOI 10.1016/0304-4157(90)90007-Y
   Bourgeois C, 1996, J MOL CELL CARDIOL, V28, P1009, DOI 10.1006/jmcc.1996.0094
   BRAY P, 1986, P NATL ACAD SCI USA, V83, P8893, DOI 10.1073/pnas.83.23.8893
   CHAUDHRY A, 1991, AM J PHYSIOL, V261, pR403, DOI 10.1152/ajpregu.1991.261.2.R403
   COOPER DMF, 1990, BRAIN RES, V523, P143, DOI 10.1016/0006-8993(90)91648-Z
   COWBURN RF, 1994, BRAIN RES, V633, P297, DOI 10.1016/0006-8993(94)91552-0
   CRAWFORD JA, 1993, J BIOL CHEM, V268, P9879
   CUSSAC D, 1990, NEUROENDOCRINOL S1, V52, pP3
   DenisHenriot D, 1996, CELL SIGNAL, V8, P225, DOI 10.1016/0898-6568(95)02058-6
   ElJamali A, 1996, J NEUROCHEM, V67, P2532
   EUROPEFINNER GN, 1993, ENDOCRINOLOGY, V132, P2484, DOI 10.1210/en.132.6.2484
   EUROPEFINNER GN, 1994, J CLIN ENDOCR METAB, V79, P1835, DOI 10.1210/jc.79.6.1835
   EuropeFinner GN, 1996, J CLIN ENDOCR METAB, V81, P1069, DOI 10.1210/jc.81.3.1069
   EVANS T, 1986, J BIOL CHEM, V261, P7052
   FEINSTEIN DL, 1992, GLIA, V5, P139, DOI 10.1002/glia.440050208
   FELDMAN AM, 1990, CIRCULATION, V81, P1341, DOI 10.1161/01.CIR.81.4.1341
   FOSTER KA, 1990, AM J PHYSIOL, V259, pH432, DOI 10.1152/ajpheart.1990.259.2.H432
   FREISSMUTH M, 1991, P NATL ACAD SCI USA, V88, P8548, DOI 10.1073/pnas.88.19.8548
   GILMAN AG, 1987, ANNU REV BIOCHEM, V56, P615, DOI 10.1146/annurev.biochem.56.1.615
   GRANNEMAN JG, 1990, J NEUROCHEM, V54, P1995, DOI 10.1111/j.1471-4159.1990.tb04903.x
   GRANNEMAN JG, 1990, ENDOCRINOLOGY, V127, P1596, DOI 10.1210/endo-127-4-1596
   GRANNEMAN JG, 1989, ENDOCRINOLOGY, V125, P2328, DOI 10.1210/endo-125-5-2328
   GRAZIANO MP, 1987, J BIOL CHEM, V262, P11375
   GRAZIANO MP, 1989, J BIOL CHEM, V264, P409
   GREEN A, 1989, BIOCHEM J, V258, P607, DOI 10.1042/bj2580607
   HABECKER BA, 1993, J NEUROCHEM, V61, P712
   Helmreich EJM, 1996, BBA-REV BIOMEMBRANES, V1286, P285, DOI 10.1016/S0304-4157(96)00013-5
   ISHIKAWA Y, 1990, J BIOL CHEM, V265, P8458
   JOHNSON MD, 1995, J GERONTOL A-BIOL, V50, pB14, DOI 10.1093/gerona/50A.1.B14
   JONES DT, 1989, SCIENCE, V244, P790, DOI 10.1126/science.2499043
   JONES DT, 1990, J BIOL CHEM, V265, P2671
   JONES DT, 1987, J BIOL CHEM, V262, P14241
   Kawai Y, 1996, J MOL CELL CARDIOL, V28, P1555, DOI 10.1006/jmcc.1996.0146
   KAWAI Y, 1991, BIOCHEM J, V274, P439, DOI 10.1042/bj2740439
   KEHLENBACH RH, 1994, NATURE, V372, P804
   KILGOUR E, 1993, FEBS LETT, V328, P271, DOI 10.1016/0014-5793(93)80942-N
   KITAMURA Y, 1989, J NEUROCHEM, V53, P249, DOI 10.1111/j.1471-4159.1989.tb07321.x
   KOZASA T, 1988, P NATL ACAD SCI USA, V85, P2081, DOI 10.1073/pnas.85.7.2081
   KVAPIL P, 1995, LIFE SCI, V57, P311, DOI 10.1016/0024-3205(95)00289-I
   KVAPIL P, 1994, EUR J BIOCHEM, V226, P193, DOI 10.1111/j.1432-1033.1994.tb20041.x
   KVAPIL P, 1995, FASEB J, V9, pA1411
   LARNER AC, 1981, J BIOL CHEM, V256, P9551
   LEVIS MJ, 1992, J CELL BIOL, V119, P1297, DOI 10.1083/jcb.119.5.1297
   Malbon CC, 1997, BIOCHEM PHARMACOL, V53, P1, DOI 10.1016/S0006-2952(96)00662-4
   MATTERA R, 1989, SCIENCE, V243, P804, DOI 10.1126/science.2536957
   MCFARLANEANDERSON N, 1992, BIOCHEM J, V282, P15, DOI 10.1042/bj2820015
   MCKENZIE FR, 1990, J BIOL CHEM, V265, P17084
   MICHEL MC, 1993, HYPERTENSION, V22, P169, DOI 10.1161/01.HYP.22.2.169
   MICHEL MC, 1994, HYPERTENSION, V23, P653, DOI 10.1161/01.HYP.23.5.653
   MILLIGAN G, 1993, TRENDS PHARMACOL SCI, V14, P413, DOI 10.1016/0165-6147(93)90064-Q
   MILLIGAN G, 1990, G PROTEINS MEDIATORS, P31
   MITCHELL FM, 1993, BIOCHEM J, V293, P495, DOI 10.1042/bj2930495
   MIYAMOTO A, 1994, EUR J PHARM-MOLEC PH, V266, P147, DOI 10.1016/0922-4106(94)90104-X
   MONTEITH MS, 1995, CLIN SCI, V89, P487, DOI 10.1042/cs0890487
   MUMBY SM, 1986, P NATL ACAD SCI USA, V83, P265, DOI 10.1073/pnas.83.2.265
   Nedergaard J., 1986, BROWN ADIPOSE TISSUE, P152
   NEGISHI M, 1992, J BIOL CHEM, V267, P2364
   NORTHUP JK, 1980, P NATL ACAD SCI-BIOL, V77, P6516, DOI 10.1073/pnas.77.11.6516
   OBREGON MJ, 1989, BIOCHEM J, V259, P341, DOI 10.1042/bj2590341
   ODONNELL JK, 1991, MOL PHARMACOL, V39, P702
   OZAWA H, 1993, BRAIN RES, V620, P174, DOI 10.1016/0006-8993(93)90289-Y
   PACE U, 1986, P NATL ACAD SCI USA, V83, P4947, DOI 10.1073/pnas.83.13.4947
   PALMER TM, 1991, BIOCHIM BIOPHYS ACTA, V1097, P193, DOI 10.1016/0925-4439(91)90035-8
   QUAN F, 1991, P NATL ACAD SCI USA, V88, P1898, DOI 10.1073/pnas.88.5.1898
   RIUS RA, 1991, FEBS LETT, V288, P51, DOI 10.1016/0014-5793(91)81001-O
   ROBISHAW JD, 1986, P NATL ACAD SCI USA, V83, P1251, DOI 10.1073/pnas.83.5.1251
   RUBENSTEIN RC, 1991, BIOCHEMISTRY-US, V30, P10769, DOI 10.1021/bi00108a023
   SCHERER NM, 1987, ARCH BIOCHEM BIOPHYS, V259, P431, DOI 10.1016/0003-9861(87)90509-1
   SCHUBERT B, 1989, SCIENCE, V245, P516, DOI 10.1126/science.2547248
   SETHI R, 1993, MOL CELL BIOCHEM, V119, P185, DOI 10.1007/BF00926870
   SHU Y, 1994, J CARDIOVASC PHARM, V23, P188, DOI 10.1097/00005344-199402000-00003
   STERNWEIS PC, 1981, J BIOL CHEM, V256, P1517
   STRASSHEIM D, 1991, BIOCHEM J, V276, P197, DOI 10.1042/bj2760197
   SVOBODA P, 1993, BIOCHEM J, V295, P655, DOI 10.1042/bj2950655
   Svoboda P, 1996, MOL PHARMACOL, V49, P646
   SVOBODA P, 1996, BIOCHEM J, V313, P761
   SWAROOP A, 1991, NUCLEIC ACIDS RES, V19, P4725, DOI 10.1093/nar/19.17.4725
   TorresMarquez ME, 1996, COMP BIOCHEM PHYS C, V115, P233, DOI 10.1016/S0742-8413(96)00105-3
   URASAWA K, 1991, JPN CIRC J, V55, P676, DOI 10.1253/jcj.55.676
   VEDIA LMY, 1989, BIOCHEM J, V261, P841, DOI 10.1042/bj2610841
   VIOLLET C, 1994, J NEUROCHEM, V63, P2231
   WALSETH TF, 1989, J BIOL CHEM, V264, P21106
   WAND GS, 1991, ALCOHOL CLIN EXP RES, V15, P705, DOI 10.1111/j.1530-0277.1991.tb00583.x
   Wang HY, 1996, INT J OBESITY, V20, pS26
   WATKINS DC, 1989, BIOCHEM BIOPH RES CO, V165, P929, DOI 10.1016/0006-291X(89)92692-2
   WATKINS DC, 1987, J BIOL CHEM, V262, P10651
   WATKINS PA, 1982, J BIOL CHEM, V257, P4719
   YAGAMI T, 1995, MOL PHARMACOL, V48, P849
   YAGAMI T, 1994, BBA-MOL CELL RES, V1222, P81, DOI 10.1016/0167-4889(94)90027-2
   YOUNG LT, 1991, DEV BRAIN RES, V61, P243
   YOUNG LT, 1991, BRAIN RES, V553, P323, DOI 10.1016/0006-8993(91)90843-K
NR 97
TC 36
Z9 40
U1 0
U2 3
PU J ENDOCRINOLOGY LTD
PI BRISTOL
PA 17/18 THE COURTYARD, WOODLANDS, ALMONDSBURY, BRISTOL BS12 4NQ, ENGLAND
SN 0952-5041
J9 J MOL ENDOCRINOL
JI J. Mol. Endocrinol.
PD APR
PY 1998
VL 20
IS 2
BP 163
EP 173
DI 10.1677/jme.0.0200163
PG 11
WC Endocrinology & Metabolism
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism
GA ZH262
UT WOS:000073089500001
PM 9584831
OA Bronze
DA 2025-04-10
ER

PT J
AU Magnani, E
   Farnetti, E
   Nicoli, D
   Casali, B
   Savoldi, L
   Focaccetti, C
   Boni, C
   Albini, A
   Banzi, M
AF Magnani, Elena
   Farnetti, Enrico
   Nicoli, Davide
   Casali, Bruno
   Savoldi, Luisa
   Focaccetti, Chiara
   Boni, Corrado
   Albini, Adriana
   Banzi, Maria
TI Fluoropyrimidine toxicity in patients with dihydropyrimidine
   dehydrogenase splice site variant: the need for further revision of dose
   and schedule
SO INTERNAL AND EMERGENCY MEDICINE
LA English
DT Article
DE Dihydropyrimidine dehydrogenase (DPD); Tumors; Fluoropyrimidine
   chemotherapy; Toxicity; Dose reduction
ID SEVERE 5-FLUOROURACIL-ASSOCIATED TOXICITY; CARDIO-ONCOLOGY;
   IVS14+1G-GREATER-THAN-A MUTATION; COLORECTAL-CARCINOMA; DPD DEFICIENCY;
   POINT MUTATION; DONOR SITE; THERAPY; GENE; CARDIOTOXICITY
AB Dihydropyrimidine dehydrogenase (DPD) is a key enzyme in the metabolic catabolism of 5-fluorouracil (5-FU) and its derivatives (capecitabine and tegafur). Complete or partial deficiency of DPD activity has been demonstrated to induce severe toxicities in cancer patients treated with fluoropyrimidine therapy. We analyzed 180 individuals that were candidates for a treatment with 5-FU class drugs for the most common DPD mutation, IVS14+1G > A, and detected four heterozygous patients. We recorded the toxicities for all 180 individuals after the first two chemotherapy cycles and found that three of the four patients, although they were treated with a dose reduction in 50 % on the basis of the genetic analysis, all showed severe toxicities that resulted in hospitalization of patient and premature discontinuation of treatment. One patient with mutated DPD was not treated with chemotherapy upon the clinician's decision because of his DPD mutated genotype and the presence of microsatellite instability. Our data suggest that greater dose reductions or alternative therapies are needed for patients with DPD IVS14+1G > A mutations.
C1 [Magnani, Elena; Boni, Corrado; Banzi, Maria] Azienda Osped ASMN, Dept Med Oncol, IRCCS, I-42123 Reggio Emilia, Italy.
   [Farnetti, Enrico; Nicoli, Davide; Casali, Bruno] Azienda Osped ASMN, Mol Biol Lab, IRCCS, I-42123 Reggio Emilia, Italy.
   [Savoldi, Luisa; Albini, Adriana] Azienda Osped ASMN, Res & Stat Dept, IRCCS, I-42123 Reggio Emilia, Italy.
   [Focaccetti, Chiara] IRCCS MultiMed, Sci & Technol Pole, Milan, Italy.
C3 IRCCS Arcispedale S. Maria Nuova; IRCCS Arcispedale S. Maria Nuova;
   IRCCS Arcispedale S. Maria Nuova; IRCCS Multimedica
RP Albini, A (corresponding author), Azienda Osped ASMN, Res & Stat Dept, IRCCS, Viale Umberto 1 50, I-42123 Reggio Emilia, Italy.
EM albini.adriana@asmn.re.it
RI Farnetti, Enrico/AAM-1371-2020; Focaccetti, Chiara/AAD-9378-2019; banzi,
   maria/AAC-2193-2020; Nicoli, Davide/V-6735-2018; Albini,
   Adriana/HLH-6147-2023
OI Banzi, Maria/0000-0001-8860-2660; Nicoli, Davide/0000-0002-1662-0103;
   Focaccetti, Chiara/0000-0002-7334-3966; Farnetti,
   Enrico/0000-0002-7858-1867; Albini, Adriana/0000-0002-9624-5103
FU Multimedica Onlus Italy; MIUR Grande Progetto Strategico [GPS DM28938];
   Associazione Italiana per la Ricerca sul Cancro Funding Source: Custom
FX We thank all the Patients involved in the study, at the Azienda
   Ospedaliera ASMN, Istituto di Ricovero e Cura a Carattere Scientifico of
   Reggio Emilia that have made this project possible. The authors also
   thank Professor Douglas Noonan (University of Insubria, Varese) that
   provided medical writing assistance and Loretta Fornaciari for
   laboratory technical support. We acknowledge AIRC (Assciazione Italiana
   Ricerca sul Cancro) to AA. Multimedica Onlus Italy and the MIUR Grande
   Progetto Strategico GPS DM28938 for support.
CR Albini A, 2012, INTERN EMERG MED, V7, P399, DOI 10.1007/s11739-012-0845-2
   Albini A, 2010, JNCI-J NATL CANCER I, V102, P14, DOI 10.1093/jnci/djp440
   Amstutz U, 2011, PHARMACOGENOMICS, V12, P1321, DOI [10.2217/PGS.11.72, 10.2217/pgs.11.72]
   DIASIO RB, 1994, J CLIN ONCOL, V12, P2239, DOI 10.1200/JCO.1994.12.11.2239
   Haller DG, 2008, J CLIN ONCOL, V26, P4544, DOI 10.1200/JCO.2008.17.1249
   MEINSMA R, 1995, DNA CELL BIOL, V14, P1, DOI 10.1089/dna.1995.14.1
   Mercier C, 2006, CLIN COLORECTAL CANC, V6, P288, DOI 10.3816/CCC.2006.n.047
   Molteni LP, 2012, BREAST J S1, V16, pS45
   NAGUIB FNM, 1985, CANCER RES, V45, P5405
   Omura Kenji, 2003, Int J Clin Oncol, V8, P132, DOI 10.1007/s10147-003-0330-z
   Punt CJA, 1998, CANCER-AM CANCER SOC, V83, P679, DOI 10.1002/(SICI)1097-0142(19980815)83:4<679::AID-CNCR8>3.0.CO;2-F
   Raschi E, 2012, INTERN EMERG MED, V7, P113, DOI 10.1007/s11739-011-0744-y
   Saif AW, 2006, CLIN COLORECTAL CANC, V5, P359, DOI 10.3816/CCC.2006.n.007
   Saif MW, 2009, JNCI-J NATL CANCER I, V101, P1543, DOI 10.1093/jnci/djp328
   Swen JJ, CLIN PHARM THER, V89, P662
   van Kuilenburg ABP, 2004, EUR J CANCER, V40, P939, DOI 10.1016/j.ejca.2003.12.004
   Van Kuilenburg ABP, 1998, ADV EXP MED BIOL, V431, P293
   van Kuilenburg ABP, 2002, PHARMACOGENETICS, V12, P555, DOI 10.1097/00008571-200210000-00007
   van Kuilenburg ABP, 2001, CLIN CANCER RES, V7, P1149
   van Kuilenburg ABP, 2000, CLIN CANCER RES, V6, P4705
   van Kuilenburg ABP, 2010, HUM GENET, V128, P529, DOI 10.1007/s00439-010-0879-3
   Vreken P, 1997, J INHERIT METAB DIS, V20, P335, DOI 10.1023/A:1005357307122
   Vreken P, 1996, J INHERIT METAB DIS, V19, P645, DOI 10.1007/BF01799841
   Wei XX, 1996, J CLIN INVEST, V98, P610, DOI 10.1172/JCI118830
   Yang CG, CANC CHEMOTHER PHARM, V67, P49
NR 25
TC 14
Z9 15
U1 0
U2 5
PU SPRINGER-VERLAG ITALIA SRL
PI MILAN
PA VIA DECEMBRIO, 28, MILAN, 20137, ITALY
SN 1828-0447
EI 1970-9366
J9 INTERN EMERG MED
JI Intern. Emerg. Med.
PD AUG
PY 2013
VL 8
IS 5
BP 417
EP 423
DI 10.1007/s11739-013-0936-8
PG 7
WC Medicine, General & Internal
WE Science Citation Index Expanded (SCI-EXPANDED)
SC General & Internal Medicine
GA 185LP
UT WOS:000321969700009
PM 23585145
DA 2025-04-10
ER

PT J
AU Zheng, XX
   Diktonaite, K
   Qiu, HY
AF Zheng, Xiaoxu
   Diktonaite, Kotryna
   Qiu, Hongyu
TI Epigenetic Reader Bromodomain-Containing Protein 4 in Aging-Related
   Vascular Pathologies and Diseases: Molecular Basis, Functional
   Relevance, and Clinical Potential
SO BIOMOLECULES
LA English
DT Review
DE aging; bromodomain-containing protein 4; epigenetic; vascular function;
   diseases
ID HISTONE ACETYLTRANSFERASE; AORTIC STIFFNESS; P-TEFB; BRD4; BET;
   INHIBITION; EXPRESSION; IDENTIFICATION; HYPERTENSION; RECOGNITION
AB Aging is a key independent risk factor of various vascular diseases, for which the regulatory mechanisms remain largely unknown. Bromodomain-containing protein 4 (BRD4) is a member of the Bromodomain and Extra-Terminal domain (BET) family and is an epigenetic reader playing diverse roles in regulating transcriptional elongation, chromatin remodeling, DNA damage response, and alternative splicing in various cells and tissues. While BRD4 was initially recognized for its involvement in cancer progression, recent studies have revealed that the aberrant expression and impaired function of BRD4 were highly associated with aging-related vascular pathology, affecting multiple key biological processes in the vascular cells and tissues, providing new insights into the understanding of vascular pathophysiology and pathogenesis of vascular diseases. This review summarizes the recent advances in BRD4 biological function, and the progression of the studies related to BRD4 in aging-associated vascular pathologies and diseases, including atherosclerosis, aortic aneurism vascular neointima formation, pulmonary hypertension, and essential hypertension, providing updated information to advance our understanding of the epigenetic mechanisms in vascular diseases during aging and paving the way for future research and therapeutic approaches.
C1 [Zheng, Xiaoxu; Diktonaite, Kotryna; Qiu, Hongyu] Georgia State Univ, Inst Biomed Sci, Ctr Mol & Translat Med, Atlanta, GA 30303 USA.
   [Qiu, Hongyu] Univ Arizona, Coll Med Phoenix, Translat Cardiovasc Res Ctr, Dept Internal Med, Phoenix, AZ 85004 USA.
C3 University System of Georgia; Georgia State University; University of
   Arizona
RP Qiu, HY (corresponding author), Georgia State Univ, Inst Biomed Sci, Ctr Mol & Translat Med, Atlanta, GA 30303 USA.
EM zhengxiaoxu.pku@gmail.com; kdiktonaite1@student.gsu.edu;
   hqiu@arizona.edu
OI Diktonaite, Kotryna/0009-0008-2374-3436
FU NIH [HL115195-01, HL137962, HL142291]
FX This work is partially supported by NIH grants HL115195-01 (H.Q.),
   HL137962 (H.Q.), and HL142291 (H.Q).
CR Alexander MR, 2012, J CLIN INVEST, V122, P70, DOI 10.1172/JCI43713
   Andrieu Guillaume, 2016, Drug Discov Today Technol, V19, P45, DOI 10.1016/j.ddtec.2016.06.004
   Brown JD, 2018, P NATL ACAD SCI USA, V115, P2144, DOI 10.1073/pnas.1711155115
   Brown JD, 2014, MOL CELL, V56, P219, DOI 10.1016/j.molcel.2014.08.024
   Cheung KL, 2021, FRONT MOL BIOSCI, V8, DOI 10.3389/fmolb.2021.728777
   Crowe BL, 2016, P NATL ACAD SCI USA, V113, P2086, DOI 10.1073/pnas.1516813113
   Dai ZY, 2019, AM J RESP CRIT CARE, V200, P806, DOI 10.1164/rccm.201904-0877ED
   Das S, 2017, NAT COMMUN, V8, DOI 10.1038/s41467-017-01629-7
   Devaiah BN, 2016, J LEUKOCYTE BIOL, V100, P679, DOI 10.1189/jlb.2RI0616-250R
   Devaiah BN, 2016, NAT STRUCT MOL BIOL, V23, P540, DOI 10.1038/nsmb.3228
   Dhalluin C, 1999, NATURE, V399, P491, DOI 10.1038/20974
   Drumond-Bock AL, 2021, MOL CANCER, V20, DOI 10.1186/s12943-021-01424-5
   Duan Q, 2016, INT J CARDIOL, V223, P428, DOI 10.1016/j.ijcard.2016.08.238
   Faggion Vinholo Thais, 2019, Aorta (Stamford), V7, P99, DOI 10.1055/s-0039-3400233
   Fernandez P, 2014, CELL REP, V9, P248, DOI 10.1016/j.celrep.2014.08.069
   Filippakopoulos P, 2012, CELL, V149, P214, DOI 10.1016/j.cell.2012.02.013
   Houzelstein D, 2002, MOL CELL BIOL, V22, P3794, DOI 10.1128/MCB.22.11.3794-3802.2002
   Ijaz T, 2021, INT J MOL SCI, V22, DOI 10.3390/ijms22116059
   Itzen F, 2014, NUCLEIC ACIDS RES, V42, P7577, DOI 10.1093/nar/gku449
   Jones MH, 1997, GENOMICS, V45, P529, DOI 10.1006/geno.1997.5000
   Jonkers I, 2015, NAT REV MOL CELL BIO, V16, P167, DOI 10.1038/nrm3953
   Josling GA, 2012, GENES-BASEL, V3, P320, DOI 10.3390/genes3020320
   Kim Dong Ho, 2015, Korean J Neurotrauma, V11, P167, DOI 10.13004/kjnt.2015.11.2.167
   Konuma T, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-16588-8
   Kulikowski E, 2021, MED RES REV, V41, P223, DOI 10.1002/med.21730
   Lee JE, 2017, NAT COMMUN, V8, DOI 10.1038/s41467-017-02403-5
   Li JX, 2022, J HEALTHC ENG, V2022, DOI 10.1155/2022/9271879
   Li L, 2021, J CELL PHYSIOL, V236, P4829, DOI 10.1002/jcp.30225
   Li YH, 2022, COMPUT MATH METHOD M, V2022, DOI 10.1155/2022/9241959
   Lin SG, 2020, HYPERTENS RES, V43, P1006, DOI 10.1038/s41440-020-0459-4
   Liu N, 2022, FRONT ONCOL, V12, DOI 10.3389/fonc.2022.847701
   Lovén J, 2013, CELL, V153, P320, DOI 10.1016/j.cell.2013.03.036
   Lu LL, 2020, CELL DEATH DIFFER, V27, P255, DOI 10.1038/s41418-019-0353-2
   Luna-Peláez N, 2019, CELL DEATH DIS, V10, DOI 10.1038/s41419-019-1792-x
   Ma B, 2022, HYPERTENSION, V79, P1777, DOI 10.1161/HYPERTENSIONAHA.121.18950
   Malik R, 2020, NAT STRUCT MOL BIOL, V27, P913, DOI 10.1038/s41594-020-0476-7
   Malvezzi F, 2021, COMMUN BIOL, V4, DOI 10.1038/s42003-021-02750-6
   Mehta PK, 2007, AM J PHYSIOL-CELL PH, V292, pC82, DOI 10.1152/ajpcell.00287.2006
   Meloche J, 2015, CIRC RES, V117, P525, DOI 10.1161/CIRCRESAHA.115.307004
   Melton E, 2021, INT J MOL SCI, V22, DOI 10.3390/ijms22168639
   Meta-analysis Global Group in Chronic Heart Failure (MAGGIC), 2012, European Heart Journal, V33, P1750, DOI 10.1093/eurheartj/ehr254
   Nakamura Y, 2007, J BIOL CHEM, V282, P4193, DOI 10.1074/jbc.M605971200
   Onuh JO, 2020, J HYPERTENS, V38, P1871, DOI 10.1097/HJH.0000000000002452
   Qiu H, 2007, CIRCULATION, V116, P669, DOI 10.1161/CIRCULATIONAHA.107.689208
   Qiu HY, 2007, PHYSIOL GENOMICS, V29, P169, DOI 10.1152/physiolgenomics.00229.2006
   Rahman S, 2011, MOL CELL BIOL, V31, P2641, DOI 10.1128/MCB.01341-10
   Rich MW, 2016, J AM COLL CARDIOL, V67, P2419, DOI 10.1016/j.jacc.2016.03.004
   Roberts TC, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-06483-7
   Ruffenach G, 2016, AM J RESP CRIT CARE, V194, P1273, DOI 10.1164/rccm.201512-2380OC
   Sancisi V, 2017, NUCLEIC ACIDS RES, V45, P11249, DOI 10.1093/nar/gkx802
   Sanders YY, 2020, JCI INSIGHT, V5, DOI 10.1172/jci.insight.137127
   Sanz-Alvarez M, 2021, CANCERS, V13, DOI 10.3390/cancers13061246
   Shang EY, 2004, GENE EXPR PATTERNS, V4, P513, DOI 10.1016/j.modgep.2004.03.002
   Shi JW, 2014, MOL CELL, V54, P728, DOI 10.1016/j.molcel.2014.05.016
   Shorstova T, 2021, BRIT J CANCER, V124, P1478, DOI 10.1038/s41416-021-01321-0
   Situ Y, 2023, FRONT ENDOCRINOL, V14, DOI 10.3389/fendo.2023.1089531
   Stoll S, 2018, INT J MOL SCI, V19, DOI 10.3390/ijms19041174
   Stratton MS, 2015, BIOCHEM CELL BIOL, V93, P149, DOI 10.1139/bcb-2014-0119
   Suarez-Alvarez B, 2017, J AM SOC NEPHROL, V28, P504, DOI 10.1681/ASN.2015080910
   Sun DL, 2021, MOL CANCER THER, V20, P1367, DOI 10.1158/1535-7163.MCT-20-0831
   Thorpe KL, 1996, IMMUNOGENETICS, V44, P391, DOI 10.1007/BF02602785
   Tyrrell DJ, 2022, ARTERIOSCL THROM VAS, V42, P1060, DOI 10.1161/ATVBAHA.122.317643
   Tzelepis K, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-07620-0
   Uppal S, 2019, CELL REP, V29, P2450, DOI 10.1016/j.celrep.2019.10.066
   Van der Feen DE, 2019, AM J RESP CRIT CARE, V200, P910, DOI 10.1164/rccm.201812-2275OC
   Verma S, 2014, EUR J CARDIO-THORAC, V45, P717, DOI 10.1093/ejcts/ezt560
   Wang BW, 2015, EBIOMEDICINE, V2, P1650, DOI 10.1016/j.ebiom.2015.09.045
   Wang H, 2020, AGING-US, V12, P9240, DOI 10.18632/aging.103200
   Wang WY, 2021, NAT COMMUN, V12, DOI 10.1038/s41467-021-24687-4
   Watson AMD, 2022, ARTERIOSCL THROM VAS, V42, P1077, DOI 10.1161/ATVBAHA.122.317892
   Wu SY, 2013, MOL CELL, V49, P843, DOI 10.1016/j.molcel.2012.12.006
   Yang YM, 2018, J AM SOC HYPERTENS, V12, pE107, DOI 10.1016/j.jash.2018.11.004
   Yang ZY, 2005, MOL CELL, V19, P535, DOI 10.1016/j.molcel.2005.06.029
   Yu XY, 2023, ANTIVIR RES, V211, DOI 10.1016/j.antiviral.2023.105552
   Zhang MX, 2019, CELL SIGNAL, V61, P20, DOI 10.1016/j.cellsig.2019.05.005
   Zhou ZJ, 2020, FRONT PHARMACOL, V11, DOI 10.3389/fphar.2020.01043
   Zhu Y, 2012, AGING CELL, V11, P741, DOI 10.1111/j.1474-9726.2012.00840.x
NR 77
TC 4
Z9 5
U1 2
U2 6
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
EI 2218-273X
J9 BIOMOLECULES
JI Biomolecules
PD JUL
PY 2023
VL 13
IS 7
AR 1135
DI 10.3390/biom13071135
PG 17
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA N2CY6
UT WOS:001035166900001
PM 37509171
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Aschrafi, A
   Meindl, N
   Firla, B
   Brandes, RP
   Steinhilber, D
AF Aschrafi, Angelique
   Meindl, Nadine
   Firla, Beate
   Brandes, Ralf P.
   Steinhilber, Dieter
TI Intracellular localization of RORα is isoform and cell line-dependent
SO BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
LA English
DT Article
DE ROR alpha; cholesterol; 293 HEK cell; HeLa cell; cellular distribution;
   nuclear receptor
ID ORPHAN NUCLEAR RECEPTOR; FLUORESCENT PROTEIN CHIMERA;
   PROGESTERONE-RECEPTOR; LIVING CELLS; GLUCOCORTICOID-RECEPTOR; ANDROGEN
   RECEPTOR; STAGGERER MOUSE; BINDING DOMAIN; EXPORT SIGNALS; DEFICIENT
   MICE
AB The retinoid-related orphan receptor alpha (ROR alpha) belongs to the nuclear receptor superfamily and comprises four isoforms generated by different promotor usage and alternative splicing. To better understand its function, the subeellular distribution of ROR alpha was investigated. We could show that subcellular distribution of ROR alpha is cell line and isoform-dependent. Isoform specific differences were mediated by the A/B domains which with the exception of ROR alpha 1 contain a signal that mediates cytoplasmic localization. The lack of this signal in ROR alpha 1 results in a complete nuclear localization and prevents cell membrane association observed for ROR alpha 2, 3, and 4. The region responsible for membrane association was identified as the C-terminal alpha-helix 12. Furthermore, the hinge region/ligand binding domain mediates nuclear localization. Our results show that isoform specific activity of ROR alpha is not only regulated by different expression and DNA binding affinities but also by different subcellular distribution. Different access to the nucleus reveals an important mechanism regulating the activity of this constitutively active nuclear receptor. (c) 2006 Elsevier B.V. All rights reserved.
C1 Univ Frankfurt, Inst Pharmaceut Chem ZAFES, D-60438 Frankfurt, Germany.
   Univ Frankfurt, Inst Cardiovasc Physiol ZAFES, D-60596 Frankfurt, Germany.
C3 Goethe University Frankfurt; Goethe University Frankfurt
RP Steinhilber, D (corresponding author), Univ Frankfurt, Inst Pharmaceut Chem ZAFES, Max Von Laue Str 9, D-60438 Frankfurt, Germany.
EM steinhilber@em.uni-frankfurt.de
RI Steinhilber, Dieter/J-3221-2012; Brandes, Ralf/L-3058-2017
OI Steinhilber, Dieter/0000-0001-8905-5208; Brandes,
   Ralf/0000-0002-8035-0048
CR Akashi M, 2005, NAT STRUCT MOL BIOL, V12, P441, DOI 10.1038/nsmb925
   [Anonymous], 1983, COLD SPRING HARBOR L
   Auwerx J, 1999, CELL, V97, P161
   BECKERANDRE M, 1993, BIOCHEM BIOPH RES CO, V194, P1371, DOI 10.1006/bbrc.1993.1976
   Besnard S, 2002, FEBS LETT, V511, P36, DOI 10.1016/S0014-5793(01)03275-6
   Black BE, 2001, CURR BIOL, V11, P1749, DOI 10.1016/S0960-9822(01)00537-1
   Chauvet C, 2002, BIOCHEM J, V364, P449, DOI 10.1042/BJ20011558
   CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
   Chopin-Delannoy S, 2003, J MOL ENDOCRINOL, V30, P197, DOI 10.1677/jme.0.0300197
   Delerive P, 2001, EMBO REP, V2, P42, DOI 10.1093/embo-reports/kve007
   Dussault I, 1998, MECH DEVELOP, V70, P147, DOI 10.1016/S0925-4773(97)00187-1
   Enmark E, 1996, MOL ENDOCRINOL, V10, P1293, DOI 10.1210/me.10.11.1293
   EVANS RM, 1988, SCIENCE, V240, P889, DOI 10.1126/science.3283939
   Fejes-Tóth G, 1998, P NATL ACAD SCI USA, V95, P2973, DOI 10.1073/pnas.95.6.2973
   Georget V, 1997, MOL CELL ENDOCRINOL, V129, P17, DOI 10.1016/S0303-7207(97)04034-3
   GERACE L, 1995, CELL, V82, P341, DOI 10.1016/0092-8674(95)90420-4
   GIGUERE V, 1994, GENE DEV, V8, P538, DOI 10.1101/gad.8.5.538
   GIGUERE V, 1986, CELL, V46, P645, DOI 10.1016/0092-8674(86)90339-9
   Glass CK, 2000, GENE DEV, V14, P121
   GUIOCHONMANTEL A, 1989, CELL, V57, P1147, DOI 10.1016/0092-8674(89)90052-4
   GUIOCHONMANTEL A, 1991, EMBO J, V10, P3851, DOI 10.1002/j.1460-2075.1991.tb04954.x
   Hamilton BA, 1996, NATURE, V379, P736, DOI 10.1038/379736a0
   Harris JM, 2002, MOL ENDOCRINOL, V16, P998, DOI 10.1210/me.16.5.998
   Htun H, 1996, P NATL ACAD SCI USA, V93, P4845, DOI 10.1073/pnas.93.10.4845
   Jarvis CI, 2002, MOL CELL ENDOCRINOL, V186, P1, DOI 10.1016/S0303-7207(01)00668-2
   Kallen J, 2004, J BIOL CHEM, V279, P14033, DOI 10.1074/jbc.M400302200
   Komeili A, 2000, CURR OPIN CELL BIOL, V12, P355, DOI 10.1016/S0955-0674(00)00100-9
   KRUST A, 1986, EMBO J, V5, P891, DOI 10.1002/j.1460-2075.1986.tb04300.x
   LAEMMLI UK, 1970, NATURE, V227, P680, DOI 10.1038/227680a0
   Levin ER, 2002, STEROIDS, V67, P471, DOI 10.1016/S0039-128X(01)00179-9
   Lim CS, 1999, MOL ENDOCRINOL, V13, P366, DOI 10.1210/me.13.3.366
   Lösel R, 2003, NAT REV MOL CELL BIO, V4, P46, DOI 10.1038/nrm1009
   Mamontova A, 1998, CIRCULATION, V98, P2738, DOI 10.1161/01.CIR.98.24.2738
   Marcinkowska E, 2001, BIOL SIGNAL RECEPT, V10, P341
   MatysiakScholze U, 1997, GENOMICS, V43, P78, DOI 10.1006/geno.1997.4757
   Métivier R, 2002, EMBO J, V21, P3443, DOI 10.1093/emboj/cdf344
   Meyer T, 2000, P NATL ACAD SCI USA, V97, P9197, DOI 10.1073/pnas.150246097
   Moraitis AN, 2003, J BIOL CHEM, V278, P52511, DOI 10.1074/jbc.M308152200
   Nakielny S, 1999, CELL, V99, P677, DOI 10.1016/S0092-8674(00)81666-9
   OMALLEY BW, 1992, MOL ENDOCRINOL, V6, P1359, DOI 10.1210/me.6.9.1359
   PICARD D, 1987, EMBO J, V6, P3333, DOI 10.1002/j.1460-2075.1987.tb02654.x
   Pozo D, 2004, J PINEAL RES, V37, P48, DOI 10.1111/j.1600-079X.2004.00135.x
   Saporita AJ, 2003, J BIOL CHEM, V278, P41998, DOI 10.1074/jbc.M302460200
   SIDMAN RL, 1962, SCIENCE, V137, P610, DOI 10.1126/science.137.3530.610
   Steinmayr M, 1998, P NATL ACAD SCI USA, V95, P3960, DOI 10.1073/pnas.95.7.3960
   Tremblay A, 1999, MOL CELL, V3, P513, DOI 10.1016/S1097-2765(00)80479-7
   Tyagi RK, 1998, MOL ENDOCRINOL, V12, P1684, DOI 10.1210/me.12.11.1684
   Watson CS, 2002, STEROIDS, V67, P429, DOI 10.1016/S0039-128X(01)00172-6
   WILSON TE, 1993, MOL CELL BIOL, V13, P861, DOI 10.1128/MCB.13.2.861
   Zhu XG, 1998, J BIOL CHEM, V273, P27058, DOI 10.1074/jbc.273.42.27058
NR 50
TC 14
Z9 16
U1 0
U2 2
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 0167-4889
J9 BBA-MOL CELL RES
JI Biochim. Biophys. Acta-Mol. Cell Res.
PD AUG
PY 2006
VL 1763
IS 8
BP 805
EP 814
DI 10.1016/j.bbamcr.2006.05.006
PG 10
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA 082NU
UT WOS:000240394400005
PM 16806533
OA Bronze
DA 2025-04-10
ER

PT J
AU Collier, TS
   Muddiman, DC
AF Collier, Timothy S.
   Muddiman, David Charles
TI Analytical strategies for the global quantification of intact proteins
SO AMINO ACIDS
LA English
DT Review
DE Proteomics; Intact proteins; Quantitation; Mass spectrometry
ID DIFFERENCE GEL-ELECTROPHORESIS; ELECTRON-CAPTURE DISSOCIATION; TOP-DOWN
   PROTEOMICS; CARDIAC TROPONIN-I; MASS-SPECTROMETRY;
   QUANTITATIVE-ANALYSIS; SELECTIVE INCORPORATION; ACCURATE QUANTITATION;
   EXPRESSION ANALYSIS; DETECTING CHANGES
AB The quantification of intact proteins is a relatively recent development in proteomics. In eukaryotic organisms, proteins are present as multiple isoforms as the result of variations in genetic code, alternative splicing, post-translational modification and other processing events. Understanding the identities and biological functions of these isoforms and how their concentrations vary across different states is the central goal of proteomics. To date, the bulk of proteomics research utilizes a "bottom-up" approach, digesting proteins into their more manageable constitutive peptides, but sacrificing information about the specific isoform and combinations of post-translational modifications present on the protein. Very specific strategies for protein quantification such as the enzyme-linked immunosorbent assay and Western blot are commonplace in laboratories and clinics, but impractical for the study of global biological changes. Herein, we describe strategies for the quantification of intact proteins, their distinct advantages, and challenges to their employment. Techniques contained in this review include the more traditional and widely employed methodology of differential gel electrophoresis and more recently developed mass spectrometry-based techniques including metabolic labeling, chemical labeling, and label-free methodologies.
C1 [Collier, Timothy S.; Muddiman, David Charles] N Carolina State Univ, Dept Chem, WM Keck FT ICR Mass Spectrometry Lab, Raleigh, NC 27695 USA.
C3 North Carolina State University
RP Muddiman, DC (corresponding author), N Carolina State Univ, Dept Chem, WM Keck FT ICR Mass Spectrometry Lab, Box 8204, Raleigh, NC 27695 USA.
EM david_muddiman@ncsu.edu
OI Muddiman, David/0000-0003-2216-499X; Collier,
   Timothy/0000-0002-1102-8741
FU NSF [MCB-0918611]; W. M. Keck Foundation; North Carolina State
   University
FX The authors wish to acknowledge funding support from NSF Grant
   MCB-0918611, the W. M. Keck Foundation, and North Carolina State
   University.
CR Ardelt P, 1998, BIOL CHEM, V379, P341, DOI 10.1515/bchm.1998.379.3.341
   Berger SJ, 2002, ANAL CHEM, V74, P4994, DOI 10.1021/ac020105f
   Bogdanov B, 2005, MASS SPECTROM REV, V24, P168, DOI 10.1002/mas.20015
   Collier TS, 2008, ANAL CHEM, V80, P4994, DOI 10.1021/ac800254z
   Collier TS, 2010, J AM SOC MASS SPECTR, V21, P879, DOI 10.1016/j.jasms.2010.01.031
   Das T, 2004, GLYCOCONJUGATE J, V20, P537
   Das T, 2003, BIOCHEM J, V373, P345, DOI 10.1042/BJ20021701
   de Godoy LMF, 2006, GENOME BIOL, V7, DOI 10.1186/gb-2006-7-6-r50
   Dillon TM, 2004, J CHROMATOGR A, V1053, P299, DOI 10.1016/j.chroma.2004.08.058
   Du Y, 2006, ANAL CHEM, V78, P686, DOI 10.1021/ac050993p
   Du Y, 2004, J PROTEOME RES, V3, P801, DOI 10.1021/pr0499489
   Ge Y, 2002, J AM CHEM SOC, V124, P672, DOI 10.1021/ja011335z
   Gharbi S, 2002, MOL CELL PROTEOMICS, V1, P91, DOI 10.1074/mcp.T100007-MCP200
   Gordon EF, 1999, J MASS SPECTROM, V34, P1055, DOI 10.1002/(SICI)1096-9888(199910)34:10<1055::AID-JMS864>3.0.CO;2-E
   Greengauz-Roberts O, 2005, PROTEOMICS, V5, P1746, DOI 10.1002/pmic.200401068
   Hanke S, 2008, J PROTEOME RES, V7, P1118, DOI 10.1021/pr7007175
   Hawkridge AM, 2005, P NATL ACAD SCI USA, V102, P17442, DOI 10.1073/pnas.0508782102
   Horn DM, 2000, J AM SOC MASS SPECTR, V11, P320, DOI 10.1016/S1044-0305(99)00157-9
   Hu QZ, 2005, J MASS SPECTROM, V40, P430, DOI 10.1002/jms.856
   Jennings KR, 2000, INT J MASS SPECTROM, V200, P479, DOI 10.1016/S1387-3806(00)00325-0
   Johnson KL, 2004, ANAL CHEM, V76, P5097, DOI 10.1021/ac0497003
   Julka S, 2004, J PROTEOME RES, V3, P350, DOI 10.1021/pr0340734
   Karp NA, 2005, PROTEOMICS, V5, P3105, DOI 10.1002/pmic.200500083
   Karp NA, 2004, PROTEOMICS, V4, P1421, DOI 10.1002/pmic.200300681
   Katrukha AG, 1998, CLIN CHEM, V44, P2433
   Kelleher NL, 1998, PROTEIN SCI, V7, P1796, DOI 10.1002/pro.5560070815
   Kelleher NL, 1999, J AM CHEM SOC, V121, P806, DOI 10.1021/ja973655h
   Kenyon GL, 2002, MOL CELL PROTEOMICS, V1, P763
   Kreil DP, 2004, BIOINFORMATICS, V20, P2026, DOI 10.1093/bioinformatics/bth193
   Labugger R, 2000, CIRCULATION, V102, P1221, DOI 10.1161/01.CIR.102.11.1221
   Lilley KS, 2002, CURR OPIN CHEM BIOL, V6, P46, DOI 10.1016/S1367-5931(01)00275-7
   LITTLE DP, 1994, ANAL CHEM, V66, P2809, DOI 10.1021/ac00090a004
   Martinovic S, 2002, J MASS SPECTROM, V37, P99, DOI 10.1002/jms.263
   Mazur MT, 2010, P NATL ACAD SCI USA, V107, P7728, DOI 10.1073/pnas.0910776107
   Meng FY, 2007, J AM SOC MASS SPECTR, V18, P226, DOI 10.1016/j.jasms.2006.09.014
   Meng FY, 2002, ANAL CHEM, V74, P2923, DOI 10.1021/ac020049i
   Oda Y, 1999, P NATL ACAD SCI USA, V96, P6591, DOI 10.1073/pnas.96.12.6591
   Ong SE, 2002, MOL CELL PROTEOMICS, V1, P376, DOI 10.1074/mcp.M200025-MCP200
   Ong SE, 2003, J PROTEOME RES, V2, P173, DOI 10.1021/pr0255708
   Parks BA, 2007, ANAL CHEM, V79, P7984, DOI 10.1021/ac070553t
   Patton WF, 2000, ELECTROPHORESIS, V21, P1123, DOI 10.1002/(SICI)1522-2683(20000401)21:6<1123::AID-ELPS1123>3.0.CO;2-E
   Pesavento JJ, 2006, ANAL CHEM, V78, P4271, DOI 10.1021/ac0600050
   Quadroni M, 1999, ELECTROPHORESIS, V20, P664, DOI 10.1002/(SICI)1522-2683(19990101)20:4/5<664::AID-ELPS664>3.0.CO;2-A
   Shaw J, 2003, PROTEOMICS, V3, P1181, DOI 10.1002/pmic.200300439
   Siuti N, 2007, NAT METHODS, V4, P817, DOI 10.1038/NMETH1097
   Syka JEP, 2004, J PROTEOME RES, V3, P621, DOI 10.1021/pr0499794
   Tonge R, 2001, PROTEOMICS, V1, P377
   Tran JC, 2008, ANAL CHEM, V80, P1568, DOI 10.1021/ac702197w
   Unlu M, 1997, ELECTROPHORESIS, V18, P2071, DOI 10.1002/elps.1150181133
   Van Hoof D, 2007, NAT METHODS, V4, P677, DOI 10.1038/nmeth0907-677
   Veenstra TD, 2000, J AM SOC MASS SPECTR, V11, P78, DOI 10.1016/S1044-0305(99)00120-8
   Vellaichamy A, 2010, ANAL CHEM, V82, P1234, DOI 10.1021/ac9021083
   Viswanathan S, 2006, NAT PROTOC, V1, P1351, DOI 10.1038/nprot.2006.234
   Waanders LF, 2007, J AM SOC MASS SPECTR, V18, P2058, DOI 10.1016/j.jasms.2007.09.001
   Wang YJ, 2005, J CHROMATOGR A, V1073, P35, DOI 10.1016/j.chroma.2004.08.140
   Washburn MP, 2002, ANAL CHEM, V74, P1650, DOI 10.1021/ac015704l
   Yan XW, 2010, ANAL CHEM, V82, P1261, DOI 10.1021/ac902163x
   Yates JR, 2006, ANAL CHEM, V78, P493, DOI 10.1021/ac0514624
   Zamdborg L, 2007, NUCLEIC ACIDS RES, V35, pW701, DOI 10.1093/nar/gkm371
   Zhang RJ, 2001, ANAL CHEM, V73, P5142, DOI 10.1021/ac010583a
   Zubarev RA, 1998, J AM CHEM SOC, V120, P3265, DOI 10.1021/ja973478k
NR 61
TC 23
Z9 27
U1 1
U2 58
PU SPRINGER WIEN
PI WIEN
PA SACHSENPLATZ 4-6, PO BOX 89, A-1201 WIEN, AUSTRIA
SN 0939-4451
EI 1438-2199
J9 AMINO ACIDS
JI Amino Acids
PD SEP
PY 2012
VL 43
IS 3
BP 1109
EP 1117
DI 10.1007/s00726-012-1285-z
PG 9
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 989BV
UT WOS:000307536100008
PM 22821264
DA 2025-04-10
ER

PT J
AU Morisaki, T
   Sermsuvitayawong, K
   Byun, SH
   Matsuda, Y
   Hidaka, K
   Morisaki, H
   Mukai, T
AF Morisaki, T
   Sermsuvitayawong, K
   Byun, SH
   Matsuda, Y
   Hidaka, K
   Morisaki, H
   Mukai, T
TI Mouse Mef2b gene: Unique member of MEF2 gene family
SO JOURNAL OF BIOCHEMISTRY
LA English
DT Article
DE development; differentiation; gene; MEF2; transcription
ID TRANSCRIPTION FACTORS; MYOGENIC LINEAGE; HEART; CELLS
AB The myocyte enhancer factor 2 (MEF2) gene family, which belongs to the MADS [MCM1, agamous, deficiens, serum response factor (SRF)] superfamily, is thought to play an important role in differentiation of myocytes, including cardiomyocytes, To better understand the mouse Mef2 gene family, the mouse Mef2b gene, which was found to be expressed in undifferentiated embryonal cells, was characterized, The Mef2b gene was found to be more than 30 kb in length, consisting of 11 exons. Eight exons correspond to coding regions and the remaining 3 exons for the 5' part are alternatively used. Two internal exons are subject to alternative splicing, resulting in production of four subtypes of mouse MEF2B peptides, Fluorescence in situ hybridization (FISH) and inter-specific backcross analysis identified the Mef2b gene locus. Mef2b gene was expressed in heart or skeletal muscle of early mouse embryo, but not in those of adult mouse, Functionally, mouse MEF2B did not exhibit DNA binding with the MEF2 consensus element in vitro, but did cause transcriptional activation of the MEF2 element, although it was less effective than human MEF2B. Based on these results, mouse MEF2B seems to have a unique character, distinct from other MEF2 family members.
C1 NATL INST RADIOL SCI,GENOME RES GRP,CHIBA 260,JAPAN.
C3 National Institutes for Quantum Science & Technology
RP Morisaki, T (corresponding author), NATL CARDIOVASC CTR,RES INST,DEPT BIOSCI,5-7-1 FUJISHIRODAI,SUITA,OSAKA 565,JAPAN.
CR BOUR BA, 1995, GENE DEV, V9, P730, DOI 10.1101/gad.9.6.730
   BREITBART RE, 1993, DEVELOPMENT, V118, P1095
   BUCKINGHAM M, 1994, CELL, V78, P15, DOI 10.1016/0092-8674(94)90568-1
   CECI JD, 1994, MAMM GENOME, V5, pS124
   FELGNER PL, 1987, P NATL ACAD SCI USA, V84, P7413, DOI 10.1073/pnas.84.21.7413
   GOSSETT LA, 1989, MOL CELL BIOL, V9, P5022, DOI 10.1128/MCB.9.11.5022
   GREPIN C, 1995, MOL CELL BIOL, V15, P4095
   HIDAKA K, 1993, MOL CELL BIOL, V13, P6469, DOI 10.1128/MCB.13.10.6469
   HIDAKA K, 1995, BIOCHEM BIOPH RES CO, V213, P555, DOI 10.1006/bbrc.1995.2167
   HOBSON GM, 1995, GENOMICS, V29, P704, DOI 10.1006/geno.1995.9007
   KAUSHAL S, 1994, SCIENCE, V266, P1236, DOI 10.1126/science.7973707
   Kawasaki E. S., 1990, PCR PROTOCOLS GUIDE, P21
   KOMURO I, 1993, P NATL ACAD SCI USA, V90, P8145, DOI 10.1073/pnas.90.17.8145
   LINTS TJ, 1993, DEVELOPMENT, V119, P419
   Lyon M. F., 1994, Mouse Genome, V92, P19
   MARTIN JF, 1993, P NATL ACAD SCI USA, V90, P5282, DOI 10.1073/pnas.90.11.5282
   MATSUDA Y, 1992, CYTOGENET CELL GENET, V61, P282, DOI 10.1159/000133423
   MCDERMOTT JC, 1993, MOL CELL BIOL, V13, P2564, DOI 10.1128/MCB.13.4.2564
   Molkentin JD, 1996, MOL CELL BIOL, V16, P3814
   POLLOCK R, 1991, GENE DEV, V5, P2327, DOI 10.1101/gad.5.12a.2327
   Sambrook J, 1989, MOL CLONING LAB MANU
   YU YT, 1992, GENE DEV, V6, P1783, DOI 10.1101/gad.6.9.1783
NR 22
TC 21
Z9 36
U1 0
U2 5
PU JAPANESE BIOCHEMICAL SOC
PI TOKYO
PA ISHIKAWA BLDG-3F, 25-16 HONGO-5-CHOME, BUNKYO-KU, TOKYO 113, JAPAN
SN 0021-924X
J9 J BIOCHEM-TOKYO
JI J. Biochem. (Tokyo)
PD NOV
PY 1997
VL 122
IS 5
BP 939
EP 946
PG 8
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA YG280
UT WOS:A1997YG28000007
PM 9443808
DA 2025-04-10
ER

PT J
AU Napoli, C
   Schiano, C
   Soricelli, A
AF Napoli, C.
   Schiano, C.
   Soricelli, A.
TI Increasing evidence of pathogenic role of the Mediator (MED) complex in
   the development of cardiovascular diseases
SO BIOCHIMIE
LA English
DT Review
DE Cardiovascular diseases; Endothelial cells; Mediator; Diabetes; Energy
   homeostasis
ID GENOMIC HYBRIDIZATION CHARACTERIZATION; SYSTEMIC ENERGY HOMEOSTASIS;
   BISPHENOL-A; INTELLECTUAL DISABILITY; PRENATAL-DIAGNOSIS; PRIMARY
   PREVENTION; RECEPTOR; TRANSCRIPTION; CELL; ATHEROSCLEROSIS
AB Cardiovascular diseases (CVDs) are the first cause of death in the World. Mediator (MED) is an evolutionarily conserved protein complex, which mediates distinct protein-protein interactions. Pathogenic events in MED subunit have been associated with human diseases. Novel increasing evidence showed that missense mutations in MED13L gene are associated with transposition of great arteries while MED12, MED13, MED15, and MED30, have been correlated with heart development. Moreover, MED23 and MED25 have been associated with heart malformations in humans. Relevantly, MED1, MED13, MED14, MED15, MED23, MED25, and CDK8, were found modify glucose and/or lipid metabolism. Indeed, MED1, MED15, MED25, and CDK8 interact in the PPAR-and SREBP-mediated signaling pathways. MED1, MED14 and MED23 are involved in adipocyte differentiation, whereas MED23 mediates smooth muscle cell differentiation. MED12, MED19, MED23, and MED30 regulate endothelial differentiation by alternative splicing mechanism. Thus, MEDs have a central role in early pathogenic events involved in CVDs representing novel targets for clinical prevention and therapeutic approaches. (C) 2019 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved.
C1 [Napoli, C.] Univ Campania L Vanvitelli, Univ Dept Adv Med & Surg Sci, Clin Dept Internal Med & Specialist Units, I-80138 Naples, Italy.
   [Schiano, C.; Soricelli, A.] IRCCS SDN, Via E Gianturco 113, I-80143 Naples, Italy.
   [Soricelli, A.] Univ Naples Parthenope, Dept Motor Sci & Healthiness, I-80134 Naples, Italy.
C3 Universita della Campania Vanvitelli; IRCCS Istituto di Ricerca
   Diagnostica e Nucleare (SDN); Parthenope University Naples
RP Schiano, C (corresponding author), IRCCS SDN, Via E Gianturco 113, I-80143 Naples, Italy.
EM tina.schiano@gmail.com
RI Soricelli, Andrea/C-1133-2009
OI Soricelli, Andrea/0000-0001-7011-7667
FU "Ricerca Finalizzata 2011-12 Grant" from Italian Ministry of Health
   [GR-2011-02349436]; "Ricerca Corrente 2018" from Italian Ministry of
   Health
FX This work was supported by "Ricerca Finalizzata 2011-12 Grant" (project
   code GR-2011-02349436) and "Ricerca Corrente 2018" from Italian Ministry
   of Health.
CR Allen BL, 2015, NAT REV MOL CELL BIO, V16, P155, DOI 10.1038/nrm3951
   Alonso-Magdalena P, 2011, NAT REV ENDOCRINOL, V7, P346, DOI 10.1038/nrendo.2011.56
   Alrob OA, 2017, J PHYSIOL BIOCHEM, V73, P307, DOI 10.1007/s13105-016-0543-z
   American Heart Association, ANN REP 2016 2017
   Ang XLL, 2005, ONCOGENE, V24, P2860, DOI 10.1038/sj.onc.1208614
   Asadollahi R, 2017, EUR J MED GENET, V60, P451, DOI 10.1016/j.ejmg.2017.06.004
   Bae S, 2015, HYPERTENSION, V65, P313, DOI 10.1161/HYPERTENSIONAHA.114.04261
   Bae S, 2012, HYPERTENSION, V60, P786, DOI 10.1161/HYPERTENSIONAHA.112.197715
   Balamotis MA, 2009, SCI SIGNAL, V2, DOI 10.1126/scisignal.1164302
   Basel-Vanagaite L, 2015, HUM GENET, V134, P577, DOI 10.1007/s00439-015-1541-x
   Becerril S, 2012, PHYSIOL GENOMICS, V44, P678, DOI 10.1152/physiolgenomics.00039.2012
   Benjamin EJ, 2017, CIRCULATION, V135, pE146, DOI [10.1161/CIR.0000000000000558, 10.1161/CIR.0000000000000485, 10.1161/CIR.0000000000000530]
   Borik S, 2011, INTENS CARE MED, V37, P1664, DOI 10.1007/s00134-011-2296-z
   Carrer M, 2012, P NATL ACAD SCI USA, V109, P15330, DOI 10.1073/pnas.1207605109
   Casamassimi A, 2007, BIOCHIMIE, V89, P1439, DOI 10.1016/j.biochi.2007.08.002
   Chen CP, 2015, TAIWAN J OBSTET GYNE, V54, P592, DOI 10.1016/j.tjog.2015.08.013
   Chen CP, 2013, GENE, V527, P405, DOI 10.1016/j.gene.2013.06.009
   Chen W, 2011, SEMIN CELL DEV BIOL, V22, P749, DOI 10.1016/j.semcdb.2011.07.026
   Chen W, 2010, P NATL ACAD SCI USA, V107, P10196, DOI 10.1073/pnas.1005626107
   Chen W, 2009, MOL CELL, V35, P755, DOI 10.1016/j.molcel.2009.09.015
   Conaway RC, 2013, BBA-GENE REGUL MECH, V1829, P69, DOI 10.1016/j.bbagrm.2012.08.017
   de Nigris F, 2018, JAMA CARDIOL, V3, P1184, DOI 10.1001/jamacardio.2018.3546
   Drew LJ, 2011, INT J DEV NEUROSCI, V29, P259, DOI 10.1016/j.ijdevneu.2010.09.007
   Dumortier O, 2014, DIABETES, V63, P3416, DOI 10.2337/db13-1431
   Ferguson SS, 2005, MOL PHARMACOL, V68, P747, DOI 10.1124/mol.105.013169
   Fondell JD, 2013, BBA-GEN SUBJECTS, V1830, P3867, DOI 10.1016/j.bbagen.2012.02.012
   Friedrichs P, 2017, DIABETOLOGIA, V60, P1354, DOI 10.1007/s00125-017-4254-y
   Gonzalez D, 2014, P NATL ACAD SCI USA, V111, P2500, DOI 10.1073/pnas.1307525111
   Grontved L, 2010, MOL CELL BIOL, V30, P2155, DOI 10.1128/MCB.01238-09
   Grueter CE, 2012, CELL, V149, P671, DOI 10.1016/j.cell.2012.03.029
   Hall DD, 2017, JCI INSIGHT, V2, DOI 10.1172/jci.insight.92476
   Han EH, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0044007
   Heinritz W, 2009, ANN HUM GENET, V73, P283, DOI 10.1111/j.1469-1809.2009.00508.x
   Iida S, 2015, GENE DEV, V29, P308, DOI 10.1101/gad.252809.114
   Khakhina S, 2014, MOL BIOL CELL, V25, P2807, DOI 10.1091/mbc.E14-05-0953
   Kleber ME, 2013, CIRC-CARDIOVASC GENE, V6, P505, DOI 10.1161/CIRCGENETICS.113.000108
   Krebs P, 2011, P NATL ACAD SCI USA, V108, P19678, DOI 10.1073/pnas.1117835108
   Leal A, 2001, AM J HUM GENET, V68, P269, DOI 10.1086/316934
   Lee M.S., 2018, MOLECULES, V23, P10
   Lind PM, 2011, ATHEROSCLEROSIS, V218, P207, DOI 10.1016/j.atherosclerosis.2011.05.001
   Maeda Y, 2002, MOL ENDOCRINOL, V16, P402, DOI 10.1210/me.16.2.402
   Malik S, 2010, NAT REV GENET, V11, P761, DOI 10.1038/nrg2901
   Melzer D, 2012, CIRCULATION, V125, P1482, DOI 10.1161/CIRCULATIONAHA.111.069153
   Mishra A, 2010, J MOL ENDOCRINOL, V44, P247, DOI 10.1677/JME-09-0137
   Montgomery RL, 2011, CIRCULATION, V124, P1537, DOI 10.1161/CIRCULATIONAHA.111.030932
   Mooij HL, 2014, J AM HEART ASSOC, V3, DOI 10.1161/JAHA.114.001274
   Mousley CJ, 2012, CELL, V148, P702, DOI 10.1016/j.cell.2011.12.026
   Muncke N, 2003, CIRCULATION, V108, P2843, DOI 10.1161/01.CIR.0000103684.77636.CD
   Nakamura D, 2010, TOXICOL LETT, V194, P16, DOI 10.1016/j.toxlet.2010.02.002
   Napoli C, 2006, CIRCULATION, V114, P2517, DOI 10.1161/CIRCULATIONAHA.105.570358
   Napoli C, 2012, CIRCULATION, V125, P2363, DOI 10.1161/CIRCULATIONAHA.111.085787
   Napoli C, 2012, BIOCHIMIE, V94, P579, DOI 10.1016/j.biochi.2011.09.016
   Napoli C, 2011, CARDIOVASC RES, V92, P367, DOI 10.1093/cvr/cvr201
   Ramadan M, 2018, SCI REP-UK, V8, DOI 10.1038/s41598-018-25719-8
   Rana R, 2011, MOL CELL BIOL, V31, P466, DOI 10.1128/MCB.00847-10
   Rienzo M, 2012, BIOCHIMIE, V94, P1828, DOI 10.1016/j.biochi.2012.04.008
   Rienzo M, 2010, BBA-GENE REGUL MECH, V1799, P487, DOI 10.1016/j.bbagrm.2010.05.001
   Rocha PP, 2010, DEVELOPMENT, V137, P2723, DOI 10.1242/dev.053660
   Rujescu D, 2018, FRONT NEUROL, V9, DOI 10.3389/fneur.2018.00591
   Sano M, 2004, EMBO J, V23, P3559, DOI 10.1038/sj.emboj.7600351
   Schiano C, 2017, J CARDIOVASC MED, V18, P742, DOI 10.2459/JCM.0000000000000536
   Schiano C, 2014, BBA-GENE REGUL MECH, V1839, P444, DOI 10.1016/j.bbagrm.2014.04.012
   Schilbach S, 2017, NATURE, V551, P204, DOI 10.1038/nature24282
   Schwartz CE, 2007, J MED GENET, V44, P472, DOI 10.1136/jmg.2006.048637
   Shankar Anoop, 2012, J Environ Public Health, V2012, P481641, DOI 10.1155/2012/481641
   Shrestha S, 2014, ARTERIOSCL THROM VAS, V34, P244, DOI 10.1161/ATVBAHA.113.302191
   Stieg DC, 2018, MOL BIOL CELL, V29, P363, DOI 10.1091/mbc.E17-08-0493
   Thayer KA, 2012, ENVIRON HEALTH PERSP, V120, P779, DOI 10.1289/ehp.1104597
   Trajkovski M, 2011, NATURE, V474, P649, DOI 10.1038/nature10112
   Trehan A, 2015, AM J MED GENET A, V167, P1374, DOI 10.1002/ajmg.a.37047
   Tutter AV, 2009, J BIOL CHEM, V284, P3709, DOI 10.1074/jbc.M805677200
   Vulto-van Silfhout AT, 2013, AM J HUM GENET, V92, P401, DOI 10.1016/j.ajhg.2013.01.007
   Wang W, 2013, TRANSCR-AUSTIN, V4, P39, DOI 10.4161/trns.22874
   Wang W, 2009, DEV CELL, V16, P764, DOI 10.1016/j.devcel.2009.04.006
   Xiaoli, 2013, TRENDS CARDIOVAS MED, V23, P269, DOI 10.1016/j.tcm.2013.03.002
   Xu JY, 2017, ENVIRON TOXICOL, V32, P970, DOI 10.1002/tox.22297
   Yamamoto T, 2017, AM J MED GENET A, V173, P1264, DOI 10.1002/ajmg.a.38168
   Yang FJ, 2006, NATURE, V442, P700, DOI 10.1038/nature04942
   Yeung SLA, 2016, AM HEART J, V182, P54, DOI 10.1016/j.ahj.2016.07.021
   Yin JW, 2012, GENE DEV, V26, P2192, DOI 10.1101/gad.192666.112
   Zhao XP, 2014, DIABETES, V63, P2464, DOI 10.2337/db13-0835
   Zhao XP, 2012, J CLIN INVEST, V122, P2417, DOI 10.1172/JCI61462
NR 82
TC 33
Z9 36
U1 4
U2 21
PU ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
PI ISSY-LES-MOULINEAUX
PA 65 RUE CAMILLE DESMOULINS, CS50083, 92442 ISSY-LES-MOULINEAUX, FRANCE
SN 0300-9084
EI 1638-6183
J9 BIOCHIMIE
JI Biochimie
PD OCT
PY 2019
VL 165
BP 1
EP 8
DI 10.1016/j.biochi.2019.06.014
PG 8
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA IX6IK
UT WOS:000485786400001
PM 31255603
DA 2025-04-10
ER

PT J
AU Garcia-Romero, N
   Esteban-Rubio, S
   Rackov, G
   Carrión-Navarro, J
   Belda-Iniesta, C
   Ayuso-Sacido, A
AF Garcia-Romero, Noemi
   Esteban-Rubio, Susana
   Rackov, Gorjana
   Carrion-Navarro, Josefa
   Belda-Iniesta, Cristobal
   Ayuso-Sacido, Angel
TI Extracellular vesicles compartment in liquid biopsies: Clinical
   application
SO MOLECULAR ASPECTS OF MEDICINE
LA English
DT Review
DE Exosomes; Extracellular microvesicles; Cancer; Molecular biomarkers
ID CIRCULATING ENDOTHELIAL MICROPARTICLES; METASTATIC COLORECTAL-CANCER;
   CELL-DERIVED MICROPARTICLES; TISSUE FACTOR-BEARING; LUNG-CANCER;
   MELANOMA EXOSOMES; NORMAL-PREGNANCY; SPLICE VARIANTS; ELEVATED LEVELS;
   EXPRESSION
AB Liquid biopsy is becoming a new source of biomarkers that complement and resolve some of the most important limitations of surgical biopsy, which are the accessibility to the diseased tissue and its heterogeneity, especially relevant for tumors. The diseased tissues release their molecule content to the bloodstream in free form, inside a cell or within extracellular vesicles (EVs). While the identification of molecular alterations in total DNA isolated from peripheral blood is already in use for some tumors that secrete large amounts of DNA, it is challenging to assay those secreting lower amounts of molecules as well as for many other non-tumoral pathologies like immunological and cardiovascular diseases. In this scenery, the compartment of diseased tissue-derived EVs will be one of the best alternatives for the detection and identification of current and new biomarkers and targets in the clinical management of these diseases. Here, we review the mechanisms of molecular internalization as well as the correlation of EV's cargo with clinical parameters in tumor and non-tumor diseases, with special emphasis in clinical application. (c) 2017 Elsevier Ltd. All rights reserved.
C1 [Garcia-Romero, Noemi; Carrion-Navarro, Josefa; Belda-Iniesta, Cristobal; Ayuso-Sacido, Angel] HM Hosp, Fdn Invest, C Ona 10, Madrid 28050, Spain.
   [Esteban-Rubio, Susana; Ayuso-Sacido, Angel] Univ San Pablo CEU, Fac Med IMMA, Madrid, Spain.
   [Rackov, Gorjana; Ayuso-Sacido, Angel] IMDEA Nanosci, Madrid, Spain.
C3 San Pablo CEU University; IMDEA Nanociencia
RP Ayuso-Sacido, A (corresponding author), HM Hosp, Fdn Invest, C Ona 10, Madrid 28050, Spain.
EM ayusosacido@gmail.com
RI Rackov, Gorjana/AAC-4954-2021; Sacido, Angel/AAV-9331-2021
OI Carrion-Navarro, Josefa/0000-0001-6661-1240; GARCIA-ROMERO,
   NOEMI/0000-0001-7744-8848; Rackov, Gorjana/0000-0001-6561-6357;
   Ayuso-Sacido, Angel/0000-0003-3919-5880; Belda Iniesta,
   Cristobal/0000-0003-3254-7492
FU Fondo de Investigaciones Sanitarias (FIS) [PI14_00077, PI17/01489];
   Miguel Servet Program del Instituto de Salud Carlos III (AAS)
   [CP11/00147]; Ministerio de Economia y Competitividad [RTC-2016-4990-1,
   RTC-2015-3846-1]; FEDER funds; FPI-CEU predoctoral fellowship
FX We are grateful for the financial support from the 'Fondo de
   Investigaciones Sanitarias (FIS) (PI14_00077, PI17/01489), the Miguel
   Servet Program (CP11/00147) del Instituto de Salud Carlos III (AAS), and
   the RTC-2016-4990-1 and RTC-2015-3846-1 from Ministerio de Economia y
   Competitividad and FEDER funds. SER was supported by FPI-CEU predoctoral
   fellowship.
CR Alegre E, 2016, CLIN CHIM ACTA, V454, P28, DOI 10.1016/j.cca.2015.12.031
   Allenson K, 2017, ANN ONCOL, V28, P741, DOI 10.1093/annonc/mdx004
   Amabile N, 2005, J AM SOC NEPHROL, V16, P3381, DOI 10.1681/ASN.2005050535
   Andriole G, 2006, EUR UROL SUPPL, V5, P737, DOI 10.1016/j.eursup.2006.06.013
   Babst M., 2012, EVERYTHING, V23, P452, DOI [10.1016/j.ceb.2011.04.008.MVB, DOI 10.1016/J.CEB.2011.04.008.MVB]
   Balaj L, 2011, NAT COMMUN, V2, DOI 10.1038/ncomms1180
   Berckmans RJ, 2002, ARTHRITIS RHEUM-US, V46, P2857, DOI 10.1002/art.10587
   Berckmans RJ, 2001, THROMB HAEMOSTASIS, V85, P639
   Bernal-Mizrachi L, 2003, AM HEART J, V145, P962, DOI 10.1016/S0002-8703(03)00103-0
   Bettaieb A, 2017, J TRANSL MED, V15, DOI 10.1186/s12967-017-1239-z
   Bi SJ, 2015, INT J CLIN EXP MED, V8, P4275
   Bobryshev YV, 2013, PATHOBIOLOGY, V80, P24, DOI 10.1159/000339430
   Boilard E, 2010, SCIENCE, V327, P580, DOI 10.1126/science.1181928
   Bolukbasi MF, 2012, MOL THER-NUCL ACIDS, V1, DOI 10.1038/mtna.2011.2
   Boulanger CM, 2006, HYPERTENSION, V48, P180, DOI 10.1161/01.HYP.0000231507.00962.b5
   Bournet B, 2016, CLIN TRANSL GASTROEN, V7, DOI 10.1038/ctg.2016.18
   Brinkmann K, 2015, CANCER RES, V75, DOI 10.1158/1538-7445.AM2015-545
   Bucciarelli P, 2012, THROMB RES, V129, P591, DOI 10.1016/j.thromres.2011.08.020
   Byers LA, 2015, CANCER-AM CANCER SOC, V121, P664, DOI 10.1002/cncr.29098
   Campello E, 2015, THROMB RES, V136, P427, DOI 10.1016/j.thromres.2015.05.029
   Campello E, 2011, THROMB RES, V127, P473, DOI 10.1016/j.thromres.2011.01.002
   Cance W. G., IMMUNOHISTOCHEMICAL
   Chirinos JA, 2005, J AM COLL CARDIOL, V45, P1467, DOI 10.1016/j.jacc.2004.12.075
   Chiva-Blanch G, 2016, INT J CARDIOL, V208, P147, DOI 10.1016/j.ijcard.2016.01.211
   Collins JA, 1997, J HISTOCHEM CYTOCHEM, V45, P923, DOI 10.1177/002215549704500702
   Colombo M., 2011, COMPOSITION SECRETIO
   de Gassart A, 2003, BLOOD, V102, P4336, DOI 10.1182/blood-2003-03-0871
   Ding WX, 2012, BIOL CHEM, V393, P547, DOI 10.1515/hsz-2012-0119
   Distler JHW, 2005, P NATL ACAD SCI USA, V102, P2892, DOI 10.1073/pnas.0409781102
   Emanueli C, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0154274
   Gabriel K, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0070047
   Galindo-Hernandez O., 2013, ARCH MED RES
   Garcia N., 2016, Sistema nacional de monitoreo de la biodiversidad, P1, DOI DOI 10.1109/SPAWC.2016.7536855
   Guduric-Fuchs J, 2012, BMC GENOMICS, V13, DOI 10.1186/1471-2164-13-357
   Guescini M, 2010, J NEURAL TRANSM, V117, P1, DOI 10.1007/s00702-009-0288-8
   Haggar Fatima A, 2009, Clin Colon Rectal Surg, V22, P191, DOI 10.1055/s-0029-1242458
   Hannafon BN, 2013, INT J MOL SCI, V14, P14240, DOI 10.3390/ijms140714240
   Hansson GK, 2005, NEW ENGL J MED, V352, P1685, DOI 10.1056/NEJMra043430
   Hao Y, 2017, SCI PROGRAMMING-NETH, V2017, DOI 10.1155/2017/2573592
   Hoefer IE, 2015, EUR HEART J, V36, P2635, DOI 10.1093/eurheartj/ehv236
   Iavello A, 2016, INT J MOL MED, V37, P958, DOI 10.3892/ijmm.2016.2488
   Im H, 2014, NAT BIOTECHNOL, V32, P490, DOI 10.1038/nbt.2886
   Jansen F, 2014, J AM HEART ASSOC, V3, DOI 10.1161/JAHA.114.001249
   Jemal Ahmedin, 2011, CA Cancer J Clin, V61, P69, DOI 10.3322/caac.20107
   Jonas R., 2015, ONCOTARGET, V7
   Kalra H, 2012, PLOS BIOL, V10, DOI 10.1371/journal.pbio.1001450
   Keyel PA, 2012, J IMMUNOL, V189, P4621, DOI 10.4049/jimmunol.1200828
   Khan S, 2014, BMC CANCER, V14, DOI 10.1186/1471-2407-14-176
   Khan S, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0046737
   Knijff-Dutmer EAJ, 2002, ARTHRITIS RHEUM-US, V46, P1498, DOI 10.1002/art.10312
   Koga H, 2005, J AM COLL CARDIOL, V45, P1622, DOI 10.1016/j.jacc.2005.02.047
   Koppers-Lalic D, 2014, CELL REP, V8, P1649, DOI 10.1016/j.celrep.2014.08.027
   Kosaka N, 2013, J BIOL CHEM, V288, P10849, DOI 10.1074/jbc.M112.446831
   Kruh-Garcia N., 2012, INTECHOPEN, V552
   Lázaro-Ibáñez E, 2014, PROSTATE, V74, P1379, DOI 10.1002/pros.22853
   Ldl L., 2000, LDL CHOLESTEROL STRO
   Leroyer AS, 2007, J AM COLL CARDIOL, V49, P772, DOI 10.1016/j.jacc.2006.10.053
   Li CCY, 2013, RNA BIOL, V10, P1333, DOI 10.4161/rna.25281
   Li J, 2017, J CELL MOL MED, V21, P838, DOI 10.1111/jcmm.12941
   Li YY, 2011, ELECTROPHORESIS, V32, P1976, DOI 10.1002/elps.201000598
   Lièvre A, 2008, J CLIN ONCOL, V26, P374, DOI 10.1200/JCO.2007.12.5906
   Lindahl B, 2000, NEW ENGL J MED, V343, P1139, DOI 10.1056/NEJM200010193431602
   Louis DN, 2016, ACTA NEUROPATHOL, V131, P803, DOI 10.1007/s00401-016-1545-1
   Machala M., 2014, SYNTENIN ALIX EXOSOM
   Manda SV., 2017, J NEUROSURG, P1
   Manterola L, 2014, NEURO-ONCOLOGY, V16, P520, DOI 10.1093/neuonc/not218
   McKiernan J, 2016, JAMA ONCOL, V2, P882, DOI 10.1001/jamaoncol.2016.0097
   Melo SA, 2014, CANCER CELL, V26, P707, DOI 10.1016/j.ccell.2014.09.005
   Menck K., 2015, J MOL CELL BIOL
   Miyake T, 2012, CANCER SCI, V103, P913, DOI 10.1111/j.1349-7006.2012.02231.x
   Momen-Heravi F, 2015, J TRANSL MED, V13, DOI 10.1186/s12967-015-0623-9
   Moon PG, 2016, ONCOTARGET, V7, P40189, DOI 10.18632/oncotarget.9561
   Moon PG, 2016, CLIN CANCER RES, V22, P1757, DOI 10.1158/1078-0432.CCR-15-0654
   Nielsen CT, 2011, ARTHRITIS RHEUM-US, V63, P3067, DOI 10.1002/art.30499
   Nielsen TO, 2004, CLIN CANCER RES, V10, P5367, DOI 10.1158/1078-0432.CCR-04-0220
   Nilsson J, 2009, BRIT J CANCER, V100, P1603, DOI 10.1038/sj.bjc.6605058
   Nozaki T, 2009, J AM COLL CARDIOL, V54, P601, DOI 10.1016/j.jacc.2009.05.022
   Okano T, 2006, PROTEOMICS, V6, P3938, DOI 10.1002/pmic.200500883
   Parker B, 2014, ANN RHEUM DIS, V73, P1144, DOI 10.1136/annrheumdis-2012-203028
   Peeters M, 2015, EUR J CANCER, V51, P1704, DOI 10.1016/j.ejca.2015.05.017
   Peinado H, 2012, NAT MED, V18, P883, DOI 10.1038/nm.2753
   Perez-Hernandez J, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0138618
   Perrotta I, 2016, ULTRASTRUCT PATHOL, V40, P101, DOI 10.3109/01913123.2016.1154912
   Poruk KE, 2013, CURR MOL MED, V13, P340
   Radu CM, 2015, SCAND J CLIN LAB INV, V75, P487, DOI 10.3109/00365513.2015.1052551
   Rodriguez PG, 2010, THROMB RES, V126, P345, DOI 10.1016/j.thromres.2010.07.006
   Ryan B, 2005, BRIT J CANCER, V92, P120, DOI 10.1038/sj.bjc.6602314
   Sameshima T, 2000, INT J CANCER, V88, P21, DOI 10.1002/1097-0215(20001001)88:1<21::AID-IJC4>3.0.CO;2-S
   Santiago-Dieppa DR, 2014, EXPERT REV MOL DIAGN, V14, P819, DOI 10.1586/14737159.2014.943193
   Sarlon-Bartoli G, 2013, J AM COLL CARDIOL, V62, P1436, DOI 10.1016/j.jacc.2013.03.078
   Sartori MT, 2013, THROMB HAEMOSTASIS, V110, P378, DOI 10.1160/TH12-12-0957
   Shao HL, 2012, NAT MED, V18, P1835, DOI 10.1038/nm.2994
   Shariat SF, 2011, ACTA ONCOL, V50, P61, DOI 10.3109/0284186X.2010.542174
   Shen BY, 2011, J BIOL CHEM, V286, P14383, DOI 10.1074/jbc.M110.208660
   Shurtleff M. J., 2016, CELLS CELL FREE REAC, P1
   Siegel RL, 2020, CA-CANCER J CLIN, V70, P7, DOI 10.3322/caac.21590
   Sinning JM, 2011, EUR HEART J, V32, P2034, DOI 10.1093/eurheartj/ehq478
   Skog J, 2008, NAT CELL BIOL, V10, P1470, DOI 10.1038/ncb1800
   Soda M, 2007, NATURE, V448, P561, DOI 10.1038/nature05945
   Solé C, 2015, NEPHROL DIAL TRANSPL, V30, P1488, DOI 10.1093/ndt/gfv128
   Stiksma J., 2014, CLIN COLORECTAL CANC
   Strotman LN, 2016, MOL DIAGN THER, V20, P429, DOI 10.1007/s40291-016-0220-5
   Subra C, 2007, BIOCHIMIE, V89, P205, DOI 10.1016/j.biochi.2006.10.014
   Takahashi T, 2012, THORAX, V67, P1067, DOI 10.1136/thoraxjnl-2011-201395
   Tan KT, 2005, DIABETIC MED, V22, P1657, DOI 10.1111/j.1464-5491.2005.01707.x
   Tang SC, 2014, WORLD J GASTROENTERO, V20, P10825, DOI 10.3748/wjg.v20.i31.10825
   Tesselaar MET, 2009, J THROMB HAEMOST, V7, P1421, DOI 10.1111/j.1538-7836.2009.03504.x
   Tetta C, 2013, ENDOCRINE, V44, P11, DOI 10.1007/s12020-012-9839-0
   Therkildsen C, 2014, ACTA ONCOL, V53, P852, DOI 10.3109/0284186X.2014.895036
   Thierry AR, 2014, NAT MED, V20, P430, DOI 10.1038/nm.3511
   Thomas Parsons J., 2003, J CELL SCI, V116, P1409
   Thompson JC, 2016, CLIN CANCER RES, V22, P5772, DOI 10.1158/1078-0432.CCR-16-1231
   van der Vos K. E., 2015, NEUROONCOL, V18
   Villarroya-Beltri C, 2013, NAT COMMUN, V4, DOI 10.1038/ncomms3980
   Vinuela-Berni V, 2015, CLIN EXP IMMUNOL, V180, P442, DOI 10.1111/cei.12598
   Wendelboe AM, 2016, CIRC RES, V118, P1340, DOI 10.1161/CIRCRESAHA.115.306841
   Williams C, 2014, CELL RES, V24, P766, DOI 10.1038/cr.2014.44
   Witwer KW, 2013, J EXTRACELL VESICLES, V2, DOI 10.3402/jev.v2i0.20360
   Yamashita T, 2013, PHARMAZIE, V68, P969, DOI 10.1691/ph.2013.3599
   Yáñez-Mó M, 2015, J EXTRACELL VESICLES, V4, DOI 10.3402/jev.v4.27066
   Yang G, 2005, CANCER-AM CANCER SOC, V103, P52, DOI 10.1002/cncr.20729
   Yang S.J., 2017, GENE
   Zhang XG, 2014, J THROMB THROMBOLYS, V37, P455, DOI 10.1007/s11239-013-1000-2
   Zhou L, 2014, ACTA PHARMACOL SIN, V35, P1103, DOI 10.1038/aps.2014.73
   Zwicker JI, 2013, BRIT J HAEMATOL, V160, P530, DOI 10.1111/bjh.12163
NR 125
TC 60
Z9 64
U1 0
U2 28
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
SN 0098-2997
EI 1872-9452
J9 MOL ASPECTS MED
JI Mol. Asp. Med.
PD APR
PY 2018
VL 60
BP 27
EP 37
DI 10.1016/j.mam.2017.11.009
PG 11
WC Biochemistry & Molecular Biology; Medicine, Research & Experimental
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Research & Experimental Medicine
GA FZ2RF
UT WOS:000427428000003
PM 29155161
DA 2025-04-10
ER

PT J
AU Gilpin, BJ
   Loechel, F
   Mattei, MG
   Engvall, E
   Albrechtsen, R
   Wewer, UM
AF Gilpin, BJ
   Loechel, F
   Mattei, MG
   Engvall, E
   Albrechtsen, R
   Wewer, UM
TI A novel, secreted form of human ADAM 12 (meltrin α) provokes myogenesis
   in vivo
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID SPERM-EGG FUSION; DISINTEGRIN-LIKE; METALLOPROTEASE; GENE; LAMININ;
   FAMILY; PROTEIN; DOMAINS; CELL; HYBRIDIZATION
AB The ADAM (A Disintegrin And Metalloprotease) family of cell-surface proteins may have an important role in cellular interactions and in modulating cellular responses, In this report we describe a novel, secreted form of human ADAM 12 (meltrin alpha), designated ADAM 12-S (S for short), and a larger, membrane-bound form designated ADAM 12-L (L for long form). These two forms arise by alternative splicing of a single gene located on chromosome 10q26. Northern blotting demonstrated that mRNAs of both forms are abundant in human term placenta and are also present in some tumor cell lines. The ADAM 12-L transcript can also be detected in normal human adult skeletal, cardiac, and smooth muscle. Human A204 embryonal rhabdomyosarcoma cells that do not differentiate into muscle cells and do not express any form of ADAM 12 were stably transfected with an ADAM 12-S minigene encoding the disintegrin domain, the cysteine-rich domain, and the unique 34 amino acid carboxyl terminus. Nude mouse tumors derived from these transfected cells contained ectopic muscle cells of apparent mouse origin as shown by species-specific markers. These results may have potential applications in the development of muscle-directed gene and cell therapies.
C1 Univ Copenhagen, Inst Mol Pathol, DK-2100 Copenhagen, Denmark.
   Fac Med Timone, F-13385 Marseille, France.
   Burnham Inst, La Jolla, CA 92037 USA.
C3 University of Copenhagen; Aix-Marseille Universite; Assistance
   Publique-Hopitaux de Marseille; Sanford Burnham Prebys Medical Discovery
   Institute
RP Wewer, UM (corresponding author), Univ Copenhagen, Inst Mol Pathol, Frederik V Vej 11, DK-2100 Copenhagen, Denmark.
RI ; Gilpin, Brent/E-3463-2013
OI Albrechtsen, Reidar/0000-0003-4180-1827; Gilpin,
   Brent/0000-0002-8109-2271
CR Alfandari D, 1997, DEV BIOL, V182, P314, DOI 10.1006/dbio.1996.8458
   ALMEIDA EAC, 1995, CELL, V81, P1095, DOI 10.1016/S0092-8674(05)80014-5
   ALTSCHUL SF, 1990, J MOL BIOL, V215, P403, DOI 10.1016/S0022-2836(05)80360-2
   Bigler D, 1997, TRENDS CELL BIOL, V7, P220, DOI 10.1016/S0962-8924(97)01058-1
   Bischoff R., 1994, SATELLITE CELL MUSCL, P97
   Black RA, 1997, NATURE, V385, P729, DOI 10.1038/385729a0
   Blaumueller CM, 1997, CELL, V90, P281, DOI 10.1016/S0092-8674(00)80336-0
   BLOBEL CP, 1992, NATURE, V356, P248, DOI 10.1038/356248a0
   Blobel CP, 1997, CELL, V90, P589, DOI 10.1016/S0092-8674(00)80519-X
   BUONANNO A, 1992, NUCLEIC ACIDS RES, V20, P539, DOI 10.1093/nar/20.3.539
   Burkin HR, 1997, GENOMICS, V40, P190, DOI 10.1006/geno.1996.4531
   CAMPBELL ID, 1993, CURR OPIN STRUC BIOL, V3, P385, DOI 10.1016/S0959-440X(05)80111-3
   Cho CH, 1996, GENOMICS, V34, P413, DOI 10.1006/geno.1996.0305
   EdwaldsGilbert G, 1997, NUCLEIC ACIDS RES, V25, P2547, DOI 10.1093/nar/25.13.2547
   EMI M, 1993, NAT GENET, V5, P151, DOI 10.1038/ng1093-151
   ENGVALL E, 1986, J CELL BIOL, V103, P2457, DOI 10.1083/jcb.103.6.2457
   Fambrough D, 1996, P NATL ACAD SCI USA, V93, P13233, DOI 10.1073/pnas.93.23.13233
   Fox J.W., 1996, Zinc Metalloproteinases in Health and Disease, P47
   HITE LA, 1994, ARCH BIOCHEM BIOPHYS, V308, P182, DOI 10.1006/abbi.1994.1026
   Huovila APJ, 1996, CURR OPIN CELL BIOL, V8, P692, DOI 10.1016/S0955-0674(96)80111-6
   Jury JA, 1997, BIOCHEM J, V321, P577, DOI 10.1042/bj3210577
   KATAGIRI T, 1995, CYTOGENET CELL GENET, V68, P39, DOI 10.1159/000133884
   Kuno K, 1997, J BIOL CHEM, V272, P556, DOI 10.1074/jbc.272.1.556
   LANDOLTMARTICORENA C, 1993, J MOL BIOL, V229, P602, DOI 10.1006/jmbi.1993.1066
   LEMIEUX N, 1992, CYTOGENET CELL GENET, V59, P311, DOI 10.1159/000133277
   MAYER BJ, 1995, CURR BIOL, V5, P364, DOI 10.1016/S0960-9822(95)00073-X
   Moss ML, 1997, NATURE, V385, P733, DOI 10.1038/385733a0
   MYLES DG, 1994, P NATL ACAD SCI USA, V91, P4195, DOI 10.1073/pnas.91.10.4195
   OTT MO, 1991, DEVELOPMENT, V111, P1097
   PAINE MJI, 1992, J BIOL CHEM, V267, P22869
   Pan DJ, 1997, CELL, V90, P271, DOI 10.1016/S0092-8674(00)80335-9
   PERRY ACF, 1995, BIOCHEM J, V312, P239, DOI 10.1042/bj3120239
   PERRY ACF, 1995, BIOCHEM J, V307, P843, DOI 10.1042/bj3070843
   PINKEL D, 1986, P NATL ACAD SCI USA, V83, P2934, DOI 10.1073/pnas.83.9.2934
   RAWLINGS ND, 1995, METHOD ENZYMOL, V248, P183
   Rooke J, 1996, SCIENCE, V273, P1227, DOI 10.1126/science.273.5279.1227
   Sambrook J, 1989, MOL CLONING LAB MANU
   SANES JR, 1990, J CELL BIOL, V111, P1685, DOI 10.1083/jcb.111.4.1685
   Schuler GD, 1996, SCIENCE, V274, P540, DOI 10.1126/science.274.5287.540
   Shilling FM, 1997, DEV BIOL, V186, P155, DOI 10.1006/dbio.1997.8586
   Vachon PH, 1996, J CELL BIOL, V134, P1483, DOI 10.1083/jcb.134.6.1483
   Vidaeus CM, 1997, MOL REPROD DEV, V46, P363
   VONHEIJNE G, 1986, NUCLEIC ACIDS RES, V14, P4683, DOI 10.1093/nar/14.11.4683
   Weskamp G, 1996, J CELL BIOL, V132, P717, DOI 10.1083/jcb.132.4.717
   WEWER UM, 1994, LAB INVEST, V71, P719
   Wewer UM, 1997, AM J PATHOL, V151, P621
   WOLFSBERG TG, 1995, J CELL BIOL, V131, P275, DOI 10.1083/jcb.131.2.275
   Wolfsberg TG, 1996, DEV BIOL, V180, P389, DOI 10.1006/dbio.1996.0313
   YAGAMIHIROMASA T, 1995, NATURE, V377, P652, DOI 10.1038/377652a0
   Yoshiyama K, 1997, GENOMICS, V41, P56, DOI 10.1006/geno.1997.4607
NR 50
TC 269
Z9 309
U1 0
U2 4
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA
SN 0021-9258
J9 J BIOL CHEM
JI J. Biol. Chem.
PD JAN 2
PY 1998
VL 273
IS 1
BP 157
EP 166
DI 10.1074/jbc.273.1.157
PG 10
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA YP612
UT WOS:000071295600026
PM 9417060
OA hybrid
DA 2025-04-10
ER

PT J
AU Jatooratthawichot, P
   Talabnin, C
   Ngiwsara, L
   Rustam, YH
   Svasti, J
   Reid, GE
   Cairns, JRK
AF Jatooratthawichot, Peeranat
   Talabnin, Chutima
   Ngiwsara, Lukana
   Rustam, Yepy Hardi
   Svasti, Jisnuson
   Reid, Gavin E.
   Ketudat Cairns, James R.
TI Effect of Expression of Human Glucosylceramidase 2 Isoforms on Lipid
   Profiles in COS-7 Cells
SO METABOLITES
LA English
DT Article
DE glycolipids; sphingolipids; cerebrosides; ceramides; lipidomics;
   enzymology
ID BETA-GLUCOSIDASE GBA2; MOLECULAR-CLONING; GLUCOCEREBROSIDASE;
   IDENTIFICATION; DEGRADATION; CHOLESTEROL; DEFICIENT; CERAMIDE; MUTATION;
   DEFECTS
AB Glucosylceramide (GlcCer) is a major membrane lipid and the precursor of gangliosides. GlcCer is mainly degraded by two enzymes, lysosomal acid beta-glucosidase (GBA) and nonlysosomal beta-glucosidase (GBA2), which may have different isoforms because of alternative splicing. To understand which GBA2 isoforms are active and how they affect glycosphingolipid levels in cells, we expressed nine human GBA2 isoforms in COS-7 cells, confirmed their expression by qRT-PCR and Western blotting, and assayed their activity to hydrolyze 4-methylumbelliferyl-beta-D-glucopyranoside (4MUG) in cell extracts. Human GBA2 isoform 1 showed high activity, while the other isoforms had activity similar to the background. Comparison of sphingolipid levels by ultra-high resolution/accurate mass spectrometry (UHRAMS) analysis showed that isoform 1 overexpression increased ceramide and decreased hexosylceramide levels. Comparison of ratios of glucosylceramides to the corresponding ceramides in the extracts indicated that GBA2 isoform 1 has broad specificity for the lipid component of glucosylceramide, suggesting that only one GBA2 isoform 1 is active and affects sphingolipid levels in the cell. Our study provides new insights into how increased breakdown of GlcCer affects cellular lipid metabolic networks.
C1 [Jatooratthawichot, Peeranat; Talabnin, Chutima; Ketudat Cairns, James R.] Suranaree Univ Technol, Inst Sci, Sch Chem, Nakhon Ratchasima 30000, Thailand.
   [Jatooratthawichot, Peeranat; Ketudat Cairns, James R.] Suranaree Univ Technol, Ctr Biomol Struct Funct & Applicat, Nakhon Ratchasima 3000, Thailand.
   [Ngiwsara, Lukana; Svasti, Jisnuson; Ketudat Cairns, James R.] Chulabhorn Res Inst, Lab Biochem, Bangkok 10210, Thailand.
   [Rustam, Yepy Hardi; Reid, Gavin E.] Univ Melbourne, Dept Biochem & Mol Biol, Parkville, Vic 3010, Australia.
   [Reid, Gavin E.] Univ Melbourne, Sch Chem, Mol Sci & Biotechnol Inst Bio21, Parkville, Vic 3010, Australia.
C3 Suranaree University of Technology; Suranaree University of Technology;
   Chulabhorn Research Institute; University of Melbourne; University of
   Melbourne
RP Cairns, JRK (corresponding author), Suranaree Univ Technol, Inst Sci, Sch Chem, Nakhon Ratchasima 30000, Thailand.; Cairns, JRK (corresponding author), Suranaree Univ Technol, Ctr Biomol Struct Funct & Applicat, Nakhon Ratchasima 3000, Thailand.; Cairns, JRK (corresponding author), Chulabhorn Res Inst, Lab Biochem, Bangkok 10210, Thailand.; Reid, GE (corresponding author), Univ Melbourne, Dept Biochem & Mol Biol, Parkville, Vic 3010, Australia.; Reid, GE (corresponding author), Univ Melbourne, Sch Chem, Mol Sci & Biotechnol Inst Bio21, Parkville, Vic 3010, Australia.
EM pj.cbsfa@gmail.com; chutima.sub@sut.ac.th; lukana@cri.or.th;
   yrustam@student.unimelb.edu.au; jisnuson@cri.or.th;
   gavin.reid@unimelb.edu.au; cairns@sut.ac.th
RI Svasti, Jisnuson/HTR-3880-2023; Ketudat Cairns, James/B-6407-2019
OI Svasti, Jisnuson/0000-0002-2217-4517; Ketudat Cairns,
   James/0000-0003-3042-1626; Jatooratthawichot,
   Peeranat/0000-0002-4646-1860; Rustam, Yepy Hardi/0000-0002-1298-9034
FU Suranaree University of Technology; National Research University Project
   of the Commission on Higher Education; Australian Research Council
   [LE160100015]; Development and a Promotion of Science and Technology
   Talents Project scholarship; Australian Research Council [LE160100015]
   Funding Source: Australian Research Council
FX Financial support was provided by Suranaree University of Technology,
   including the National Research University Project of the Commission on
   Higher Education, and also from the Australian Research Council to GER
   (LE160100015). PJ was supported by a Development and a Promotion of
   Science and Technology Talents Project scholarship.
CR Abdul-Hammed M, 2017, J LIPID RES, V58, P563, DOI 10.1194/jlr.M073510
   Akiyama H, 2020, J BIOL CHEM, V295, P5257, DOI 10.1074/jbc.RA119.012502
   Akiyama H, 2013, BIOCHEM BIOPH RES CO, V441, P838, DOI 10.1016/j.bbrc.2013.10.145
   Bielawski J, 2006, METHODS, V39, P82, DOI 10.1016/j.ymeth.2006.05.004
   Boot RG, 2007, J BIOL CHEM, V282, P1305, DOI 10.1074/jbc.M610544200
   Bouscary A, 2019, FRONT PHARMACOL, V10, DOI 10.3389/fphar.2019.00883
   Burke DG, 2013, J INHERIT METAB DIS, V36, P869, DOI 10.1007/s10545-012-9561-3
   Charoenwattanasatien R, 2016, ACS CHEM BIOL, V11, P1891, DOI 10.1021/acschembio.6b00192
   Couttas TA, 2020, METABOLITES, V10, DOI 10.3390/metabo10060236
   D'Angelo G, 2007, NATURE, V449, P62, DOI 10.1038/nature06097
   Hammer MB, 2013, AM J HUM GENET, V92, P245, DOI 10.1016/j.ajhg.2012.12.012
   Hannun YA, 2008, NAT REV MOL CELL BIO, V9, P139, DOI 10.1038/nrm2329
   Haugarvoll K, 2017, PLOS ONE, V12, DOI 10.1371/journal.pone.0169309
   Kakouri AC, 2020, INT J MOL SCI, V21, DOI 10.3390/ijms21186722
   Körschen HG, 2013, J BIOL CHEM, V288, P3381, DOI 10.1074/jbc.M112.414714
   La Cognata V, 2015, NEUROGENETICS, V16, P245, DOI 10.1007/s10048-015-0449-x
   Lee RG, 2020, J CELL SCI, V133, DOI 10.1242/jcs.240374
   Lydic TA, 2015, METHODS, V87, P83, DOI 10.1016/j.ymeth.2015.04.014
   Lydic TA, 2014, J LIPID RES, V55, P1797, DOI 10.1194/jlr.D050302
   Malekkou A, 2020, MOL GENET GENOM MED, V8, DOI 10.1002/mgg3.1090
   Malekkou A, 2018, INT J MOL SCI, V19, DOI 10.3390/ijms19103099
   Marques ARA, 2016, J LIPID RES, V57, P451, DOI 10.1194/jlr.M064923
   Marques ARA, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0135889
   Martin E, 2013, AM J HUM GENET, V92, P238, DOI 10.1016/j.ajhg.2012.11.021
   Matern H, 2001, J BIOL CHEM, V276, P37929
   Matern H, 1997, J BIOL CHEM, V272, P11261
   Mistry PK, 2014, P NATL ACAD SCI USA, V111, P4934, DOI 10.1073/pnas.1400768111
   Nastase A, 2020, CANCER GENOM PROTEOM, V17, P587, DOI 10.21873/cgp.20215
   Ogura K, 2002, NEUROCHEM RES, V27, P779, DOI 10.1023/A:1020252823191
   Radin NS, 2003, BIOORGAN MED CHEM, V11, P2123, DOI 10.1016/S0968-0896(02)00609-0
   Raju D, 2015, PLOS GENET, V11, DOI 10.1371/journal.pgen.1005063
   Ridley CM, 2013, J BIOL CHEM, V288, P26052, DOI 10.1074/jbc.M113.463562
   Sakamoto W, 2018, J LIPID RES, V59, P2116, DOI 10.1194/jlr.M088187
   SARMIENTOS F, 1986, EUR J BIOCHEM, V160, P527, DOI 10.1111/j.1432-1033.1986.tb10071.x
   Schonauer S, 2017, J BIOL CHEM, V292, P6177, DOI 10.1074/jbc.M116.762831
   SHAPIRO SS, 1965, BIOMETRIKA, V52, P591, DOI 10.1093/biomet/52.3-4.591
   Sorli SC, 2013, FASEB J, V27, P489, DOI 10.1096/fj.12-215152
   Sultana S, 2020, PLOS ONE, V15, DOI 10.1371/journal.pone.0233856
   Sultana S, 2015, BIOCHEM BIOPH RES CO, V465, P35, DOI 10.1016/j.bbrc.2015.07.112
   Summers SA, 2006, PROG LIPID RES, V45, P42, DOI 10.1016/j.plipres.2005.11.002
   Tracey TJ, 2018, FRONT MOL NEUROSCI, V11, DOI 10.3389/fnmol.2018.00010
   VANWEELY S, 1993, BIOCHIM BIOPHYS ACTA, V1181, P55, DOI 10.1016/0925-4439(93)90090-N
   Votsi C, 2014, ANN HUM GENET, V78, P13, DOI 10.1111/ahg.12045
   Ward AJ, 2010, J PATHOL, V220, P152, DOI 10.1002/path.2649
   Waterhouse A, 2018, NUCLEIC ACIDS RES, V46, pW296, DOI 10.1093/nar/gky427
   Wilkening G, 1998, J BIOL CHEM, V273, P30271, DOI 10.1074/jbc.273.46.30271
   Xu YH, 2011, MOL GENET METAB, V102, P436, DOI 10.1016/j.ymgme.2010.12.014
   Yildiz Y, 2006, J CLIN INVEST, V116, P2985, DOI 10.1172/JCI29224
   Zeidan YH, 2007, TRENDS MOL MED, V13, P327, DOI 10.1016/j.molmed.2007.06.002
   Zhou HL, 1998, J BIOL CHEM, V273, P16568, DOI 10.1074/jbc.273.26.16568
NR 50
TC 8
Z9 8
U1 0
U2 7
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
EI 2218-1989
J9 METABOLITES
JI Metabolites
PD DEC
PY 2020
VL 10
IS 12
AR 488
DI 10.3390/metabo10120488
PG 19
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA PK0YZ
UT WOS:000602182100001
PM 33261081
OA Green Submitted, Green Published, gold
DA 2025-04-10
ER

PT J
AU Kuo, IYT
   Wölfle, SE
   Hill, CE
AF Kuo, Ivana Y. -T.
   Woelfle, Stephanie E.
   Hill, Caryl E.
TI T-type calcium channels and vascular function: the new kid on the block?
SO JOURNAL OF PHYSIOLOGY-LONDON
LA English
DT Review
ID SMOOTH-MUSCLE-CELLS; CAPILLARY ENDOTHELIAL-CELLS; TERMINAL
   MESENTERIC-ARTERY; RAT BASILAR ARTERY; CA2+ CHANNELS; GUINEA-PIG;
   CEREBRAL-ARTERIES; K+ CHANNELS; SUBARACHNOID HEMORRHAGE; ALTERNATIVE
   STRUCTURES
AB While L-type voltage-dependent calcium channels have long been considered the predominant source of calcium for myogenic constriction, recent studies of both cerebral and systemic circulations have provided evidence for the prominent expression of other members of the voltage-dependent calcium channel family, in particular the low voltage activated T-type channels. Although physiological studies have not supported the involvement of a classical low voltage activated, T-type channel in vascular function, evidence is accumulating that points to the involvement of a non-L-type, high voltage activated channel with sensitivity to T-type channel antagonists. We propose that this may arise due to expression of a T-type channel splice variant with unique biophysical characteristics resulting in a more depolarised profile. Expression of these channels in smooth muscle cells would broaden the voltage range over which sustained calcium influx occurs, while expression of T-type channels in endothelial cells could provide a feedback mechanism to prevent excessive vasoconstriction. Perturbation of this balance during pathophysiological conditions by upregulation of channel expression and endothelial dysfunction could contribute to vasospastic conditions and therapy-refractory hypertension.
C1 [Kuo, Ivana Y. -T.; Woelfle, Stephanie E.; Hill, Caryl E.] Australian Natl Univ, John Curtin Sch Med Res, Div Neurosci, Canberra, ACT 0200, Australia.
C3 Australian National University; John Curtin School of Medical Research
RP Hill, CE (corresponding author), Australian Natl Univ, John Curtin Sch Med Res, Div Neurosci, GPO Box 334, Canberra, ACT 0200, Australia.
EM caryl.hill@anu.edu.au
RI Hill, Caryl/D-8972-2011
OI Kuo, Ivana/0000-0002-9867-2408
FU National Health and Medical Research Council of Australia [471420]
FX The authors acknowledge financial support from the National Health and
   Medical Research Council of Australia (ID 471420).
CR Ball CJ, 2009, HYPERTENSION, V53, P654, DOI 10.1161/HYPERTENSIONAHA.108.125831
   Berra-Romani R, 2005, AM J PHYSIOL-HEART C, V289, pH137, DOI 10.1152/ajpheart.01156.2004
   BOSSU JL, 1989, FEBS LETT, V255, P377, DOI 10.1016/0014-5793(89)81126-3
   BOSSU JL, 1992, PFLUG ARCH EUR J PHY, V420, P200, DOI 10.1007/BF00374991
   BOSSU JL, 1992, FEBS LETT, V299, P239, DOI 10.1016/0014-5793(92)80123-X
   Braunstein TH, 2009, J VASC RES, V46, P138, DOI 10.1159/000151767
   BREGESTOVSKI PD, 1989, J MOL CELL CARDIOL, V21, P103, DOI 10.1016/0022-2828(89)90844-4
   Catterall WA, 2005, PHARMACOL REV, V57, P411, DOI 10.1124/pr.57.4.5
   Cens T, 2006, PROG BIOPHYS MOL BIO, V90, P104, DOI 10.1016/j.pbiomolbio.2005.05.013
   Chemin J, 2001, BIOPHYS J, V80, P1238, DOI 10.1016/S0006-3495(01)76100-0
   Chen CC, 2003, SCIENCE, V302, P1416, DOI 10.1126/science.1089268
   Cheng XY, 2007, J BIOL CHEM, V282, P29211, DOI 10.1074/jbc.M610623200
   Cheng XY, 2009, AM J PHYSIOL-HEART C, V297, pH680, DOI 10.1152/ajpheart.00109.2009
   Chiang CS, 2009, CIRC RES, V104, P522, DOI 10.1161/CIRCRESAHA.108.184051
   Chouabe C, 1998, MOL PHARMACOL, V54, P695
   Chuang RSI, 1998, NAT NEUROSCI, V1, P668, DOI 10.1038/3669
   Cueni L, 2008, NAT NEUROSCI, V11, P683, DOI 10.1038/nn.2124
   DAUT J, 1988, J PHYSIOL-LONDON, V402, P237, DOI 10.1113/jphysiol.1988.sp017202
   Dolphin AC, 1999, J PHYSIOL-LONDON, V519, P35, DOI 10.1111/j.1469-7793.1999.0035o.x
   Dolphin AC, 2009, CURR OPIN NEUROBIOL, V19, P237, DOI 10.1016/j.conb.2009.06.006
   Emerick MC, 2006, PROTEINS, V64, P320, DOI 10.1002/prot.20877
   Epstein Murray, 2007, J Clin Hypertens (Greenwich), V9, P2, DOI 10.1111/j.1524-6175.2007.06171.x
   FARACI FM, 1990, CIRC RES, V66, P8, DOI 10.1161/01.RES.66.1.8
   Feng MG, 2004, AM J PHYSIOL-RENAL, V286, pF331, DOI 10.1152/ajprenal.00251.2003
   Furukawa T, 2004, BRIT J PHARMACOL, V143, P1050, DOI 10.1038/sj.bjp.0705944
   Gomora JC, 1999, MOL PHARMACOL, V56, P1192, DOI 10.1124/mol.56.6.1192
   GORDIENKO DV, 1994, AM J PHYSIOL, V266, pF325, DOI 10.1152/ajprenal.1994.266.2.F325
   Green PJ, 2001, J PHYSIOL-LONDON, V533, P467, DOI 10.1111/j.1469-7793.2001.0467a.x
   Gustafsson F, 2001, AM J PHYSIOL-HEART C, V280, pH582, DOI 10.1152/ajpheart.2001.280.2.H582
   Hansen JP, 2004, J MOL CELL CARDIOL, V37, P1147, DOI 10.1016/j.yjmcc.2004.08.005
   Hansen PB, 2001, CIRC RES, V89, P630, DOI 10.1161/hh1901.097126
   Hayashi K, 2005, J PHARMACOL SCI, V99, P221, DOI 10.1254/jphs.FMJ05002X6
   Hayashi K, 2007, CIRC RES, V100, P342, DOI 10.1161/01.RES.0000256155.31133.49
   Heady TN, 2001, JPN J PHARMACOL, V85, P339, DOI 10.1254/jjp.85.339
   Hill CE, 2001, MED RES REV, V21, P1
   HIRANO Y, 1989, AM J PHYSIOL, V256, pH1478, DOI 10.1152/ajpheart.1989.256.5.H1478
   Hobom M, 2000, EUR J NEUROSCI, V12, P1217, DOI 10.1046/j.1460-9568.2000.01009.x
   Hu H, 1998, MOL PHARMACOL, V53, P902
   Huang LP, 2004, J PHARMACOL EXP THER, V309, P193, DOI 10.1124/jpet.103.060814
   Iftinca M, 2007, NAT NEUROSCI, V10, P854, DOI 10.1038/nn1921
   Ishiguro M, 2005, CIRC RES, V96, P419, DOI 10.1161/01.RES.0000157670.49936.da
   Jensen LJ, 2004, BRIT J PHARMACOL, V142, P709, DOI 10.1038/sj.bjp.0705841
   Kaku T, 2003, JPN J PHYSIOL, V53, P165, DOI 10.2170/jjphysiol.53.165
   Klöckner U, 1999, EUR J NEUROSCI, V11, P4171, DOI 10.1046/j.1460-9568.1999.00849.x
   Knot HJ, 1998, J PHYSIOL-LONDON, V508, P199, DOI 10.1111/j.1469-7793.1998.199br.x
   Koschak A, 2001, J BIOL CHEM, V276, P22100, DOI 10.1074/jbc.M101469200
   Kotecha N, 2005, AM J PHYSIOL-HEART C, V289, pH1326, DOI 10.1152/ajpheart.00323.2005
   Kuo IY, 2010, J CEREBR BLOOD F MET, V30, P1226, DOI 10.1038/jcbfm.2010.11
   Lacinová L, 2004, ARCH BIOCHEM BIOPHYS, V425, P207, DOI 10.1016/j.abb.2004.03.010
   LANGTON PD, 1993, J PHYSIOL-LONDON, V469, P535, DOI 10.1113/jphysiol.1993.sp019828
   Lee JH, 1999, BIOPHYS J, V77, P3034, DOI 10.1016/S0006-3495(99)77134-1
   Lee JH, 1999, J NEUROSCI, V19, P1912
   Li Z, 2010, J MEMBRANE BIOL, V233, P23, DOI 10.1007/s00232-009-9221-1
   Liao P, 2005, CARDIOVASC RES, V68, P197, DOI 10.1016/j.cardiores.2005.06.024
   Liao P, 2007, J BIOL CHEM, V282, P35133, DOI 10.1074/jbc.M705478200
   Loutzenhiser R, 1997, AM J PHYSIOL-RENAL, V273, pF307, DOI 10.1152/ajprenal.1997.273.2.F307
   Low AM, 1996, CLIN EXP PHARMACOL P, V23, P310, DOI 10.1111/j.1440-1681.1996.tb02829.x
   Mangoni ME, 2006, CIRC RES, V98, P1422, DOI 10.1161/01.RES.0000225862.14314.49
   Matchkov VV, 2004, J GEN PHYSIOL, V123, P121, DOI 10.1085/jgp.200308972
   McHugh D, 1996, J PHYSIOL-LONDON, V492, P359, DOI 10.1113/jphysiol.1996.sp021314
   McSherry IN, 2005, CELL CALCIUM, V38, P23, DOI 10.1016/j.ceca.2005.03.007
   Mees SD., 2007, COCHRANE DB SYST REV, V2007, P3, DOI [DOI 10.1002/14651858.CD000277.PUB3, 10.1002/14651858.CD000277.pub3]
   Mittman S, 1999, NEUROSCI LETT, V274, P143, DOI 10.1016/S0304-3940(99)00716-8
   Moosmang S, 2006, CIRC RES, V98, P105, DOI 10.1161/01.RES.0000197851.11031.9c
   Moosmang S, 2003, EMBO J, V22, P6027, DOI 10.1093/emboj/cdg583
   Morita H, 1999, CIRC RES, V85, P596, DOI 10.1161/01.RES.85.7.596
   Morita H, 2002, BRIT J PHARMACOL, V137, P467, DOI 10.1038/sj.bjp.0704892
   Navarro-Gonzalez MF, 2009, CLIN EXP PHARMACOL P, V36, P55, DOI 10.1111/j.1440-1681.2008.05035.x
   Nikitina E, 2007, J PHYSIOL-LONDON, V580, P523, DOI 10.1113/jphysiol.2006.126128
   Nikitina E, 2010, J NEUROSURG, V113, P870, DOI 10.3171/2010.2.JNS091038
   Nilius B, 1997, BRIT J PHARMACOL, V121, P547, DOI 10.1038/sj.bjp.0701140
   Perez-Reyes E, 2003, PHYSIOL REV, V83, P117, DOI 10.1152/physrev.00018.2002
   Perez-Reyes E, 2006, CELL CALCIUM, V40, P89, DOI 10.1016/j.ceca.2006.04.012
   Pesic A, 2004, CIRC RES, V94, pE97, DOI 10.1161/01.RES.0000131495.93500.3c
   Pignier C, 2000, AM J PHYSIOL-HEART C, V279, pH2259, DOI 10.1152/ajpheart.2000.279.5.H2259
   QUAYLE JM, 1993, AM J PHYSIOL, V264, pH470, DOI 10.1152/ajpheart.1993.264.2.H470
   Rodman DM, 2005, CIRC RES, V96, P864, DOI 10.1161/01.RES.0000163066.07472.ff
   Shcheglovitov A, 2007, BBA-BIOMEMBRANES, V1768, P1406, DOI 10.1016/j.bbamem.2007.02.017
   Shcheglovitov A, 2008, FEBS LETT, V582, P3765, DOI 10.1016/j.febslet.2008.10.013
   Shin MC, 2008, N-S ARCH PHARMACOL, V377, P411, DOI 10.1007/s00210-007-0239-6
   Sidach SS, 2002, J NEUROSCI, V22, P2023, DOI 10.1523/JNEUROSCI.22-06-02023.2002
   Siegl D, 2005, CIRC RES, V97, P781, DOI 10.1161/01.RES.0000186193.22438.6c
   SIMARD JM, 1991, PFLUG ARCH EUR J PHY, V417, P528, DOI 10.1007/BF00370950
   SOMLYO AV, 1968, J PHARMACOL EXP THER, V159, P129
   TAKEDA K, 1987, PFLUG ARCH EUR J PHY, V410, P385, DOI 10.1007/BF00586515
   Tanaka H, 2004, J PHARMACOL SCI, V96, P499, DOI 10.1254/jphs.RCJ04001X
   Tang ZZ, 2008, BBA-MOL CELL RES, V1783, P118, DOI 10.1016/j.bbamcr.2007.11.003
   Tang ZZ, 2004, J BIOL CHEM, V279, P44335, DOI 10.1074/jbc.M407023200
   Tomassoni D, 2008, CLIN EXP HYPERTENS, V30, P744, DOI 10.1080/10641960802580232
   Uebele VN, 2009, J CLIN INVEST, V119, P1659, DOI 10.1172/JCI36954
   VANBREEMEN C, 1989, ANNU REV PHYSIOL, V51, P315, DOI 10.1146/annurev.physiol.51.1.315
   Vinet R, 1999, AM J PHYSIOL-HEART C, V276, pH1313, DOI 10.1152/ajpheart.1999.276.4.H1313
   Welling A, 1997, CIRC RES, V81, P526, DOI 10.1161/01.RES.81.4.526
   Welsh DG, 1998, AM J PHYSIOL-HEART C, V274, pH178, DOI 10.1152/ajpheart.1998.274.1.H178
   WILDE DW, 1994, HYPERTENSION, V24, P739, DOI 10.1161/01.HYP.24.6.739
   WORLEY JF, 1991, AM J PHYSIOL, V261, pH1951, DOI 10.1152/ajpheart.1991.261.6.H1951
   Wu SW, 2003, CIRC RES, V93, P346, DOI 10.1161/01.RES.0000087148.75363.8F
   Wyatt CN, 1998, J PHYSIOL-LONDON, V510, P347, DOI 10.1111/j.1469-7793.1998.347bk.x
   Xia J, 1998, AM J PHYSIOL-HEART C, V274, pH323, DOI 10.1152/ajpheart.1998.274.1.H323
   Yamamoto Yoshimichi, 2005, Journal of Smooth Muscle Research, V41, P77, DOI 10.1540/jsmr.41.77
   Yoo HY, 2008, PFLUG ARCH EUR J PHY, V456, P549, DOI 10.1007/s00424-007-0438-5
   Zhong XL, 2006, HUM MOL GENET, V15, P1497, DOI 10.1093/hmg/ddl068
NR 102
TC 43
Z9 57
U1 0
U2 8
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0022-3751
EI 1469-7793
J9 J PHYSIOL-LONDON
JI J. Physiol.-London
PD FEB 11
PY 2011
VL 589
IS 4
BP 783
EP 795
DI 10.1113/jphysiol.2010.199497
PG 13
WC Neurosciences; Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology; Physiology
GA 726RI
UT WOS:000287743400008
PM 21173074
OA Green Published
DA 2025-04-10
ER

PT J
AU Kapurniotu, A
   Gokce, O
   Bernhagen, J
AF Kapurniotu, Aphrodite
   Gokce, Ozgun
   Bernhagen, Juergen
TI The Multitasking Potential of Alarmins and Atypical Chemokines
SO FRONTIERS IN MEDICINE
LA English
DT Review
DE alarmin; chemokine; cytokine; moonlighting; promiscuity; inflammation;
   cardiovascular disease; MIF protein family
ID MIGRATION INHIBITORY FACTOR; MOBILITY GROUP BOX-1; EOSINOPHIL-DERIVED
   NEUROTOXIN; CHROMATIN PROTEIN HMGB1; TRANSFER-RNA SYNTHETASE;
   POSTTRANSLATIONAL MODIFICATIONS; NONCLASSICAL PATHWAY;
   FUNCTIONAL-ACTIVITY; ADAPTIVE IMMUNITY; CRYSTAL-STRUCTURE
AB When the human genome was sequenced, it came as a surprise that it contains "only" 21,306 protein-coding genes. However, complexity and diversity are multiplied by alternative splicing, non-protein-coding transcripts, or post-translational modifications (PTMs) on proteome level. Here, we discuss how the multi-tasking potential of proteins can substantially enhance the complexity of the proteome further, while at the same time offering mechanisms for the fine-regulation of cell responses. Discoveries over the past two decades have led to the identification of "surprising" and previously unrecognized functionalities of long known cytokines, inflammatory mediators, and intracellular proteins that have established novel molecular networks in physiology, inflammation, and cardiovascular disease. In this mini-review, we focus on alarmins and atypical chemokines such as high-mobility group box protein-1 (HMGB-1) and macrophage migration-inhibitory factor (MIF)-type proteins that are prototypical examples of these classes, featuring a remarkable multitasking potential that allows for an elaborate fine-tuning of molecular networks in the extra-and intracellular space that may eventually give rise to novel "task"-based precision medicine intervention strategies.
C1 [Kapurniotu, Aphrodite] Tech Univ Munich, Div Peptide Biochem, Freising Weihenstephan, Germany.
   [Gokce, Ozgun] Klinikum Univ Munchen, Inst Stroke & Dementia Res, Syst Neurosci Lab, Munich, Germany.
   [Bernhagen, Juergen] Ludwig Maximilians Univ Munchen, Klinikum Univ Munchen, Inst Stroke & Dementia Res, Dept Vasc Biol, Munich, Germany.
   [Bernhagen, Juergen] Munich Heart Alliance, Munich, Germany.
   [Bernhagen, Juergen] Munich Cluster Syst Neurol SyNergy, Munich, Germany.
C3 Technical University of Munich; University of Munich; University of
   Munich; Munich Heart Alliance; University of Munich
RP Bernhagen, J (corresponding author), Ludwig Maximilians Univ Munchen, Klinikum Univ Munchen, Inst Stroke & Dementia Res, Dept Vasc Biol, Munich, Germany.; Bernhagen, J (corresponding author), Munich Heart Alliance, Munich, Germany.; Bernhagen, J (corresponding author), Munich Cluster Syst Neurol SyNergy, Munich, Germany.
EM juergen.bernhagen@med.uni-muenchen.de
RI gokce, ozgun/AIB-3978-2022
OI gokce, ozgun/0000-0001-6319-404X
FU Deutsche Forschungsgemeinschaft (DFG) [SFB1123-A03]; DFG [EXC 1010
   SyNergy]; NARSAD Young Investigator Grant
FX This work was supported by Deutsche Forschungsgemeinschaft (DFG) grant
   SFB1123-A03 to JB and AK, and by DFG within the framework of Munich
   Cluster for Systems Neurology (EXC 1010 SyNergy) to JB; OG received
   funding from a NARSAD Young Investigator Grant.
CR Alampour-Rajabi S, 2015, FASEB J, V29, P4497, DOI 10.1096/fj.15-273904
   Alard JE, 2015, SCI TRANSL MED, V7, DOI 10.1126/scitranslmed.aad5330
   Andersson U, 2002, J LEUKOCYTE BIOL, V72, P1084
   Andersson U, 2011, ANNU REV IMMUNOL, V29, P139, DOI 10.1146/annurev-immunol-030409-101323
   Bachelerie F, 2014, PHARMACOL REV, V66, P1, DOI 10.1124/pr.113.007724
   Bech-Otschir D, 2001, EMBO J, V20, P1630, DOI 10.1093/emboj/20.7.1630
   Becker R, 2016, NAT MED, V22, P452, DOI 10.1038/nm0516-452
   Bernhagen J, 2007, NAT MED, V13, P587, DOI 10.1038/nm1567
   Bertini R, 1999, J EXP MED, V189, P1783, DOI 10.1084/jem.189.11.1783
   Bertolino P, 1996, CRIT REV IMMUNOL, V16, P359
   Bianchi ME, 2007, J LEUKOCYTE BIOL, V81, P1, DOI 10.1189/jlb.0306164
   Bianchi ME, 2017, IMMUNOL REV, V280, P74, DOI 10.1111/imr.12601
   Bloom J, 2016, EXPERT OPIN THER TAR, V20, P1463, DOI 10.1080/14728222.2016.1251582
   Bonaldi T, 2003, EMBO J, V22, P5551, DOI 10.1093/emboj/cdg516
   Bucala R., 1996, FASEB J, V7, P19
   Calandra T, 2003, NAT REV IMMUNOL, V3, P791, DOI 10.1038/nri1200
   Chan JK, 2012, J CLIN INVEST, V122, P2711, DOI 10.1172/JCI62423
   Charo IF, 2006, NEW ENGL J MED, V354, P610, DOI 10.1056/NEJMra052723
   Cho Y, 2010, P NATL ACAD SCI USA, V107, P11313, DOI 10.1073/pnas.1002716107
   Crump MP, 1997, EMBO J, V16, P6996, DOI 10.1093/emboj/16.23.6996
   Czura CJ, 2001, J ENDOTOXIN RES, V7, P315, DOI 10.1177/09680519010070041401
   DAVID JR, 1966, P NATL ACAD SCI USA, V56, P72, DOI 10.1073/pnas.56.1.72
   Dayawansa NH, 2014, CLIN SCI, V127, P149, DOI 10.1042/CS20130828
   De Buck M, 2016, CYTOKINE GROWTH F R, V30, P55, DOI 10.1016/j.cytogfr.2015.12.010
   Degryse B, 2003, FEBS LETT, V553, P11, DOI 10.1016/S0014-5793(03)01027-5
   Dickerhof N, 2015, FREE RADICAL BIO MED, V89, P498, DOI 10.1016/j.freeradbiomed.2015.09.009
   Döring Y, 2017, CIRCULATION, V136, P388, DOI 10.1161/CIRCULATIONAHA.117.027646
   Dupont N, 2011, EMBO J, V30, P4701, DOI 10.1038/emboj.2011.398
   Filip AM, 2009, J BIOL CHEM, V284, P7977, DOI 10.1074/jbc.M808620200
   Flaster H, 2007, MOL ENDOCRINOL, V21, P1267, DOI 10.1210/me.2007-0065
   Flieger O, 2003, FEBS LETT, V551, P78, DOI 10.1016/S0014-5793(03)00900-1
   Foell D, 2007, J LEUKOCYTE BIOL, V81, P28, DOI 10.1189/jlb.0306170
   Frye BC, 2009, EMBO REP, V10, P783, DOI 10.1038/embor.2009.81
   Gleissner CA, 2008, ARTERIOSCL THROM VAS, V28, P1920, DOI 10.1161/ATVBAHA.108.169417
   Greven D, 2010, EXPERT OPIN THER TAR, V14, P253, DOI 10.1517/14728220903551304
   Harris HE, 2012, NAT REV RHEUMATOL, V8, P195, DOI 10.1038/nrrheum.2011.222
   Hertelendy J, 2018, CURR MED CHEM, V25, P601, DOI 10.2174/0929867324666170714114200
   Hofmann MA, 1999, CELL, V97, P889, DOI 10.1111/j.1365-2222.2011.03714.x
   Hoover DM, 2002, J BIOL CHEM, V277, P37647, DOI 10.1074/jbc.M203907200
   Horuk R, 1999, IMMUNOL TODAY, V20, P89, DOI 10.1016/S0167-5699(98)01396-6
   Howard OMZ, 2005, BLOOD, V105, P4207, DOI 10.1182/blood-2004-07-2697
   Howard OMZ, 2002, J EXP MED, V196, P781, DOI 10.1084/jem.20020186
   Hudson JD, 1999, J EXP MED, V190, P1375, DOI 10.1084/jem.190.10.1375
   Israelson A, 2015, NEURON, V86, P218, DOI 10.1016/j.neuron.2015.02.034
   Klasen C, 2014, J IMMUNOL, V192, P5273, DOI 10.4049/jimmunol.1302209
   Kleemann R, 2000, NATURE, V408, P211, DOI 10.1038/35041591
   Kleemann R, 2010, MEDIAT INFLAMM, V2010, DOI 10.1155/2010/610479
   Kok T, 2018, DRUG DISCOV TODAY, V23, P1910, DOI 10.1016/j.drudis.2018.06.017
   Kraemer S, 2013, CURR MED CHEM, V20, P2524, DOI 10.2174/09298673113209990117
   Kraemer S, 2011, FASEB J, V25, P894, DOI 10.1096/fj.10-168559
   Lacy M, 2018, SCI REP-UK, V8, DOI 10.1038/s41598-018-23554-5
   Leng L, 2003, J EXP MED, V197, P1467, DOI 10.1084/jem.20030286
   Ley K, 2003, MICROCIRCULATION, V10, P289, DOI 10.1038/sj.mn.7800194
   Leyton-Jaimes MF, 2016, P NATL ACAD SCI USA, V113, P10198, DOI 10.1073/pnas.1604600113
   Liston A, 2017, NAT REV IMMUNOL, V17, P208, DOI 10.1038/nri.2016.151
   Lolis E, 2003, EXPERT OPIN THER TAR, V7, P153, DOI 10.1517/eott.7.2.153.23778
   Loos T, 2009, METHOD ENZYMOL, V461, P3, DOI 10.1016/S0076-6879(09)05401-9
   Lotze MT, 2005, NAT REV IMMUNOL, V5, P331, DOI 10.1038/nri1594
   Lu B, 2014, EXPERT REV CLIN IMMU, V10, P713, DOI 10.1586/1744666X.2014.909730
   Ludwig A, 2007, THROMB HAEMOSTASIS, V97, P694
   Lue H, 2007, ONCOGENE, V26, P5046, DOI 10.1038/sj.onc.1210318
   Luedike P, 2012, CIRCULATION, V125, P1880, DOI 10.1161/CIRCULATIONAHA.111.069104
   Lusso P, 2006, EMBO J, V25, P447, DOI 10.1038/sj.emboj.7600947
   Ma F, 2017, PHYSIOL REP, V5, DOI 10.14814/phy2.13549
   MATZINGER P, 1994, ANNU REV IMMUNOL, V12, P991, DOI 10.1146/annurev.immunol.12.1.991
   Merk M, 2012, CYTOKINE, V59, P10, DOI 10.1016/j.cyto.2012.03.014
   Merk M, 2011, P NATL ACAD SCI USA, V108, pE577, DOI 10.1073/pnas.1102941108
   Merk M, 2009, J IMMUNOL, V182, P6896, DOI 10.4049/jimmunol.0803710
   Miller EJ, 2008, NATURE, V451, P578, DOI 10.1038/nature06504
   Morand EF, 2006, NAT REV DRUG DISCOV, V5, P399, DOI 10.1038/nrd2029
   Nemajerova A, 2007, EMBO J, V26, P987, DOI 10.1038/sj.emboj.7601564
   Nickel W, 2009, NAT REV MOL CELL BIO, V10, P148, DOI 10.1038/nrm2617
   Noels H, 2009, TRENDS CARDIOVAS MED, V19, P76, DOI 10.1016/j.tcm.2009.05.002
   O'Reilly C, 2016, MED RES REV, V36, P440, DOI 10.1002/med.21385
   Oppenheim JJ, 2003, ANN RHEUM DIS, V62, P17, DOI 10.1136/ard.62.suppl_2.ii17
   Oppenheim JJ, 2005, CURR OPIN IMMUNOL, V17, P359, DOI 10.1016/j.coi.2005.06.002
   Oppenheim JJ, 2007, ADV EXP MED BIOL, V601, P185
   Pandolfi F, 2016, CLIN THER, V38, P1017, DOI 10.1016/j.clinthera.2016.02.028
   Panstruga R, 2015, BMC EVOL BIOL, V15, DOI 10.1186/s12862-015-0337-x
   Pawig L, 2015, FRONT IMMUNOL, V6, DOI 10.3389/fimmu.2015.00429
   Pertea M, 2018, bioRxiv
   Pohl J, 2016, THROMB HAEMOSTASIS, V115, P200, DOI 10.1160/TH15-05-0436
   Proost P, 2006, BIOCHEM SOC T, V34, P997, DOI 10.1042/BST0340997
   Proost P, 1998, J IMMUNOL, V160, P4034
   Qi DK, 2014, J CLIN INVEST, V124, P3540, DOI 10.1172/JCI73061
   Qi D, 2009, J CLIN INVEST, V119, P3807, DOI 10.1172/JCI39738
   Qin L, 2015, SCIENCE, V347, P1117, DOI 10.1126/science.1261064
   Rajagopalan L, 2006, BIOSCIENCE REP, V26, P325, DOI 10.1007/s10540-006-9025-9
   Rajasekaran D, 2016, J BIOL CHEM, V291, P15881, DOI 10.1074/jbc.M116.717751
   Rassaf T, 2014, CARDIOVASC RES, V102, P321, DOI 10.1093/cvr/cvu071
   Rauen T, 2009, J BIOL CHEM, V284, P26928, DOI 10.1074/jbc.M109.046599
   Roehrl J, 2008, J BIOL CHEM, V283, P5414, DOI 10.1074/jbc.M709103200
   Röhrl J, 2010, J IMMUNOL, V184, P6688, DOI 10.4049/jimmunol.0903984
   Roger T, 2016, P NATL ACAD SCI USA, V113, pE997, DOI 10.1073/pnas.1514018113
   Scaffidi P, 2002, NATURE, V418, P191, DOI 10.1038/nature00858
   Schindler L, 2018, REDOX BIOL, V15, P135, DOI 10.1016/j.redox.2017.11.028
   Schiraldi M, 2012, J EXP MED, V209, P551, DOI 10.1084/jem.20111739
   Schmitz C, 2018, FASEB J, V32, P4428, DOI 10.1096/fj.201800058R
   Schober A, 2008, J MOL MED, V86, P761, DOI 10.1007/s00109-008-0334-2
   Shulman Z, 2012, NAT IMMUNOL, V13, P67, DOI 10.1038/ni.2173
   Shvil N, 2018, CELL DEATH DIS, V9, DOI 10.1038/s41419-017-0130-4
   Soehnlein O, 2008, BLOOD, V112, P1461, DOI 10.1182/blood-2008-02-139634
   Stros M, 2010, BBA-GENE REGUL MECH, V1799, P101, DOI 10.1016/j.bbagrm.2009.09.008
   Sun HW, 1996, P NATL ACAD SCI USA, V93, P5191, DOI 10.1073/pnas.93.11.5191
   Thelen M, 2001, NAT IMMUNOL, V2, P129, DOI 10.1038/84224
   Thelen M, 2008, NAT IMMUNOL, V9, P953, DOI 10.1038/ni.f.207
   Thelen M, 2010, CURR OPIN PHARMACOL, V10, P38, DOI 10.1016/j.coph.2009.09.004
   Thiele M, 2005, ANTIOXID REDOX SIGN, V7, P1234, DOI 10.1089/ars.2005.7.1234
   Thiele M, 2015, J IMMUNOL, V195, P2343, DOI 10.4049/jimmunol.1500572
   Tillmann S, 2013, FRONT IMMUNOL, V4, DOI 10.3389/fimmu.2013.00115
   Tilstam PV, 2017, EXPERT OPIN THER TAR, V21, P671, DOI 10.1080/14728222.2017.1336227
   Trivedi-Parmar V, 2018, J MED CHEM, V61, P8104, DOI 10.1021/acs.jmedchem.8b00589
   van Horssen R, 2006, CYTOKINE GROWTH F R, V17, P339, DOI 10.1016/j.cytogfr.2006.08.001
   Venereau E, 2016, PHARMACOL RES, V111, P534, DOI 10.1016/j.phrs.2016.06.031
   Vénéreau E, 2015, FRONT IMMUNOL, V6, DOI 10.3389/fimmu.2015.00422
   Venereau E, 2012, J EXP MED, V209, P1519, DOI 10.1084/jem.20120189
   Venter JC, 2001, SCIENCE, V291, P1304, DOI 10.1126/science.1058040
   Vogl T, 2007, NAT MED, V13, P1042, DOI 10.1038/nm1638
   Wakasugi K, 2002, P NATL ACAD SCI USA, V99, P173, DOI 10.1073/pnas.012602099
   Wakasugi K, 1999, J BIOL CHEM, V274, P23155, DOI 10.1074/jbc.274.33.23155
   Wakasugi K, 1999, SCIENCE, V284, P147, DOI 10.1126/science.284.5411.147
   Wang HC, 1999, SCIENCE, V285, P248, DOI 10.1126/science.285.5425.248
   Wang YF, 2016, SCIENCE, V354, DOI 10.1126/science.aad6872
   Wantha S, 2013, CIRC RES, V112, P792, DOI 10.1161/CIRCRESAHA.112.300666
   Weber C, 2008, P NATL ACAD SCI USA, V105, P16278, DOI 10.1073/pnas.0804017105
   Wu BL, 2010, SCIENCE, V330, P1066, DOI 10.1126/science.1194396
   Xu L, 2015, PHYS CHEM CHEM PHYS, V17, P3370, DOI 10.1039/c4cp05095a
   Yang D, 2003, BLOOD, V102, P3396, DOI 10.1182/blood-2003-01-0151
   Yang D, 1999, SCIENCE, V286, P525, DOI 10.1126/science.286.5439.525
   Yang D, 2004, ANNU REV IMMUNOL, V22, P181, DOI 10.1146/annurev.immunol.22.012703.104603
   Yang H, 2005, J LEUKOCYTE BIOL, V78, P1, DOI 10.1189/jlb.1104648
   Yang H, 2002, J ENDOTOXIN RES, V8, P469, DOI 10.1179/096805102125001091
   Yang H, 2001, SHOCK, V15, P247, DOI 10.1097/00024382-200115040-00001
   Yang H, 2013, J LEUKOCYTE BIOL, V93, P865, DOI 10.1189/jlb.1212662
   Yang H, 2012, MOL MED, V18, P250, DOI 10.2119/molmed.2011.00389
   Yang HA, 2010, P NATL ACAD SCI USA, V107, P11942, DOI 10.1073/pnas.1003893107
   Yang H, 2010, BBA-GENE REGUL MECH, V1799, P149, DOI 10.1016/j.bbagrm.2009.11.019
   Yu SL, 2013, EXPERT REV CLIN IMMU, V9, P739, DOI 10.1586/1744666X.2013.814428
   Zaitseva M, 2003, BBA-BIOMEMBRANES, V1614, P51, DOI 10.1016/S0005-2736(03)00162-7
   Zernecke A, 2008, CIRCULATION, V117, P1594, DOI 10.1161/CIRCULATIONAHA.107.729125
   Zheng YH, 2015, NAT CELL BIOL, V17, P1348, DOI 10.1038/ncb3222
NR 141
TC 61
Z9 63
U1 0
U2 3
PU FRONTIERS MEDIA SA
PI LAUSANNE
PA AVENUE DU TRIBUNAL FEDERAL 34, LAUSANNE, CH-1015, SWITZERLAND
EI 2296-858X
J9 FRONT MED-LAUSANNE
JI Front. Med.
PD JAN 23
PY 2019
VL 6
AR 3
DI 10.3389/fmed.2019.00003
PG 12
WC Medicine, General & Internal
WE Science Citation Index Expanded (SCI-EXPANDED)
SC General & Internal Medicine
GA HI6TO
UT WOS:000456588500001
PM 30729111
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Versteeg, HH
AF Versteeg, Henri H.
TI Tissue Factor: Old and New Links with Cancer Biology
SO SEMINARS IN THROMBOSIS AND HEMOSTASIS
LA English
DT Article
DE blood clotting; integrins; tumor biology; stem cells; protease-activated
   receptors
ID FACTOR CYTOPLASMIC DOMAIN; TO-MESENCHYMAL TRANSITION; MOLECULAR-WEIGHT
   HEPARIN; HUMAN ENDOTHELIAL-CELLS; GROWTH-FACTOR RECEPTOR; BREAST-CANCER;
   FACTOR EXPRESSION; COLORECTAL-CANCER; FACTOR VIIA; VENOUS
   THROMBOEMBOLISM
AB Blood coagulation is one of the most profound factors that influence cancer progression. Especially the initiator of coagulation, tissue factor (TF), has been subject to many studies investigating the overlap between coagulation and cancer. It has been known for decades that TF is a risk factor for metastasis, and in mouse models, TF drives metastasis in a coagulation-dependent manner. However, TF also serves as a cellular receptor to drive primary tumor growth and tumor angiogenesis. Nevertheless, recent studies have indicated that TF plays more fundamental roles in cancer biology. TF regulates tumor cell dormancy, is associated with cancer stem cell behavior, epithelial-to-mesenchymal transition, and dictates establishment of the tumor cell premetastatic niche. Especially with regard to these recent roles attributed to TF, no clear idea exists on the exact molecular pathways that are initiated by TF. Finally, TF alternative splicing results in an isoform with different characteristics and functions in cancer. In this review, a summary will be given on both the established as well as the new aspects of TF function in cancer progression.
C1 Leiden Univ, Med Ctr, Einthoven Lab Expt Vasc Med, Dept Internal Med, NL-2333 ZA Leiden, Netherlands.
C3 Leiden University; Leiden University Medical Center (LUMC); Leiden
   University - Excl LUMC
RP Versteeg, HH (corresponding author), Leiden Univ, Med Ctr, Einthoven Lab Expt Vasc Med, Dept Internal Med, Room C7-14,Albinusdreef 2, NL-2333 ZA Leiden, Netherlands.
EM h.h.versteeg@lumc.nl
RI Versteeg, Henri/G-1783-2018
OI Versteeg, Henri/0000-0003-4294-175X
FU Netherlands Organization for Scientific Research (NWO) [91710329]
FX This work was made possible through funding by the Netherlands
   Organization for Scientific Research (NWO), VIDI Grant number 91710329.
CR Abe K, 1999, P NATL ACAD SCI USA, V96, P8663, DOI 10.1073/pnas.96.15.8663
   Ahamed J, 2006, P NATL ACAD SCI USA, V103, P13932, DOI 10.1073/pnas.0606411103
   Arderiu G, 2012, J THROMB HAEMOST, V10, P1895, DOI 10.1111/j.1538-7836.2012.04848.x
   Arderiu G, 2011, ARTERIOSCL THROM VAS, V31, P2607, DOI 10.1161/ATVBAHA.111.233536
   BAZAN JF, 1990, P NATL ACAD SCI USA, V87, P6934, DOI 10.1073/pnas.87.18.6934
   Belting M, 2004, NAT MED, V10, P502, DOI 10.1038/nm1037
   Bogdanov VY, 2003, NAT MED, V9, P458, DOI 10.1038/nm841
   Bretschneider E, 2003, THROMB HAEMOSTASIS, V90, P704, DOI 10.1160/TH03-04-0203
   Brüggemann LW, 2008, J CELL MOL MED, V12, P2622, DOI 10.1111/j.1582-4934.2008.00316.x
   Cáceres JF, 2002, TRENDS GENET, V18, P186, DOI 10.1016/S0168-9525(01)02626-9
   Camerer E, 2000, P NATL ACAD SCI USA, V97, P5255, DOI 10.1073/pnas.97.10.5255
   Camerer E, 2000, J BIOL CHEM, V275, P6580, DOI 10.1074/jbc.275.9.6580
   Camerer E, 1996, J BIOL CHEM, V271, P29034, DOI 10.1074/jbc.271.46.29034
   Chandradas S, 2010, J LEUKOCYTE BIOL, V87, P147, DOI 10.1189/jlb.0409252
   Collier MEW, 2010, ARTERIOSCL THROM VAS, V30, P1810, DOI 10.1161/ATVBAHA.110.211854
   Collier MEW, 2008, MOL CANCER RES, V6, P1807, DOI 10.1158/1541-7786.MCR-08-0109
   Conn EM, 2008, J BIOL CHEM, V283, P26518, DOI 10.1074/jbc.M803337200
   Dorfleutner A, 2004, MOL BIOL CELL, V15, P4416, DOI 10.1091/mbc.E03-09-0640
   Eisenreich A, 2009, CIRC J, V73, P1746, DOI 10.1253/circj.CJ-99-0225
   Eisenreich A, 2009, CIRC RES, V104, P589, DOI 10.1161/CIRCRESAHA.108.183905
   Findlay VJ, 2014, CANCER GENE THER, V21, P181, DOI 10.1038/cgt.2014.15
   Fischer EG, 1999, J CLIN INVEST, V104, P1213, DOI 10.1172/JCI7750
   Gessler F, 2010, NEUROSCIENCE, V165, P1312, DOI 10.1016/j.neuroscience.2009.11.049
   Gil-Bernabé AM, 2012, BLOOD, V119, P3164, DOI 10.1182/blood-2011-08-376426
   KAKKAR AK, 1995, BRIT J SURG, V82, P1101, DOI 10.1002/bjs.1800820831
   Klerk CPW, 2005, J CLIN ONCOL, V23, P2130, DOI 10.1200/JCO.2005.03.134
   Kocatürk B, 2013, P NATL ACAD SCI USA, V110, P11517, DOI 10.1073/pnas.1307100110
   Lee AYY, 2005, J CLIN ONCOL, V23, P2123, DOI 10.1200/JCO.2005.03.133
   Lin ZM, 2014, ASIAN PAC J CANCER P, V15, P643, DOI 10.7314/APJCP.2014.15.2.643
   Lyman GH, 2009, J CLIN ONCOL, V27, P4821, DOI 10.1200/JCO.2009.22.3032
   Magnus N, 2014, P NATL ACAD SCI USA, V111, P3544, DOI 10.1073/pnas.1314118111
   Magnus N, 2010, BLOOD, V116, P815, DOI 10.1182/blood-2009-10-250639
   Mallini P, 2014, CANCER TREAT REV, V40, P341, DOI 10.1016/j.ctrv.2013.09.008
   Milsom C, 2007, J THROMB HAEMOST, V5, P2550, DOI 10.1111/j.1538-7836.2007.02766.x
   Milsom CC, 2008, CANCER RES, V68, P10068, DOI 10.1158/0008-5472.CAN-08-2067
   Morris DR, 2006, CANCER RES, V66, P307, DOI 10.1158/0008-5472.CAN-05-1735
   Nakanishi-Matsui M, 2000, NATURE, V404, P609, DOI 10.1038/35007085
   Nowak DG, 2008, J CELL SCI, V121, P3487, DOI 10.1242/jcs.016410
   Pabla N, 2012, P NATL ACAD SCI USA, V109, P197, DOI 10.1073/pnas.1104767109
   Palumbo JS, 2007, BLOOD, V110, P133, DOI 10.1182/blood-2007-01-065995
   Palumbo JS, 2005, BLOOD, V105, P178, DOI 10.1182/blood-2004-06-2272
   Peña E, 2013, J THROMB HAEMOST, V11, P1880, DOI 10.1111/jth.12327
   Pengo V, 2011, BLOOD, V117, P1707, DOI 10.1182/blood-2010-08-304758
   Reinhardt C, 2008, J CLIN INVEST, V118, P1110, DOI 10.1172/JCI32376
   Riewald M, 2002, SCIENCE, V296, P1880, DOI 10.1126/science.1071699
   Rollin J, 2010, J THROMB HAEMOST, V8, P607, DOI 10.1111/j.1538-7836.2009.03713.x
   Rong Y, 2005, CANCER RES, V65, P1406, DOI 10.1158/0008-5472.CAN-04-3376
   Rydén L, 2010, INT J CANCER, V126, P2330, DOI 10.1002/ijc.24921
   Saito Y, 2011, EUR J CANCER, V47, P2230, DOI 10.1016/j.ejca.2011.04.028
   Schaffner F, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0061071
   Schaffner F, 2010, BLOOD, V116, P6106, DOI 10.1182/blood-2010-06-289314
   Schulman S, 2000, NEW ENGL J MED, V342, P1953, DOI 10.1056/NEJM200006293422604
   Seto S, 2000, CANCER, V88, P295, DOI 10.1002/(SICI)1097-0142(20000115)88:2<295::AID-CNCR8>3.0.CO;2-U
   Shigemori C, 1998, THROMB HAEMOSTASIS, V80, P894
   Slatter TL, 2011, BLOOD, V117, P5166, DOI 10.1182/blood-2010-11-321851
   Song HB, 2012, ONCOL REP, V28, P2057, DOI 10.3892/or.2012.2048
   Sun L, 2013, ACTA ONCOL, V52, P842, DOI 10.3109/0284186X.2013.705890
   Tian ML, 2011, CANCER BIOL THER, V12, P896, DOI 10.4161/cbt.12.10.17679
   Timp JF, 2013, BLOOD, V122, P1712, DOI 10.1182/blood-2013-04-460121
   Ünü B, 2014, THROMB RES, V133, pS76, DOI 10.1016/S0049-3848(14)50013-8
   Unruh D, 2014, INT J CANCER, V134, P9, DOI 10.1002/ijc.28327
   van den Berg YW, 2009, P NATL ACAD SCI USA, V106, P19497, DOI 10.1073/pnas.0905325106
   van den Berg YW, 2012, BLOOD, V119, P924, DOI 10.1182/blood-2011-06-317685
   Versteeg HH, 2008, CANCER RES, V68, P7219, DOI 10.1158/0008-5472.CAN-08-0419
   Versteeg HH, 2008, BLOOD, V111, P190, DOI 10.1182/blood-2007-07-101048
   Versteeg HH, 2013, PHYSIOL REV, V93, P327, DOI 10.1152/physrev.00016.2011
   Versteeg HH, 2000, J BIOL CHEM, V275, P28750, DOI 10.1074/jbc.M907635199
   Versteeg HH, 2004, CIRC RES, V94, P1032, DOI 10.1161/01.RES.0000125625.18597.AD
   Versteeg HH, 2004, ONCOGENE, V23, P410, DOI 10.1038/sj.onc.1207066
   Versteeg HH, 2003, J THROMB HAEMOST, V1, P1012, DOI 10.1046/j.1538-7836.2003.00205.x
   Versteeg HH, 2002, J BIOL CHEM, V277, P27065, DOI 10.1074/jbc.M110325200
   VU TKH, 1991, CELL, V64, P1057, DOI 10.1016/0092-8674(91)90261-V
   Yeh HH, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0075287
   Yokota N, 2009, BRIT J CANCER, V101, P2023, DOI 10.1038/sj.bjc.6605406
   Yu JL, 2005, BLOOD, V105, P1734, DOI 10.1182/blood-2004-05-2042
   Yu J, 2008, ARTERIOSCL THROM VAS, V28, P1975, DOI 10.1161/ATVBAHA.108.175083
   Zhang JQ, 2008, INT J COLORECTAL DIS, V23, P971, DOI 10.1007/s00384-008-0496-y
   ZHANG YM, 1994, J CLIN INVEST, V94, P1320, DOI 10.1172/JCI117451
NR 78
TC 30
Z9 33
U1 0
U2 6
PU THIEME MEDICAL PUBL INC
PI NEW YORK
PA 333 SEVENTH AVE, NEW YORK, NY 10001 USA
SN 0094-6176
EI 1098-9064
J9 SEMIN THROMB HEMOST
JI Semin. Thromb. Hemost.
PD OCT
PY 2015
VL 41
IS 7
BP 747
EP 755
DI 10.1055/s-0035-1556048
PG 9
WC Hematology; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Hematology; Cardiovascular System & Cardiology
GA CT0NW
UT WOS:000362494200010
PM 26408927
DA 2025-04-10
ER

PT J
AU Zhang, WZ
   Xia, XF
   Reisenauer, MR
   Rieg, T
   Lang, F
   Kuhl, D
   Vallon, V
   Kone, BC
AF Zhang, Wenzheng
   Xia, Xuefeng
   Reisenauer, Mary Rose
   Rieg, Timo
   Lang, Florian
   Kuhl, Dietmar
   Vallon, Volker
   Kone, Bruce C.
TI Aldosterone-induced Sgk1 relieves Dot1a-Af9-mediated transcriptional
   repression of epithelial Na<SUP>+</SUP> channel α
SO JOURNAL OF CLINICAL INVESTIGATION
LA English
DT Article
ID GLUCOCORTICOID-INDUCIBLE KINASE; SODIUM-CHANNEL; 5'-FLANKING REGION;
   FUSION PARTNER; EXPRESSION; SUBUNIT; KIDNEY; GENE; PHOSPHORYLATION;
   METHYLATION
AB Ahlosterone plays a major role in the regulation of salt balance and the pathophysiology of cardiovascular and renal diseases. Many aldosterone-regulated genes - including that encoding the epithelial Na+ channel (ENaC), a key arbiter of Na+ transport in the kidney and other epithelia - have been identified, but the mechanisms by which the hormone modifies chromatin structure and thus transcription remain unknown. We previously described the basal repression of ENaC alpha. by a complex containing the histone H3 Lys79 methyltransferase disruptor of telomeric silencing alternative splice variant a (Dotla) and the putative transcription factor ALL1-fused gene from chromosome 9 (Af9) as well as the release of this repression by aldosterone treatment. Here we provide evidence from renal collecting duct cells and serum- and glucocorticoid-induced kinase-1 (Sgk1) WT and knockout mice that Sgk1 phosphorylated Af9, thereby impairing the Dotla-Af9 interaction and leading to targeted histone H3 Lys79 hypomethylation at the ENaC alpha promoter and derepression of ENaC alpha transcription. Thus, Af9 is a physiologic target of Sgk1, and Sgk1 negatively regulates the Dotla-Af9 repressor complex that controls transcription of ENaC alpha and likely other aldosterone-induced genes.
C1 Univ Texas, Sch Med, Dept Internal Med, Houston, TX 77030 USA.
   Univ Texas, Sch Med, Dept Integrat Biol & Pharmacol, Houston, TX USA.
   Univ Calif San Diego, Dept Med, San Diego, CA 92103 USA.
   Univ Calif San Diego, Dept Pharmacol, San Diego, CA 92103 USA.
   VA Med Ctr, San Diego, CA USA.
   Univ Tubingen, Dept Physiol, Tubingen, Germany.
   Free Univ Berlin, Dept Biol Chem & Pharm, D-1000 Berlin, Germany.
   Brown Fdn Inst Mol Med Prevent Human Dis, Houston, TX USA.
C3 University of Texas System; University of Texas System; University of
   California System; University of California San Diego; University of
   California System; University of California San Diego; Eberhard Karls
   University of Tubingen; Free University of Berlin
RP Zhang, WZ (corresponding author), Univ Texas, Sch Med, Dept Internal Med, 6431 Fannin,MSB 1-150, Houston, TX 77030 USA.
EM Wenzheng.Zhang@uth.tmc.edu; bruce.c.kone@uth.tmc.edu
RI Rieg, Timo/W-7478-2019; Kuhl, Dietmar/A-4689-2009
OI Vallon, Volker/0000-0002-9211-2063; Kuhl, Dietmar/0000-0002-4772-6701;
   Rieg, Timo/0000-0001-6082-662X
FU NIDDK NIH HHS [K01 DK70834, R01 DK075065, K01 DK070834, R01 DK47981, R01
   DK047981] Funding Source: Medline
CR Asher C, 1996, AM J PHYSIOL-CELL PH, V271, pC605, DOI 10.1152/ajpcell.1996.271.2.C605
   Boyd C, 2005, AM J PHYSIOL-RENAL, V288, pF505, DOI 10.1152/ajprenal.00242.2004
   Chen SY, 1999, P NATL ACAD SCI USA, V96, P2514, DOI 10.1073/pnas.96.5.2514
   Debonneville C, 2001, EMBO J, V20, P7052, DOI 10.1093/emboj/20.24.7052
   Erfurth F, 2004, LEUKEMIA, V18, P92, DOI 10.1038/sj.leu.2403200
   Escoubet B, 1997, AM J PHYSIOL-CELL PH, V272, pC1482, DOI 10.1152/ajpcell.1997.272.5.C1482
   Feng Q, 2002, CURR BIOL, V12, P1052, DOI 10.1016/S0960-9822(02)00901-6
   Gumz ML, 2003, AM J PHYSIOL-RENAL, V285, pF664, DOI 10.1152/ajprenal.00353.2002
   Hemenway CS, 2001, ONCOGENE, V20, P3798, DOI 10.1038/sj.onc.1204478
   Hou JH, 2002, J AM SOC NEPHROL, V13, P1190, DOI 10.1097/01.ASN.0000013702.73570.3B
   Huang DY, 2006, AM J PHYSIOL-REG I, V290, pR935, DOI 10.1152/ajpregu.00382.2005
   Huang DY, 2004, J AM SOC NEPHROL, V15, P885, DOI 10.1097/01.ASN.0000120368.59693.A8
   IIDA S, 1993, JPN J CANCER RES, V84, P532, DOI 10.1111/j.1349-7006.1993.tb00172.x
   Ku NO, 1998, EMBO J, V17, P1892, DOI 10.1093/emboj/17.7.1892
   Lang F, 2006, PHYSIOL REV, V86, P1151, DOI 10.1152/physrev.00050.2005
   Masilamani S, 1999, J CLIN INVEST, V104, pR19, DOI 10.1172/JCI7840
   McAvoy T, 1999, BIOCHEMISTRY-US, V38, P12943, DOI 10.1021/bi991227d
   Métivier R, 2003, CELL, V115, P751, DOI 10.1016/S0092-8674(03)00934-6
   Mick VE, 2001, MOL ENDOCRINOL, V15, P575, DOI 10.1210/me.15.4.575
   Min JR, 2003, CELL, V112, P711, DOI 10.1016/S0092-8674(03)00114-4
   Nie ZQ, 2003, MOL CELL BIOL, V23, P2942, DOI 10.1128/MCB.23.8.2942-2952.2003
   Okada Y, 2005, CELL, V121, P167, DOI 10.1016/j.cell.2005.02.020
   Ono S, 1997, PFLUG ARCH EUR J PHY, V434, P756, DOI 10.1007/s004240050462
   Rong R, 2004, ONCOGENE, V23, P8447, DOI 10.1038/sj.onc.1207794
   Sayegh R, 1999, J BIOL CHEM, V274, P12431, DOI 10.1074/jbc.274.18.12431
   Seebohm G, 2005, CELL PHYSIOL BIOCHEM, V16, P255, DOI 10.1159/000089851
   Srinivasan RS, 2003, ONCOGENE, V22, P3395, DOI 10.1038/sj.onc.1206361
   Thomas CP, 2004, CURR OPIN NEPHROL HY, V13, P541, DOI 10.1097/00041552-200409000-00010
   Vallon V, 2005, AM J PHYSIOL-REG I, V289, pR395, DOI 10.1152/ajpregu.00731.2004
   Vallon V, 2005, AM J PHYSIOL-REG I, V288, pR4, DOI 10.1152/ajpregu.00369.2004
   Vallon V, 2006, J MOL MED, V84, P396, DOI 10.1007/s00109-005-0027-z
   van Leeuwen F, 2002, CELL, V109, P745, DOI 10.1016/S0092-8674(02)00759-6
   Weger S, 1999, J VIROL, V73, P260, DOI 10.1128/JVI.73.1.260-269.1999
   Wulff P, 2002, J CLIN INVEST, V110, P1263, DOI 10.1172/JCI200215696
   Yoo D, 2003, J BIOL CHEM, V278, P23066, DOI 10.1074/jbc.M212301200
   Zhang QM, 2003, INT J RADIAT BIOL, V79, P281, DOI 10.1080/0955300031000096289
   Zhang WZ, 2006, AM J PHYSIOL-CELL PH, V290, pC936, DOI 10.1152/ajpcell.00431.2005
   Zhang WZ, 2004, BIOCHEM J, V377, P641, DOI 10.1042/BJ20030839
NR 38
TC 129
Z9 146
U1 0
U2 8
PU AMER SOC CLINICAL INVESTIGATION INC
PI ANN ARBOR
PA 2015 MANCHESTER RD, ANN ARBOR, MI 48104 USA
SN 0021-9738
EI 1558-8238
J9 J CLIN INVEST
JI J. Clin. Invest.
PD MAR
PY 2007
VL 117
IS 3
BP 773
EP 783
DI 10.1172/JCI29850
PG 11
WC Medicine, Research & Experimental
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Research & Experimental Medicine
GA 142PR
UT WOS:000244662500037
PM 17332896
OA Green Accepted, Bronze, Green Published
DA 2025-04-10
ER

PT J
AU Meunier, C
   Bordereaux, D
   Porten, F
   Gisselbrecht, S
   Chrétien, S
   Courtois, G
AF Meunier, C
   Bordereaux, D
   Porten, F
   Gisselbrecht, S
   Chrétien, S
   Courtois, G
TI Cloning and characterization of a family of proteins associated with Mpl
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID SPINOCEREBELLAR ATAXIA TYPE-2; THROMBOPOIETIN RECEPTOR; C-MPL; TYROSINE
   PHOSPHORYLATION; MEGAKARYOCYTE GROWTH; 3-KINASE ACTIVATION; KINASE
   PATHWAY; DOMAIN; GENE; DIFFERENTIATION
AB Thrombopoietin (TPO) controls the formation of megakaryocytes and platelets from hematopoietic stem cells via activation of the c-Mpl receptor and multiple downstream signal transduction pathways. We used two-hybrid screening to identify new proteins that interacted with the cytoplasmic domain of Mpl, and we found a new family of proteins designated A2D (for Ataxin-2 Domain protein). The A2D are 130-kDa proteins that have three regions similar to those of Ataxin-2, the gene product causing familial type 2 spinocerebellar ataxia. A2D has several isoforms with different C-terminal domains, all produced from a single gene by alternative splicing. Northern blotting indicated that the A2D gene is widely expressed in immortalized cell lines and hematopoietic and fetal tissues. A2D proteins were constitutively associated with Mpl in vivo in human hematopoietic UT7 cells. TPO also caused the release of A2D from the activated receptor, and the phosphorylation of A2D on tyrosines residues was dependent on the Mpl C-terminal domain. Finally, A2D bound to the unstimulated erythropoietin receptor, whereas erythropoietin caused dissociation from the erythropoietin receptor, suggesting that A2D proteins are new components of the cytokine signaling system.
C1 ICGM, INSERM, U363, F-75014 Paris, France.
C3 Institut National de la Sante et de la Recherche Medicale (Inserm);
   Universite de Montpellier
RP ICGM, INSERM, U363, 27 Rue Faubourg St Jacques, F-75014 Paris, France.
EM courtois@cochin.inserm.fr
RI Chretien, Stany/M-5166-2018; PORTEU, Francoise/I-8445-2016
OI PORTEU, Francoise/0000-0002-2403-4163; courtois,
   genevieve/0000-0001-6370-5575
CR Abramovich C, 1997, EMBO J, V16, P260, DOI 10.1093/emboj/16.2.260
   Aguiar J, 1999, BIOCHEM BIOPH RES CO, V254, P315, DOI 10.1006/bbrc.1998.9929
   BENIT L, 1994, J VIROL, V68, P5270
   Bouscary D, 2001, ONCOGENE, V20, P2197, DOI 10.1038/sj.onc.1204317
   Bunting S, 1997, BLOOD, V90, P3423, DOI 10.1182/blood.V90.9.3423
   CHERIF D, 1989, HUM GENET, V81, P358, DOI 10.1007/BF00283691
   COURTOIS G, 1995, J VIROL, V69, P2794, DOI 10.1128/JVI.69.5.2794-2800.1995
   Cwirla SE, 1997, SCIENCE, V276, P1696, DOI 10.1126/science.276.5319.1696
   Dorsch M, 1999, BLOOD, V94, P2676, DOI 10.1182/blood.V94.8.2676.420k28_2676_2685
   Drachman JG, 1999, J BIOL CHEM, V274, P13480, DOI 10.1074/jbc.274.19.13480
   DRACHMAN JG, 1995, J BIOL CHEM, V270, P4979, DOI 10.1074/jbc.270.10.4979
   Drachman JG, 1997, P NATL ACAD SCI USA, V94, P2350, DOI 10.1073/pnas.94.6.2350
   Fichelson S, 1999, BLOOD, V94, P1601, DOI 10.1182/blood.V94.5.1601.417k19_1601_1613
   FromontRacine M, 1997, NAT GENET, V16, P277, DOI 10.1038/ng0797-277
   Garcia J, 2001, MOL CELL BIOL, V21, P2659, DOI 10.1128/MCB.21.8.2659-2670.2001
   Gaur M, 2001, BLOOD, V97, P1653, DOI 10.1182/blood.V97.6.1653
   Geijsen N, 1999, ONCOGENE, V18, P5126, DOI 10.1038/sj.onc.1202896
   Geijsen N, 2001, SCIENCE, V293, P1136, DOI 10.1126/science.1059157
   Guillard C, 2001, J BIOL CHEM, V276, P2007, DOI 10.1074/jbc.M003527200
   Hinnen A, 1992, Biotechnology, V24, P337
   Imbert G, 1996, NAT GENET, V14, P285, DOI 10.1038/ng1196-285
   KAUSHANSKY K, 1995, THROMB HAEMOSTASIS, V74, P521
   Kaushansky K, 1997, STEM CELLS, V15, P97, DOI 10.1002/stem.5530150813
   Kimura S, 1998, P NATL ACAD SCI USA, V95, P1195, DOI 10.1073/pnas.95.3.1195
   Klockgether T, 1997, NAT MED, V3, P149, DOI 10.1038/nm0297-149
   Koyano S, 1999, NEUROSCI LETT, V273, P117, DOI 10.1016/S0304-3940(99)00656-4
   Lorenzetti D, 1997, NEUROLOGY, V49, P1009, DOI 10.1212/WNL.49.4.1009
   Luoh SM, 2000, MOL CELL BIOL, V20, P507, DOI 10.1128/MCB.20.2.507-515.2000
   Matsuda S, 1996, ONCOGENE, V12, P705
   METHIA N, 1995, CR ACAD SCI III-VIE, V318, P479
   Miyakawa Y, 2000, J BIOL CHEM, V275, P32214, DOI 10.1074/jbc.M005080200
   Miyakawa Y, 1997, BLOOD, V89, P2789, DOI 10.1182/blood.V89.8.2789
   Miyakawa Y, 2001, J BIOL CHEM, V276, P2494, DOI 10.1074/jbc.M002633200
   Mowen KA, 2001, CELL, V104, P731, DOI 10.1016/S0092-8674(01)00269-0
   Muslin AJ, 1996, CELL, V84, P889, DOI 10.1016/S0092-8674(00)81067-3
   NEER EJ, 1995, CELL, V80, P249, DOI 10.1016/0092-8674(95)90407-7
   PALLARD C, 1995, EMBO J, V14, P2847, DOI 10.1002/j.1460-2075.1995.tb07284.x
   Porteu F, 1996, MOL CELL BIOL, V16, P2473
   Pulst SM, 1996, NAT GENET, V14, P269, DOI 10.1038/ng1196-269
   Rojnuckarin P, 1999, BLOOD, V94, P1273, DOI 10.1182/blood.V94.4.1273.416k04_1273_1282
   Rouyez MC, 1997, MOL CELL BIOL, V17, P4991, DOI 10.1128/MCB.17.9.4991
   Sahba S, 1998, GENOMICS, V47, P359, DOI 10.1006/geno.1997.5131
   Sanpei K, 1996, NAT GENET, V14, P277, DOI 10.1038/ng1196-277
   SATO T, 1995, FEBS LETT, V358, P113, DOI 10.1016/0014-5793(94)01406-Q
   Sattler M, 1997, J CELL PHYSIOL, V171, P28
   Shibata H, 2000, HUM MOL GENET, V9, P1303, DOI 10.1093/hmg/9.9.1303
   Solar GP, 1998, BLOOD, V92, P4, DOI 10.1182/blood.V92.1.4.413k38_4_10
   SOUYRI M, 1990, CELL, V63, P1137, DOI 10.1016/0092-8674(90)90410-G
   Wallach D, 1998, CURR OPIN IMMUNOL, V10, P131, DOI 10.1016/S0952-7915(98)80240-9
   Wendling F, 1998, EUR CYTOKINE NETW, V9, P221
NR 50
TC 23
Z9 30
U1 0
U2 0
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
SN 0021-9258
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD MAR 15
PY 2002
VL 277
IS 11
BP 9139
EP 9147
DI 10.1074/jbc.M105970200
PG 9
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 531DK
UT WOS:000174400600055
PM 11784712
OA hybrid
DA 2025-04-10
ER

PT J
AU Soares, JB
   Leite-Moreira, AF
AF Soares, Joao-Bruno
   Leite-Moreira, Adelino F.
TI Ghrelin, des-acyl ghrelin and obestatin: Three pieces of the same puzzle
SO PEPTIDES
LA English
DT Review
DE ghrelin; des-acyl ghrelin; obestatin; GHS-R1a; ghrelin gene
ID HORMONE SECRETAGOGUE RECEPTOR; ACTIVATED PROTEIN-KINASE; INCREASES
   FOOD-INTAKE; BROWN ADIPOSE-TISSUE; OCTANOYL GHRELIN; IN-VIVO;
   BIOLOGICAL-ACTIVITY; DESACYL GHRELIN; ACID-SECRETION; FUNCTIONAL
   RECEPTOR
AB The major active product of ghrelin gene is a 28-amino acid peptide acylated at the serine 3 position with an octanoyl group, called simply ghrelin. Ghrelin has a multiplicity of physiological functions, affecting GH release, food intake, energy and glucose homeostasis, gastrointestinal, cardiovascular, pulmonary and immune function, cell proliferation and differentiation and bone physiology. Nevertheless, recent developments have shown that ghrelin gene can generate various bioactive molecules besides ghrelin, mainly des-acyl ghrelin and obestatin, obtained from alternative splicing or from extensive post-translational modification. Although their receptors have not yet been identified, they have already proven to be active, having intriguingly subtle but opposite physiological actions to ghrelin. This suggests the existence of a novel endocrine system with multiple effector elements which not only may have opposite actions but may regulate the action of each other. In this review, we summarize the steps which lead to the production of the different ghrelin gene products and examine the most significant differences between them in terms of structure and actions. (C) 2008 Elsevier Inc. All rights reserved.
C1 [Soares, Joao-Bruno; Leite-Moreira, Adelino F.] Univ Porto, Serv Fisiol, Fac Med, P-4200319 Oporto, Portugal.
C3 Universidade do Porto
RP Leite-Moreira, AF (corresponding author), Univ Porto, Serv Fisiol, Fac Med, P-4200319 Oporto, Portugal.
EM amoreira@med.up.pt
RI Leite-Moreira, Adelino/A-1463-2018
OI Cruz Soares, Joao Bruno/0009-0009-6596-2482; Leite-Moreira,
   Adelino/0000-0001-7808-3596
CR Akamizu T, 2005, J CLIN ENDOCR METAB, V90, P6, DOI 10.1210/jc.2004-1640
   Ariyasu H, 2005, ENDOCRINOLOGY, V146, P355, DOI 10.1210/en.2004-0629
   Asakawa A, 2005, GUT, V54, P18, DOI 10.1136/gut.2004.038737
   Baldanzi G, 2002, J CELL BIOL, V159, P1029, DOI 10.1083/jcb.200207165
   Bang AS, 2007, J ENDOCRINOL, V192, P313, DOI 10.1677/JOE-06-0021
   Barazzoni R, 2005, AM J PHYSIOL-ENDOC M, V288, pE228, DOI 10.1152/ajpendo.00115.2004
   Barreiro ML, 2004, ENDOCRINOLOGY, V145, P4825, DOI 10.1210/en.2004-0732
   Bassil AK, 2007, BRIT J PHARMACOL, V150, P58, DOI 10.1038/sj.bjp.0706969
   Beaumont NJ, 2003, J BIOL CHEM, V278, P8877, DOI 10.1074/jbc.C200575200
   Bedendi I, 2003, EUR J PHARMACOL, V476, P87, DOI 10.1016/S0014-2999(03)02083-1
   Bednarek MA, 2000, J MED CHEM, V43, P4370, DOI 10.1021/jm0001727
   Bodart V, 2002, CIRC RES, V90, P844, DOI 10.1161/01.RES.0000016164.02525.B4
   Bresciani E, 2006, J ENDOCRINOL INVEST, V29, pRC16, DOI 10.1007/BF03344175
   Broglio F, 2003, J CLIN ENDOCR METAB, V88, P4268, DOI 10.1210/jc.2002-021940
   Brzozowski T, 2004, REGUL PEPTIDES, V120, P39, DOI 10.1016/j.regpep.2004.02.010
   Brzozowski Tomasz, 2005, Inflammopharmacology, V13, P45, DOI 10.1163/156856005774423971
   Burdyga G, 2006, AM J PHYSIOL-GASTR L, V290, pG1289, DOI 10.1152/ajpgi.00543.2005
   Camiña JP, 2007, J CELL PHYSIOL, V211, P1, DOI 10.1002/jcp.20925
   Camiña JP, 2006, J NEUROENDOCRINOL, V18, P65, DOI 10.1111/j.1365-2826.2005.01379.x
   Caminos JE, 2003, ENDOCRINOLOGY, V144, P1594, DOI 10.1210/en.2002-221058
   Carlini VP, 2007, BIOCHEM BIOPH RES CO, V352, P907, DOI 10.1016/j.bbrc.2006.11.112
   Carlini VP, 2002, BIOCHEM BIOPH RES CO, V299, P739, DOI 10.1016/S0006-291X(02)02740-7
   Cassoni P, 2006, J ENDOCRINOL INVEST, V29, P781, DOI 10.1007/BF03347371
   Cassoni P, 2004, EUR J ENDOCRINOL, V150, P173, DOI 10.1530/eje.0.1500173
   Cassoni P, 2001, J CLIN ENDOCR METAB, V86, P1738, DOI 10.1210/jc.86.4.1738
   Chang L, 2004, J CARDIOVASC PHARM, V43, P165, DOI 10.1097/00005344-200402000-00001
   Chang L, 2003, EUR J PHARMACOL, V473, P171, DOI 10.1016/S0014-2999(03)01972-1
   Chanoine JP, 2006, HORM RES, V66, P81, DOI 10.1159/000093585
   Chanoine JP, 2004, ENDOCRINOLOGY, V145, P3813, DOI 10.1210/en.2004-0053
   CHARTREL N, 2005, SCIENCE, V310, P996
   Chen CY, 2005, INT J MOL MED, V16, P695
   Chen HY, 2004, ENDOCRINOLOGY, V145, P2607, DOI 10.1210/en.2003-1596
   Conconi MT, 2004, PEPTIDES, V25, P2179, DOI 10.1016/j.peptides.2004.08.011
   Couce ME, 2006, J ENDOCRINOL INVEST, V29, P599, DOI 10.1007/BF03344158
   Cummings DE, 2004, AM J PHYSIOL-ENDOC M, V287, pE297, DOI 10.1152/ajpendo.00582.2003
   Date Y, 2000, ENDOCRINOLOGY, V141, P4255, DOI 10.1210/en.141.11.4255
   de la Cour CD, 2004, REGUL PEPTIDES, V120, P23, DOI 10.1016/j.regpep.2004.02.008
   De Smet B, 2007, NEUROGASTROENT MOTIL, V19, P211, DOI 10.1111/j.1365-2982.2006.00883.x
   De Vriese C, 2007, ENDOCRINOLOGY, V148, P2355, DOI 10.1210/en.2006-1281
   Delhanty PJD, 2006, J ENDOCRINOL, V188, P37, DOI 10.1677/joe.1.06404
   Depoortere I, 2005, EUR J PHARMACOL, V515, P160, DOI 10.1016/j.ejphar.2005.04.008
   Dixit VD, 2004, J CLIN INVEST, V114, P57, DOI 10.1172/JCI200421134
   Dixit VD, 2007, J CLIN INVEST, V117, P2778, DOI 10.1172/JCI30248
   Dun SL, 2006, J ENDOCRINOL, V191, P481, DOI 10.1677/joe.1.06944
   Duxbury MS, 2003, BIOCHEM BIOPH RES CO, V309, P464, DOI 10.1016/j.bbrc.2003.08.024
   El Eter E, 2007, J GASTROEN HEPATOL, V22, P1791, DOI 10.1111/j.1440-1746.2006.04696.x
   Fernández-Fernández R, 2005, NEUROENDOCRINOLOGY, V82, P245, DOI 10.1159/000092753
   Filigheddu N, 2007, MOL BIOL CELL, V18, P986, DOI 10.1091/mbc.E06-05-0402
   Frascarelli S, 2003, BASIC RES CARDIOL, V98, P401, DOI 10.1007/s00395-003-0434-7
   Fujino K, 2003, J PHYSIOL-LONDON, V550, P227, DOI 10.1113/jphysiol.2003.040600
   Fukushima N, 2005, J BONE MINER RES, V20, P790, DOI 10.1359/JBMR.041237
   Gauna C, 2005, J CLIN ENDOCR METAB, V90, P1055, DOI 10.1210/jc.2004-1069
   Gaytan F, 2004, J CLIN ENDOCR METAB, V89, P400, DOI 10.1210/jc.2003-031375
   Gaytan F, 2003, J CLIN ENDOCR METAB, V88, P879, DOI 10.1210/jc.2002-021196
   Ghelardoni S, 2006, J ENDOCRINOL INVEST, V29, P115, DOI 10.1007/BF03344083
   Gnanapavan S, 2002, J CLIN ENDOCR METAB, V87, P2988, DOI 10.1210/jc.87.6.2988
   Gonzalez-Rey E, 2006, GASTROENTEROLOGY, V130, P1707, DOI 10.1053/j.gastro.2006.01.041
   Gourcerol G, 2007, REGUL PEPTIDES, V141, P1, DOI 10.1016/j.regpep.2006.12.023
   Granata R, 2006, J ENDOCRINOL INVEST, V29, pRC19, DOI 10.1007/BF03347367
   GRANATA R, 2007, DIABETES
   Green BD, 2007, PEPTIDES, V28, P981, DOI 10.1016/j.peptides.2007.02.003
   Guan XM, 1997, MOL BRAIN RES, V48, P23, DOI 10.1016/S0169-328X(97)00071-5
   Guo ZF, 2007, J CLIN ENDOCR METAB, V92, P1875, DOI 10.1210/jc.2006-2306
   Harada T, 2008, BIOL PSYCHIAT, V63, P245, DOI 10.1016/j.biopsych.2007.04.005
   Hehir MP, 2008, AM J OBSTET GYNECOL, V198, DOI 10.1016/j.ajog.2007.09.040
   Heijboer AC, 2006, DIABETOLOGIA, V49, P732, DOI 10.1007/s00125-006-0138-2
   Hewson AK, 2000, J NEUROENDOCRINOL, V12, P1047, DOI 10.1046/j.1365-2826.2000.00584.x
   Holst B, 2007, ENDOCRINOLOGY, V148, P13, DOI 10.1210/en.2006-0933
   Hosoda H, 2000, J BIOL CHEM, V275, P21995, DOI 10.1074/jbc.M002784200
   Hosoda H, 2004, CLIN CHEM, V50, P1077, DOI 10.1373/clinchem.2003.025841
   Hosoda H, 2003, J BIOL CHEM, V278, P64, DOI 10.1074/jbc.M205366200
   Howard AD, 1996, SCIENCE, V273, P974, DOI 10.1126/science.273.5277.974
   Iglesias MJ, 2007, J ENDOCRINOL INVEST, V30, P470, DOI 10.1007/BF03346330
   Jeffery PL, 2005, ENDOCRINOLOGY, V146, P432, DOI 10.1210/en.2003-1466
   Jeffery PL, 2002, J ENDOCRINOL, V172, pR7, DOI 10.1677/joe.0.172R007
   Kanamoto N, 2004, ENDOCRINOLOGY, V145, P4144, DOI 10.1210/en.2003-1718
   Kapica M, 2007, J PHYSIOL PHARMACOL, V58, P123
   Kasimay Ö, 2006, HEPATOL RES, V36, P11, DOI 10.1016/j.hepres.2006.06.009
   Kawamura K, 2003, ENDOCRINOLOGY, V144, P2623, DOI 10.1210/en.2003-0033
   Kim MS, 2004, MOL ENDOCRINOL, V18, P2291, DOI 10.1210/me.2003-0459
   Kishimoto M, 2003, BIOCHEM BIOPH RES CO, V305, P186, DOI 10.1016/S0006-291X(03)00722-8
   Kleinz MJ, 2006, CARDIOVASC RES, V69, P227, DOI 10.1016/j.cardiores.2005.09.001
   Kojima M, 1999, NATURE, V402, P656, DOI 10.1038/45230
   Kojima M, 2005, PHYSIOL REV, V85, P495, DOI 10.1152/physrev.00012.2004
   Koo GC, 2001, J IMMUNOL, V166, P4195, DOI 10.4049/jimmunol.166.6.4195
   Lagaud GJ, 2007, BIOCHEM BIOPH RES CO, V357, P264, DOI 10.1016/j.bbrc.2007.03.138
   Lago R, 2007, ANN RHEUM DIS, V66, P1399, DOI 10.1136/ard.2006.068155
   LANFRANCO F, 2006, P 88 END SOC M ENDO2, P93
   Lauwers E, 2006, BIOCHEM BIOPH RES CO, V351, P21, DOI 10.1016/j.bbrc.2006.09.141
   Lawrence CB, 2002, ENDOCRINOLOGY, V143, P155, DOI 10.1210/en.143.1.155
   Leite-Moreira AF, 2007, DRUG DISCOV TODAY, V12, P276, DOI 10.1016/j.drudis.2007.02.009
   Li L, 2006, ACTA PHARMACOL SIN, V27, P527, DOI 10.1111/j.1745-7254.2006.00319.x
   Li WG, 2004, CIRCULATION, V109, P2221, DOI 10.1161/01.CIR.0000127956.43874.F2
   Li Y, 2006, AM J PHYSIOL-GASTR L, V290, pG1350, DOI 10.1152/ajpgi.00493.2005
   Lin YZ, 2004, HYPERTENSION, V43, P977, DOI 10.1161/01.HYP.0000122803.91559.55
   Maccarinelli G, 2005, J ENDOCRINOL, V184, P249, DOI 10.1677/joe.1.05837
   Malagón MM, 2003, ENDOCRINOLOGY, V144, P5372, DOI 10.1210/en.2003-0723
   Martini AC, 2006, ENDOCRINOLOGY, V147, P2374, DOI 10.1210/en.2005-1422
   Matsuda K, 2006, PEPTIDES, V27, P2321, DOI 10.1016/j.peptides.2006.03.028
   Matsumoto M, 2001, BIOCHEM BIOPH RES CO, V287, P142, DOI 10.1006/bbrc.2001.5553
   Mazzocchi G, 2004, PEPTIDES, V25, P1269, DOI 10.1016/j.peptides.2004.05.011
   MESZAROSOVA M, 2007, ANIM REPROD SCI
   Mozid AM, 2003, HORM METAB RES, V35, P455
   Muccioli G, 2004, EUR J PHARMACOL, V498, P27, DOI 10.1016/j.ejphar.2004.07.066
   Murata M, 2002, J BIOL CHEM, V277, P5667, DOI 10.1074/jbc.M103898200
   Nagaya N, 2001, J CLIN ENDOCR METAB, V86, P5854, DOI 10.1210/jc.86.12.5854
   Nagaya N, 2001, AM J PHYSIOL-REG I, V280, pR1483, DOI 10.1152/ajpregu.2001.280.5.R1483
   Nakahara K, 2006, ENDOCRINOLOGY, V147, P1333, DOI 10.1210/en.2005-0708
   Nishi Y, 2005, ENDOCRINOLOGY, V146, P2709, DOI 10.1210/en.2004-0645
   Nishi Y, 2005, ENDOCRINOLOGY, V146, P2255, DOI 10.1210/en.2004-0695
   Nogueiras R, 2007, ENDOCRINOLOGY, V148, P21, DOI 10.1210/en.2006-0915
   Ott V, 2002, HORM METAB RES, V34, P640, DOI 10.1055/s-2002-38261
   PARK JM, 2008, EXP BIOL MED MAYWOOD, V233, P148
   Patel AD, 2006, REGUL PEPTIDES, V134, P17, DOI 10.1016/j.regpep.2005.11.001
   Patterson M, 2005, J CLIN ENDOCR METAB, V90, P2205, DOI 10.1210/jc.2004-1641
   Pemberton C, 2003, BIOCHEM BIOPH RES CO, V310, P567, DOI 10.1016/j.bbrc.2003.09.045
   Pemberton CJ, 2004, AM J PHYSIOL-HEART C, V287, pH1522, DOI 10.1152/ajpheart.00193.2004
   Pénicaud L, 2006, CURR OPIN CLIN NUTR, V9, P458, DOI 10.1097/01.mco.0000232908.84483.e0
   Popovic V, 2003, J CLIN ENDOCR METAB, V88, P3450, DOI 10.1210/jc.2003-030211
   Qader SS, 2008, REGUL PEPTIDES, V146, P230, DOI 10.1016/j.regpep.2007.09.017
   Rak A, 2008, GROWTH HORM IGF RES, V18, P221, DOI 10.1016/j.ghir.2007.09.004
   Rocha-Sousa A, 2006, EXP EYE RES, V83, P1179, DOI 10.1016/j.exer.2006.06.005
   Rossi F, 2007, ATHEROSCLEROSIS, V192, P291, DOI 10.1016/j.atherosclerosis.2006.07.021
   Salehi A, 2004, REGUL PEPTIDES, V118, P143, DOI 10.1016/j.regpep.2003.12.001
   Samson WK, 2007, AM J PHYSIOL-REG I, V292, pR637, DOI 10.1152/ajpregu.00395.2006
   Sato M, 2006, BIOCHEM BIOPH RES CO, V350, P598, DOI 10.1016/j.bbrc.2006.09.088
   Seoane LM, 2006, J ENDOCRINOL INVEST, V29, pRC13, DOI 10.1007/BF03344174
   Shanado Y, 2004, BIOCHEM BIOPH RES CO, V325, P1487, DOI 10.1016/j.bbrc.2004.10.193
   Shimbara T, 2004, NEUROSCI LETT, V369, P75, DOI 10.1016/j.neulet.2004.07.060
   Shimizu Y, 2006, J PHYSIOL-LONDON, V576, P329, DOI 10.1113/jphysiol.2006.116160
   Sibilia V, 2006, J ENDOCRINOL INVEST, V29, pRC31, DOI 10.1007/BF03349204
   Sibilia V, 2006, J NEUROENDOCRINOL, V18, P122, DOI 10.1111/j.1365-2826.2005.01391.x
   Soares JB, 2006, PEPTIDES, V27, P1616, DOI 10.1016/j.peptides.2005.12.007
   Sun YX, 2008, ENDOCRINOLOGY, V149, P843, DOI 10.1210/en.2007-0271
   Sun YX, 2003, MOL CELL BIOL, V23, P7973, DOI 10.1128/MCB.23.22.7973-7981.2003
   Sun YX, 2004, P NATL ACAD SCI USA, V101, P4679, DOI 10.1073/pnas.0305930101
   Szentirmai E, 2006, NEUROSCI LETT, V404, P222, DOI 10.1016/j.neulet.2006.05.053
   Tachibana T, 2006, NEUROSCI LETT, V405, P241, DOI 10.1016/j.neulet.2006.07.019
   Tack J, 2006, GUT, V55, P327, DOI 10.1136/gut.2004.060426
   Tack J, 2005, ALIMENT PHARM THER, V22, P847, DOI 10.1111/j.1365-2036.2005.02658.x
   Tang-Christensen M, 2004, ENDOCRINOLOGY, V145, P4645, DOI 10.1210/en.2004-0529
   Tena-Sempere M, 2002, ENDOCRINOLOGY, V143, P717, DOI 10.1210/en.143.2.717
   Tesauro M, 2005, CIRCULATION, V112, P2986, DOI 10.1161/CIRCULATIONAHA.105.553883
   Thompson NM, 2004, ENDOCRINOLOGY, V145, P234, DOI 10.1210/en.2003-0899
   Tigno XT, 2003, CLIN HEMORHEOL MICRO, V29, P409
   Toshinai K, 2006, ENDOCRINOLOGY, V147, P2306, DOI 10.1210/en.2005-1357
   Toshinai K, 2003, ENDOCRINOLOGY, V144, P1506, DOI 10.1210/en.2002-220788
   Tsubone T, 2005, REGUL PEPTIDES, V130, P97, DOI 10.1016/j.regpep.2005.04.004
   Tsubota Y, 2005, NEUROREPORT, V16, P163, DOI 10.1097/00001756-200502080-00019
   van der Lely AJ, 2004, ENDOCR REV, V25, P426, DOI 10.1210/er.2002-0029
   Volante M, 2002, J CLIN ENDOCR METAB, V87, P1300, DOI 10.1210/jc.87.3.1300
   Wang WG, 2008, REGUL PEPTIDES, V146, P169, DOI 10.1016/j.regpep.2007.09.007
   Wei W, 2005, ENDOCRINOLOGY, V146, P1611, DOI 10.1210/en.2004-1306
   Weikel JC, 2003, AM J PHYSIOL-ENDOC M, V284, pE407, DOI 10.1152/ajpendo.00184.2002
   Williams DL, 2003, ENDOCRINOLOGY, V144, P5184, DOI 10.1210/en.2003-1059
   Wren AM, 2001, J CLIN ENDOCR METAB, V86, P5992, DOI 10.1210/jc.86.12.5992
   Yakabi K, 2006, DIGEST DIS SCI, V51, P1313, DOI 10.1007/s10620-005-9002-3
   Yamamoto D, 2007, REGUL PEPTIDES, V138, P141, DOI 10.1016/j.regpep.2006.09.001
   Yasuda T, 2003, NEUROSCI LETT, V349, P75, DOI 10.1016/S0304-3940(03)00789-4
   Yeh AH, 2005, CLIN CANCER RES, V11, P8295, DOI 10.1158/1078-0432.CCR-05-0443
   Yoshimoto A, 2002, J AM SOC NEPHROL, V13, P2748, DOI 10.1097/01.ASN.0000032420.12455.74
   Zhang JV, 2005, SCIENCE, V310, P996, DOI 10.1126/science.1117255
   Zhao CM, 2008, CELL TISSUE RES, V331, P575, DOI 10.1007/s00441-007-0514-3
   Zhu XR, 2006, J BIOL CHEM, V281, P38867, DOI 10.1074/jbc.M607955200
   Zizzari P, 2007, ENDOCRINOLOGY, V148, P1648, DOI 10.1210/en.2006-1231
NR 165
TC 155
Z9 182
U1 0
U2 16
PU ELSEVIER SCIENCE INC
PI NEW YORK
PA STE 800, 230 PARK AVE, NEW YORK, NY 10169 USA
SN 0196-9781
EI 1873-5169
J9 PEPTIDES
JI Peptides
PD JUL
PY 2008
VL 29
IS 7
BP 1255
EP 1270
DI 10.1016/j.peptides.2008.02.018
PG 16
WC Biochemistry & Molecular Biology; Endocrinology & Metabolism;
   Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Endocrinology & Metabolism;
   Pharmacology & Pharmacy
GA 324AE
UT WOS:000257489100022
PM 18396350
OA Green Published
DA 2025-04-10
ER

PT J
AU Chen, M
   Zhu, JY
   Luo, HY
   Mu, WJ
   Guo, L
AF Chen, Min
   Zhu, Jieying
   Luo, Hongyang
   Mu, Wangjing
   Guo, Liang
TI The journey towards physiology and pathology: Tracing the path of
   neuregulin 4
SO GENES & DISEASES
LA English
DT Review
DE Angiogenesis; Cardiovascular diseases; Inflammation; Insulin resistance;
   Lipid and glucose metabolism; NAFLD; Neurobiogenesis; Obesity
ID NECROSIS-FACTOR-ALPHA; GENE-EXPRESSION; PROSTATE-CANCER; ADIPOSE-TISSUE;
   ERBB4 ISOFORM; GROWTH-FACTOR; BROWN; CARCINOMA; VARIANTS; PRODUCTS
AB Neuregulin 4 (Nrg4), an epidermal growth factor (EGF) family member, can bind to and activate the ErbB4 receptor tyrosine kinase. Nrg4 has five different isoforms by alternative splicing and performs a wide variety of functions. Nrg4 is involved in a spectrum of physiological processes including neurobiogenesis, lipid metabolism, glucose metabolism, thermogenesis, and angiogenesis. In pathological processes, Nrg4 inhibits inflammatory factor levels and suppresses apoptosis in inflammatory diseases. In addition, Nrg4 could ameliorate obesity, insulin resistance, and cardiovascular diseases. Furthermore, Nrg4 improves non-alcoholic fatty liver disease (NAFLD) by promoting autophagy, improving lipid metabolism, and inhibiting cell death of hepatocytes. Besides, Nrg4 is closely related to the development of cancer, hyperthyroidism, and some other diseases. Therefore, elucidation of the functional role and mechanisms of Nrg4 will provide a clearer view of the therapeutic potential and possible risks of Nrg4. & COPY; 2023 The Authors. Publishing services by Elsevier B.V. on behalf of KeAi Communications Co., Ltd. This is an open access article under the CC BY-NC-ND license (http://creativecommons. org/licenses/by-nc-nd/4.0/).
C1 [Chen, Min; Zhu, Jieying; Luo, Hongyang; Mu, Wangjing; Guo, Liang] Shanghai Univ Sport, Sch Exercise & Hlth, Shanghai Frontiers Sci Res Base Exercise & Metab H, Shanghai 200438, Peoples R China.
C3 Shanghai University of Sport
RP Guo, L (corresponding author), Shanghai Univ Sport, Sch Exercise & Hlth, Shanghai Frontiers Sci Res Base Exercise & Metab H, Shanghai 200438, Peoples R China.
EM guoliang@sus.edu.cn
RI Mu, wangjing/GSD-3101-2022
OI Chen, Min/0009-0000-8956-0028; Guo, Liang/0000-0001-7353-8336
FU Program for Overseas High- level Talents at Shanghai Institutions of
   Higher Learning (China) [2022100]; National Natural Science Foundation
   of China [32070751, 31871435]
FX <BOLD>Funding</BOLD> This work was supported by The Program for Overseas
   High- level Talents at Shanghai Institutions of Higher Learning (China)
   (No. 2022100 to L.G.) and the National Natural Science Foundation of
   China (No. 32070751 and 31871435 to L.G.) .
CR Alizadeh Mona, 2021, Arch Med Deporte, V38, P389, DOI 10.18176/archmeddeporte.00066
   Amsellem-Ouazana D, 2006, J UROLOGY, V175, P1127, DOI 10.1016/S0022-5347(05)00317-4
   Bernard JK, 2012, J BIOL CHEM, V287, DOI 10.1074/jbc.M112.400846
   Cao SS, 2021, BIOSCIENCE REP, V41, DOI 10.1042/BSR20211658
   Chen M, 2023, GENES DIS, V10, P877, DOI 10.1016/j.gendis.2021.12.023
   Chen ZM, 2017, MOL METAB, V6, P863, DOI 10.1016/j.molmet.2017.03.016
   Christian M, 2015, ADIPOCYTE, V4, P50, DOI 10.4161/adip.29853
   Comas F, 2019, FRONT PHYSIOL, V10, DOI 10.3389/fphys.2019.00039
   Dai YN, 2015, METABOLISM, V64, P1667, DOI 10.1016/j.metabol.2015.08.013
   Diaz-Saez F, 2021, INT J MOL SCI, V22, DOI 10.3390/ijms222312960
   Diwanji D, 2021, NATURE, V600, P339, DOI 10.1038/s41586-021-04084-z
   Ebi M, 2011, MOL MED REP, V4, P1151, DOI 10.3892/mmr.2011.542
   Elenius K, 1997, J BIOL CHEM, V272, P26761, DOI 10.1074/jbc.272.42.26761
   Elenius K, 1999, ONCOGENE, V18, P2607, DOI 10.1038/sj.onc.1202612
   Fagerberg L, 2014, MOL CELL PROTEOMICS, V13, P397, DOI 10.1074/mcp.M113.035600
   Guo D, 2021, FRONT PHYSIOL, V12, DOI 10.3389/fphys.2021.667330
   Guo L, 2019, J BIOL CHEM, V294, P11805, DOI 10.1074/jbc.RA119.008708
   Guo L, 2019, J BIOL CHEM, V294, P9642, DOI [10.1074/jbc.RA119.008419, 10.1074/jbc.ra119.008419]
   Guo L, 2017, J CLIN INVEST, V127, P4449, DOI 10.1172/JCI96324
   Guo L, 2016, MOL CELL BIOL, V36, P2553, DOI 10.1128/MCB.00227-16
   Guo YY, 2022, NAT METAB, V4, P1352, DOI 10.1038/s42255-022-00644-3
   Guo YY, 2019, J BIOL CHEM, V294, P15014, DOI 10.1074/jbc.RA119.009936
   Harari D, 1999, ONCOGENE, V18, P2681, DOI 10.1038/sj.onc.1202631
   Hayes NVL, 2008, ONCOGENE, V27, P715, DOI 10.1038/sj.onc.1210689
   Hayes NVL, 2007, CLIN CANCER RES, V13, P3147, DOI 10.1158/1078-0432.CCR-06-2237
   Hayes NVL, 2011, ENDOCR-RELAT CANCER, V18, P39, DOI 10.1677/ERC-10-0112
   Henriques F, 2020, CELL REP, V32, DOI 10.1016/j.celrep.2020.107998
   Howard L, 2021, DEV NEUROBIOL, V81, P139, DOI 10.1002/dneu.22803
   Jiang J, 2016, SCI REP-UK, V6, DOI 10.1038/srep36710
   Junttila TT, 2000, TRENDS CARDIOVAS MED, V10, P304, DOI 10.1016/S1050-1738(01)00065-2
   Kabeya Y, 2004, J CELL SCI, V117, P2805, DOI 10.1242/jcs.01131
   Kainulainen V, 2000, J BIOL CHEM, V275, P8641, DOI 10.1074/jbc.275.12.8641
   Kissig M, 2016, CELL, V166, P258, DOI 10.1016/j.cell.2016.06.038
   Kralisch S, 2018, DIABETES METAB, V44, P150, DOI 10.1016/j.diabet.2017.06.001
   Kralisch S, 2019, EUR J ENDOCRINOL, V181, P151, DOI 10.1530/EJE-19-0017
   Lee HW, 2021, CIRCULATION, V144, P1308, DOI 10.1161/CIRCULATIONAHA.121.054071
   Li BY, 2022, MOL METAB, V61, DOI 10.1016/j.molmet.2022.101500
   Li M, 2019, ENDOCR CONNECT, V8, P728, DOI 10.1530/EC-19-0175
   Liberale L, 2020, EUR J CLIN INVEST, V50, DOI 10.1111/eci.13306
   Liu Y, 2018, J BIOL CHEM, V293, P14012, DOI 10.1074/jbc.RA118.004401
   Luo Hong-Yang, 2023, Genes Dis, V10, P915, DOI 10.1016/j.gendis.2022.06.005
   Lyne JC, 1997, CANCER J SCI AM, V3, P21
   Ma YJ, 2016, SCI REP-UK, V6, DOI 10.1038/srep26242
   Marshall C, 2006, BREAST CANCER RES TR, V96, P163, DOI 10.1007/s10549-005-9073-z
   Martínez C, 2022, FRONT PHYSIOL, V13, DOI 10.3389/fphys.2022.950791
   McElroy SJ, 2014, AM J PATHOL, V184, P2768, DOI 10.1016/j.ajpath.2014.06.015
   Memon AA, 2004, BRIT J CANCER, V91, P2034, DOI 10.1038/sj.bjc.6602251
   Mu WJ, 2021, INT J MOL SCI, V22, DOI 10.3390/ijms222111512
   Naito H, 2020, INT IMMUNOL, V32, P295, DOI 10.1093/intimm/dxaa008
   Ng YK, 2014, MELANOMA RES, V24, P207, DOI 10.1097/CMR.0000000000000060
   Nielsen TO, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0094606
   Nugroho DB, 2018, BIOCHEM BIOPH RES CO, V504, P427, DOI 10.1016/j.bbrc.2018.08.197
   Nugroho DB, 2018, BIOCHEM BIOPH RES CO, V503, P378, DOI 10.1016/j.bbrc.2018.06.043
   Orhan C, 2021, FRONT VET SCI, V8, DOI 10.3389/fvets.2021.617789
   Paramo B, 2021, ENEURO, V8, DOI 10.1523/ENEURO.0288-20.2021
   Paramo B, 2019, J NEUROPATH EXP NEUR, V78, P725, DOI 10.1093/jnen/nlz046
   Paramo B, 2018, EXP NEUROL, V302, P85, DOI 10.1016/j.expneurol.2018.01.002
   Peng WQ, 2021, DIABETES, V70, P1458, DOI 10.2337/db20-1210
   Rabanal-Ruiz Y, 2017, ESSAYS BIOCHEM, V61, P565, DOI 10.1042/EBC20170027
   Rahimzadeh M, 2020, SCI REP-UK, V10, DOI 10.1038/s41598-020-62680-x
   Ravichandran KS, 2001, ONCOGENE, V20, P6322, DOI 10.1038/sj.onc.1204776
   Rio C, 2000, J BIOL CHEM, V275, P10379, DOI 10.1074/jbc.275.14.10379
   Rosell M, 2014, AM J PHYSIOL-ENDOC M, V306, pE945, DOI 10.1152/ajpendo.00473.2013
   Ruan H, 2002, DIABETES, V51, P3176, DOI 10.2337/diabetes.51.11.3176
   Saeidi A, 2022, FRONT PHYSIOL, V12, DOI 10.3389/fphys.2021.797574
   Schumacher MA, 2021, AM J PHYSIOL-GASTR L, V320, pG990, DOI 10.1152/ajpgi.00296.2020
   Schumacher MA, 2017, CELL DEATH DIS, V8, DOI 10.1038/cddis.2017.42
   Shi JB, 2019, AM J TRANSL RES, V11, P5501
   Shi LF, 2022, NAT METAB, V4, P1573, DOI 10.1038/s42255-022-00671-0
   Shi LF, 2022, CALCIFIED TISSUE INT, V110, P131, DOI 10.1007/s00223-021-00897-2
   Song NJ, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0162228
   Sundvall M, 2007, ONCOGENE, V26, P6905, DOI 10.1038/sj.onc.1210501
   Temur M, 2017, GINEKOL POL, V88, P517, DOI 10.5603/GP.a2017.0095
   Vidal GA, 2005, J BIOL CHEM, V280, P19777, DOI 10.1074/jbc.M412457200
   Villarroya J, 2019, J ENDOCRINOL, V243, pR19, DOI 10.1530/JOE-19-0295
   Wang GX, 2014, NAT MED, V20, P1436, DOI 10.1038/nm.3713
   Wang R, 2020, ENDOCR RES, V45, P190, DOI 10.1080/07435800.2020.1721528
   Wang R, 2019, CLIN OBES, V9, DOI 10.1111/cob.12289
   Wang Y, 2019, FRONT PHYSIOL, V10, DOI 10.3389/fphys.2019.00494
   Wang Y, 2019, PLOS ONE, V14, DOI 10.1371/journal.pone.0225705
   Williams CC, 2004, J CELL BIOL, V167, P469, DOI 10.1083/jcb.200403155
   Xia TW, 2019, BIOMED RES INT, V2019, DOI 10.1155/2019/4039472
   Yan PJ, 2020, DIABETOL METAB SYNDR, V12, DOI 10.1186/s13098-020-00550-2
   Yan PJ, 2019, CYTOKINE, V113, P356, DOI 10.1016/j.cyto.2018.10.007
   Yang F, 2021, J NUTR BIOCHEM, V93, DOI 10.1016/j.jnutbio.2021.108628
   Yoon JC, 2001, NATURE, V413, P131, DOI 10.1038/35093050
   Zeng H, 2018, AM J PHYSIOL-ENDOC M, V315, pE583, DOI 10.1152/ajpendo.00166.2018
   Zhang L, 2021, THER ADV ENDOCRINOL, V12, DOI 10.1177/20420188211049614
   Zhang L, 2017, ENDOCRINE, V57, P535, DOI 10.1007/s12020-017-1324-3
   Zhang LL, 2019, LIFE SCI, V217, P185, DOI 10.1016/j.lfs.2018.12.006
   Zhang P, 2022, CELL METAB, V34, P1359, DOI 10.1016/j.cmet.2022.07.010
   Zhu B, 2020, EUR J PHARMACOL, V884, DOI 10.1016/j.ejphar.2020.173350
   Zhu JY, 2023, GENES DIS, V10, P1833, DOI 10.1016/j.gendis.2022.03.018
   Zhu JY, 2022, METABOLISM, V134, DOI 10.1016/j.metabol.2022.155241
NR 94
TC 15
Z9 16
U1 3
U2 18
PU KEAI PUBLISHING LTD
PI BEIJING
PA 16 DONGHUANGCHENGGEN NORTH ST, Building 5, Room 411, BEIJING, DONGCHENG
   DISTRICT 100009, PEOPLES R CHINA
SN 2352-4820
EI 2352-3042
J9 GENES DIS
JI Genes Dis.
PD MAR
PY 2024
VL 11
IS 2
DI 10.1016/j.gendis.2023.03.021
PG 14
WC Biochemistry & Molecular Biology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Genetics & Heredity
GA S7LR2
UT WOS:001072953000001
PM 37692526
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Öklü, R
   Hesketh, R
AF Öklü, R
   Hesketh, R
TI The latent transforming growth factor β binding protein (LTBP) family
SO BIOCHEMICAL JOURNAL
LA English
DT Review
DE atherosclerosis; cancer; fibrillin; Marfan's syndrome; TGF beta
ID SMOOTH-MUSCLE CELLS; FIBROBLAST EXTRACELLULAR-MATRIX; MOLECULAR-WEIGHT
   COMPLEX; RECEPTOR-TYPE-II; TGF-BETA; MANNOSE 6-PHOSPHATE;
   MARFAN-SYNDROME; FACTOR-BETA-1 PRECURSOR; CANCER-CELLS; STRUCTURAL
   CHARACTERIZATION
AB The transforming growth factor beta (TGF beta) cytokines are a multifunctional family that exert a wide variety of effects on both normal and transformed mammalian cells. The secretion and activation of TGF betas is regulated by their association with latency-associated proteins and latent TGF beta binding proteins (LTBPs). Over the past few years, three members of the LTBP family have been identified, in addition to the protoype LTBP1 first sequenced in 1990. Three of the LTBP family are expressed in a variety of isoforms as a consequence of alternative splicing. This review summarizes the differences between the isoforms in terms of the effects on domain structure and hence possible function. The close identity between LTBPs and members of the fibrillin family, mutations in which have been linked directly to Marfan's syndrome, suggests that anomalous expression of LTBPs may be associated with disease. Recent data indicating that differential expression of LTBP1 isoforms occurs during the development of coronary heart disease is considered, together with evidence that modulation of LTBP function, and hence of TGF beta activity, is associated with a variety of cancers.
C1 Univ Cambridge, Dept Biochem, Sect Cardiovasc Biol, Cambridge CB2 1QW, England.
   Northwestern Univ, Sch Med, Lake Shore Ctr, Chicago, IL 60611 USA.
C3 University of Cambridge; Northwestern University
RP Univ Cambridge, Dept Biochem, Sect Cardiovasc Biol, Tennis Court Rd, Cambridge CB2 1QW, England.
EM t.r.hesketh@bioc.cam.ac.uk
RI oklu, rahmi/AAY-4676-2021
OI Oklu, Rahmi/0000-0003-4984-1778
CR Ades LC, 1996, J MED GENET, V33, P665, DOI 10.1136/jmg.33.8.665
   ANZANO MA, 1983, P NATL ACAD SCI-BIOL, V80, P6264, DOI 10.1073/pnas.80.20.6264
   Bashir MM, 1996, INT J BIOCHEM CELL B, V28, P531, DOI 10.1016/1357-2725(95)00167-0
   Blobe GC, 2000, NEW ENGL J MED, V342, P1350, DOI 10.1056/NEJM200005043421807
   BONEWALD LF, 1994, J CELL BIOCHEM, V55, P350, DOI 10.1002/jcb.240550312
   BRUNNER AM, 1988, MOL CELL BIOL, V8, P2229, DOI 10.1128/MCB.8.5.2229
   CARMELIET P, 1994, NATURE, V368, P419, DOI 10.1038/368419a0
   CHAUDHRY A, 1994, ANTICANCER RES, V14, P2085
   COLOSETTI P, 1993, FEBS LETT, V320, P140, DOI 10.1016/0014-5793(93)80079-A
   CORSON GM, 1993, GENOMICS, V17, P476, DOI 10.1006/geno.1993.1350
   Crawford SE, 1998, CELL, V93, P1159, DOI 10.1016/S0092-8674(00)81460-9
   Cui W, 1996, CELL, V86, P531, DOI 10.1016/S0092-8674(00)80127-0
   DALLAS SL, 1994, J BIOL CHEM, V269, P6815
   DALLAS SL, 1995, J CELL BIOL, V131, P539, DOI 10.1083/jcb.131.2.539
   DAMSTRUP L, 1993, BRIT J CANCER, V67, P1015, DOI 10.1038/bjc.1993.186
   DELARCO JE, 1978, P NATL ACAD SCI USA, V75, P4001
   DENNIS PA, 1991, P NATL ACAD SCI USA, V88, P580, DOI 10.1073/pnas.88.2.580
   DIETZ HC, 1993, SCIENCE, V259, P680, DOI 10.1126/science.8430317
   EKLOV S, 1993, CANCER RES, V53, P3193
   Fang JM, 1997, BBA-GENE STRUCT EXPR, V1354, P219, DOI 10.1016/S0167-4781(97)00104-8
   FLAUMENHAFT R, 1993, J CELL BIOL, V120, P995, DOI 10.1083/jcb.120.4.995
   FULOP C, 1993, J BIOL CHEM, V268, P17377
   GIBSON MA, 1995, MOL CELL BIOL, V15, P6932
   Giltay R, 1997, FEBS LETT, V411, P164, DOI 10.1016/S0014-5793(97)00685-6
   Gleizes PE, 1996, J BIOL CHEM, V271, P29891, DOI 10.1074/jbc.271.47.29891
   GLICK AB, 1993, P NATL ACAD SCI USA, V90, P6076, DOI 10.1073/pnas.90.13.6076
   Gohongi T, 1999, NAT MED, V5, P1203, DOI 10.1038/13524
   Gong WR, 1998, GASTROENTEROLOGY, V114, P352, DOI 10.1016/S0016-5085(98)70488-3
   Grady WM, 1999, CANCER RES, V59, P320
   GRAINGER DJ, 1995, NAT MED, V1, P74, DOI 10.1038/nm0195-74
   GRAINGER DJ, 1994, BIOCHEM J, V299, P227, DOI 10.1042/bj2990227
   GRAINGER DJ, 1994, NATURE, V370, P460, DOI 10.1038/370460a0
   GRAINGER DJ, 1995, NAT MED, V1, P1067, DOI 10.1038/nm1095-1067
   GRAINGER DJ, 1995, BIOL REV, V70, P571, DOI 10.1111/j.1469-185X.1995.tb01652.x
   GRAINGER DJ, 1993, SCIENCE, V260, P1655, DOI 10.1126/science.8503012
   Grainger DJ, 2000, CYTOKINE GROWTH F R, V11, P133, DOI 10.1016/S1359-6101(99)00037-4
   HENRIKSEN R, 1995, LAB INVEST, V73, P213
   Hojo M, 1999, NATURE, V397, P530, DOI 10.1038/17401
   Hori Y, 1998, KIDNEY INT, V53, P1616, DOI 10.1046/j.1523-1755.1998.00908.x
   Hyytiäinen M, 1998, J BIOL CHEM, V273, P20669, DOI 10.1074/jbc.273.32.20669
   IGNOTZ RA, 1986, J BIOL CHEM, V261, P4337
   INAGAKI M, 1993, P NATL ACAD SCI USA, V90, P5359, DOI 10.1073/pnas.90.11.5359
   JIRTLE RL, 1993, CANCER RES, V53, P3849
   KANZAKI T, 1995, ARTERIOSCL THROM VAS, V15, P1951, DOI 10.1161/01.ATV.15.11.1951
   KANZAKI T, 1990, CELL, V61, P1051, DOI 10.1016/0092-8674(90)90069-Q
   Karonen T, 1997, BRIT J DERMATOL, V137, P51, DOI 10.1111/j.1365-2133.1997.tb03700.x
   KIMCHI A, 1988, SCIENCE, V240, P196, DOI 10.1126/science.2895499
   KIRSCHENLOHR HL, 1995, CARDIOVASC RES, V29, P848, DOI 10.1016/S0008-6363(96)88622-6
   KIRSCHENLOHR HL, 1993, AM J PHYSIOL, V265, pC571, DOI 10.1152/ajpcell.1993.265.2.C571
   KOJIMA S, 1993, J CELL BIOL, V121, P439, DOI 10.1083/jcb.121.2.439
   KOLI K, 1995, CANCER RES, V55, P1540
   Koski C, 1999, J BIOL CHEM, V274, P32619, DOI 10.1074/jbc.274.46.32619
   KOVACINA KS, 1989, BIOCHEM BIOPH RES CO, V160, P393, DOI 10.1016/0006-291X(89)91669-0
   LI X, 1995, MAMM GENOME, V6, P42, DOI 10.1007/BF00350892
   Liu WG, 1996, HUM MOL GENET, V5, P1581, DOI 10.1093/hmg/5.10.1581
   Liu WG, 1997, NAT GENET, V16, P328, DOI 10.1038/ng0897-328
   MAEDA J, 1993, CLIN EXP IMMUNOL, V92, P32
   MAJESKY MW, 1991, J CLIN INVEST, V88, P904, DOI 10.1172/JCI115393
   MASSAGUE J, 1990, ANNU REV CELL BIOL, V6, P597, DOI 10.1146/annurev.cb.06.110190.003121
   Mathews KR, 1997, AM J HUM GENET, V61, pA44
   MCDONALD CC, 1991, BRIT MED J, V303, P435, DOI 10.1136/bmj.303.6800.435
   METCALFE JC, 1995, BIOCHEM SOC T, V23, P403, DOI 10.1042/bst0230403
   MIYAZONO K, 1989, NATURE, V338, P158, DOI 10.1038/338158a0
   MIYAZONO K, 1992, J BIOL CHEM, V267, P5668
   MIYAZONO K, 1991, EMBO J, V10, P1091, DOI 10.1002/j.1460-2075.1991.tb08049.x
   MIYAZONO K, 1988, J BIOL CHEM, V263, P6407
   MIZOI T, 1993, CANCER RES, V53, P183
   MOREN A, 1994, J BIOL CHEM, V269, P32469
   Munger JS, 1997, KIDNEY INT, V51, P1376, DOI 10.1038/ki.1997.188
   NABEL EG, 1993, P NATL ACAD SCI USA, V90, P10759, DOI 10.1073/pnas.90.22.10759
   Nakajima Y, 1997, J CELL BIOL, V136, P193, DOI 10.1083/jcb.136.1.193
   Nakayama M, 1997, NEPHRON, V76, P82, DOI 10.1159/000190145
   Nishio E, 1997, BIOCHEM BIOPH RES CO, V232, P1, DOI 10.1006/bbrc.1997.6213
   NUNES I, 1995, J IMMUNOL, V155, P1450
   Nunes I, 1997, J CELL BIOL, V136, P1151, DOI 10.1083/jcb.136.5.1151
   OKADA F, 1989, J BIOCHEM, V106, P304, DOI 10.1093/oxfordjournals.jbchem.a122849
   Öklü R, 1998, FEBS LETT, V425, P281, DOI 10.1016/S0014-5793(98)00257-9
   Öklü R, 1998, FEBS LETT, V435, P143, DOI 10.1016/S0014-5793(98)01054-0
   Olofsson A, 1995, J BIOL CHEM, V270, P31294, DOI 10.1074/jbc.270.52.31294
   OLOFSSON A, 1992, J BIOL CHEM, V267, P19482
   PARK KC, 1994, P NATL ACAD SCI USA, V91, P8772, DOI 10.1073/pnas.91.19.8772
   Parsons-Wingerter P, 2000, MICROVASC RES, V59, P221, DOI 10.1006/mvre.1999.2213
   Poltorak Z, 1997, J BIOL CHEM, V272, P7151, DOI 10.1074/jbc.272.11.7151
   PURCHIO AF, 1988, J BIOL CHEM, V263, P14211
   Raghunath M, 1998, J INVEST DERMATOL, V111, P559, DOI 10.1046/j.1523-1747.1998.00339.x
   REBAY I, 1991, CELL, V67, P687, DOI 10.1016/0092-8674(91)90064-6
   Reckless J, 1997, CIRCULATION, V95, P1542
   Reinhardt DP, 2000, J BIOL CHEM, V275, P12339, DOI 10.1074/jbc.275.16.12339
   Reinhardt DP, 1997, J BIOL CHEM, V272, P7368, DOI 10.1074/jbc.272.11.7368
   ROBERTS AB, 1980, P NATL ACAD SCI-BIOL, V77, P3494, DOI 10.1073/pnas.77.6.3494
   ROBERTS DJ, 1986, GRASS FORAGE SCI, V41, P71, DOI 10.1111/j.1365-2494.1986.tb01794.x
   ROSE JR, 1993, FASEB J, V7, pA1208, DOI 10.1096/fasebj.7.13.8405806
   Saharinen J, 1996, EMBO J, V15, P245, DOI 10.1002/j.1460-2075.1996.tb00355.x
   Saharinen J, 1998, J BIOL CHEM, V273, P18459, DOI 10.1074/jbc.273.29.18459
   SAKAI LY, 1986, J CELL BIOL, V103, P2499, DOI 10.1083/jcb.103.6.2499
   SATO Y, 1989, J CELL BIOL, V109, P309, DOI 10.1083/jcb.109.1.309
   SATO Y, 1993, J CELL BIOL, V123, P1249, DOI 10.1083/jcb.123.5.1249
   Schulick AH, 1998, P NATL ACAD SCI USA, V95, P6983, DOI 10.1073/pnas.95.12.6983
   Shipley JM, 2000, MOL CELL BIOL, V20, P4879, DOI 10.1128/MCB.20.13.4879-4887.2000
   SHULL MM, 1992, NATURE, V359, P693, DOI 10.1038/359693a0
   Siese A, 1999, SCAND J IMMUNOL, V49, P139
   SMAS CM, 1994, BIOCHEMISTRY-US, V33, P9257, DOI 10.1021/bi00197a029
   Smith JD, 1999, CIRC RES, V84, P1212, DOI 10.1161/01.RES.84.10.1212
   STENMAN G, 1994, CYTOGENET CELL GENET, V66, P117, DOI 10.1159/000133680
   SUN LZ, 1994, J BIOL CHEM, V269, P26449
   Taipale J, 1996, J HISTOCHEM CYTOCHEM, V44, P875, DOI 10.1177/44.8.8756760
   TAIPALE J, 1994, J CELL BIOL, V124, P171, DOI 10.1083/jcb.124.1.171
   TAKETAZU F, 1994, LAB INVEST, V70, P620
   TAMAKI K, 1995, LAB INVEST, V73, P81
   Tamaki K, 1996, J AM SOC NEPHROL, V7, P2578
   TSUJI T, 1990, P NATL ACAD SCI USA, V87, P8835, DOI 10.1073/pnas.87.22.8835
   VANLAETHEM JL, 1995, GASTROENTEROLOGY, V108, P1873, DOI 10.1016/0016-5085(95)90152-3
   VanLaethem JL, 1996, DIGEST DIS SCI, V41, P1741, DOI 10.1007/BF02088739
   VanLaethem JL, 1997, PANCREAS, V15, P41, DOI 10.1097/00006676-199707000-00006
   Verderio E, 1999, J HISTOCHEM CYTOCHEM, V47, P1417, DOI 10.1177/002215549904701108
   Villanueva A, 1998, ONCOGENE, V17, P1969, DOI 10.1038/sj.onc.1202118
   Wada T, 1997, KIDNEY INT, pS182
   WAHL SM, 1987, P NATL ACAD SCI USA, V84, P5788, DOI 10.1073/pnas.84.16.5788
   WAKEFIELD LM, 1988, J BIOL CHEM, V263, P7646
   WALTER J, 1993, NEPHROL DIAL TRANSPL, V8, P1428
   Wang SN, 1997, CANCER RES, V57, P2543
   Williams JK, 1997, ARTERIOSCL THROM VAS, V17, P403, DOI 10.1161/01.ATV.17.2.403
   WOLF YG, 1994, J CLIN INVEST, V93, P1172, DOI 10.1172/JCI117070
   WRANN M, 1987, EMBO J, V6, P1633, DOI 10.1002/j.1460-2075.1987.tb02411.x
   YAMAZAKI M, 1994, AM J PATHOL, V144, P221
   Yang YB, 1997, BIOCHEMISTRY-US, V36, P11923, DOI 10.1021/bi9710479
   Yin WS, 1998, BIOCHEM BIOPH RES CO, V245, P454, DOI 10.1006/bbrc.1998.8456
   YIN WS, 1995, J BIOL CHEM, V270, P10147, DOI 10.1074/jbc.270.17.10147
   Yin WS, 1998, BBA-PROTEIN STRUCT M, V1383, P340, DOI 10.1016/S0167-4838(98)00003-X
   Yuan XM, 1997, EMBO J, V16, P6659, DOI 10.1093/emboj/16.22.6659
   ZHANG H, 1994, J CELL BIOL, V124, P855, DOI 10.1083/jcb.124.5.855
NR 131
TC 156
Z9 196
U1 0
U2 8
PU PORTLAND PRESS LTD
PI LONDON
PA CHARLES DARWIN HOUSE, 12 ROGER STREET, LONDON WC1N 2JU, ENGLAND
SN 0264-6021
EI 1470-8728
J9 BIOCHEM J
JI Biochem. J.
PD DEC 15
PY 2000
VL 352
BP 601
EP 610
DI 10.1042/0264-6021:3520601
PN 3
PG 10
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 388JQ
UT WOS:000166177700001
PM 11104663
OA Green Published
DA 2025-04-10
ER

PT J
AU Bassez, G
   Camand, OJA
   Cacheux, V
   Kobetz, A
   Moal, FDL
   Marchant, D
   Catala, M
   Abitbol, M
   Goossens, M
AF Bassez, G
   Camand, OJA
   Cacheux, V
   Kobetz, A
   Moal, FDL
   Marchant, D
   Catala, M
   Abitbol, M
   Goossens, M
TI Pleiotropic and diverse expression of ZFHX1B gene transcripts
   during mouse and human development supports the various clinical
   manifestations of the "Mowat-Wilson" syndrome
SO NEUROBIOLOGY OF DISEASE
LA English
DT Article
DE cardiovascular system; human and mouse development; mRNA species;
   neurogenesis; Smad-interacting protein-1 (SIP1); TGF-beta; signaling;
   ZFHX1B
ID SMAD-INTERACTING PROTEIN-1; MENTAL RETARDATION SYNDROME; TGF-BETA
   SUPERFAMILY; HIRSCHSPRUNG-DISEASE; KNOCKOUT MICE; MUTATIONS; SIP1;
   DEFECTS; DIFFERENTIATION; DELINEATION
AB ZFHX1B encodes Smad-interacting protein 1, a transcriptional corepressor involved in the transforming growth factors beta (TGFbeta) signaling pathway. ZFHX1B mutations cause a complex developmental phenotype characterized by severe mental retardation (MR) and multiple congenital defects. We compared the distribution of ZFHX1B transcripts during mouse and human embryogenesis as well as in adult mice and humans. This showed that this gene is strongly transcribed at an early stage in the developing peripheral and central nervous systems of both mice and humans, in all neuronal regions of the brains of 25-week human fetuses and adult mice, and at varying levels in numerous nonneural tissues. Northern blot analysis suggested that ZFHX1B undergoes tissue-specific alternative splicing in both species. These results strongly suggest that ZFHX1B determines the transcriptional levels of target genes in various tissues through the combinatorial interactions of its isoforms with different Smad proteins. Thus, as well as causing neural defects, ZFHX1B mutations may also cause other malformations. (C) 2004 Elsevier Inc. All rights reserved.
C1 Hop Henri Mondor, AP HP, INSERM, U468, F-94010 Creteil, France.
   Hop Henri Mondor, AP HP, Serv Biochim & Genet, F-94010 Creteil, France.
   Fac Med Necker Enfants Malad, CERTO, Paris, France.
   Univ Paris 06, Fac Pitie Salpetriere, Lab Histol & Embryol, Paris, France.
   Univ Paris 06, Fac Pitie Salpetriere, CNRS, UMR 7000, Paris, France.
C3 Institut National de la Sante et de la Recherche Medicale (Inserm);
   Universite Paris-Est-Creteil-Val-de-Marne (UPEC); Assistance Publique
   Hopitaux Paris (APHP); Hopital Universitaire Henri-Mondor - APHP;
   Assistance Publique Hopitaux Paris (APHP); Universite
   Paris-Est-Creteil-Val-de-Marne (UPEC); Hopital Universitaire
   Henri-Mondor - APHP; Universite Paris Cite; Sorbonne Universite; Centre
   National de la Recherche Scientifique (CNRS); Sorbonne Universite
RP Hop Henri Mondor, AP HP, INSERM, U468, F-94010 Creteil, France.
EM michel.goossens@im3.inserm.fr
RI Bassez, Guillaume/AAD-3033-2022
OI Bassez, Guillaume/0000-0002-2044-1052; Marchant,
   Dominique/0000-0003-4841-7254; Catala, Martin/0000-0003-1554-9007
CR ABITBOL M, 1993, NAT GENET, V4, P147, DOI 10.1038/ng0693-147
   Amiel J, 2001, AM J HUM GENET, V69, P1370, DOI 10.1086/324342
   Barlow AJ, 1997, DEVELOPMENT, V124, P391
   Bernasconi A, 2001, ANN NEUROL, V49, P770, DOI 10.1002/ana.1013
   Cacheux V, 2001, HUM MOL GENET, V10, P1503, DOI 10.1093/hmg/10.14.1503
   Chang H, 1999, DEVELOPMENT, V126, P1631
   Chen FF, 2002, BIOCHEM J, V364, P571, DOI 10.1042/BJ20011703
   Comijn J, 2001, MOL CELL, V7, P1267, DOI 10.1016/S1097-2765(01)00260-X
   Eisaki A, 2000, BIOCHEM BIOPH RES CO, V271, P151, DOI 10.1006/bbrc.2000.2545
   Espinosa-Parrilla Y, 2002, MECH DEVELOP, V114, P187, DOI 10.1016/S0925-4773(02)00062-X
   Francis-West P, 1998, MECH DEVELOP, V75, P3, DOI 10.1016/S0925-4773(98)00082-3
   Furuta Y, 1997, DEVELOPMENT, V124, P2203
   Garavelli L, 2003, AM J MED GENET A, V116A, P385, DOI 10.1002/ajmg.a.10855
   Hager-Theodorides AL, 2002, J IMMUNOL, V169, P5496, DOI 10.4049/jimmunol.169.10.5496
   KINGSLEY DM, 1992, CELL, V71, P399, DOI 10.1016/0092-8674(92)90510-J
   Liem KF, 2000, DEVELOPMENT, V127, P4855
   Mowat DR, 2003, J MED GENET, V40, P305, DOI 10.1136/jmg.40.5.305
   Mowat DR, 1998, J MED GENET, V35, P617, DOI 10.1136/jmg.35.8.617
   O'Rahilly R., 1987, DEV STAGES HUMAN EMB, P306
   Rosivatz E, 2002, AM J PATHOL, V161, P1881, DOI 10.1016/S0002-9440(10)64464-1
   Sanford LP, 1997, DEVELOPMENT, V124, P2659
   Shah NM, 1996, CELL, V85, P331, DOI 10.1016/S0092-8674(00)81112-5
   Shah SB, 1997, DEVELOPMENT, V124, P5127
   Tylzanowski P, 2001, J BIOL CHEM, V276, P40001, DOI 10.1074/jbc.M104112200
   Van de Putte T, 2003, AM J HUM GENET, V72, P465, DOI 10.1086/346092
   van Grunsven LA, 2000, MECH DEVELOP, V94, P189, DOI 10.1016/S0925-4773(00)00318-X
   Verschueren K, 1999, J BIOL CHEM, V274, P20489, DOI 10.1074/jbc.274.29.20489
   Wakamatsu N, 2001, NAT GENET, V27, P369, DOI 10.1038/86860
   Waldrip WR, 1998, CELL, V92, P797, DOI 10.1016/S0092-8674(00)81407-5
   Wilson M, 2003, AM J MED GENET A, V119A, P257, DOI 10.1002/ajmg.a.20053
   WISNIEWSKI KE, 1991, AM J MED GENET, V38, P476, DOI 10.1002/ajmg.1320380267
   Yamada K, 2001, AM J HUM GENET, V69, P1178, DOI 10.1086/324343
   Yoneda M, 2002, NEUROLOGY, V59, P1637, DOI 10.1212/01.WNL.0000034842.78350.4E
   Zweier C, 2002, AM J MED GENET, V108, P177, DOI 10.1002/ajmg.10226
NR 34
TC 43
Z9 47
U1 0
U2 0
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0969-9961
EI 1095-953X
J9 NEUROBIOL DIS
JI Neurobiol. Dis.
PD MAR
PY 2004
VL 15
IS 2
BP 240
EP 250
DI 10.1016/j.nbd.2003.10.004
PG 11
WC Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA 802OW
UT WOS:000220173800009
PM 15006694
DA 2025-04-10
ER

PT J
AU Thayer, SA
   Usachev, YM
   Pottorf, WJ
AF Thayer, SA
   Usachev, YM
   Pottorf, WJ
TI Modulating Ca<SUP>2+</SUP> clearance from neurons
SO FRONTIERS IN BIOSCIENCE-LANDMARK
LA English
DT Review
DE intracellular Ca2+ concentration; neuron; plasma membrane Ca2+ ATPase;
   PMCA; sarcoplasmic and endoplasmic reticulum Ca2+ ATPase; SERCA;
   mitochondrion; Na+/Ca2+ exchange; NCX; pharmacology; phosphorylation;
   brain; alternative splicing; Ca2+ signaling; review
ID MITOCHONDRIAL PERMEABILITY TRANSITION; PROTEIN-KINASE-C; SODIUM-CALCIUM
   EXCHANGE; PLASMA-MEMBRANE CA2+-ATPASE; CYCLIC ADP-RIBOSE; CARDIAC
   SARCOPLASMIC-RETICULUM; POST-SPIKE HYPERPOLARIZATION; BULLFROG
   SYMPATHETIC NEURONS; CALMODULIN-BINDING DOMAIN; ADRENAL CHROMAFFIN CELLS
AB Neurons are exquisitely sensitive to the duration, amplitude and localization of transient increases in intracellular Ca2+ concentration ([Ca2+](i)). Modulation of Ca2+ uptake into the mitochondrion and endoplasmic reticulum, and efflux via he plasma membrane Ca2+ pump and Na+/Ca2+ exchange profoundly affect the shape of [Ca2+](i) signals. Ca2+ clearance mechanisms are modulated by other signaling pathways, are sensitive to metabolic state and have a memory of the recent history of cell activation. We present here examples of pharmacologic and endogenous regulation of Ca2+ sequestration and efflux in neurons. Ca2+ clearance mechanisms differentially shape [Ca2+](i) signals based on heir affinity, capacity and location; their modulation alters specific neuronal functions. The increasingly apparent diversity of the molecular entities that make up the [Ca2+](i) regulatory system reveals new sites for modulation. Specialized Ca2+ clearance mechanisms participate in unique cellular functions and thus, are important targets for pharmacological and physiological regulation of the neuron.
C1 Univ Minnesota, Sch Med, Dept Pharmacol, Minneapolis, MN 55455 USA.
C3 University of Minnesota System; University of Minnesota Twin Cities
RP Univ Minnesota, Sch Med, Dept Pharmacol, 6-120 Jackson Hall,321 Church St SE, Minneapolis, MN 55455 USA.
EM thayer@med.umn.edu
OI Usachev, Yuriy/0000-0002-6948-4627
CR ANDREEVA N, 1991, BRAIN RES, V548, P322, DOI 10.1016/0006-8993(91)91141-M
   Ankarcrona M, 1996, FEBS LETT, V394, P321, DOI 10.1016/0014-5793(96)00959-3
   Antonsson B, 1997, SCIENCE, V277, P370, DOI 10.1126/science.277.5324.370
   Arnaudeau S, 2001, J BIOL CHEM, V276, P29430, DOI 10.1074/jbc.M103274200
   ASANO S, 1995, J NEUROCHEM, V64, P2437
   Augustine GJ, 2001, CURR OPIN NEUROBIOL, V11, P320, DOI 10.1016/S0959-4388(00)00214-2
   Baba-Aissa F, 1998, MOL CHEM NEUROPATHOL, V33, P199, DOI 10.1007/BF02815182
   Babcock DF, 1997, J CELL BIOL, V136, P833, DOI 10.1083/jcb.136.4.833
   BAKER PF, 1984, CURR TOP MEMBR TRANS, V22, P195
   Baron KT, 1997, EUR J PHARMACOL, V340, P295, DOI 10.1016/S0014-2999(97)01433-7
   BASSANI RA, 1995, PFLUG ARCH EUR J PHY, V430, P573, DOI 10.1007/BF00373894
   BAUDRY M, 1994, NEUROSCI LETT, V171, P151, DOI 10.1016/0304-3940(94)90627-0
   Beard NA, 2002, BIOPHYS J, V82, P310, DOI 10.1016/S0006-3495(02)75396-4
   BENHAM CD, 1992, J PHYSIOL-LONDON, V455, P567, DOI 10.1113/jphysiol.1992.sp019316
   Bernardi P, 1999, PHYSIOL REV, V79, P1127, DOI 10.1152/physrev.1999.79.4.1127
   Berridge MJ, 2000, NAT REV MOL CELL BIO, V1, P11, DOI 10.1038/35036035
   Berridge MJ, 1998, NEURON, V21, P13, DOI 10.1016/S0896-6273(00)80510-3
   BEZPROZVANNY I, 1991, NATURE, V351, P751, DOI 10.1038/351751a0
   BIDEN TJ, 1986, J BIOL CHEM, V261, P7223
   Blaustein MP, 1999, PHYSIOL REV, V79, P763, DOI 10.1152/physrev.1999.79.3.763
   Blaustein MP, 1996, ANN NY ACAD SCI, V779, P300, DOI 10.1111/j.1749-6632.1996.tb44803.x
   Bouron A, 1996, NEURON, V17, P969, DOI 10.1016/S0896-6273(00)80227-5
   Bouron A, 2000, FEBS LETT, V470, P269, DOI 10.1016/S0014-5793(00)01340-5
   Brini M, 2000, EMBO J, V19, P4926, DOI 10.1093/emboj/19.18.4926
   Brocard JB, 2001, J PHYSIOL-LONDON, V531, P793, DOI 10.1111/j.1469-7793.2001.0793h.x
   Brustovetsky N, 2000, J NEUROSCI, V20, P8229, DOI 10.1523/JNEUROSCI.20-22-08229.2000
   Budd SL, 1996, J NEUROCHEM, V66, P403, DOI 10.1046/j.1471-4159.1996.66010403.x
   Budd SL, 2000, P NATL ACAD SCI USA, V97, P6161, DOI 10.1073/pnas.100121097
   Buntinas L, 2001, BBA-BIOENERGETICS, V1504, P248, DOI 10.1016/S0005-2728(00)00254-1
   BURK SE, 1989, J BIOL CHEM, V264, P18561
   Burrone J, 2002, NEURON, V33, P101, DOI 10.1016/S0896-6273(01)00565-7
   Calabresi P, 1999, STROKE, V30, P1687, DOI 10.1161/01.STR.30.8.1687
   CARAFOLI E, 1994, FASEB J, V8, P993, DOI 10.1096/fasebj.8.13.7926378
   Caride AJ, 1999, J BIOL CHEM, V274, P35227, DOI 10.1074/jbc.274.49.35227
   Caride AJ, 2001, J BIOL CHEM, V276, P39797, DOI 10.1074/jbc.M104380200
   Caride AJ, 2001, CELL CALCIUM, V30, P49, DOI 10.1054/ceca.2001.0212
   CARONI P, 1981, J BIOL CHEM, V256, P9371
   Carter AG, 2002, J NEUROSCI, V22, P21, DOI 10.1523/JNEUROSCI.22-01-00021.2002
   Castilho RF, 1999, J NEUROCHEM, V72, P1394, DOI 10.1046/j.1471-4159.1999.721394.x
   CHARD PS, 1993, J PHYSIOL-LONDON, V472, P341, DOI 10.1113/jphysiol.1993.sp019950
   Chaudhary J, 2001, AM J PHYSIOL-CELL PH, V280, pC1027, DOI 10.1152/ajpcell.2001.280.4.C1027
   CHEEK TR, 1991, BIOCHEM J, V275, P697, DOI 10.1042/bj2750697
   Chin D, 2000, TRENDS CELL BIOL, V10, P322, DOI 10.1016/S0962-8924(00)01800-6
   COLL RJ, 1992, J BIOL CHEM, V267, P21584
   Collins RO, 2001, CELL CALCIUM, V30, P41, DOI 10.1054/ceca.2001.0209
   Colvin RA, 1998, NEUROREPORT, V9, P3091, DOI 10.1097/00001756-199809140-00032
   Colyer J, 1998, ANN NY ACAD SCI, V853, P79, DOI 10.1111/j.1749-6632.1998.tb08258.x
   Connor JA, 1999, CAN J PHYSIOL PHARM, V77, P722, DOI 10.1139/cjpp-77-9-722
   Cordoba-Rodriguez R, 1999, P NATL ACAD SCI USA, V96, P7650, DOI 10.1073/pnas.96.14.7650
   CROMPTON M, 1977, EUR J BIOCHEM, V79, P549, DOI 10.1111/j.1432-1033.1977.tb11839.x
   CROMPTON M, 1976, EUR J BIOCHEM, V69, P429, DOI 10.1111/j.1432-1033.1976.tb10927.x
   Csordás G, 2001, CELL CALCIUM, V29, P249, DOI 10.1054/ceca.2000.0191
   CURRIE KPM, 1992, MOL BIOL CELL, V3, P1415, DOI 10.1091/mbc.3.12.1415
   David G, 2000, J NEUROSCI, V20, P7290
   DeFelipe J, 1997, J CHEM NEUROANAT, V14, P1, DOI 10.1016/S0891-0618(97)10013-8
   DIPOLO R, 1979, J GEN PHYSIOL, V73, P91, DOI 10.1085/jgp.73.1.91
   DiPolo R, 1997, FEBS LETT, V401, P6, DOI 10.1016/S0014-5793(96)01416-0
   DiPolo R, 1999, BBA-REV BIOMEMBRANES, V1422, P57, DOI 10.1016/S0005-2736(99)00002-4
   DIXON DA, 1989, J BIOL CHEM, V264, P13612
   Donato R, 2001, INT J BIOCHEM CELL B, V33, P637, DOI 10.1016/S1357-2725(01)00046-2
   Dou DX, 1996, BRAIN RES, V723, P8, DOI 10.1016/0006-8993(96)00167-9
   Doutheil J, 1999, CELL CALCIUM, V25, P419, DOI 10.1054/ceca.1999.0042
   Du GG, 2001, P NATL ACAD SCI USA, V98, P13625, DOI 10.1073/pnas.241516898
   DUCHEN MR, 1992, BIOCHEM J, V283, P41, DOI 10.1042/bj2830041
   East JM, 2000, MOL MEMBR BIOL, V17, P189, DOI 10.1080/09687680010009646
   Ellgaard L, 2001, CURR OPIN CELL BIOL, V13, P431, DOI 10.1016/S0955-0674(00)00233-7
   Empson RM, 1997, J BIOL CHEM, V272, P20967, DOI 10.1074/jbc.272.34.20967
   Emptage NJ, 2001, NEURON, V29, P197, DOI 10.1016/S0896-6273(01)00190-8
   Enyedi A, 1997, J BIOL CHEM, V272, P27525, DOI 10.1074/jbc.272.44.27525
   Enyedi A, 1996, J BIOL CHEM, V271, P32461, DOI 10.1074/jbc.271.50.32461
   ENYEDI A, 1994, J BIOL CHEM, V269, P41
   Favre CJ, 1996, J BIOL CHEM, V271, P14925, DOI 10.1074/jbc.271.25.14925
   Fernández-Chacón R, 2001, NATURE, V410, P41, DOI 10.1038/35065004
   Fierro L, 1998, J PHYSIOL-LONDON, V510, P499, DOI 10.1111/j.1469-7793.1998.499bk.x
   FINCH EA, 1991, SCIENCE, V252, P443, DOI 10.1126/science.2017683
   Finch EA, 1998, NATURE, V396, P753, DOI 10.1038/25541
   Fomina AF, 1999, J NEUROSCI, V19, P3711
   Fontaine E, 1998, J BIOL CHEM, V273, P25734, DOI 10.1074/jbc.273.40.25734
   Fortea MI, 2001, J BIOL CHEM, V276, P37266, DOI 10.1074/jbc.M103949200
   FOSKETT JK, 1992, AM J PHYSIOL, V262, pC656, DOI 10.1152/ajpcell.1992.262.3.C656
   Frank K, 2000, ANN MED, V32, P572, DOI 10.3109/07853890008998837
   FRIEL DD, 1992, NEURON, V8, P1109, DOI 10.1016/0896-6273(92)90132-W
   FRIEL DD, 1992, J PHYSIOL-LONDON, V450, P217, DOI 10.1113/jphysiol.1992.sp019125
   FRIEL DD, 1994, J NEUROSCI, V14, P4007
   Gafni J, 1997, NEURON, V19, P723, DOI 10.1016/S0896-6273(00)80384-0
   Garaschuk O, 1997, J PHYSIOL-LONDON, V502, P13, DOI 10.1111/j.1469-7793.1997.013bl.x
   GARCIA ML, 1988, BIOCHEMISTRY-US, V27, P2410, DOI 10.1021/bi00407a024
   GARCIA ML, 1990, J BIOL CHEM, V265, P3763
   GATTO C, 1995, BIOCHEM, P905
   GHOSH A, 1995, SCIENCE, V268, P239, DOI 10.1126/science.7716515
   Gilabert JA, 2000, EMBO J, V19, P6401, DOI 10.1093/emboj/19.23.6401
   Gilad GM, 1998, INT J DEV NEUROSCI, V16, P271, DOI 10.1016/S0736-5748(98)00033-1
   GLEASON E, 1994, NEURON, V13, P1109, DOI 10.1016/0896-6273(94)90049-3
   GLEASON E, 1995, J NEUROSCI, V15, P3612
   GOMEZ TM, 1995, NEURON, V14, P1233, DOI 10.1016/0896-6273(95)90270-8
   Green AK, 1997, CELL CALCIUM, V22, P99, DOI 10.1016/S0143-4160(97)90110-X
   GRIFFITHS EJ, 1991, BIOCHEM J, V274, P611, DOI 10.1042/bj2740611
   Gunter TE, 2000, CELL CALCIUM, V28, P285, DOI 10.1054/ceca.2000.0168
   GUNTESKIHAMBLIN AM, 1988, J BIOL CHEM, V263, P15032
   Györke I, 1998, BIOPHYS J, V75, P2801, DOI 10.1016/S0006-3495(98)77723-9
   Haeseleer F, 2002, BIOCHEM BIOPH RES CO, V290, P615, DOI 10.1006/bbrc.2001.6228
   Halestrap AP, 1997, J BIOL CHEM, V272, P3346, DOI 10.1074/jbc.272.6.3346
   He SW, 1998, J NEUROSCI, V18, P4833
   He ZP, 2000, AM J PHYSIOL-CELL PH, V278, pC661, DOI 10.1152/ajpcell.2000.278.4.C661
   Heizmann Claus W., 1993, Acta Neurobiologiae Experimentalis (Warsaw), V53, P15
   Heizmann CW, 1998, BIOMETALS, V11, P383, DOI 10.1023/A:1009212521172
   Herlitze S, 2001, P NATL ACAD SCI USA, V98, P4699, DOI 10.1073/pnas.051628998
   Herrington J, 1996, NEURON, V16, P219, DOI 10.1016/S0896-6273(00)80038-0
   Herscher CJ, 1996, BIOCHEMISTRY-US, V35, P14917, DOI 10.1021/bi961879r
   Hewitt KE, 2001, BRAIN RES, V898, P281, DOI 10.1016/S0006-8993(01)02195-3
   Hilgemann DW, 1996, SCIENCE, V273, P956, DOI 10.1126/science.273.5277.956
   Hillman DE, 1996, NEUROSCIENCE, V72, P315, DOI 10.1016/0306-4522(95)00518-8
   HOFMANN F, 1994, J BIOL CHEM, V269, P24298
   Hongpaisan J, 2001, J GEN PHYSIOL, V118, P101, DOI 10.1085/jgp.118.1.101
   Hoyt KR, 1998, MOL PHARMACOL, V53, P742, DOI 10.1124/mol.53.4.742
   ICHAS F, 1994, FEBS LETT, V348, P211, DOI 10.1016/0014-5793(94)00615-6
   Ichas F, 1997, CELL, V89, P1145, DOI 10.1016/S0092-8674(00)80301-3
   Ichas F, 1998, BBA-BIOENERGETICS, V1366, P33, DOI 10.1016/S0005-2728(98)00119-4
   Ishida H, 2001, CIRC RES, V89, P856, DOI 10.1161/hh2201.100341
   Iwamoto T, 1996, J BIOL CHEM, V271, P22391, DOI 10.1074/jbc.271.37.22391
   Iwamoto T, 1998, BIOCHEMISTRY-US, V37, P17230, DOI 10.1021/bi981521q
   JAMES PH, 1989, BIOCHEMISTRY-US, V28, P4253, DOI 10.1021/bi00436a020
   JENSEN JR, 1987, J NEUROCHEM, V48, P765, DOI 10.1111/j.1471-4159.1987.tb05583.x
   John LM, 1998, J CELL BIOL, V142, P963, DOI 10.1083/jcb.142.4.963
   Jonas EA, 1999, SCIENCE, V286, P1347, DOI 10.1126/science.286.5443.1347
   JOUAVILLE LS, 1995, NATURE, V377, P438, DOI 10.1038/377438a0
   Juhaszova M, 2000, EUR J NEUROSCI, V12, P839, DOI 10.1046/j.1460-9568.2000.00974.x
   Kaftan EJ, 2000, J BIOL CHEM, V275, P25465, DOI 10.1074/jbc.M000903200
   KAWASAKI H, 1995, PROTEIN PROFILE, V2, P305
   KEETON TP, 1993, J BIOL CHEM, V268, P2740
   Khaspekov L, 1999, EUR J NEUROSCI, V11, P3194, DOI 10.1046/j.1460-9568.1999.00743.x
   KIEDROWSKI L, 1994, NEURON, V12, P295, DOI 10.1016/0896-6273(94)90272-0
   Kim-Han JS, 2001, J NEUROCHEM, V79, P658, DOI 10.1046/j.1471-4159.2001.00604.x
   Kimura J, 1999, BRIT J PHARMACOL, V128, P969, DOI 10.1038/sj.bjp.0702869
   KLRAEV A, 2001, J BIOL CHEM, V276, P23161
   Kluck RM, 1997, SCIENCE, V275, P1132, DOI 10.1126/science.275.5303.1132
   KRAJEWSKI S, 1993, CANCER RES, V53, P4701
   Kristal BS, 1997, J NEUROCHEM, V69, P524
   KUBA K, 1983, PFLUG ARCH EUR J PHY, V399, P194, DOI 10.1007/BF00656714
   Lalli MJ, 2001, CIRC RES, V89, P160
   LAPIDUS RG, 1994, J BIOL CHEM, V269, P18931
   LATTANZIO FA, 1987, J BIOL CHEM, V262, P2711
   Lee HC, 1997, PHYSIOL REV, V77, P1133, DOI 10.1152/physrev.1997.77.4.1133
   LEHNINGER AL, 1974, P NATL ACAD SCI USA, V71, P1520, DOI 10.1073/pnas.71.4.1520
   Leissring MA, 2000, J CELL BIOL, V149, P793, DOI 10.1083/jcb.149.4.793
   Litsky ML, 1997, BIOCHEMISTRY-US, V36, P7071, DOI 10.1021/bi970180y
   LLINAS R, 1992, SCIENCE, V256, P677, DOI 10.1126/science.1350109
   LO TM, 1993, AM J PHYSIOL-CELL PH, V33, pC641
   Lukyanenko V, 2001, CIRC RES, V89, P614, DOI 10.1161/hh1901.098066
   Luo DL, 2000, GEN PHARMACOL-VASC S, V34, P211, DOI 10.1016/S0306-3623(00)00064-1
   LUTHER PW, 1992, J NEUROSCI, V12, P4898
   LYTTON J, 1992, J BIOL CHEM, V267, P14483
   Mahajan NP, 1998, NAT BIOTECHNOL, V16, P547, DOI 10.1038/nbt0698-547
   Majewska A, 2000, J NEUROSCI, V20, P1722
   Matlib MA, 1998, J BIOL CHEM, V273, P10223, DOI 10.1074/jbc.273.17.10223
   MATSUOKA S, 1994, J PHYSIOL-LONDON, V476, P443, DOI 10.1113/jphysiol.1994.sp020146
   MATTSON MP, 1989, FASEB J, V3, P2519, DOI 10.1096/fasebj.3.13.2572500
   Mattson MP, 2000, TRENDS NEUROSCI, V23, P222, DOI 10.1016/S0166-2236(00)01548-4
   McCleskey EW, 1999, ANNU REV PHYSIOL, V61, P835, DOI 10.1146/annurev.physiol.61.1.835
   MCCORMACK JG, 1993, BIOCHEM SOC T, V21, P793, DOI 10.1042/bst0210793
   MEYER T, 1992, SCIENCE, V256, P1199, DOI 10.1126/science.256.5060.1199
   Michalak M, 1998, BIOCHEM CELL BIOL, V76, P779, DOI 10.1139/bcb-76-5-779
   MISSIAEN L, 1992, EUR J PHARM-MOLEC PH, V227, P391, DOI 10.1016/0922-4106(92)90156-P
   Miyata M, 2000, NEURON, V28, P233, DOI 10.1016/S0896-6273(00)00099-4
   Monteith GR, 1998, J PHARMACOL TOXICOL, V40, P183, DOI 10.1016/S1056-8719(99)00004-0
   Montero M, 1997, J CELL BIOL, V139, P601, DOI 10.1083/jcb.139.3.601
   Montero M, 2000, NAT CELL BIOL, V2, P57, DOI 10.1038/35000001
   Moore KA, 1998, J NEUROPHYSIOL, V79, P688, DOI 10.1152/jn.1998.79.2.688
   MOUDY AM, 1995, P NATL ACAD SCI USA, V92, P729, DOI 10.1073/pnas.92.3.729
   MULLER CE, 1993, BIOCHEM PHARMACOL, V46, P1825, DOI 10.1016/0006-2952(93)90589-O
   Murata M, 2001, CIRC RES, V89, P891, DOI 10.1161/hh2201.100205
   Murphy AN, 1996, P NATL ACAD SCI USA, V93, P9893, DOI 10.1073/pnas.93.18.9893
   Narasimhan K, 1998, J NEUROPHYSIOL, V80, P2963, DOI 10.1152/jn.1998.80.6.2963
   Narayanan N, 1997, BASIC RES CARDIOL, V92, P25, DOI 10.1007/BF00794065
   NARAYANAN N, 1991, BIOCHIM BIOPHYS ACTA, V1070, P83, DOI 10.1016/0005-2736(91)90149-3
   Narita M, 1998, P NATL ACAD SCI USA, V95, P14681, DOI 10.1073/pnas.95.25.14681
   NEYSES L, 1985, J BIOL CHEM, V260, P283
   Nguyen HN, 2002, BRAIN RES, V924, P159, DOI 10.1016/S0006-8993(01)03229-2
   NICHOLLS D, 1982, BIOCHIM BIOPHYS ACTA, V683, P57, DOI 10.1016/0304-4173(82)90013-1
   Nicholls DG, 1999, ANN NY ACAD SCI, V893, P1, DOI 10.1111/j.1749-6632.1999.tb07813.x
   Nicholls DG, 2000, PHYSIOL REV, V80, P315, DOI 10.1152/physrev.2000.80.1.315
   NICHOLLS DG, 1978, BIOCHEM J, V176, P463, DOI 10.1042/bj1760463
   NICHOLLS DG, 1992, BIOENERGETICS, P207
   Nicotera P, 1998, CELL CALCIUM, V23, P173, DOI 10.1016/S0143-4160(98)90116-6
   ONEAL SG, 1979, BIOCHEM BIOPH RES CO, V89, P845, DOI 10.1016/0006-291X(79)91855-2
   OU WJ, 1995, J BIOL CHEM, V270, P18051, DOI 10.1074/jbc.270.30.18051
   Padua RA, 1998, AM J PHYSIOL-CELL PH, V274, pC615, DOI 10.1152/ajpcell.1998.274.3.C615
   Palmi M, 1999, BIOCHEM PHARMACOL, V58, P1123, DOI 10.1016/S0006-2952(99)00183-5
   Pan CY, 1998, BIOCHEM J, V336, P305, DOI 10.1042/bj3360305
   Pan CY, 1997, J NEUROCHEM, V69, P1085
   Parekh AB, 1997, PHYSIOL REV, V77, P901, DOI 10.1152/physrev.1997.77.4.901
   Park BJ, 2001, MOL BIOL CELL, V12, P2835, DOI 10.1091/mbc.12.9.2835
   Patel S, 1999, CELL CALCIUM, V25, P247, DOI 10.1054/ceca.1999.0021
   Peng YY, 1996, J NEUROSCI, V16, P6703
   PENG YY, 1993, NEURON, V10, P465, DOI 10.1016/0896-6273(93)90334-N
   Penniston JT, 1998, J MEMBRANE BIOL, V165, P101, DOI 10.1007/s002329900424
   PerezTerzic C, 1997, BIOESSAYS, V19, P787, DOI 10.1002/bies.950190908
   Petersen OH, 1999, TRENDS NEUROSCI, V22, P488, DOI 10.1016/S0166-2236(99)01456-3
   PETRONILLI V, 1993, J BIOL CHEM, V268, P1011
   Petronilli V, 2001, J BIOL CHEM, V276, P12030, DOI 10.1074/jbc.M010604200
   PETRONILLI V, 1994, J BIOL CHEM, V269, P16638
   Philipp S, 1998, EMBO J, V17, P4274, DOI 10.1093/emboj/17.15.4274
   Philipson KD, 2000, ANNU REV PHYSIOL, V62, P111, DOI 10.1146/annurev.physiol.62.1.111
   Pilitsis JG, 2001, BRAIN RES, V916, P192, DOI 10.1016/S0006-8993(01)02896-7
   Posner A S, 1978, Ann N Y Acad Sci, V307, P248, DOI 10.1111/j.1749-6632.1978.tb41955.x
   Pottorf WJ, 2000, J AUTON PHARMACOL, V20, P281, DOI 10.1046/j.1365-2680.2000.00194.x
   POTTORF WJ, 2001, SOC NEUR ABST, V27
   POZZAN T, 1994, PHYSIOL REV, V74, P595, DOI 10.1152/physrev.1994.74.3.595
   Pozzan T, 2000, EUR J BIOCHEM, V267, P5269, DOI 10.1046/j.1432-1327.2000.01567.x
   PREHN JHM, 1994, P NATL ACAD SCI USA, V91, P12599, DOI 10.1073/pnas.91.26.12599
   Putcha GV, 1999, J NEUROSCI, V19, P7476, DOI 10.1523/JNEUROSCI.19-17-07476.1999
   Putney JW, 2001, J CELL SCI, V114, P2223
   Putney JW, 2000, NEURON, V27, P411, DOI 10.1016/S0896-6273(00)00048-9
   Quednau BD, 1997, AM J PHYSIOL-CELL PH, V272, pC1250, DOI 10.1152/ajpcell.1997.272.4.C1250
   Rego AC, 2001, J NEUROSCI, V21, P1893, DOI 10.1523/JNEUROSCI.21-06-01893.2001
   Reichert SA, 2001, J NEUROSCI, V21, P6608, DOI 10.1523/JNEUROSCI.21-17-06608.2001
   Rettig J, 1997, J NEUROSCI, V17, P6647
   Reyes-Harde M, 1999, P NATL ACAD SCI USA, V96, P4061, DOI 10.1073/pnas.96.7.4061
   Rizzuto R, 1998, SCIENCE, V280, P1763, DOI 10.1126/science.280.5370.1763
   RIZZUTO R, 1993, SCIENCE, V262, P744, DOI 10.1126/science.8235595
   Robb-Gaspers LD, 1998, BBA-BIOENERGETICS, V1366, P17, DOI 10.1016/S0005-2728(98)00118-2
   Robb-Gaspers LD, 1998, EMBO J, V17, P4987, DOI 10.1093/emboj/17.17.4987
   Roderick HL, 2000, J CELL BIOL, V149, P1235, DOI 10.1083/jcb.149.6.1235
   Rogister F, 2001, EUR J MED CHEM, V36, P597, DOI 10.1016/S0223-5234(01)01247-8
   ROTTENBERG H, 1990, BIOCHIM BIOPHYS ACTA, V1016, P77, DOI 10.1016/0005-2728(90)90009-S
   Ruiz F, 2000, EUR J PHARMACOL, V404, P29, DOI 10.1016/S0014-2999(00)00584-7
   Rys-Sikora KE, 1998, J BIOL CHEM, V273, P32627, DOI 10.1074/jbc.273.49.32627
   Sabatini BL, 2001, CURR OPIN NEUROBIOL, V11, P349, DOI 10.1016/S0959-4388(00)00218-X
   SAGARA Y, 1992, J BIOL CHEM, V267, P12606
   Sah P, 1996, TRENDS NEUROSCI, V19, P150, DOI 10.1016/S0166-2236(96)80026-9
   Sakaba T, 2001, NEURON, V32, P1119, DOI 10.1016/S0896-6273(01)00543-8
   SANCHEZARMASS S, 1987, AM J PHYSIOL, V252, pC595, DOI 10.1152/ajpcell.1987.252.6.C595
   Scanlon JM, 2000, CELL CALCIUM, V28, P317, DOI 10.1054/ceca.2000.0171
   SCHARFMAN HE, 1989, SCIENCE, V246, P257, DOI 10.1126/science.2508225
   Schröder UH, 1999, NEUROPHARMACOLOGY, V38, P319, DOI 10.1016/S0028-3908(98)00198-1
   Scorrano L, 2001, J BIOL CHEM, V276, P12035, DOI 10.1074/jbc.M010603200
   Scotti AL, 1999, PHILOS T ROY SOC B, V354, P357, DOI 10.1098/rstb.1999.0387
   SEIDLER NW, 1989, J BIOL CHEM, V264, P17816
   Shimizu H, 1997, CELL CALCIUM, V21, P31, DOI 10.1016/S0143-4160(97)90094-4
   Shmigol A, 1998, PFLUG ARCH EUR J PHY, V437, P158, DOI 10.1007/s004240050761
   SIEGL PKS, 1984, P NATL ACAD SCI-BIOL, V81, P3238, DOI 10.1073/pnas.81.10.3238
   SLATER EC, 1973, BIOCHIM BIOPHYS ACTA, V301, P129, DOI 10.1016/0304-4173(73)90002-5
   SLAUGHTER RS, 1988, BIOCHEMISTRY-US, V27, P2403, DOI 10.1021/bi00407a023
   Smith AB, 1996, J PHYSIOL-LONDON, V497, P657, DOI 10.1113/jphysiol.1996.sp021797
   Soderling TR, 2000, CURR OPIN NEUROBIOL, V10, P375, DOI 10.1016/S0959-4388(00)00090-8
   SOLEM LE, 1993, TOXICOL APPL PHARM, V121, P50, DOI 10.1006/taap.1993.1128
   Sorrentino V, 2000, CURR OPIN GENET DEV, V10, P662, DOI 10.1016/S0959-437X(00)00139-8
   SPARAGNA GC, 1995, J BIOL CHEM, V270, P27510, DOI 10.1074/jbc.270.46.27510
   Spitzer NC, 2000, BIOESSAYS, V22, P811
   Sridhar TS, 1997, J NEUROSCI, V17, P428, DOI 10.1523/JNEUROSCI.17-01-00428.1997
   STAHL WL, 1992, MOL BRAIN RES, V16, P223, DOI 10.1016/0169-328X(92)90229-5
   Stauffer TP, 1997, BRAIN RES, V748, P21, DOI 10.1016/S0006-8993(96)01282-6
   Stout AK, 1998, NAT NEUROSCI, V1, P366, DOI 10.1038/1577
   Strehler EE, 2001, PHYSIOL REV, V81, P21, DOI 10.1152/physrev.2001.81.1.21
   SZABO I, 1992, J BIOL CHEM, V267, P2940
   Szentesi P, 2001, J GEN PHYSIOL, V118, P355, DOI 10.1085/jgp.118.4.355
   Taguchi J, 2000, ACTA NEUROPATHOL, V100, P153, DOI 10.1007/s004019900165
   Tang YG, 1997, NEURON, V18, P483, DOI 10.1016/S0896-6273(00)81248-9
   Tang YM, 2000, J NEUROCHEM, V74, P702, DOI 10.1046/j.1471-4159.2000.740702.x
   TERADA H, 1990, ENVIRON HEALTH PERSP, V87, P213, DOI 10.2307/3431027
   THASTRUP O, 1990, P NATL ACAD SCI USA, V87, P2466, DOI 10.1073/pnas.87.7.2466
   THAYER SA, 1990, J PHYSIOL-LONDON, V425, P85, DOI 10.1113/jphysiol.1990.sp018094
   THOMAS D, 1994, METHOD CELL BIOL, V40, P65
   Thrower EC, 2000, J BIOL CHEM, V275, P36049, DOI 10.1074/jbc.M000970200
   Tominaga M, 1998, NEURON, V21, P531, DOI 10.1016/S0896-6273(00)80564-4
   TREVES S, 1992, BIOCHEM J, V287, P579, DOI 10.1042/bj2870579
   TREVES S, 1990, BIOCHEM J, V271, P473, DOI 10.1042/bj2710473
   Triggle DJ, 1999, EUR J PHARMACOL, V375, P311, DOI 10.1016/S0014-2999(99)00329-5
   Tse FW, 1997, NEURON, V18, P121, DOI 10.1016/S0896-6273(01)80051-9
   Tsoi M, 1998, J BIOL CHEM, V273, P4155, DOI 10.1074/jbc.273.7.4155
   Unitt JF, 1999, BIOORGAN MED CHEM, V7, P1891, DOI 10.1016/S0968-0896(99)00166-2
   Usachev YM, 2002, NEURON, V33, P113, DOI 10.1016/S0896-6273(01)00557-8
   Usachev YM, 1999, BIOESSAYS, V21, P743, DOI 10.1002/(SICI)1521-1878(199909)21:9<743::AID-BIES5>3.0.CO;2-M
   Usachev YM, 1997, J NEUROSCI, V17, P7404
   Usachev YM, 1999, J PHYSIOL-LONDON, V519, P115, DOI 10.1111/j.1469-7793.1999.0115o.x
   VERBOOMEN H, 1992, BIOCHEM J, V286, P591, DOI 10.1042/bj2860591
   Verdru P, 1997, J NEUROPHYSIOL, V77, P484, DOI 10.1152/jn.1997.77.1.484
   Verma AK, 1996, J BIOL CHEM, V271, P3714
   Votyakova TV, 2001, J NEUROCHEM, V79, P266, DOI 10.1046/j.1471-4159.2001.00548.x
   Wang C, 1997, BIOCHEM BIOPH RES CO, V233, P86, DOI 10.1006/bbrc.1997.6398
   WANG GJ, 1995, NEUROSCI LETT, V186, P139, DOI 10.1016/0304-3940(95)11305-G
   Wang GJ, 2002, J NEUROPHYSIOL, V87, P740, DOI 10.1152/jn.00345.2001
   Wang GJ, 1996, J NEUROPHYSIOL, V76, P1611, DOI 10.1152/jn.1996.76.3.1611
   Wang SSH, 2000, NAT NEUROSCI, V3, P1266, DOI 10.1038/81792
   Watano T, 1996, BRIT J PHARMACOL, V119, P555, DOI 10.1111/j.1476-5381.1996.tb15708.x
   WERTH JL, 1994, J NEUROSCI, V14, P348
   Werth JL, 1996, J NEUROSCI, V16, P1008
   WETTWER E, 1992, PHARMACOL TOXICOL, V71, P95, DOI 10.1111/j.1600-0773.1992.tb00526.x
   WHITE RJ, 1995, J NEUROSCI, V15, P1318
   White RJ, 1996, J NEUROSCI, V16, P5688
   Wilcox RA, 1998, TRENDS PHARMACOL SCI, V19, P467, DOI 10.1016/S0165-6147(98)01260-7
   Wolfe MS, 1999, NATURE, V398, P513, DOI 10.1038/19077
   Wong HN, 1998, J BIOL CHEM, V273, P17227, DOI 10.1074/jbc.273.27.17227
   WU KD, 1995, AM J PHYSIOL-CELL PH, V269, pC775, DOI 10.1152/ajpcell.1995.269.3.C775
   Xu KL, 2001, NEURON, V31, P957, DOI 10.1016/S0896-6273(01)00432-9
   Xu L, 1998, ANN NY ACAD SCI, V853, P130
   Yang J, 1997, SCIENCE, V275, P1129, DOI 10.1126/science.275.5303.1129
   Yoo AS, 2000, NEURON, V27, P561, DOI 10.1016/S0896-6273(00)00066-0
   Zacharias DA, 1997, MOL BRAIN RES, V45, P173, DOI 10.1016/S0169-328X(97)00009-0
   ZACHARIAS DA, 1995, MOL BRAIN RES, V28, P263, DOI 10.1016/0169-328X(94)00215-Z
   Zenisek D, 2000, NEURON, V25, P229, DOI 10.1016/S0896-6273(00)80885-5
   Zhang YL, 1999, J NEUROSCI, V19, P3307
   Zhao FY, 2001, J BIOL CHEM, V276, P13810, DOI 10.1074/jbc.M006104200
   Zhong N, 2001, J NEUROSCI, V21, P9598, DOI 10.1523/JNEUROSCI.21-24-09598.2001
   ZHOU ZA, 1993, J PHYSIOL-LONDON, V469, P245, DOI 10.1113/jphysiol.1993.sp019813
   Zipfel GJ, 2000, J NEUROTRAUM, V17, P857, DOI 10.1089/neu.2000.17.857
   ZORATTI M, 1995, BBA-REV BIOMEMBRANES, V1241, P139, DOI 10.1016/0304-4157(95)00003-A
   Zucker RS, 1999, CURR OPIN NEUROBIOL, V9, P305, DOI 10.1016/S0959-4388(99)80045-2
   Zylinska L, 1998, BBA-MOL CELL RES, V1448, P99, DOI 10.1016/S0167-4889(98)00128-1
NR 309
TC 70
Z9 78
U1 0
U2 4
PU IMR PRESS
PI ROBINSON
PA 112 ROBINSON RD, ROBINSON, SINGAPORE
SN 2768-6701
EI 2768-6698
J9 FRONT BIOSCI-LANDMRK
JI Front. Biosci.
PD MAY
PY 2002
VL 7
BP D1255
EP D1279
DI 10.2741/thayer
PG 25
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA 548ZE
UT WOS:000175419400015
PM 11991858
OA Bronze
DA 2025-04-10
ER

PT J
AU O'Brien, M
   McCarthy, T
   Jenkins, D
   Paul, P
   Dausset, J
   Carosella, ED
   Moreau, P
AF O'Brien, M
   McCarthy, T
   Jenkins, D
   Paul, P
   Dausset, J
   Carosella, ED
   Moreau, P
TI Altered HLA-G transcription in pre-eclampsia is associated with
   allele specific inheritance:: possible role of the HLA-G gene in
   susceptibility to the disease
SO CELLULAR AND MOLECULAR LIFE SCIENCES
LA English
DT Article
DE pre-eclampsia; HLA-G; alternative splicing; polymorphism
ID PREGNANCY-INDUCED HYPERTENSION; FIRST-TRIMESTER TROPHOBLAST; CLASS-I; G
   EXPRESSION; EXTRAVILLOUS TROPHOBLASTS; MESSENGER-RNA; CELL-SURFACE;
   PREECLAMPSIA; ANTIGEN; POLYMORPHISM
AB Pre-eclampsia is a disorder of human pregnancy occuring in 5-10 % of all births, and represents the leading cause of infant morbidity and mortality and maternal death. In pre-eclampsia, invasion of fetal trophoblasts into maternal arteries during early pregnancy is shallow or absent. Here we examined the hypothesis that HLA-G, a non-classical class I HLA expressed in cytotrophoblasts, may act as a key gene in pre-eclampsia. We analysed HLA-G at the level of transcription and genotyped a silent CAC-CAT polymorphism in exon 3 and a 14-by insertion/deletion in the 3' untranslated region. A deficit in levels of the HLA-G3 transcript was observed in mild pre-eclampsia compared to normal placentas. The distribution of HLA-G polymorphisms was different between normal and pre-eclampsia samples. A correlation between the alteration in transcription of the HLA-G gene and certain HLA-G genotypes was also observed. Thus we provide the first evidence for a possible role of HLA-G in genetic susceptibility to, and pathogenesis of preeclampsia.
C1 Hop St Louis, Inst Hematol, DRM, DSV,Serv Rech Hematoimmunol,CEA, F-75010 Paris, France.
   Natl Univ Ireland Univ Coll Cork, Dept Biochem, Cork, Ireland.
   Natl Univ Ireland Univ Coll Cork, Dept Obstet & Gynaecol, Cork, Ireland.
   Fdn Jean Dausset, F-75010 Paris, France.
C3 CEA; Assistance Publique Hopitaux Paris (APHP); Universite Paris Cite;
   Hopital Universitaire Saint-Louis - APHP; University College Cork;
   University College Cork; Foundation Jean Dausset-CEPH
RP Moreau, P (corresponding author), Hop St Louis, Inst Hematol, DRM, DSV,Serv Rech Hematoimmunol,CEA, 1 Ave Claude Vellefaux, F-75010 Paris, France.
RI Moreau, Philippe/HKN-2799-2023; PAUL, Pascale/R-1484-2016
OI Moreau, Philippe/0000-0002-2868-7401; PAUL, Pascale/0000-0002-6734-4479;
   O'Brien, Margaret/0000-0002-9306-6871
CR ARNGRIMSSON R, 1990, BRIT J OBSTET GYNAEC, V97, P762, DOI 10.1111/j.1471-0528.1990.tb02569.x
   Arngrimsson R, 1997, AM J HUM GENET, V61, P354, DOI 10.1086/514843
   Bainbridge DRJ, 2000, J REPROD IMMUNOL, V47, P1, DOI 10.1016/S0165-0378(00)00056-5
   Blaschitz A, 1997, EUR J IMMUNOL, V27, P3380, DOI 10.1002/eji.1830271237
   Castro MJ, 2000, TISSUE ANTIGENS, V56, P232, DOI 10.1034/j.1399-0039.2000.560305.x
   CHESLEY LC, 1986, BRIT J OBSTET GYNAEC, V93, P898, DOI 10.1111/j.1471-0528.1986.tb08006.x
   COLBERN GT, 1994, AM J OBSTET GYNECOL, V170, P1244, DOI 10.1016/S0002-9378(94)70134-2
   Crisa L, 1997, J EXP MED, V186, P289, DOI 10.1084/jem.186.2.289
   GERAGHTY DE, 1987, P NATL ACAD SCI USA, V84, P9145, DOI 10.1073/pnas.84.24.9145
   Goldman-Wohl DS, 2000, MOL HUM REPROD, V6, P88, DOI 10.1093/molehr/6.1.88
   Hara N, 1996, AM J REPROD IMMUNOL, V36, P349
   HARRISON G, 1993, HUM MOL GENET, V2, P2220
   Harrison GA, 1997, AM J HUM GENET, V60, P1158
   Hiby SE, 1999, TISSUE ANTIGENS, V53, P1, DOI 10.1034/j.1399-0039.1999.530101.x
   HOULIHAN JM, 1995, J IMMUNOL, V154, P5665
   HUMPHREY KE, 1995, BRIT J OBSTET GYNAEC, V102, P707, DOI 10.1111/j.1471-0528.1995.tb11427.x
   Hviid TVF, 1998, HUM IMMUNOL, V59, P87, DOI 10.1016/S0198-8859(97)00259-0
   ISHITANI A, 1992, P NATL ACAD SCI USA, V89, P3947, DOI 10.1073/pnas.89.9.3947
   Kirszenbaum M, 1999, J REPROD IMMUNOL, V43, P105, DOI 10.1016/S0165-0378(99)00025-X
   KOVATS S, 1990, SCIENCE, V248, P220, DOI 10.1126/science.2326636
   Le Gal FA, 1999, INT IMMUNOL, V11, P1351, DOI 10.1093/intimm/11.8.1351
   Lie RT, 1998, BRIT MED J, V316, P1343, DOI 10.1136/bmj.316.7141.1343
   Lim KH, 1997, AM J PATHOL, V151, P1809
   Llano M, 1998, EUR J IMMUNOL, V28, P2854, DOI 10.1002/(SICI)1521-4141(199809)28:09<2854::AID-IMMU2854>3.0.CO;2-W
   Mallet V, 2000, HUM IMMUNOL, V61, P212, DOI 10.1016/S0198-8859(99)00166-4
   MCMASTER MT, 1995, J IMMUNOL, V154, P3771
   Menier C, 2000, HUM IMMUNOL, V61, P1118, DOI 10.1016/S0198-8859(00)00194-4
   Moreau P, 1999, INT IMMUNOL, V11, P803, DOI 10.1093/intimm/11.5.803
   MOREAU P, 1995, CR ACAD SCI III-VIE, V318, P837
   Ober C, 1998, PLACENTA, V19, P127, DOI 10.1016/S0143-4004(98)90000-5
   ONNO M, 1994, HUM IMMUNOL, V41, P79, DOI 10.1016/0198-8859(94)90089-2
   Paul P, 2000, HUM IMMUNOL, V61, P1138, DOI 10.1016/S0198-8859(00)00197-X
   Pipkin FB, 1999, BIOL NEONATE, V76, P325, DOI 10.1159/000014175
   Rebmann V, 2001, TISSUE ANTIGENS, V57, P15, DOI 10.1034/j.1399-0039.2001.057001015.x
   Riteau B, 2001, J IMMUNOL, V166, P5018, DOI 10.4049/jimmunol.166.8.5018
   ROBERTS JM, 1993, LANCET, V341, P1447, DOI 10.1016/0140-6736(93)90889-O
   RouasFreiss N, 1997, P NATL ACAD SCI USA, V94, P11520, DOI 10.1073/pnas.94.21.11520
   Sohda S, 1997, J MED GENET, V34, P525, DOI 10.1136/jmg.34.6.525
   Vaughan P, 1998, NUCLEIC ACIDS RES, V26, P810, DOI 10.1093/nar/26.3.810
   Wang J, 1998, J NEPHROL, V11, P53
   WARD K, 1993, NAT GENET, V4, P59, DOI 10.1038/ng0593-59
   Yang YP, 1996, J IMMUNOL, V156, P4224
NR 42
TC 137
Z9 147
U1 0
U2 7
PU BIRKHAUSER VERLAG AG
PI BASEL
PA VIADUKSTRASSE 40-44, PO BOX 133, CH-4010 BASEL, SWITZERLAND
SN 1420-682X
J9 CELL MOL LIFE SCI
JI Cell. Mol. Life Sci.
PD NOV
PY 2001
VL 58
IS 12-13
BP 1943
EP 1949
DI 10.1007/PL00000828
PG 7
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA 500WD
UT WOS:000172649800017
PM 11766889
OA Green Published
DA 2025-04-10
ER

PT J
AU Lahat, N
   Rahat, MA
   Ballan, M
   Weiss-Cerem, L
   Engelmayer, M
   Bitterman, H
AF Lahat, N
   Rahat, MA
   Ballan, M
   Weiss-Cerem, L
   Engelmayer, M
   Bitterman, H
TI Hypoxia reduces CD80 expression on monocytes but enhances their
   LPS-stimulated TNF-α secretion
SO JOURNAL OF LEUKOCYTE BIOLOGY
LA English
DT Article
DE reoxygenation; CD86; HLA-DR
ID TUMOR-NECROSIS-FACTOR; ISCHEMIA-REPERFUSION; ANTIGEN PRESENTATION;
   INTESTINAL ISCHEMIA; AUTOIMMUNE-DISEASE; ARTERY-OCCLUSION;
   TISSUE-INJURY; SEPSIS; SHOCK; INFLAMMATION
AB Monocytes/macrophages in ischemic tissues are involved in inflammation and suppression of adaptive immunity via secretion of proinflammatory cytokines and reduced ability to trigger T cells, respectively. We subjected human mononuclear cells and mouse macrophages to hypoxia and reoxygenation, the main constituents of ischemia and reperfusion, and added lipopolysaccharide (LPS) to simulate bacterial translocation, which frequently accompanies ischemia. We monitored the secretion of tumor necrosis factor alpha (TNF-alpha) and the surface expression of human leukocyte antigen-DR and the costimulatory molecules CD80 and CD86 on monocytes/macrophages. Hypoxia selectively reduced the surface expression of CD80 (P<0.01), and synergistically with LPS, it enhanced TNF-alpha secretion (P<0.003). Reoxygenation reversed both phenomena. In the mouse macrophage cell line RAW 264.7, hypoxia reduced the surface expression of CD80 and increased its concentrations in the supernatants (P<0.01). Down-regulation of the mRNA coding for the membrane-anchored CD80 was observed, suggesting that hypoxia triggers alternative splicing to generate soluble CD80. Cumulatively, these results suggest that hypoxia simultaneously affects monocytes/macrophages to enhance inflammation and reduce their ability to initiate adaptive-immunity responses associated with ischemic injury.
C1 Carmel Hosp, Rappaport Family Inst Res Med Sci, Res Immunol Unit, Ischemia Shock Res Lab, IL-34362 Haifa, Israel.
   Carmel Hosp, Rappaport Family Inst Res Med Sci, Res Immunol Unit, IL-34362 Haifa, Israel.
   Technion Israel Inst Technol, Rappaport Fac Med, Haifa, Israel.
C3 Clalit Health Services; Carmel Medical Center; Technion Israel Institute
   of Technology; Rappaport Faculty of Medicine; Technion Israel Institute
   of Technology; Rappaport Faculty of Medicine; Clalit Health Services;
   Carmel Medical Center; Technion Israel Institute of Technology;
   Rappaport Faculty of Medicine
RP Rahat, MA (corresponding author), Carmel Hosp, Rappaport Family Inst Res Med Sci, Res Immunol Unit, Ischemia Shock Res Lab, 7 Michal St, IL-34362 Haifa, Israel.
RI Rahat, M.A./AAF-1184-2020
OI Rahat, Michal Amit/0000-0002-1881-1173
CR Anderson DE, 1999, CURR OPIN IMMUNOL, V11, P677, DOI 10.1016/S0952-7915(99)00036-9
   AYALA A, 1990, IMMUNOLOGY, V70, P33
   AYALA A, 1992, CYTOKINE, V4, P66, DOI 10.1016/1043-4666(92)90039-T
   Ayala C, 2001, LINGUA FRANCA, V11, P5
   BEUTLER B, 1988, ANNU REV BIOCHEM, V57, P505, DOI 10.1146/annurev.bi.57.070188.002445
   BITTERMAN H, 1988, P SOC EXP BIOL MED, V188, P265
   BITTERMAN H, 1991, J CLIN IMMUNOL, V11, P184, DOI 10.1007/BF00917424
   COHEN S, 1992, LYMPHOKINE CYTOK RES, V11, P215
   De Greef KE, 2001, KIDNEY INT, V60, P1415, DOI 10.1046/j.1523-1755.2001.0600041415.x
   Deitch EA, 1990, MULTIPLE ORGAN FAILU, P40
   Faas SJ, 2000, J IMMUNOL, V164, P6340, DOI 10.4049/jimmunol.164.12.6340
   GAMBLE JR, 1990, SCIENCE, V249, P414
   GRANGER DN, 1995, ANNU REV PHYSIOL, V57, P311, DOI 10.1146/annurev.ph.57.030195.001523
   GROTZ MRW, 1995, SHOCK, V3, P362
   Guida E, 1998, CELL PHYSIOL BIOCHEM, V8, P75, DOI 10.1159/000016272
   HAN J, 1991, J IMMUNOL, V146, P1843
   HAN J, 1990, J EXP MED, V171, P465, DOI 10.1084/jem.171.2.465
   Harris NL, 2001, J IMMUNOL, V166, P4908, DOI 10.4049/jimmunol.166.8.4908
   Kolber MA, 2001, CELL IMMUNOL, V214, P35, DOI 10.1006/cimm.2001.1882
   KUCHROO VK, 1995, CELL, V80, P707, DOI 10.1016/0092-8674(95)90349-6
   Lederer JA, 1999, SHOCK, V11, P153, DOI 10.1097/00024382-199903000-00001
   Leeper-Woodford SK, 1999, AM J PHYSIOL-LUNG C, V276, pL909, DOI 10.1152/ajplung.1999.276.6.L909
   LEFER AM, 1993, ANNU REV PHARMACOL, V33, P71, DOI 10.1146/annurev.pa.33.040193.000443
   LEFER AM, 1983, HDB SHOCK TRAUMA, P291
   Lemaire LCJM, 1999, DIGEST SURG, V16, P222, DOI 10.1159/000018731
   LEVINE RL, 1993, FASEB J, V7, P1242, DOI 10.1096/fasebj.7.13.8405809
   Lin RY, 1996, J MED, V27, P303
   Lu P, 1997, CURR OPIN IMMUNOL, V9, P858, DOI 10.1016/S0952-7915(97)80190-2
   Manna PP, 2001, TRANSPLANTATION, V72, P1563, DOI 10.1097/00007890-200111150-00015
   McDermott MF, 1999, CELL, V97, P133, DOI 10.1016/S0092-8674(00)80721-7
   McHugh RS, 1998, CLIN IMMUNOL IMMUNOP, V87, P50, DOI 10.1006/clin.1997.4503
   MEAGER A, 1989, J IMMUNOL METHODS, V116, P1, DOI 10.1016/0022-1759(89)90306-2
   MITSUDO S, 1992, SURG CLIN N AM, V72, P43
   Oberholzer C, 2001, FASEB J, V15, P879, DOI 10.1096/fj.00-058rev
   PATEL A, 1992, SURG CLIN N AM, V72, P31
   POLK HC, 1986, ANN SURG, V204, P282
   REDMOND HP, 1992, SURGERY, V111, P647
   Rosengart MR, 2000, SHOCK, V13, P183, DOI 10.1097/00024382-200003000-00003
   SCANNELL G, 1993, J SURG RES, V54, P281, DOI 10.1006/jsre.1993.1044
   Song GY, 2000, SURGERY, V128, P133, DOI 10.1067/msy.2000.107282
   Song GY, 2000, J SURG RES, V91, P141, DOI 10.1006/jsre.2000.5928
   Takada M, 1997, J CLIN INVEST, V100, P1199, DOI 10.1172/JCI119632
   Takala A, 2002, ANN MED, V34, P614, DOI 10.1080/078538902321117841
   TIANO G, 1994, SURGERY, V116, P332
   Tjardes T, 2002, SHOCK, V17, P1, DOI 10.1097/00024382-200201000-00001
   VanGool SW, 1996, IMMUNOL REV, V153, P47
   VANOTTEREN GM, 1995, AM J RESP CELL MOL, V13, P399, DOI 10.1165/ajrcmb.13.4.7546769
   ZIMMERMAN BJ, 1992, SURG CLIN N AM, V72, P65
NR 48
TC 46
Z9 56
U1 1
U2 7
PU FEDERATION AMER SOC EXP BIOL
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3998 USA
SN 0741-5400
J9 J LEUKOCYTE BIOL
JI J. Leukoc. Biol.
PD AUG
PY 2003
VL 74
IS 2
BP 197
EP 205
DI 10.1189/jlb.0303105
PG 9
WC Cell Biology; Hematology; Immunology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Hematology; Immunology
GA 755FC
UT WOS:000187392000008
PM 12885936
DA 2025-04-10
ER

PT J
AU Hofmann, WK
   Kalina, U
   Wagner, S
   Seipelt, G
   Ries, C
   Hoelzer, D
   Ottmann, OG
AF Hofmann, WK
   Kalina, U
   Wagner, S
   Seipelt, G
   Ries, C
   Hoelzer, D
   Ottmann, OG
TI Characterization of defective megakaryocytic development in patients
   with myelodysplastic syndromes
SO EXPERIMENTAL HEMATOLOGY
LA English
DT Article
DE myelodysplastic syndrome; CD34(+) cells; megakaryocyte growth and
   development factor; C-mpl receptor
ID MYELOBLASTIC-LEUKEMIA CELLS; C-MPL LIGAND; RECOMBINANT HUMAN
   THROMBOPOIETIN; ACUTE MYELOID-LEUKEMIA; PLATELET PRODUCTION; RECEPTOR
   MPL; GROWTH; EXPRESSION; STIMULATION; CLONING
AB Megakaryocytic differentiation of progenitor cells was investigated in nine patients with low-risk myelodysplastic syndromes (MDS) (eight refractory anemia [RA] and one RA with ringed sideroblasts [RARS]) and five patients,vith high-risk MDS (two RA with excess of blasts [RAEB] and three RAEB in transformation [RAEB-T]), Bone marrow-derived CD34(+) cells were enriched to a purity of 87% +/- 2% (mean +/- SEM) and assayed in short-term suspension cultures in the presence of 10 ng/mL of PEGylated recombinant human megakaryocyte (MK) growth and development factor (PEG-rHuMGDF) and in addition to 50 ng/mL stem cell factor and 10 ng/mL interleukin-3, Cells of the megakaryocytic lineage were identified by flow cytometric analysis of CD42b (GP1b) and mature MKs by morphologic criteria. Transcription of c-mpl receptor-specific mRNA in the CD34(+) cells of these patients was investigated by full-length reverse transcriptase polymerase chain reaction of the p form of c-mpl as well as of the alternative splice product c-mpl k, CD34(+) cells from seven healthy bone marrow donors served as controls. Differentiation along the MK pathway was stimulated in five patients with RA, C-mpl mRNA was expressed in the CD34(+) cells in all cases, In three low-risk patients the capacity for in vitro MK growth was absent or minimal even though mRNA for c-mpl receptor was detected in the CD34(+) cells of this group as well, In patients with high-risk MDS, PEG-rHuMGDF stimulated in vitro MK growth from CD34(+) cells in only one of five cases. As in the patients with low-risk MDS, c-mpl mRNA for both c-mpl p and c-mpl k splicing products was detected. These results indicate that the in vitro response to stimulation with c-mpl ligand discriminates between two groups of patients with low-risk MDS and that the observed defect in megakaryocytic development is unrelated to the level of c-mpl expression in both low-risk and high-risk MDS. (C) 1999 International Society for Experimental Hematology. Published by Elsevier Science Inc.
C1 Univ Frankfurt Hosp, Dept Hematol, D-60590 Frankfurt, Germany.
C3 Goethe University Frankfurt; Goethe University Frankfurt Hospital
RP Hofmann, WK (corresponding author), Univ Frankfurt Hosp, Dept Hematol, D-60590 Frankfurt, Germany.
RI Ries, Christian/A-9687-2012; Ottmann, Oliver/D-5007-2016
OI Ottmann, Oliver/0000-0001-9559-1330
CR Adams JA, 1997, BRIT J HAEMATOL, V99, P139, DOI 10.1046/j.1365-2141.1997.3543166.x
   BANU N, 1995, BLOOD, V86, P1331, DOI 10.1182/blood.V86.4.1331.bloodjournal8641331
   BARTLEY TD, 1994, CELL, V77, P1117, DOI 10.1016/0092-8674(94)90450-2
   BOUSCARY D, 1995, LEUKEMIA, V9, P783
   DEBILI N, 1995, BLOOD, V85, P391, DOI 10.1182/blood.V85.2.391.bloodjournal852391
   DESAUVAGE FJ, 1994, NATURE, V369, P533, DOI 10.1038/369533a0
   Drexler HG, 1996, LEUKEMIA, V10, P1405
   GREENBERG SM, 1987, J BIOL CHEM, V262, P3269
   GURNEY AL, 1994, SCIENCE, V265, P1445, DOI 10.1126/science.8073287
   Hofmann WK, 1996, SEMIN HEMATOL, V33, P177
   HUNT P, 1995, BLOOD, V86, P540, DOI 10.1182/blood.V86.2.540.bloodjournal862540
   KAUSHANSKY K, 1995, BLOOD, V86, P419, DOI 10.1182/blood.V86.2.419.bloodjournal862419
   KAUSHANSKY K, 1994, NATURE, V369, P568, DOI 10.1038/369568a0
   LOK S, 1994, NATURE, V369, P565, DOI 10.1038/369565a0
   Matsumura I, 1996, BLOOD, V88, P3074, DOI 10.1182/blood.V88.8.3074.bloodjournal8883074
   Matsumura I, 1996, LEUKEMIA LYMPHOMA, V23, P533, DOI 10.3109/10428199609054861
   MATSUMURA I, 1995, BLOOD, V86, P703, DOI 10.1182/blood.V86.2.703.bloodjournal862703
   Moliterno AR, 1998, NEW ENGL J MED, V338, P572, DOI 10.1056/NEJM199802263380903
   MORELLA KK, 1995, BLOOD, V86, P557, DOI 10.1182/blood.V86.2.557.bloodjournal862557
   Motoji T, 1996, BRIT J HAEMATOL, V94, P513, DOI 10.1046/j.1365-2141.1996.d01-1832.x
   Piacibello W, 1997, LEUKEMIA, V11, P531, DOI 10.1038/sj.leu.2400603
   Quentmeier H, 1996, LEUKEMIA, V10, P297
   TOHYAMA K, 1995, BRIT J HAEMATOL, V91, P795, DOI 10.1111/j.1365-2141.1995.tb05391.x
   Usuki K, 1996, STEM CELLS, V14, P558, DOI 10.1002/stem.140558
   VIGON I, 1993, BLOOD, V82, P877
   VIGON I, 1992, P NATL ACAD SCI USA, V89, P5640, DOI 10.1073/pnas.89.12.5640
   Wetzler M, 1997, J CLIN ONCOL, V15, P2262, DOI 10.1200/JCO.1997.15.6.2262
   Zwierzina H, 1998, LEUKEMIA, V12, P59, DOI 10.1038/sj.leu.2400901
NR 28
TC 19
Z9 21
U1 0
U2 2
PU ELSEVIER SCIENCE INC
PI NEW YORK
PA 655 AVENUE OF THE AMERICAS, NEW YORK, NY 10010 USA
SN 0301-472X
J9 EXP HEMATOL
JI Exp. Hematol.
PD MAR
PY 1999
VL 27
IS 3
BP 395
EP 400
DI 10.1016/S0301-472X(98)00077-0
PG 6
WC Hematology; Medicine, Research & Experimental
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Hematology; Research & Experimental Medicine
GA 174HN
UT WOS:000079028800002
PM 10089900
OA Bronze
DA 2025-04-10
ER

PT J
AU Sheibani, N
   Sorenson, CM
   Frazier, WA
AF Sheibani, N
   Sorenson, CM
   Frazier, WA
TI Tissue specific expression alternatively spliced murine PECAM-1 isoforms
SO DEVELOPMENTAL DYNAMICS
LA English
DT Article
DE PECAM-1; cell adhesion molecule; endothelial cells; angiogenesis; signal
   transduction
ID CELL-ADHESION MOLECULE-1; PROTEIN-TYROSINE-PHOSPHATASE; VASCULAR
   ENDOTHELIAL-CELLS; CYTOPLASMIC DOMAIN; CD31; PHOSPHORYLATION;
   ACTIVATION; AGGREGATION; LIGAND; THROMBOSPONDIN-1
AB PECAM-1 (CD31) is a cell adhesion molecule that is highly expressed at the sites of endothelial cell-cell contact and at lower levels on the surface of platelets and leukocytes, It is a member of the immunoglobulin gene superfamily and undergoes alternative splicing to generate several isoforms that differ only in their cytoplasmic domains. The tissue distribution of the expression of different PECAM-1 isoforms has not been previously defined. We have examined PECAM-1 expression in various mouse tissues and endothelial cells. PECAM-1 mRNA was highly expressed in lung, heart, and kidney, and to a lower extent in brain and liver, Most endothelial cells in culture expressed high levels of PECAM-1 mRNA; however, normal mouse brain endothelial cells rapidly lost PECAM-1 expression in culture. To examine the tissue distribution of PECAM-1 isoform expression, RT/PCR was performed on the RNA isolated from various mouse tissues and mouse endothelial cells. Cloning and sequencing of the cDNA products indicated that most tissues and endothelial cells expressed several PECAM-1 isoforms at different frequencies. The PECAM-1 isoform that lacks exons 14 and 15 was most frequently detected in all cases. A novel PECAM-1 isoform that lacks exons 12 and 14 was detected in brain. An antibody to the extracellular domain of PECAM-1 reacted with two major bands, at 130 kDa and 110-120 kDa, in lysates prepared from endothelial cells or kidneys at different stages of development. An antibody prepared against PECAM-1 exon 14, which reacts only with cytoplasmic domain of PECAM-1 isoforms that contain exon 14, failed to react with the major lower molecular weight form of PECAM-1 in these lysates. Therefore, PECAM-1 isoforms that lack exon 14 are expressed in endothelial cells and tissues in developmentally regulated fashion. These results illustrate that multiple PECAM-1 isoforms are expressed in various mouse tissues and endothelial cells. Understanding the distribution of PECAM-1 isoforms, and the identity of intracellular proteins with which they may interact, will help to elucidate the role of PECAM-1 in endothelial cell-cell interactions and morphogenesis, Dev Dyn 1999;214:44-54. (C) 1999 Wiley-Liss, Inc.
C1 Washington Univ, Sch Med, Dept Biochem & Mol Biophys, St Louis, MO 63110 USA.
   Washington Univ, Sch Med, Div Renal, St Louis, MO 63110 USA.
C3 Washington University (WUSTL); Washington University (WUSTL)
RP Sheibani, N (corresponding author), Washington Univ, Sch Med, Dept Biochem & Mol Biophys, Box 8231,660 S Euclid Ave, St Louis, MO 63110 USA.
RI Sheibani, Nader/AAG-2379-2020
FU NCI NIH HHS [CA 65872] Funding Source: Medline; NIDDK NIH HHS [DK 20579]
   Funding Source: Medline
CR ADES EW, 1992, J INVEST DERMATOL, V99, P683, DOI 10.1111/1523-1747.ep12613748
   ALBELDA SM, 1990, J CELL BIOL, V110, P1227, DOI 10.1083/jcb.110.4.1227
   BALDWIN HS, 1994, DEVELOPMENT, V120, P2539
   Berman ME, 1996, J IMMUNOL, V156, P1515
   Buckley CD, 1996, J CELL SCI, V109, P437
   Cao MY, 1998, J BIOL CHEM, V273, P15765, DOI 10.1074/jbc.273.25.15765
   Deaglio S, 1998, J IMMUNOL, V160, P395
   DeLisser HM, 1997, AM J PATHOL, V151, P671
   DeLisser HM, 1997, TRENDS CARDIOVAS MED, V7, P203, DOI 10.1016/S1050-1738(97)00049-2
   DELISSER HM, 1993, J BIOL CHEM, V268, P16037
   DUBOIS NA, 1991, EXP CELL RES, V196, P302, DOI 10.1016/0014-4827(91)90265-V
   Famiglietti J, 1997, J CELL BIOL, V138, P1425, DOI 10.1083/jcb.138.6.1425
   Ferrero E, 1996, CANCER RES, V56, P3211
   Jackson DE, 1997, J BIOL CHEM, V272, P24868, DOI 10.1074/jbc.272.40.24868
   Jackson DE, 1997, J BIOL CHEM, V272, P6986, DOI 10.1074/jbc.272.11.6986
   Kalra VK, 1996, AM J PHYSIOL-HEART C, V271, pH2025, DOI 10.1152/ajpheart.1996.271.5.H2025
   KIRSCHBAUM NE, 1994, BLOOD, V84, P4028, DOI 10.1182/blood.V84.12.4028.bloodjournal84124028
   KOSEKI C, 1992, J CELL BIOL, V119, P1327, DOI 10.1083/jcb.119.5.1327
   Lu TT, 1997, J BIOL CHEM, V272, P14442, DOI 10.1074/jbc.272.22.14442
   Lu TT, 1996, P NATL ACAD SCI USA, V93, P11808, DOI 10.1073/pnas.93.21.11808
   Masuda M, 1997, FEBS LETT, V408, P331, DOI 10.1016/S0014-5793(97)00457-2
   MULLER WA, 1995, J LEUKOCYTE BIOL, V57, P523, DOI 10.1002/jlb.57.4.523
   NEWMAN PJ, 1992, J CELL BIOL, V119, P239, DOI 10.1083/jcb.119.1.239
   Newman PJ, 1997, J CLIN INVEST, V99, P3, DOI 10.1172/JCI119129
   NEWMAN PJ, 1990, SCIENCE, V247, P1219, DOI 10.1126/science.1690453
   Osawa M, 1997, EUR J CELL BIOL, V72, P229
   PIALI L, 1995, J CELL BIOL, V130, P451, DOI 10.1083/jcb.130.2.451
   RISAU W, 1995, FASEB J, V9, P926, DOI 10.1096/fasebj.9.10.7615161
   Sagawa K, 1997, J BIOL CHEM, V272, P13412, DOI 10.1074/jbc.272.20.13412
   Sagawa K, 1997, J BIOL CHEM, V272, P31086, DOI 10.1074/jbc.272.49.31086
   SAXEN L, 1987, PEDIATR NEPHROL, V1, P385, DOI 10.1007/BF00849241
   Sheibani N, 1997, MOL BIOL CELL, V8, P1329, DOI 10.1091/mbc.8.7.1329
   Sheibani N, 1998, MOL BIOL CELL, V9, P701, DOI 10.1091/mbc.9.4.701
   Sheibani N, 1998, BIOTECHNIQUES, V25, P28, DOI 10.2144/98251bm05
   SHEIBANI N, 1995, P NATL ACAD SCI USA, V92, P6788, DOI 10.1073/pnas.92.15.6788
   SHEIBANI N, 1994, KERATINOCYTE METHODS, P167
   Sun J, 1996, J BIOL CHEM, V271, P18561, DOI 10.1074/jbc.271.31.18561
   SWERLICK RA, 1991, J INVEST DERMATOL, V97, P190, DOI 10.1111/1523-1747.ep12479643
   TANAKA Y, 1992, J EXP MED, V176, P245, DOI 10.1084/jem.176.1.245
   XIE Y, 1993, P NATL ACAD SCI USA, V90, P5569, DOI 10.1073/pnas.90.12.5569
   YAN HC, 1995, J BIOL CHEM, V270, P23672, DOI 10.1074/jbc.270.40.23672
NR 41
TC 46
Z9 50
U1 0
U2 3
PU WILEY-LISS
PI NEW YORK
PA DIV JOHN WILEY & SONS INC, 605 THIRD AVE, NEW YORK, NY 10158-0012 USA
SN 1058-8388
J9 DEV DYNAM
JI Dev. Dyn.
PD JAN
PY 1999
VL 214
IS 1
BP 44
EP 54
DI 10.1002/(SICI)1097-0177(199901)214:1<44::AID-DVDY5>3.0.CO;2-L
PG 11
WC Anatomy & Morphology; Developmental Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Anatomy & Morphology; Developmental Biology
GA 154TJ
UT WOS:000077904700005
PM 9915575
DA 2025-04-10
ER

PT J
AU Chaudhuri, T
   Mukherjea, M
   Sachdev, S
   Randall, JD
   Sarkar, S
AF Chaudhuri, T
   Mukherjea, M
   Sachdev, S
   Randall, JD
   Sarkar, S
TI Role of the fetal and α/β exons in the function of fast skeletal
   troponin T isoforms:: Correlation with altered Ca<SUP>2+</SUP>
   regulation associated with development
SO JOURNAL OF MOLECULAR BIOLOGY
LA English
DT Article
DE Ca2+ regulation; fast skeletal muscle troponin T isoforms; fetal and
   alpha/beta peptides; recombinant troponin T variants
ID HUMAN CARDIAC TROPONIN; PHOTO-CROSS-LINKING; CONFORMATIONAL TRANSITION;
   CRYSTAL-STRUCTURE; DELETION MUTANTS; BINDING-SITE; I BINDING; X-RAY;
   MUSCLE; TROPOMYOSIN
AB In mammalian fast skeletal muscle, constitutive and alternative splicing from a single troponin T (TnT) gene produce multiple developmentally regulated and tissue specific TnT isoforms. Two exons, alpha (exon 16) and beta (exon 17), located near the 3' end of the gene and coding for two different 14 amino acid residue peptides are spliced in a mutually exclusive manner giving rise to the adult TnT alpha and the fetal TnT beta isoforms. In addition, an acidic peptide coded by a fetal (f) exon located between exons 8 and 9 near the 5' end of the gene, is specifically present in TnT beta and absent in the adult isoforms. To define the functional role of the f and alpha/beta exons, we constructed combinations of TnT cDNAs from a single human fetal fast skeletal TnT beta cDNA clone in order to circumvent the problem of N-terminal sequence heterogeneity present in wild-type TnT isoforms, irrespective of the stage of development. Nucleotide sequences of these constructs, viz. TnT alpha, TnT alpha+f, TnT beta-f and TnT beta are identical, except for the presence or absence of the alpha or beta and f exons. Our results, using the recombinant TnT isoforms in different functional in vitro assays, show that the presence of the f peptide in the N-terminal T1 region of TnT, has a strong inhibitory effect on binary interactions between TnT and other thin filament proteins, TnI, TnC and Tm. The presence of the f peptide + led to reduced Ca2+-dependent ATPase activity in a reconstituted thin filament, whereas the contribution of the alpha and beta peptides in the biological activity of TnT was primarily modulatory. These results indicate that the f peptide confers an inhibitory effect on the biological function of fast skeletal TnT and this can be correlated with changes in the Ca2+ regulation associated with development in fast skeletal muscle. (c) 2005 Elsevier Ltd. All rights reserved.
C1 Tufts Univ, Sackler Sch Grad Biomed Sci, Program Cell Mol & Dev Biol, Boston, MA 02111 USA.
   Tufts Univ, Sch Med, Dept Anat & Cellular Biol, Boston, MA 02111 USA.
   Tufts Univ, Sch Vet Med, Dept Basic Sci, North Grafton, MA 01536 USA.
C3 Tufts University; Tufts University; Tufts University
RP Tufts Univ, Sackler Sch Grad Biomed Sci, Program Cell Mol & Dev Biol, 136 Harrison Ave, Boston, MA 02111 USA.
EM priya.sarkar@tufts.edu
RI Sachdev, Sean/JFK-0694-2023
FU NICHD NIH HHS [P01-HD 23681] Funding Source: Medline; PHS HHS [R01-H1
   39374] Funding Source: Medline
CR ANDERSON PAW, 1991, CIRC RES, V69, P1226, DOI 10.1161/01.RES.69.5.1226
   BERS D, 1999, METHOD CELL BIOL, V40, P4
   Blumenschein TMA, 2001, J BIOL CHEM, V276, P36606, DOI 10.1074/jbc.M105130200
   BREITBART RE, 1986, J MOL BIOL, V188, P313, DOI 10.1016/0022-2836(86)90157-9
   BRIGGS MM, 1993, DEV BIOL, V158, P503, DOI 10.1006/dbio.1993.1208
   Briggs MM, 1996, AM J PHYSIOL-CELL PH, V270, pC298, DOI 10.1152/ajpcell.1996.270.1.C298
   BRISSON JR, 1986, BIOCHEMISTRY-US, V25, P4548, DOI 10.1021/bi00364a014
   CHONG PCS, 1982, J BIOL CHEM, V257, P1667
   FARAH CS, 1994, J BIOL CHEM, V269, P5230
   FARAH CS, 1995, FASEB J, V9, P755, DOI 10.1096/fasebj.9.9.7601340
   FISHER D, 1995, J BIOL CHEM, V270, P25455, DOI 10.1074/jbc.270.43.25455
   FUJIMORI K, 1990, NATURE, V345, P182, DOI 10.1038/345182a0
   GAGNE SM, 1995, NAT STRUCT BIOL, V2, P784, DOI 10.1038/nsb0995-784
   Gomes AV, 2002, J BIOL CHEM, V277, P35341, DOI 10.1074/jbc.M204118200
   Gordon AM, 2000, PHYSIOL REV, V80, P853, DOI 10.1152/physrev.2000.80.2.853
   GRABAREK Z, 1981, J BIOL CHEM, V256, P3121
   GRABAREK Z, 1990, NATURE, V345, P132, DOI 10.1038/345132a0
   GULATI J, 1994, BIOCHEM BIOPH RES CO, V202, P384, DOI 10.1006/bbrc.1994.1939
   HERZBERG O, 1985, NATURE, V313, P653, DOI 10.1038/313653a0
   HERZBERG O, 1986, J BIOL CHEM, V261, P2638
   HO SN, 1989, GENE, V77, P51, DOI 10.1016/0378-1119(89)90358-2
   Houdusse A, 1997, STRUCTURE, V5, P1695, DOI 10.1016/S0969-2126(97)00315-8
   Jha PK, 1996, BIOCHEMISTRY-US, V35, P16573, DOI 10.1021/bi9622433
   Jha PK, 1996, BIOCHEMISTRY-US, V35, P11026, DOI 10.1021/bi960406h
   Jin JP, 2000, AM J PHYSIOL-CELL PH, V279, pC1067, DOI 10.1152/ajpcell.2000.279.4.C1067
   Jin JP, 2000, BIOCHEMISTRY-US, V39, P11702, DOI 10.1021/bi9927437
   LEAVIS PC, 1984, CRC CR REV BIOCH MOL, V16, P235, DOI 10.3109/10409238409108717
   LESZYK J, 1988, BIOCHEMISTRY-US, V27, P6983, DOI 10.1021/bi00418a047
   Li MX, 1999, BIOCHEMISTRY-US, V38, P8289, DOI 10.1021/bi9901679
   Luo Y, 2000, J MOL BIOL, V296, P899, DOI 10.1006/jmbi.1999.3495
   MacFarland SM, 2002, ARCH BIOCHEM BIOPHYS, V405, P241, DOI 10.1016/S0003-9861(02)00370-3
   MAK AS, 1981, J MOL BIOL, V149, P541, DOI 10.1016/0022-2836(81)90486-1
   Malnic B, 1998, J BIOL CHEM, V273, P10594, DOI 10.1074/jbc.273.17.10594
   Mao CJ, 1996, GENOMICS, V31, P385, DOI 10.1006/geno.1996.0064
   MARGOSSIAN SS, 1982, METHOD ENZYMOL, V85, P55
   McKay RT, 1998, BIOCHEMISTRY-US, V37, P12419, DOI 10.1021/bi9809019
   McKay RT, 1999, BIOCHEMISTRY-US, V38, P5478
   MESNARD L, 1995, CIRC RES, V76, P687, DOI 10.1161/01.RES.76.4.687
   Mukhopadhyay S, 2005, J BIOL CHEM, V280, P538, DOI 10.1074/jbc.M409537200
   Ogut O, 2000, J BIOL CHEM, V275, P26089, DOI 10.1074/jbc.M910360199
   OGUT O, 1999, AM J PHYS, pC1162
   OLAH GA, 1994, BIOCHEMISTRY-US, V33, P8233, DOI 10.1021/bi00193a009
   OLAH GA, 1994, BIOCHEMISTRY-US, V33, P12800, DOI 10.1021/bi00209a011
   PAN BS, 1991, J BIOL CHEM, V266, P12432
   PAN BS, 1992, J BIOL CHEM, V267, P23052
   PARDEE JD, 1982, METHOD CELL BIOL, V24, P271
   PEARLSTONE JR, 1977, CAN J BIOCHEM CELL B, V55, P1032, DOI 10.1139/o77-154
   PEARLSTONE JR, 1983, J BIOL CHEM, V258, P2534
   PEARLSTONE JR, 1985, CAN J BIOCHEM CELL B, V63, P212, DOI 10.1139/o85-030
   Perry SV, 1999, MOL CELL BIOCHEM, V190, P9, DOI 10.1023/A:1006939307715
   Perry SV, 1998, J MUSCLE RES CELL M, V19, P575
   PHILLIPS GN, 1986, J MOL BIOL, V192, P111, DOI 10.1016/0022-2836(86)90468-7
   REISER PJ, 1992, J PHYSIOL-LONDON, V449, P573, DOI 10.1113/jphysiol.1992.sp019102
   SAMSON F, 1992, GENOMICS, V13, P1374, DOI 10.1016/0888-7543(92)90077-6
   SCHACHAT FH, 1987, J MOL BIOL, V198, P551, DOI 10.1016/0022-2836(87)90300-7
   Schaertl S, 1995, BIOCHEMISTRY-US, V34, P15890, DOI 10.1021/bi00049a003
   SHIPSKY CM, 1995, BIOCHEMISTRY-US, V34, P15953
   SMILLIE LB, 1982, METHOD ENZYMOL, V85, P234
   Stefancsik R, 1998, P NATL ACAD SCI USA, V95, P957, DOI 10.1073/pnas.95.3.957
   Stefancsik R, 2003, COMP FUNCT GENOM, V4, P609, DOI 10.1002/cfg.343
   Stone DB, 1998, J MOL BIOL, V281, P689, DOI 10.1006/jmbi.1998.1965
   Strynadka NCJ, 1997, J MOL BIOL, V273, P238, DOI 10.1006/jmbi.1997.1257
   SUNDARALINGAM M, 1985, SCIENCE, V227, P945, DOI 10.1126/science.3969570
   Takeda S, 2003, NATURE, V424, P35, DOI 10.1038/nature01780
   Tobacman LS, 1996, ANNU REV PHYSIOL, V58, P447, DOI 10.1146/annurev.ph.58.030196.002311
   Vassylyev DG, 1998, P NATL ACAD SCI USA, V95, P4847, DOI 10.1073/pnas.95.9.4847
   Vinogradova MV, 2005, P NATL ACAD SCI USA, V102, P5038, DOI 10.1073/pnas.0408882102
   Wang J, 1998, BIOCHEMISTRY-US, V37, P14519, DOI 10.1021/bi9812322
   WANG ZY, 1990, J BIOL CHEM, V265, P4953
   WANG ZY, 1992, P NATL ACAD SCI USA, V89, P11814, DOI 10.1073/pnas.89.24.11814
   WU QL, 1994, DNA CELL BIOL, V13, P217, DOI 10.1089/dna.1994.13.217
   YATES LD, 1983, J BIOL CHEM, V258, P5770
   YATES LD, 1983, J MOL BIOL, V168, P123, DOI 10.1016/S0022-2836(83)80326-X
   ZOT AS, 1987, ANNU REV BIOPHYS BIO, V16, P535
NR 74
TC 22
Z9 26
U1 0
U2 0
PU ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
PI LONDON
PA 24-28 OVAL RD, LONDON NW1 7DX, ENGLAND
SN 0022-2836
EI 1089-8638
J9 J MOL BIOL
JI J. Mol. Biol.
PD SEP 9
PY 2005
VL 352
IS 1
BP 58
EP 71
DI 10.1016/j.jmb.2005.06.066
PG 14
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 963VT
UT WOS:000231835000006
PM 16081096
DA 2025-04-10
ER

PT J
AU Brown, CA
   Lanning, RW
   McKinney, KQ
   Salvino, AR
   Cherniske, E
   Crowe, CA
   Darras, BT
   Gominak, S
   Greenberg, CR
   Grosmann, C
   Heydemann, P
   Mendell, JR
   Pober, BR
   Sasaki, T
   Shapiro, F
   Simpson, DA
   Suchowersky, O
   Spence, JE
AF Brown, CA
   Lanning, RW
   McKinney, KQ
   Salvino, AR
   Cherniske, E
   Crowe, CA
   Darras, BT
   Gominak, S
   Greenberg, CR
   Grosmann, C
   Heydemann, P
   Mendell, JR
   Pober, BR
   Sasaki, T
   Shapiro, F
   Simpson, DA
   Suchowersky, O
   Spence, JE
TI Novel and recurrent mutations in lamin A/C in patients with
   Emery-Dreifuss muscular dystrophy
SO AMERICAN JOURNAL OF MEDICAL GENETICS
LA English
DT Article
DE Emery-Dreifuss muscular dystrophy; EDMD; lamin A/C; mutation
ID INTERMEDIATE FILAMENT PROTEINS; FAMILIAL PARTIAL LIPODYSTROPHY; CAUSE
   AUTOSOMAL-DOMINANT; CHROMATIN BINDING-SITE; NUCLEAR-ENVELOPE;
   PRELAMIN-A; ROD DOMAIN; GENE; MEMBRANE; TAIL
AB Emery-Dreifuss muscular dystrophy (EDMD) is characterized by slowly progressive muscle wasting and weakness; early contractures of the elbows, Achilles tendons, and spine; and cardiomyopathy associated with cardiac conduction defects. Clinically indistinguishable X-linked and autosomal forms of EDMD have been described. Mutations in the STA gene, encoding the nuclear envelope protein emerin, are responsible for X-linked EDMD, while mutations in the LMNA gene encoding lamins A and C by alternative splicing have been found in patients with autosomal dominant, autosomal recessive, and sporadic forms of EDMD. We report mutations in LMNA found in four familial and seven sporadic cases of EDMD, including seven novel mutations. Nine missense mutations and two small in-frame deletions were detected distributed throughout the gene. Most mutations (7/11) were detected within the LMNA exons encoding the central rod domain common to both lamins A/C. All of these missense mutations alter residues in the lamin A/C proteins conserved throughout evolution, implying an essential structural and/or functional role of these residues. One severely affected patient possesed two mutations, one specific to lamin A that may modify the phenotype of this patient. Mutations in LMNA were frequently identified among patients with sporadic and familial forms of EDMD. Further studies are needed to identify the factors modifying disease phenotype among patients harboring mutations within lamin A/C and to determine the effect of various mutations on lamin A/C structure and function. (C) 2001 Wiley-Liss, Inc.
C1 Carolinas Med Ctr, Dept Pediat, Charlotte, NC 28203 USA.
   Yale Univ, Sch Med, Dept Genet, New Haven, CT 06510 USA.
   Metrohlth Med Ctr, Dept Pediat, Cleveland, OH USA.
   Childrens Hosp, Dept Neurol, Boston, MA 02115 USA.
   Harvard Univ, Sch Med, Dept Genet, Boston, MA USA.
   Camino Med Grp, Dept Neurol, Sunnyvale, CA USA.
   Hlth Sci Ctr, Winnipeg, MB, Canada.
   Childrens Hosp, Dept Neurol, San Diego, CA USA.
   Rush Presbyterian St Lukes Med Ctr, Chicago, IL 60612 USA.
   Ohio State Univ, Dept Neurol, Columbus, OH 43210 USA.
   Childrens Hosp, Dept Orthoped, Boston, MA 02115 USA.
   Michigan Inst Neurol Disorders, Farmingham, MI USA.
   Univ Calgary, Dept Clin Neurosci, Calgary, AB, Canada.
   Univ Calgary, Dept Med Genet, Calgary, AB, Canada.
C3 Carolinas Medical Center; Yale University; MetroHealth System; Harvard
   University; Harvard University Medical Affiliates; Boston Children's
   Hospital; Harvard University; Harvard Medical School; Palo Alto Medical
   Foundation Research Institute; University of Manitoba; Children's
   Hospital Research Institute of Manitoba; Children's Hospital Los
   Angeles; Rush University; University System of Ohio; Ohio State
   University; Harvard University; Harvard University Medical Affiliates;
   Boston Children's Hospital; University of Calgary; University of Calgary
RP Carolinas Med Ctr, Dept Pediat Res, POB 32861, Charlotte, NC 28232 USA.
EM cbrown@carolinas.org
OI McKinney, Kimberly/0000-0001-9176-4986; Grosmann,
   Carla/0000-0002-4752-0797; Darras, Basil/0000-0002-1536-8145
CR Barton RM, 1999, J BIOL CHEM, V274, P30008, DOI 10.1074/jbc.274.42.30008
   BIONE S, 1994, NAT GENET, V8, P323, DOI 10.1038/ng1294-323
   Bonne G, 2000, ANN NEUROL, V48, P170, DOI 10.1002/1531-8249(200008)48:2<170::AID-ANA6>3.0.CO;2-J
   Bonne G, 1999, NAT GENET, V21, P285, DOI 10.1038/6799
   Brodsky GL, 2000, CIRCULATION, V101, P473, DOI 10.1161/01.CIR.101.5.473
   Broers JLV, 1997, HISTOCHEM CELL BIOL, V107, P505, DOI 10.1007/s004180050138
   Cao H, 2000, HUM MOL GENET, V9, P109, DOI 10.1093/hmg/9.1.109
   Clements L, 2000, BIOCHEM BIOPH RES CO, V267, P709, DOI 10.1006/bbrc.1999.2023
   di Barletta MR, 2000, AM J HUM GENET, V66, P1407, DOI 10.1086/302869
   DRAETTA G, 1990, TRENDS BIOCHEM SCI, V15, P378, DOI 10.1016/0968-0004(90)90235-4
   EMERY AEH, 1989, J MED GENET, V26, P637, DOI 10.1136/jmg.26.10.637
   Fairley EAL, 1999, J CELL SCI, V112, P2571
   Fatkin D, 1999, NEW ENGL J MED, V341, P1715, DOI 10.1056/NEJM199912023412302
   Felice KJ, 2000, NEUROLOGY, V55, P275, DOI 10.1212/WNL.55.2.275
   FISHER DZ, 1986, P NATL ACAD SCI USA, V83, P6450, DOI 10.1073/pnas.83.17.6450
   FUCHS E, 1994, ANNU REV BIOCHEM, V63, P345, DOI 10.1146/annurev.bi.63.070194.002021
   Furukawa K, 1998, J BIOL CHEM, V273, P4213, DOI 10.1074/jbc.273.7.4213
   GLASS CA, 1993, EMBO J, V12, P4413, DOI 10.1002/j.1460-2075.1993.tb06126.x
   HEALD R, 1990, CELL, V61, P579, DOI 10.1016/0092-8674(90)90470-Y
   HOGER TH, 1991, EXP CELL RES, V197, P280, DOI 10.1016/0014-4827(91)90434-V
   LIN F, 1993, J BIOL CHEM, V268, P16321
   LUTZ RJ, 1992, P NATL ACAD SCI USA, V89, P3000, DOI 10.1073/pnas.89.7.3000
   Manilal S, 1998, HUM MOL GENET, V7, P855, DOI 10.1093/hmg/7.5.855
   Manilal S, 1996, HUM MOL GENET, V5, P801, DOI 10.1093/hmg/5.6.801
   MCCORMICK MB, 1993, J CELL BIOL, V122, P395, DOI 10.1083/jcb.122.2.395
   MCKEON FD, 1986, NATURE, V319, P463, DOI 10.1038/319463a0
   Morris GE, 1999, HUM MOL GENET, V8, P1847, DOI 10.1093/hmg/8.10.1847
   Muchir A, 2000, HUM MOL GENET, V9, P1453, DOI 10.1093/hmg/9.9.1453
   Nagano A, 1996, NAT GENET, V12, P254, DOI 10.1038/ng0396-254
   Nigg E A, 1992, Semin Cell Biol, V3, P245, DOI 10.1016/1043-4682(92)90026-R
   Parry DAD, 1995, INTERMEDIATE FILAMEN
   PETER M, 1990, CELL, V61, P591, DOI 10.1016/0092-8674(90)90471-P
   Shackleton S, 2000, NAT GENET, V24, P153, DOI 10.1038/72807
   Speckman RA, 2000, AM J HUM GENET, V67, P388
   Speckman RA, 2000, AM J HUM GENET, V66, P1192, DOI 10.1086/302836
   Stuurman N, 1996, J STRUCT BIOL, V117, P1, DOI 10.1006/jsbi.1996.0064
   Stuurman N, 1998, J STRUCT BIOL, V122, P42, DOI 10.1006/jsbi.1998.3987
   TANIURA H, 1995, J CELL BIOL, V131, P33, DOI 10.1083/jcb.131.1.33
   WEBER K, 1989, FEBS LETT, V257, P411, DOI 10.1016/0014-5793(89)81584-4
   WORMAN HJ, 1990, J CELL BIOL, V111, P1535, DOI 10.1083/jcb.111.4.1535
   Wydner KL, 1996, GENOMICS, V32, P474, DOI 10.1006/geno.1996.0146
   Yates JRW, 1999, NEUROMUSCULAR DISORD, V9, P199, DOI 10.1016/S0960-8966(98)00095-9
NR 42
TC 94
Z9 102
U1 0
U2 1
PU WILEY-LISS
PI HOBOKEN
PA DIV JOHN WILEY & SONS INC, 111 RIVER ST, HOBOKEN, NJ 07030 USA
SN 0148-7299
EI 1096-8628
J9 AM J MED GENET
JI Am. J. Med. Genet.
PD SEP 1
PY 2001
VL 102
IS 4
BP 359
EP 367
DI 10.1002/ajmg.1463
PG 9
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA 465XQ
UT WOS:000170615600010
PM 11503164
DA 2025-04-10
ER

PT J
AU Brodowski, L
   Schröder-Heurich, B
   von Hardenberg, S
   Richter, K
   von Kaisenberg, CS
   Dittrich-Breiholz, O
   Meyer, N
   Dörk, T
   von Versen-Höynck, F
AF Brodowski, Lars
   Schroeder-Heurich, Bianca
   von Hardenberg, Sandra
   Richter, Katja
   von Kaisenberg, Constantin S.
   Dittrich-Breiholz, Oliver
   Meyer, Nadia
   Doerk, Thilo
   von Versen-Hoeynck, Frauke
TI MicroRNA Profiles of Maternal and Neonatal Endothelial Progenitor Cells
   in Preeclampsia
SO INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
LA English
DT Article
DE preeclampsia; cardiovascular morbidity; endothelial progenitor cells;
   miRNA; hsa-miR-1270
ID HYPERTENSIVE DISORDERS; EXPRESSION; PREGNANCY; DISEASE; WOMEN; DICER;
   RISK; PROLIFERATION; ANGIOGENESIS; PLACENTA
AB Preeclampsia is associated with an increased cardiovascular morbidity of mother and offspring, thus contributing to a substantial burden in women and children's health. It has been proven that endothelial progenitor cell (EPC) numbers and functional characteristics are impaired in cardiovascular disease and preeclampsia, although causative factors for the latter have remained elusive. MicroRNA (miRNA) modifications are a potential mechanism through which exposure to an altered environment translates into the development of chronic disease. In this study, we examined whether development of preeclampsia corresponds to alterations of miRNAs in maternal- and cord-blood-derived EPC. To test this end, we analyzed maternal and neonatal miRNAs via RNA sequencing from endothelial cells of preeclamptic and healthy controls in different cell culture passages. We were able to demonstrate differentially represented miRNAs in all groups. Hsa-miR-1270 showed significantly different levels in cord blood EPC from preeclampsia versus control and was negatively correlated with mRNA levels of its predicted targets ANGPTL7 and TFRC. Transfection with an hsa-miR-1270 inhibitor decreased the tube formation capacity and chemotactic motility but did not change proliferation in vitro. Target predictions and gene set enrichment analyses identified alternative splicing as a significantly enriched pathway for hsa-miR-1270. The top miRNAs in three other groups were predicted to target transcriptional and developmental pathways. Here, we showed for the first time significantly different levels of miRNAs and differently represented mRNA levels of predicted target genes in EPC derived from preeclampsia. Understanding the effects of preeclampsia on the epigenetic mechanisms of EPC will be crucial and may provide initial insights for further evaluation of the benefits of therapies targeting this cell population.
C1 [Brodowski, Lars; Schroeder-Heurich, Bianca; von Hardenberg, Sandra; Richter, Katja; Meyer, Nadia; Doerk, Thilo; von Versen-Hoeynck, Frauke] Hannover Med Sch, Gynecol Res Unit, Carl Neuberg Str 1, D-30625 Hannover, Germany.
   [von Kaisenberg, Constantin S.; von Versen-Hoeynck, Frauke] Hannover Med Sch, Dept Obstet & Gynecol, Carl Neuberg Str 1, D-30625 Hannover, Germany.
   [Dittrich-Breiholz, Oliver] Hannover Med Sch, Res Core Unit Genom, Carl Neuberg Str 1, D-30625 Hannover, Germany.
C3 Hannover Medical School; Hannover Medical School; Hannover Medical
   School
RP von Versen-Höynck, F (corresponding author), Hannover Med Sch, Gynecol Res Unit, Carl Neuberg Str 1, D-30625 Hannover, Germany.; von Versen-Höynck, F (corresponding author), Hannover Med Sch, Dept Obstet & Gynecol, Carl Neuberg Str 1, D-30625 Hannover, Germany.
EM Brodowski.Lars@mh-hannover.de; Schroeder-Heurich.Bianca@mh-hannover.de;
   vonHardenberg.Sandra@mh-hannover.de; Richter.Katja@mh-hannover.de;
   vonKaisenberg.Constantin@mh-hannover.de; Dittrich.Oliver@mh-hannover.de;
   Meyer.Nadia@mh-hannover.de; Doerk.Thilo@mh-hannover.de;
   vonVersen-Hoeynck.Frauke@mh-hannover.de
RI von Versen-Höynck, Frauke/H-3719-2019; von Kaisenberg,
   Constantin/AAR-2756-2021; Dork, Thilo/J-8620-2012; von Versen-Hoynck,
   Frauke/P-7160-2017
OI Dork, Thilo/0000-0002-9458-0282; von Versen-Hoynck,
   Frauke/0000-0002-1924-5695; Schroder-Heurich, Bianca/0000-0002-5996-2373
FU Boehringer Ingelheim Foundation; German Research Foundation [DFG VE
   490/15-1, DO 761/17-1]; German Research Foundation (DFG); Open Access
   Publication Fond of Hannover Medical School (MHH)
FX This research was funded by The Boehringer Ingelheim Foundation with an
   Exploration Grant to Frauke von Versen-Hoynck and a grant by the German
   Research Foundation to Frauke von Versen-Hoynck (DFG VE 490/15-1) and
   Thilo Dork (DO 761/17-1). We acknowledge support by the German Research
   Foundation (DFG) and the Open Access Publication Fond of Hannover
   Medical School (MHH).
CR Ackerman W, 2016, AM J OBSTET GYNECOL, V214, pS261, DOI 10.1016/j.ajog.2015.10.520
   Agarwal V, 2015, ELIFE, V4, DOI 10.7554/eLife.05005
   Ambros V, 2004, NATURE, V431, P350, DOI 10.1038/nature02871
   Apicella C, 2019, INT J MOL SCI, V20, DOI 10.3390/ijms20112837
   Asahara T, 1997, SCIENCE, V275, P964, DOI 10.1126/science.275.5302.964
   Baker CD, 2012, EUR RESPIR J, V40, P1516, DOI 10.1183/09031936.00017312
   Beavers KR, 2015, ADV DRUG DELIVER REV, V88, P123, DOI 10.1016/j.addr.2014.12.006
   Blake JA, 2015, NUCLEIC ACIDS RES, V43, pD1049, DOI 10.1093/nar/gku1179
   Brennan GP, 2018, PLOS ONE, V13, DOI 10.1371/journal.pone.0207952
   Brodowski L, 2019, FRONT CELL DEV BIOL, V7, DOI [10.3389/fceil.2019.00032, 10.3389/fcell.2019.00032]
   Brown MC, 2013, EUR J EPIDEMIOL, V28, P1, DOI 10.1007/s10654-013-9762-6
   Carmeliet P, 2005, NATURE, V438, P932, DOI 10.1038/nature04478
   Carmeliet P, 2003, NAT MED, V9, P653, DOI 10.1038/nm0603-653
   Colpaert RMW, 2019, CELLS-BASEL, V8, DOI 10.3390/cells8070737
   Comes N, 2011, GENES CELLS, V16, P243, DOI 10.1111/j.1365-2443.2010.01483.x
   Davis EF, 2012, PEDIATRICS, V129, pE1552, DOI 10.1542/peds.2011-3093
   El-Gebali S, 2019, NUCLEIC ACIDS RES, V47, pD427, DOI 10.1093/nar/gky995
   Enquobahrie DA, 2011, AM J OBSTET GYNECOL, V204, DOI 10.1016/j.ajog.2010.09.004
   Fraser A, 2013, HYPERTENSION, V62, P614, DOI 10.1161/HYPERTENSIONAHA.113.01513
   Grundmann M, 2012, AM J PHYSIOL-CELL PH, V303, pC954, DOI 10.1152/ajpcell.00030.2012
   Gunel T, 2011, GENET MOL RES, V10, P4034, DOI 10.4238/2011.November.8.5
   Hromadnikova I, 2013, MEDIAT INFLAMM, V2013, DOI 10.1155/2013/186041
   Hromadnikova I, 2012, J MOL DIAGN, V14, P160, DOI 10.1016/j.jmoldx.2011.11.003
   Kanehisa M, 2019, NUCLEIC ACIDS RES, V47, pD590, DOI 10.1093/nar/gky962
   Khatun R, 2003, PLACENTA, V24, P870, DOI 10.1016/S0143-4004(03)00138-3
   Khoo CP, 2017, SCI REP-UK, V7, DOI 10.1038/srep44137
   King Thomas F J, 2014, J Stem Cells, V9, P93, DOI jsc.2014.9.2.93
   Kuehbacher A, 2007, CIRC RES, V101, P59, DOI 10.1161/CIRCRESAHA.107.153916
   Lin C, 2009, AM J HYPERTENS, V22, P1014, DOI 10.1038/ajh.2009.101
   Liu K, 2019, J CELL PHYSIOL, V234, P11380, DOI 10.1002/jcp.27795
   Luppi P, 2010, REPROD SCI, V17, P643, DOI 10.1177/1933719110366164
   Lv Y, 2019, J CELL PHYSIOL, V234, P1052, DOI 10.1002/jcp.27291
   Mellis D, 2018, BIOCHEM SOC T, V46, P11, DOI 10.1042/BST20170037
   Palmer KR, 2017, MOL HUM REPROD, V23, P69, DOI 10.1093/molehr/gaw077
   Powers RW, 2008, REPROD SCI, V15, P374, DOI 10.1177/1933719107311780
   Rosenfeld N, 2008, NAT BIOTECHNOL, V26, P462, DOI 10.1038/nbt1392
   Santulli G, 2016, J CELL PHYSIOL, V231, P1638, DOI 10.1002/jcp.25276
   Schmidt-Lucke C, 2005, CIRCULATION, V111, P2981, DOI 10.1161/CIRCULATIONAHA.104.504340
   Schröder-Heurich B, 2019, FASEB J, V33, P9142, DOI 10.1096/fj.201802750RR
   Stojanovska V, 2016, BIOL REPROD, V94, DOI 10.1095/biolreprod.115.135780
   Suárez Y, 2008, P NATL ACAD SCI USA, V105, P14082, DOI 10.1073/pnas.0804597105
   Suárez Y, 2007, CIRC RES, V100, P1164, DOI 10.1161/01.RES.0000265065.26744.17
   Szklarczyk D, 2019, NUCLEIC ACIDS RES, V47, pD607, DOI [10.1093/nar/gky1131, 10.1093/nar/gkac1000]
   Takahashi Y, 2010, CLIN SCI, V119, P395, DOI 10.1042/CS20100003
   Tranquilli AL, 2014, PREGNANCY HYPERTENS, V4, P97, DOI 10.1016/j.preghy.2014.02.001
   Van Craenenbroeck AH, 2016, ANN TRANSL MED, V4, DOI 10.21037/atm.2016.12.34
   von Versen-Höynck F, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0098990
   Wei L, 2019, ONCOTARGETS THER, V12, P4839, DOI 10.2147/OTT.S192521
   Werner N, 2005, NEW ENGL J MED, V353, P999, DOI 10.1056/NEJMoa043814
   Xiang W, 2005, INT J GYNECOL OBSTET, V89, P103, DOI 10.1016/j.ijgo.2004.12.041
   Yang Q, 2011, CLIN CHIM ACTA, V412, P2167, DOI 10.1016/j.cca.2011.07.029
   Yi TB, 2019, BIOMED PHARMACOTHER, V109, P2357, DOI 10.1016/j.biopha.2018.08.150
   Zhang Y, 2012, J CELL MOL MED, V16, P249, DOI 10.1111/j.1582-4934.2011.01291.x
   Zhao GF, 2014, J BIOMED SCI, V21, DOI 10.1186/s12929-014-0081-3
NR 54
TC 16
Z9 16
U1 1
U2 4
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
SN 1661-6596
EI 1422-0067
J9 INT J MOL SCI
JI Int. J. Mol. Sci.
PD MAY
PY 2021
VL 22
IS 10
AR 5320
DI 10.3390/ijms22105320
PG 20
WC Biochemistry & Molecular Biology; Chemistry, Multidisciplinary
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Chemistry
GA SS8KC
UT WOS:000662000500001
PM 34070163
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Chen, SY
   Nunez, S
   Reilly, MP
   Foulkes, AS
AF Chen, Siying
   Nunez, Sara
   Reilly, Muredach P.
   Foulkes, Andrea S.
TI Bayesian variable selection for post-analytic interrogation of
   susceptibility loci
SO BIOMETRICS
LA English
DT Article
DE Bayesian variable selection (BVS); Genome-wide association studies
   (GWAS); Long non-coding RNAs (lncRNAs); Protein coding gene-level
   testing; Regulatory elements; Spike and slab prior
ID GENOME-WIDE ASSOCIATION; RARE VARIANTS; ENRICHMENT ANALYSIS; GENE;
   METAANALYSIS; EVOLUTION; PRIORS; LASSO
AB Understanding the complex interplay among protein coding genes and regulatory elements requires rigorous interrogation with analytic tools designed for discerning the relative contributions of overlapping genomic regions. To this aim, we offer a novel application of Bayesian variable selection (BVS) for classifying genomic class level associations using existing large meta-analysis summary level resources. This approach is applied using the expectation maximization variable selection (EMVS) algorithm to typed and imputed SNPs across 502 protein coding genes (PCGs) and 220 long intergenic non-coding RNAs (lncRNAs) that overlap 45 known loci for coronary artery disease (CAD) using publicly available Global Lipids Gentics Consortium (GLGC) (Teslovich et al., 2010; Willer et al., 2013) meta-analysis summary statistics for low-density lipoprotein cholesterol (LDL-C). The analysis reveals 33 PCGs and three lncRNAs across 11 loci with >50% posterior probabilities for inclusion in an additive model of association. The findings are consistent with previous reports, while providing some new insight into the architecture of LDL-cholesterol to be investigated further. As genomic taxonomies continue to evolve, additional classes such as enhancer elements and splicing regions, can easily be layered into the proposed analysis framework. Moreover, application of this approach to alternative publicly available meta-analysis resources, or more generally as a post-analytic strategy to further interrogate regions that are identified through single point analysis, is straightforward. All coding examples are implemented in R version 3.2.1 and provided as supplemental material.
C1 [Chen, Siying; Nunez, Sara; Foulkes, Andrea S.] Mt Holyoke Coll, Dept Math & Stat, S Hadley, MA 01075 USA.
   [Reilly, Muredach P.] Columbia Univ, Dept Med, Div Cardiol, New York, NY USA.
   [Reilly, Muredach P.] Columbia Univ, Irving Inst Clin & Translat Res, New York, NY USA.
C3 Mount Holyoke College; Columbia University; Columbia University
RP Foulkes, AS (corresponding author), Mt Holyoke Coll, Dept Math & Stat, S Hadley, MA 01075 USA.
EM afoulkes@mtholyoke.edu
RI Chen, Siying/IUP-2697-2023
OI Reilly, Muredach/0000-0002-3035-9386
FU NHLBI [R01-HL107196, K24-HL107643, R01-HL113147]
FX The authors thank Ed George and Veronika Rockova for helpful discussions
   and providing the R code for the EMVS algorithm. Support for this
   research was provided by NHLBI R01-HL107196 (SC, SN, MPR, and ASF);
   K24-HL107643 (MPR); and R01-HL113147 (MPR).
CR [Anonymous], BAYESIAN ANAL TBA
   Bauer RC, 2015, J CLIN INVEST, V125, P3809, DOI 10.1172/JCI77095
   Beasley TM, 2009, BEHAV GENET, V39, P580, DOI 10.1007/s10519-009-9281-0
   Cabili MN, 2011, GENE DEV, V25, P1915, DOI 10.1101/gad.17446611
   Crosby J, 2014, NEW ENGL J MED, V371, P22, DOI 10.1056/NEJMoa1307095
   Deloukas P, 2013, NAT GENET, V45, P25, DOI 10.1038/ng.2480
   Derrien T, 2012, GENOME RES, V22, P1775, DOI 10.1101/gr.132159.111
   Do R, 2015, NATURE, V518, P102, DOI 10.1038/nature13917
   Douvris A, 2014, J AM HEART ASSOC, V3, DOI 10.1161/JAHA.114.000884
   Foulkes AS, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0054812
   GEORGE EI, 1993, J AM STAT ASSOC, V88, P881, DOI 10.2307/2290777
   Hernández-Lobato D, 2013, J MACH LEARN RES, V14, P1891
   Hu YJ, 2013, AM J HUM GENET, V93, P236, DOI 10.1016/j.ajhg.2013.06.011
   Huang HL, 2011, PLOS GENET, V7, DOI 10.1371/journal.pgen.1002177
   Laurie CC, 2010, GENET EPIDEMIOL, V34, P591, DOI 10.1002/gepi.20516
   Lee S, 2013, AM J HUM GENET, V93, P42, DOI 10.1016/j.ajhg.2013.05.010
   Li BS, 2008, AM J HUM GENET, V83, P311, DOI 10.1016/j.ajhg.2008.06.024
   Li F, 2010, J AM STAT ASSOC, V105, P1202, DOI 10.1198/jasa.2010.tm08177
   Li JH, 2015, ANN APPL STAT, V9, P640, DOI 10.1214/15-AOAS808
   Li MX, 2011, AM J HUM GENET, V88, P283, DOI 10.1016/j.ajhg.2011.01.019
   Liu DJJ, 2014, NAT GENET, V46, P200, DOI 10.1038/ng.2852
   Liu JZ, 2010, AM J HUM GENET, V87, P139, DOI 10.1016/j.ajhg.2010.06.009
   Liu J, 2013, BIOSTATISTICS, V14, P205, DOI 10.1093/biostatistics/kxs034
   Luo L, 2010, EUR J HUM GENET, V18, P1045, DOI 10.1038/ejhg.2010.62
   Peltola T, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0049445
   Peltola T, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0029115
   Peng B, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0067672
   Peng G, 2010, EUR J HUM GENET, V18, P111, DOI 10.1038/ejhg.2009.115
   Qian J, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0148218
   Reed E, 2015, STAT MED, V34, P3769, DOI 10.1002/sim.6605
   Reilly MP, 2011, LANCET, V377, P383, DOI 10.1016/S0140-6736(10)61996-4
   Rocková V, 2014, METRON, V72, P217, DOI 10.1007/s40300-014-0047-y
   Rocková V, 2014, J AM STAT ASSOC, V109, P828, DOI 10.1080/01621459.2013.869223
   Rosenbloom KR, 2015, NUCLEIC ACIDS RES, V43, pD670, DOI 10.1093/nar/gku1177
   Schunkert H, 2011, NAT GENET, V43, P333, DOI [10.1038/ng.784, 10.1161/CIRCGENETICS.111.960443]
   Schurink Anouk, 2012, BMC Proc, V6 Suppl 2, pS8, DOI 10.1186/1753-6561-6-S2-S8
   Segrè AV, 2010, PLOS GENET, V6, DOI 10.1371/journal.pgen.1001058
   Strong A, 2014, CURR OPIN LIPIDOL, V25, P350, DOI 10.1097/MOL.0000000000000110
   Subramanian A, 2005, P NATL ACAD SCI USA, V102, P15545, DOI 10.1073/pnas.0506580102
   Teslovich TM, 2010, NATURE, V466, P707, DOI 10.1038/nature09270
   Ulitsky I, 2013, CELL, V154, P26, DOI 10.1016/j.cell.2013.06.020
   Valdar W, 2012, GENET EPIDEMIOL, V36, P451, DOI 10.1002/gepi.21639
   Weng LJ, 2011, BMC BIOINFORMATICS, V12, DOI 10.1186/1471-2105-12-99
   Willer CJ, 2013, NAT GENET, V45, P1274, DOI 10.1038/ng.2797
   Wu MC, 2011, AM J HUM GENET, V89, P82, DOI 10.1016/j.ajhg.2011.05.029
   Wu MC, 2010, AM J HUM GENET, V86, P929, DOI 10.1016/j.ajhg.2010.05.002
   Zhang L, 2014, J R STAT SOC C-APPL, V63, P595, DOI 10.1111/rssc.12053
   Zhang XS, 2014, BMC GENET, V15, DOI 10.1186/s12863-014-0130-7
NR 48
TC 2
Z9 2
U1 0
U2 10
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0006-341X
EI 1541-0420
J9 BIOMETRICS
JI Biometrics
PD JUN
PY 2017
VL 73
IS 2
BP 603
EP 614
DI 10.1111/biom.12620
PG 12
WC Biology; Mathematical & Computational Biology; Statistics & Probability
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Life Sciences & Biomedicine - Other Topics; Mathematical & Computational
   Biology; Mathematics
GA EX8DG
UT WOS:000403478400023
PM 27858978
OA Green Submitted
DA 2025-04-10
ER

PT J
AU Miller, BM
   Bloemink, MJ
   Nyitrai, M
   Bernstein, SI
   Geeves, MA
AF Miller, Becky M.
   Bloemink, Marieke J.
   Nyitrai, Miklos
   Bernstein, Sanford I.
   Geeves, Michael A.
TI A variable domain near the ATP-binding site in Drosophila muscle
   myosin is part of the communication pathway between the nucleotide and
   actin-binding sites
SO JOURNAL OF MOLECULAR BIOLOGY
LA English
DT Article
DE muscle; myosin; Drosophila; kinetics; nucleotides
ID N-TERMINAL REGIONS; HEAVY-CHAIN GENE; HYPERTROPHIC CARDIOMYOPATHY;
   MICROGRAM QUANTITIES; ALTERNATIVE DOMAIN; FUNCTIONAL DOMAINS;
   SKELETAL-MUSCLE; SWISS-MODEL; ADP RELEASE; ACTOMYOSIN
AB Drosophila expresses several muscle myosin isoforms from a single gene by alternatively splicing six of the 19 exons. Here we investigate exon 7, which codes for a region in the upper 50 kDa domain near the nucleotide-binding pocket. This region is of interest because it is also the place where a large insert is found in myosin VI and where several cardiomyopathy mutations have been identified in human cardiac myosin. We expressed and purified chimeric muscle myosins from Drosophila, each varying at exon 7. Two chimeras exchanged the entire exon 7 domain between the indirect flight muscle (IFI, normally containing exon 7d) and embryonic body wall muscle (EMB, normally containing exon 7a) isoforms to create IFT-7a and EMB-7d. The second two chimeras replaced each half of the exon 7a domain in EMB with the corresponding portion of exon 7d to create EMB-7a/7d and EMB7d/7a. Transient kinetic studies of the motor domain from these myosin isoforms revealed changes in several kinetic parameters between the IFI or EMB isoforms and the chimeras. Of significance were changes in nucleotide binding, which differed in the presence and absence of actin, consistent with a model in which the exon 7 domain is part of the communication pathway between the nucleotide and actin-binding sites. Homology models of the structures suggest how the exon 7 domain might modulate this pathway. (c) 2007 Elsevier Ltd. All rights reserved.
C1 Univ Kent, Dept Biosci, Canterbury CT2 7NJ, Kent, England.
   San Diego State Univ, Dept Biol, San Diego, CA 92182 USA.
   San Diego State Univ, Inst Mol Biol, San Diego, CA 92182 USA.
C3 University of Kent; California State University System; San Diego State
   University; California State University System; San Diego State
   University
RP Geeves, MA (corresponding author), Univ Kent, Dept Biosci, Canterbury CT2 7NJ, Kent, England.
EM m.a.geeves@kent.ac.uk
RI Geeves, Michael/F-7583-2011
OI Bernstein, Sanford/0000-0001-7094-5390; Geeves,
   Michael/0000-0002-9364-8898; Nyitrai, Miklos/0000-0002-6229-4337;
   Bloemink, Marieke Johanna/0000-0001-9441-2783
FU NIGMS NIH HHS [GM32443, R37 GM032443, R01 GM032443] Funding Source:
   Medline; Wellcome Trust [079003, 070021] Funding Source: Medline
CR Arnold K, 2006, BIOINFORMATICS, V22, P195, DOI 10.1093/bioinformatics/bti770
   BARANY M, 1967, J GEN PHYSIOL, V50, P197, DOI 10.1085/jgp.50.6.197
   BERNSTEIN SI, 1983, NATURE, V302, P393, DOI 10.1038/302393a0
   Clark RJ, 2003, J MUSCLE RES CELL M, V24, P315
   COLLIER VL, 1990, GENE DEV, V4, P885, DOI 10.1101/gad.4.6.885
   Conibear PB, 2003, NAT STRUCT BIOL, V10, P831, DOI 10.1038/nsb986
   Cope MJTV, 1996, STRUCTURE, V4, P969, DOI 10.1016/S0969-2126(96)00103-7
   Cremo CR, 1998, BIOCHEMISTRY-US, V37, P1969, DOI 10.1021/bi9722406
   CRIPPS RM, 1994, J CELL BIOL, V126, P689, DOI 10.1083/jcb.126.3.689
   Geeves MA, 1999, ANNU REV BIOCHEM, V68, P687, DOI 10.1146/annurev.biochem.68.1.687
   Geeves MA, 2005, CELL MOL LIFE SCI, V62, P1462, DOI 10.1007/s00018-005-5015-5
   GEORGE EL, 1989, MOL CELL BIOL, V9, P2957, DOI 10.1128/MCB.9.7.2957
   HAMRELL BB, 1978, PFLUG ARCH EUR J PHY, V377, P119, DOI 10.1007/BF00582841
   HASTINGS GA, 1991, J CELL BIOL, V114, P263, DOI 10.1083/jcb.114.2.263
   Havndrup O, 2003, CARDIOVASC RES, V57, P347, DOI 10.1016/S0008-6363(02)00711-3
   Holmes KC, 2003, NATURE, V425, P423, DOI 10.1038/nature02005
   Hooft RWW, 1996, NATURE, V381, P272, DOI 10.1038/381272a0
   Littlefield KP, 2003, AM J PHYSIOL-CELL PH, V284, pC1031, DOI 10.1152/ajpcell.00474.2002
   Lutz GJ, 2000, MICROSC RES TECHNIQ, V50, P443, DOI 10.1002/1097-0029(20000915)50:6<443::AID-JEMT3>3.0.CO;2-5
   MARGOSSIAN SS, 1982, METHOD ENZYMOL, V85, P55
   Ménétrey J, 2005, NATURE, V435, P779, DOI 10.1038/nature03592
   Miller BM, 2005, J MOL BIOL, V353, P14, DOI 10.1016/j.jmb.2005.08.012
   Miller BM, 2003, J BIOL CHEM, V278, P50293, DOI 10.1074/jbc.M308318200
   PARDEE JD, 1982, METHOD ENZYMOL, V85, P164
   Risal D, 2004, P NATL ACAD SCI USA, V101, P8930, DOI 10.1073/pnas.0403002101
   RUBIN GM, 1982, SCIENCE, V218, P348, DOI 10.1126/science.6289436
   Schwede T, 2003, NUCLEIC ACIDS RES, V31, P3381, DOI 10.1093/nar/gkg520
   SPUDICH JA, 1971, J BIOL CHEM, V246, P4866
   Swank DM, 2006, BIOPHYS J, V90, P2427, DOI 10.1529/biophysj.105.075184
   Swank DM, 2004, BIOPHYS J, V87, P1805, DOI 10.1529/biophysj.103.032078
   Swank DM, 2003, J BIOL CHEM, V278, P17475, DOI 10.1074/jbc.M212727200
   Swank DM, 2002, NAT CELL BIOL, V4, P312, DOI 10.1038/ncb776
   Swank DM, 2001, J BIOL CHEM, V276, P15117, DOI 10.1074/jbc.M008379200
   Swank DM, 2006, P NATL ACAD SCI USA, V103, P17543, DOI 10.1073/pnas.0604972103
   Tyska MJ, 2002, CELL MOTIL CYTOSKEL, V51, P1, DOI 10.1002/cm.10014
   Van Driest SL, 2004, J AM COLL CARDIOL, V44, P602, DOI 10.1016/j.jacc.2004.04.039
   Volkmann N, 2003, P NATL ACAD SCI USA, V100, P3227, DOI 10.1073/pnas.0536510100
   Volkmann N, 2000, NAT STRUCT BIOL, V7, P1147
   Webb MR, 2001, BIOPHYS J, V81, P1562, DOI 10.1016/S0006-3495(01)75810-9
   Weiss S, 2000, J MUSCLE RES CELL M, V21, P423, DOI 10.1023/A:1005690106951
   Wells L, 1996, EMBO J, V15, P4454, DOI 10.1002/j.1460-2075.1996.tb00822.x
   WEST JJ, 1967, J BIOL CHEM, V242, P1140
   Yu B, 2005, J CLIN PATHOL, V58, P479, DOI 10.1136/jcp.2004.021642
   Zhang SX, 2001, MECH DEVELOP, V101, P35, DOI 10.1016/S0925-4773(00)00549-9
NR 44
TC 23
Z9 25
U1 0
U2 5
PU ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
PI LONDON
PA 24-28 OVAL RD, LONDON NW1 7DX, ENGLAND
SN 0022-2836
EI 1089-8638
J9 J MOL BIOL
JI J. Mol. Biol.
PD MAY 11
PY 2007
VL 368
IS 4
BP 1051
EP 1066
DI 10.1016/j.jmb.2007.02.042
PG 16
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 164WJ
UT WOS:000246265200011
PM 17379245
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Lipkin, SM
   Chao, EC
   Moreno, V
   Rozek, LS
   Rennert, H
   Pinchev, M
   Dizon, D
   Rennert, G
   Kopelovich, L
   Gruber, SB
AF Lipkin, Steven M.
   Chao, Elizabeth C.
   Moreno, Victor
   Rozek, Laura S.
   Rennert, Hedy
   Pinchev, Mila
   Dizon, Diana
   Rennert, Gad
   Kopelovich, Levy
   Gruber, Stephen B.
TI Genetic Variation in 3-Hydroxy-3-Methylglutaryl CoA Reductase Modifies
   the Chemopreventive Activity of Statins for Colorectal Cancer
SO CANCER PREVENTION RESEARCH
LA English
DT Article
ID COENZYME-A REDUCTASE; LIPOPROTEIN CHOLESTEROL RESPONSE; INDUCED
   APOPTOSIS; RISK; COMBINATION; INHIBITOR; SIMVASTATIN; PRAVASTATIN;
   CARCINOMA; CELLS
AB Genetic variation in 3-hydroxy-3-methylglutaryl CoA reductase (HMGCR), the rate-limiting enzyme in cholesterol synthesis, modifies the effect of statins on serum cholesterol levels. Long-term use of statins is associated with a reduced risk of colorectal cancer (CRC) in some, but not all, studies. We genotyped variants in 40 candidate genes important for cholesterol synthesis and metabolism in a population-based case-control study of CRC involving 2,138 incident cases and 2,049 population-based controls. We identified a single-nucleotide polymorphism in the HMGCR gene that significantly modified the protective association between statins and CRC risk. Compared with nonusers, the unadjusted odds ratio of CRC among statin users with the A/A genotype of rs12654264 in HMGCR was 0.3 (95% confidence interval, 0.18-0.51) and among statin users with the T/T genotype was 0.66 (95% confidence interval, 0.41-1.06; P-interaction = 0.0012). This genetic variant (A/A genotype of rs12654264) also was associated with lower serum levels of low-density lipoprotein among all cases and controls. In colon cancer cell lines, the reduction in cholesterol levels after statin treatment was substantially stronger in cells carrying the A/A genotype, and this difference was related to alternative splicing involving the HMGCR statin-binding domain. We anticipate that these data may advance the development of personalized statin use for reducing the risk of cancer as well as cardiovascular disease among the approximately 25 million people currently using statins worldwide. Cancer Prev Res; 3(5); 597-603. (C) 2010 AACR.
C1 [Lipkin, Steven M.] Weill Cornell Sch Med, Dept Med, New York, NY USA.
   [Chao, Elizabeth C.; Dizon, Diana] Univ Calif Irvine, Dept Med, Irvine, CA 92717 USA.
   [Moreno, Victor; Rozek, Laura S.; Gruber, Stephen B.] Univ Michigan, Dept Internal Med, Ann Arbor, MI 48109 USA.
   [Moreno, Victor; Gruber, Stephen B.] Univ Michigan, Dept Epidemiol, Ann Arbor, MI 48109 USA.
   [Rozek, Laura S.] Univ Michigan, Dept Environm Hlth Sci, Ann Arbor, MI 48109 USA.
   [Gruber, Stephen B.] Univ Michigan, Dept Human Genet, Ann Arbor, MI 48109 USA.
   [Moreno, Victor] ICO, IDIBELL, Barcelona, Spain.
   [Moreno, Victor] Univ Barcelona, Barcelona, Spain.
   [Rennert, Hedy; Pinchev, Mila; Rennert, Gad] Technion Israel Inst Technol, Clalit Hlth Serv Natl Canc Control Ctr, Haifa, Israel.
   [Rennert, Hedy; Pinchev, Mila; Rennert, Gad] Technion Israel Inst Technol, Dept Community Med & Epidemiol, Carmel Med Ctr, Haifa, Israel.
   [Rennert, Hedy; Pinchev, Mila; Rennert, Gad] Technion Israel Inst Technol, Bruce Rappaport Fac Med, IL-31096 Haifa, Israel.
   [Kopelovich, Levy] NCI, Canc Prevent Div, Rockville, MD USA.
C3 Cornell University; University of California System; University of
   California Irvine; University of Michigan System; University of
   Michigan; University of Michigan System; University of Michigan;
   University of Michigan System; University of Michigan; University of
   Michigan System; University of Michigan; Institut d'Investigacio
   Biomedica de Bellvitge (IDIBELL); University of Barcelona; University of
   Barcelona; Technion Israel Institute of Technology; Clalit Health
   Services; Clalit Health Services; Carmel Medical Center; Technion Israel
   Institute of Technology; Technion Israel Institute of Technology;
   Rappaport Faculty of Medicine; National Institutes of Health (NIH) -
   USA; NIH National Cancer Institute (NCI)
RP Lipkin, SM (corresponding author), Weill Cornell Med Coll, Room 718 HSS, New York, NY 10021 USA.
EM stl2012@med.cornell.edu; sgruber@umich.edu
RI Moreno, Victor/A-1697-2010
OI Moreno, Victor/0000-0002-2818-5487; Rennert, Gad/0000-0002-8512-068X
FU National Cancer Institute [N01-CN43308, R01 CA81488]; University of
   Michigan Cancer Center [5 P30 CA46592]; Spanish Secretaria de Estado de
   Universidades e Investigacion [PR2006-0474]; Irving Weinstein and Ravitz
   Foundation; National Cancer Institute [P30CA046592] Funding Source: NIH
   RePORTER
FX National Cancer Institute grants N01-CN43308 (S. M. Lipkin) and R01
   CA81488 (S. B. Gruber), University of Michigan Cancer Center Support
   Grant 5 P30 CA46592, Spanish Secretaria de Estado de Universidades e
   Investigacion grant PR2006-0474 (V. Moreno), and the Irving Weinstein
   and Ravitz Foundation (S. B. Gruber).
CR Agarwal B, 1999, GASTROENTEROLOGY, V117, P838, DOI 10.1016/S0016-5085(99)70342-2
   Bonovas S, 2007, J CLIN ONCOL, V25, P3462, DOI 10.1200/JCO.2007.10.8936
   Burkhardt R, 2008, ARTERIOSCL THROM VAS, V28, P2078, DOI 10.1161/ATVBAHA.108.172288
   Chasman DI, 2004, JAMA-J AM MED ASSOC, V291, P2821, DOI 10.1001/jama.291.23.2821
   DEGROOT E, 1995, AM J CARDIOL, V76, pC40, DOI 10.1016/S0002-9149(99)80469-X
   Hachem C, 2009, AM J GASTROENTEROL, V104, P1241, DOI 10.1038/ajg.2009.64
   Hentosh P, 2001, MOL CARCINOGEN, V32, P154, DOI 10.1002/mc.1074
   Iakoubova OA, 2008, J AM COLL CARDIOL, V51, P449, DOI 10.1016/j.jacc.2007.10.017
   Jin ZY, 2002, CELL CYCLE, V1, P82, DOI 10.4161/cc.1.1.104
   Kaneko R, 2007, J BIOL CHEM, V282, P19273, DOI 10.1074/jbc.M610350200
   Kathiresan S, 2008, NEW ENGL J MED, V358, P1240, DOI 10.1056/NEJMoa0706728
   Krauss RM, 2008, CIRCULATION, V117, P1537, DOI 10.1161/CIRCULATIONAHA.107.708388
   LaRosa JC, 2000, JAMA-J AM MED ASSOC, V283, P2936
   Link E, 2008, NEW ENGL J MED, V359, P789, DOI 10.1056/NEJMoa0801936
   Lippman SM, 2009, CANCER RES, V69, P5269, DOI 10.1158/0008-5472.CAN-09-1750
   Manuel DG, 2006, BMJ-BRIT MED J, V332, P1419, DOI 10.1136/bmj.38849.487546.DE
   Medina MW, 2008, CIRCULATION, V118, P355, DOI 10.1161/CIRCULATIONAHA.108.773267
   Nübel T, 2004, FASEB J, V18, P140, DOI 10.1096/fj.03-0261fje
   Packham C, 1999, J PUBLIC HEALTH MED, V21, P60, DOI 10.1093/pubmed/21.1.60
   PIEGORSCH WW, 1994, STAT MED, V13, P153, DOI 10.1002/sim.4780130206
   Poynter JN, 2005, NEW ENGL J MED, V352, P2184, DOI 10.1056/NEJMoa043792
   Puccetti L, 2002, EUR J CLIN INVEST, V32, P901, DOI 10.1046/j.1365-2362.2002.01086.x
   Sacks FM, 1998, CIRCULATION, V97, P1446
   SHEAR CL, 1992, CIRCULATION, V85, P1293, DOI 10.1161/01.CIR.85.4.1293
   Singh H, 2009, AM J GASTROENTEROL, V104, P3015, DOI 10.1038/ajg.2009.574
   Solé X, 2006, BIOINFORMATICS, V22, P1928, DOI 10.1093/bioinformatics/btl268
   Swamy MV, 2006, CANCER RES, V66, P7370, DOI 10.1158/0008-5472.CAN-05-4619
   Swamy MV, 2002, INT J ONCOL, V20, P753
   van Hout BA, 2001, EUR HEART J, V22, P751, DOI 10.1053/euhj.2000.2308
   Wächtershäuser A, 2001, CARCINOGENESIS, V22, P1061, DOI 10.1093/carcin/22.7.1061
NR 30
TC 64
Z9 69
U1 0
U2 11
PU AMER ASSOC CANCER RESEARCH
PI PHILADELPHIA
PA 615 CHESTNUT ST, 17TH FLOOR, PHILADELPHIA, PA 19106-4404 USA
SN 1940-6207
EI 1940-6215
J9 CANCER PREV RES
JI Cancer Prev. Res.
PD MAY
PY 2010
VL 3
IS 5
BP 597
EP 603
DI 10.1158/1940-6207.CAPR-10-0007
PG 7
WC Oncology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Oncology
GA 591IP
UT WOS:000277294000005
PM 20403997
OA Green Submitted, Bronze
DA 2025-04-10
ER

PT J
AU Bone, WP
   Siewert, KM
   Jha, A
   Klarin, D
   Damrauer, SM
   Chang, KM
   Tsao, PS
   Assimes, TL
   Ritchie, MD
   Voight, BF
AF Bone, William P.
   Siewert, Katherine M.
   Jha, Anupama
   Klarin, Derek
   Damrauer, Scott M.
   Chang, Kyong-Mi
   Tsao, Philip S.
   Assimes, Themistocles L.
   Ritchie, Marylyn D.
   Voight, Benjamin F.
TI Multi-trait association studies discover pleiotropic loci between
   Alzheimer's disease and cardiometabolic traits
SO ALZHEIMERS RESEARCH & THERAPY
LA English
DT Article
DE Pleiotropy; Cardiometabolic traits; Multi-trait GWAS; Colocalization
ID ANGIOTENSIN-CONVERTING ENZYME; ACE; METAANALYSIS; IMMUNITY; HSV-1; RISK
AB Background Identification of genetic risk factors that are shared between Alzheimer's disease (AD) and other traits, i.e., pleiotropy, can help improve our understanding of the etiology of AD and potentially detect new therapeutic targets. Previous epidemiological correlations observed between cardiometabolic traits and AD led us to assess the pleiotropy between these traits. Methods We performed a set of bivariate genome-wide association studies coupled with colocalization analysis to identify loci that are shared between AD and eleven cardiometabolic traits. For each of these loci, we performed colocalization with Genotype-Tissue Expression (GTEx) project expression quantitative trait loci (eQTL) to identify candidate causal genes. Results We identified three previously unreported pleiotropic trait associations at known AD loci as well as four novel pleiotropic loci. One associated locus was tagged by a low-frequency coding variant in the gene DOCK4 and is potentially implicated in its alternative splicing. Colocalization with GTEx eQTL data identified additional candidate genes for the loci we detected, including ACE, the target of the hypertensive drug class of ACE inhibitors. We found that the allele associated with decreased ACE expression in brain tissue was also associated with increased risk of AD, providing human genetic evidence of a potential increase in AD risk from use of an established anti-hypertensive therapeutic. Conclusion Our results support a complex genetic relationship between AD and these cardiometabolic traits, and the candidate causal genes identified suggest that blood pressure and immune response play a role in the pleiotropy between these traits.
C1 [Bone, William P.; Siewert, Katherine M.] Univ Penn, Perelman Sch Med, Genom & Computat Biol Grad Grp, Philadelphia, PA 19104 USA.
   [Jha, Anupama] Univ Penn, Dept Comp & Informat Sci, Sch Engn & Appl Sci, Philadelphia, PA 19104 USA.
   [Klarin, Derek] Boston VA Healthcare Syst, Boston, MA 02130 USA.
   [Klarin, Derek] Harvard Med Sch, Massachusetts Gen Hosp, Ctr Genom Med, Boston, MA 02114 USA.
   [Klarin, Derek] Broad Inst MIT & Harvard, Program Med & Populat Genet, Cambridge, MA 02142 USA.
   [Damrauer, Scott M.] Univ Penn, Perelman Sch Med, Dept Med, Philadelphia, PA 19104 USA.
   [Damrauer, Scott M.; Chang, Kyong-Mi; Voight, Benjamin F.] Corporal Michael Crescenz VA Med Ctr, Philadelphia, PA 19104 USA.
   [Damrauer, Scott M.; Chang, Kyong-Mi] Univ Penn, Perelman Sch Med, Dept Surg, Philadelphia, PA 19104 USA.
   [Tsao, Philip S.; Assimes, Themistocles L.] VA Palo Alto Hlth Care Syst, Palo Alto, CA 94550 USA.
   [Tsao, Philip S.; Assimes, Themistocles L.] Stanford Univ, Sch Med, Dept Med, Stanford, CA 94305 USA.
   [Ritchie, Marylyn D.; Voight, Benjamin F.] Univ Penn, Dept Genet, Perelman Sch Med, Philadelphia, PA 19104 USA.
   [Ritchie, Marylyn D.; Voight, Benjamin F.] Univ Penn, Inst Biomed Informat, Perelman Sch Med, Philadelphia, PA 19104 USA.
   [Ritchie, Marylyn D.] Univ Penn, Ctr Precis Med, Perelman Sch Med, Philadelphia, PA 19104 USA.
   [Voight, Benjamin F.] Univ Penn, Dept Syst Pharmacol & Translat Therapeut, Perelman Sch Med, Philadelphia, PA 19104 USA.
   [Voight, Benjamin F.] Univ Penn, Inst Translat Med & Therapeut, Perelman Sch Med, Philadelphia, PA 19104 USA.
C3 University of Pennsylvania; University of Pennsylvania; Harvard
   University; Harvard University Medical Affiliates; US Department of
   Veterans Affairs; Veterans Health Administration (VHA); VA Boston
   Healthcare System; Harvard University; Harvard University Medical
   Affiliates; Massachusetts General Hospital; Harvard Medical School;
   Harvard University; Massachusetts Institute of Technology (MIT); Broad
   Institute; University of Pennsylvania; University of Pennsylvania; US
   Department of Veterans Affairs; Veterans Health Administration (VHA); VA
   Palo Alto Health Care System; Stanford University; University of
   Pennsylvania; University of Pennsylvania; University of Pennsylvania;
   University of Pennsylvania; University of Pennsylvania
RP Voight, BF (corresponding author), Corporal Michael Crescenz VA Med Ctr, Philadelphia, PA 19104 USA.; Voight, BF (corresponding author), Univ Penn, Dept Genet, Perelman Sch Med, Philadelphia, PA 19104 USA.; Voight, BF (corresponding author), Univ Penn, Inst Biomed Informat, Perelman Sch Med, Philadelphia, PA 19104 USA.; Voight, BF (corresponding author), Univ Penn, Dept Syst Pharmacol & Translat Therapeut, Perelman Sch Med, Philadelphia, PA 19104 USA.; Voight, BF (corresponding author), Univ Penn, Inst Translat Med & Therapeut, Perelman Sch Med, Philadelphia, PA 19104 USA.
EM bvoight@pennmedicine.upenn.edu
RI Jha, Anupama/P-2249-2019; Voight, Benjamin/F-1775-2011; Ritchie,
   Marylyn/C-1114-2012; Assimes, Themistocles/D-9696-2015
OI Nguyen, Xuan-Mai T./0000-0001-6299-3763; Klarin,
   Derek/0000-0002-4636-5780; Hauser, Elizabeth/0000-0003-0367-9189; Sun,
   Yan/0000-0002-2838-1824; Assimes, Themistocles/0000-0003-2349-0009;
   Tsao, Philip/0000-0001-7274-9318; Voight, Benjamin/0000-0002-6205-9994;
   Moorman, Jonathan/0000-0002-6102-6541; Siewert,
   Katherine/0000-0002-3658-5245; Mathew, Roy O/0000-0002-5582-3165; Jha,
   Anupama/0000-0003-3029-2086; Chang, Kyong-Mi/0000-0001-6811-9364
FU Department of Veterans Affairs Office of RD award [I01-BX003362,
   IK2-CX001780]; American Heart Association [20PRE35120109]; National
   Institutes of Health [DK101478, P50GM115318-01]; Linda Pechenik Montague
   Investigator Award; American Heart Association (AHA) [20PRE35120109]
   Funding Source: American Heart Association (AHA)
FX This research is based on data from the Million Veteran Program, Office
   of Research and Development, Veterans Health Administration, and was
   supported by the Department of Veterans Affairs Office of R&D award
   I01-BX003362 (to P.S.T. and K.M.C) and IK2-CX001780 (to S.M.D). This
   publication does not represent the views of the Department of Veteran
   Affairs or the United States Government. This work was supported by the
   American Heart Association (20PRE35120109 to W.P.B.), the National
   Institutes of Health (DK101478 to B.F.V. and P50GM115318-01 to M.D.R.),
   and a Linda Pechenik Montague Investigator Award (to B.F.V.).
CR 1000 Genomes Project Consortium, 2012, Nature, V491, P56, DOI 10.1038/nature11632
   Andrade V, 2020, LARGE METAANALYSIS G
   Attems J, 2014, BMC MED, V12, DOI 10.1186/s12916-014-0206-2
   Broce IJ, 2019, ACTA NEUROPATHOL, V137, P209, DOI 10.1007/s00401-018-1928-6
   Broholm C, 2016, DIABETOLOGIA, V59, P2664, DOI 10.1007/s00125-016-4099-9
   Bulik-Sullivan BK, 2015, NAT GENET, V47, P291, DOI 10.1038/ng.3211
   Buniello A, 2019, NUCLEIC ACIDS RES, V47, pD1005, DOI 10.1093/nar/gky1120
   Carithers LJ, 2015, BIOPRESERV BIOBANK, V13, P311, DOI 10.1089/bio.2015.0032
   Chávez-Gutiérrez L, 2012, EMBO J, V31, P2261, DOI 10.1038/emboj.2012.79
   Chen Q, 2002, J CELL BIOL, V158, P79, DOI 10.1083/jcb.200110151
   Evangelou E, 2018, NAT GENET, V50, P1412, DOI 10.1038/s41588-018-0205-x
   Frost GR, 2019, FRONT AGING NEUROSCI, V11, DOI 10.3389/fnagi.2019.00337
   Giambartolomei C, 2018, BIOINFORMATICS, V34, P2538, DOI 10.1093/bioinformatics/bty147
   Giambartolomei C, 2014, PLOS GENET, V10, DOI 10.1371/journal.pgen.1004383
   Hackinger S, 2017, OPEN BIOL, V7, DOI 10.1098/rsob.170125
   Hemani G, 2018, ELIFE, V7, DOI 10.7554/eLife.34408
   Heneka MT, 2015, NAT IMMUNOL, V16, P229, DOI 10.1038/ni.3102
   Hormozdiari F, 2016, AM J HUM GENET, V99, P1245, DOI 10.1016/j.ajhg.2016.10.003
   Jansen IE, 2019, NAT GENET, V51, P404, DOI 10.1038/s41588-018-0311-9
   Jochemsen HM, 2014, ALZHEIMERS RES THER, V6, DOI 10.1186/alzrt257
   Jordan DM, 2019, GENOME BIOL, V20, DOI 10.1186/s13059-019-1844-7
   Kehoe PG, 1999, NAT GENET, V21, P71, DOI 10.1038/5009
   Klarin D, 2018, NAT GENET, V50, P1514, DOI 10.1038/s41588-018-0222-9
   Kunkle BW, 2019, NAT GENET, V51, P414, DOI 10.1038/s41588-019-0358-2
   Lehmann DJ, 2005, AM J EPIDEMIOL, V162, P305, DOI 10.1093/aje/kwi202
   Liu SY, 2019, J BIOL CHEM, V294, P9760, DOI 10.1074/jbc.RA118.006420
   Lu YC, 2016, NAT COMMUN, V7, DOI 10.1038/ncomms10495
   Mahajan A, 2018, NAT GENET, V50, P1505, DOI 10.1038/s41588-018-0241-6
   Miners S, 2009, AM J TRANSL RES, V1, P163
   Neubauer B, 2018, HYPERTENSION, V71, P1075, DOI 10.1161/HYPERTENSIONAHA.117.10357
   Ouchi N, 2011, NAT REV IMMUNOL, V11, P85, DOI 10.1038/nri2921
   Park J, 2018, SCIENCE, V360, P758, DOI 10.1126/science.aar2131
   Piacentini R, 2014, FRONT PHARMACOL, V5, DOI 10.3389/fphar.2014.00097
   Pruim RJ, 2010, BIOINFORMATICS, V26, P2336, DOI 10.1093/bioinformatics/btq419
   Pulit SL, 2019, HUM MOL GENET, V28, P166, DOI 10.1093/hmg/ddy327
   Purcell S, 2007, AM J HUM GENET, V81, P559, DOI 10.1086/519795
   Ravona-Springer Ramit, 2003, Dialogues Clin Neurosci, V5, P7
   Reitz C, 2013, CURR ATHEROSCLER REP, V15, DOI 10.1007/s11883-012-0307-3
   Santos Claudia Y, 2017, Alzheimers Dement (Amst), V7, P69, DOI 10.1016/j.dadm.2017.01.005
   Shi Lei, 2013, Commun Integr Biol, V6, pe26839, DOI 10.4161/cib.26839
   Solovieff N, 2013, NAT REV GENET, V14, P483, DOI 10.1038/nrg3461
   Srinivasan K, 2016, NAT COMMUN, V7, DOI 10.1038/ncomms11295
   Stearns FW, 2010, GENETICS, V186, P767, DOI 10.1534/genetics.110.122549
   Thome AD, 2018, MOL NEURODEGENER, V13, DOI 10.1186/s13024-018-0293-1
   van der Harst P, 2018, CIRC RES, V122, P433, DOI [10.1161/CIRCRESAHA.117.312086, 10.1161/circresaha.117.312086]
   Wagner GP, 2011, NAT REV GENET, V12, P204, DOI 10.1038/nrg2949
   WALKER VM, 2019, INT J EPIDEMIOL
   Watanabe K, 2019, NAT GENET, V51, P1339, DOI 10.1038/s41588-019-0481-0
   Wen XQ, 2015, PLOS GENET, V11, DOI 10.1371/journal.pgen.1005176
   Wozniak MA, 2009, J PATHOL, V217, P131, DOI 10.1002/path.2449
   Wu WJ, 2011, SCI CHINA LIFE SCI, V54, P359, DOI 10.1007/s11427-011-4160-3
   Yang JA, 2011, AM J HUM GENET, V88, P76, DOI 10.1016/j.ajhg.2010.11.011
   Yengo L, 2018, HUM MOL GENET, V27, P3641, DOI 10.1093/hmg/ddy271
   Zhao SD, 2017, J AM STAT ASSOC, V112, P1032, DOI 10.1080/01621459.2016.1270825
NR 54
TC 20
Z9 21
U1 0
U2 11
PU BMC
PI LONDON
PA CAMPUS, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
EI 1758-9193
J9 ALZHEIMERS RES THER
JI Alzheimers Res. Ther.
PD JAN
PY 2021
VL 13
IS 1
AR 34
DI 10.1186/s13195-021-00773-z
PG 14
WC Clinical Neurology; Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA QC4LS
UT WOS:000614805000001
PM 33541420
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Karam, CN
   Warren, CM
   Rajan, S
   de Tombe, PP
   Wieczorek, DF
   Solaro, RJ
AF Karam, Chehade N.
   Warren, Chad M.
   Rajan, Sudarsan
   de Tombe, Pieter P.
   Wieczorek, David F.
   Solaro, R. John
TI Expression of tropomyosin-κ induces dilated cardiomyopathy and depresses
   cardiac myofilament tension by mechanisms involving cross-bridge
   dependent activation and altered tropomyosin phosphorylation
SO JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
LA English
DT Article
DE Calcium sensitivity; Tension cost; Thin filament regulation; ATPase;
   Sarcomeric proteins
ID ALPHA-TROPOMYOSIN; COOPERATIVE BINDING; BETA-TROPOMYOSIN;
   THIN-FILAMENTS; PROTEIN-KINASE; TROPONIN-C; CALCIUM; MUSCLE; MYOSIN;
   ADULT
AB Tropomyosin-kappa (TPM1-kappa) is a newly discovered tropomyosin (TM) isoform that is exclusively expressed in the human heart and generated by an alternative splicing of the alpha-TM gene. We reported that TPM1-kappa expression was increased in the hearts of patients with chronic dilated cardiomyopathy (DCM). To increase our understanding of the significance of this shift in isoform population, we generated transgenic (TG) mice expressing TPM1-kappa in the cardiac compartment where TPM1-kappa replaces 90% of the native TM. We previously showed that there was a significant inhibition of the ability of strongly bound cross-bridges to induce activation of TG myofilaments (Rajan et al., Circulation 121: 410-418, 2010). Here, we compared the force-Ca2+ relations in detergent extracted (skinned) fiber bundles isolated from non-transgenic (NTG) and TG-TPM1-kappa hearts at two sarcomere lengths (SLs). Our data demonstrated a significant decrease in the Ca2+ sensitivity of the myofilaments from TG-TPM1-kappa hearts with no change in the maximum developed tension, length-dependent activation, and the ratio of ATPase rate to tension. There was also no difference in the affinity and cooperativity of Ca2+-binding to troponin in thin filaments reconstituted with either TPM1-kappa or alpha-TM. We also compared protein phosphorylation in NTG and TG-TPM1-kappa myofilaments. There was a decrease in the total phosphorylation of TPM1-kappa compared to alpha-TM, but no significant change in other major sarcomeric proteins. Our results identify a novel mode of myofilament desensitization to Ca2+ associated with a DCM linked switch in TM isoform population.
C1 [Karam, Chehade N.; Warren, Chad M.; Solaro, R. John] Univ Illinois, Dept Physiol & Biophys, Cardiovasc Res Ctr, Coll Med, Chicago, IL 60612 USA.
   [Rajan, Sudarsan; Wieczorek, David F.] Univ Cincinnati, Dept Mol Genet Biochem & Microbiol, Coll Med, Cincinnati, OH 45267 USA.
   [de Tombe, Pieter P.] Loyola Univ, Dept Cell & Mol Physiol, Stritch Sch Med, Chicago, IL 60153 USA.
C3 University of Illinois System; University of Illinois Chicago;
   University of Illinois Chicago Hospital; University System of Ohio;
   University of Cincinnati; Loyola University Chicago
RP Solaro, RJ (corresponding author), Univ Illinois, Dept Physiol & Biophys, Cardiovasc Res Ctr, Coll Med, 835 S Wolcott Ave,M-C 901, Chicago, IL 60612 USA.
EM solarorj@uic.edu
FU American Heart Association; NIH [PO1 HL062426, RO1 HL022231, RO1
   HL081680, RO1 HL071952]
FX The authors would like to thank both Dr. Tomoyoshi Kobayashi for his
   help with the TnC binding measurements and Bindiya G. Patel for her
   assistance with the 2D-DIGE experiments. This work was supported by
   American Heart Association-Midwest Pre-Doctoral Fellowship (CNK) and by
   NIH Grants PO1 HL062426 (RJS, PdeT), RO1 HL022231 (RJS), RO1 HL081680,
   and RO1 HL071952 (DFW).
CR Davis JP, 2007, BIOPHYS J, V92, P3195, DOI 10.1529/biophysj.106.095406
   de Tombe PP, 2007, J PHYSIOL-LONDON, V584, P591, DOI 10.1113/jphysiol.2007.138693
   Denz CR, 2004, BIOCHEM BIOPH RES CO, V320, P1291, DOI 10.1016/j.bbrc.2004.06.084
   DETOMBE PP, 1995, CIRC RES, V76, P734, DOI 10.1161/01.RES.76.5.734
   FABIATO A, 1988, METHOD ENZYMOL, V157, P378
   HEELEY DH, 1989, J BIOL CHEM, V264, P2424
   Jagatheesan G, 2007, AM J PHYSIOL-HEART C, V293, pH949, DOI 10.1152/ajpheart.01341.2006
   Kobayashi T, 2006, J BIOL CHEM, V281, P13471, DOI 10.1074/jbc.M509561200
   Kobayashi T, 1999, BBA-PROTEIN STRUCT M, V1430, P214, DOI 10.1016/S0167-4838(99)00002-3
   Lakdawala NK, 2010, J AM COLL CARDIOL, V55, P320, DOI 10.1016/j.jacc.2009.11.017
   Lehrer SS, 1997, BIOCHEMISTRY-US, V36, P13449, DOI 10.1021/bi971568w
   MILLAR NC, 1990, J BIOL CHEM, V265, P20234
   MONTEIRO PB, 1994, J BIOL CHEM, V269, P10461
   Muthuchamy M, 1995, J BIOL CHEM, V270, P30593, DOI 10.1074/jbc.270.51.30593
   Olson TM, 2001, J MOL CELL CARDIOL, V33, P723, DOI 10.1006/jmcc.2000.1339
   Patton C, 2004, CELL CALCIUM, V35, P427, DOI 10.1016/j.ceca.2003.10.006
   Pieples K, 2002, AM J PHYSIOL-HEART C, V283, pH1344, DOI 10.1152/ajpheart.00351.2002
   Rajan S, 2007, CIRC RES, V101, P205, DOI 10.1161/CIRCRESAHA.107.148379
   Rajan S, 2010, CIRCULATION, V121, P410, DOI 10.1161/CIRCULATIONAHA.109.889725
   Rao VS, 2009, CELL MOTIL CYTOSKEL, V66, P10, DOI 10.1002/cm.20321
   Robinson P, 2007, CIRC RES, V101, P1266, DOI 10.1161/CIRCRESAHA.107.156380
   Solaro RJ, 2009, IDRUGS, V12, P243
   SOLARO RJ, 1988, CIRC RES, V63, P779, DOI 10.1161/01.RES.63.4.779
   Sumandea MP, 2003, J BIOL CHEM, V278, P35135, DOI 10.1074/jbc.M306325200
   Sun YB, 2010, J MOL CELL CARDIOL, V48, P859, DOI 10.1016/j.yjmcc.2009.11.019
   TRYBUS KM, 1980, P NATL ACAD SCI-BIOL, V77, P7209, DOI 10.1073/pnas.77.12.7209
   Vahebi S, 2007, CIRC RES, V100, P408, DOI 10.1161/01.RES.0000258116.60404.ad
   VanBuren P, 2010, CIRCULATION, V121, P351, DOI 10.1161/CIR.0b013e3181d0b947
   Wannenburg T, 1997, AM J PHYSIOL-HEART C, V273, pH2428, DOI 10.1152/ajpheart.1997.273.5.H2428
   Warren CM, 2008, PROTEOMICS, V8, P100, DOI 10.1002/pmic.200700772
   Wolska BM, 1999, CIRC RES, V84, P745
   Yuan C, 2008, AM J PHYSIOL-HEART C, V295, pH647, DOI 10.1152/ajpheart.00357.2008
NR 32
TC 22
Z9 24
U1 1
U2 3
PU SPRINGER
PI DORDRECHT
PA VAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDS
SN 0142-4319
EI 1573-2657
J9 J MUSCLE RES CELL M
JI J. Muscle Res. Cell Motil.
PD MAR
PY 2011
VL 31
IS 5-6
BP 315
EP 322
DI 10.1007/s10974-010-9237-2
PG 8
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA 735XD
UT WOS:000288453000004
PM 21221740
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Gallagher, PG
   Forget, BG
AF Gallagher, PG
   Forget, BG
TI An alternate promoter directs expression of a truncated, muscle-specific
   isoform of the human ankyrin 1 gene
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID HUMAN ERYTHROCYTE ANKYRIN; LINKED DILATED CARDIOMYOPATHY; POLYMERASE-II
   TRANSCRIPTION; MYOSIN LIGHT CHAIN-1; SKELETAL-MUSCLE; DYSTROPHIN GENE;
   CARDIAC-MUSCLE; RAT-BRAIN; HEREDITARY SPHEROCYTOSIS; BINDING PROTEINS
AB Ankyrin I, an erythrocyte membrane protein that links the underlying cytoskeleton to the plasma membrane, is also expressed in brain and muscle. We cloned a truncated, muscle-specific ankyrin 1 cDNA composed of novel 5' sequences and 3' sequences previously identified in the last 3 exons of the human ankyrin 1 erythroid gene. Northern blot analysis revealed expression restricted to cardiac and skeletal muscle tissues. Deduced amino acid sequence of this muscle cDNA predicted a peptide of 155 amino acids in length with a hydrophobic NH, terminus. Cloning of the corresponding chromosomal gene revealed that the ankyrin 1 muscle transcript is composed of four exons spread over similar to 10 kilobase pairs of DNA. Reverse transcriptase-polymerase chain reaction of skeletal muscle cDNA identified multiple cDNA isoforms created by alternative splicing. The ankyrin 1 muscle promoter was identified as a (G + C)-rich promoter located >200 kilobase pairs from the ankyrin 1 erythroid promoter. An ankyrin 1 muscle promoter fragment directed high level expression of a reporter gene in cultured C2C12 muscle cells, but not in HeLa or K562 (erythroid) cells. DNA-protein interactions were identified in vitro at a single Spl and two E box consensus binding sites contained within the promoter. A MyoD cDNA expression plasmid transactivated an ankyrin 1 muscle promoter fragment/reporter gene plasmid in a dose-dependent fashion in both HeLa and K562 cells. A polyclonal antibody raised to human ankyrin 1 muscle-specific sequences reacted with peptides of 28 and 30 kDa on immunoblots of human skeletal muscle.
C1 Yale Univ, Sch Med, Dept Pediat, New Haven, CT 06520 USA.
   Yale Univ, Sch Med, Dept Internal Med, New Haven, CT 06520 USA.
   Yale Univ, Sch Med, Dept Genet, New Haven, CT 06520 USA.
C3 Yale University; Yale University; Yale University
RP Gallagher, PG (corresponding author), Yale Univ, Sch Med, Dept Pediat, 333 Cedar St,POB 208064, New Haven, CT 06520 USA.
EM Patrick_Gallagher@QM.Yale.edu
CR AHN AH, 1993, NAT GENET, V3, P283, DOI 10.1038/ng0493-283
   ALTSCHUL SF, 1990, J MOL BIOL, V215, P403, DOI 10.1016/S0022-2836(05)80360-2
   ANDREWS NC, 1991, NUCLEIC ACIDS RES, V19, P2499, DOI 10.1093/nar/19.9.2499
   BENNETT V, 1992, J BIOL CHEM, V267, P8703
   BENNETT V, 1983, METHOD ENZYMOL, V96, P313
   BIRKENMEIER CS, 1993, J BIOL CHEM, V268, P9533
   BIRKENMEIER CS, 1993, BLOOD, V82, pA5
   BUCKINGHAM ME, 1985, ESSAYS BIOCHEM, V20, P77
   BUSHBY KMD, 1991, HUM GENET, V88, P195
   CARTHEW RW, 1985, CELL, V43, P439, DOI 10.1016/0092-8674(85)90174-6
   CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
   CRAIG SW, 1983, CELL MOTIL CYTOSKEL, V3, P449, DOI 10.1002/cm.970030513
   DAVIS J, 1983, J BIOL CHEM, V258, P7757
   DAVIS LH, 1992, J BIOL CHEM, V267, P18966
   DAVIS LH, 1991, J BIOL CHEM, V266, P11163
   DAVIS LH, 1990, J BIOL CHEM, V265, P10589
   Devarajan P, 1996, J CELL BIOL, V133, P819, DOI 10.1083/jcb.133.4.819
   DONOGHUE MJ, 1991, J CELL BIOL, V115, P423, DOI 10.1083/jcb.115.2.423
   Eber SW, 1996, NAT GENET, V13, P214, DOI 10.1038/ng0696-214
   EDWARDS JBDM, 1991, NUCLEIC ACIDS RES, V19, P5227, DOI 10.1093/nar/19.19.5227
   FLUCHER BE, 1990, NEURON, V5, P339, DOI 10.1016/0896-6273(90)90170-K
   FLUCHER BE, 1989, NEURON, V3, P163, DOI 10.1016/0896-6273(89)90029-9
   FROHMAN MA, 1988, P NATL ACAD SCI USA, V85, P8998, DOI 10.1073/pnas.85.23.8998
   GALLAGHER PG, 1994, BLOOD, V84, pA361
   Gallagher PG, 1997, J BIOL CHEM, V272, P19220, DOI 10.1074/jbc.272.31.19220
   *GEN COMP GROUP, 1994, PROGR MAN WISC PACK
   GREPIN C, 1994, MOL CELL BIOL, V14, P3115, DOI 10.1128/MCB.14.5.3115
   HALL TG, 1987, J BIOL CHEM, V262, P10537
   HARTZOG GA, 1993, MOL CELL BIOL, V13, P44, DOI 10.1128/MCB.13.1.44
   Hoock TC, 1997, J CELL BIOL, V136, P1059, DOI 10.1083/jcb.136.5.1059
   HOROWITZ DS, 1994, TRENDS GENET, V10, P100, DOI 10.1016/0168-9525(94)90233-X
   IP HS, 1994, MOL CELL BIOL, V14, P7517, DOI 10.1128/MCB.14.11.7517
   JAROLIM P, 1992, BLOOD S, V80, pA144
   JAVAHERY R, 1994, MOL CELL BIOL, V14, P116, DOI 10.1128/MCB.14.1.116
   KADONAGA JT, 1986, TRENDS BIOCHEM SCI, V11, P20, DOI 10.1016/0968-0004(86)90226-4
   KORDELI E, 1990, J CELL BIOL, V110, P1341, DOI 10.1083/jcb.110.4.1341
   KORDELI E, 1991, J CELL BIOL, V114, P1243, DOI 10.1083/jcb.114.6.1243
   KORDELI E, 1995, J BIOL CHEM, V270, P2352, DOI 10.1074/jbc.270.5.2352
   KOZAK M, 1986, CELL, V44, P283, DOI 10.1016/0092-8674(86)90762-2
   KUNIMOTO M, 1991, J CELL BIOL, V115, P1319, DOI 10.1083/jcb.115.5.1319
   LAMBERT S, 1990, P NATL ACAD SCI USA, V87, P1730, DOI 10.1073/pnas.87.5.1730
   LAMBERT S, 1993, J NEUROSCI, V13, P3725
   LAMBERT S, 1993, EUR J BIOCHEM, V211, P1, DOI 10.1111/j.1432-1033.1993.tb19863.x
   LASSAR AB, 1989, CELL, V58, P823, DOI 10.1016/0092-8674(89)90935-5
   LAVERRIERE AC, 1994, J BIOL CHEM, V269, P23177
   LUX SE, 1990, NATURE, V344, P36, DOI 10.1038/344036a0
   LUX SE, 1909, BLOOD PRINCIPLES PRA, P1701
   MASON P, 1993, GENE TRANSCRIPTION P, P47
   McGrew MJ, 1996, MOL CELL BIOL, V16, P4524
   MOISEYEV VS, 1987, LANCET, V2, P853
   MOLKENTIN JD, 1994, MOL CELL BIOL, V14, P4947, DOI 10.1128/MCB.14.7.4947
   MOON RT, 1985, J CELL BIOL, V100, P152, DOI 10.1083/jcb.100.1.152
   MORROW JS, 1996, HDB PHYSL, P485
   MUNTONI F, 1995, AM J HUM GENET, V56, P151
   MUNTONI F, 1995, J CLIN INVEST, V96, P693, DOI 10.1172/JCI118112
   MUNTONI F, 1993, NEW ENGL J MED, V329, P921, DOI 10.1056/NEJM199309233291304
   NABESHIMA YI, 1984, NATURE, V308, P333, DOI 10.1038/308333a0
   NELSON WJ, 1985, J CELL BIOL, V100, P1726, DOI 10.1083/jcb.100.5.1726
   NELSON WJ, 1984, P NATL ACAD SCI-BIOL, V81, P3292, DOI 10.1073/pnas.81.11.3292
   NG SY, 1985, MOL CELL BIOL, V5, P2720, DOI 10.1128/MCB.5.10.2720
   Olson EN, 1996, SCIENCE, V272, P671, DOI 10.1126/science.272.5262.671
   OTTO E, 1991, J CELL BIOL, V114, P241, DOI 10.1083/jcb.114.2.241
   PARDO JV, 1983, P NATL ACAD SCI-BIOL, V80, P1008, DOI 10.1073/pnas.80.4.1008
   PERIASAMY M, 1984, J BIOL CHEM, V259, P3595
   PETERS LL, 1993, BLOOD, V81, P2144
   PETERS LL, 1993, SEMIN HEMATOL, V30, P85
   PETERS LL, 1991, J CELL BIOL, V114, P1233, DOI 10.1083/jcb.114.6.1233
   PETERS LL, 1995, J CELL BIOL, V130, P313, DOI 10.1083/jcb.130.2.313
   PLATT OS, 1993, J BIOL CHEM, V268, P24421
   Porter GA, 1997, CELL MOTIL CYTOSKEL, V37, P7, DOI 10.1002/(SICI)1097-0169(1997)37:1<7::AID-CM2>3.0.CO;2-7
   ROBERT B, 1984, CELL, V39, P129, DOI 10.1016/0092-8674(84)90198-3
   RUBENSTEIN PA, 1990, BIOESSAYS, V12, P309, DOI 10.1002/bies.950120702
   SHAPIRO MB, 1987, NUCLEIC ACIDS RES, V15, P7155, DOI 10.1093/nar/15.17.7155
   SPENCER SE, 1987, NEUROLOGY, V37, P645, DOI 10.1212/WNL.37.4.645
   STRAUSS F, 1984, CELL, V37, P889, DOI 10.1016/0092-8674(84)90424-0
   STREHLER EE, 1985, MOL CELL BIOL, V5, P3168, DOI 10.1128/MCB.5.11.3168
   THUERAUF DJ, 1994, J BIOL CHEM, V269, P17772
   WINKELMANN JC, 1993, BLOOD, V81, P3173
   WINKELMANN JC, 1990, J BIOL CHEM, V265, P20449
   WINKELMANN JC, 1990, J BIOL CHEM, V265, P11827
   YAMAGATA T, 1995, MOL CELL BIOL, V15, P3830
   Zhou DX, 1997, J CELL BIOL, V136, P621, DOI 10.1083/jcb.136.3.621
NR 82
TC 68
Z9 75
U1 0
U2 5
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA
SN 0021-9258
J9 J BIOL CHEM
JI J. Biol. Chem.
PD JAN 16
PY 1998
VL 273
IS 3
BP 1339
EP 1348
DI 10.1074/jbc.273.3.1339
PG 10
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA YQ670
UT WOS:000071411500014
PM 9430667
OA hybrid
DA 2025-04-10
ER

PT J
AU Arystarkhova, E
   Sweadner, KJ
AF Arystarkhova, E
   Sweadner, KJ
TI Isoform-specific monoclonal antibodies to Na,K-ATPase alpha subunits -
   Evidence for a tissue-specific post-translational modification of the
   alpha subunit
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID SODIUM DODECYL-SULFATE; CENTRAL-NERVOUS-SYSTEM; RAT CARDIAC VENTRICLE;
   NA+-K+-ATPASE; CATALYTIC SUBUNIT; BETA-SUBUNIT; DIFFERENTIAL EXPRESSION;
   ENZYMATIC-PROPERTIES; GEL-ELECTROPHORESIS; SKELETAL-MUSCLE
AB Monoclonal antibodies to isoforms of the Na,K-ATPase have become important tools in the study of the enzyme's distribution, physiological roles, and gene regulation, and when their epitopes are defined, they are useful in the study of enzyme structure as well. Evidence is presented that the alpha 3-specific antibody McBX3 recognizes an unusual epitope that is not present on alpha 3 in the heart. The epitope, which is also found in kidney oil from some species, was mapped to a site on the large intracellular loop near the ATP binding site. DNA sequencing of reverse transcribed-PCR products encompassing the corresponding regions from alpha 3 from brain (where McBX3 recognizes alpha 3) and heart demonstrated that the tissue difference in epitope is not due to alternative splicing of the mRNA. Instead, hydroxylamine sensitivity indicated that the antibody recognizes a post-translational modification. The epitope for a new antibody for alpha 3, XVIF9-G10, was mapped to a site near the N terminus, a location analogous to the sites for the well-characterized antibodies McK1 (alpha 1) and McB2 (alpha 2). The antibody XVIF9-G10 reacted with the alpha 3 of the heart as well as that of the brain; however, McBX3 and XVIF9-G10 both stained the same cellular structures in sections of the rat retina. A new alpha 1-specific antibody, 6F, was characterized and mapped to another site near the N terminus; this antibody has broader species specificity than the other well-characterized alpha 1 antibody, McK1.
C1 MASSACHUSETTS GEN HOSP, MEMBRANE BIOL LAB, CHARLESTOWN, MA 02129 USA.
C3 Harvard University; Harvard University Medical Affiliates; Massachusetts
   General Hospital
RI Arystarkhova, Elena/KZU-2474-2024
FU NHLBI NIH HHS [HL 36271] Funding Source: Medline
CR ABBOTT A, 1992, BIOCHEMISTRY-US, V31, P11236, DOI 10.1021/bi00160a039
   ABBOTT A, 1993, BIOCHEMISTRY-US, V32, P3511, DOI 10.1021/bi00064a040
   ARYSTARKHOVA EA, 1991, BIOPHYS J, V59, pA340
   BALL WJ, 1987, BIOCHIM BIOPHYS ACTA, V916, P100, DOI 10.1016/0167-4838(87)90216-0
   BAYER R, 1990, BIOCHEMISTRY-US, V29, P2251, DOI 10.1021/bi00461a007
   BENALLAL M, 1994, EXPERIENTIA, V50, P664, DOI 10.1007/BF01952869
   BERREBIBERTRAND I, 1994, FEBS LETT, V348, P55, DOI 10.1016/0014-5793(94)00550-8
   BLANCO G, 1994, P NATL ACAD SCI USA, V91, P8542, DOI 10.1073/pnas.91.18.8542
   BORNSTEIN P, 1970, BIOCHEMISTRY-US, V9, P2408, DOI 10.1021/bi00814a004
   BROWN D, 1996, IN PRESS J HISTOCHEM
   CLEVELAND DW, 1977, J BIOL CHEM, V252, P1102
   DALY SE, 1994, J BIOL CHEM, V269, P23944
   FELSENFELD DP, 1988, J BIOL CHEM, V263, P10932
   GHOSH S, 1990, J BIOL CHEM, V265, P2935
   HSU YM, 1989, BIOCHEMISTRY-US, V28, P569, DOI 10.1021/bi00428a023
   HUNDAL HS, 1994, MOL MEMBR BIOL, V11, P255, DOI 10.3109/09687689409160435
   JEWELL EA, 1991, J BIOL CHEM, V266, P16925
   JORGENSEN PL, 1988, METHOD ENZYMOL, V156, P29
   JORGENSEN PL, 1988, METHOD ENZYMOL, V156, P291
   JUST I, 1995, BIOCHEMISTRY-US, V34, P326, DOI 10.1021/bi00001a040
   KARLISH SJD, 1990, P NATL ACAD SCI USA, V87, P4566, DOI 10.1073/pnas.87.12.4566
   KAUFMAN JF, 1984, J BIOL CHEM, V259, P7230
   Landon, 1977, Methods Enzymol, V47, P145
   LINGREL JB, 1990, PROG NUCLEIC ACID RE, V38, P37
   LUCCHESI PA, 1991, J BIOL CHEM, V266, P9327
   LYTTON J, 1985, BIOCHEM BIOPH RES CO, V132, P764, DOI 10.1016/0006-291X(85)91198-2
   MCGRAIL KM, 1990, EUR J NEUROSCI, V2, P170, DOI 10.1111/j.1460-9568.1990.tb00409.x
   MCGRAIL KM, 1991, J NEUROSCI, V11, P381, DOI 10.1523/jneurosci.11-02-00381.1991
   MUNZER JS, 1994, J BIOL CHEM, V269, P16668
   NAGANO K, 1965, BIOCHEM BIOPH RES CO, V19, P759, DOI 10.1016/0006-291X(65)90324-4
   OHLENDIECK K, 1991, NEURON, V7, P499, DOI 10.1016/0896-6273(91)90301-F
   ORLOWSKI J, 1988, J BIOL CHEM, V263, P10436
   OVCHINNIKOV YA, 1987, FEBS LETT, V217, P269, DOI 10.1016/0014-5793(87)80676-2
   OVCHINNIKOV YA, 1988, FEBS LETT, V227, P235, DOI 10.1016/0014-5793(88)80905-0
   OVCHINNIKOV YA, 1988, FEBS LETT, V233, P87, DOI 10.1016/0014-5793(88)81361-9
   PEDEMONTE CH, 1992, BIOCHEMISTRY-US, V31, P10465, DOI 10.1021/bi00158a008
   PEDEMONTE CH, 1990, P NATL ACAD SCI USA, V87, P9789, DOI 10.1073/pnas.87.24.9789
   PIETRINI G, 1992, P NATL ACAD SCI USA, V89, P8414, DOI 10.1073/pnas.89.18.8414
   RUSSO JJ, 1990, AM J PHYSIOL, V259, pC968, DOI 10.1152/ajpcell.1990.259.6.C968
   SCHAGGER H, 1987, ANAL BIOCHEM, V166, P368, DOI 10.1016/0003-2697(87)90587-2
   SCHNEIDER BG, 1990, EXP EYE RES, V51, P553, DOI 10.1016/0014-4835(90)90086-A
   SHAMRAJ OI, 1991, BIOCHEM BIOPH RES CO, V179, P1434, DOI 10.1016/0006-291X(91)91733-S
   SHULL GE, 1986, BIOCHEMISTRY-US, V25, P8125, DOI 10.1021/bi00373a001
   SHYJAN AW, 1990, P NATL ACAD SCI USA, V87, P1178, DOI 10.1073/pnas.87.3.1178
   SHYJAN AW, 1989, BIOCHEMISTRY-US, V28, P4531, DOI 10.1021/bi00437a002
   SUMBILLA C, 1993, J BIOL CHEM, V268, P21185
   SUN Y, 1992, AM J PHYSIOL, V262, pC1491, DOI 10.1152/ajpcell.1992.262.6.C1491
   SWEADNER KJ, 1987, P NATL ACAD SCI USA, V84, P8404, DOI 10.1073/pnas.84.23.8404
   SWEADNER KJ, 1985, J BIOL CHEM, V260, P9016
   SWEADNER KJ, 1992, ANN NY ACAD SCI, V671, P217, DOI 10.1111/j.1749-6632.1992.tb43798.x
   SWEADNER KJ, 1991, ANAL BIOCHEM, V194, P130, DOI 10.1016/0003-2697(91)90159-Q
   SWEADNER KJ, 1985, J BIOL CHEM, V260, P1508
   SWEADNER KJ, 1988, METHOD ENZYMOL, V156, P65
   SWEADNER KJ, 1994, CIRC RES, V74, P669, DOI 10.1161/01.RES.74.4.669
   SWEADNER KJ, 1989, BIOCHIM BIOPHYS ACTA, V988, P185, DOI 10.1016/0304-4157(89)90019-1
   TAI MM, 1989, BIOCHEMISTRY-US, V28, P3183, DOI 10.1021/bi00434a011
   TAKEYASU K, 1988, J BIOL CHEM, V263, P4347
   Therien AG, 1996, J BIOL CHEM, V271, P7104, DOI 10.1074/jbc.271.12.7104
   URAYAMA O, 1989, J BIOL CHEM, V264, P8271
   URAYAMA O, 1988, BIOCHEM BIOPH RES CO, V156, P796, DOI 10.1016/S0006-291X(88)80914-8
   WATTS AG, 1991, P NATL ACAD SCI USA, V88, P7425, DOI 10.1073/pnas.88.16.7425
NR 61
TC 84
Z9 86
U1 0
U2 2
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
SN 0021-9258
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD SEP 20
PY 1996
VL 271
IS 38
BP 23407
EP 23417
DI 10.1074/jbc.271.38.23407
PG 11
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA VH768
UT WOS:A1996VH76800072
PM 8798546
OA hybrid
DA 2025-04-10
ER

PT J
AU Souidi, A
   Nakamori, M
   Zmojdzian, M
   Jagla, T
   Renaud, Y
   Jagla, K
AF Souidi, Anissa
   Nakamori, Masayuki
   Zmojdzian, Monika
   Jagla, Teresa
   Renaud, Yoan
   Jagla, Krzysztof
TI Deregulations of miR-1 and its target Multiplexin promote dilated
   cardiomyopathy associated with myotonic dystrophy type 1
SO EMBO REPORTS
LA English
DT Article
DE dilated cardiomyopathy; Drosophila; miR-1; Multiplexin; myotonic
   dystrophy type 1
ID BINDING PROTEIN-BETA; EXPANDED CTG REPEATS; INCREASES TRANSLATION;
   EXTRACELLULAR-MATRIX; DROSOPHILA MODEL; MOUSE MODEL; IN-VIVO; CUGBP1;
   MBNL; ABNORMALITIES
AB Myotonic dystrophy type 1 (DM1) is the most common muscular dystrophy in adults. It is caused by the excessive expansion of noncoding CTG repeats, which when transcribed affects the functions of RNA-binding factors with adverse effects on alternative splicing, processing, and stability of a large set of muscular and cardiac transcripts. Among these effects, inefficient processing and down-regulation of muscle- and heart-specific miRNA, miR-1, have been reported in DM1 patients, but the impact of reduced miR-1 on DM1 pathogenesis has been unknown. Here, we use Drosophila DM1 models to explore the role of miR-1 in cardiac dysfunction in DM1. We show that miR-1 down-regulation in the heart leads to dilated cardiomyopathy (DCM), a DM1-associated phenotype. We combined in silico screening for miR-1 targets with transcriptional profiling of DM1 cardiac cells to identify miR-1 target genes with potential roles in DCM. We identify Multiplexin (Mp) as a new cardiac miR-1 target involved in DM1. Mp encodes a collagen protein involved in cardiac tube formation in Drosophila. Mp and its human ortholog Col15A1 are both highly enriched in cardiac cells of DCM-developing DM1 flies and in heart samples from DM1 patients with DCM, respectively. When overexpressed in the heart, Mp induces DCM, whereas its attenuation rescues the DCM phenotype of aged DM1 flies. Reduced levels of miR-1 and consecutive up-regulation of its target Mp/Col15A1 might be critical in DM1-associated DCM.
C1 [Souidi, Anissa; Zmojdzian, Monika; Jagla, Teresa; Renaud, Yoan; Jagla, Krzysztof] Clermont Auvergne Univ, iGReD Genet Reprod & Dev Inst, Clermont Ferrand, France.
   [Nakamori, Masayuki] Osaka Univ, Grad Sch Med, Dept Neurol, Suita, Japan.
C3 Universite Clermont Auvergne (UCA); The University of Osaka
RP Jagla, K (corresponding author), Clermont Auvergne Univ, iGReD Genet Reprod & Dev Inst, Clermont Ferrand, France.
EM christophe.jagla@uca.fr
RI Jagla, Krzysztof/E-4144-2016; Nakamori, Masayuki/ABE-2169-2020
OI Nakamori, Masayuki/0000-0003-4714-3044
FU AFM-Telethon strategic grant; Intramural Research Grant [2-5]
FX We would like to thank Drosophila Bloomington and VDRC stock centers.
   This work was funded by the AFM-Telethon strategic grant to MyoNeurAlp
   consortium (to K.J.) and Intramural Research Grant (2-5) for
   Neurological and Psychiatric Disorders of National Center of Neurology
   and Psychiatry (to M.N.).
CR Auxerre-Plantié E, 2019, ELIFE, V8, DOI 10.7554/eLife.51114
   Chang KT, 2017, CIRC RES, V121, P1140, DOI 10.1161/CIRCRESAHA.117.311281
   Dasgupta T, 2012, WIRES RNA, V3, P104, DOI 10.1002/wrna.107
   de Haro M, 2006, HUM MOL GENET, V15, P2138, DOI 10.1093/hmg/ddl137
   de Haro M, 2013, PLOS GENET, V9, DOI 10.1371/journal.pgen.1003445
   Eklund L, 2001, P NATL ACAD SCI USA, V98, P1194, DOI 10.1073/pnas.031444798
   Fardaei M, 2002, HUM MOL GENET, V11, P805, DOI 10.1093/hmg/11.7.805
   Fardaei M, 2001, NUCLEIC ACIDS RES, V29, P2766, DOI 10.1093/nar/29.13.2766
   Fernandez-Costa JM, 2013, HUM MOL GENET, V22, P704, DOI 10.1093/hmg/dds478
   Fulga TA, 2015, NAT COMMUN, V6, DOI 10.1038/ncomms8279
   Garcia-Lopez A, 2008, PLOS ONE, V3, DOI 10.1371/journal.pone.0001595
   Gil-Cayuela C, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0168130
   Griffiths-Jones S, 2006, NUCLEIC ACIDS RES, V34, pD140, DOI 10.1093/nar/gkj112
   Groh WJ, 2008, NEW ENGL J MED, V358, P2688, DOI 10.1056/NEJMoa062800
   Harpaz N, 2013, PLOS GENET, V9, DOI 10.1371/journal.pgen.1003597
   Hermans MCE, 2012, J CARDIOVASC MAGN R, V14, DOI 10.1186/1532-429X-14-48
   Houseley JM, 2005, HUM MOL GENET, V14, P873, DOI 10.1093/hmg/ddi080
   Huguet A, 2012, PLOS GENET, V8, DOI 10.1371/journal.pgen.1003043
   Ikeda S, 2007, PHYSIOL GENOMICS, V31, P367, DOI 10.1152/physiolgenomics.00144.2007
   Isserlin R, 2015, MOL BIOSYST, V11, P239, DOI 10.1039/c4mb00265b
   Kalsotra A, 2014, CELL REP, V6, P336, DOI 10.1016/j.celrep.2013.12.025
   Katoh T, 2015, NUCLEIC ACIDS RES, V43, P7521, DOI 10.1093/nar/gkv669
   Koshelev M, 2010, HUM MOL GENET, V19, P1066, DOI 10.1093/hmg/ddp570
   Kura B, 2020, INT J MOL SCI, V21, DOI 10.3390/ijms21030700
   Kuyumcu-Martinez NM, 2007, MOL CELL, V28, P68, DOI 10.1016/j.molcel.2007.07.027
   Langmead B, 2012, NAT METHODS, V9, P357, DOI [10.1038/NMETH.1923, 10.1038/nmeth.1923]
   Lee JE, 2009, BIOCHEM SOC T, V37, P1281, DOI 10.1042/BST0371281
   Lee KY, 2013, EMBO MOL MED, V5, P1887, DOI 10.1002/emmm.201303275
   LIN AE, 1989, J AM COLL CARDIOL, V13, P262, DOI 10.1016/0735-1097(89)90582-2
   Louzao-Martinez L, 2016, INT J CARDIOL, V220, P634, DOI 10.1016/j.ijcard.2016.06.253
   Masuda A, 2012, SCI REP-UK, V2, DOI 10.1038/srep00209
   Mathieu J, 1999, NEUROLOGY, V52, P1658, DOI 10.1212/WNL.52.8.1658
   McNally EM, 2017, CIRC RES, V121, P731, DOI 10.1161/CIRCRESAHA.116.309396
   Meola G, 2015, BBA-MOL BASIS DIS, V1852, P594, DOI 10.1016/j.bbadis.2014.05.019
   Meyer F, 2009, DEV GROWTH DIFFER, V51, P483, DOI 10.1111/j.1440-169X.2009.01111.x
   Nakamori M, 2008, NEUROLOGY, V70, P677, DOI 10.1212/01.wnl.0000302174.08951.cf
   Nakamori M, 2011, MOL THER, V19, P2222, DOI 10.1038/mt.2011.191
   NGUYEN HH, 1988, J AM COLL CARDIOL, V11, P662, DOI 10.1016/0735-1097(88)91547-1
   Ocorr Karen, 2009, J Vis Exp, DOI 10.3791/1435
   Orengo JP, 2008, P NATL ACAD SCI USA, V105, P2646, DOI 10.1073/pnas.0708519105
   Papa Andrea Antonio, 2018, Acta Myol, V37, P267
   Pelargonio G, 2002, HEART, V88, P665, DOI 10.1136/heart.88.6.665
   Philips AV, 1998, SCIENCE, V280, P737, DOI 10.1126/science.280.5364.737
   Picchio L, 2018, DIS MODEL MECH, V11, DOI 10.1242/dmm.031849
   Picchio L, 2013, HUM MOL GENET, V22, P2795, DOI 10.1093/hmg/ddt127
   Rao PK, 2009, CIRC RES, V105, P585, DOI 10.1161/CIRCRESAHA.109.200451
   Rasi K, 2010, CIRC RES, V107, P1241, DOI 10.1161/CIRCRESAHA.110.222133
   Rau F, 2011, NAT STRUCT MOL BIOL, V18, P840, DOI 10.1038/nsmb.2067
   Schilling L, 2013, BMC MUSCULOSKEL DIS, V14, DOI 10.1186/1471-2474-14-338
   Souidi A, 2021, CELLS-BASEL, V10, DOI 10.3390/cells10113078
   Souidi A, 2018, INT J MOL SCI, V19, DOI 10.3390/ijms19124104
   Timchenko LT, 2006, J BIOL CHEM, V281, P32806, DOI 10.1074/jbc.M605701200
   Timchenko NA, 2005, J BIOL CHEM, V280, P20549, DOI 10.1074/jbc.M409563200
   Vlasova IA, 2008, MOL CELL, V29, P263, DOI 10.1016/j.molcel.2007.11.024
   Wang ET, 2015, GENOME RES, V25, P858, DOI 10.1101/gr.184390.114
   Wang GS, 2007, J CLIN INVEST, V117, P2802, DOI 10.1172/JCI32308
   Wei YS, 2014, CELL RES, V24, P278, DOI 10.1038/cr.2014.12
   Wolf MJ, 2012, TRENDS CARDIOVAS MED, V22, P55, DOI 10.1016/j.tcm.2012.06.012
NR 58
TC 5
Z9 5
U1 0
U2 5
PU SPRINGERNATURE
PI LONDON
PA CAMPUS, 4 CRINAN ST, LONDON, N1 9XW, ENGLAND
SN 1469-221X
EI 1469-3178
J9 EMBO REP
JI EMBO Rep.
PD APR 5
PY 2023
VL 24
IS 4
DI 10.15252/embr.202256616
EA FEB 2023
PG 16
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA C8NA7
UT WOS:000940363200001
PM 36852954
OA Green Submitted, hybrid, Green Published
DA 2025-04-10
ER

PT J
AU Ye, B
   Li, LW
   Xu, HD
   Chen, YP
   Li, FQ
AF Ye, Bo
   Li, Liwen
   Xu, Haodong
   Chen, Yiping
   Li, Faqian
TI Opposing roles of TCF7/LEF1 and TCF7L2 in cyclin D2 and Bmp4 expression
   and cardiomyocyte cell cycle control during late heart development
SO LABORATORY INVESTIGATION
LA English
DT Article
ID WNT/BETA-CATENIN; BETA-CATENIN; GENE-EXPRESSION; PROLIFERATION;
   PROMOTER; DIFFERENTIATION; REGULATOR; PATHWAYS; SIGNALS; BINDING
AB Bone morphogenetic protein (BMP) and Wnt pathways regulate cell proliferation and differentiation, but how these two pathways interact and mediate their nuclear actions in the heart, especially during late cardiac development, remains poorly defined. T-cell factor (TCF) and lymphoid enhancer factor (LEF) family transcriptional factors, including Lef1, Tcf7, Tcf7l1, and Tcf71l2, are important nuclear mediators of canonical Wnt/beta-catenin signaling throughout cardiac development. We reveal that these TCF/LEF family members direct heart maturation through distinct temporal and spatial control. TCF7 and LEF1 decrease while TCF7L1 and TCF7L2 remain relatively stable during heart development. LEF1 is mainly expressed in mesenchymal cells in valvular regions. TCF7 and TCF7L1 are detected in the nucleus of mesothelial and endothelial cells, but not in cardiomyocytes or mesenchymal cells. Tcf712 is the primary TCF/LEF family member in cardiomyocytes and undergoes alternative splicing during heart development. A TCF7L2 intensity gradient opposite to that of beta-catenin and cardiomyocyte proliferative activity is present in fetal hearts. Wnt activation by cardiac deletion of APC, a negative Wnt regulator, dramatically increases Cyclin D2 and Bmp4 expression. BMP signal transducing transcription factors, the mothers against decapentaplegic homologs (SMADs) are increasingly phosphorylated upon Wnt activation. LEF1/TCF7 displaces TCF7L2 and cooperates with pSMAD 1/5/8 in the regulatory elements of Cyclin D2 and Bmp4 promoters to promote beta-catenin recruitment and transcriptional activation. Finally, we demonstrate that TCF7L2 is a transcriptional suppressor of Cyclin D2 and Bmp 4 in a cardiac cell line by overexpression and knockdown experiments.
C1 [Ye, Bo; Li, Faqian] Univ Minnesota, Dept Lab Med & Pathol, Dwan Variety Club Cardiovasc Res Ctr, Room 293,425 E River Pkwy, Minneapolis, MN 55455 USA.
   [Li, Liwen; Chen, Yiping] Tulane Univ, Dept Cell & Mol Biol, New Orleans, LA 70118 USA.
   [Xu, Haodong] Univ Washington, Dept Pathol Anat Pathol, Med Ctr, Seattle, WA 98195 USA.
   [Li, Faqian] Univ Minnesota, Lillehei Heart Inst, Minneapolis, MN 55455 USA.
   [Li, Faqian] Univ Minnesota, Masonic Canc Ctr, Minneapolis, MN 55455 USA.
C3 University of Minnesota System; University of Minnesota Twin Cities;
   Tulane University; University of Washington; University of Washington
   Seattle; University of Minnesota System; University of Minnesota Twin
   Cities; University of Minnesota System; University of Minnesota Twin
   Cities
RP Li, FQ (corresponding author), Univ Minnesota, Dept Lab Med & Pathol, Dwan Variety Club Cardiovasc Res Ctr, Room 293,425 E River Pkwy, Minneapolis, MN 55455 USA.; Li, FQ (corresponding author), Univ Minnesota, Lillehei Heart Inst, Minneapolis, MN 55455 USA.; Li, FQ (corresponding author), Univ Minnesota, Masonic Canc Ctr, Minneapolis, MN 55455 USA.
EM lif@umn.edu
RI li, Liwen/AAO-7497-2020; Ye, Bo/X-7115-2019; cheng, heping/A-7299-2011
OI Ye, Bo/0000-0002-1728-6506; Li, Faqian/0000-0002-9954-095X
FU National Institute of Health (NIH) [R01 HL111480]; American Heart
   Association Greater River Affiliate [10GRNT4460014]; Lawrence J. and
   Florence A. DeGeorge Charitable Trust [10GRNT4460014]; NIH [R01
   HL122793, R01 HL136326]; American Heart Association (AHA)
   [10GRNT4460014] Funding Source: American Heart Association (AHA)
FX We thank Drs. Tetsuo Noda, Michael D. Schneider, and Bart O. Williams
   for their generosity to share mouse models with the scientific
   community. We also appreciate the technical support and data processing
   by Genomics Research Center of University of Rochester. The project
   described was supported by the National Institute of Health (NIH) grant
   R01 HL111480 (FL) and a Grant-in-Aid award 10GRNT4460014 (FL) from the
   American Heart Association Greater River Affiliate and the Lawrence J.
   and Florence A. DeGeorge Charitable Trust. HX is supported by the NIH
   R01 HL122793. YC and LL were supported by the NIH grant R01 HL136326.
CR Agah R, 1997, J CLIN INVEST, V100, P169, DOI 10.1172/JCI119509
   Ai D, 2007, P NATL ACAD SCI USA, V104, P9319, DOI 10.1073/pnas.0701212104
   Angus-Hill ML, 2011, P NATL ACAD SCI USA, V108, P4914, DOI 10.1073/pnas.1102300108
   Arce L, 2006, ONCOGENE, V25, P7492, DOI 10.1038/sj.onc.1210056
   Cadigan KM, 2012, CSH PERSPECT BIOL, V4, DOI 10.1101/cshperspect.a007906
   Clevers H, 2006, CELL, V127, P469, DOI 10.1016/j.cell.2006.10.018
   Cohen ED, 2007, J CLIN INVEST, V117, P1794, DOI 10.1172/JCI31731
   Cole AM, 2010, CANCER RES, V70, P8149, DOI 10.1158/0008-5472.CAN-10-0315
   He TC, 1998, SCIENCE, V281, P1509, DOI 10.1126/science.281.5382.1509
   Hikasa H, 2011, J BIOL CHEM, V286, DOI 10.1074/jbc.M110.185280
   HILL RE, 1989, GENE DEV, V3, P26, DOI 10.1101/gad.3.1.26
   Hou N, 2016, CIRC-HEART FAIL, V9, DOI 10.1161/CIRCHEARTFAILURE.116.003010
   Hu MC, 2005, DEVELOPMENT, V132, P215, DOI 10.1242/dev.01573
   Hurlstone AFL, 2003, NATURE, V425, P633, DOI 10.1038/nature02028
   Hussein SM, 2003, J BIOL CHEM, V278, P48805, DOI 10.1074/jbc.M305472200
   Klaus A, 2007, P NATL ACAD SCI USA, V104, P18531, DOI 10.1073/pnas.0703113104
   Kwon C, 2007, P NATL ACAD SCI USA, V104, P10894, DOI 10.1073/pnas.0704044104
   Lei S, 2004, J BIOL CHEM, V279, P42492, DOI 10.1074/jbc.M404025200
   Merrill BJ, 2004, DEVELOPMENT, V131, P263, DOI 10.1242/dev.00935
   Muzumdar MD, 2007, GENESIS, V45, P593, DOI 10.1002/dvg.20335
   Nguyen H, 2009, NAT GENET, V41, P1068, DOI 10.1038/ng.431
   O'Connell DJ, 2012, SCI SIGNAL, V5, DOI 10.1126/scisignal.2002414
   Olson EN, 2006, SCIENCE, V313, P1922, DOI 10.1126/science.1132292
   OOSTERWEGEL M, 1993, DEVELOPMENT, V118, P439
   Qu JX, 2007, J MOL CELL CARDIOL, V43, P319, DOI 10.1016/j.yjmcc.2007.06.006
   Reynolds A, 2014, GUT, V63, P610, DOI 10.1136/gutjnl-2012-304067
   Sansom OJ, 2004, GENE DEV, V18, P1385, DOI 10.1101/gad.287404
   Sedmera D, 2003, ANAT REC PART A, V274A, P773, DOI 10.1002/ar.a.10085
   Seoane J, 2004, CELL, V117, P211, DOI 10.1016/S0092-8674(04)00298-3
   Shi YG, 1998, CELL, V94, P585, DOI 10.1016/S0092-8674(00)81600-1
   Shibata H, 1997, SCIENCE, V278, P120, DOI 10.1126/science.278.5335.120
   Shtutman M, 1999, P NATL ACAD SCI USA, V96, P5522, DOI 10.1073/pnas.96.10.5522
   St Amand TR, 2000, DEV BIOL, V217, P323, DOI 10.1006/dbio.1999.9547
   Tang W, 2008, P NATL ACAD SCI USA, V105, P9697, DOI 10.1073/pnas.0804709105
   Tetsu O, 1999, NATURE, V398, P422, DOI 10.1038/18884
   TRAVIS A, 1991, GENE DEV, V5, P880, DOI 10.1101/gad.5.5.880
   Visel A, 2004, NUCLEIC ACIDS RES, V32, pD552, DOI 10.1093/nar/gkh029
   Wang H, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0163267
   Weise A, 2010, NUCLEIC ACIDS RES, V38, P1964, DOI 10.1093/nar/gkp1197
   Ye B, 2015, J MOL CELL CARDIOL, V89, P287, DOI 10.1016/j.yjmcc.2015.10.018
   Yi YP, 2002, HYPERTENSION, V39, P1058, DOI 10.1161/01.HYP0000019130.09167.3B
NR 41
TC 23
Z9 25
U1 0
U2 9
PU NATURE PUBLISHING GROUP
PI NEW YORK
PA 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA
SN 0023-6837
EI 1530-0307
J9 LAB INVEST
JI Lab. Invest.
PD JUN
PY 2019
VL 99
IS 6
BP 807
EP 818
DI 10.1038/s41374-019-0204-2
PG 12
WC Medicine, Research & Experimental; Pathology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Research & Experimental Medicine; Pathology
GA IC8VU
UT WOS:000471260900006
PM 30778164
OA Green Accepted, Bronze
DA 2025-04-10
ER

PT J
AU Liu, X
   Wang, QW
   Zhao, JJ
   Chang, HT
   Zhu, RX
AF Liu, Xu
   Wang, Qianwen
   Zhao, Jingjing
   Chang, Hongtao
   Zhu, Ruixia
TI Inflammation-Related circRNA Polymorphism and Ischemic Stroke Prognosis
SO JOURNAL OF MOLECULAR NEUROSCIENCE
LA English
DT Article
DE Ischemic stroke; Prognosis; circRNA; Polymorphism; Inflammation
ID CIRCULAR RNA DLGAP4; EXPRESSION; OUTCOMES; MIR-143
AB CircRNAs belong to a novel class of noncoding RNAs that are generated by exons of genes by alternative mRNA splicing and involved in pathophysiological processes of ischemic stroke by regulating neuro-inflammation. A total of 982 patients were enrolled in our study for stroke recovery analysis. The aim of our study was to first explore the association between the inflammation-related circRNA polymorphism and functional outcome 3 months after ischemic stroke by using multivariate logistic regression model. Next, we further investigated the role of circRNA polymorphism in predicting stroke recurrence by using Cox proportional hazard regression model. Five circRNA polymorphisms were genotyped by using polymerase chain reaction and ligation detection reaction method. We identified circ-STAT3 (signal transducer and activator of transcription) rs2293152 GG genotype to be associated with poorer recovery 90 days after stroke (OR = 1.452, 95% CI: 1.165-4.362, p = 0.016). After adjusting for confound factors, the association for rs2293152 with 3 months outcome after IS was stronger, suggesting a mechanism that rs2293152 is an independent risk factor for stroke recovery (OR = 2.255, 95% CI: 1.034-2.038, p = 0.031). However, no other circRNA polymorphisms (circ-DLGAP4 rs41274714, circ-TRAF2 rs10870141, circ-ITCH rs10485505, rs4911154) were associated with functional outcome 3 months after stroke in any genetic models. Subgroup analysis revealed that the negative effect of rs2293152 GG genotype was greater in female and older patients, subjects with history of hypertension. Additionally, all the circRNA polymorphisms were not correlated with recurrent risk of ischemic stroke. Our results indicated that circ-STAT3 might be a novel biomarker for predicting functional outcome after stroke and an important contributor to the ischemic stroke recovery.
C1 [Liu, Xu; Wang, Qianwen; Zhao, Jingjing; Chang, Hongtao; Zhu, Ruixia] China Med Univ, Affiliated Hosp 1, Dept Neurol, Shenyang 110001, Peoples R China.
C3 China Medical University
RP Zhu, RX (corresponding author), China Med Univ, Affiliated Hosp 1, Dept Neurol, Shenyang 110001, Peoples R China.
EM zrx_200626313@163.com
RI WANG, QIANWEN/KVY-5475-2024
OI zhu, ruixia/0000-0002-2683-4674
FU Natural Science Foundation of Liaoning province of China [2019-MS-364];
   National Natural Science Foundation of China [81501006]
FX This study was supported by Natural Science Foundation of Liaoning
   province of China (2019-MS-364) and the National Natural Science
   Foundation of China (81501006).
CR Ahmed I, 2019, RNA, V25, P1765, DOI 10.1261/rna.071654.119
   Arboix A, 2006, EUR NEUROL, V56, P6, DOI 10.1159/000094249
   Bai Y, 2018, J NEUROSCI, V38, P32, DOI 10.1523/JNEUROSCI.1348-17.2017
   Burd CE, 2010, PLOS GENET, V6, DOI 10.1371/journal.pgen.1001233
   Chen LL, 2016, NAT REV MOL CELL BIO, V17, P205, DOI 10.1038/nrm.2015.32
   Chen S, 2017, J NEUROINFLAMM, V14, DOI 10.1186/s12974-017-0963-x
   Dong ZF, 2020, J CELL PHYSIOL, V235, P2609, DOI 10.1002/jcp.29165
   Gao JN, 2017, INT J MOL SCI, V18, DOI 10.3390/ijms18030608
   Guo WZ, 2017, ONCOTARGET, V8, P48169, DOI 10.18632/oncotarget.18327
   Holdt LM, 2016, NAT COMMUN, V7, DOI 10.1038/ncomms12429
   Jeck WR, 2014, NAT BIOTECHNOL, V32, P453, DOI 10.1038/nbt.2890
   Jia L, 2019, MOL BRAIN, V12, DOI 10.1186/s13041-019-0525-5
   Li X, 2018, MOL CELL, V71, P428, DOI 10.1016/j.molcel.2018.06.034
   Lindgren A, 2016, STROKE, V47, P2427, DOI 10.1161/STROKEAHA.116.010648
   Liu ZL, 2019, GENOME BIOL, V20, DOI 10.1186/s13059-019-1701-8
   Paraboschi EM, 2018, FRONT GENET, V9, DOI 10.3389/fgene.2018.00647
   Shen C, 2013, J MOL NEUROSCI, V49, P559, DOI 10.1007/s12031-012-9856-8
   Shen L, 2019, STROKE VASC NEUROL, V4, P96, DOI 10.1136/svn-2018-000206
   Stanne TM, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0114156
   Wang QW, 2020, EXPERT REV MOL DIAGN, V20, P1039, DOI 10.1080/14737159.2020.1826313
   Wang ST, 2019, NEOPLASMA, V66, P232, DOI 10.4149/neo_2018_180710N460
   Wang WZ, 2017, CIRCULATION, V135, P759, DOI 10.1161/CIRCULATIONAHA.116.025250
   Zhang K, 2020, ARCH TOXICOL, V94, P325, DOI 10.1007/s00204-019-02624-1
   Zhou YL, 2020, AGING-US, V12, P13076, DOI 10.18632/aging.103398
   Zhu XQ, 2019, INT J CLIN EXP PATHO, V12, P941
   Zuo L, 2020, STROKE, V51, P319, DOI 10.1161/STROKEAHA.119.027348
NR 26
TC 26
Z9 30
U1 1
U2 16
PU SPRINGERNATURE
PI LONDON
PA CAMPUS, 4 CRINAN ST, LONDON, N1 9XW, ENGLAND
SN 0895-8696
EI 1559-1166
J9 J MOL NEUROSCI
JI J. Mol. Neurosci.
PD OCT
PY 2021
VL 71
IS 10
BP 2126
EP 2133
DI 10.1007/s12031-021-01889-5
EA JUL 2021
PG 8
WC Biochemistry & Molecular Biology; Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Neurosciences & Neurology
GA WD9IN
UT WOS:000673754800001
PM 34273101
OA Green Submitted
DA 2025-04-10
ER

PT J
AU Jiao, YQ
   Zhang, XJ
   Yang, ZS
AF Jiao, Yaqi
   Zhang, Xiaojuan
   Yang, Zhenshan
TI SUMO-specific proteases: SENPs in oxidative stress-related signaling and
   diseases
SO BIOFACTORS
LA English
DT Review
DE cancer; oxidative stress; ROS; SENP; SUMO
ID ISCHEMIA-REPERFUSION INJURY; MOLECULAR-MECHANISMS; REDOX REGULATION;
   DESUMOYLATION; PROTECTS; MITOCHONDRIA; ISOPEPTIDASE; EXPRESSION;
   APOPTOSIS; CELLS
AB Oxidative stress is employed to depict a series of responses detrimental to normal cellular functions resulting from an imbalance between intracellular oxidants, mainly reactive oxygen species and antioxidant defenses. Oxidative stress often contributes to the development of various diseases, including cancer, cardiovascular diseases, and neurodegenerative diseases. In this process, the relationship between small ubiquitin-like modifier (SUMO) and oxidative stress has garnered significant attention, with its posttranslational modification (PTM) frequently serving as a marker of oxidative stress status. Sentrin/SUMO-specific proteases (SENPs), affected by alternative splicing, PTMs such as phosphorylation and ubiquitination, and various protein interactions, are crucial molecules in the SUMO process. The human SENP family has six members (SENP1-3, SENP5-7), which are classified into two categories based on sequence similarity, substrate specificity, and subcellular location. They have two core functions in the human body: first, by cleaving the precursor SUMO and exposing the C-terminal glycine, they initiate the SUMO process; second, they can specifically recognize and dissociate SUMO proteins bound to substrates, a process known as deSUMOylation. However, the connection between deSUMOylation and oxidative stress remains a relatively unexplored area despite their strong association with oxidative diseases such as cancer and cardiovascular disease. This article aims to illustrate the significant contribution of SENPs to the oxidative stress pathway through deSUMOylation by reviewing their structure and classification, their roles in oxidative stress, and the changes in their expression and activity in several typical oxidative stress-related diseases.
   The mechanism of SENPs involved in human oxidative stress-related diseases. image
C1 [Jiao, Yaqi] Ocean Univ China, Key Lab Evolut & Marine Biodivers, Minist Educ, Qingdao, Peoples R China.
   [Jiao, Yaqi] Ocean Univ China, Inst Evolut & Marine Biodivers, Qingdao, Peoples R China.
   [Jiao, Yaqi] Ocean Univ China, Coll Marine Life Sci, Qingdao, Peoples R China.
   [Zhang, Xiaojuan] Univ Groningen, Dept Cell Biochem, Groningen, Netherlands.
   [Yang, Zhenshan] Lund Univ, Dept Clin Sci Lund, Div Oncol, Lund, Sweden.
   [Yang, Zhenshan] Lund Univ, Dept Clin Sci, Div Oncol, S-22381 Lund, Sweden.
C3 Ocean University of China; Ocean University of China; Ocean University
   of China; University of Groningen; Lund University; Lund University
RP Yang, ZS (corresponding author), Lund Univ, Dept Clin Sci, Div Oncol, S-22381 Lund, Sweden.
EM zhenshan.yang@med.lu.se
RI Zhang, Xiaojuan/KBB-5504-2024; Yang, Zhenshan/HCI-7069-2022
OI Yang, Zhenshan/0000-0001-6987-9947; Zhang, Xiaojuan/0009-0005-1579-6851
CR Allen CL, 2009, INT J STROKE, V4, P461, DOI 10.1111/j.1747-4949.2009.00387.x
   Bai RR, 2022, AGEING RES REV, V77, DOI 10.1016/j.arr.2022.101619
   Bailey D, 2002, J GEN VIROL, V83, P2951, DOI 10.1099/0022-1317-83-12-2951
   Barford D, 2004, CURR OPIN STRUC BIOL, V14, P679, DOI 10.1016/j.sbi.2004.09.012
   Bawa-Khalfe T, 2012, P NATL ACAD SCI USA, V109, P17466, DOI 10.1073/pnas.1209378109
   Bernstock JD, 2018, FASEB J, V32, P1677, DOI 10.1096/fj.201700711R
   Bruick RK, 2001, SCIENCE, V294, P1337, DOI 10.1126/science.1066373
   Cai H, 2021, FREE RADICAL BIO MED, V171, P272, DOI 10.1016/j.freeradbiomed.2021.05.026
   Cai R, 2015, J MOL CELL CARDIOL, V79, P115, DOI 10.1016/j.yjmcc.2014.11.014
   Cai R, 2012, J BIOL CHEM, V287, P44464, DOI 10.1074/jbc.M112.422626
   Cava C, 2021, MEDICINA-LITHUANIA, V57, DOI 10.3390/medicina57030261
   Chen X, 2022, CELL DEATH DIFFER, V29, P337, DOI 10.1038/s41418-021-00857-1
   Cheng J, 2007, CELL, V131, P584, DOI 10.1016/j.cell.2007.08.045
   Cheng Y, 2015, MOL MED REP, V12, P2009, DOI 10.3892/mmr.2015.3662
   Chouchani ET, 2014, NATURE, V515, P431, DOI 10.1038/nature13909
   Claessens LA, 2024, TRENDS CELL BIOL, V34, P901, DOI 10.1016/j.tcb.2024.01.002
   Claessens LA, 2023, NAT COMMUN, V14, DOI 10.1038/s41467-023-41623-w
   Cui CP, 2017, GUT, V66, P2149, DOI 10.1136/gutjnl-2016-313264
   Dangoumau A, 2021, INT J MOL SCI, V22, DOI 10.3390/ijms22041796
   Dou H, 2010, MOL CELL, V39, P333, DOI 10.1016/j.molcel.2010.07.021
   Du SC, 2019, CANCER CELL INT, V19, DOI 10.1186/s12935-018-0722-9
   Eltzschig HK, 2011, NAT MED, V17, P1391, DOI 10.1038/nm.2507
   Ferdaoussi M, 2015, J CLIN INVEST, V125, P3847, DOI 10.1172/JCI82498
   Finkbeiner E, 2011, EMBO J, V30, P1067, DOI 10.1038/emboj.2011.33
   Forman HJ, 2021, NAT REV DRUG DISCOV, V20, P689, DOI 10.1038/s41573-021-00233-1
   Gao LC, 2018, J GENET GENOMICS, V45, P125, DOI 10.1016/j.jgg.2017.12.002
   Goeres J, 2011, MOL BIOL CELL, V22, P4868, DOI 10.1091/mbc.E10-12-0953
   Goncharov RG, 2023, MOL BIOL+, V57, P1143, DOI 10.1134/S0026893323060067
   Gong L, 2006, J BIOL CHEM, V281, P15869, DOI 10.1074/jbc.M511658200
   Gu JM, 2014, CARDIOVASC RES, V104, P83, DOI 10.1093/cvr/cvu177
   Guo C, 2013, EMBO J, V32, P1514, DOI 10.1038/emboj.2013.65
   Haindl M, 2008, EMBO REP, V9, P273, DOI 10.1038/embor.2008.3
   Hang J, 2002, J BIOL CHEM, V277, P19961, DOI 10.1074/jbc.M201799200
   He JL, 2020, INT J MOL SCI, V21, DOI 10.3390/ijms21165657
   He Q, 2023, INT J MOL SCI, V24, DOI 10.3390/ijms24032544
   Heo KS, 2015, J CLIN INVEST, V125, P1299, DOI 10.1172/JCI76453
   Heusch G, 2020, NAT REV CARDIOL, V17, P773, DOI 10.1038/s41569-020-0403-y
   Hickey CM, 2012, NAT REV MOL CELL BIO, V13, P755, DOI 10.1038/nrm3478
   Hu ZL, 2021, MOL CELL, V81, P940, DOI 10.1016/j.molcel.2020.12.024
   Huang C, 2009, EMBO J, V28, P2748, DOI 10.1038/emboj.2009.210
   Huang WJ, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0032960
   Infantino V, 2021, INT J MOL SCI, V22, DOI 10.3390/ijms22115703
   Itahana Y, 2006, MOL CELL BIOL, V26, P4675, DOI 10.1128/MCB.01830-05
   Jia YY, 2020, J EXP CLIN CANC RES, V39, DOI 10.1186/s13046-020-01547-5
   Jiang M, 2011, CELL DEATH DIFFER, V18, P1005, DOI 10.1038/cdd.2010.168
   Jing XM, 2019, MOL CANCER, V18, DOI 10.1186/s12943-019-1089-9
   Kim EY, 2015, J MOL CELL CARDIOL, V78, P154, DOI 10.1016/j.yjmcc.2014.08.003
   Kim EY, 2012, J MOL CELL CARDIOL, V52, P638, DOI 10.1016/j.yjmcc.2011.11.011
   Kuo ML, 2008, CELL CYCLE, V7, P3378, DOI 10.4161/cc.7.21.6930
   Lee YJ, 2013, NEUROMOL MED, V15, P771, DOI 10.1007/s12017-013-8239-9
   Li X, 2022, BIOMATERIALS, V291, DOI 10.1016/j.biomaterials.2022.121904
   Lima CD, 2008, J BIOL CHEM, V283, P32045, DOI 10.1074/jbc.M805655200
   Liu X, 2023, EXP CELL RES, V433, DOI 10.1016/j.yexcr.2023.113822
   Liu X, 2013, PLOS PATHOG, V9, DOI 10.1371/journal.ppat.1003480
   Liu Y, 2023, CELL REP, V42, DOI 10.1016/j.celrep.2023.112041
   Luo YY, 2023, CHINESE MED J-PEKING, V136, P2496, DOI 10.1097/CM9.0000000000002757
   Mao M, 2022, CELL BIOSCI, V12, DOI 10.1186/s13578-022-00850-2
   McMillan LE, 2011, NEUROSCI LETT, V502, P201, DOI 10.1016/j.neulet.2011.07.045
   Mu MC, 2023, CELL DEATH DIFFER, V30, P2393, DOI 10.1038/s41418-023-01228-8
   Mukhopadhyay D, 2007, TRENDS BIOCHEM SCI, V32, P286, DOI 10.1016/j.tibs.2007.05.002
   Mukhopadhyay D, 2010, J CELL BIOL, V188, P681, DOI 10.1083/jcb.200909008
   Murphy MP, 2009, BIOCHEM J, V417, P1, DOI 10.1042/BJ20081386
   Nan J, 2022, EXP MOL MED, V54, P72, DOI 10.1038/s12276-021-00723-7
   Nayak A, 2014, GENOME BIOL, V15, DOI 10.1186/s13059-014-0422-2
   Nishida T, 2000, EUR J BIOCHEM, V267, P6423, DOI 10.1046/j.1432-1327.2000.01729.x
   Nisticò R, 2014, FRONT PHARMACOL, V5, DOI 10.3389/fphar.2014.00063
   Plascencia-Villa G, 2021, ANTIOXID REDOX SIGN, V34, P591, DOI 10.1089/ars.2020.8134
   Ramachandra CJA, 2021, FREE RADICAL BIO MED, V166, P297, DOI 10.1016/j.freeradbiomed.2021.02.040
   Rawlings N, 2019, PLOS ONE, V14, DOI 10.1371/journal.pone.0213331
   Seidman JG, 2001, CELL, V104, P557, DOI 10.1016/S0092-8674(01)00242-2
   Semenza GL, 2003, NAT REV CANCER, V3, P721, DOI 10.1038/nrc1187
   Shah AK, 2021, ANTIOXIDANTS-BASEL, V10, DOI 10.3390/antiox10060931
   Shao CC, 2018, MOL CANCER, V17, DOI 10.1186/s12943-018-0869-y
   Shen LN, 2009, BIOCHEM J, V421, P223, DOI 10.1042/BJ20090246
   Shimizu Y, 2016, J MOL CELL CARDIOL, V97, P56, DOI 10.1016/j.yjmcc.2016.04.008
   Sies H, 2020, NAT REV MOL CELL BIO, V21, P363, DOI 10.1038/s41580-020-0230-3
   Sies H, 2017, ANNU REV BIOCHEM, V86, P715, DOI 10.1146/annurev-biochem-061516-045037
   Sies H, 2015, REDOX BIOL, V4, P180, DOI 10.1016/j.redox.2015.01.002
   Singh A, 2019, MOLECULES, V24, DOI 10.3390/molecules24081583
   Soares ES, 2022, IBRO NEUROSCI REP, V12, P142, DOI 10.1016/j.ibneur.2022.01.003
   Sorrentino A, 2020, BRIT J PHARMACOL, V177, P3162, DOI 10.1111/bph.15093
   Stefanska B, 2014, CLIN CANCER RES, V20, P3118, DOI 10.1158/1078-0432.CCR-13-0283
   Sun ML, 2020, CNS NEUROSCI THER, V26, P815, DOI 10.1111/cns.13398
   Taghvaei S, 2022, FRONT PHARMACOL, V13, DOI 10.3389/fphar.2022.817990
   Tokarz P, 2021, CANCERS, V13, DOI 10.3390/cancers13092059
   Vergari E, 2012, BIOMOLECULES, V2, P269, DOI 10.3390/biom2020269
   Wada H, 2020, J MOL NEUROSCI, V70, P2007, DOI 10.1007/s12031-020-01604-w
   Wang CY, 2019, INT J BIOL SCI, V15, P395, DOI 10.7150/ijbs.27256
   Wang L, 2022, EXP CELL RES, V419, DOI 10.1016/j.yexcr.2022.113281
   Wang LR, 2022, KIDNEY DIS-BASEL, V8, P424, DOI 10.1159/000525308
   Wang TS, 2019, MOL CELL, V75, P823, DOI 10.1016/j.molcel.2019.06.008
   Waters E, 2022, EMBO REP, V23, DOI 10.15252/embr.201948754
   Weeraratna AT, 2007, EXP CELL RES, V313, P450, DOI 10.1016/j.yexcr.2006.10.028
   Wei B, 2018, CANCER RES, V78, P2171, DOI 10.1158/0008-5472.CAN-17-2288
   Willems PHGM, 2015, CELL METAB, V22, P207, DOI 10.1016/j.cmet.2015.06.006
   Wu JJ, 2016, ONCOTARGET, V7, P58995, DOI 10.18632/oncotarget.10636
   Wu ZQ, 2022, J CLIN INVEST, V132, DOI 10.1172/JCI155224
   Xia K, 2024, FREE RADICAL BIO MED, V210, P378, DOI 10.1016/j.freeradbiomed.2023.11.040
   Xia Q, 2023, ISCIENCE, V26, DOI 10.1016/j.isci.2023.106953
   Xia Q, 2021, THERANOSTICS, V11, P7450, DOI 10.7150/thno.60277
   Xu RX, 2015, CELL PHYSIOL BIOCHEM, V35, P913, DOI 10.1159/000369748
   Xu Z, 2008, FASEB J, V22, P127, DOI 10.1096/fj.06-7871com
   Yan S, 2010, EMBO J, V29, P3773, DOI 10.1038/emboj.2010.245
   Yang D, 2022, J AM HEART ASSOC, V11, DOI 10.1161/JAHA.122.027004
   Yeh ETH, 2000, GENE, V248, P1, DOI 10.1016/S0378-1119(00)00139-6
   Yu F, 2001, P NATL ACAD SCI USA, V98, P9630, DOI 10.1073/pnas.181341498
   Zhang HJ, 2016, CELL DEATH DIS, V7, DOI 10.1038/cddis.2016.290
   Zhang QS, 2016, ONCOL LETT, V12, P217, DOI 10.3892/ol.2016.4558
   Zhang Y, 2018, EUR REV MED PHARMACO, V22, P2778, DOI 10.26355/eurrev_201805_14975
   Zhou HJ, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-05812-2
   Zhu HR, 2015, CELL REP, V13, P1183, DOI 10.1016/j.celrep.2015.09.083
   Zhu MY, 2023, MOL THER, V31, P3052, DOI 10.1016/j.ymthe.2023.08.014
   Zunino R, 2007, J CELL SCI, V120, P1178, DOI 10.1242/jcs.03418
   Zunino R, 2009, J BIOL CHEM, V284, P17783, DOI 10.1074/jbc.M901902200
NR 114
TC 1
Z9 1
U1 8
U2 17
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0951-6433
EI 1872-8081
J9 BIOFACTORS
JI Biofactors
PD SEP
PY 2024
VL 50
IS 5
BP 910
EP 921
DI 10.1002/biof.2055
EA MAR 2024
PG 12
WC Biochemistry & Molecular Biology; Endocrinology & Metabolism
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Endocrinology & Metabolism
GA I2Q4H
UT WOS:001193806100001
PM 38551331
DA 2025-04-10
ER

PT J
AU Poyatos-García, J
   Martí, P
   Liquori, A
   Muelas, N
   Pitarch, I
   Martinez-Dolz, L
   Rodríguez, B
   Gonzalez-Quereda, L
   Damiá, M
   Aller, E
   Selva-Gimenez, M
   Vilchez, R
   Diaz-Manera, J
   Alonso-Pérez, J
   Barcena, JE
   Jauregui, A
   Gámez, J
   Aladrén, JA
   Fernández, A
   Montolio, M
   Azorin, I
   Hervas, D
   Casasús, A
   Nieto, M
   Gallano, P
   Sevilla, T
   Vilchez, JJ
AF Poyatos-Garcia, Javier
   Marti, Pilar
   Liquori, Alessandro
   Muelas, Nuria
   Pitarch, Inmaculada
   Martinez-Dolz, Luis
   Rodriguez, Benjamin
   Gonzalez-Quereda, Lidia
   Damia, Maria
   Aller, Elena
   Selva-Gimenez, Marta
   Vilchez, Roger
   Diaz-Manera, Jordi
   Alonso-Perez, Jorge
   Eulalio Barcena, Jose
   Jauregui, Amaia
   Gamez, Josep
   Angel Aladren, Jesus
   Fernandez, Ariadna
   Montolio, Marisol
   Azorin, Inmaculada
   Hervas, David
   Casasus, Ana
   Nieto, Marisa
   Gallano, Pia
   Sevilla, Teresa
   Jesus Vilchez, Juan
TI Dystrophinopathy Phenotypes and Modifying Factors in DMD Exon
   45-55 Deletion
SO ANNALS OF NEUROLOGY
LA English
DT Article
ID BECKER MUSCULAR-DYSTROPHY; GENE; MUTATIONS; QUANTIFICATION; IMPAIRMENT;
   SEVERITY; ISOFORM; MALES
AB Objective Duchenne muscular dystrophy (DMD) exon 45-55 deletion (del45-55) has been postulated as a model that could treat up to 60% of DMD patients, but the associated clinical variability and complications require clarification. We aimed to understand the phenotypes and potential modifying factors of this dystrophinopathy subset. Methods This cross-sectional, multicenter cohort study applied clinical and functional evaluation. Next generation sequencing was employed to identify intronic breakpoints and their impact on the Dp140 promotor, intronic long noncoding RNA, and regulatory splicing sequences. DMD modifiers (SPP1, LTBP4, ACTN3) and concomitant mutations were also assessed. Haplotypes were built using DMD single nucleotide polymorphisms. Dystrophin expression was evaluated via immunostaining, Western blotting, reverse transcription polymerase chain reaction (PCR), and droplet digital PCR in 9 muscle biopsies. Results The series comprised 57 subjects (23 index) expressing Becker phenotype (28%), isolated cardiopathy (19%), and asymptomatic features (53%). Cognitive impairment occurred in 90% of children. Patients were classified according to 10 distinct index-case breakpoints; 4 of them were recurrent due to founder events. A specific breakpoint (D5) was associated with severity, but no significant effect was appreciated due to the changes in intronic sequences. All biopsies showed dystrophin expression of >67% and traces of alternative del45-57 transcript that were not deemed pathogenically relevant. Only the LTBP4 haplotype appeared associated the presence of cardiopathy among the explored extragenic factors. Interpretation We confirmed that del45-55 segregates a high proportion of benign phenotypes, severe cases, and isolated cardiac and cognitive presentations. Although some influence of the intronic breakpoint position and the LTBP4 modifier may exist, the pathomechanisms responsible for the phenotypic variability remain largely unresolved. ANN NEUROL 2022
C1 [Poyatos-Garcia, Javier; Marti, Pilar; Muelas, Nuria; Selva-Gimenez, Marta; Vilchez, Roger; Azorin, Inmaculada; Casasus, Ana; Nieto, Marisa; Sevilla, Teresa; Jesus Vilchez, Juan] Hlth Res Inst Hosp La Fe IIS La Fe, Neuromuscular & Ataxias Res Grp, Valencia, Spain.
   [Poyatos-Garcia, Javier; Marti, Pilar; Muelas, Nuria; Selva-Gimenez, Marta; Vilchez, Roger; Azorin, Inmaculada; Casasus, Ana; Nieto, Marisa; Sevilla, Teresa; Jesus Vilchez, Juan] Ctr Biomed Network Res Rare Dis CIBERER, Valencia, Spain.
   [Poyatos-Garcia, Javier; Marti, Pilar; Muelas, Nuria; Selva-Gimenez, Marta; Vilchez, Roger; Azorin, Inmaculada; Casasus, Ana; Nieto, Marisa; Sevilla, Teresa; Jesus Vilchez, Juan] CB06 05 0091, U763, Valencia, Spain.
   [Liquori, Alessandro] Hlth Res Inst Hosp La Fe IIS La Fe, Hematol Res Grp, Valencia, Spain.
   [Liquori, Alessandro] Ctr Biomed Network Res Canc CIBERONC, Madrid, Spain.
   [Liquori, Alessandro] GB16 12 00284, Madrid, Spain.
   [Muelas, Nuria; Pitarch, Inmaculada; Damia, Maria; Sevilla, Teresa; Jesus Vilchez, Juan] Univ Valencia, Neuromuscular Referral Ctr, European Reference Network Rare Neuromuscular Dis, Valencia, Spain.
   [Muelas, Nuria; Pitarch, Inmaculada; Damia, Maria; Aller, Elena; Sevilla, Teresa; Jesus Vilchez, Juan] Polytech La Fe Hosp, Valencia, Spain.
   [Pitarch, Inmaculada; Damia, Maria] Univ Valencia, Neuropediat Dept, Valencia, Spain.
   [Martinez-Dolz, Luis] Univ Valencia, Cardiol Dept, Valencia, Spain.
   [Martinez-Dolz, Luis] Polytech La Fe Hosp, IIS La Fe, Valencia, Spain.
   [Martinez-Dolz, Luis] Ctr Biomed Network Res Cardiovasc Dis CIBERCV, Valencia, Spain.
   [Rodriguez, Benjamin; Gonzalez-Quereda, Lidia; Gallano, Pia] Hosp Santa Creu & Sant Pau, Genet Dept, IIB St Pau, Barcelona, Spain.
   [Rodriguez, Benjamin; Gonzalez-Quereda, Lidia; Gallano, Pia] Ctr Biomed Network Res Rare Dis CIBERER, U745, U705, CB06 07 0011, Barcelona, Spain.
   [Aller, Elena] Univ Valencia, Genet Unit, Valencia, Spain.
   [Diaz-Manera, Jordi; Alonso-Perez, Jorge] Hosp Santa Creu & Sant Pau, Neuromuscular Disorders Unit, European Reference Network Rare Neuromuscular Dis, Neurol Dept, Barcelona, Spain.
   [Diaz-Manera, Jordi; Alonso-Perez, Jorge; Gamez, Josep] Autonomous Univ Barcelona, Barcelona, Spain.
   [Diaz-Manera, Jordi; Alonso-Perez, Jorge] Ctr Biomed Network Res Rare Dis CIBERER, U762, CB06 05 0030, Barcelona, Spain.
   [Eulalio Barcena, Jose; Jauregui, Amaia] Cruces Univ Hosp, Neurol Serv, Neuromuscular Sect, Baracaldo, Spain.
   [Gamez, Josep] GMA Clin, Neurol Dept, European Reference Network Rare Neuromuscular Dis, Barcelona, Spain.
   [Angel Aladren, Jesus; Fernandez, Ariadna] Calahorra Hosp Fdn, Calahorra, Spain.
   [Montolio, Marisol] Duchenne Parent Project Spain, Madrid, Spain.
   [Montolio, Marisol] Fac Biol, Dept Cell Biol Physiol & Immunol, Barcelona, Spain.
   [Hervas, David] Univ Politecn Valencia, Dept Appl Stat & Operat Res & Qual, Valencia, Spain.
   [Sevilla, Teresa; Jesus Vilchez, Juan] Univ Valencia, Dept Med, Valencia, Spain.
C3 CIBER - Centro de Investigacion Biomedica en Red; CIBERER; University of
   Valencia; University of Valencia; University of Valencia; CIBER - Centro
   de Investigacion Biomedica en Red; CIBERCV; Hospital of Santa Creu i
   Sant Pau; CIBER - Centro de Investigacion Biomedica en Red; CIBERER;
   University of Valencia; Hospital of Santa Creu i Sant Pau; Autonomous
   University of Barcelona; CIBER - Centro de Investigacion Biomedica en
   Red; CIBERER; Hospital Universitario Cruces; University of Barcelona;
   Universitat Politecnica de Valencia; University of Valencia
RP Vilchez, JJ (corresponding author), Hlth Res Inst Hosp La Fe IIS La Fe, Neuromuscular & Ataxias Res Grp, Valencia, Spain.; Vilchez, JJ (corresponding author), La Fe Hosp, Hlth Res Inst La Fe, Neuromuscular Referral Ctr, Neuromuscular Res Grp, Av Fernando Abril Martorell 106, Valencia 46026, Spain.
EM juan.vilchez@uv.es
RI Hervas, David/HTS-1661-2023; Sevilla, Teresa/L-3292-2017;
   Gonzalez-Quereda, Lidia/E-7669-2013; Aller, Elena/A-4803-2010; Marti,
   Pilar/MVW-3120-2025; Poyatos-García, Javier/JYQ-0753-2024; Hervas,
   David/L-1322-2016; Martinez-Dolz, Luis/X-4627-2018; liquori,
   alessandro/K-7934-2015
OI Sevilla, Teresa/0000-0003-4716-2667; Hervas, David/0000-0003-0635-4961;
   Gonzalez, Lidia/0000-0003-0715-6414; Marti, Pilar/0000-0002-1022-9314;
   Martinez-Dolz, Luis/0000-0001-5145-8191; Gamez,
   Josep/0000-0003-3127-7486; Pitarch Castellano,
   Inmaculada/0000-0002-3864-7374; Damia-Vidal, Maria/0000-0003-2933-8438;
   Poyatos-Garcia, Javier/0000-0003-3117-4743; Azorin,
   Inmaculada/0009-0009-6169-3844; Alonso-Perez, Jorge/0000-0001-8866-5186;
   liquori, alessandro/0000-0002-4842-5986; Muelas Gomez,
   Nuria/0000-0002-2349-7481
FU Fundacion Isabel Gemio [2018/0200]; GVA fellowship [APOSTD2021/212];
   Instituto de Salud Carlos III (ISCIII) Madrid [PI16/00316]; Conselleria
   de Sanitat, Generalitat Valenciana [PROMETEO/2019075,
   PROMETEO/2018/135]; Duchenne Parent Project Spain [2018/0541]; ISCIII
   [PI18/01585, PI19/01178]
FX We acknowledge Fundacion Isabel Gemio for the financial support of this
   project and for the PhD grant to J.P.-G. (2018/0200). A.L. is a
   recipient of the GVA fellowship APOSTD2021/212. N.M. and J.J.V. are
   funded by PI16/00316 supported by Instituto de Salud Carlos III (ISCIII)
   Madrid and by PROMETEO/2019075 supported by Conselleria de Sanitat,
   Generalitat Valenciana. I.P. and M.D. are funded by Duchenne Parent
   Project Spain (2018/0541). P.G. and L.G.-Q. are funded by PI18/01585
   supported by ISCIII. T.S. is funded by PROMETEO/2018/135 (Conselleria de
   Sanitat, Generalitat Valenciana) and by PI19/01178 (ISCIII).
CR Anthony K, 2014, NEUROLOGY, V83, P2062, DOI 10.1212/WNL.0000000000001025
   Anthony K, 2011, BRAIN, V134, P3544, DOI 10.1093/brain/awr291
   Aoki Y, 2012, P NATL ACAD SCI USA, V109, P13763, DOI 10.1073/pnas.1204638109
   Bardoni A, 1999, LANCET, V353, P897, DOI 10.1016/S0140-6736(98)05801-2
   Bello L, 2019, J CLIN MED, V8, DOI 10.3390/jcm8050649
   Bello L, 2016, SCI REP-UK, V6, DOI 10.1038/srep32439
   Béroud C, 2007, HUM MUTAT, V28, P196, DOI 10.1002/humu.20428
   Bonne G, 2017, NEUROMUSCULAR DISORD, V27, P1152, DOI 10.1016/j.nmd.2017.10.005
   Bougé AL, 2017, SCI REP-UK, V7, DOI 10.1038/srep39094
   Bovolenta M, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0045328
   Darras BT., GENEREVIEWS, P1993
   Echigoya Y, 2019, MOL THER, V27, P2005, DOI 10.1016/j.ymthe.2019.07.012
   Echigoya Y, 2015, MOL THER-NUCL ACIDS, V4, DOI 10.1038/mtna.2014.76
   Felisari G, 2000, NEUROLOGY, V55, P559, DOI 10.1212/WNL.55.4.559
   Ferreiro V, 2009, MUSCLE NERVE, V39, P239, DOI 10.1002/mus.21193
   Findlay AR, 2015, ANN NEUROL, V77, P668, DOI 10.1002/ana.24365
   Flanigan KM, 2009, HUM MUTAT, V30, P1657, DOI 10.1002/humu.21114
   Gargaun E, 2021, BIOMEDICINES, V9, DOI 10.3390/biomedicines9020219
   Geng C, 2021, FRONT GENET, V12, DOI 10.3389/fgene.2021.638220
   Gentil C, 2012, HUM MOL GENET, V21, P3449, DOI 10.1093/hmg/dds176
   Gurvich OL, 2009, HUM MUTAT, V30, P633, DOI 10.1002/humu.20913
   Mbakam CH, 2022, FRONT MED-LAUSANNE, V9, DOI 10.3389/fmed.2022.859930
   Hinton VJ, 2007, DEV MED CHILD NEUROL, V49, P123, DOI 10.1111/j.1469-8749.2007.00123.x
   Ishmukhametova A, 2012, EUR J HUM GENET, V20, P1096, DOI 10.1038/ejhg.2012.51
   Kaspar RW, 2009, CIRC-CARDIOVASC GENE, V2, P544, DOI 10.1161/CIRCGENETICS.109.867242
   Kerst B, 2000, NEUROMUSCULAR DISORD, V10, P572, DOI 10.1016/S0960-8966(00)00150-4
   Lambert JT, 2020, MUSCLE NERVE, V61, P156, DOI 10.1002/mus.26750
   Lee J, 2018, PLOS ONE, V13, DOI 10.1371/journal.pone.0197084
   Liquori A, 2016, HUM MUTAT, V37, P184, DOI 10.1002/humu.22926
   Miyazaki D, 2009, J HUM GENET, V54, P127, DOI 10.1038/jhg.2008.8
   Muntoni F, 2003, LANCET NEUROL, V2, P731, DOI 10.1016/S1474-4422(03)00585-4
   Nakamura A, 2017, J HUM GENET, V62, P459, DOI 10.1038/jhg.2016.152
   Nakamura A, 2008, J CLIN NEUROSCI, V15, P757, DOI 10.1016/j.jocn.2006.12.012
   Nicolas A, 2015, HUM MOL GENET, V24, P1267, DOI 10.1093/hmg/ddu537
   North KN, 1996, NEUROLOGY, V46, P461, DOI 10.1212/WNL.46.2.461
   Ousterout DG, 2015, NAT COMMUN, V6, DOI 10.1038/ncomms7244
   Ponikowski P, 2016, EUR HEART J, V37, P2129, DOI 10.1093/eurheartj/ehw128
   Pons R, 2017, MUSCLE NERVE, V55, P46, DOI 10.1002/mus.25190
   Poplin R., 2017, bioRxiv, DOI 10.1101/201178
   Ricotti V, 2016, DEV MED CHILD NEUROL, V58, P77, DOI 10.1111/dmcn.12922
   Sironi M, 2003, FEBS LETT, V537, P30, DOI 10.1016/S0014-5793(03)00066-8
   Soblechero-Martín P, 2021, SCI REP-UK, V11, DOI 10.1038/s41598-021-97730-5
   Suzuki H, 2016, INT J MOL SCI, V17, DOI 10.3390/ijms17101722
   Taglia Antonella, 2015, Acta Myol, V34, P9
   Tuffery-Giraud S, 2017, HUM GENET, V136, P1155, DOI 10.1007/s00439-017-1820-9
   van den Bergen JC, 2014, J NEUROL NEUROSUR PS, V85, P747, DOI 10.1136/jnnp-2013-306350
   Verheul RC, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0162467
   Young CS, 2016, CELL STEM CELL, V18, P533, DOI 10.1016/j.stem.2016.01.021
   Young HK, 2008, J CHILD NEUROL, V23, P155, DOI 10.1177/0883073807307975
NR 49
TC 9
Z9 9
U1 2
U2 9
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0364-5134
EI 1531-8249
J9 ANN NEUROL
JI Ann. Neurol.
PD NOV
PY 2022
VL 92
IS 5
BP 793
EP 806
DI 10.1002/ana.26461
EA SEP 2022
PG 14
WC Clinical Neurology; Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA 5M3NS
UT WOS:000850539500001
PM 35897138
OA Green Published, hybrid
DA 2025-04-10
ER

PT J
AU Fisher, JB
   Kim, MS
   Blinka, S
   Ge, ZD
   Wan, TN
   Duris, C
   Christian, D
   Twaroski, K
   North, P
   Auchampach, J
   Lough, J
AF Fisher, Joseph B.
   Kim, Min-Su
   Blinka, Steven
   Ge, Zhi-Dong
   Wan, Tina
   Duris, Christine
   Christian, Desirae
   Twaroski, Kirk
   North, Paula
   Auchampach, John
   Lough, John
TI Stress-Induced Cell-Cycle Activation in Tip60 Haploinsufficient Adult
   Cardiomyocytes
SO PLOS ONE
LA English
DT Article
ID CARDIAC MYOCYTES; GENE-EXPRESSION; BINDING DOMAIN; DNA-SYNTHESIS; P53
   PATHWAY; HEART; PROLIFERATION; APOPTOSIS; PROTEIN; REPAIR
AB Background: Tat-interactive protein 60 (Tip60) is a member of the MYST family of histone acetyltransferases. Studies using cultured cells have shown that Tip60 has various functions including DNA repair, apoptosis and cell-cycle regulation. We globally ablated the Tip60 gene (Htatip), observing that Tip60-null embryos die at the blastocyst stage (Hu et al. Dev. Dyn. 238:2912;2009). Although adult heterozygous (Tip60(+/-)) mice reproduce normally without a haploinsufficient phenotype, stress caused by Myc over-expression induced B-cell lymphoma in Tip60(+/-) adults, suggesting that Tip60 is a tumor suppressor (Gorrini et al. Nature 448: 1063; 2007). These findings prompted assessment of whether Tip60, alternative splicing of which generates two predominant isoforms termed Tip60 alpha and Tip60 beta, functions to suppress the cell-cycle in adult cardiomyocytes.
   Methodology/Principal Findings: Western blotting revealed that Tip60 alpha is the predominant Tip60 isoprotein in the embryonic heart, transitioning at neonatal stages to Tip60 beta, which is the only isoprotein in the adult heart wherein it is highly enriched. Over-expression of Tip60 beta, but not Tip60 alpha, inhibited cell proliferation in NIH3T3 cells; and, Tip60-haploinsufficient cultured neonatal cardiomyocytes exhibited increased cell-cycle activity. To address whether Tip60 beta suppresses the cardiomyocyte cell-cycle in the adult heart, hypertrophic stress was induced in Tip60(+/+) and Tip(+/-) littermates via two methods, Myc over-expression and aortic banding. Based on immunostaining cell-cycle markers and western blotting cyclin D, stress increased cardiomyocyte cell-cycle mobilization in Tip60(+/-) hearts, in comparison with Tip60(+/+) littermates. Aortic-banded Tip60(+/-) hearts also exhibited significantly decreased apoptosis.
   Conclusions/Significance: These findings provide evidence that Tip60 may function in a tumor suppressor pathway(s) to maintain adult cardiomyocytes in replicative senescence.
C1 [Fisher, Joseph B.; Kim, Min-Su; Blinka, Steven; Christian, Desirae; Twaroski, Kirk; Lough, John] Med Coll Wisconsin, Dept Cell Biol Neurobiol & Anat, Milwaukee, WI 53226 USA.
   [Fisher, Joseph B.; Kim, Min-Su; Blinka, Steven; Ge, Zhi-Dong; Wan, Tina; Christian, Desirae; Twaroski, Kirk; Auchampach, John; Lough, John] Med Coll Wisconsin, Ctr Cardiovasc, Milwaukee, WI 53226 USA.
   [Ge, Zhi-Dong; Wan, Tina; Auchampach, John] Med Coll Wisconsin, Dept Pharmacol & Toxicol, Milwaukee, WI 53226 USA.
   [Duris, Christine; North, Paula] Med Coll Wisconsin, Dept Pathol, Div Pediat Pathol, Milwaukee, WI 53226 USA.
C3 Medical College of Wisconsin; Medical College of Wisconsin; Medical
   College of Wisconsin; Medical College of Wisconsin
RP Fisher, JB (corresponding author), Med Coll Wisconsin, Dept Cell Biol Neurobiol & Anat, Milwaukee, WI 53226 USA.
EM jlough@mcw.edu
RI Kim, Chang/H-4759-2011
OI Blinka, Steven/0000-0002-0776-5677
FU National Institutes of Health [HL089471]; American Heart Association
   [0810108Z]; American Heart Association (AHA) [0810108Z] Funding Source:
   American Heart Association (AHA)
FX This work was supported by National Institutes of Health Grant HL089471
   (JL) and by Predoctoral Fellowship #0810108Z from the American Heart
   Association (JBF). The funders had no role in study design, data
   collection and analysis, decision to publish, or preparation of the
   manuscript.
CR Ahuja P, 2010, J CLIN INVEST, V120, P1494, DOI 10.1172/JCI38331
   Banerjee I, 2007, AM J PHYSIOL-HEART C, V293, pH1883, DOI 10.1152/ajpheart.00514.2007
   Bergmann O, 2009, SCIENCE, V324, P98, DOI 10.1126/science.1164680
   Berns K, 2004, NATURE, V428, P431, DOI 10.1038/nature02371
   Bersell K, 2009, CELL, V138, P257, DOI 10.1016/j.cell.2009.04.060
   Engel FB, 2005, GENE DEV, V19, P1175, DOI 10.1101/gad.1306705
   Gehrking KM, 2011, HUM MOL GENET, V20, P2204, DOI 10.1093/hmg/ddr108
   Gevry N, 2007, GENE DEV, V21, P1869, DOI 10.1101/gad.1545707
   Gorrini C, 2007, NATURE, V448, P1063, DOI 10.1038/nature06055
   Hass MR, 2005, J BIOL CHEM, V280, P36895, DOI 10.1074/jbc.M502861200
   Hu YF, 2009, DEV DYNAM, V238, P2912, DOI 10.1002/dvdy.22110
   Ikura T, 2000, CELL, V102, P463, DOI 10.1016/S0092-8674(00)00051-9
   IZUMO S, 1988, P NATL ACAD SCI USA, V85, P339, DOI 10.1073/pnas.85.2.339
   Kajstura J, 2010, CIRC RES, V107, P1374, DOI 10.1161/CIRCRESAHA.110.231498
   KIM KK, 1994, J BIOL CHEM, V269, P22607
   Kim MS, 2006, J BIOL CHEM, V281, P15082, DOI 10.1074/jbc.M513593200
   Kühn B, 2007, NAT MED, V13, P962, DOI 10.1038/nm1619
   Lee HJ, 2001, J BIOL CHEM, V276, P16597, DOI 10.1074/jbc.C000909200
   Lee Y, 2009, APOPTOSIS, V14, P536, DOI 10.1007/s10495-008-0302-x
   Legube G, 2004, J BIOL CHEM, V279, P44825, DOI 10.1074/jbc.M407478200
   Legube G, 2002, EMBO J, V21, P1704, DOI 10.1093/emboj/21.7.1704
   Lehner B, 2006, NAT GENET, V38, P896, DOI 10.1038/ng1844
   LITTLEWOOD TD, 1995, NUCLEIC ACIDS RES, V23, P1686, DOI 10.1093/nar/23.10.1686
   Lough JW, 2002, DEV DYNAM, V223, P419, DOI 10.1002/dvdy.10058
   MacLellan WR, 2005, MOL CELL BIOL, V25, P2486, DOI 10.1128/MCB.25.6.2486-2497.2005
   McAllister D, 2002, GENE, V289, P169, DOI 10.1016/S0378-1119(02)00546-2
   Meckert PC, 2005, CARDIOVASC RES, V67, P116, DOI 10.1016/j.cardiores.2005.02.017
   Muckova K, 2006, AM J PHYSIOL-RENAL, V290, pF70, DOI 10.1152/ajprenal.00358.2004
   Narita M, 2003, CELL, V113, P703, DOI 10.1016/S0092-8674(03)00401-X
   Oh H, 2001, P NATL ACAD SCI USA, V98, P10308, DOI 10.1073/pnas.191169098
   Pajcini KV, 2010, CELL STEM CELL, V7, P198, DOI 10.1016/j.stem.2010.05.022
   Peña AN, 2011, EXP CELL RES, V317, P1534, DOI 10.1016/j.yexcr.2011.02.001
   Porrello ER, 2011, SCIENCE, V331, P1078, DOI 10.1126/science.1200708
   Sapountzi V, 2006, INT J BIOCHEM CELL B, V38, P1496, DOI 10.1016/j.biocel.2006.03.003
   Sdek P, 2011, J CELL BIOL, V194, P407, DOI 10.1083/jcb.201012049
   Soonpaa MH, 1998, CIRC RES, V83, P15, DOI 10.1161/01.RES.83.1.15
   Sun PQ, 2007, CELL, V128, P295, DOI 10.1016/j.cell.2006.11.050
   Sun YL, 2009, NAT CELL BIOL, V11, P1376, DOI 10.1038/ncb1982
   Sykes SM, 2006, MOL CELL, V24, P841, DOI 10.1016/j.molcel.2006.11.026
   Tang Y, 2008, CELL, V133, P612, DOI 10.1016/j.cell.2008.03.025
   Tang Y, 2006, MOL CELL, V24, P827, DOI 10.1016/j.molcel.2006.11.021
   Tyteca S, 2006, MOL CELL, V24, P807, DOI 10.1016/j.molcel.2006.12.005
   Voss AK, 2009, BIOESSAYS, V31, P1050, DOI 10.1002/bies.200900051
   Xiao GS, 2001, CIRC RES, V89, P1122, DOI 10.1161/hh2401.100742
   Yamamoto T, 1997, J BIOL CHEM, V272, P30595, DOI 10.1074/jbc.272.49.30595
   Zhang Y, 2010, PLOS ONE, V5, DOI [10.1371/journal.pone.0015300, 10.1371/journal.pone.0012559]
   Zhong WG, 2006, EMBO J, V25, P3869, DOI 10.1038/sj.emboj.7601252
   Zhu WQ, 2009, PEDIATR CARDIOL, V30, P710, DOI 10.1007/s00246-009-9408-3
NR 48
TC 16
Z9 17
U1 0
U2 4
PU PUBLIC LIBRARY SCIENCE
PI SAN FRANCISCO
PA 185 BERRY ST, STE 1300, SAN FRANCISCO, CA 94107 USA
SN 1932-6203
J9 PLOS ONE
JI PLoS One
PD FEB 14
PY 2012
VL 7
IS 2
AR e31569
DI 10.1371/journal.pone.0031569
PG 12
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA 925CF
UT WOS:000302737400036
PM 22348108
OA Green Submitted, gold, Green Published
DA 2025-04-10
ER

PT J
AU Abebe, EC
   Mengstie, MA
   Seid, MA
   Malik, T
   Dejenie, TA
AF Abebe, Endeshaw Chekol
   Mengstie, Misganaw Asmamaw
   Seid, Mohammed Abdu
   Malik, Tabarak
   Dejenie, Tadesse Asmamaw
TI The evolving roles of alarin in physiological and disease conditions,
   and its future potential clinical implications
SO FRONTIERS IN ENDOCRINOLOGY
LA English
DT Review
DE alarin; the galanin family; neuropeptides; physiological role; clinical
   implications
ID GALANIN-LIKE PEPTIDE; SYMPATHETIC AFFERENT REFLEX; MTOR SIGNALING
   PATHWAY; STIMULATES FOOD-INTAKE; NEUROPEPTIDE-Y; BODY-WEIGHT; SUPEROXIDE
   ANIONS; NERVOUS-SYSTEM; ENERGY-BALANCE; CHRONIC STRESS
AB Alarin is a member of the galanin family of neuropeptides that is widely expressed in the central nervous system and peripheral tissues in humans and rodents. It was initially isolated fifteen years ago in ganglionic cells of human neuroblastoma. Subsequently, it was demonstrated to be broadly distributed in the blood vessels, skin, eyes, peripheral and central nervous systems, thymus, gastrointestinal tract, and endocrine organs of different species. Alarin is a 25 amino acid neuropeptide derived from the alternative splicing of the GALP gene, missing exon 3. It is found to be involved in several physiological functions that include feeding behavior, energy homeostasis, glucose homeostasis, body temperature, and reproduction. It has also vasoactive, anti-inflammatory, anti-edema, and antimicrobial activities. However, the physiological effects of alarin have not been fully elucidated and the receptors that mediate these effects are not currently known. Unearthing the novel biological effects of alarin and its unidentified receptors will therefore be a task in future biomedical research.In addition, alarin is involved in various disease conditions, such as metabolic syndrome, obesity, insulin resistance, type 2 diabetes, diabetic retinopathy, hypertension, cardiac fibrosis, polycystic ovarian syndrome, and depression. Thus, alarin may serve as a promising tool for future pharmacological treatment and diagnosis. But further research is awaited to confirm whether alarin has a protective or pathological role in these diseases. This article provides a comprehensive review on the evolving implications of alarin in a variety of physiological and disease conditions, and its future perspectives.
C1 [Abebe, Endeshaw Chekol; Mengstie, Misganaw Asmamaw] Debre Tabor Univ, Coll Hlth Sci, Dept Med Biochem, Debre Tabor, Ethiopia.
   [Seid, Mohammed Abdu] Debre Tabor Univ, Coll Hlth Sci, Dept Physiol, Debre Tabor, Ethiopia.
   [Malik, Tabarak; Dejenie, Tadesse Asmamaw] Univ Gondar, Coll Med & Hlth Sci, Dept Med Biochem, Gondar, Ethiopia.
C3 University of Gondar
RP Abebe, EC (corresponding author), Debre Tabor Univ, Coll Hlth Sci, Dept Med Biochem, Debre Tabor, Ethiopia.
EM endeshawchekole@gmail.com
RI Dejenie, Tadesse/AAA-4194-2021; Abebe, Endeshaw/AHE-4369-2022; Asmamaw,
   Misganaw/IAR-9902-2023; Seid, Mohammed Abdu/ABM-9450-2022; MALIK,
   TABARAK/M-3672-2014
OI Abdu Seid, Mohammed/0000-0002-3197-5332; MALIK,
   TABARAK/0000-0002-8332-7927; Asmamaw Dejenie,
   Tadesse/0000-0002-2033-6113; Chekol Abebe, Endeshaw/0000-0002-5035-6633
CR Absalan A, 2012, INDIAN J CLIN BIOCHE, V27, P351, DOI 10.1007/s12291-012-0214-y
   Alarslan P, 2018, CUR OP GYN OBS, V1, P72, DOI [DOI 10.18314/COGO.V1I1.1284, 10.18314/cogo.v1i1.1284]
   BLOCH GJ, 1993, PHYSIOL BEHAV, V54, P615, DOI 10.1016/0031-9384(93)90068-Q
   Boughton CK, 2010, BRIT J PHARMACOL, V161, P601, DOI 10.1111/j.1476-5381.2010.00893.x
   Caron A, 2017, ANN NY ACAD SCI, V1391, P35, DOI 10.1111/nyas.13263
   Chan CB, 2011, J NEUROSCI, V31, P8083, DOI 10.1523/JNEUROSCI.1129-11.2011
   Cunningham MJ, 2002, ENDOCRINOLOGY, V143, P755, DOI 10.1210/en.143.3.755
   De Smet K, 2005, BIOTECHNOL LETT, V27, P1337, DOI 10.1007/s10529-005-0936-5
   Dwyer JM, 2012, INT J NEUROPSYCHOPH, V15, P429, DOI 10.1017/S1461145711001702
   Eberhard N, 2013, J NEURO-ONCOL, V114, P165, DOI 10.1007/s11060-013-1177-4
   Eberhard N, 2012, J MOL NEUROSCI, V46, P18, DOI 10.1007/s12031-011-9546-y
   Fang X, 2018, CELL PHYSIOL BIOCHEM, V51, P2041, DOI 10.1159/000495823
   Filkins, 1985, RETICULOENDOTHELIAL, P339, DOI [10.1007/978-1-4613-2353-2_14, DOI 10.1007/978-1-4613-2353-2_14]
   Fraley GS, 2013, NEUROPEPTIDES, V47, P37, DOI 10.1016/j.npep.2012.08.007
   Fraley GS, 2012, NEUROPEPTIDES, V46, P99, DOI 10.1016/j.npep.2011.12.003
   Fraley GS, 2004, HORM BEHAV, V46, P551, DOI 10.1016/j.yhbeh.2004.04.008
   Gong JX, 2019, PEPTIDES, V118, DOI 10.1016/j.peptides.2019.170101
   Gong R, 2006, J BIOL CHEM, V281, P18802, DOI 10.1074/jbc.M512524200
   Gorkem U, 2022, J OBSTET GYNAECOL RE, V48, P980, DOI 10.1111/jog.15176
   Gül FC, 2022, BMC OPHTHALMOL, V22, DOI 10.1186/s12886-022-02403-0
   Gundlach AL, 2001, CLIN EXP PHARMACOL P, V28, P100, DOI 10.1046/j.1440-1681.2001.03411.x
   Guo LL, 2014, J ENDOCRINOL, V223, P217, DOI 10.1530/JOE-14-0102
   Han Y, 2011, J APPL PHYSIOL, V110, P646, DOI 10.1152/japplphysiol.00908.2010
   Hansen KR, 2003, ENDOCRINOLOGY, V144, P4709, DOI 10.1210/en.2003-0748
   Hoeffer CA, 2010, TRENDS NEUROSCI, V33, P67, DOI 10.1016/j.tins.2009.11.003
   Holub BS, 2011, INT J ANTIMICROB AG, V38, P76, DOI 10.1016/j.ijantimicag.2011.02.019
   Hu WJ, 2019, MEDICINE, V98, DOI 10.1097/MD.0000000000016428
   Jabari S, 2019, HISTOCHEM CELL BIOL, V151, P513, DOI 10.1007/s00418-018-1763-9
   Jernigan CS, 2011, PROG NEURO-PSYCHOPH, V35, P1774, DOI 10.1016/j.pnpbp.2011.05.010
   Johnson GL, 2002, SCIENCE, V298, P1911, DOI 10.1126/science.1072682
   Kageyama H, 2013, J MOL NEUROSCI, V50, P443, DOI 10.1007/s12031-013-9952-4
   Kauffman AS, 2005, HORM BEHAV, V48, P141, DOI 10.1016/j.yhbeh.2005.01.010
   Kilinc F, 2020, ACTA ENDOCRINOL-BUCH, V16, P165, DOI 10.4183/aeb.2020.165
   Krasnow SM, 2003, ENDOCRINOLOGY, V144, P813, DOI 10.1210/en.2002-220982
   Kuo LE, 2008, ANN NY ACAD SCI, V1148, P232, DOI 10.1196/annals.1410.035
   Kur J, 2012, PROG RETIN EYE RES, V31, P377, DOI 10.1016/j.preteyeres.2012.04.004
   Kura B, 2020, INT J MOL SCI, V21, DOI 10.3390/ijms21010358
   KYRKOULI SE, 1990, PEPTIDES, V11, P995, DOI 10.1016/0196-9781(90)90023-X
   Lang R, 2007, PHARMACOL THERAPEUT, V115, P177, DOI 10.1016/j.pharmthera.2007.05.009
   Lawrence C, 2011, FRONT NEUROENDOCRIN, V32, P1, DOI 10.1016/j.yfrne.2010.06.001
   Lawrence CB, 2002, J NEUROENDOCRINOL, V14, P853, DOI 10.1046/j.1365-2826.2002.00846.x
   Li JS, 2021, AMINO ACIDS, V53, P1079, DOI 10.1007/s00726-021-03005-8
   Li Man-Qin, 2019, Zhongguo Dang Dai Er Ke Za Zhi, V21, P983
   Li MM, 2022, INT J ENDOCRINOL, V2022, DOI 10.1155/2022/2009724
   Li NX, 2010, SCIENCE, V329, P959, DOI 10.1126/science.1190287
   Li P, 2012, NEUROSCIENCE, V223, P388, DOI 10.1016/j.neuroscience.2012.07.048
   MALENDOWICZ LK, 1994, ENDOCR RES, V20, P307, DOI 10.1080/07435809409035866
   Man PS, 2008, J NEUROENDOCRINOL, V20, P128, DOI 10.1111/j.1365-2826.2007.01625.x
   MAZZOCCHI G, 1992, RES EXP MED, V192, P373, DOI 10.1007/BF02576294
   Mikó A, 2017, NEUROPEPTIDES, V64, P117, DOI 10.1016/j.npep.2016.09.001
   Miko Alexandra, 2014, Temperature (Austin), V1, P51, DOI 10.4161/temp.29790
   Morise T, 2000, J HUM HYPERTENS, V14, P807, DOI 10.1038/sj.jhh.1001114
   Ohtaki T, 1999, J BIOL CHEM, V274, P37041, DOI 10.1074/jbc.274.52.37041
   Ouchi N, 2011, NAT REV IMMUNOL, V11, P85, DOI 10.1038/nri2921
   Pfalzgraff A, 2018, FRONT PHARMACOL, V9, DOI 10.3389/fphar.2018.00281
   Rahn KH, 1999, J HYPERTENS, V17, pS11
   Robinson MJ, 1997, CURR OPIN CELL BIOL, V9, P180, DOI 10.1016/S0955-0674(97)80061-0
   Santic R, 2007, P NATL ACAD SCI USA, V104, P10217, DOI 10.1073/pnas.0608585104
   Santic R, 2006, J MOL NEUROSCI, V29, P145, DOI 10.1385/JMN:29:2:145
   Schmidhuber SM, 2007, J INVEST DERMATOL, V127, P716, DOI 10.1038/sj.jid.5700569
   Schrödl F, 2013, EXP EYE RES, V106, P74, DOI 10.1016/j.exer.2012.11.009
   Spranger J, 2003, DIABETES, V52, P812, DOI 10.2337/diabetes.52.3.812
   Stoyanovitch AG, 2005, DIABETES, V54, P2471, DOI 10.2337/diabetes.54.8.2471
   Székely M, 2005, NEUROPEPTIDES, V39, P103, DOI 10.1016/j.npep.2005.01.005
   SZEKELY M, 1979, ACTA PHYSIOL HUNG, V53, P265
   TATEMOTO K, 1983, FEBS LETT, V164, P124, DOI 10.1016/0014-5793(83)80033-7
   Tyczewska M, 2022, ADV CLIN EXP MED, V31, P643, DOI 10.17219/acem/146775
   Tyczewska M, 2019, ADV CLIN EXP MED, V28, P737, DOI 10.17219/acem/95039
   Van Der Kolk N, 2010, NEUROPEPTIDES, V44, P333, DOI 10.1016/j.npep.2010.04.001
   Wada A, 2013, BIOCHEM BIOPH RES CO, V434, P223, DOI 10.1016/j.bbrc.2013.03.045
   Wada N, 2016, HANDBOOK OF HORMONES: COMPARATIVE ENDOCRINOLOGY FOR BASIC AND CLINICAL RESEARCH, P209, DOI 10.1016/B978-0-12-801028-0.00164-1
   Wang M, 2015, BEHAV BRAIN RES, V280, P128, DOI 10.1016/j.bbr.2014.11.039
   Wang M, 2014, PEPTIDES, V56, P163, DOI 10.1016/j.peptides.2014.04.009
   Wang Q, 2020, NEUROPEPTIDES, V80, DOI 10.1016/j.npep.2020.102021
   Waterson MJ, 2015, CELL METAB, V22, P962, DOI 10.1016/j.cmet.2015.09.026
   Yildirim E, 2021, GYNECOL ENDOCRINOL, V37, P1128, DOI 10.1080/09513590.2021.1950683
   Yoon SC, 2008, NEUROSCI LETT, V434, P23, DOI 10.1016/j.neulet.2008.01.020
   Zhang F, 2014, ACTA PHYSIOL, V212, P17, DOI 10.1111/apha.12342
   Zhang YX, 2020, NAT REV CARDIOL, V17, P170, DOI 10.1038/s41569-019-0260-8
   Zhang ZW, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0139327
   Zheng S, 2013, TRENDS GENET, V29, P442, DOI 10.1016/j.tig.2013.04.003
   Zhou X, 2021, DIABET METAB SYND OB, V14, P379, DOI 10.2147/DMSO.S290072
   Zhuang FZ, 2016, BEHAV BRAIN RES, V313, P158, DOI 10.1016/j.bbr.2016.06.057
   Zhuang FZ, 2016, PEPTIDES, V76, P115, DOI 10.1016/j.peptides.2016.01.002
NR 84
TC 5
Z9 5
U1 1
U2 8
PU FRONTIERS MEDIA SA
PI LAUSANNE
PA AVENUE DU TRIBUNAL FEDERAL 34, LAUSANNE, CH-1015, SWITZERLAND
SN 1664-2392
J9 FRONT ENDOCRINOL
JI Front. Endocrinol.
PD SEP 29
PY 2022
VL 13
AR 1028982
DI 10.3389/fendo.2022.1028982
PG 16
WC Endocrinology & Metabolism
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism
GA 5I7LH
UT WOS:000868533300001
PM 36246892
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Seeley, M
   Huang, W
   Chen, ZY
   Wolff, WO
   Lin, XY
   Xu, XL
AF Seeley, Michael
   Huang, Wei
   Chen, Zhenyue
   Wolff, William Oscar
   Lin, Xueying
   Xu, Xiaolei
TI Depletion of zebrafish titin reduces cardiac contractility by disrupting
   the assembly of Z-discs and A-bands
SO CIRCULATION RESEARCH
LA English
DT Article
DE zebrafish; sarcomere; genetics; cardiac muscle
ID DILATED CARDIOMYOPATHY; HYPERTROPHIC CARDIOMYOPATHY; MUSCULAR-DYSTROPHY;
   KINASE DOMAIN; PROTEIN TITIN; DANIO-RERIO; M-LINE; MUSCLE; GIANT; GENE
AB The genetic study of titin has been notoriously difficult because of its size and complicated alternative splicing routes. Here, we have used zebrafish as an animal model to investigate the functions of individual titin isoforms. We identified 2 titin orthologs in zebrafish, ttna and ttnb, and annotated the full-length genomic sequences for both genes. We found that ttna, but not ttnb, is required for sarcomere assembly in the heart as well as the subsequent establishment of cardiac contractility. In fact, ttna is the earliest sarcomeric mRNA that is expressed in the heart, which makes it an early molecular marker for cardiomyocyte differentiation. Surprisingly, ttna is required for later steps of sarcomere assembly, including the assembly of Z-discs and A-bands, but not for early steps such as the assembly of Z-bodies and nonstriated myosin filaments. Reduction of individual titin isoforms in vivo using morpholino-modified antisense oligonucleotides indicated that ( 1) both N2B exon-containing and N2A exon-containing isoforms of ttna are required for sarcomere assembly in the heart; ( 2) N2A exon-containing isoforms of both ttna and ttnb are required for sarcomere assembly in the somites; and ( 3) the N2B exon-containing isoforms of ttnb are expressed later than other titin isoforms and are probably involved in modulating their expression; however, these isoforms of ttnb are not required for sarcomere assembly. Collectively, our results reveal distinct functions of different titin isoforms and suggest that various phenotypes in "titinopathies" may be attributable to the disruption of different titin isoforms.
C1 Mayo Clin, Coll Med, Dept Biochem & Mol Biol, Div Cardiovasc Dis, Rochester, MN 55905 USA.
   Shanghai Jiao Tong Univ, Ruijin Hosp, Dept Cardiol, Sch Med, Shanghai 200030, Peoples R China.
C3 Mayo Clinic; Shanghai Jiao Tong University
RP Xu, XL (corresponding author), Mayo Clin, Coll Med, Dept Biochem & Mol Biol, Div Cardiovasc Dis, GU1701C,200 1st St SW, Rochester, MN 55905 USA.
EM xu.xiaolei@mayo.edu
FU NHLBI NIH HHS [HL81753-01, R01 HL081753, R01 HL081753-02] Funding
   Source: Medline
CR Bang ML, 2001, CIRC RES, V89, P1065, DOI 10.1161/hh2301.100981
   Bos JM, 2006, MOL GENET METAB, V88, P78, DOI 10.1016/j.ymgme.2005.10.008
   Brette F, 2003, CIRC RES, V92, P1182, DOI 10.1161/01.RES.0000074908.17214.FD
   Clark KA, 2002, ANNU REV CELL DEV BI, V18, P637, DOI 10.1146/annurev.cellbio.18.012502.105840
   Costa ML, 2003, BRAZ J MED BIOL RES, V36, P1117, DOI 10.1590/S0100-879X2003000800019
   Devoto SH, 1996, DEVELOPMENT, V122, P3371
   Freiburg A, 2000, CIRC RES, V86, P1114
   Gerull B, 2002, NAT GENET, V30, P201, DOI 10.1038/ng815
   Granzier HL, 2004, CIRC RES, V94, P284, DOI 10.1161/01.RES.0000117769.88862.F8
   Gregorio CC, 1999, CURR OPIN CELL BIOL, V11, P18, DOI 10.1016/S0955-0674(99)80003-9
   Hackman JPV, 2003, ANN MED, V35, P434, DOI 10.1080/07853890310012797
   Hackman P, 2002, AM J HUM GENET, V71, P492, DOI 10.1086/342380
   Itoh-Satoh M, 2002, BIOCHEM BIOPH RES CO, V291, P385, DOI 10.1006/bbrc.2002.6448
   Knöll R, 2002, CELL, V111, P943, DOI 10.1016/s0092-8674(02)01226-6
   LABEIT S, 1995, SCIENCE, V270, P293, DOI 10.1126/science.270.5234.293
   Lahmers S, 2004, CIRC RES, V94, P505, DOI 10.1161/01.RES.0000115522.52554.86
   Lange S, 2006, TRENDS CELL BIOL, V16, P11, DOI 10.1016/j.tcb.2005.11.007
   Lange S, 2005, SCIENCE, V308, P1599, DOI 10.1126/science.1110463
   Lange S, 2002, J CELL SCI, V115, P4925, DOI 10.1242/jcs.00181
   McElhinny AS, 2002, J CELL BIOL, V157, P125, DOI 10.1083/jcb.200108089
   Miller G, 2003, J CELL SCI, V116, P4811, DOI 10.1242/jcs.00768
   Miller MK, 2004, TRENDS CELL BIOL, V14, P119, DOI 10.1016/j.tcb.2004.01.003
   Miller MK, 2003, J MOL BIOL, V333, P951, DOI 10.1016/j.jmb.2003.09.012
   Musa H, 2006, J CELL SCI, V119, P4322, DOI 10.1242/jcs.03198
   Nasevicius A, 2000, NAT GENET, V26, P216, DOI 10.1038/79951
   Opitz CA, 2004, CIRC RES, V94, P967, DOI 10.1161/01.RES.0000124301.48193.E1
   Pelster B, 1996, CIRC RES, V79, P358, DOI 10.1161/01.RES.79.2.358
   Person V, 2000, J CELL SCI, V113, P3851
   Sanger JW, 2001, J CELL BIOL, V154, P21, DOI 10.1083/jcb.200106072
   Satoh M, 1999, BIOCHEM BIOPH RES CO, V262, P411, DOI 10.1006/bbrc.1999.1221
   Sorimachi H, 1995, J BIOL CHEM, V270, P31158, DOI 10.1074/jbc.270.52.31158
   Tskhovrebova L, 2003, NAT REV MOL CELL BIO, V4, P679, DOI 10.1038/nrm1198
   van der Ven PFM, 2000, J CELL SCI, V113, P1405
   Van der Ven PFM, 1999, J MUSCLE RES CELL M, V20, P569, DOI 10.1023/A:1005569225773
   Wanga J., 2001, Journal of Submicroscopic Cytology and Pathology, V33, P275
   Warren CM, 2004, MECH DEVELOP, V121, P1301, DOI 10.1016/j.mod.2004.07.003
   Weinert S, 2006, J CELL BIOL, V173, P559, DOI 10.1083/jcb.200601014
   Xu XL, 2002, NAT GENET, V30, P205, DOI 10.1038/ng816
   Xu YF, 2000, DEV DYNAM, V219, P201, DOI 10.1002/1097-0177(2000)9999:9999<::AID-DVDY1043>3.3.CO;2-9
   Yelon D, 1999, DEV BIOL, V214, P23, DOI 10.1006/dbio.1999.9406
   Zhang Y, 2000, J CELL SCI, V113, P3103
NR 41
TC 71
Z9 88
U1 0
U2 6
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA 530 WALNUT ST, PHILADELPHIA, PA 19106-3621 USA
SN 0009-7330
J9 CIRC RES
JI Circ.Res.
PD FEB 2
PY 2007
VL 100
IS 2
BP 238
EP 245
DI 10.1161/01.RES.0000255758.69821.b5
PG 8
WC Cardiac & Cardiovascular Systems; Hematology; Peripheral Vascular
   Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology; Hematology
GA 132KT
UT WOS:000243942400011
PM 17170364
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Kocher, O
   Yesilaltay, A
   Cirovic, C
   Pal, R
   Rigotti, A
   Krieger, M
AF Kocher, O
   Yesilaltay, A
   Cirovic, C
   Pal, R
   Rigotti, A
   Krieger, M
TI Targeted disruption of the PDZK1 gene in mice causes tissue-specific
   depletion of the high density lipoprotein receptor scavenger receptor
   class B type I and altered lipoprotein metabolism
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID AUTOSOMAL RECESSIVE HYPERCHOLESTEROLEMIA; DOMAIN-CONTAINING PROTEIN;
   SR-BI; LIPID-METABOLISM; HUMAN CARCINOMAS; ADAPTER PROTEIN;
   DOWN-REGULATION; LDL RECEPTOR; IDENTIFICATION; EXPRESSION
AB PDZK1, a multi-PDZ domain containing adaptor protein, interacts with various membrane proteins, including the high density lipoprotein (HDL) receptor scavenger receptor class B type I (SR-BI). Here we show that PDZK1 controls in a tissue-specific and post-transcriptional fashion the expression of SR-BI in vivo. SR-BI protein expression in PDZK1 knock-out (KO) mice was reduced by 95% in the liver, 50% in the proximal intestine, and not affected in steroidogenic organs (adrenal, ovary, and testis). Thus, PDZK1 joins a growing list of adaptors that control tissue-specific activity of cell surface receptors. Hepatic expression of SR-BII, a minor splice variant with an alternative C-terminal cytoplasmic domain, was not affected in PDZK1 KO mice, suggesting that binding of PDZK1 to SR-BI is required for controlling hepatic SR-BI expression. The loss of hepatic SR-BI was the likely cause of the elevation in plasma total and HDL cholesterol and the increase in HDL particle size in PDZK1 KO mice, phenotypes similar to those observed in SR-BI KO mice. PDZK1 KO mice differed from SR-BI KO mice in that the ratio of unesterified to total plasma cholesterol was normal, females were fertile, and cholesteryl ester stores in steroidogenic organs were essentially unaffected. These differences may be due to nearly normal extrahepatic expression of SR-BI in PDZK1 KO mice. The PDZK1-dependent regulation of hepatic SR-BI and, thus, lipoprotein metabolism supports the proposal that this adaptor may represent a new target for therapeutic intervention in cardiovascular disease.
C1 Beth Israel Deaconess Med Ctr, Dept Pathol, Boston, MA 02215 USA.
   Harvard Univ, Sch Med, Boston, MA 02215 USA.
   MIT, Dept Biol, Cambridge, MA 02139 USA.
   Pontificia Univ Catolica Chile, Fac Med, Dept Gastroenterol, Santiago, Chile.
C3 Harvard University; Harvard University Medical Affiliates; Beth Israel
   Deaconess Medical Center; Harvard University; Harvard Medical School;
   Massachusetts Institute of Technology (MIT); Pontificia Universidad
   Catolica de Chile
RP Kocher, O (corresponding author), Beth Israel Deaconess Med Ctr, Dept Pathol, 330 Brookline Ave, Boston, MA 02215 USA.
RI Krieger, Marco/AAE-8611-2020
FU FIC NIH HHS [TW006153] Funding Source: Medline; NHLBI NIH HHS [HL64737,
   HL66105] Funding Source: Medline
CR Acton S, 1996, SCIENCE, V271, P518, DOI 10.1126/science.271.5248.518
   Arai T, 1999, P NATL ACAD SCI USA, V96, P12050, DOI 10.1073/pnas.96.21.12050
   Braun A, 2003, P NATL ACAD SCI USA, V100, P7283, DOI 10.1073/pnas.1237725100
   Braun A, 2002, CIRC RES, V90, P270, DOI 10.1161/hh0302.104462
   BROWN MS, 1986, SCIENCE, V232, P33
   Garcia CK, 2001, SCIENCE, V292, P1394, DOI 10.1126/science.1060458
   Gentzsch M, 2003, J BIOL CHEM, V278, P6440, DOI 10.1074/jbc.M211050200
   Gisler SM, 2001, J BIOL CHEM, V276, P9206, DOI 10.1074/jbc.M008745200
   GLASS C, 1983, P NATL ACAD SCI-BIOL, V80, P5435, DOI 10.1073/pnas.80.17.5435
   GLOMSET JA, 1968, J LIPID RES, V9, P155
   Gu XJ, 2000, J BIOL CHEM, V275, P29993, DOI 10.1074/jbc.275.39.29993
   He GC, 2002, J BIOL CHEM, V277, P44044, DOI 10.1074/jbc.M208539200
   Hung AY, 2002, J BIOL CHEM, V277, P5699, DOI 10.1074/jbc.R100065200
   Ikemoto M, 2000, P NATL ACAD SCI USA, V97, P6538, DOI 10.1073/pnas.100114397
   Ji Y, 1997, J BIOL CHEM, V272, P20982, DOI 10.1074/jbc.272.34.20982
   Kocher O, 1998, LAB INVEST, V78, P117
   Kocher O, 2003, MOL CELL BIOL, V23, P1175, DOI 10.1128/MCB.23.4.1175-1180.2003
   Kocher O, 1996, AM J PATHOL, V149, P493
   Kocher O, 1999, LAB INVEST, V79, P1161
   Kocher O, 1995, CLIN CANCER RES, V1, P1209
   Krieger M, 1999, CURR OPIN LIPIDOL, V10, P491, DOI 10.1097/00041433-199912000-00003
   Krieger M, 1999, ANNU REV BIOCHEM, V68, P523, DOI 10.1146/annurev.biochem.68.1.523
   Landschulz KT, 1996, J CLIN INVEST, V98, P984, DOI 10.1172/JCI118883
   Liang KH, 1999, KIDNEY INT, V56, P621, DOI 10.1046/j.1523-1755.1999.00585.x
   Mardones P, 2003, J BIOL CHEM, V278, P7884, DOI 10.1074/jbc.M211627200
   Miettinen HE, 2001, J CLIN INVEST, V108, P1717, DOI 10.1172/JCI13288
   Pawson T, 1997, SCIENCE, V278, P2075, DOI 10.1126/science.278.5346.2075
   Rigotti A, 2003, ENDOCR REV, V24, P357, DOI 10.1210/er.2001-0037
   Rigotti A, 1997, P NATL ACAD SCI USA, V94, P12610, DOI 10.1073/pnas.94.23.12610
   Rigotti A, 1996, J BIOL CHEM, V271, P33545, DOI 10.1074/jbc.271.52.33545
   Silver DL, 2003, J BIOL CHEM, V278, P28528, DOI 10.1074/jbc.M304109200
   Silver DL, 2002, J BIOL CHEM, V277, P34042, DOI 10.1074/jbc.M206584200
   STEIN Y, 1983, BIOCHIM BIOPHYS ACTA, V752, P98, DOI 10.1016/0005-2760(83)90237-0
   Trigatti B, 1999, P NATL ACAD SCI USA, V96, P9322, DOI 10.1073/pnas.96.16.9322
   Van Eck M, 2003, J BIOL CHEM, V278, P23699, DOI 10.1074/jbc.M211233200
   Voshol PJ, 2001, BIOCHEM J, V356, P317, DOI 10.1042/0264-6021:3560317
   Wang SS, 2000, CELL, V103, P169, DOI 10.1016/S0092-8674(00)00096-9
   Webb NR, 1998, J BIOL CHEM, V273, P15241, DOI 10.1074/jbc.273.24.15241
   Webb NR, 1997, J LIPID RES, V38, P1490
   Wilund KR, 2002, HUM MOL GENET, V11, P3019, DOI 10.1093/hmg/11.24.3019
   Witt W, 2000, J LIPID RES, V41, P2009
   Zuliani G, 1999, ARTERIOSCL THROM VAS, V19, P802, DOI 10.1161/01.ATV.19.3.802
NR 42
TC 146
Z9 167
U1 0
U2 5
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
SN 0021-9258
J9 J BIOL CHEM
JI J. Biol. Chem.
PD DEC 26
PY 2003
VL 278
IS 52
BP 52820
EP 52825
DI 10.1074/jbc.M310482200
PG 6
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 756LX
UT WOS:000187480700101
PM 14551195
OA hybrid
DA 2025-04-10
ER

PT J
AU Chowdhury, HM
   Sharmin, N
   Baran, MY
   Long, L
   Morrell, NW
   Trembath, RC
   Nasim, MT
AF Chowdhury, H. M.
   Sharmin, N.
   Baran, Merve Yuzbasioglu
   Long, L.
   Morrell, N. W.
   Trembath, R. C.
   Nasim, Md Talat
TI BMPRII deficiency impairs apoptosis via the BMPRII-ALK1-BclX-mediated
   pathway in pulmonary arterial hypertension
SO HUMAN MOLECULAR GENETICS
LA English
DT Article
ID BONE MORPHOGENETIC PROTEIN; SMOOTH-MUSCLE; CELL PROLIFERATION; BCL-XL;
   EXPRESSION; GROWTH; RECEPTOR; ACTIVATION; INHIBITION; CONTRIBUTES
AB Pulmonary arterial hypertension (PAH) is a devastating cardiovascular disorder characterized by the remodelling of pre-capillary pulmonary arteries. The vascular remodelling observed in PAH patients results from excessive proliferation and apoptosis resistance of pulmonary arterial smooth muscle cells (PASMCs) and pulmonary arterial endothelial cells (PAECs). We have previously demonstrated that mutations in the type II receptor for bone morphogenetic protein (BMPRII) underlie the majority of the familial and inherited forms of the disease. We have further demonstrated that BMPRII deficiency promotes excessive proliferation and attenuates apoptosis in PASMCs, but the underlying mechanisms remain unclear. The major objective of this study is to investigate how BMPRII deficiency impairs apoptosis in PAH. Using multidisciplinary approaches, we demonstrate that deficiency in the expression of BMPRII impairs apoptosis by modulating the alternative splicing of the apoptotic regulator, B-cell lymphoma X (Bcl-x) transcripts: a finding observed in circulating leukocytes and lungs of PAH subjects, hypoxia-induced PAH rat lungs as well as in PASMCs and PAECs. BMPRII deficiency elicits cell specific effects: promoting the expression of Bcl-xL transcripts in PASMCs while inhibiting it in ECs, thus exerting differential apoptotic effects in these cells. The pro-survival effect of BMPRII receptor is mediated through the activin receptor-like kinase 1 (ALK1) but not the ALK3 receptor. Finally, we show that BMPRII interacts with the ALK1 receptor and pathogenic mutations in the BMPR2 gene abolish this interaction. Taken together, dysfunctional BMPRII responsiveness impairs apoptosis via the BMPRII-ALK1-Bcl-xL pathway in PAH. We suggest Bcl-xL as a potential biomarker and druggable target.
C1 [Chowdhury, H. M.; Trembath, R. C.; Nasim, Md Talat] Kings Coll London, Dept Med & Mol Genet, London SE1 9RT, England.
   [Sharmin, N.; Baran, Merve Yuzbasioglu; Nasim, Md Talat] Univ Bradford, Sch Pharm & Med Sci, Bradford BD7 1DP, W Yorkshire, England.
   [Sharmin, N.] Univ Dhaka, Dept Pharmaceut Technol, Dhaka 1000, Bangladesh.
   [Baran, Merve Yuzbasioglu] Hacettepe Univ, Fac Pharm, Dept Pharmacognosy, TR-06100 Ankara, Turkey.
   [Long, L.; Morrell, N. W.] Univ Cambridge, Dept Med, Div Resp Med, Cambridge CB2 0QQ, England.
   [Trembath, R. C.; Nasim, Md Talat] Guys & St Thomas NHS Fdn Trust, Biomed Res Ctr, NIHR, London SE1 9RT, England.
   [Trembath, R. C.; Nasim, Md Talat] Kings Coll London, London SE1 9RT, England.
   [Nasim, Md Talat] CHASA, Lalmonirhat 5500, Bangladesh.
C3 University of London; King's College London; University of Bradford;
   University of Dhaka; Hacettepe University; University of Cambridge;
   University of London; King's College London; Guy's & St Thomas' NHS
   Foundation Trust; University of London; King's College London
RP Nasim, MT (corresponding author), Univ Bradford, Sch Pharm & Med Sci, Bradford BD7 1DP, W Yorkshire, England.
EM t.nasim@bradford.ac.uk
RI ; YUZBASIOGLU BARAN, MERVE/AAS-1642-2020
OI Nasim, Talat/0000-0003-1968-5663; YUZBASIOGLU BARAN,
   MERVE/0000-0002-7482-0429; Morrell, Nicholas/0000-0001-5700-9792
FU Department of Health via the National Institute for Health Research
   (NIHR) Comprehensive Biomedical Research Centre award; King's College
   London; Heptagon Life Science Proof of Concept Fund [KCL24]; Great
   Britain Sasakawa Foundation [B70]; Royal Society [43049]; Medical
   Research Council [G900865]; University of Bradford [003200,
   66006/001NAS, DH005]; Commonwealth Scholarship Commission; Scientific
   and Technological Research Council of Turkey (TUBITAK)
FX Department of Health via the National Institute for Health Research
   (NIHR) Comprehensive Biomedical Research Centre award to Guy's & St
   Thomas' National Health Service (NHS) Foundation Trust in partnership
   with King's College London (fellowship awarded to M.T.N.); Heptagon Life
   Science Proof of Concept Fund (grant KCL24 to M.T.N.); the Great Britain
   Sasakawa Foundation (grant B70 to M.T.N.); the Royal Society (grant
   43049 to M.T.N.); the Medical Research Council (grant G900865 to R.C.T.,
   M.T.N. and N.W.M.); University of Bradford (grants 003200, 66006/001NAS
   and DH005 to M.T.N.); Commonwealth Scholarship Commission (scholarship
   to N.S.); UK and Scientific and Technological Research Council of Turkey
   (TUBITAK; scholarship to M.Y.B.).
CR Atkinson C, 2002, CIRCULATION, V105, P1672, DOI 10.1161/01.CIR.0000012754.72951.3D
   Chowdhury HM, 2018, HUM MOL GENET, V27, P373, DOI 10.1093/hmg/ddx409
   Dai Y, 2010, PLOS ONE, V5, DOI 10.1371/journal.pone.0014153
   David L, 2007, BLOOD, V109, P1953, DOI 10.1182/blood-2006-07-034124
   Feng B, 2004, CELL IMMUNOL, V232, P9, DOI 10.1016/j.cellimm.2005.01.006
   Gaine SP, 1998, LANCET, V352, P719, DOI 10.1016/S0140-6736(98)02111-4
   Geraci MW, 2001, CIRC RES, V88, P555, DOI 10.1161/01.RES.88.6.555
   Gräf S, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-03672-4
   Hadinnapola C, 2017, CIRCULATION, V136, P2022, DOI 10.1161/CIRCULATIONAHA.117.028351
   Harrison RE, 2003, J MED GENET, V40, P865, DOI 10.1136/jmg.40.12.865
   Ishida W, 2000, J BIOL CHEM, V275, P6075, DOI 10.1074/jbc.275.9.6075
   Kasof GM, 2001, ONCOGENE, V20, P7965, DOI 10.1038/sj.onc.1204985
   König HG, 2005, J CELL BIOL, V168, P1077, DOI 10.1083/jcb.200407027
   Lagna G, 2006, AM J PHYSIOL-LUNG C, V291, pL1059, DOI 10.1152/ajplung.00180.2006
   Lane KB, 2000, NAT GENET, V26, P81, DOI 10.1038/79226
   Long L, 2006, CIRC RES, V98, P818, DOI 10.1161/01.RES.0000215809.47923.fd
   Long L, 2015, NAT MED, V21, P777, DOI 10.1038/nm.3877
   Long L, 2009, CIRCULATION, V119, P566, DOI 10.1161/CIRCULATIONAHA.108.821504
   Tu L, 2011, AM J RESP CELL MOL, V45, P311, DOI 10.1165/rcmb.2010-0317OC
   Montero J, 2018, CELL DEATH DIFFER, V25, P56, DOI 10.1038/cdd.2017.183
   Morrell NW, 2009, J AM COLL CARDIOL, V54, pS20, DOI 10.1016/j.jacc.2009.04.018
   Morrell NW, 1999, AM J PHYSIOL-LUNG C, V277, pL440, DOI 10.1152/ajplung.1999.277.3.L440
   Morrell NW, 2001, CIRCULATION, V104, P790, DOI 10.1161/hc3201.094152
   Nasim MT, 2008, HUM MOL GENET, V17, P1683, DOI 10.1093/hmg/ddn059
   Nasim MT, 2006, NAT PROTOC, V1, P1022, DOI 10.1038/nprot.2006.148
   Nasim MT, 2012, HUM MOL GENET, V21, P2548, DOI 10.1093/hmg/dds073
   Nasim MT, 2011, HUM MUTAT, V32, P1385, DOI 10.1002/humu.21605
   Nasim MT, 2005, NUCLEIC ACIDS RES, V33, DOI 10.1093/nar/gni066
   Ogo T, 2013, AM J RESP CELL MOL, V48, P733, DOI 10.1165/rcmb.2012-0049OC
   Qian J, 2009, MOL CANCER THER, V8, P101, DOI 10.1158/1535-7163.MCT-08-0973
   Scharpfenecker M, 2007, J CELL SCI, V120, P964, DOI 10.1242/jcs.002949
   Shabestari RM, 2017, BIOMED PHARMACOTHER, V87, P274, DOI 10.1016/j.biopha.2016.12.070
   Spender LC, 2009, CELL DEATH DIFFER, V16, P593, DOI 10.1038/cdd.2008.183
   Sugimori K, 2005, J BONE MINER METAB, V23, P411, DOI 10.1007/s00774-005-0622-7
   Suzuki YJ, 2007, AM J RESP CELL MOL, V36, P678, DOI 10.1165/rcmb.2006-0359OC
   Teichert-Kuliszewska K, 2006, CIRC RES, V98, P209, DOI 10.1161/01.RES.0000200180.01710.e6
   Trembath R. C., 2001, Journal of Heart and Lung Transplantation, V20, P175, DOI 10.1016/S1053-2498(00)00352-1
   Trembath RC, 2001, NEW ENGL J MED, V345, P325, DOI 10.1056/NEJM200108023450503
   Valdimarsdottir G, 2002, CIRCULATION, V106, P2263, DOI 10.1161/01.CIR.0000033830.36431.46
   Xiang H, 2006, MOL CELL BIOL, V26, P8599, DOI 10.1128/MCB.01062-06
   Zhang ML, 2015, P NATL ACAD SCI USA, V112, P12480, DOI 10.1073/pnas.1516208112
   Zhang S, 2003, AM J PHYSIOL-LUNG C, V285, pL740, DOI 10.1152/ajplung.00284.2002
   Zhang XL, 2017, ONCOTARGET, V8, P63923, DOI 10.18632/oncotarget.19209
NR 43
TC 15
Z9 15
U1 0
U2 6
PU OXFORD UNIV PRESS
PI OXFORD
PA GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND
SN 0964-6906
EI 1460-2083
J9 HUM MOL GENET
JI Hum. Mol. Genet.
PD JUL 1
PY 2019
VL 28
IS 13
BP 2161
EP 2173
DI 10.1093/hmg/ddz047
PG 13
WC Biochemistry & Molecular Biology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Genetics & Heredity
GA IH1OD
UT WOS:000474259700005
PM 30809644
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Torok, R
   Salamon, A
   Sumegi, E
   Zadori, D
   Veres, G
   Molnar, MF
   Vecsei, L
   Klivenyi, P
AF Torok, Rita
   Salamon, Andras
   Sumegi, Evelin
   Zadori, Denes
   Veres, Gabor
   Molnar, Mate Fort
   Vecsei, Laszlo
   Klivenyi, Peter
TI Effect of MPTP on mRNA expression of PGC-1α in mouse brain
SO BRAIN RESEARCH
LA English
DT Article
DE FL-PGC-1 alpha; NT-PGC-1 alpha; CNS-PGC-1 alpha; MPTP; Preconditioning;
   Dopamine
ID FOCAL CEREBRAL-ISCHEMIA; AGE-OF-ONSET; PARKINSONS-DISEASE;
   3-NITROPROPIONIC ACID; HUNTINGTONS-DISEASE; ALPHA-SYNUCLEIN; MODEL;
   TOLERANCE; ISOFORM; PGC-1
AB The peroxisome proliferator-activated receptor-gamma (PPAR gamma) coactivator 1 alpha (PGC-1 alpha) is a key regulator of mitochondrial biogenesis, respiration and adaptive thermogenesis. Besides the full-length protein (FLPGC-1 alpha), several other functionally active PGC-la isoforms were identified as a result of alternative splicing (e.g., N-truncated PGC-1 alpha; NT-PGC-1 alpha) or alternative promoter usage (e.g., central nervous system specific PGC-1 alpha isoforms; CNS-PGC-1 alpha). Achieving neuroprotection via CNS-targeted pharmacological stimulation is limited due to poor penetration of the blood brain barrier (BBB) by the proposed pharmaceutical agents, so preconditioning emerged as another option. The current study aimed to examine of how the expression levels of FL-, NT-, CNS- and reference PGC-1 alpha isoforms change in different brain regions following various 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) treatment regimens, including chronic low-dose treatment for preconditioning. Ninety minutes following the acute treatment regimen, the expression levels of FL-, NT- and CNS-PGC-la isoforms increased significantly in the striatum, cortex and cerebellum. However, this elevation diminished 7 days following the last MPTP injection in the acute treatment regimen. The chronic low-dose administration of MPTP, which did not cause significant toxic effects in light of the relatively unaltered dopamine levels, did not result in any significant change of PGC-1 alpha expression. The elevation of PGC-1 alpha levels following acute treatment may demonstrate a short-term compensatory mechanism against mitochondrial damage induced by the complex I inhibitor MPTP. However, drug-induced preconditioning by chronic low-dose MPTP seems not to induce protective responses via the PGC-1 alpha system. (C) 2017 Elsevier B.V. All rights reserved.
C1 [Torok, Rita; Salamon, Andras; Sumegi, Evelin; Zadori, Denes; Molnar, Mate Fort; Vecsei, Laszlo; Klivenyi, Peter] Univ Szeged, Dept Neurol, Semmelweis U 6, H-6725 Szeged, Hungary.
   [Veres, Gabor; Vecsei, Laszlo] Hungarian Acad Sci, MTA SZTE Neurosci Res Grp, Semmelweis U 6, H-6725 Szeged, Hungary.
   [Veres, Gabor; Vecsei, Laszlo] Univ Szeged, Semmelweis U 6, H-6725 Szeged, Hungary.
C3 Szeged University; Hungarian Academy of Sciences; Neuroscience Research
   Group, HAS; Szeged University
RP Klivenyi, P (corresponding author), Univ Szeged, Dept Neurol, Semmelweis U 6, H-6725 Szeged, Hungary.
EM klivenyi.peter@med.u-szeged.hu
RI Vecsei, Laszlo/ABA-6137-2021; Klivenyi, Peter/LOR-7860-2024; Gábor,
   Veres/AAG-2564-2020; Zadori, Denes/B-4907-2012
OI Zadori, Denes/0000-0003-0749-7980; Salamon, Andras/0000-0002-9946-8230;
   Veres, Gabor/0000-0003-4413-779X; Klivenyi, Peter/0000-0002-5389-3266;
   Maszlag-Torok, Rita/0000-0003-1697-331X
FU Hungarian Brain Research Program [KTIA_13_NAP-A-II/18]; MTA-SZTE
   Neuroscience Research Group; Hungarian Academy of Sciences
FX The study was supported by the Hungarian Brain Research Program - Grant
   No. KTIA_13_NAP-A-II/18 and MTA-SZTE Neuroscience Research Group. Denes
   Zadori was supported by the Janos Bolyai Research Scholarship of the
   Hungarian Academy of Sciences.
CR Bayer H, 2017, NEUROBIOL DIS, V97, P36, DOI 10.1016/j.nbd.2016.11.001
   Binienda Z, 1998, NEUROSCI LETT, V251, P173, DOI 10.1016/S0304-3940(98)00539-4
   Bose A, 2016, J NEUROCHEM, V139, P216, DOI 10.1111/jnc.13731
   Breidert T, 2002, J NEUROCHEM, V82, P615, DOI 10.1046/j.1471-4159.2002.00990.x
   Brouillet E, 2005, J NEUROCHEM, V95, P1521, DOI 10.1111/j.1471-4159.2005.03515.x
   Chang JS, 2012, J BIOL CHEM, V287, P9100, DOI 10.1074/jbc.M111.320200
   Choi J, 2013, BIOCHEM BIOPH RES CO, V435, P671, DOI 10.1016/j.bbrc.2013.05.041
   Ciron C, 2012, HUM MOL GENET, V21, P1861, DOI 10.1093/hmg/ddr618
   Ciron C, 2015, ACTA NEUROPATHOL COM, V3, DOI 10.1186/s40478-015-0200-8
   Clark J, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0048925
   Clark J, 2011, BMC MED GENET, V12, DOI 10.1186/1471-2350-12-69
   Dehmer T, 2004, J NEUROCHEM, V88, P494, DOI 10.1046/j.1471-4159.2003.02210.x
   Ebrahim AS, 2010, NEUROSCI LETT, V473, P120, DOI 10.1016/j.neulet.2010.02.034
   Eschbach J, 2015, ANN NEUROL, V77, P15, DOI 10.1002/ana.24294
   Forno LS, 1996, J NEUROPATH EXP NEUR, V55, P259, DOI 10.1097/00005072-199603000-00001
   Forno Lysia S., 1993, V60, P600
   Harris JB, 2004, J NEUROL NEUROSUR PS, V75, P29, DOI 10.1136/jnnp.2004.046318
   Horiguchi T, 2003, STROKE, V34, P1015, DOI 10.1161/01.STR.0000063404.27912.5B
   JAVITCH JA, 1985, P NATL ACAD SCI USA, V82, P2173, DOI 10.1073/pnas.82.7.2173
   Kalinderi K, 2016, ACTA NEUROL SCAND, V134, P314, DOI 10.1111/ane.12563
   Knutti D, 2001, TRENDS ENDOCRIN MET, V12, P360, DOI 10.1016/S1043-2760(01)00457-X
   Kurosaki R, 2004, PHARMACOL BIOCHEM BE, V78, P143, DOI 10.1016/j.pbb.2004.03.006
   Livak KJ, 2001, METHODS, V25, P402, DOI 10.1006/meth.2001.1262
   Martínez-Redondo V, 2015, DIABETOLOGIA, V58, P1969, DOI 10.1007/s00125-015-3671-z
   Mudò G, 2012, CELL MOL LIFE SCI, V69, P1153, DOI 10.1007/s00018-011-0850-z
   Rees EM, 2014, MOVEMENT DISORD, V29, P1648, DOI 10.1002/mds.25984
   Riepe MW, 1997, J CEREBR BLOOD F MET, V17, P257, DOI 10.1097/00004647-199703000-00002
   Ruas JL, 2012, CELL, V151, P1319, DOI 10.1016/j.cell.2012.10.050
   Soyal SM, 2012, HUM MOL GENET, V21, P3461, DOI 10.1093/hmg/dds177
   St-Pierre J, 2006, CELL, V127, P397, DOI 10.1016/j.cell.2006.09.024
   Su XM, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0134087
   Swanson CR, 2013, PPAR RES, V2013, DOI 10.1155/2013/582809
   TAKADA M, 1993, NEUROSCI LETT, V150, P49, DOI 10.1016/0304-3940(93)90105-T
   Tan RH, 2016, ANN NEUROL, V79, P295, DOI 10.1002/ana.24565
   Tomai F, 1999, CIRCULATION, V100, P559, DOI 10.1161/01.CIR.100.5.559
   Török R, 2015, CELL MOL NEUROBIOL, V35, P293, DOI 10.1007/s10571-014-0124-z
   Wiegand F, 1999, J CEREBR BLOOD F MET, V19, P1229, DOI 10.1097/00004647-199911000-00007
   Wu T, 2013, BRAIN, V136, P696, DOI 10.1093/brain/aws360
   Zheng B, 2010, SCI TRANSL MED, V2, DOI 10.1126/scitranslmed.3001059
NR 39
TC 11
Z9 14
U1 0
U2 5
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 0006-8993
EI 1872-6240
J9 BRAIN RES
JI Brain Res.
PD APR 1
PY 2017
VL 1660
BP 20
EP 26
DI 10.1016/j.brainres.2017.01.032
PG 7
WC Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA EQ3XA
UT WOS:000398006100003
PM 28161458
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Liu, X
   Shao, YJ
   Tu, JZC
   Sun, JP
   Dong, B
   Wang, ZC
   Zhou, JR
   Chen, L
   Tao, J
   Chen, JM
AF Liu, Xiang
   Shao, Yijia
   Tu, Jiazichao
   Sun, Jiapan
   Dong, Bing
   Wang, Zhichao
   Zhou, Jianrong
   Chen, Long
   Tao, Jun
   Chen, Jimei
TI TMAO-Activated Hepatocyte-Derived Exosomes Impair Angiogenesis
   via Repressing CXCR4
SO FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY
LA English
DT Article
DE trimethylamine-N-oxide; hepatocyte-derived exosomes; endothelial
   function; angiogenesis; C-X-C motif chemokine receptor 4; alternative
   polyadenylation
ID TRIMETHYLAMINE-N-OXIDE; CELLS; REENDOTHELIALIZATION;
   PHOSPHATIDYLCHOLINE; ATHEROSCLEROSIS; METABOLISM; INJURY; MICE
AB Objective: Trimethylamine-N-oxide (TMAO) was found to play crucial roles in vascular endothelial function. However, the exact molecular mechanisms are not yet entirely clear. Recently, we found that exosomes (Exos) isolated from TMAO-treated hepatocytes (TMAO-Exos) contained a distinctive profile of miRNAs compared to those from the TMAO-free group (Control-Exos). Furthermore, TMAO-Exos could notably promote inflammation, damage vascular endothelial cells (VECs), and impair endothelium-dependent vasodilation. This study aimed to further evaluate the effects of TMAO-Exos on VECs and explore the underlying mechanisms.Methods: Exos were isolated from the hepatocyte culture supernatant with or without TMAO, using differential centrifugation. Then, VECs were treated with these Exos for 48 h and subjected to RNA-sequencing for detecting the changes of alternative polyadenylation (APA) and mRNA. After validation by qPCR and western blotting, the recombinant viruses were used to mediate the overexpression of C-X-C motif chemokine receptor 4 (CXCR4). The in vitro VEC function was evaluated by cell migration and tube formation, and in vivo angiogenesis was investigated in hindlimb ischemia models.Results: Exos released from hepatocytes were differentially regulated by TMAO; both could be taken up by VECs; and furthermore, TMAO-Exos significantly reduced cell migration and tube formation in vitro and impaired perfusion recovery and angiogenesis after hindlimb ischemia, by down-regulating the CXCR4 expression. However, TMAO-Exos failed to regulate the splicing events, at least in this experimental setting, which suggested that TMAO-Exos may affect CXCR4 expression via an APA-independent manner.Conclusions: Our findings revealed a novel indirect mechanism by which TMAO impaired endothelial function through stimulating hepatocytes to produce Exos that possessed distinctive activity. The crosstalk between the liver and vascular endothelial mediated by these Exos may offer a new target for restraining the harmful effects induced by TMAO.
C1 [Liu, Xiang; Tu, Jiazichao; Zhou, Jianrong; Chen, Jimei] Guangdong Prov Peoples Hosp, Guangdong Acad Med Sci, Guangdong Cardiovasc Inst, Dept Cardiac Surg, Guangzhou, Peoples R China.
   [Liu, Xiang; Tu, Jiazichao; Zhou, Jianrong; Chen, Jimei] Guangdong Prov Key Lab South China Struct Heart D, Guangzhou, Peoples R China.
   [Liu, Xiang; Tu, Jiazichao; Zhou, Jianrong; Chen, Jimei] South China Univ Technol, Sch Med, Guangzhou, Peoples R China.
   [Shao, Yijia; Dong, Bing; Wang, Zhichao; Tao, Jun] Sun Yat Sen Univ, Affiliated Hosp 1, Dept Hypertens & Vasc Dis, Guangzhou, Peoples R China.
   [Shao, Yijia; Dong, Bing; Wang, Zhichao; Tao, Jun] Sun Yat Sen Univ, NHC Key Lab Assisted Circulat, Guangzhou, Peoples R China.
   [Sun, Jiapan] Hong Kong Univ Sci & Technol, Med Ctr, Shenzhen Peking Univ, Peking Univ,Shenzhen Hosp,Dept Geriatr, Shenzhen, Peoples R China.
   [Chen, Long] Southern Med Univ, Shenzhen Hosp, Int Med Dept, Shenzhen, Peoples R China.
C3 Guangdong Academy of Medical Sciences & Guangdong General Hospital;
   Southern Medical University - China; South China University of
   Technology; Sun Yat Sen University; Sun Yat Sen University; Hong Kong
   University of Science & Technology; Peking University; Southern Medical
   University - China
RP Chen, JM (corresponding author), Guangdong Prov Peoples Hosp, Guangdong Acad Med Sci, Guangdong Cardiovasc Inst, Dept Cardiac Surg, Guangzhou, Peoples R China.; Chen, JM (corresponding author), Guangdong Prov Key Lab South China Struct Heart D, Guangzhou, Peoples R China.; Chen, JM (corresponding author), South China Univ Technol, Sch Med, Guangzhou, Peoples R China.; Tao, J (corresponding author), Sun Yat Sen Univ, Affiliated Hosp 1, Dept Hypertens & Vasc Dis, Guangzhou, Peoples R China.; Tao, J (corresponding author), Sun Yat Sen Univ, NHC Key Lab Assisted Circulat, Guangzhou, Peoples R China.; Chen, L (corresponding author), Southern Med Univ, Shenzhen Hosp, Int Med Dept, Shenzhen, Peoples R China.
EM chenl_sz@smu.edu.cn; taojungz123@163.com; jimei_1965@outlook.com
FU National Key Research and Development Program of China [2018YFC1002600,
   2020YFC2008005]; Guangdong peak project; Science and Technology Projects
   in Guangzhou [202102021149, 202002020030]; Postdoctoral Scientific
   Research Start-up Fund Project of Guangdong Provincial People's Hospital
   [BY012021052]; National Nature Science Foundation of China [82100451,
   81670226]; Guangdong Natural Science Foundation of Guangdong
   [2020A1515011264]
FX This work was supported by the National Key Research and Development
   Program of China (No. 2018YFC1002600 and No. 2020YFC2008005), the
   Guangdong peak project (No. DFJH 2019), the Science and Technology
   Projects in Guangzhou (No. 202102021149 and No. 202002020030), the
   Postdoctoral Scientific Research Start-up Fund Project of Guangdong
   Provincial People's Hospital (BY012021052), the National Nature Science
   Foundation of China (No. 82100451 and No. 81670226), and the Guangdong
   Natural Science Foundation of Guangdong (2020A1515011264).
CR Bowler E, 2019, INT J MOL SCI, V20, DOI 10.3390/ijms20092067
   Brown JM, 2018, NAT REV MICROBIOL, V16, P171, DOI 10.1038/nrmicro.2017.149
   Brunt VE, 2020, HYPERTENSION, V76, P101, DOI 10.1161/HYPERTENSIONAHA.120.14759
   Chen LD, 2020, BIOCHEM BIOPH RES CO, V530, P95, DOI 10.1016/j.bbrc.2020.06.093
   Chen L, 2010, CARDIOVASC RES, V88, P462, DOI 10.1093/cvr/cvq207
   Chen SF, 2019, CELL METAB, V30, P1141, DOI 10.1016/j.cmet.2019.08.021
   Cheng M, 2019, NAT COMMUN, V10, DOI 10.1038/s41467-019-08895-7
   Ciullo A, 2019, INT J MOL SCI, V20, DOI 10.3390/ijms20030468
   Coffey AR, 2019, PHYSIOL GENOMICS, V51, P59, DOI 10.1152/physiolgenomics.00079.2018
   Döring Y, 2017, CIRCULATION, V136, P388, DOI 10.1161/CIRCULATIONAHA.117.027646
   Fareh M, 2012, CELL DEATH DIFFER, V19, P232, DOI 10.1038/cdd.2011.89
   Fu YG, 2018, GENOME RES, V28, P1656, DOI 10.1101/gr.231506.117
   Fu YG, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0145477
   Fu YG, 2011, GENOME RES, V21, P741, DOI 10.1101/gr.115295.110
   Gruber AJ, 2019, NAT REV GENET, V20, P599, DOI 10.1038/s41576-019-0145-z
   Guo MH, 2020, ACTA BIOCH BIOPH SIN, V52, P791, DOI 10.1093/abbs/gmaa065
   Hirsova P, 2016, GASTROENTEROLOGY, V150, P956, DOI 10.1053/j.gastro.2015.12.037
   Ibrahim A, 2016, ANNU REV PHYSIOL, V78, P67, DOI 10.1146/annurev-physiol-021115-104929
   Ji YD, 2021, NAT METAB, V3, P1163, DOI 10.1038/s42255-021-00444-1
   Jiang FJ, 2020, J HEPATOL, V72, P156, DOI 10.1016/j.jhep.2019.09.014
   Ke YL, 2018, FREE RADICAL BIO MED, V116, P88, DOI 10.1016/j.freeradbiomed.2018.01.007
   Kern J, 2008, ARTERIOSCL THROM VAS, V28, P478, DOI 10.1161/ATVBAHA.107.160432
   Kourembanas S, 2015, ANNU REV PHYSIOL, V77, P13, DOI 10.1146/annurev-physiol-021014-071641
   Li TJ, 2017, FRONT PHYSIOL, V8, DOI 10.3389/fphys.2017.00350
   Li XSM, 2017, EUR HEART J, V38, P814, DOI 10.1093/eurheartj/ehw582
   Liu X, 2021, ANN TRANSL MED, V9, DOI 10.21037/atm-21-5043
   Liu X, 2022, FOOD SCI NUTR, V10, P295, DOI 10.1002/fsn3.2671
   Liu YR, 2020, MEDIAT INFLAMM, V2020, DOI 10.1155/2020/4634172
   Luo X, 2021, WORLD J GASTROENTERO, V27, DOI 10.3748/wjg.v27.i14.1419
   Momen-Heravi F, 2015, SCI REP-UK, V5, DOI 10.1038/srep09991
   Murphy PA, 2018, ELIFE, V7, DOI 10.7554/eLife.29494
   Murphy PA, 2014, ARTERIOSCL THROM VAS, V34, P2042, DOI 10.1161/ATVBAHA.114.303879
   Nagarajan SR, 2019, AM J PHYSIOL-ENDOC M, V316, pE578, DOI 10.1152/ajpendo.00365.2018
   Nakao Y, 2021, FRONT CELL DEV BIOL, V9, DOI 10.3389/fcell.2021.735001
   Noels H, 2014, ARTERIOSCL THROM VAS, V34, P1209, DOI 10.1161/ATVBAHA.113.302878
   Nojima H, 2016, PLOS ONE, V11, DOI 10.1371/journal.pone.0161443
   Ogino N, 2021, LIFE SCI, V278, DOI 10.1016/j.lfs.2021.119588
   Ou ZJ, 2016, AM J PHYSIOL-ENDOC M, V311, pE781, DOI 10.1152/ajpendo.00218.2016
   Petit I, 2007, TRENDS IMMUNOL, V28, P299, DOI 10.1016/j.it.2007.05.007
   Seldin MM, 2016, J AM HEART ASSOC, V5, DOI 10.1161/JAHA.115.002767
   Shannon P, 2003, GENOME RES, V13, P2498, DOI 10.1101/gr.1239303
   Singh GB, 2019, INT J MOL SCI, V20, DOI 10.3390/ijms20143570
   Szklarczyk D, 2019, NUCLEIC ACIDS RES, V47, pD607, DOI [10.1093/nar/gky1131, 10.1093/nar/gkac1000]
   Tang WHW, 2014, J AM COLL CARDIOL, V64, P1908, DOI 10.1016/j.jacc.2014.02.617
   Tang WHW, 2013, NEW ENGL J MED, V368, P1575, DOI 10.1056/NEJMoa1109400
   Vidal M, 2019, TRAFFIC, V20, P815, DOI 10.1111/tra.12687
   Wang XH, 2014, J MOL CELL CARDIOL, V74, P139, DOI 10.1016/j.yjmcc.2014.05.001
   Wang ZN, 2011, NATURE, V472, P57, DOI 10.1038/nature09922
   WU JC, 1994, P NATL ACAD SCI USA, V91, P674, DOI 10.1073/pnas.91.2.674
   Xia XJ, 2020, J AM HEART ASSOC, V9, DOI 10.1161/JAHA.119.014120
   Yu BB, 2019, EBIOMEDICINE, V42, P64, DOI 10.1016/j.ebiom.2019.03.031
   Zernecke A, 2008, CIRC RES, V102, P209, DOI 10.1161/CIRCRESAHA.107.160697
   Zhang L, 2015, SCI REP-UK, V5, DOI 10.1038/srep13403
   Zheng B, 2017, MOL THER, V25, P1279, DOI 10.1016/j.ymthe.2017.03.031
   Zhou L, 2018, J CARDIOVASC PHARM, V72, P176, DOI 10.1097/FJC.0000000000000611
   Zhu WF, 2016, CELL, V165, P111, DOI 10.1016/j.cell.2016.02.011
   Ziegler ME, 2016, ANGIOGENESIS, V19, P359, DOI 10.1007/s10456-016-9509-6
NR 57
TC 12
Z9 14
U1 1
U2 15
PU FRONTIERS MEDIA SA
PI LAUSANNE
PA AVENUE DU TRIBUNAL FEDERAL 34, LAUSANNE, CH-1015, SWITZERLAND
SN 2296-634X
J9 FRONT CELL DEV BIOL
JI Front. Cell. Dev. Biol.
PD JAN 31
PY 2022
VL 9
AR 804049
DI 10.3389/fcell.2021.804049
PG 13
WC Cell Biology; Developmental Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Developmental Biology
GA ZC5RW
UT WOS:000757578100001
PM 35174166
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Pujol-Lereis, LM
   Liebisch, G
   Schick, T
   Lin, YC
   Grassmann, F
   Uchida, K
   Zipfel, PF
   Fauser, S
   Skerka, C
   Weber, BHF
AF Pujol-Lereis, Luciana M.
   Liebisch, Gerhard
   Schick, Tina
   Lin, Yuchen
   Grassmann, Felix
   Uchida, Koji
   Zipfel, Peter F.
   Fauser, Sascha
   Skerka, Christine
   Weber, Bernhard H. F.
TI Evaluation of serum sphingolipids and the influence of genetic risk
   factors in age-related macular degeneration
SO PLOS ONE
LA English
DT Article
ID COMPLEMENT FACTOR-H; STRESS-INDUCED APOPTOSIS; GENOME-WIDE ASSOCIATION;
   OXIDATIVE STRESS; DENSITY-LIPOPROTEIN; PLASMA CERAMIDES;
   CHOLESTEROL-METABOLISM; CARDIOVASCULAR-DISEASE; FATTY-ACIDS;
   MALONDIALDEHYDE
AB Sphingolipids are bioactive molecules associated with oxidative stress, inflammation, and neurodegenerative diseases, but poorly studied in the context of age-related macular degeneration (AMD), a prevalent sight-threatening disease of the ageing retina. Here, we found higher serum levels of hexosylceramide (HexCer) d18:1/16:0 in patients with choroidal neovascularization (CNV) and geographic atrophy (GA), two manifestations of late stage AMD, and higher ceramide (Cer) d18:1/16:0 levels in GA patients. A sensitivity analysis of genetic variants known to be associated with late stage AMD showed that rs1061170 (p.Y402H) in the complement factor H (CFH) gene influences the association of Cer d18:1/ 16:0 with GA. To understand the possible influence of this genetic variant on ceramide levels, we established a cell-based assay to test the modulation of genes in the ceramide metabolism by factor H-like protein 1 (FHL-1), an alternative splicing variant of CFH that also harbors the 402 residue. We first showed that malondialdehyde-acetaldehyde adducts, an oxidation product commonly found in AMD retinas, induces an increase in ceramide levels in WERI-Rb1 cells in accordance with an increased expression of ceramide synthesis genes. Then, we observed that cells exposed to the non-risk FHL-1 :Y402, but not the risk associated variant FHL-1 :H402 or full-length CFH, downregulated ceramide synthase 2 and ceramide glucosyltransferase gene expression. Together, our findings show that serum ceramide and hexosylceramide species are altered in AMD patients and that ceramide levels may be influenced by AMD associated risk variants.
C1 [Pujol-Lereis, Luciana M.; Grassmann, Felix; Weber, Bernhard H. F.] Univ Regensburg, Inst Human Genet, Regensburg, Germany.
   [Liebisch, Gerhard] Univ Regensburg, Inst Clin Chem & Lab Med, Regensburg, Germany.
   [Schick, Tina; Fauser, Sascha] Univ Hosp Cologne, Dept Ophthalmol, Cologne, Germany.
   [Lin, Yuchen; Zipfel, Peter F.; Skerka, Christine] Leibniz Inst Nat Prod Res & Infect Biol, Dept Infect Biol, Jena, Germany.
   [Uchida, Koji] Univ Tokyo, Grad Sch Agr & Life Sci, Tokyo, Japan.
   [Fauser, Sascha] F Hoffmann La Roche, Basel, Switzerland.
   [Pujol-Lereis, Luciana M.] CIDIE CONICET, Ctr Invest & Desarrollo Inmunol & Enfermedades In, Cordoba, Argentina.
C3 University of Regensburg; University of Regensburg; University of
   Cologne; Leibniz Association; Hans Knoll Institute (HKI); University of
   Tokyo; Roche Holding
RP Pujol-Lereis, LM; Weber, BHF (corresponding author), Univ Regensburg, Inst Human Genet, Regensburg, Germany.; Pujol-Lereis, LM (corresponding author), CIDIE CONICET, Ctr Invest & Desarrollo Inmunol & Enfermedades In, Cordoba, Argentina.
EM lpujollereis@cidie.ucc.edu.ar; bweb@klinik.uni-regensburg.de
RI ; Liebisch, Gerhard/G-6130-2010
OI Uchida, Koji/0000-0003-3894-5299; Liebisch, Gerhard/0000-0003-4886-0811;
   Grassmann, Felix/0000-0003-1390-7528; Pujol Lereis, Luciana
   Mercedes/0000-0002-7009-2743
FU Alexander von Humboldt Foundation; institutional funds of Titel Group 77
   (Institute of Human Genetics); Bavarian State Ministry of Education and
   Cultural Affairs, Science and the Arts; National Scientific and
   Technical Research Council (CONICET) from Argentina; F. Hoffmann - La
   Roche
FX The work was supported by the Alexander von Humboldt Foundation and
   institutional funds of Titel Group 77 (Institute of Human Genetics).
   LMPL was supported by the Alexander von Humboldt Foundation as a Georg
   Forster Postdoctoral Fellow, and by a Grant for female scientists from
   the Bavarian State Ministry of Education and Cultural Affairs, Science
   and the Arts, and is now supported by The National Scientific and
   Technical Research Council (CONICET) from Argentina. F. Hoffmann - La
   Roche provided support in the form of salary for Dr. Sascha Fauser, but
   did not have any additional role in the study. The funders had no role
   in study design, data collection and analysis, decision to publish, or
   preparation of the manuscript. The specific roles of the authors are
   articulated in the 'author contributions' section.
CR Abrahan CE, 2010, INVEST OPHTH VIS SCI, V51, P1171, DOI 10.1167/iovs.09-3909
   Acar N, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0035102
   Ambreen F, 2014, J PAK MED ASSOC, V64, P664
   Bartke N, 2009, J LIPID RES, V50, pS91, DOI 10.1194/jlr.R800080-JLR200
   BASU SK, 1976, P NATL ACAD SCI USA, V73, P3178, DOI 10.1073/pnas.73.9.3178
   BENJAMINI Y, 1995, J R STAT SOC B, V57, P289, DOI 10.1111/j.2517-6161.1995.tb02031.x
   Blachnio-Zabielska A, 2016, ADV MED SCI-POLAND, V61, P72, DOI 10.1016/j.advms.2015.09.006
   BLIGH EG, 1959, CAN J BIOCHEM PHYS, V37, P911
   Bode GH, 2014, J IMMUNOL, V192, P1154, DOI 10.4049/jimmunol.1301673
   Butt AL, 2011, OPHTHALMOLOGY, V118, P1380, DOI 10.1016/j.ophtha.2010.11.007
   Cackett P, 2008, AM J OPHTHALMOL, V146, P960, DOI 10.1016/j.ajo.2008.06.026
   Chen W, 2010, P NATL ACAD SCI USA, V107, P7401, DOI 10.1073/pnas.0912702107
   Clark SJ, 2014, J IMMUNOL, V193, P4962, DOI 10.4049/jimmunol.1401613
   Cougnard-Grégoire A, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0090973
   Cutler RG, 2004, P NATL ACAD SCI USA, V101, P2070, DOI 10.1073/pnas.0305799101
   Davari MH, 2013, J RES HEALTH SCI, V13, P98
   Demirkan A, 2013, J PSYCHIATR RES, V47, P357, DOI 10.1016/j.jpsychires.2012.11.001
   Dossarps D, 2016, OPHTHALMIC RES, V56, P41, DOI 10.1159/000444059
   Edwards AO, 2005, SCIENCE, V308, P421, DOI 10.1126/science.1110189
   Erdreich-Epstein A, 2000, CANCER RES, V60, P707
   Erke MG, 2014, ACTA OPHTHALMOL, V92, P662, DOI 10.1111/aos.12346
   Fauser S, 2011, INVEST OPHTH VIS SCI, V52, P5525, DOI 10.1167/iovs.10-6827
   Fonteh AN, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0125597
   Fox TE, 2006, DIABETES, V55, P3573, DOI 10.2337/db06-0539
   FRAENKELCONRAT H, 1949, J BIOL CHEM, V177, P385
   Fritsche LG, 2016, NAT GENET, V48, P134, DOI 10.1038/ng.3448
   Fritsche LG, 2013, NAT GENET, V45, P433, DOI 10.1038/ng.2578
   Futerman AH, 2004, EMBO REP, V5, P777, DOI 10.1038/sj.embor.7400208
   German OL, 2006, INVEST OPHTH VIS SCI, V47, P1658, DOI 10.1167/iovs.05-1310
   Gorusupudi A, 2016, J LIPID RES, V57, P499, DOI 10.1194/jlr.P065540
   Grassmann F, 2017, GENOME MED, V9, DOI 10.1186/s13073-017-0418-0
   Grassmann F, 2017, GENETICS, V205, P919, DOI 10.1534/genetics.116.195966
   Hannun YA, 2008, NAT REV MOL CELL BIO, V9, P139, DOI 10.1038/nrm2329
   Hellwage J, 1997, BIOCHEM J, V326, P321, DOI 10.1042/bj3260321
   Hyman L, 2000, ARCH OPHTHALMOL-CHIC, V118, P351, DOI 10.1001/archopht.118.3.351
   Hynes RO, 2002, CELL, V110, P673, DOI 10.1016/S0092-8674(02)00971-6
   Jakobsdottir J, 2005, AM J HUM GENET, V77, P389, DOI 10.1086/444437
   Kang S, 2007, HISTOPATHOLOGY AGE R, P1
   Kannan R, 2004, FREE RADICAL BIO MED, V37, P166, DOI 10.1016/j.freeradbiomed.2004.04.011
   Kim M, 2017, J ALZHEIMERS DIS, V60, P809, DOI 10.3233/JAD-160645
   KLEIN R, 1993, OPHTHALMOLOGY, V100, P406
   Klein RJ, 2005, SCIENCE, V308, P385, DOI 10.1126/science.1109557
   Klein R, 2014, AM J OPHTHALMOL, V158, P513, DOI 10.1016/j.ajo.2014.05.027
   Klein Ronald, 2003, Ophthalmology, V110, P1273, DOI 10.1016/S0161-6420(03)00599-2
   Klein R, 2010, ARCH OPHTHALMOL-CHIC, V128, P750, DOI 10.1001/archophthalmol.2010.92
   Kuhn S, 1996, EUR J IMMUNOL, V26, P2383, DOI 10.1002/eji.1830261017
   KUHN S, 1995, J IMMUNOL, V155, P5663
   Larsen PJ, 2014, MOL METAB, V3, P252, DOI 10.1016/j.molmet.2014.01.011
   Liebisch G, 1999, J LIPID RES, V40, P1539
   Liebisch G, 2004, BBA-MOL CELL BIOL L, V1686, P108, DOI 10.1016/j.bbalip.2004.09.003
   Liebisch G, 2013, J LIPID RES, V54, P1523, DOI 10.1194/jlr.M033506
   Merle BMJ, 2014, INVEST OPHTH VIS SCI, V55, P2010, DOI 10.1167/iovs.14-13916
   Merle BMJ, 2013, J NUTR, V143, P505, DOI 10.3945/jn.112.171033
   Mielke MM, 2017, J ALZHEIMERS DIS, V60, P819, DOI 10.3233/JAD-160925
   Mielke MM, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0073094
   Mielke MM, 2012, NEUROLOGY, V79, P633, DOI 10.1212/WNL.0b013e318264e380
   Mielke MM, 2010, NEUROBIOL AGING, V31, P17, DOI 10.1016/j.neurobiolaging.2008.03.011
   Neale BM, 2010, P NATL ACAD SCI USA, V107, P7395, DOI 10.1073/pnas.0912019107
   Nita M, 2016, OXID MED CELL LONGEV, V2016, DOI 10.1155/2016/3164734
   Nixon GF, 2009, BRIT J PHARMACOL, V158, P982, DOI 10.1111/j.1476-5381.2009.00281.x
   Nowak M, 2005, CLIN EXP MED, V4, P183, DOI 10.1007/s10238-004-0054-z
   Pandey MK, 2017, NATURE, V543, P108, DOI 10.1038/nature21368
   Paun CC, 2015, INVEST OPHTH VIS SCI, V56, P7766, DOI 10.1167/iovs.15-17035
   Poli V, 1998, J BIOL CHEM, V273, P29279, DOI 10.1074/jbc.273.45.29279
   Ristau T, 2014, INVEST OPHTH VIS SCI, V55, P210, DOI 10.1167/iovs.13-13248
   Rivera A, 2005, HUM MOL GENET, V14, P3227, DOI 10.1093/hmg/ddi353
   Sanvicens N, 2006, J NEUROCHEM, V98, P1432, DOI 10.1111/j.1471-4159.2006.03977.x
   Savica Rodolfo, 2016, Alzheimers Dement (Amst), V3, P43
   SCHUTZE S, 1992, CELL, V71, P765, DOI 10.1016/0092-8674(92)90553-O
   Seidova SF, 2009, DOC OPHTHALMOL, V118, P151, DOI 10.1007/s10633-008-9142-9
   Shaaban SA, 1998, INVEST OPHTH VIS SCI, V39, P885
   Sun L, 2011, PLOS ONE, V6, DOI 10.1371/journal.pone.0019477
   Swinkels M, 2018, SCI REP-UK, V8, DOI 10.1038/s41598-017-18395-7
   Tan JSL, 2007, OPHTHALMOLOGY, V114, P1143, DOI 10.1016/j.ophtha.2006.09.033
   Totan Y, 2001, BRIT J OPHTHALMOL, V85, P1426, DOI 10.1136/bjo.85.12.1426
   Van Brocklyn JR, 2012, COMP BIOCHEM PHYS B, V163, P26, DOI 10.1016/j.cbpb.2012.05.006
   van Leeuwen R, 2004, AM J OPHTHALMOL, V137, P750, DOI 10.1016/S0002-9394(03)01089-4
   Weismann D, 2011, NATURE, V478, P76, DOI 10.1038/nature10449
   Wiesner P, 2009, J LIPID RES, V50, P574, DOI 10.1194/jlr.D800028-JLR200
   Wong WL, 2014, LANCET GLOB HEALTH, V2, pE106, DOI 10.1016/S2214-109X(13)70145-1
   Xing Y, 2016, J ALZHEIMERS DIS, V52, P1029, DOI 10.3233/JAD-151158
   Yamada S, 2001, J LIPID RES, V42, P1187
   Ye FX, 2016, FREE RADICAL BIO MED, V94, P121, DOI 10.1016/j.freeradbiomed.2016.02.027
NR 83
TC 21
Z9 21
U1 0
U2 3
PU PUBLIC LIBRARY SCIENCE
PI SAN FRANCISCO
PA 1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA
SN 1932-6203
J9 PLOS ONE
JI PLoS One
PD AUG 2
PY 2018
VL 13
IS 8
DI 10.1371/journal.pone.0200739
PG 20
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA GP3UD
UT WOS:000440778600017
PM 30071029
OA gold, Green Published, Green Submitted
DA 2025-04-10
ER

PT J
AU Perry, SV
AF Perry, SV
TI Vertebrate tropomyosin: distribution, properties and function
SO JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
LA English
DT Review
ID MUSCLE THIN FILAMENT; AMINO-ACID-SEQUENCE; IN-VITRO MOTILITY; FAMILIAL
   HYPERTROPHIC CARDIOMYOPATHY; ALTERNATIVELY SPLICED EXONS;
   ULCERATIVE-COLITIS UC; FLUORESCENCE ENERGY-TRANSFER; EQUINE PLATELET
   TROPOMYOSIN; RABBIT SKELETAL TROPOMYOSIN; CROSS-REACTIVE ALLERGEN
AB Tropomyosin (TM) is widely distributed in all cell types associated with actin as a fibrous molecule composed of two alpha -helical chains arranged as a coiled-coil. It is localised, polymerised end to end, along each of the two grooves of the F-actin filament providing structural stability and modulating the filament function. To accommodate the wide range of functions associated with actin filaments that occur in eucaryote cells TM exists in a large number isoforms, over 20 of which have been identified. These isoforms which are expressed by alternative promoters and alternative RNA processing of four genes, TPM1, 2, 3 and 4, all conform to a general pattern of structure. Their amino acid sequences consist of an integral number, six or seven in vertebrates, of quasiequivalent regions of about 40 residues that are considered to represent the actin-binding regions of the molecule. In addition to the variable regions a large part of the polypeptide chains of the TM isoforms, mainly centrally located and expressed by five exons, is invariant. Many of the isoforms are tissue and filament specific in their distribution implying that the exons expressed in them and the regions of the molecule they represent are of significance for the function of the filament system with which they are associated. In the case of muscle there is clear evidence that the TM moves its position on the F-actin filament during contraction and it is therefore considered to play an important part in the regulation of the process. It is uncertain how the role of TM in muscle compares to that in non-muscle systems and if its function in the former tissue is unique to muscle.
C1 Univ Birmingham, Sch Med, Dept Physiol, Div Med Sci, Birmingham B15 2TT, W Midlands, England.
C3 University of Birmingham
RP Univ Birmingham, Sch Med, Dept Physiol, Div Med Sci, Birmingham B15 2TT, W Midlands, England.
CR AKI T, 1995, J ALLERGY CLIN IMMUN, V96, P74, DOI 10.1016/S0091-6749(95)70035-8
   Akutsu S, 2000, ZOOL SCI, V17, P871, DOI 10.2108/zsj.17.871
   Almenar-Queralt A, 1999, J BIOL CHEM, V274, P28466, DOI 10.1074/jbc.274.40.28466
   AMPHLETT GW, 1976, FEBS LETT, V63, P22, DOI 10.1016/0014-5793(76)80186-X
   ASTBURY WT, 1948, BIOCHEM J, V43, P282, DOI 10.1042/bj0430282
   Asturias JA, 1999, J IMMUNOL, V162, P4342
   Ayuso R, 1999, ANN ALLERG ASTHMA IM, V83, P399, DOI 10.1016/S1081-1206(10)62837-2
   BABCOCK GG, 1994, J BIOL CHEM, V269, P27510
   Bacchiocchi C, 2000, BIOPHYS J, V78, p364A
   Bacchiocchi C, 1999, BIOPHYS J, V76, pA154
   BAILEY K, 1948, BIOCHEM J, V43, P271, DOI 10.1042/bj0430271
   BAILEY K, 1957, BIOCHIM BIOPHYS ACTA, V24, P612, DOI 10.1016/0006-3002(57)90255-X
   BAILEY K, 1951, BIOCHEM J, V49, P23, DOI 10.1042/bj0490023
   BAILEY K, 1948, BIOCHEM J, V43, P279, DOI 10.1042/bj0430279
   BAILEY K, 1946, NATURE, V157, P368, DOI 10.1038/157368b0
   BAILEY K, 1956, PUBBL STAZ ZOOL NAPO, V29, P96
   BALASUBRAMANIAN MK, 1992, NATURE, V360, P84, DOI 10.1038/360084a0
   BARANY M, 1980, ANNU REV PHYSIOL, V42, P275, DOI 10.1146/annurev.ph.42.030180.001423
   BASI GS, 1986, J BIOL CHEM, V261, P817
   Bear RS, 1944, J AM CHEM SOC, V66, P1297, DOI 10.1021/ja01236a027
   BIANCONE L, 1995, GASTROENTEROLOGY, V109, P3, DOI 10.1016/0016-5085(95)90263-5
   Biancone L, 1998, CLIN EXP IMMUNOL, V113, P198
   BILLETER R, 1981, FEBS LETT, V132, P133, DOI 10.1016/0014-5793(81)80446-2
   Bing W, 2000, BIOCHEM J, V350, P693, DOI 10.1042/0264-6021:3500693
   Bing W, 2000, J MOL CELL CARDIOL, V32, P1489, DOI 10.1006/jmcc.2000.1182
   Bing W, 1997, BIOCHEM BIOPH RES CO, V236, P760, DOI 10.1006/bbrc.1997.7045
   Bing W, 1999, BIOPHYS J, V76, pA36
   Bing W, 1998, J BIOL CHEM, V273, P15016, DOI 10.1074/jbc.273.24.15016
   BIVIN DB, 1991, BIOPHYS J, V59, P880, DOI 10.1016/S0006-3495(91)82300-1
   BODWELL CE, 1967, ARCH BIOCHEM BIOPHYS, V122, P246, DOI 10.1016/0003-9861(67)90145-2
   BOROVIKOV YS, 1993, BIOCHIM BIOPHYS ACTA, V1163, P280, DOI 10.1016/0167-4838(93)90163-L
   Bottinelli R, 1998, CIRC RES, V82, P106
   BRANDT PW, 1987, J MOL BIOL, V195, P885, DOI 10.1016/0022-2836(87)90492-X
   BREMEL RD, 1973, COLD SPRING HARB SYM, V37, P267, DOI 10.1101/SQB.1973.037.01.037
   BRETSCHER A, 1986, NATURE, V321, P726, DOI 10.1038/321726b0
   BRETSCHER A, 1985, J CELL BIOL, V100, P1656, DOI 10.1083/jcb.100.5.1656
   BRISSON JR, 1986, BIOCHEMISTRY-US, V25, P4548, DOI 10.1021/bi00364a014
   BRONSON DD, 1982, J BIOL CHEM, V257, P3937
   BROSCHAT KO, 1990, J BIOL CHEM, V265, P21323
   BROSCHAT KO, 1989, BIOCHEMISTRY-US, V28, P8501, DOI 10.1021/bi00447a035
   BROSCHAT KO, 1986, J BIOL CHEM, V261, P3350
   Buck SH, 1999, BIOPHYS J, V76, pA28
   Burton David J., 1998, Journal of Molecular and Cellular Cardiology, V30, pA38
   BUTTERS CA, 1993, J BIOL CHEM, V268, P15565
   CabralLilly D, 1997, BIOPHYS J, V73, P1763, DOI 10.1016/S0006-3495(97)78206-7
   CARSTEN ME, 1968, BIOCHEMISTRY-US, V7, P960, DOI 10.1021/bi00843a012
   CENSULLO R, 1994, J MOL BIOL, V243, P520, DOI 10.1006/jmbi.1994.1677
   CHACKO S, 1977, P NATL ACAD SCI USA, V74, P129, DOI 10.1073/pnas.74.1.129
   CHACKO S, 1990, J BIOL CHEM, V265, P2105
   Chandy IK, 1999, BIOCHEMISTRY-US, V38, P9286, DOI 10.1021/bi983073s
   Cho YJ, 2000, J BIOCHEM MOL BIOL, V33, P531
   CHO YJ, 1990, J BIOL CHEM, V265, P538
   CHO YJ, 1991, P NATL ACAD SCI USA, V88, P10153, DOI 10.1073/pnas.88.22.10153
   CHONG PCS, 1982, J BIOL CHEM, V257, P9152
   Chu KH, 2000, MAR BIOTECHNOL, V2, P499
   CLAYTON L, 1988, J MOL BIOL, V201, P507, DOI 10.1016/0022-2836(88)90633-X
   COHEN C, 1966, SCIENCE, V152, P794, DOI 10.1126/science.152.3723.794
   COHEN I, 1972, J MOL BIOL, V68, P383, DOI 10.1016/0022-2836(72)90220-3
   COLUCCIO LM, 1994, J CELL BIOL, V127, P1497, DOI 10.1083/jcb.127.6.1497
   CORSI A, 1958, BIOCHEM J, V68, P12, DOI 10.1042/bj0680012
   COTE G, 1978, FEBS LETT, V91, P237, DOI 10.1016/0014-5793(78)81181-8
   COTE GP, 1978, FEBS LETT, V94, P131, DOI 10.1016/0014-5793(78)80922-3
   COTE GP, 1981, J BIOL CHEM, V256, P1999
   COTE GP, 1981, J BIOL CHEM, V256, P7257
   COTE GP, 1981, MOL CELL BIOCHEM, V57, P127
   CRICK FHC, 1953, ACTA CRYSTALLOGR, V6, P689, DOI 10.1107/S0365110X53001964
   CUMMINS P, 1974, BIOCHEM J, V141, P43, DOI 10.1042/bj1410043
   CUMMINS P, 1973, BIOCHEM J, V133, P765, DOI 10.1042/bj1330765
   CUTICCHIA AJ, 1993, HUMAN GENE MAPPING C
   DABROWSKA R, 1983, J MUSCLE RES CELL M, V4, P143, DOI 10.1007/BF00712027
   DAS KM, 1993, J IMMUNOL, V150, P2487
   DAUL CB, 1994, INT ARCH ALLERGY IMM, V105, P49, DOI 10.1159/000236802
   DEBELLE I, 1987, BIOCHIM BIOPHYS ACTA, V925, P17, DOI 10.1016/0304-4165(87)90143-7
   DERTERROSSIAN E, 1981, J MOL BIOL, V153, P147, DOI 10.1016/0022-2836(81)90531-3
   DOHLMAN JG, 1993, BIOCHEM BIOPH RES CO, V195, P686, DOI 10.1006/bbrc.1993.2100
   DREES B, 1995, J CELL BIOL, V128, P383, DOI 10.1083/jcb.128.3.383
   EATON BL, 1976, SCIENCE, V192, P1337, DOI 10.1126/science.131972
   EATON BL, 1975, BIOCHEMISTRY-US, V14, P2718, DOI 10.1021/bi00683a025
   EBASHI S, 1963, NATURE, V200, P1010, DOI 10.1038/2001010a0
   EISENBER.E, 1970, J BIOL CHEM, V245, P2451
   EISENBERG E, 1974, J BIOL CHEM, V249, P4742
   ElMezgueldi M, 1996, J BIOL CHEM, V271, P28161, DOI 10.1074/jbc.271.45.28161
   ELSALEH SC, 1984, J BIOL CHEM, V259, P1014
   ERDELYI M, 1995, NATURE, V377, P524, DOI 10.1038/377524a0
   Evans CC, 2000, AM J PHYSIOL-HEART C, V279, pH2414, DOI 10.1152/ajpheart.2000.279.5.H2414
   FATIGATI V, 1984, J BIOL CHEM, V259, P4383
   FINE RE, 1975, J MOL BIOL, V95, P447, DOI 10.1016/0022-2836(75)90202-8
   FINE RE, 1973, NATURE-NEW BIOL, V245, P182, DOI 10.1038/newbio245182a0
   Fowler VM, 1996, CURR OPIN CELL BIOL, V8, P86, DOI 10.1016/S0955-0674(96)80052-4
   FOWLER VM, 1993, J CELL BIOL, V120, P411, DOI 10.1083/jcb.120.2.411
   FOWLER VM, 1990, J CELL BIOL, V111, P471, DOI 10.1083/jcb.111.2.471
   FOWLER VM, 1987, J BIOL CHEM, V262, P12792
   FOWLER VM, 1984, J BIOL CHEM, V259, P5978
   FUJIME S, 1971, J MOL BIOL, V62, P251, DOI 10.1016/0022-2836(71)90144-6
   Fujita A, 2000, CLIN CHIM ACTA, V299, P179, DOI 10.1016/S0009-8981(00)00296-5
   Fujita H, 1999, BIOPHYS J, V77, P1540, DOI 10.1016/S0006-3495(99)77001-3
   GEEVES MA, 1994, BIOPHYS J, V67, P273, DOI 10.1016/S0006-3495(94)80478-3
   Geeves MA, 2000, BIOCHEMISTRY-US, V39, P9345, DOI 10.1021/bi0002232
   Geng X, 2000, GASTROENTEROLOGY, V118, pA260, DOI 10.1016/S0016-5085(00)83114-5
   Geng X, 1998, GASTROENTEROLOGY, V114, P912, DOI 10.1016/S0016-5085(98)70310-5
   Gerson JH, 1999, J BIOL CHEM, V274, P17545, DOI 10.1074/jbc.274.25.17545
   GIMONA M, 1995, P NATL ACAD SCI USA, V92, P9776, DOI 10.1073/pnas.92.21.9776
   Gimona M., 1996, Biochemistry of Smooth Muscle Contraction, P91
   Goldmann WH, 2000, BIOCHEM BIOPH RES CO, V276, P1225, DOI 10.1006/bbrc.2000.3608
   Golitsina N, 1997, BIOCHEMISTRY-US, V36, P4637, DOI 10.1021/bi962970y
   Golitsina NL, 2000, BIOPHYS J, V78, p364A
   GOODWIN LO, 1991, J BIOL CHEM, V266, P8408
   Grabarek Z, 2000, BIOPHYS J, V78, p364A
   Graceffa P, 1999, BIOCHEMISTRY-US, V38, P11984, DOI 10.1021/bi9825495
   Graceffa P, 2000, J BIOL CHEM, V275, P17143, DOI 10.1074/jbc.M001979200
   GREENE LE, 1980, P NATL ACAD SCI-BIOL, V77, P2616, DOI 10.1073/pnas.77.5.2616
   Greenfield NJ, 1998, BIOCHEMISTRY-US, V37, P7834, DOI 10.1021/bi973167m
   GREGORIO CC, 1995, NATURE, V377, P83, DOI 10.1038/377083a0
   Gunning P, 1998, BIOESSAYS, V20, P892, DOI 10.1002/(SICI)1521-1878(199811)20:11<892::AID-BIES4>3.0.CO;2-D
   GUNNING P, 1990, DEV BIOL, V138, P443, DOI 10.1016/0012-1606(90)90210-A
   HAD L, 1994, J CELL SCI, V107, P2961
   HALL CE, 1945, J APPL PHYS, V16, P459, DOI 10.1063/1.1707615
   Hammell RL, 1996, J BIOL CHEM, V271, P4236
   Hammell RL, 1997, J BIOL CHEM, V272, P22409, DOI 10.1074/jbc.272.36.22409
   HANSON J, 1964, PROC R SOC SER B-BIO, V160, P449, DOI 10.1098/rspb.1964.0055
   HANSON J, 1963, J MOL BIOL, V6, P46, DOI 10.1016/S0022-2836(63)80081-9
   HASELGROVE JC, 1973, COLD SPRING HARB SYM, V37, P341, DOI 10.1101/SQB.1973.037.01.044
   HEALD RW, 1988, J BIOL CHEM, V263, P5254
   HEELEY DA, 1982, FEBS LETT, V146, P115, DOI 10.1016/0014-5793(82)80716-3
   HEELEY DH, 1987, J BIOL CHEM, V262, P9971
   HEELEY DH, 1989, J BIOL CHEM, V264, P2424
   HEELEY DH, 1985, BIOCHEM J, V226, P461, DOI 10.1042/bj2260461
   HEELEY DH, 1983, FEBS LETT, V152, P282, DOI 10.1016/0014-5793(83)80396-2
   HEGMANN TE, 1989, J CELL BIOL, V109, P1141, DOI 10.1083/jcb.109.3.1141
   HELFMAN DM, 1984, J BIOL CHEM, V259, P4136
   HELFMAN DM, 1994, SOC GEN PHY, V49, P105
   HELFMAN DM, 1986, MOL CELL BIOL, V6, P3582, DOI 10.1128/MCB.6.11.3582
   HENDRICKS M, 1981, P NATL ACAD SCI-BIOL, V78, P5633, DOI 10.1073/pnas.78.9.5633
   HILL LE, 1992, J BIOL CHEM, V267, P16106
   Hirano K, 2000, EUR J PHARMACOL, V406, P209, DOI 10.1016/S0014-2999(00)00681-6
   HitchcockDeGregori SE, 1996, J BIOL CHEM, V271, P3600
   HITCHCOCKDEGREGORI SE, 1988, ARCH BIOCHEM BIOPHYS, V264, P410, DOI 10.1016/0003-9861(88)90306-2
   HITCHCOCKDEGREGORI SE, 1990, J MOL BIOL, V214, P885, DOI 10.1016/0022-2836(90)90343-K
   HITCHCOCKDEGREGORI SE, 1994, ADV EXP MED BIOL, V358, P85
   HITCHCOCKDEGREGORI SE, 1987, J BIOL CHEM, V262, P9730
   HITCHCOCKDEGREGORI SE, 1988, BIOCHEMISTRY-US, V27, P9182, DOI 10.1021/bi00426a016
   Hnath EJ, 1996, BIOPHYS J, V71, P1920, DOI 10.1016/S0006-3495(96)79391-8
   HODGES RS, 1970, BIOCHEM BIOPH RES CO, V41, P987, DOI 10.1016/0006-291X(70)90182-8
   Hodgkinson JL, 2000, J MUSCLE RES CELL M, V21, P115, DOI 10.1023/A:1005697301043
   Hoit BD, 1999, CIRCULATION, V100, P761
   HOLMES KC, 1985, BIOPHYS J S, V68, P2
   HORIUCHI KY, 1988, BIOCHEMISTRY-US, V27, P8388, DOI 10.1021/bi00422a014
   HUXLEY HE, 1971, BIOCHEM J, V125, pP85, DOI 10.1042/bj1250085P
   HUXLEY HE, 1973, COLD SPRING HARB SYM, V37, P361, DOI 10.1101/SQB.1973.037.01.046
   HUXLEY HE, 1970, 8 INT C BIOCH INT
   HUXLEY HE, 1960, CELL BIOCH PHYSL MOR, V1, P365
   ITOH T, 1989, NATURE, V338, P164, DOI 10.1038/338164a0
   JACKSON P, 1975, BIOCHEM J, V151, P85, DOI 10.1042/bj1510085
   JANCSO A, 1991, J BIOL CHEM, V266, P5891
   Jenkins RE, 1998, P NATL ACAD SCI USA, V95, P7550, DOI 10.1073/pnas.95.13.7550
   JOHNSON P, 1977, BIOCHEMISTRY-US, V16, P2264, DOI 10.1021/bi00629a035
   JOHNSON P, 1975, BIOCHEM BIOPH RES CO, V64, P1316, DOI 10.1016/0006-291X(75)90836-0
   JOHNSON P, 1978, BIOCHEM BIOPH RES CO, V82, P1013, DOI 10.1016/0006-291X(78)90884-7
   KABSCH W, 1992, ANNU REV BIOPH BIOM, V21, P49, DOI 10.1146/annurev.bb.21.060192.000405
   KAMINER B, 1972, J CELL BIOL, V55, pA129
   KANG BC, 1990, CLIN REV ALLERG, V8, P87
   KATZ AM, 1964, J BIOL CHEM, V239, P3304
   KAWAMURA M, 1970, J BIOCHEM-TOKYO, V67, P437, DOI 10.1093/oxfordjournals.jbchem.a129267
   KEISER T, 1985, FEBS LETT, V187, P76, DOI 10.1016/0014-5793(85)81218-7
   Kesari KV, 1999, CLIN EXP IMMUNOL, V118, P219
   Khanna AK, 1997, J AUTOIMMUN, V10, P99, DOI 10.1006/jaut.1996.0107
   Kimura S, 1999, EUR J BIOCHEM, V263, P396, DOI 10.1046/j.1432-1327.1999.00505.x
   Kobayashi T, 2000, BIOCHEMISTRY-US, V39, P86, DOI 10.1021/bi991903b
   KOJIMA H, 1994, P NATL ACAD SCI USA, V91, P12962, DOI 10.1073/pnas.91.26.12962
   KOMINZ DR, 1966, ARCH BIOCHEM BIOPHYS, V115, P583, DOI 10.1016/0003-9861(66)90078-6
   KOMINZ DR, 1957, NATURE, V179, P206, DOI 10.1038/179206b0
   Korman V, 1998, BIOPHYS J, V74, pA347
   Korman VL, 2000, BIOPHYS J, V78, p436A
   Korman VL, 2000, J BIOL CHEM, V275, P22470, DOI 10.1074/jbc.M002939200
   Kostyukova A, 2000, EUR J BIOCHEM, V267, P6470, DOI 10.1046/j.1432-1327.2000.01738.x
   KRESS M, 1986, J MOL BIOL, V188, P325, DOI 10.1016/0022-2836(86)90158-0
   KUOKANG W, 2000, J BIOL CHEM, V275, P40594
   LAING NG, 1995, NAT GENET, V9, P75, DOI 10.1038/ng0195-75
   LAKI K, 1962, ARCH BIOCHEM BIOPHYS, V98, P323, DOI 10.1016/0003-9861(62)90190-X
   LAKI K, 1959, FED PROC, V18, P85
   LAL AA, 1986, BIOCHEMISTRY-US, V25, P1154, DOI 10.1021/bi00353a031
   Landis C, 1999, BIOPHYS J, V76, pA154
   Landis CA, 1997, J BIOL CHEM, V272, P14051, DOI 10.1074/jbc.272.22.14051
   LANDSCHULZ WH, 1988, SCIENCE, V240, P1759, DOI 10.1126/science.3289117
   LAU SYM, 1985, J BIOL CHEM, V260, P7257
   LAZARIDES E, 1975, J CELL BIOL, V65, P549, DOI 10.1083/jcb.65.3.549
   LAZARIDES E, 1976, J SUPRAMOL STR CELL, V5, P531, DOI 10.1002/jss.400050410
   LEESMILLER JP, 1991, BIOESSAYS, V13, P429, DOI 10.1002/bies.950130902
   LEESMILLER JP, 1990, J MOL BIOL, V213, P399, DOI 10.1016/S0022-2836(05)80202-5
   LEESMILLER JP, 1990, MOL CELL BIOL, V10, P1729, DOI 10.1128/MCB.10.4.1729
   LEGER J, 1976, PFLUG ARCH EUR J PHY, V362, P271, DOI 10.1007/BF00581181
   Lehman W, 2000, BIOPHYS J, V78, p399A
   LEHMAN W, 1993, BIOCHIM BIOPHYS ACTA, V1203, P53, DOI 10.1016/0167-4838(93)90035-P
   LEHMAN W, 1994, NATURE, V368, P65, DOI 10.1038/368065a0
   LEHMAN W, 1995, J MOL BIOL, V251, P191, DOI 10.1006/jmbi.1995.0425
   Lehman W, 2001, BIOPHYS J, V80, p356A
   Lehman W, 2000, J MOL BIOL, V302, P593, DOI 10.1006/jmbi.2000.4080
   Lehman W., 1996, BIOCH SMOOTH MUSCLE, P47
   LEHRER SS, 1991, BIOCHEMISTRY-US, V30, P5682, DOI 10.1021/bi00237a007
   LEHRER SS, 1989, SCIENCE, V246, P926, DOI 10.1126/science.2814515
   Lehrer SS, 1997, BIOCHEMISTRY-US, V36, P13449, DOI 10.1021/bi971568w
   Lehrer SS, 1997, BIOPHYS J, V72, pMP198
   LEHRER SS, 1994, J MUSCLE RES CELL M, V15, P232
   LEHRER SS, 1982, J BIOL CHEM, V257, P8073
   Lehrer SS, 1998, J MOL BIOL, V277, P1081, DOI 10.1006/jmbi.1998.1654
   LEHRER SS, 1975, P NATL ACAD SCI USA, V72, P3377, DOI 10.1073/pnas.72.9.3377
   LEONARDI CL, 1982, BIOCHIM BIOPHYS ACTA, V720, P154, DOI 10.1016/0167-4889(82)90007-6
   Leung PSC, 1996, J ALLERGY CLIN IMMUN, V98, P954, DOI 10.1016/S0091-6749(96)80012-1
   LEUNG PSC, 1994, J ALLERGY CLIN IMMUN, V94, P882, DOI 10.1016/0091-6749(94)90156-2
   LEVINE BA, 1999, J MUSCLE RES CELL M, V20, P828
   Levitsky DI, 2000, EUR J BIOCHEM, V267, P1869, DOI 10.1046/j.1432-1327.2000.01192.x
   LEWIS WG, 1983, FEBS LETT, V156, P269, DOI 10.1016/0014-5793(83)80511-0
   LEWIS WG, 1980, J BIOL CHEM, V255, P6854
   Lin J J, 1997, Int Rev Cytol, V170, P1, DOI 10.1016/S0074-7696(08)61619-8
   LIN JJC, 1985, J CELL BIOL, V100, P692, DOI 10.1083/jcb.100.3.692
   LIN JJC, 1988, J CELL BIOL, V107, P563, DOI 10.1083/jcb.107.2.563
   LIU H, 1989, CELL, V57, P233, DOI 10.1016/0092-8674(89)90961-6
   LIU HP, 1992, J CELL BIOL, V118, P285, DOI 10.1083/jcb.118.2.285
   LORENZ M, 1995, J MOL BIOL, V246, P108, DOI 10.1006/jmbi.1994.0070
   LOWY J, 1970, NATURE, V227, P46, DOI 10.1038/227046a0
   LOWY J, 1973, COLD SPRING HARB SYM, V37, P353, DOI 10.1101/SQB.1973.037.01.045
   MACLEOD AR, 1985, P NATL ACAD SCI USA, V82, P7835, DOI 10.1073/pnas.82.23.7835
   MACLEOD AR, 1988, MOL CELL BIOL, V8, P433, DOI 10.1128/MCB.8.1.433
   MACLEOD AR, 1987, J MOL BIOL, V194, P1, DOI 10.1016/0022-2836(87)90710-8
   MAK A, 1978, P NATL ACAD SCI USA, V75, P3588, DOI 10.1073/pnas.75.8.3588
   MAK AS, 1981, BIOCHEM BIOPH RES CO, V101, P208, DOI 10.1016/S0006-291X(81)80032-0
   Marston S, 1998, ACTA PHYSIOL SCAND, V164, P401, DOI 10.1111/j.1365-201X.1998.tb10696.x
   MARSTON S, 1990, BIOCHEM J, V272, P305, DOI 10.1042/bj2720305
   Marston S.B., 1996, BIOCH SMOOTH MUSCLE, P77
   MARSTON SB, 1991, BIOCHEM J, V279, P1
   MARSTON SB, 1993, J BIOL CHEM, V268, P12317
   MARTONOSI A, 1962, J BIOL CHEM, V237, P2795
   MARUYAMA K, 1964, ARCH BIOCHEM BIOPHYS, V105, P142, DOI 10.1016/0003-9861(64)90245-0
   MATSUMURA F, 1983, J BIOL CHEM, V258, P3954
   MATSUMURA F, 1985, J BIOL CHEM, V260, P3851
   MATSUMURA F, 1983, J BIOL CHEM, V258, P6636
   Matsumura F, 1993, CURR OPIN CELL BIOL, V5, P70, DOI 10.1016/S0955-0674(05)80010-9
   Matsuura Y, 2000, J MOL BIOL, V296, P579, DOI 10.1006/jmbi.1999.3467
   MAUPINSZAMIER P, 1978, J CELL BIOL, V77, P837, DOI 10.1083/jcb.77.3.837
   Maytum R, 2000, BIOCHEMISTRY-US, V39, P11913, DOI 10.1021/bi000977g
   McElhinny AS, 2001, J BIOL CHEM, V276, P583, DOI 10.1074/jbc.M005693200
   MCGHEE JD, 1974, J MOL BIOL, V86, P469, DOI 10.1016/0022-2836(74)90031-X
   MCKILLOP DFA, 1993, BIOPHYS J, V65, P693, DOI 10.1016/S0006-3495(93)81110-X
   MCLACHLAN AD, 1975, J MOL BIOL, V98, P293, DOI 10.1016/S0022-2836(75)80119-7
   MCLACHLAN AD, 1976, J MOL BIOL, V103, P271, DOI 10.1016/0022-2836(76)90313-2
   Michele DE, 1999, J CLIN INVEST, V104, P1575, DOI 10.1172/JCI7842
   Michele DE, 2000, BIOPHYS J, V78, p399A
   MIKI M, 1989, J BIOCHEM, V106, P651, DOI 10.1093/oxfordjournals.jbchem.a122911
   MIKI M, 1991, BIOCHEMISTRY-US, V30, P5625, DOI 10.1021/bi00236a042
   MILLIGAN RA, 1987, J CELL BIOL, V105, P29, DOI 10.1083/jcb.105.1.29
   MILLIGAN RA, 1990, NATURE, V348, P217, DOI 10.1038/348217a0
   Miyazawa H, 1996, J ALLERGY CLIN IMMUN, V98, P948, DOI 10.1016/S0091-6749(96)80011-X
   Mogensen J, 1999, J CLIN INVEST, V103, pR39, DOI 10.1172/JCI6460
   MONTARRAS D, 1981, J BIOL CHEM, V256, P4081
   MONTEIRO PB, 1994, J BIOL CHEM, V269, P10461
   MONTGOMERY K, 1984, J BIOL CHEM, V259, P5555
   MOODY C, 1990, J MUSCLE RES CELL M, V11, P176, DOI 10.1007/BF01766496
   MOORE GE, 1985, J MUSCLE RES CELL M, V6, P513, DOI 10.1007/BF00712587
   MOORE PB, 1970, J MOL BIOL, V50, P279, DOI 10.1016/0022-2836(70)90192-0
   Moraczewska J, 2000, BIOCHEMISTRY-US, V39, P6891, DOI 10.1021/bi000242b
   Moraczewska J, 1999, BIOCHEMISTRY-US, V38, P15885, DOI 10.1021/bi991816j
   Moraczewska J, 2000, BIOPHYS J, V79, P3217, DOI 10.1016/S0006-3495(00)76554-4
   MORRIS EP, 1984, BIOCHEMISTRY-US, V23, P2214, DOI 10.1021/bi00305a018
   Muthuchamy M, 1997, TRENDS CARDIOVAS MED, V7, P124, DOI 10.1016/S1050-1738(97)00004-2
   NAGASHIMA H, 1982, J MOL BIOL, V155, P409, DOI 10.1016/0022-2836(82)90479-X
   NAKAJIMATANIGUCHI C, 1995, J MOL CELL CARDIOL, V27, P2053, DOI 10.1016/0022-2828(95)90026-8
   NAKAMURA F, 1993, J BIOL CHEM, V268, P6194
   Niitsu Y, 2000, GASTROENTEROLOGY, V118, pA355, DOI 10.1016/S0016-5085(00)83522-2
   NOVY RE, 1993, BIOCHIM BIOPHYS ACTA, V1162, P255, DOI 10.1016/0167-4838(93)90289-4
   NOVY RE, 1993, CELL MOTIL CYTOSKEL, V26, P248, DOI 10.1002/cm.970260308
   OBRIEN EJ, 1971, PHILOS T ROY SOC B, V261, P201, DOI 10.1098/rstb.1971.0051
   Ogut O, 2000, J BIOL CHEM, V275, P26089, DOI 10.1074/jbc.M910360199
   Ogut O, 2000, BIOPHYS J, V78, p364A
   OLSON TM, 2001, IN PRESS J MOL CELLU
   Onuma EK, 2000, CLIN EXP IMMUNOL, V121, P466, DOI 10.1046/j.1365-2249.2000.01330.x
   Orlov VN, 1998, FEBS LETT, V433, P241, DOI 10.1016/S0014-5793(98)00923-5
   OTEY CA, 1988, CELL MOTIL CYTOSKEL, V9, P337, DOI 10.1002/cm.970090406
   OTSUKI I, 1971, J BIOCH, V86, P491
   Panzani R C, 1994, Allergol Immunopathol (Madr), V22, P167
   PARRY DAD, 1974, BIOCHEM BIOPH RES CO, V57, P216, DOI 10.1016/S0006-291X(74)80379-7
   PARRY DAD, 1973, J MOL BIOL, V75, P33, DOI 10.1016/0022-2836(73)90527-5
   PAYNE MR, 1984, TIBS, P361
   PEARLSTONE JR, 1983, J BIOL CHEM, V258, P2534
   Percival JM, 2000, CELL MOTIL CYTOSKEL, V47, P189, DOI 10.1002/1097-0169(200011)47:3<189::AID-CM3>3.0.CO;2-C
   Perry SV, 1999, MOL CELL BIOCHEM, V190, P9, DOI 10.1023/A:1006939307715
   PERRY SV, 1958, BIOCHEM J, V68, P5, DOI 10.1042/bj0680005
   PERRY SV, 1973, COLD SPRING HARB SYM, V37, P251, DOI 10.1101/SQB.1973.037.01.035
   Perry SV, 1998, J MUSCLE RES CELL M, V19, P575
   Perry SV., 1996, Molecular Mechanisms in Striated Muscle
   PERRY SV, 1997, COMPR BIOCHEM, V40, P383
   PERRY SV, 1975, P 9 M FED EUR BIOCH, V31, P163
   PHILLIPS GN, 1979, NATURE, V278, P413, DOI 10.1038/278413a0
   PHILLIPS GN, 1987, J MOL BIOL, V195, P219, DOI 10.1016/0022-2836(87)90339-1
   PHILLIPS GN, 1986, J MOL BIOL, V192, P111, DOI 10.1016/0022-2836(86)90468-7
   Pieples K, 2000, BIOCHEMISTRY-US, V39, P8291, DOI 10.1021/bi000047x
   Pieples K, 1999, BIOPHYS J, V76, pA41
   PITTENGER MF, 1995, J CELL SCI, V108, P3253
   PITTENGER MF, 1992, J CELL BIOL, V118, P841, DOI 10.1083/jcb.118.4.841
   PITTENGER MF, 1994, CURR OPIN CELL BIOL, V6, P96, DOI 10.1016/0955-0674(94)90122-8
   POOLE KJV, 1995, BIOPHYS J, V68, pS348
   POTTER JD, 1974, BIOCHEMISTRY-US, V13, P2697, DOI 10.1021/bi00710a007
   PRAGAY DA, 1968, ARCH BIOCHEM BIOPHYS, V125, P727, DOI 10.1016/0003-9861(68)90507-9
   PRATJE E, 1972, FEBS LETT, V27, P89, DOI 10.1016/0014-5793(72)80416-2
   RAYMENT I, 1993, SCIENCE, V261, P58, DOI 10.1126/science.8316858
   REDWOOD CS, 1990, FEBS LETT, V270, P53, DOI 10.1016/0014-5793(90)81233-E
   REDWOOD CS, 1993, J BIOL CHEM, V268, P10969
   Redwood CS, 1999, CARDIOVASC RES, V44, P20, DOI 10.1016/S0008-6363(99)00213-8
   Reese G, 1997, INT ARCH ALLERGY IMM, V113, P240, DOI 10.1159/000237558
   Reese G, 1999, INT ARCH ALLERGY IMM, V119, P247, DOI 10.1159/000024201
   Regitz-Zagrosek V, 2000, CIRCULATION, V102, pE112
   RIBOLOW H, 1977, ARCH BIOCHEM BIOPHYS, V179, P718, DOI 10.1016/0003-9861(77)90162-X
   Robinson JM, 2000, BIOPHYS J, V78, p365A
   Rosol M, 2000, BIOPHYS J, V78, P908, DOI 10.1016/S0006-3495(00)76648-3
   RUIZOPAZO N, 1987, J BIOL CHEM, V262, P4755
   Saeki K, 2000, BIOCHEM BIOPH RES CO, V275, P428, DOI 10.1006/bbrc.2000.3321
   Saeki K, 1996, BIOCHEMISTRY-US, V35, P14465, DOI 10.1021/bi961292c
   Sakamaki S, 1996, GASTROENTEROLOGY, V110, pA1007
   Sakamaki S, 2000, GUT, V47, P236, DOI 10.1136/gut.47.2.236
   SALVIATI G, 1982, BIOCHEM J, V207, P261, DOI 10.1042/bj2070261
   SANDERS C, 1985, J BIOL CHEM, V260, P7264
   SANGER JW, 1983, J CELL BIOL, V96, P961, DOI 10.1083/jcb.96.4.961
   Sano K, 2000, EUR J BIOCHEM, V267, P4870, DOI 10.1046/j.1432-1327.2000.01549.x
   Sano K, 2000, J BIOCHEM-TOKYO, V127, P1095
   SCHACHAT FH, 1987, J MOL BIOL, V198, P551, DOI 10.1016/0022-2836(87)90300-7
   Schaertl S, 1995, BIOCHEMISTRY-US, V34, P15890, DOI 10.1021/bi00049a003
   SCHAUB MC, 1971, BIOCHEM J, V123, P367, DOI 10.1042/bj1230367
   SCHAUB MC, 1967, BIOCHEM J, V105, P1235, DOI 10.1042/bj1051235
   SHANTI KN, 1993, J IMMUNOL, V151, P5354
   SHEN BW, 1986, J CELL BIOL, V102, P997, DOI 10.1083/jcb.102.3.997
   SHIGEKAWA M, 1973, J BIOCHEM, V73, P1135, DOI 10.1093/oxfordjournals.jbchem.a130185
   Shishido T, 2000, J BIOCHEM-TOKYO, V127, P253, DOI 10.1093/oxfordjournals.jbchem.a022602
   Smillie L.B., 1996, BIOCH SMOOTH MUSCLE, P63
   SMILLIE LB, 1979, TRENDS BIOCHEM SCI, V4, P151, DOI 10.1016/0968-0004(79)90003-3
   SMITH CWJ, 1987, J BIOL CHEM, V262, P116
   SOBUE K, 1982, BIOMED RES-TOKYO, V3, P188, DOI 10.2220/biomedres.3.188
   SOBUE K, 1981, P NATL ACAD SCI-BIOL, V78, P5652, DOI 10.1073/pnas.78.9.5652
   SODEK J, 1972, P NATL ACAD SCI USA, V69, P3800, DOI 10.1073/pnas.69.12.3800
   Spindler MK, 1999, CIRCULATION, V100, P268
   SPUDICH JA, 1972, J MOL BIOL, V72, P619, DOI 10.1016/0022-2836(72)90180-5
   Squire JM, 1998, FASEB J, V12, P761, DOI 10.1096/fasebj.12.10.761
   STAMM S, 1993, P NATL ACAD SCI USA, V90, P9857, DOI 10.1073/pnas.90.21.9857
   STEINBACH JH, 1980, EXP NEUROL, V67, P655, DOI 10.1016/0014-4886(80)90134-X
   STEWART M, 1975, NATURE, V257, P331, DOI 10.1038/257331a0
   STEWART M, 1975, FEBS LETT, V53, P5, DOI 10.1016/0014-5793(75)80668-5
   STONE D, 1974, P 9 FEBS M, V31, P125
   Strand J, 2000, BIOPHYS J, V78, p364A
   Straub F., 1942, Stud. Inst. Med. Chem. Univ. Szeged, VII, P3
   STULL JT, 1977, J BIOL CHEM, V252, P851
   SUNG LA, 1994, BIOCHEM BIOPH RES CO, V201, P627, DOI 10.1006/bbrc.1994.1747
   SUNG LA, 2000, RED CELLS, V95, P1473
   Sussman MA, 1998, CIRC RES, V82, P94
   Sussman MA, 1999, AM J PATHOL, V155, P2101, DOI 10.1016/S0002-9440(10)65528-9
   Sussman MA, 1996, CELL TISSUE RES, V285, P287, DOI 10.1007/s004410050646
   SYSKA H, 1976, BIOCHEM J, V153, P375, DOI 10.1042/bj1530375
   SZILAGYI L, 1982, BIOCHIM BIOPHYS ACTA, V709, P204, DOI 10.1016/0167-4838(82)90462-9
   TAKAHASHI K, 1986, BIOCHEM BIOPH RES CO, V141, P20, DOI 10.1016/S0006-291X(86)80328-X
   TAKEBAYASHI T, 1977, BIOCHIM BIOPHYS ACTA, V492, P357, DOI 10.1016/0005-2795(77)90086-1
   TAKENAGA K, 1994, J CELL BIOL, V124, P757, DOI 10.1083/jcb.124.5.757
   TAKENAGA K, 1990, BIOCHIM BIOPHYS ACTA, V1087, P101, DOI 10.1016/0167-4781(90)90129-P
   TALBOT JA, 1981, J BIOL CHEM, V256, P2798
   TALBOT K, 1983, J MOL BIOL, V164, P159, DOI 10.1016/0022-2836(83)90091-8
   TANAKA H, 1972, BIOCHIM BIOPHYS ACTA, V278, P556, DOI 10.1016/0005-2795(72)90015-3
   TANAKA H, 1971, BIOCHIM BIOPHYS ACTA, V253, P274, DOI 10.1016/0005-2728(71)90253-2
   TAWADA Y, 1975, J BIOCHEM, V78, P65
   TAYLOR KA, 1981, J MOL BIOL, V147, P297, DOI 10.1016/0022-2836(81)90442-3
   Temm-Grove CJ, 1998, CELL MOTIL CYTOSKEL, V40, P393, DOI 10.1002/(SICI)1097-0169(1998)40:4<393::AID-CM7>3.0.CO;2-C
   TemmGrove CJ, 1996, CELL MOTIL CYTOSKEL, V33, P223, DOI 10.1002/(SICI)1097-0169(1996)33:3<223::AID-CM6>3.0.CO;2-B
   Tetzlaff MT, 1996, EMBO J, V15, P1247, DOI 10.1002/j.1460-2075.1996.tb00466.x
   THIERFELDER L, 1994, CELL, V77, P701, DOI 10.1016/0092-8674(94)90054-X
   Tobacman LS, 1999, CIRCULATION, V100, P276
   Towbin JA, 1998, CURR OPIN CELL BIOL, V10, P131, DOI 10.1016/S0955-0674(98)80096-3
   TROMBITAS K, 1990, J MUSCLE RES CELL M, V11, P445, DOI 10.1007/BF01739764
   TSAO TC, 1951, BIOCHEM J, V49, P27, DOI 10.1042/bj0490027
   URBANCIKOVA M, 1994, J BIOL CHEM, V269, P24310
   VanBuren P, 1999, P NATL ACAD SCI USA, V96, P12488, DOI 10.1073/pnas.96.22.12488
   Vera C, 2000, ARCH BIOCHEM BIOPHYS, V378, P16, DOI 10.1006/abbi.2000.1802
   Vera C, 2000, FASEB J, V14, pA100
   VIBERT P, 1993, J CELL BIOL, V123, P313, DOI 10.1083/jcb.123.2.313
   Vibert P, 1997, J MOL BIOL, V266, P8, DOI 10.1006/jmbi.1996.0800
   VIBERT PJ, 1972, J MOL BIOL, V71, P757, DOI 10.1016/0022-2828(72)90044-2
   WALSH TP, 1985, J MOL BIOL, V182, P265, DOI 10.1016/0022-2836(85)90344-4
   WATSON MH, 1990, J BIOL CHEM, V265, P18860
   WEBER A, 1994, J CELL BIOL, V127, P1627, DOI 10.1083/jcb.127.6.1627
   WEBER K, 1969, J BIOL CHEM, V244, P4406
   WEGNER A, 1982, J MOL BIOL, V161, P217, DOI 10.1016/0022-2836(82)90149-8
   WEGNER A, 1988, BIOCHEMISTRY-US, V27, P6994, DOI 10.1021/bi00418a049
   WEGNER A, 1981, BIOCHEMISTRY-US, V20, P5633, DOI 10.1021/bi00522a043
   WEHLAND J, 1980, EXP CELL RES, V127, P397, DOI 10.1016/0014-4827(80)90444-9
   WEIGT C, 1990, FEBS LETT, V260, P266, DOI 10.1016/0014-5793(90)80119-4
   WEINBERGER RP, 1993, J CELL BIOL, V120, P205, DOI 10.1083/jcb.120.1.205
   Wernicke D, 1999, CIRCULATION, V100, P268
   WHITBY FG, 1992, J MOL BIOL, V227, P441, DOI 10.1016/0022-2836(92)90899-U
   Whitby FG, 2000, PROTEINS, V38, P49
   WHITE SP, 1987, NATURE, V325, P826, DOI 10.1038/325826a0
   WILLADSEN KA, 1992, J BIOL CHEM, V267, P23746
   WILLIAMS DL, 1983, BIOCHEMISTRY-US, V22, P2770, DOI 10.1021/bi00280a027
   WILLIAMS DL, 1984, BIOCHEMISTRY-US, V23, P4150, DOI 10.1021/bi00313a022
   WITTEMAN AM, 1994, INT ARCH ALLERGY IMM, V105, P56, DOI 10.1159/000236803
   Wong WW, 1998, BIOPHYS J, V74, pA264
   WOODS EF, 1967, J BIOL CHEM, V242, P2859
   WOODS EF, 1966, J MOL BIOL, V16, P581, DOI 10.1016/S0022-2836(66)80199-7
   Xu C, 1999, BIOPHYS J, V77, P985, DOI 10.1016/S0006-3495(99)76949-3
   YAGI N, 1989, J MOL BIOL, V208, P359, DOI 10.1016/0022-2836(89)90396-3
   YAMASHIROMATSUMURA S, 1988, J CELL BIOL, V106, P1973, DOI 10.1083/jcb.106.6.1973
   YANG YZ, 1979, J BIOL CHEM, V254, P7137
   YANG YZ, 1977, J BIOL CHEM, V252, P3374
NR 406
TC 387
Z9 447
U1 0
U2 38
PU SPRINGER
PI DORDRECHT
PA VAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDS
SN 0142-4319
EI 1573-2657
J9 J MUSCLE RES CELL M
JI J. Muscle Res. Cell Motil.
PD JAN
PY 2001
VL 22
IS 1
BP 5
EP 49
DI 10.1023/A:1010303732441
PG 45
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA 446LD
UT WOS:000169514000002
PM 11563548
DA 2025-04-10
ER

PT J
AU Cardoso, TF
   Quintanilla, R
   Castelló, A
   González-Prendes, R
   Amills, M
   Cánovas, A
AF Figueiredo Cardoso, Taina
   Quintanilla, Raquel
   Castello, Anna
   Gonzalez-Prendes, Rayner
   Amills, Marcel
   Canovas, Angela
TI Differential expression of mRNA isoforms in the skeletal muscle of pigs
   with distinct growth and fatness profiles
SO BMC GENOMICS
LA English
DT Article
DE Alternative splicing; mRNA isoform; Swine; Differential expression
ID GENE-EXPRESSION; FATTY-ACID; IDENTIFICATION; TRANSCRIPT; QUANTIFICATION;
   CHOLESTEROL; ANNOTATION; GENOME
AB Background: The identification of genes differentially expressed in the skeletal muscle of pigs displaying distinct growth and fatness profiles might contribute to identify the genetic factors that influence the phenotypic variation of such traits. So far, the majority of porcine transcriptomic studies have investigated differences in gene expression at a global scale rather than at the mRNA isoform level. In the current work, we have investigated the differential expression of mRNA isoforms in the gluteus medius (GM) muscle of 52 Duroc HIGH (increased backfat thickness, intramuscular fat and saturated and monounsaturated fatty acids contents) and LOW pigs (opposite phenotype, with an increased polyunsaturated fatty acids content).
   Results: Our analysis revealed that 10.9% of genes expressed in the GM muscle generate alternative mRNA isoforms, with an average of 2.9 transcripts per gene. By using two different pipelines, one based on the CLC Genomics Workbench and another one on the STAR, RSEM and DESeq2 softwares, we have identified 10 mRNA isoforms that both pipelines categorize as differentially expressed in HIGH vs LOW pigs (P-value < 0.01 and +/- 0.6 log(2)fold-change). Only five mRNA isoforms, produced by the ITGA5, SEMA4D, LITAF, TIMP1 and ANXA2 genes, remain significant after correction for multiple testing (q-value < 0.05 and +/- 0.6 log2fold-change), being upregulated in HIGH pigs.
   Conclusions: The increased levels of specific ITGA5, LITAF, TIMP1 and ANXA2 mRNA isoforms in HIGH pigs is consistent with reports indicating that the overexpression of these four genes is associated with obesity and metabolic disorders in humans. A broader knowledge about the functional attributes of these mRNA variants would be fundamental to elucidate the consequences of transcript diversity on the determinism of porcine phenotypes of economic interest.
C1 [Figueiredo Cardoso, Taina; Castello, Anna; Gonzalez-Prendes, Rayner; Amills, Marcel] CSIC IRTA UAB UB, Dept Anim Genet, CRAG, Campus Univ Autonoma Barcelona, Barcelona 08193, Spain.
   [Figueiredo Cardoso, Taina] Minist Educ Brazil, CAPES Fdn, BR-70040020 Brasilia, DF, Brazil.
   [Quintanilla, Raquel] Inst Res & Technol Food & Agr IRTA, Anim Breeding & Genet Programme, Caldes De Montbui 08140, Spain.
   [Castello, Anna; Amills, Marcel] Univ Autonoma Barcelona, Dept Ciencia Anim & Dels Aliments, E-08193 Barcelona, Spain.
   [Canovas, Angela] Univ Guelph, Dept Anim Biosci, Ctr Genet Improvement Livestock, Guelph, ON, Canada.
C3 Consejo Superior de Investigaciones Cientificas (CSIC); Centre de
   Recerca en Agrigenomica (CRAG); University of Barcelona; Autonomous
   University of Barcelona; IRTA; Coordenacao de Aperfeicoamento de Pessoal
   de Nivel Superior (CAPES); IRTA; Autonomous University of Barcelona;
   University of Guelph
RP Amills, M (corresponding author), CSIC IRTA UAB UB, Dept Anim Genet, CRAG, Campus Univ Autonoma Barcelona, Barcelona 08193, Spain.; Amills, M (corresponding author), Univ Autonoma Barcelona, Dept Ciencia Anim & Dels Aliments, E-08193 Barcelona, Spain.; Cánovas, A (corresponding author), Univ Guelph, Dept Anim Biosci, Ctr Genet Improvement Livestock, Guelph, ON, Canada.
EM marcel.amills@uab.cat; acanovas@uoguelph.ca
RI Amills, Marcel/C-7156-2008; Cánovas, Angela/AAG-6282-2020;
   Gonzalez-Prendes, Rayner/AAC-1158-2020; Quintanilla, Raquel/I-8997-2012;
   Castello Farre, Anna/K-9637-2015; Figueiredo Cardoso, Taina/U-3286-2018
OI Castello Farre, Anna/0000-0001-8497-6251; Gonzalez Prendes,
   Rayner/0000-0003-3679-4685; Figueiredo Cardoso,
   Taina/0000-0002-6038-7521
FU Spanish Ministry of Economy and Competitivity [AGL2013-48742-C2-1-R,
   AGL2013-48742-C2-2-R, SEV-2015-0533]; Agency for Management of
   University [2014 SGR 1528]; Research Grants of the Generalitat de
   Catalunya [2014 SGR 1528]; CAPES Foundation-Coordination of Improvement
   of Higher Education, Ministry of Education of the Federal Government of
   Brazil; Spanish Ministry of Education [FPU12/00860]
FX Part of the research presented in this publication was funded by grants
   AGL2013-48742-C2-1-R and AGL2013-48742-C2-2-R awarded by the Spanish
   Ministry of Economy and Competitivity and grant 2014 SGR 1528 from the
   Agency for Management of University and Research Grants of the
   Generalitat de Catalunya. We also acknowledge the support of the Spanish
   Ministry of Economy and Competitivity for the Center of Excellence
   Severo Ochoa 2016-2019 (SEV-2015-0533) grant awarded to the Centre for
   Research in Agricultural Genomics (CRAG). Taina Figueiredo Cardoso was
   funded with a fellowship from the CAPES Foundation-Coordination of
   Improvement of Higher Education, Ministry of Education of the Federal
   Government of Brazil. Rayner GonzalezPrendes was funded with a FPU Ph.D.
   grant from the Spanish Ministry of Education (FPU12/00860). Thanks also
   to the CERCA Programme of the Generalitat de Catalunya. The funders had
   no role in study design, data collection and analysis, decision to
   publish or preparation of the manuscript.
CR Alamancos GP, 2015, RNA, V21, P1521, DOI 10.1261/rna.051557.115
   Andersson L, 2015, GENOME BIOL, V16, DOI 10.1186/s13059-015-0622-4
   Ayuso M, 2015, MEAT SCI, V108, P9, DOI 10.1016/j.meatsci.2015.04.017
   Barash Y, 2010, NATURE, V465, P53, DOI 10.1038/nature09000
   Batra J, 2012, J BIOL CHEM, V287, P15935, DOI 10.1074/jbc.M112.341156
   Birney E, 2007, NATURE, V447, P799, DOI 10.1038/nature05874
   Bolger AM, 2014, BIOINFORMATICS, V30, P2114, DOI 10.1093/bioinformatics/btu170
   Braunschweig U, 2014, GENOME RES, V24, P1774, DOI 10.1101/gr.177790.114
   Cánovas A, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0035583
   Cánovas A, 2010, BMC GENOMICS, V11, DOI 10.1186/1471-2164-11-372
   Chacko E, 2009, BMC GENOMICS, V10, pS3
   Dobin A, 2013, BIOINFORMATICS, V29, P15, DOI 10.1093/bioinformatics/bts635
   Eswaran J, 2013, SCI REP, V3, P93
   FRIEDEWALD WT, 1972, CLIN CHEM, V18
   Gallardo D, 2008, PHYSIOL GENOMICS, V35, P199, DOI 10.1152/physiolgenomics.90249.2008
   GomisRuth FX, 1997, NATURE, V389, P77, DOI 10.1038/37995
   Hartley SW, 2016, NUCLEIC ACIDS RES, V44, DOI 10.1093/nar/gkw501
   Ji ZZ, 2011, CHINESE MED J-PEKING, V124, P177, DOI 10.3760/cma.j.issn.0366-6999.2011.02.004
   Kim N, 2007, NUCLEIC ACIDS RES, V35, pD93, DOI 10.1093/nar/gkl884
   Koltes JE, 2015, BMC GENOMICS, V16, DOI 10.1186/s12864-015-1635-9
   Kroll JE, 2015, PEERJ, V3, DOI 10.7717/peerj.1419
   Li B, 2011, BMC BIOINFORMATICS, V12, DOI 10.1186/1471-2105-12-323
   Lindholm ME, 2014, FASEB J, V28, P4571, DOI 10.1096/fj.14-255000
   Livak KJ, 2001, METHODS, V25, P402, DOI 10.1006/meth.2001.1262
   Love MI, 2014, GENOME BIOL, V15, DOI 10.1186/s13059-014-0550-8
   Ma JH, 2014, J DIABETES RES, V2014, DOI 10.1155/2014/160140
   Mach N, 2006, J ANIM SCI, V84, P3039, DOI 10.2527/jas.2005-632
   Meissburger B, 2011, DIABETOLOGIA, V54, P1468, DOI 10.1007/s00125-011-2093-9
   Mockenhaupt S, 2015, SEMIN CELL DEV BIOL, V47-48, P32, DOI 10.1016/j.semcdb.2015.10.018
   Puig-Oliveras A, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0099720
   Reyes A, 2018, NUCLEIC ACIDS RES, V46, P582, DOI 10.1093/nar/gkx1165
   Robinson MD, 2008, BIOSTATISTICS, V9, P321, DOI 10.1093/biostatistics/kxm030
   ROTH T, 1993, P NATL ACAD SCI USA, V90, P9640, DOI 10.1073/pnas.90.20.9640
   Salameh A, 2016, JCI INSIGHT, V1, DOI 10.1172/jci.insight.86351
   Schurch NJ, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0094270
   Shenker S, 2015, RNA, V21, P14, DOI 10.1261/rna.046037.114
   Taneri B, 2004, GENOME BIOL, V5, DOI 10.1186/gb-2004-5-10-r75
   Trapnell C, 2010, NAT BIOTECHNOL, V28, P511, DOI 10.1038/nbt.1621
   Wang ET, 2008, NATURE, V456, P470, DOI 10.1038/nature07509
   Xie Y, 2014, GENE, V534, P189, DOI 10.1016/j.gene.2013.10.061
   Yao Y, 2016, GENOMICS, V107, P170, DOI 10.1016/j.ygeno.2016.03.003
   Zhang C, 2017, BMC GENOMICS, V18, DOI 10.1186/s12864-017-4002-1
   Zhang SH, 2016, GENE, V575, P531, DOI 10.1016/j.gene.2015.09.026
   Zhu HQ, 2017, INT J BIOL SCI, V13, P1489, DOI 10.7150/ijbs.21637
NR 44
TC 28
Z9 31
U1 0
U2 8
PU BMC
PI LONDON
PA CAMPUS, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
SN 1471-2164
J9 BMC GENOMICS
JI BMC Genomics
PD FEB 14
PY 2018
VL 19
AR 145
DI 10.1186/s12864-018-4515-2
PG 12
WC Biotechnology & Applied Microbiology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biotechnology & Applied Microbiology; Genetics & Heredity
GA FW7QF
UT WOS:000425518400002
PM 29444639
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Arvela, E
   Venermo, M
   Söderström, M
   Albäck, A
   Lepäntalo, M
AF Arvela, Eva
   Venermo, Maarit
   Soderstrom, Maria
   Alback, Anders
   Lepantalo, Mauri
TI Outcome of Infrainguinal Single-Segment Great Saphenous Vein Bypass for
   Critical Limb Ischemia is Superior to Alternative Autologous Vein
   Bypass, Especially in Patients With High Operative Risk
SO ANNALS OF VASCULAR SURGERY
LA English
DT Article
ID LOWER-EXTREMITY REVASCULARIZATION; GLOMERULAR-FILTRATION-RATE; SERUM
   CREATININE; ARM VEIN; FEMOROPOPLITEAL BYPASS; GRAFT STENOSIS;
   SURVEILLANCE; POPLITEAL; CONDUIT; PATENCY
AB Background: Single-segment great saphenous vein (ssGSV) is the conduit of choice in infrainguinal bypass for critical limb ischemia (CLI). The aim of this study was to assess results of other autologous vein grafts and risk factors for graft stenosis development and graft failure. The purpose was also to evaluate outcome of patients with high operative risk undergoing infrainguinal alternative autologous vein bypass for CLI.
   Methods: We retrospectively reviewed 1,109 consecutive infrainguinal bypasses performed between 2000 and 2007 for CLI. Rate and type of operations needed to maintain graft patency were evaluated. Outcome of different types of vein grafts in terms of primary patency, assisted primary patency, secondary patency, and limb salvage was assessed using Kaplan-Meier method. Predictors of poor outcome as well as patient-and graft-related risk factors for graft revision and graft failure were analyzed using multivariate analysis.
   Results: Median follow-up period was 37 (0-121) months. Primary patency, assisted primary patency, secondary patency, and limb salvage at 1 and 3 years were significantly better in ssGSV graft group than in alternative autologous vein graft (AAVG) group-74.4% and 67.1% versus 53.7% and 42.0% (P < 0.0001), 82.8% and 78.2% versus 67.2% and 57.8% (P < 0.0001), 84.8% and 80.8% versus 69.9% and 61.4% (P < 0.0001), and 88.9% and 86.9% versus 83.0% and 77.2% (P < 0.0001), respectively. In multivariate analysis, non-ssGSV graft was the only independent risk factor for the graft stenosis development (relative risk [RR]: 2.62, 95% confidence interval [CI]: 1.56-4.38, P < 0.0001), for graft occlusion (RR: 2.27, 95% CI: 1.52-3.40, P < 0.0001), and for graft failure (stenosis or occlusion) (RR: 2.00, 95% CI: 1.39-2.88, P < 0.0001). Revision rate of non-ssGSV conduits was higher than that of ssGSV grafts (18% vs. 12%, P = 0.007). High-risk patients (age of >80 years, coronary artery disease, estimated glomerular filtration rate of < 30 mL/min/1.73 m(2)) who underwent bypass with arm vein or spliced vein had extremely poor outcome (1-year leg salvage rate and survival rate of 71.4% and 28.6%, respectively).
   Conclusion: The ssGSV graft is superior to any other autologous vein graft in terms of midterm patency and leg salvage. It also needs less maintenance procedures than AAVGs. Non-ssGSV graft is independent predictor of both graft stenosis development and graft failure. Acceptable patency and leg salvage rates can also be achieved with AAVGs. However, patients with high operative risk and non-ssGSV graft bypass have poor outcome.
C1 [Arvela, Eva; Venermo, Maarit; Soderstrom, Maria; Alback, Anders; Lepantalo, Mauri] Univ Helsinki, Dept Vasc Surg, Cent Hosp, FI-00029 Helsinki, Finland.
C3 University of Helsinki; Helsinki University Central Hospital
RP Arvela, E (corresponding author), Univ Helsinki, Dept Vasc Surg, Cent Hosp, POB 340, FI-00029 Helsinki, Finland.
EM eva.arvela@hus.fi
OI Venermo, Maarit/0000-0001-8814-0988
CR Alback A, 1996, ANN CHIR GYNAECOL FE, V85, P325
   Armstrong PA, 2004, J VASC SURG, V40, P724, DOI 10.1016/j.jvs.2004.07.037
   Arvela E, 2008, EUR J VASC ENDOVASC, V36, P77, DOI 10.1016/j.ejvs.2008.01.018
   Arvela E, 2011, BRIT J SURG, V98, P518, DOI 10.1002/bjs.7390
   Arvela E, 2010, J VASC SURG, V52, P616, DOI 10.1016/j.jvs.2010.04.013
   BELKIN M, 1995, J VASC SURG, V21, P282, DOI 10.1016/S0741-5214(95)70269-5
   Chew DKW, 2001, J VASC SURG, V33, P259, DOI 10.1067/mva.2001.112699
   Davies AH, 2005, CIRCULATION, V112, P1985, DOI 10.1161/CIRCULATIONAHA.104.518738
   Faries PL, 2000, J VASC SURG, V31, P50, DOI 10.1016/S0741-5214(00)70067-X
   Faries PL, 2000, J VASC SURG, V31, P1119, DOI 10.1016/S0741-5214(00)90101-0
   Faries PL, 2000, J VASC SURG, V32, P1080, DOI 10.1067/mva.2000.111279
   Gentile AT, 1996, J VASC SURG, V23, P272, DOI 10.1016/S0741-5214(96)70271-9
   GRIGG MJ, 1988, BRIT J SURG, V75, P737, DOI 10.1002/bjs.1800750806
   IDU MM, 1992, EUR J VASCULAR SURG, V6, P456, DOI 10.1016/S0950-821X(05)80616-4
   Idu MM, 1999, EUR J VASC ENDOVASC, V17, P15, DOI 10.1053/ejvs.1998.0676
   Kertai MD, 2003, CLIN NEPHROL, V59, P17
   Klinkert P, 2004, EUR J VASC ENDOVASC, V27, P357, DOI 10.1016/j.ejvs.2003.12.027
   Levey AS, 2006, ANN INTERN MED, V145, P247, DOI 10.7326/0003-4819-145-4-200608150-00004
   Levey AS, 1999, ANN INTERN MED, V130, P461, DOI 10.7326/0003-4819-130-6-199903160-00002
   LUNDELL A, 1993, CLIN PHYSIOL, V13, P547, DOI 10.1111/j.1475-097X.1993.tb00470.x
   LUNDELL A, 1995, J VASC SURG, V21, P26, DOI 10.1016/S0741-5214(95)70241-5
   Maithel SK, 2006, AM J NEPHROL, V26, P612, DOI 10.1159/000098150
   Norgren L, 2007, EUR J VASC ENDOVASC, V33, pS5, DOI 10.1016/j.ejvs.2006.09.024
   Pereira CE, 2006, J VASC SURG, V44, P510, DOI 10.1016/j.jvs.2006.04.054
   PLECHA FR, 1985, J VASC SURG, V2, P769, DOI 10.1067/mva.1985.avs0020769
   Robinson KD, 1997, J VASC SURG, V26, P425, DOI 10.1016/S0741-5214(97)70035-1
   Rutherford RB, 1997, J VASC SURG, V26, P517, DOI 10.1016/S0741-5214(97)70045-4
   Schanzer A, 2007, J VASC SURG, V46, P1180, DOI 10.1016/j.jvs.2007.08.033
   Schanzer A, 2009, J VASC SURG, V50, P769, DOI 10.1016/j.jvs.2009.05.055
   SEABROOK GR, 1991, J VASC SURG, V13, P646
   SLADEN JG, 1981, AM J SURG, V141, P546, DOI 10.1016/0002-9610(81)90045-3
   Söderström M, 2010, SCAND J SURG, V99, P230
   SZILAGYI DE, 1973, ANN SURG, V178, P232, DOI 10.1097/00000658-197309000-00002
   Taylor SM, 2009, J VASC SURG, V50, P534, DOI 10.1016/j.jvs.2009.03.030
   VARTY K, 1993, EUR J VASCULAR SURG, V7, P567, DOI 10.1016/S0950-821X(05)80371-8
   WHITTEMORE AD, 1981, ANN SURG, V193, P35, DOI 10.1097/00000658-198101000-00006
   Wilson YG, 1996, EUR J VASC ENDOVASC, V11, P164, DOI 10.1016/S1078-5884(96)80046-3
NR 37
TC 40
Z9 44
U1 0
U2 3
PU ELSEVIER SCIENCE INC
PI NEW YORK
PA STE 800, 230 PARK AVE, NEW YORK, NY 10169 USA
SN 0890-5096
EI 1615-5947
J9 ANN VASC SURG
JI Ann. Vasc. Surg.
PD APR
PY 2012
VL 26
IS 3
BP 396
EP 403
DI 10.1016/j.avsg.2011.08.013
PG 8
WC Surgery; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Surgery; Cardiovascular System & Cardiology
GA 913BZ
UT WOS:000301847700014
PM 22285375
DA 2025-04-10
ER

PT J
AU Ihara, D
   Mizukoshi, M
   Tabuchi, A
AF Ihara, Daisuke
   Mizukoshi, Miho
   Tabuchi, Akiko
TI Brain-derived neurotrophic factor (BDNF) downregulates mRNA levels of
   suppressor of cancer cell invasion (SCAI) variants in cortical neurons
SO GENES TO CELLS
LA English
DT Article
DE BDNF; ERK; MKL; MRTF; SCAI; SRF
ID INHIBITOR; SRF; TRANSCRIPTION
AB Suppressor of cancer cell invasion (SCAI) acts as a transcriptional repressor of serum response factor (SRF)-mediated gene expression by binding to megakaryoblastic leukemia (MKL)/myocardin-related transcription factor (MRTF), which is an SRF transcriptional coactivator. Growing evidence suggests that SCAI is a negative regulator of neuronal morphology, whereas MKL2/MRTFB is a positive regulator. The mRNA expression of SCAI is downregulated during brain development, suggesting that a reduction in SCAI contributes to the reduced suppression of SRF-mediated gene induction, thus increasing dendritic complexity and developing neuronal circuits. In the present study, we hypothesized that brain-derived neurotrophic factor (BDNF), which is important for neuronal plasticity and development, might alter SCAI mRNA levels. We therefore investigated the effects of BDNF on SCAI mRNA levels in primary cultured cortical neurons. Furthermore, because alternative splicing generates several SCAI variants in the brain, we measured SCAI variant mRNA after BDNF stimulation. Both SCAI variant 1 and total SCAI mRNA expression levels were downregulated by BDNF. Moreover, the extracellular signal-regulated protein kinase/mitogen-activated protein kinase (ERK/MAPK) pathway was involved in the BDNF-mediated decrease in SCAI mRNA expression. Our findings provide insights into the molecular mechanism underlying a neurotrophic factor switch for the repressive transcriptional complex that includes SCAI.
C1 [Ihara, Daisuke; Mizukoshi, Miho; Tabuchi, Akiko] Univ Toyama, Grad Sch Med & Pharmaceut Sci, Lab Mol Neurobiol, Toyama, Japan.
   [Tabuchi, Akiko] Univ Toyama, Grad Sch Med & Pharmaceut Sci, Lab Mol Neurobiol, 2630 Sugitani, Toyama 9300194, Japan.
C3 University of Toyama; University of Toyama
RP Tabuchi, A (corresponding author), Univ Toyama, Grad Sch Med & Pharmaceut Sci, Lab Mol Neurobiol, 2630 Sugitani, Toyama 9300194, Japan.
EM atabuchi@pha.u-toyama.ac.jp
FU Japan Society for the Promotion of Science [JP26460064, JP18K06625,
   JP23H03305, JP20K15989]; KAKENHI; Uehara Memorial Foundation; Smoking
   Research Foundation; Grants-in-Aid for Scientific Research [20K15989,
   23K27995] Funding Source: KAKEN
FX The authors are grateful to Sumitomo Pharma Co., Ltd. for providing us
   with BDNF. This work was supported by KAKENHI (grant numbers JP26460064,
   JP18K06625, and JP23H03305 to Akiko Tabuchi and JP20K15989 to Daisuke
   Ihara), the Uehara Memorial Foundation (to Akiko Tabuchi), the Smoking
   Research Foundation (to Akiko Tabuchi). We thank Bronwen Gardner, PhD,
   from Edanz () for editing a draft of this manuscript. Part of Figure 1
   has been published previously in Mizukoshi et al. (2020).
CR Brandt DT, 2009, NAT CELL BIOL, V11, P557, DOI 10.1038/ncb1862
   Chandía-Cristi A, 2023, INT J MOL SCI, V24, DOI 10.3390/ijms24031944
   Etkin A, 2006, NEURON, V50, P127, DOI 10.1016/j.neuron.2006.03.013
   Favata MF, 1998, J BIOL CHEM, V273, P18623, DOI 10.1074/jbc.273.29.18623
   Ihara D, 2023, BIOL PHARM BULL, V46, P636, DOI 10.1248/bpb.b22-00825
   Iram T, 2022, NATURE, V605, P509, DOI 10.1038/s41586-022-04722-0
   Ishikawa M, 2010, J BIOL CHEM, V285, P32734, DOI 10.1074/jbc.M110.118745
   Kalita K, 2006, J NEUROSCI, V26, P10020, DOI 10.1523/JNEUROSCI.2644-06.2006
   Kikuchi K, 2019, J NEUROCHEM, V148, P204, DOI 10.1111/jnc.14596
   Medjkane S, 2009, NAT CELL BIOL, V11, P257, DOI 10.1038/ncb1833
   Mizukoshi M, 2020, BIOCHEM BIOPH RES CO, V529, P615, DOI 10.1016/j.bbrc.2020.06.064
   Park H, 2013, NAT REV NEUROSCI, V14, P7, DOI 10.1038/nrn3379
   Ramanan N, 2005, NAT NEUROSCI, V8, P759, DOI 10.1038/nn1462
   Smith RJ, 1996, J PHARMACOL EXP THER, V278, P320
   Tabuchi A, 2022, NEUROCHEM RES, V47, P2545, DOI 10.1007/s11064-022-03632-x
   Tabuchi A, 2021, FRONT MOL NEUROSCI, V14, DOI 10.3389/fnmol.2021.767842
   VLAHOS CJ, 1994, J BIOL CHEM, V269, P5241
NR 17
TC 0
Z9 1
U1 0
U2 0
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 1356-9597
EI 1365-2443
J9 GENES CELLS
JI Genes Cells
PD JAN
PY 2024
VL 29
IS 1
BP 99
EP 105
DI 10.1111/gtc.13086
EA NOV 2023
PG 7
WC Cell Biology; Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Genetics & Heredity
GA DV7J2
UT WOS:001109732200001
PM 38009531
DA 2025-04-10
ER

PT J
AU Hwang, I
   Gottlieb, PD
AF Hwang, I
   Gottlieb, PD
TI The Bop gene adjacent to the mouse CD8b gene encodes distinct
   zinc-finger proteins expressed in CTLs and in muscle
SO JOURNAL OF IMMUNOLOGY
LA English
DT Article
ID BETA-CHAIN; MHC CLASS; T-CELLS; NEGATIVE SELECTION; POSITIVE SELECTION;
   ALPHA-3 DOMAIN; MESSENGER-RNAS; LYT-2; RECOGNITION; LYMPHOCYTE
AB The Bop gene (for CD8b opposite) is located immediately upstream of the mouse CD86 gene. Expression of Bop gene transcripts was previously observed in several long term CTL lines and in thymus. The present studies demonstrate that expression of the Bop gene in lymphocytes appears to be confined to CD8-positive cells, and that Bop gene expression is inducible by Con A. They further show that a single Bop gene encodes protein products with distinct amino-terminal sequences that are expressed in CTLs (t-BOP) and in cardiac and skeletal muscle (skm-BOP), as well as what appears to be a noncoding cDNA (t-ncb) expressed only in CTLs. The t-BOP and t-ncb cDNAs in CTLs result from alternative splicing of a single primary transcript, whereas the Bop transcripts expressed in CTLs and in muscle appear to be transcribed from different promoters. The BOP proteins expressed in CTLs and muscle contain zinc finger-like motifs with homology to those of the ETO/MTG8 proto-oncogene and several other proteins of interest. Western blot analysis with a hamster anti-BOP mAb have detected the BOP protein in muscle cells and in COS 7 cells transfected with Bop cDNA constructs.
C1 UNIV TEXAS, DEPT MICROBIOL, AUSTIN, TX 78712 USA.
C3 University of Texas System; University of Texas Austin
CR AUSUBEL FM, 1994, EXPRESSION PURIFICAT
   BOYD RT, 1986, P NATL ACAD SCI USA, V83, P9134, DOI 10.1073/pnas.83.23.9134
   BOYSE EA, 1971, TRANSPLANTATION, V11, P351, DOI 10.1097/00007890-197103000-00021
   BOYSE EA, 1968, PROC R SOC SER B-BIO, V170, P175, DOI 10.1098/rspb.1968.0032
   BRENNER CA, 1989, BIOTECHNIQUES, V7, P1096
   CHIRGWIN JM, 1979, BIOCHEMISTRY-US, V18, P5294, DOI 10.1021/bi00591a005
   CHO SG, 1991, P NATL ACAD SCI USA, V88, P5197, DOI 10.1073/pnas.88.12.5197
   COLEMAN JE, 1992, ANNU REV BIOCHEM, V61, P897, DOI 10.1146/annurev.bi.61.070192.004341
   CONNOLLY JM, 1988, J EXP MED, V168, P325, DOI 10.1084/jem.168.1.325
   CROOKS MEC, 1994, IMMUNITY, V1, P277
   DURDA PJ, 1976, J EXP MED, V144, P476, DOI 10.1084/jem.144.2.476
   DURDA PJ, 1978, J IMMUNOL, V121, P983
   FEINSTEIN PG, 1995, GENETICS, V140, P573
   FUNGLEUNG WP, 1993, EUR J IMMUNOL, V23, P212, DOI 10.1002/eji.1830230133
   GAJEWSKI TF, 1991, J IMMUNOL, V146, P1750
   GILLIS S, 1977, NATURE, V268, P154, DOI 10.1038/268154a0
   GORMAN SD, 1988, J IMMUNOL, V140, P3646
   GU JJ, 1992, IMMUNOGENETICS, V36, P283
   HWANG I, 1995, IMMUNOGENETICS, V42, P353, DOI 10.1007/BF00179396
   ITANO A, 1994, IMMUNITY, V1, P287, DOI 10.1016/1074-7613(94)90080-9
   KISHI F, 1993, GENE, V133, P243
   KOZAK M, 1991, J CELL BIOL, V115, P887, DOI 10.1083/jcb.115.4.887
   LEDBETTER JA, 1981, J EXP MED, V153, P1503, DOI 10.1084/jem.153.6.1503
   LEE WH, 1994, INT IMMUNOL, V6, P1307, DOI 10.1093/intimm/6.9.1307
   Meyers S, 1995, CRIT REV EUKAR GENE, V5, P365, DOI 10.1615/CritRevEukarGeneExpr.v5.i3-4.70
   MONACO JJ, 1990, SCIENCE, V250, P1723, DOI 10.1126/science.2270487
   MONACO JJ, 1992, IMMUNOL TODAY, V13, P173, DOI 10.1016/0167-5699(92)90122-N
   MOUNT SM, 1982, NUCLEIC ACIDS RES, V10, P459, DOI 10.1093/nar/10.2.459
   NAKAYAMA K, 1994, SCIENCE, V263, P1131, DOI 10.1126/science.8108731
   NIMAN HL, 1983, P NATL ACAD SCI-BIOL, V80, P4949, DOI 10.1073/pnas.80.16.4949
   NORMENT AM, 1988, NATURE, V336, P79, DOI 10.1038/336079a0
   OWENS GP, 1991, MOL CELL BIOL, V11, P4177, DOI 10.1128/MCB.11.8.4177
   PARNES JR, 1989, ADV IMMUNOL, V44, P265, DOI 10.1016/S0065-2776(08)60644-6
   PRICE MG, 1993, J BIOL CHEM, V268, P21800
   REILLY EB, 1980, J IMMUNOL, V125, P2245
   SABATH DE, 1990, GENE, V91, P185, DOI 10.1016/0378-1119(90)90087-8
   SALTER RD, 1989, NATURE, V338, P345, DOI 10.1038/338345a0
   SANCHEZGARCIA I, 1994, TRENDS GENET, V10, P315, DOI 10.1016/0168-9525(94)90034-5
   SWAIN SL, 1983, IMMUNOL REV, V74, P129, DOI 10.1111/j.1600-065X.1983.tb01087.x
   VEILLETTE A, 1988, CELL, V55, P301, DOI 10.1016/0092-8674(88)90053-0
   WEISS A, 1994, CELL, V76, P263, DOI 10.1016/0092-8674(94)90334-4
   YOUN HJ, 1988, IMMUNOGENETICS, V28, P353, DOI 10.1007/BF00364234
   ZAMOYSKA R, 1994, IMMUNITY, V1, P243, DOI 10.1016/1074-7613(94)90075-2
NR 43
TC 32
Z9 37
U1 0
U2 0
PU AMER ASSOC IMMUNOLOGISTS
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA
SN 0022-1767
EI 1550-6606
J9 J IMMUNOL
JI J. Immunol.
PD FEB 1
PY 1997
VL 158
IS 3
BP 1165
EP 1174
PG 10
WC Immunology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Immunology
GA WE020
UT WOS:A1997WE02000018
PM 9013956
DA 2025-04-10
ER

PT J
AU Hirao, H
   Kojima, H
   Dery, KJ
   Nakamura, K
   Kadono, K
   Zhai, Y
   Farmer, DG
   Kaldas, FM
   Kupiec-Weglinski, JW
AF Hirao, Hirofumi
   Kojima, Hidenobu
   Dery, Kenneth J.
   Nakamura, Kojiro
   Kadono, Kentaro
   Zhai, Yuan
   Farmer, Douglas G.
   Kaldas, Fady M.
   Kupiec-Weglinski, Jerzy W.
TI Neutrophil CEACAM1 determines susceptibility to NETosis by regulating
   the S1PR2/S1PR3 axis in liver
SO JOURNAL OF CLINICAL INVESTIGATION
LA English
DT Article
ID EXTRACELLULAR TRAPS; SPHINGOSINE 1-PHOSPHATE; ISCHEMIA; TARGET; ATPASE;
   INFLAMMATION; EXPRESSION; CELLS
AB Neutrophils, the largest innate immune cell population in humans, are the primary proinflammatory sentinel in the ischemia-reperfusion injury (IRI) mechanism in orthotopic liver transplantation (OLT). Carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1, CC1, or CD66a) is essential in neutrophil activation and serves as a checkpoint regulator of innate immune-driven IRI cascade in OLT. Although CC1 alternative splicing generates two functionally distinct short and long cytoplasmic isoforms, their role in neutrophil activation remains unknown. Here, we undertook molecular and functional studies to interrogate the significance of neutrophil CC1 signaling in mouse and human OLT recipients. In the experimental arm, we employed a mouse OLT model to document that ablation of recipient-derived neutrophil CC1-long (CC1-L) isotype aggravated hepatic IRI by promoting neutrophil extracellular traps (NETs). Notably, by regulating the S1P-S1PR2/S1PR3 axis, neutrophil CC1-L determined susceptibility to NET formation via autophagy signaling. In the clinical arm, liver grafts from 55 transplant patients selectively enriched for neutrophil CC1-L showed relative resistance to ischemia-reperfusion (IR) stress/ tissue damage, improved hepatocellular function, and clinical outcomes. In conclusion, despite neutrophils being considered a principal villain in peritransplant tissue injury, their CC1-L isoform may serve as a regulator of IR stress resistance/NETosis in human and mouse OLT recipients.
C1 [Hirao, Hirofumi; Kojima, Hidenobu; Dery, Kenneth J.; Nakamura, Kojiro; Kadono, Kentaro; Zhai, Yuan; Farmer, Douglas G.; Kaldas, Fady M.; Kupiec-Weglinski, Jerzy W.] UCLA, David Geffen Sch Med, Div Liver & Pancreas Transplantat, Dumont UCLA Transplantat Ctr,Dept Surg, Los Angeles, CA USA.
   [Nakamura, Kojiro] Kyoto Univ, Grad Sch Med, Dept Surg, Div Hepato Biliary Pancreat Surg & Transplantat,D, Kyoto, Japan.
   [Kupiec-Weglinski, Jerzy W.] UCLA, David Geffen Sch Med, Dept Pathol & Lab Med, Los Angeles, CA USA.
   [Kupiec-Weglinski, Jerzy W.] Dumont UCLA Transplant Ctr, 77-120 CHS, 10833 Le Conte Ave, Los Angeles, CA 90095 USA.
C3 University of California System; University of California Los Angeles;
   University of California Los Angeles Medical Center; David Geffen School
   of Medicine at UCLA; Kyoto University; University of California System;
   University of California Los Angeles; University of California Los
   Angeles Medical Center; David Geffen School of Medicine at UCLA
RP Kupiec-Weglinski, JW (corresponding author), Dumont UCLA Transplant Ctr, 77-120 CHS, 10833 Le Conte Ave, Los Angeles, CA 90095 USA.
EM jkupiec@mednet.ucla.edu
RI Nakamura, Kojiro/AFN-3737-2022
OI Hirao, Hirofumi/0000-0001-6975-2436; Dery, Kenneth/0000-0003-4238-4092
FU NIH [P01 AI120944, R01 DK062357, DK107533, DK102110]; National Institute
   of Allergy and Infectious Diseases [P01AI120944] Funding Source: NIH
   RePORTER; National Institute of Diabetes and Digestive and Kidney
   Diseases [R01DK062357] Funding Source: NIH RePORTER
FX Acknowledgments This work was supported by NIH grants P01 AI120944 (to
   JWKW, YZ, and FMK) , R01 DK062357, DK107533, and DK102110 (to JWKW) .
CR Al Alam N, 2016, BIOCHEM CELL BIOL, V94, P371, DOI 10.1139/bcb-2016-0025
   Bajwa A, 2016, J AM SOC NEPHROL, V27, P1076, DOI 10.1681/ASN.2015010095
   Bryan AM, 2018, CELL MICROBIOL, V20, DOI 10.1111/cmi.12836
   Castanheira FVS, 2019, BLOOD, V133, P2178, DOI 10.1182/blood-2018-11-844530
   Chakkour Mohamed, 2019, Cell Physiol Biochem, V53, P518, DOI 10.33594/000000155
   Chakrabarty S, 2022, ADIPOCYTE, V11, P69, DOI 10.1080/21623945.2021.2021700
   Chen KW, 2018, SCI IMMUNOL, V3, DOI 10.1126/sciimmunol.aar6676
   Chen LS, 2018, CELL DEATH DIS, V9, DOI 10.1038/s41419-018-0538-5
   Chen SH, 2004, J BIOL CHEM, V279, P7988, DOI 10.1074/jbc.M305351200
   Chen T, 2021, FRONT IMMUNOL, V12, DOI 10.3389/fimmu.2021.775267
   Chen W, 2021, TRANSPL IMMUNOL, V65, DOI 10.1016/j.trim.2020.101347
   Chicca IJ, 2018, FRONT IMMUNOL, V9, DOI 10.3389/fimmu.2018.00337
   Dery KJ, 2011, J BIOL CHEM, V286, DOI 10.1074/jbc.M110.204057
   Douda DN, 2014, BLOOD, V123, P597, DOI 10.1182/blood-2013-09-526707
   Fedele AO, 2020, BIOSCIENCE REP, V40, DOI 10.1042/BSR20200905
   Gao Y, 2016, CELL DEATH DIS, V7, DOI 10.1038/cddis.2016.236
   Geng TY, 2015, J LIPID RES, V56, P2359, DOI 10.1194/jlr.M063511
   Germic N, 2017, IMMUNOLOGY, V152, P517, DOI 10.1111/imm.12790
   Ghosh Sumona, 2010, Hepat Med, V2010, P69
   Heo JY, 2019, BIOMOL THER, V27, P373, DOI 10.4062/biomolther.2018.215
   Hirao H, 2022, NAT REV GASTRO HEPAT, V19, P239, DOI 10.1038/s41575-021-00549-8
   Hoitsma AJ, 2011, NEPHROL DIAL TRANSPL, V26, P3802, DOI 10.1093/ndt/gfr503
   Hooper KM, 2022, J CELL BIOL, V221, DOI 10.1083/jcb.202105112
   Huang H, 2015, HEPATOLOGY, V62, P600, DOI 10.1002/hep.27841
   Itakura A, 2013, AM J PHYSIOL-CELL PH, V305, pC348, DOI 10.1152/ajpcell.00108.2013
   Ito T, 2018, J SURG RES, V222, P139, DOI 10.1016/j.jss.2017.09.048
   Jorch SK, 2017, NAT MED, V23, P279, DOI 10.1038/nm.4294
   Kageyama S, 2018, HEPATOLOGY, V68, P258, DOI 10.1002/hep.29787
   Kim WM, 2019, SEMIN IMMUNOL, V42, DOI 10.1016/j.smim.2019.101296
   King A, 2017, GASTROENTEROLOGY, V153, P233, DOI 10.1053/j.gastro.2017.03.022
   Klionsky DJ, 2021, EMBO J, V40, DOI 10.15252/embj.2021108863
   Kuczia P, 2020, CLIN TRANSL ALLERGY, V10, DOI 10.1186/s13601-020-00337-8
   Kwong Eric K, 2019, Liver Res, V3, P19, DOI 10.1016/j.livres.2019.02.003
   Lee H, 2021, GLIA, V69, P1110, DOI 10.1002/glia.23952
   Lee KH, 2017, AUTOIMMUN REV, V16, P1160, DOI 10.1016/j.autrev.2017.09.012
   Li YQ, 2014, SURGERY, V156, P229, DOI 10.1016/j.surg.2014.04.009
   Liang XF, 2020, BIOMED PHARMACOTHER, V126, DOI 10.1016/j.biopha.2020.110065
   Liao CY, 2018, FRONT IMMUNOL, V9, DOI 10.3389/fimmu.2018.02980
   Liberman R, 2014, J BIOL CHEM, V289, P1355, DOI 10.1074/jbc.M113.524561
   Liu HY, 2021, FRONT PHARMACOL, V11, DOI 10.3389/fphar.2020.598007
   Lu RZ, 2012, PLOS PATHOG, V8, DOI 10.1371/journal.ppat.1002597
   Masucci MT, 2020, FRONT IMMUNOL, V11, DOI 10.3389/fimmu.2020.01749
   McInturff AM, 2012, BLOOD, V120, P3118, DOI 10.1182/blood-2012-01-405993
   Nagahashi M, 2018, CANCER SCI, V109, P3671, DOI 10.1111/cas.13802
   Nakamura K, 2020, J CLIN INVEST, V130, P2689, DOI 10.1172/JCI133142
   Nakamura K, 2017, J HEPATOL, V67, P1232, DOI 10.1016/j.jhep.2017.08.010
   Njeim R, 2020, J MOL ENDOCRINOL, V65, pR65, DOI 10.1530/JME-20-0128
   Nojima H, 2016, J HEPATOL, V64, P60, DOI 10.1016/j.jhep.2015.07.030
   Park WJ, 2020, MOL CELLS, V43, P419, DOI 10.14348/molcells.2020.0054
   Rayes RF, 2020, J IMMUNOL, V204, P2285, DOI 10.4049/jimmunol.1900240
   Reber LL, 2017, J EXP MED, V214, P1249, DOI 10.1084/jem.20161238
   Remijsen Q, 2011, CELL RES, V21, P290, DOI 10.1038/cr.2010.150
   Rosazza T, 2021, FEBS J, V288, P3334, DOI 10.1111/febs.15589
   Sanagawa A, 2016, MOL MED REP, V14, P1841, DOI 10.3892/mmr.2016.5451
   Silk E, 2017, CELL DEATH DIS, V8, DOI 10.1038/cddis.2017.52
   Smith P, 2017, INT J MOL SCI, V18, DOI 10.3390/ijms18102027
   Sollberger G, 2018, SCI IMMUNOL, V3, DOI 10.1126/sciimmunol.aar6689
   Song F, 2018, ANESTHESIOLOGY, V129, P311, DOI 10.1097/ALN.0000000000002196
   SUZUKI S, 1993, TRANSPLANTATION, V55, P1265
   Taniguchi M, 2012, J BIOL CHEM, V287, DOI 10.1074/jbc.M112.416552
   Thålin C, 2018, PLOS ONE, V13, DOI 10.1371/journal.pone.0191231
   Verstockt B, 2022, NAT REV GASTRO HEPAT, V19, P351, DOI 10.1038/s41575-021-00574-7
   Wang J, 2022, ALIMENT PHARM THER, V55, P277, DOI 10.1111/apt.16741
   Warnatsch A, 2015, SCIENCE, V349, P316, DOI 10.1126/science.aaa8064
   Woodfin A, 2011, NAT IMMUNOL, V12, P761, DOI 10.1038/ni.2062
   Wu XT, 2022, FRONT IMMUNOL, V13, DOI 10.3389/fimmu.2022.781273
   Yang JJ, 2018, CELL PHYSIOL BIOCHEM, V49, P1677, DOI 10.1159/000493611
   Yi ZJ, 2020, HEPATOLOGY, V72, P1394, DOI 10.1002/hep.31147
   Zhan YQ, 2022, J IMMUNOL, V208, P968, DOI 10.4049/jimmunol.2100593
   Zhang HJ, 2020, FRONT IMMUNOL, V11, DOI 10.3389/fimmu.2020.00987
   Zhao XH, 2021, CELL IMMUNOL, V359, DOI 10.1016/j.cellimm.2020.104243
   Zhao XH, 2020, CELL DEATH DIS, V11, DOI 10.1038/s41419-020-2582-1
NR 72
TC 23
Z9 25
U1 0
U2 13
PU AMER SOC CLINICAL INVESTIGATION INC
PI ANN ARBOR
PA 2015 MANCHESTER RD, ANN ARBOR, MI 48104 USA
SN 0021-9738
EI 1558-8238
J9 J CLIN INVEST
JI J. Clin. Invest.
PD FEB 1
PY 2023
VL 133
IS 3
AR e162940
DI 10.1172/JCI162940
PG 20
WC Medicine, Research & Experimental
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Research & Experimental Medicine
GA 9H7QR
UT WOS:000939023300004
PM 36719377
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Kiladjian, JJ
   Elkassar, N
   Hetet, G
   Briere, J
   Grandchamp, B
   Gardin, C
AF Kiladjian, JJ
   Elkassar, N
   Hetet, G
   Briere, J
   Grandchamp, B
   Gardin, C
TI Study of the thrombopoietin receptor in essential thrombocythemia
SO LEUKEMIA
LA English
DT Article
DE essential thrombocythemia; thrombocytosis; megakaryocytes; c-mpl
ID MEGAKARYOCYTE COLONY FORMATION; PROTOONCOGENE C-MPL; MYELOPROLIFERATIVE
   DISORDERS; ERYTHROPOIETIN RECEPTOR; MOLECULAR-CLONING; GM-CSF; MEMBER;
   GROWTH; CELL; TRANSCRIPTION
AB Essential thrombocythemia (ET) is a myeloproliferative disorder associated with megakaryocytic hyperplasia and thrombocytosis. In this disease, in vitro autonomous growth of megakaryocytic colonies has been demonstrated by various investigators. This phenomenon is impaired by the inhibition of the thrombopoietin/c-mpl pathway. In order to evaluate the potential role of mutations of the receptor gene in the origin of this autonomous growth, we compared the expression of c-mpl mRNA isoforms in platelets derived from ET patients and normal subjects, Overlapping c-mpl PCR fragments derived from four ET patients were sequenced to search for small mutations, In the 10 ET and five normal samples we studied, relative expression of the c-mpl isoforms was identical, New variants of Mpl-P and K isoforms, Mpl-P2 and K2 were detected, Cloning of these isoforms indicated that they are produced by alternative splicing of exon 9 sequences shared by Mpl-P and K. Their predicted amino acid sequence would be deleted by 24 aminoacids, upstream of the WSSWS box of the second domain of c-mpl. Two sequence variations, leading to DNA restriction polymorphisms, were present in the extracellular and Mpl-K intracytoplasmic domains. Both were present in normal and ET samples, excluding mutations of c-mpl as a cause of ET.
C1 FAC XAVIER BICHAT,U409,INSERM,F-75018 PARIS,FRANCE.
   HOP BEAUJON,SERV HEMATOL CLIN,CLICHY,FRANCE.
   ASSOC CLAUDE BERNARD,PARIS,FRANCE.
C3 Institut National de la Sante et de la Recherche Medicale (Inserm);
   Universite Paris Cite; Universite Paris Cite; Assistance Publique
   Hopitaux Paris (APHP); Hopital Universitaire Beaujon - APHP
RI Kiladjian, Jean-Jacques/K-5345-2019
OI Kiladjian, Jean-Jacques/0000-0002-8121-438X
CR ALEXANDER WS, 1995, ONCOGENE, V10, P795
   DAndrea RJ, 1996, BLOOD, V87, P2641, DOI 10.1182/blood.V87.7.2641.bloodjournal8772641
   Debili N., 1996, Blood, V88, p98A
   ElKassar N, 1997, BLOOD, V89, P128, DOI 10.1182/blood.V89.1.128.128_128_134
   FIALKOW PJ, 1981, BLOOD, V58, P916
   Fielder PJ, 1996, BLOOD, V87, P2154, DOI 10.1182/blood.V87.6.2154.bloodjournal8762154
   HAN ZC, 1989, EXP HEMATOL, V17, P46
   JUVONEN E, 1993, BRIT J HAEMATOL, V83, P192, DOI 10.1111/j.1365-2141.1993.tb08271.x
   KAUSHANSKY K, 1995, BLOOD, V86, P419, DOI 10.1182/blood.V86.2.419.bloodjournal862419
   KOBAYASHI S, 1993, BRIT J HAEMATOL, V83, P539, DOI 10.1111/j.1365-2141.1993.tb04688.x
   KOMATSU N, 1986, BRIT J HAEMATOL, V64, P241, DOI 10.1111/j.1365-2141.1986.tb04116.x
   Kutti J, 1996, LEUKEMIA LYMPHOMA, V22, P41, DOI 10.3109/10428199609074359
   LI Y, 1994, BRIT J HAEMATOL, V87, P471, DOI 10.1111/j.1365-2141.1994.tb08300.x
   Li Y, 1996, BRIT J HAEMATOL, V92, P60, DOI 10.1046/j.1365-2141.1996.00297.x
   Li Yan, 1995, Blood, V86, p48A
   Lofton-Day C., 1995, Blood, V86, p594A
   METHIA N, 1993, BLOOD, V82, P1395
   MIGNOTTE V, 1994, GENOMICS, V20, P5, DOI 10.1006/geno.1994.1120
   MURPHY S, 1983, CLIN HAEMATOL, V12, P89
   NAKAMURA Y, 1992, SCIENCE, V257, P1138, DOI 10.1126/science.257.5073.1138
   Nand S, 1996, AM J HEMATOL, V52, P42, DOI 10.1002/(SICI)1096-8652(199605)52:1<42::AID-AJH7>3.0.CO;2-6
   PEARSON TC, 1991, BRIT J HAEMATOL, V78, P145, DOI 10.1111/j.1365-2141.1991.tb04408.x
   Pitcher L., 1996, British Journal of Haematology, V93, P168
   SABATH DF, 1996, BLOOD S1, V88, pA93
   SCHIMMENTI LA, 1995, EXP HEMATOL, V23, P1341
   SKODA RC, 1993, EMBO J, V12, P2645, DOI 10.1002/j.1460-2075.1993.tb05925.x
   TSUKAMOTO N, 1994, BRIT J HAEMATOL, V86, P253, DOI 10.1111/j.1365-2141.1994.tb04723.x
   VIGON I, 1993, ONCOGENE, V8, P2607
   VIGON I, 1992, P NATL ACAD SCI USA, V89, P5640, DOI 10.1073/pnas.89.12.5640
   Westwood NB, 1996, LEUKEMIA LYMPHOMA, V22, P95, DOI 10.3109/10428199609074366
NR 30
TC 60
Z9 62
U1 0
U2 3
PU STOCKTON PRESS
PI BASINGSTOKE
PA HOUNDMILLS, BASINGSTOKE, HAMPSHIRE, ENGLAND RG21 6XS
SN 0887-6924
J9 LEUKEMIA
JI Leukemia
PD NOV
PY 1997
VL 11
IS 11
BP 1821
EP 1826
DI 10.1038/sj.leu.2400845
PG 6
WC Oncology; Hematology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Oncology; Hematology
GA YE776
UT WOS:A1997YE77600005
PM 9369413
DA 2025-04-10
ER

PT J
AU Willecke, K
   Eiberger, J
   Degen, J
   Eckardt, D
   Romualdi, A
   Güldenagel, M
   Deutsch, U
   Söhl, G
AF Willecke, K
   Eiberger, J
   Degen, J
   Eckardt, D
   Romualdi, A
   Güldenagel, M
   Deutsch, U
   Söhl, G
TI Structural and functional diversity of connexin genes in the mouse and
   human genome
SO BIOLOGICAL CHEMISTRY
LA English
DT Review
DE alternative splicing; connexin-deficient mice; human connexin genes;
   human connexin mutants; mouse connexin genes
ID GAP-JUNCTION GENE; CARDIAC CONDUCTION ABNORMALITIES; MICE LACKING
   CONNEXIN43; CONNEXIN40-DEFICIENT MICE; MOLECULAR-CLONING; INOSITOL
   1,4,5-TRISPHOSPHATE; CONNEXIN32-DEFICIENT MICE; SENSORINEURAL DEAFNESS;
   INTERCELLULAR CHANNELS; TARGETED DISRUPTION
AB Gap junctions are clustered channels between contacting cells through which direct intercellular communication via diffusion of ions and metabolites can occur. Two hemichannels, each built up of six connexin protein subunits in the plasma membrane of adjacent cells, can dock to each other to form conduits between cells. We have recently screened mouse and human genomic data bases and have found 19 connexin (Cx) genes in the mouse genome and 20 connexin genes in the human genome. One mouse connexin gene and two human connexin genes do not appear to have orthologs in the other genome. With three exceptions, the characterized connexin genes comprise two exons whereby the complete reading frame is located on the second exon. Targeted ablation of eleven mouse connexin genes revealed basic insights into the functional diversity of the connexin gene family. In addition, the phenotypes of human genetic disorders caused by mutated connexin genes further complement our understanding of connexin functions in the human organism. In this review we compare currently identified connexin genes in both the mouse and human genome and discuss the functions of gap junctions deduced from targeted mouse mutants and human genetic disorders.
C1 Univ Bonn, Inst Genet, Abt Mol Genet, D-53117 Bonn, Germany.
   Max Planck Inst Physiol & Clin Res, D-61231 Bad Nauheim, Germany.
   Max Planck Inst G, D-48149 Munster, Germany.
C3 University of Bonn; Max Planck Society; Max Planck Society
RP Univ Bonn, Inst Genet, Abt Mol Genet, D-53117 Bonn, Germany.
OI Deutsch, Urban/0000-0003-4265-6262
CR Baruch A, 2001, J BIOL CHEM, V276, P28999, DOI 10.1074/jbc.M103628200
   BENNETT MVL, 1994, SOC GEN PHY, V49, P223
   BERGOFFEN J, 1993, SCIENCE, V262, P2039, DOI 10.1126/science.8266101
   Bevilacqua LM, 2000, J INTERV CARD ELECTR, V4, P459, DOI 10.1023/A:1009800328836
   BEYER EC, 1987, J CELL BIOL, V105, P2621, DOI 10.1083/jcb.105.6.2621
   BRITZCUNNINGHAM SH, 1995, NEW ENGL J MED, V332, P1323, DOI 10.1056/NEJM199505183322002
   CALABRESE A, 2001, IN PRESS CELL COMMUN
   Chanson M, 1998, J CELL BIOL, V141, P1267, DOI 10.1083/jcb.141.5.1267
   Charollais A, 2000, J CLIN INVEST, V106, P235, DOI 10.1172/JCI9398
   Condorelli DF, 1998, EUR J NEUROSCI, V10, P1202, DOI 10.1046/j.1460-9568.1998.00163.x
   de Wit C, 2000, CIRC RES, V86, P649, DOI 10.1161/01.RES.86.6.649
   Deans MR, 2001, NEURON, V31, P477, DOI 10.1016/S0896-6273(01)00373-7
   Eiberger J, 2001, CELL COMMUN ADHES, V8, P163, DOI 10.3109/15419060109080717
   ELFGANG C, 1995, J CELL BIOL, V129, P805, DOI 10.1083/jcb.129.3.805
   Feigenspan A, 2001, J NEUROSCI, V21, P230, DOI 10.1523/JNEUROSCI.21-01-00230.2001
   FISHMAN GI, 1991, GENOMICS, V10, P250, DOI 10.1016/0888-7543(91)90507-B
   Gabriel HD, 1998, J CELL BIOL, V140, P1453, DOI 10.1083/jcb.140.6.1453
   Gabriel HD, 2001, EUR J BIOCHEM, V268, P1749, DOI 10.1046/j.1432-1327.2001.02040.x
   Gebbia M, 1996, CIRCULATION, V94, P1909, DOI 10.1161/01.CIR.94.8.1909
   Giepmans BNG, 1998, CURR BIOL, V8, P931, DOI 10.1016/S0960-9822(07)00375-2
   Gong XH, 1997, CELL, V91, P833, DOI 10.1016/S0092-8674(00)80471-7
   Grifa A, 1999, NAT GENET, V23, P16, DOI 10.1038/12612
   Groenewegen WA, 1998, CARDIOVASC RES, V38, P463, DOI 10.1016/S0008-6363(97)00325-8
   Güldenagel M, 2001, J NEUROSCI, V21, P6036, DOI 10.1523/JNEUROSCI.21-16-06036.2001
   Güldenagel M, 2000, J COMP NEUROL, V425, P193
   Gutstein DE, 2001, CIRC RES, V88, P333, DOI 10.1161/01.RES.88.3.333
   Hagendorff A, 1999, CIRCULATION, V99, P1508, DOI 10.1161/01.CIR.99.11.1508
   HENNEMANN H, 1992, EUR J CELL BIOL, V57, P51
   HENNEMANN H, 1992, EUR J CELL BIOL, V58, P81
   Hormuzdi SG, 2001, NEURON, V31, P487, DOI 10.1016/S0896-6273(01)00387-7
   Houghton FD, 1999, DEV GENET, V24, P5, DOI 10.1002/(SICI)1520-6408(1999)24:1/2<5::AID-DVG2>3.0.CO;2-F
   Jacob A, 2001, DNA CELL BIOL, V20, P11, DOI 10.1089/10445490150504657
   Juneja SC, 1999, BIOL REPROD, V60, P1263, DOI 10.1095/biolreprod60.5.1263
   Kandel E.R., 1995, Principles of Neural Science
   Kelsell DP, 1997, NATURE, V387, P80, DOI 10.1038/387080a0
   Kiang DT, 1997, GENE, V199, P165, DOI 10.1016/S0378-1119(97)00365-X
   Kidder GM, 2001, FRONT BIOSCI, V6, pD731, DOI 10.2741/Kidder
   Kirchhoff S, 2000, CIRC RES, V87, P399
   Kirchhoff S, 1998, CURR BIOL, V8, P299, DOI 10.1016/S0960-9822(98)70114-9
   KOZAK M, 1989, J CELL BIOL, V108, P229, DOI 10.1083/jcb.108.2.229
   Krüger O, 2000, DEVELOPMENT, V127, P4179
   KRUGER O, 2002, IN PRESS J VASC RES
   Kumar NM, 1996, CELL, V84, P381, DOI 10.1016/S0092-8674(00)81282-9
   Kumar P, 2000, EDN, V45, P127
   Lampe PD, 2000, ARCH BIOCHEM BIOPHYS, V384, P205, DOI 10.1006/abbi.2000.2131
   Lautermann J, 1998, CELL TISSUE RES, V294, P415, DOI 10.1007/s004410051192
   Liao Y, 2001, P NATL ACAD SCI USA, V98, P9989, DOI 10.1073/pnas.171305298
   Liu GP, 2000, INT J SYST SCI, V31, P63, DOI 10.1080/002077200291460
   Lo CW, 1999, TRENDS CARDIOVAS MED, V9, P63, DOI 10.1016/S1050-1738(99)00015-8
   Lo CW, 1996, J BIOENERG BIOMEMBR, V28, P379, DOI 10.1007/BF02110114
   Macari F, 2000, AM J HUM GENET, V67, P1296
   Mackay D, 1999, AM J HUM GENET, V64, P1357, DOI 10.1086/302383
   Maestrini E, 1999, HUM MOL GENET, V8, P1237, DOI 10.1093/hmg/8.7.1237
   MAKOWSKI L, 1977, J CELL BIOL, V74, P629, DOI 10.1083/jcb.74.2.629
   Manthey D, 2001, J MEMBRANE BIOL, V181, P137, DOI 10.1007/s00232-001-0017-1
   Manthey D, 1999, J BIOL CHEM, V274, P14716, DOI 10.1074/jbc.274.21.14716
   Maschhoff KL, 2000, AM J MED GENET, V97, P280, DOI 10.1002/1096-8628(200024)97:4<280::AID-AJMG1278>3.0.CO;2-N
   Meda P, 1996, CLIN EXP PHARMACOL P, V23, P1053, DOI 10.1111/j.1440-1681.1996.tb01168.x
   Nelles E, 1996, P NATL ACAD SCI USA, V93, P9565, DOI 10.1073/pnas.93.18.9565
   NEUHAUS IM, 1995, GENE, V158, P257, DOI 10.1016/0378-1119(94)00899-4
   NIELSEN PA, 2000, MOL BIOL CELL
   Niessen H, 2000, J CELL SCI, V113, P1365
   Niessen H, 2000, FEBS LETT, V466, P112, DOI 10.1016/S0014-5793(99)01770-6
   Pal JD, 1999, AM J PHYSIOL-CELL PH, V276, pC1443, DOI 10.1152/ajpcell.1999.276.6.C1443
   Phelan P, 2001, BIOESSAYS, V23, P388, DOI 10.1002/bies.1057
   Plum A, 2000, CURR BIOL, V10, P1083, DOI 10.1016/S0960-9822(00)00690-4
   Plum A, 2001, DEV BIOL, V231, P334, DOI 10.1006/dbio.2000.0148
   Rabionet R, 2000, HUM MUTAT, V16, P190, DOI 10.1002/1098-1004(200009)16:3<190::AID-HUMU2>3.3.CO;2-9
   REAUME AG, 1995, SCIENCE, V267, P1831, DOI 10.1126/science.7892609
   Richard G, 2000, EXP DERMATOL, V9, P77, DOI 10.1034/j.1600-0625.2000.009002077.x
   Richard G, 1998, HUM GENET, V103, P393, DOI 10.1007/s004390050839
   Rousset B, 1996, ANN ENDOCRINOL-PARIS, V57, P476
   SCHWARZ HJ, 1992, SOMAT CELL MOLEC GEN, V18, P351, DOI 10.1007/BF01235758
   Serre-Beinier V, 2000, DIABETES, V49, P727, DOI 10.2337/diabetes.49.5.727
   Seul KH, 2000, BBA-GENE STRUCT EXPR, V1492, P499, DOI 10.1016/S0167-4781(00)00122-6
   Seul KH, 1997, GENOMICS, V46, P120, DOI 10.1006/geno.1997.5025
   Simon AM, 1997, NATURE, V385, P525, DOI 10.1038/385525a0
   Simon AM, 1998, CURR BIOL, V8, P295, DOI 10.1016/S0960-9822(98)70113-7
   Sohl G, 1996, EUR J CELL BIOL, V69, P267
   Söhl G, 2001, EXP CELL RES, V266, P177, DOI 10.1006/excr.2001.5209
   Söhl G, 2001, BIOL CHEM, V382, P973, DOI 10.1515/BC.2001.122
   Söhl G, 1998, FEBS LETT, V428, P27, DOI 10.1016/S0014-5793(98)00479-7
   Söhl G, 2000, BRAIN RES REV, V32, P138, DOI 10.1016/S0165-0173(99)00074-0
   Splitt MP, 1997, HEART, V77, P369, DOI 10.1136/hrt.77.4.369
   Tamaddon HS, 2000, CIRC RES, V87, P929, DOI 10.1161/01.RES.87.10.929
   Temme A, 2001, PFLUG ARCH EUR J PHY, V442, P961, DOI 10.1007/s004240100623
   Temme A, 2000, J HEPATOL, V32, P627, DOI 10.1016/S0168-8278(00)80225-1
   Teubner B, 2001, J NEUROSCI, V21, P1117
   Theis M, 2001, GENESIS, V29, P1, DOI 10.1002/1526-968X(200101)29:1<1::AID-GENE1000>3.0.CO;2-0
   Toyofuku T, 1998, J BIOL CHEM, V273, P12725, DOI 10.1074/jbc.273.21.12725
   UNWIN PNT, 1980, NATURE, V283, P545, DOI 10.1038/283545a0
   Vaidya D, 2001, CIRC RES, V88, P1196, DOI 10.1161/hh1101.091107
   Valiunas V, 1999, PFLUG ARCH EUR J PHY, V437, P846, DOI 10.1007/s004240050854
   van Rijen HVM, 2001, CIRCULATION, V103, P1591
   Venance L, 2000, P NATL ACAD SCI USA, V97, P10260, DOI 10.1073/pnas.160037097
   Verheule S, 1999, J CARDIOVASC ELECTR, V10, P1380, DOI 10.1111/j.1540-8167.1999.tb00194.x
   Werner R, 2000, IUBMB LIFE, V50, P173, DOI 10.1080/152165400300001480
   White TW, 1998, J CELL BIOL, V143, P815, DOI 10.1083/jcb.143.3.815
   White TW, 1999, ANNU REV PHYSIOL, V61, P283, DOI 10.1146/annurev.physiol.61.1.283
   Ya J, 1998, CIRC RES, V82, P360, DOI 10.1161/01.RES.82.3.360
   Yeager M, 1996, CURR OPIN STRUC BIOL, V6, P183, DOI 10.1016/S0959-440X(96)80073-X
   Yeager M, 1998, CURR OPIN STRUC BIOL, V8, P517, DOI 10.1016/S0959-440X(98)80131-0
   YU W, 1994, P ROY SOC B-BIOL SCI, V255, P125, DOI 10.1098/rspb.1994.0018
NR 103
TC 959
Z9 1123
U1 2
U2 56
PU WALTER DE GRUYTER GMBH
PI BERLIN
PA GENTHINER STRASSE 13, D-10785 BERLIN, GERMANY
SN 1431-6730
EI 1437-4315
J9 BIOL CHEM
JI Biol. Chem.
PD MAY
PY 2002
VL 383
IS 5
BP 725
EP 737
DI 10.1515/BC.2002.076
PG 13
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 565RA
UT WOS:000176382200002
PM 12108537
OA Green Published
DA 2025-04-10
ER

PT J
AU Ohlsson, S
   Lainka, E
   Hünseler, C
   Bergmann, C
   Cirak, S
   Baba, HA
   Hoyer, PF
AF Ohlsson, Sinja
   Lainka, Elke
   Huenseler, Christoph
   Bergmann, Carsten
   Cirak, Sebahattin
   Baba, Hideo A.
   Hoyer, Peter F.
TI CD55 Deficiency With Budd-Chiari Syndrome Treated by Liver
   Transplantation and Eculizumab
SO PEDIATRICS
LA English
DT Article
ID PROTEIN
AB We report the case of a male patient who had a history of early-onset protein-losing enteropathy, chronic diarrhea, and repeated thrombotic events since early childhood. He developed Budd-Chiari syndrome with consequent acute liver failure that required liver transplantation when he was 12 years old. The initial graft failed to function and he required retransplantation. Steroid-resistant rejection complicated the clinical course after the second transplant. Treatment with antithymocyte globulin stabilized graft function but abdominal symptoms and enteral protein loss persisted. The patient remained dependent on intravenous albumin and immunoglobulin. Extended work-up for thrombophilia was unremarkable. Flow cytometry analysis of the peripheral blood cells revealed an unexplained CD55 deficiency. By sequencing of CD55 and, later, exclusion of alternative rare diseases by whole-exome sequencing, we discovered a novel, likely pathogenic homozygous splice-site variant in CD55 c.578 + 5G>A, NM_000574.4, OMIM 125240. The staining of liver and colon biopsies revealed a lack of CD55 protein expression. After initiation of treatment with eculizumab, the patient achieved and has maintained a complete clinical remission throughout 56 months of follow-up. We recommend testing for CD55 deficiency in patients with protein-losing enteropathy. In addition, CD55 deficiency should be considered in the differential diagnosis of patients with Budd-Chiari syndrome in whom an underlying cause is uncertain.
C1 [Ohlsson, Sinja; Lainka, Elke; Hoyer, Peter F.] Univ Duisburg Essen, Univ Childrens Hosp Essen, Dept Pediat 2, Pediat Gastroenterol Hepatol & Liver Transplantat, Essen, Germany.
   [Huenseler, Christoph] Univ Cologne, Fac Med, Dept Pediat, Cologne, Germany.
   [Huenseler, Christoph] Univ Cologne, Univ Hosp Cologne, Cologne, Germany.
   [Bergmann, Carsten] Med Genet Mainz, Mainz, Germany.
   [Cirak, Sebahattin] Univ Ulm, Univ Childrens Hosp Ulm, Sect Social Pediat Ctr & Neuropediat, Ulm, Germany.
   [Baba, Hideo A.] Univ Duisburg Essen, Univ Hosp Essen, Inst Pathol, Essen, Germany.
   [Lainka, Elke] Univ Childrens Hosp, Hufelandstr 55, D-45149 Essen, Germany.
C3 University of Duisburg Essen; University of Cologne; University of
   Cologne; Ulm University; University of Duisburg Essen; University of
   Duisburg Essen
RP Lainka, E (corresponding author), Univ Childrens Hosp, Hufelandstr 55, D-45149 Essen, Germany.
EM elke.lainka@uk-essen.de
FU Cologne Center for Genomics
FX We thank the patient and his family for their support; and Cologne
   Center for Genomics for conducting the whole-exome sequencing.
CR Garcia-Pagán JC, 2023, NEW ENGL J MED, V388, P1307, DOI 10.1056/NEJMra2207738
   Hagin D, 2021, J CLIN IMMUNOL, V41, P477, DOI 10.1007/s10875-020-00910-7
   Houge G, 2022, EUR J HUM GENET, V30, P150, DOI 10.1038/s41431-021-00903-z
   Kurolap A, 2023, HUM GENET, V142, P683, DOI 10.1007/s00439-021-02428-3
   Kurolap A, 2019, J PEDIATR GASTR NUTR, V68, P325, DOI 10.1097/MPG.0000000000002198
   Kurolap A, 2017, NEW ENGL J MED, V377, P87, DOI 10.1056/NEJMc1707173
   Kurolap RNA, 2017, NEW ENGL J MED, V377, P1500
   Liu JN, 2005, J EXP MED, V201, P567, DOI 10.1084/jem.20040863
   Lu H, 2017, NAT GENET, V49, P1025, DOI 10.1038/ng.3871
   LUBLIN DM, 1989, ANNU REV IMMUNOL, V7, P35, DOI 10.1146/annurev.immunol.7.1.35
   Ozen A, 2021, NAT IMMUNOL, V22, P128, DOI 10.1038/s41590-020-00830-z
   Ozen A, 2017, NEW ENGL J MED, V377, P52, DOI 10.1056/NEJMoa1615887
NR 12
TC 1
Z9 1
U1 0
U2 4
PU AMER ACAD PEDIATRICS
PI Itasca
PA 345 Park Boulevard, Itasca, IL, UNITED STATES
SN 0031-4005
EI 1098-4275
J9 PEDIATRICS
JI Pediatrics
PD DEC
PY 2023
VL 152
IS 6
AR e2022059335
DI 10.1542/peds.2022-059335
PG 6
WC Pediatrics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Pediatrics
GA GQ1F8
UT WOS:001154036100042
PM 38018238
DA 2025-04-10
ER

PT J
AU Turunen, TA
   Roberts, TC
   Laitinen, P
   Väänänen, MA
   Korhonen, P
   Maim, T
   Ylä-Herttuala, S
   Turunen, MP
AF Turunen, Tiia A.
   Roberts, Thomas C.
   Laitinen, Pia
   Vaananen, Mari-Anna
   Korhonen, Paula
   Maim, Tarja
   Yla-Herttuala, Seppo
   Turunen, Mikko P.
TI Changes in nuclear and cytoplasmic microRNA distribution in response to
   hypoxic stress
SO SCIENTIFIC REPORTS
LA English
DT Article
ID MIRNA TARGET SITES; TRANSCRIPTIONAL ACTIVATION; RNA INTERFERENCE; MATURE
   MICRORNAS; UP-REGULATION; HUMAN-CELLS; DNA-DAMAGE; EXPRESSION; PROMOTER;
   MIR-210
AB MicroRNAs (miRNAs) are small non-coding RNAs that have well-characterized roles in cytoplasmic gene regulation, where they act by binding to mRNA transcripts and inhibiting their translation (i.e. post-transcriptional gene silencing, PTGS). However, miRNAs have also been implicated in transcriptional gene regulation and alternative splicing, events that are restricted to the cell nucleus. Here we performed nuclear-cytoplasmic fractionation in a mouse endothelial cell line and characterized the localization of miRNAs in response to hypoxia using small RNA sequencing. A highly diverse population of abundant miRNA species was detected in the nucleus, of which the majority (56%) was found to be preferentially localized in one compartment or the other. Induction of hypoxia resulted in changes in miRNA levels in both nuclear and cytoplasmic compartments, with the majority of changes being restricted to one location and not the other. Notably, the classical hypoxamiR (miR-210-3p) was highly up-regulated in the nuclear compartment after hypoxic stimulus. These findings reveal a previously unappreciated level of molecular complexity in the physiological response occurring in ischemic tissue. Furthermore, widespread differential miRNA expression in the nucleus strongly suggests that these small RNAs are likely to perform extensive nuclear regulatory functions in the general case.
C1 [Turunen, Tiia A.; Laitinen, Pia; Vaananen, Mari-Anna; Korhonen, Paula; Maim, Tarja; Yla-Herttuala, Seppo; Turunen, Mikko P.] Univ Eastern Finland, AI Virtanen Inst Mol Sci, Yliopistonranta 1E, Kuopio 70210, Finland.
   [Roberts, Thomas C.] Univ Oxford, Dept Paediat, South Parks Rd, Oxford OX1 3QX, England.
   [Roberts, Thomas C.] Sanford Burnham Prebys Med Discovery Inst, Dev Aging & Regenerat Program, 10901 North Torrey Pines Rd, La Jolla, CA 92037 USA.
   [Yla-Herttuala, Seppo] Kuopio Univ Hosp, Heart Ctr, POB 100, Kuopio 70029, Finland.
   [Yla-Herttuala, Seppo] Kuopio Univ Hosp, Gene Therapy Unit, POB 100, Kuopio 70029, Finland.
C3 University of Eastern Finland; University of Oxford; Sanford Burnham
   Prebys Medical Discovery Institute; Kuopio University Hospital;
   University of Eastern Finland; University of Eastern Finland Hospital;
   Kuopio University Hospital; University of Eastern Finland; University of
   Eastern Finland Hospital
RP Turunen, TA (corresponding author), Univ Eastern Finland, AI Virtanen Inst Mol Sci, Yliopistonranta 1E, Kuopio 70210, Finland.
EM mikko.turunen@uef.fi
RI Roberts, Thomas/AAI-3183-2020; Turunen, Tiia/AAQ-2086-2021; Turunen,
   Mikko/H-5339-2019
OI Malm, Tarja/0000-0002-9530-7472
FU Academy of Finland Center of Excellence [268376]; Finnish Foundation for
   Cardiovascular Research; Instrumentarium Science Foundation; ERC
   advanced grant (CleverGenes); Academy of Finland (AKA) [268376] Funding
   Source: Academy of Finland (AKA)
FX This work was funded by Academy of Finland Center of Excellence and
   project funding #268376, The Finnish Foundation for Cardiovascular
   Research, Instrumentarium Science Foundation and ERC advanced grant
   (CleverGenes).
CR Adilakshmi T, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0039674
   Ahlenstiel CL, 2012, NUCLEIC ACIDS RES, V40, P1579, DOI 10.1093/nar/gkr891
   Alló M, 2009, NAT STRUCT MOL BIOL, V16, P717, DOI 10.1038/nsmb.1620
   Andersen CL, 2004, CANCER RES, V64, P5245, DOI 10.1158/0008-5472.CAN-04-0496
   Benhamed M, 2012, NAT CELL BIOL, V14, P266, DOI 10.1038/ncb2443
   Berezhna SY, 2006, P NATL ACAD SCI USA, V103, P7682, DOI 10.1073/pnas.0600148103
   Bolger AM, 2014, BIOINFORMATICS, V30, P2114, DOI 10.1093/bioinformatics/btu170
   Castanotto D, 2018, P NATL ACAD SCI USA, V115, pE5756, DOI 10.1073/pnas.1721346115
   Castanotto D, 2009, P NATL ACAD SCI USA, V106, P21655, DOI 10.1073/pnas.0912384106
   Chan YC, 2012, MICROCIRCULATION, V19, P215, DOI 10.1111/j.1549-8719.2011.00154.x
   Chi SW, 2009, NATURE, V460, P479, DOI 10.1038/nature08170
   Edgar R, 2002, NUCLEIC ACIDS RES, V30, P207, DOI 10.1093/nar/30.1.207
   Fang Z., 2011, PLOS ONE, V6, P1
   Fasanaro P, 2009, J BIOL CHEM, V284, P35134, DOI 10.1074/jbc.M109.052779
   Filipowicz W, 2005, CURR OPIN STRUC BIOL, V15, P331, DOI 10.1016/j.sbi.2005.05.006
   Francia S, 2012, NATURE, V488, P231, DOI 10.1038/nature11179
   Gagnon KT, 2014, NAT PROTOC, V9, P2045, DOI 10.1038/nprot.2014.135
   Gagnon KT, 2014, CELL REP, V6, P211, DOI 10.1016/j.celrep.2013.12.013
   Giannakakis A, 2008, CANCER BIOL THER, V7, P255, DOI 10.4161/cbt.7.2.5297
   Hausser J, 2013, GENOME RES, V23, P604, DOI 10.1101/gr.139758.112
   Heinz S, 2010, MOL CELL, V38, P576, DOI 10.1016/j.molcel.2010.05.004
   Hutchinson JN, 2007, BMC GENOMICS, V8, DOI 10.1186/1471-2164-8-39
   Hwang HW, 2007, SCIENCE, V315, P97, DOI 10.1126/science.1136235
   Jeffries CD, 2011, RNA, V17, P675, DOI 10.1261/rna.2006511
   Khudayberdiev SA, 2013, FRONT MOL NEUROSCI, V6, DOI 10.3389/fnmol.2013.00043
   Kim DH, 2008, P NATL ACAD SCI USA, V105, P16230, DOI 10.1073/pnas.0808830105
   Kochan-Jamrozy K, 2019, CELL SIGNAL, V54, P150, DOI 10.1016/j.cellsig.2018.11.020
   Kornblihtt AR, 2006, NAT STRUCT MOL BIOL, V13, P5, DOI 10.1038/nsmb0106-5
   Kriegel AJ, 2018, J BIOL CHEM, V293, P14080, DOI 10.1074/jbc.RA117.001705
   Laham-Karam N, 2018, ANTIOXID REDOX SIGN, V29, P813, DOI 10.1089/ars.2017.7248
   Langlois MA, 2005, J BIOL CHEM, V280, P16949, DOI 10.1074/jbc.M501591200
   Langmead B, 2012, NAT METHODS, V9, P357, DOI [10.1038/NMETH.1923, 10.1038/nmeth.1923]
   Leucci E., 2013, SCI REP, V3, P1
   Leung AKL, 2015, TRENDS CELL BIOL, V25, P601, DOI 10.1016/j.tcb.2015.07.005
   Li LC, 2006, P NATL ACAD SCI USA, V103, P17337, DOI 10.1073/pnas.0607015103
   Liao JY, 2010, PLOS ONE, V5, DOI 10.1371/journal.pone.0010563
   Liu J, 2012, NUCLEIC ACIDS RES, V40, P1240, DOI 10.1093/nar/gkr780
   Lopez P, 2016, MOL CELL BIOL, V36, P1480, DOI 10.1128/MCB.01096-15
   LOVE MI, 2014, GENOME BIOL, V15
   Majid S, 2010, CANCER-AM CANCER SOC, V116, P5637, DOI 10.1002/cncr.25488
   Matsui M, 2013, NUCLEIC ACIDS RES, V41, P10086, DOI 10.1093/nar/gkt777
   Nallamshetty S, 2013, FREE RADICAL BIO MED, V64, P20, DOI 10.1016/j.freeradbiomed.2013.05.022
   Park CW, 2010, RNA BIOL, V7, P606, DOI 10.4161/rna.7.5.13215
   Place RF, 2008, P NATL ACAD SCI USA, V105, P1608, DOI 10.1073/pnas.0707594105
   Pulkkinen K, 2008, FEBS LETT, V582, P2397, DOI 10.1016/j.febslet.2008.05.048
   Robb GB, 2005, NAT STRUCT MOL BIOL, V12, P133, DOI 10.1038/nsmb886
   Roberts TC, 2014, APPLIED RNAI: FROM FUNDAMENTAL RESEARCH TO THERAPEUTIC APPLICATIONS, P19
   Roberts TC, 2014, MOL THER-NUCL ACIDS, V3, DOI 10.1038/mtna.2014.40
   Roberts TC, 2013, ESSAYS BIOCHEM, V54, P127, DOI [10.1042/BSE0540127, 10.1042/bse0540127]
   Sarshad AA, 2018, MOL CELL, V71, P1040, DOI 10.1016/j.molcel.2018.07.020
   Shuaib M., 2019, bioRxiv
   Tan YL, 2009, BMC MOL BIOL, V10, DOI 10.1186/1471-2199-10-12
   Tang KF, 2008, J CELL BIOL, V182, P233, DOI 10.1083/jcb.200801169
   Turunen MP, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0089979
   Turunen MP, 2009, CIRC RES, V105, P604, DOI 10.1161/CIRCRESAHA.109.200774
   von Brandenstein Melanie, 2018, Oncotarget, V9, P32855, DOI 10.18632/oncotarget.26023
   Voutila J, 2017, MOL THER, V25, P2705, DOI 10.1016/j.ymthe.2017.07.018
   Wang CH, 2014, FEBS LETT, V588, P4654, DOI 10.1016/j.febslet.2014.10.037
   Wei Y, 2014, J BIOL CHEM, V289, P10270, DOI 10.1074/jbc.C113.541417
   Younger ST, 2009, BIOORG MED CHEM LETT, V19, P3791, DOI 10.1016/j.bmcl.2009.04.032
   Zardo G, 2012, BLOOD, V119, P4034, DOI 10.1182/blood-2011-08-371344
   Zhang XR, 2014, CELL, V158, P607, DOI 10.1016/j.cell.2014.05.047
   Zhang XY, 2019, BMC CANCER, V19, DOI 10.1186/s12885-018-5246-0
NR 63
TC 55
Z9 59
U1 0
U2 9
PU NATURE PORTFOLIO
PI BERLIN
PA HEIDELBERGER PLATZ 3, BERLIN, 14197, GERMANY
SN 2045-2322
J9 SCI REP-UK
JI Sci Rep
PD JUL 17
PY 2019
VL 9
AR 10332
DI 10.1038/s41598-019-46841-1
PG 12
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA IJ3VL
UT WOS:000475832500008
PM 31316122
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Du, M
   Roy, KM
   Zhong, LH
   Shen, Z
   Meyers, HE
   Nichols, RC
AF Du, M
   Roy, KM
   Zhong, LH
   Shen, Z
   Meyers, HE
   Nichols, RC
TI VEGF gene expression is regulated post-transcriptionally in macrophages
SO FEBS JOURNAL
LA English
DT Article
DE VEGF; mRNA stability; 3 ' UTR; AURE; macrophage
ID ENDOTHELIAL-GROWTH-FACTOR; FACTOR MESSENGER-RNA; AU-RICH ELEMENTS;
   RHEUMATOID-ARTHRITIS; FACTOR RECEPTOR-1; ISCHEMIC TISSUES; STRESS
   GRANULES; SYNOVIAL TISSUE; PROTEIN-BINDING; HYPOXIA
AB The macrophage is critical to the innate immune response and contributes to human diseases, including inflammatory arthritis and plaque formation in atherosclerosis. Vascular endothelial growth factor (VEGF) is an angiogenic cytokine that is produced by macrophages. To study the regulation of VEGF production in macrophages we show that stimulation of monocyte-macrophage-like RAW-264.7 cells by lipopolysaccharide (LPS) increases expression of VEGF mRNA and protein. Three alternative splicing VEGF mRNA isoforms are produced, and the stability of VEGF mRNA increases following cellular activation. To study post-transcriptional regulation of the VEGF gene the 3'-untranslated region (3' UTR) was introduced into the 3' UTR of the luciferase gene in a reporter construct. In both RAW-264.7 cells and thioglycollate-elicited macrophages, the 3' UTR sequence dramatically reduces reporter expression. Treatment with activators of macrophages, including LPS, lipoteichoic acid, and VEGF protein, stimulates expression of 3' UTR reporters. Finally, mapping studies of the 3' UTR of VEGF mRNA show that deletion of the heterogeneous nuclear ribonucleoprotein L binding site affects basal reporter expression in RAW-264.7 cells, but does not affect reporter activation with LPS. Together these results demonstrate that a post-transcriptional mechanism contributes to VEGF gene expression in activated macrophage cells.
C1 Vet Adm Res Serv, White River Jct, VT 05009 USA.
   Dartmouth Coll, Hitchcock Med Ctr, Dartmouth Med Sch, Dept Immunol & Microbiol, Hanover, NH 03756 USA.
   Dartmouth Coll, Hitchcock Med Ctr, Dartmouth Med Sch, Dept Med, Hanover, NH 03756 USA.
C3 Dartmouth College; Dartmouth College
RP Vet Adm Res Serv, Mailstop 151,215 N Main St, White River Jct, VT 05009 USA.
EM ralph.c.nichols@dartmouth.edu
FU NCRR NIH HHS [P20RR16437] Funding Source: Medline; NIAMS NIH HHS
   [R03-AR47393] Funding Source: Medline
CR Afuwape AO, 2002, HISTOL HISTOPATHOL, V17, P961, DOI 10.14670/HH-17.961
   AIELLO LP, 1994, NEW ENGL J MED, V331, P1480, DOI 10.1056/NEJM199412013312203
   Bakheet T, 2001, NUCLEIC ACIDS RES, V29, P246, DOI 10.1093/nar/29.1.246
   Boado RJ, 2002, J NEUROCHEM, V80, P552, DOI 10.1046/j.0022-3042.2001.00756.x
   Burke B, 2003, AM J PATHOL, V163, P1233, DOI 10.1016/S0002-9440(10)63483-9
   CHEN CYA, 1995, TRENDS BIOCHEM SCI, V20, P465, DOI 10.1016/S0968-0004(00)89102-1
   Ciais D, 2004, ONCOGENE, V23, P8673, DOI 10.1038/sj.onc.1207939
   Claffey KP, 1998, MOL BIOL CELL, V9, P469, DOI 10.1091/mbc.9.2.469
   Coles LS, 2004, EUR J BIOCHEM, V271, P648, DOI 10.1111/j.1432-1033.2003.03968.x
   De Bandt M, 2003, J IMMUNOL, V171, P4853, DOI 10.4049/jimmunol.171.9.4853
   Dibbens JA, 2001, BBA-GENE STRUCT EXPR, V1518, P57, DOI 10.1016/S0167-4781(01)00167-1
   Ecsedy JA, 1998, J LIPID RES, V39, P2218
   FAVA RA, 1994, J EXP MED, V180, P341, DOI 10.1084/jem.180.1.341
   Ferrara N, 1999, KIDNEY INT, V56, P794, DOI 10.1046/j.1523-1755.1999.00610.x
   Firestein GS, 2003, NATURE, V423, P356, DOI 10.1038/nature01661
   Gerber HP, 2003, J MOL MED, V81, P20, DOI 10.1007/s00109-002-0397-4
   Goldberg-Cohen I, 2002, J BIOL CHEM, V277, P13635, DOI 10.1074/jbc.M108703200
   GOODWIN EC, 1992, J BIOL CHEM, V267, P16330
   Griffin ME, 2004, BIOCHEM BIOPH RES CO, V318, P977, DOI 10.1016/j.bbrc.2004.01.128
   Hiratsuka S, 2002, CANCER CELL, V2, P289, DOI 10.1016/S1535-6108(02)00153-8
   Hiratsuka S, 2001, CANCER RES, V61, P1207
   Iwahashi M, 2004, ARTHRITIS RHEUM-US, V50, P1457, DOI 10.1002/art.20219
   Kedersha N, 2005, J CELL BIOL, V169, P871, DOI 10.1083/jcb.200502088
   Keene JD, 2002, MOL CELL, V9, P1161, DOI 10.1016/S1097-2765(02)00559-2
   Kinne RW, 2000, ARTHRITIS RES, V2, P189, DOI 10.1186/ar86
   Levy AP, 1996, J BIOL CHEM, V271, P25492, DOI 10.1074/jbc.271.41.25492
   LEVY AP, 1995, J BIOL CHEM, V270, P13333, DOI 10.1074/jbc.270.22.13333
   Levy AP, 1996, J BIOL CHEM, V271, P2746, DOI 10.1074/jbc.271.5.2746
   Levy NS, 1997, BBA-GENE STRUCT EXPR, V1352, P167, DOI 10.1016/S0167-4781(97)00052-3
   Levy NS, 1998, J BIOL CHEM, V273, P6417, DOI 10.1074/jbc.273.11.6417
   Luttun A, 2002, NAT MED, V8, P831, DOI 10.1038/nm731
   Mangus DA, 2003, GENOME BIOL, V4, DOI 10.1186/gb-2003-4-7-223
   Matsumoto Y, 2002, J IMMUNOL, V168, P5824, DOI 10.4049/jimmunol.168.11.5824
   Pagès G, 2000, J BIOL CHEM, V275, P26484, DOI 10.1074/jbc.M002104200
   Paleolog EM, 2002, ARTHRITIS RES THER, V4, pS81, DOI 10.1186/ar575
   Philipp W, 2000, INVEST OPHTH VIS SCI, V41, P2514
   Renner W, 2000, J VASC RES, V37, P443, DOI 10.1159/000054076
   Rozen S, 2000, Methods Mol Biol, V132, P365
   Salomonsson L, 2002, EUR J CLIN INVEST, V32, P767, DOI 10.1046/j.1365-2362.2002.01072.x
   Sawano A, 2001, BLOOD, V97, P785, DOI 10.1182/blood.V97.3.785
   Shibata M, 2001, HISTOCHEM CELL BIOL, V116, P471, DOI 10.1007/s00418-001-0336-4
   Shih SC, 1999, J BIOL CHEM, V274, P1359, DOI 10.1074/jbc.274.3.1359
   Shihab FS, 2002, KIDNEY INT, V62, P422, DOI 10.1046/j.1523-1755.2002.00452.x
   Sirenko OI, 1997, MOL CELL BIOL, V17, P3898, DOI 10.1128/MCB.17.7.3898
   Tang KC, 2002, AM J PHYSIOL-HEART C, V283, pH1497, DOI 10.1152/ajpheart.00813.2001
   Thomas MG, 2005, MOL BIOL CELL, V16, P405, DOI 10.1091/mbc.E04-06-0516
   Tourrière H, 2002, BIOCHIMIE, V84, P821, DOI 10.1016/S0300-9084(02)01445-1
   Uthoff SMS, 2002, INT J CANCER, V101, P32, DOI 10.1002/ijc.10552
   Weihrauch D, 1998, AM J PHYSIOL-HEART C, V275, pH969, DOI 10.1152/ajpheart.1998.275.3.H969
   Xiong M, 1998, AM J PATHOL, V153, P587, DOI 10.1016/S0002-9440(10)65601-5
   Xu NH, 1997, MOL CELL BIOL, V17, P4611, DOI 10.1128/MCB.17.8.4611
NR 51
TC 24
Z9 29
U1 1
U2 11
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 1742-464X
EI 1742-4658
J9 FEBS J
JI FEBS J.
PD FEB
PY 2006
VL 273
IS 4
BP 732
EP 745
DI 10.1111/j.1742-4658.2006.05106.x
PG 14
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 007MU
UT WOS:000234974600006
PM 16441660
OA Bronze
DA 2025-04-10
ER

PT J
AU Chang, JY
   Monroe, DM
   Oliver, JA
   Roberts, HR
AF Chang, JY
   Monroe, DM
   Oliver, JA
   Roberts, HR
TI TFPIβ, a second product from the mouse tissue factor pathway inhibitor
   (TFPI) gene
SO THROMBOSIS AND HAEMOSTASIS
LA English
DT Article
ID CORONARY HEART-DISEASE; 3RD KUNITZ DOMAIN; COAGULATION INHIBITOR;
   FACTOR-XA; DENSITY LIPOPROTEIN; HEPARIN; EXPRESSION; SEQUENCE; SITE;
   PURIFICATION
AB Tissue factor pathway inhibitor (TFPI) contains three Kunitz domains separated by two connecting regions. We have cloned another naturally occurring TFPI gene product from a mouse lung cDNA library which we have called TFPI beta. TFPI beta is derived from alternative splicing of the TFPI gene. Analysis of the cDNA shows that mouse TFPI beta protein is identical to TFPI from the N'-terminus through the second connecting region. However, mouse TFPI beta possesses neither a third Kunitz domain nor an Arg, Lys-rich C'-terminus but instead has a completely different C'-terminal (beta-domain) sequence which is not homologous to any known protein. Northern blot analyses show that the tissues for mouse TFPI beta synthesis are heart and lung; in contrast, TFPI appears in Northern blots of heart and spleen. Both TFPI beta and TFPI messages first appear in 7-day-old mouse embryos, but only the TFPI mRNA persists until 17 days. Purified recombinant TFPI beta shows an apparent molecular weight of 38 kDa. Kinetic studies indicate that mouse TFPI beta is a slow-binding enzyme inhibitor for human factor Xa. in addition, heparin does not enhance the inhibition of factor Xa by mouse TFPI beta although it does accelerate factor Xa inhibition by TFPI.
C1 Univ N Carolina, Ctr Thrombosis & Hemostasis, Chapel Hill, NC 27599 USA.
C3 University of North Carolina; University of North Carolina Chapel Hill
RP Chang, JY (corresponding author), Univ N Carolina, Ctr Thrombosis & Hemostasis, 932 Mary Ellen Jones Bldg,CB 7035, Chapel Hill, NC 27599 USA.
OI Monroe, Dougald/0000-0002-0493-2943
FU NHLBI NIH HHS [HL-06350] Funding Source: Medline
CR ABUMIYA T, 1995, J BIOCHEM-TOKYO, V118, P178, DOI 10.1093/oxfordjournals.jbchem.a124874
   AUSTIN MA, 1988, JAMA-J AM MED ASSOC, V260, P1917
   BAJAJ MS, 1990, P NATL ACAD SCI USA, V87, P8869, DOI 10.1073/pnas.87.22.8869
   Chang JY, 1998, THROMB HAEMOSTASIS, V79, P306
   ENGELMAN DM, 1986, ANNU REV BIOPHYS BIO, V15, P321, DOI 10.1146/annurev.bb.15.060186.001541
   ENJYOJI K, 1992, J BIOCHEM-TOKYO, V111, P681, DOI 10.1093/oxfordjournals.jbchem.a123818
   ENJYOJI K, 1995, BIOCHEMISTRY-US, V34, P5725, DOI 10.1021/bi00017a004
   GIRARD TJ, 1989, THROMB RES, V55, P37, DOI 10.1016/0049-3848(89)90454-4
   GIRARD TJ, 1989, NATURE, V338, P518, DOI 10.1038/338518a0
   GIRARD TJ, 1994, BIOCHEM J, V303, P923, DOI 10.1042/bj3030923
   GORDON T, 1977, AM J MED, V62, P707, DOI 10.1016/0002-9343(77)90874-9
   HUANG ZF, 1993, J BIOL CHEM, V268, P26950
   Huang ZF, 1997, BLOOD, V90, P944, DOI 10.1182/blood.V90.3.944.944_944_951
   Hynes R. O, 1990, FIBRONECTINS
   KAMEI S, 1994, J BIOCHEM-TOKYO, V115, P708, DOI 10.1093/oxfordjournals.jbchem.a124400
   Kaufman M., 1995, The Atlas of Mouse Development
   KOWAKA T, 1995, ARTERIOSCL THROM VAS, V15, P504
   LEFF SE, 1986, ANNU REV BIOCHEM, V55, P1091, DOI 10.1146/annurev.biochem.55.1.1091
   MANIATIS T, 1991, SCIENCE, V251, P33, DOI 10.1126/science.1824726
   NOVOTNY WF, 1991, BLOOD, V78, P394
   NOVOTNY WF, 1988, BLOOD, V72, P2020
   NOVOTNY WF, 1989, J BIOL CHEM, V264, P18832
   Rio Donald C., 1992, Gene Expression, V2, P1
   SANDSET PM, 1988, THROMB RES, V50, P803, DOI 10.1016/0049-3848(88)90340-4
   SANGER F, 1977, P NATL ACAD SCI USA, V74, P5463, DOI 10.1073/pnas.74.12.5463
   SCANU AM, 1991, CLIN CARDIOL, V14, P35, DOI 10.1002/clc.4960141306
   SHARP PA, 1994, CELL, V77, P805, DOI 10.1016/0092-8674(94)90130-9
   VALENTIN S, 1993, BLOOD COAGUL FIBRIN, V4, P713, DOI 10.1097/00001721-199304050-00007
   WESSELSCHMIDT R, 1992, BLOOD, V79, P2004
   WESSELSCHMIDT R, 1993, BLOOD COAGUL FIBRIN, V4, P661, DOI 10.1097/00001721-199304050-00001
   WESSELSCHMIDT RL, 1990, NUCLEIC ACIDS RES, V18, P6440, DOI 10.1093/nar/18.21.6440
   WUN TC, 1988, J BIOL CHEM, V263, P6001
NR 32
TC 55
Z9 58
U1 0
U2 0
PU F K SCHATTAUER VERLAG GMBH
PI STUTTGART
PA P O BOX 10 45 43, LENZHALDE 3, D-70040 STUTTGART, GERMANY
SN 0340-6245
J9 THROMB HAEMOSTASIS
JI Thromb. Haemost.
PD JAN
PY 1999
VL 81
IS 1
BP 45
EP 49
PG 5
WC Hematology; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Hematology; Cardiovascular System & Cardiology
GA 158LK
UT WOS:000078116800010
PM 9974373
DA 2025-04-10
ER

PT J
AU Pieters, M
   Wolberg, AS
AF Pieters, Marlien
   Wolberg, Alisa S.
TI Fibrinogen and fibrin: An illustrated review
SO RESEARCH AND PRACTICE IN THROMBOSIS AND HAEMOSTASIS
LA English
DT Review
DE factor XIII; fibrin; fibrinogen; fibrinolysis; hemostasis; infection;
   thrombosis
ID CROSS-LINKING; GAMMA-CHAIN; CLOT PROPERTIES; PLASMINOGEN-ACTIVATOR;
   THROMBIN GENERATION; FACTOR-XIII; PLASMA; ALPHA; LYSIS; MICE
AB Since its discovery over 350 years ago, studies of fibrinogen have revealed remarkable characteristics. Its complex structure as a large (340 kDa) hexameric homodimer supports complex roles in hemostasis and homeostasis. Fibrinogen synthesis is regulated at the transcriptional and translational levels, undergoing both constitutive (basal) secretion from liver, and inducible upregulation in response to inflammatory events. In addition, alternative splicing yields fibrinogen variants with unique properties and contributions to coagulation biochemistry. During coagulation, fibrinogen conversion to fibrin occurs via thrombin-mediated proteolytic cleavage that produces intermediate protofibrils and then mature fibers that provide remarkable biochemical and mechanical stability to clots. Fibrin formation, structure, and stability are regulated by various genetic, biochemical, and environmental factors, allowing for dynamic kinetics of fibrin formation and structure. Interactions between fibrinogen and/or fibrin and plasma proteins and receptors on platelets, leukocytes, endothelial cells, and other cells enable complex functions in hemostasis, thrombosis, pregnancy, inflammation, infection, cancer, and other pathologies. Disorders in fibrinogen concentration and/or function increase risk of bleeding, thrombosis, and infection. This illustrated review covers fundamental aspects of fibrinogen and fibrin biology, biochemistry, biophysics, epidemiology, and clinical applications. Continued efforts to enhance our understanding of fibrinogen and fibrin in these processes are likely to advance treatment and prevention of many human diseases.
C1 [Pieters, Marlien] North West Univ, Ctr Excellence Nutr, Potchefstroom, South Africa.
   [Wolberg, Alisa S.] Univ N Carolina, Dept Pathol & Lab Med, Chapel Hill, NC 27515 USA.
C3 North West University - South Africa; University of North Carolina;
   University of North Carolina Chapel Hill
RP Wolberg, AS (corresponding author), Univ N Carolina, Dept Pathol & Lab Med, Chapel Hill, NC 27515 USA.
EM alisa_wolberg@med.unc.edu
RI Pieters, Marlien/AAI-1711-2020; Wolberg, Alisa/LEN-3884-2024
OI Wolberg, Alisa/0000-0002-2845-2303; Pieters, Marlien/0000-0003-2849-6370
FU South African Medical Research Council; Academy of Medical Sciences UK
   (Newton Fund Advanced Fellowship Grant); National Institutes of Health
   [R01HL126974]
FX M. Pieters is supported by funding from the South African Medical
   Research Council and the Academy of Medical Sciences UK (Newton Fund
   Advanced Fellowship Grant). A.S. Wolberg is supported by funding from
   the National Institutes of Health (R01HL126974)
CR Aleman MM, 2014, J CLIN INVEST, V124, P3590, DOI 10.1172/JCI75386
   Allan P, 2012, J THROMB HAEMOST, V10, P1072, DOI 10.1111/j.1538-7836.2012.04717.x
   Alshehri OM, 2015, BLOOD, V126, P1601, DOI 10.1182/blood-2015-04-641654
   ALTIERI DC, 1990, J BIOL CHEM, V265, P12119
   Ariëns RAS, 2013, J THROMB HAEMOST, V11, P294, DOI 10.1111/jth.12229
   Bannish BE, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-06383-w
   Bannish BE, 2014, MATH MED BIOL, V31, P17, DOI 10.1093/imammb/dqs029
   BLINC A, 1991, THROMB HAEMOSTASIS, V65, P549
   Bridge KI, 2014, THROMB HAEMOSTASIS, V112, P901, DOI 10.1160/TH14-02-0184
   Bucay I, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0116350
   Byrnes JR, 2015, BLOOD, V126, P1940, DOI 10.1182/blood-2015-06-652263
   Casini A, 2018, J THROMB HAEMOST, V16, P1887, DOI 10.1111/jth.14216
   Celinska-Löwenhoff M, 2018, RHEUMATOLOGY, V57, P1340, DOI 10.1093/rheumatology/key089
   Cho JH, 2006, BLOOD, V107, P3555, DOI 10.1182/blood-2005-10-4168
   CHUNG DW, 1984, BIOCHEMISTRY-US, V23, P4232, DOI 10.1021/bi00313a033
   Cieslik J, 2018, BLOOD, V131, P797, DOI 10.1182/blood-2017-07-798306
   Collet JP, 2005, BLOOD, V106, P3824, DOI 10.1182/blood-2005-05-2150
   Collet JP, 2000, ARTERIOSCL THROM VAS, V20, P1354, DOI 10.1161/01.ATV.20.5.1354
   Cronjé HT, 2017, MATRIX BIOL, V60-61, P16, DOI 10.1016/j.matbio.2016.10.005
   de Bosch NB, 2002, THROMB HAEMOSTASIS, V88, P253
   de Willige SU, 2009, BLOOD, V114, P3994, DOI 10.1182/blood-2009-05-217968
   Domingues MM, 2016, BLOOD, V127, P487, DOI 10.1182/blood-2015-06-652214
   Duval C, 2014, THROMB HAEMOSTASIS, V111, P842, DOI 10.1160/TH13-10-0855
   Fish RJ, 2014, BLOOD, V123, P2278, DOI 10.1182/blood-2013-12-547182
   Fish RJ, 2012, THROMB HAEMOSTASIS, V108, P419, DOI 10.1160/TH12-04-0273
   Flick MJ, 2004, J CLIN INVEST, V113, P1596, DOI 10.1172/JCI200420741
   Folsom AR, 2016, THROMB RES, V139, P44, DOI 10.1016/j.thromres.2016.01.008
   FORRESTER JM, 1995, MED HIST, V39, P477, DOI 10.1017/S0025727300060385
   Gulledge AA, 2003, ARTERIOSCL THROM VAS, V23, P130, DOI 10.1161/01.ATV.0000041037.06509.C2
   Helms CC, 2012, BIOPHYS J, V102, P168, DOI 10.1016/j.bpj.2011.11.4016
   Hoffman M., 2008, Cardiovascular & Hematological Agents in Medicinal Chemistry, V6, P206, DOI 10.2174/187152508784871981
   Holmback K, 1996, EMBO J, V15, P5760, DOI 10.1002/j.1460-2075.1996.tb00962.x
   Houser JR, 2010, BIOPHYS J, V99, P3038, DOI 10.1016/j.bpj.2010.08.060
   Hudson NE, 2017, BIOMED RES INT, V2017, DOI 10.1155/2017/2748340
   Jaimes CE, 2018, J THROMB HAEMOST, V16, P2070, DOI 10.1111/jth.14248
   Kollman JM, 2009, BIOCHEMISTRY-US, V48, P3877, DOI 10.1021/bi802205g
   Kotzé RCM, 2014, THROMB RES, V134, P963, DOI 10.1016/j.thromres.2014.08.018
   KUNITADA S, 1992, BLOOD, V79, P1420
   Li W, 2017, BIOMED RES INT, V2017, DOI 10.1155/2017/6385628
   Li W, 2017, ACTA BIOMATER, V60, P264, DOI 10.1016/j.actbio.2017.07.037
   Liu W, 2006, SCIENCE, V313, P634, DOI 10.1126/science.1127317
   Longstaff C, 2011, BLOOD, V117, P661, DOI 10.1182/blood-2010-06-290338
   Macrae FL, 2018, J CLIN INVEST, V128, P3356, DOI 10.1172/JCI98734
   Macrae FL, 2016, SEMIN THROMB HEMOST, V42, P344, DOI 10.1055/s-0036-1572353
   Medved L, 2003, THROMB HAEMOSTASIS, V89, P409
   MOSESSON MW, 1972, J BIOL CHEM, V247, P5223
   O'Brien ET, 2008, P NATL ACAD SCI USA, V105, P19438, DOI 10.1073/pnas.0804865105
   OTOOLE TE, 1990, CELL REGUL, V1, P883, DOI 10.1091/mbc.1.12.883
   Prasad JM, 2015, BLOOD, V126, P2047, DOI 10.1182/blood-2015-04-639849
   Redman CM, 2001, ANN NY ACAD SCI, V936, P480
   Rijken DC, 2016, J THROMB HAEMOST, V14, P1453, DOI 10.1111/jth.13354
   SAKATA Y, 1980, J CLIN INVEST, V65, P290, DOI 10.1172/JCI109671
   SAKHAROV DV, 1995, CIRCULATION, V92, P1883, DOI 10.1161/01.CIR.92.7.1883
   Scott EM, 2004, ARTERIOSCL THROM VAS, V24, P1558, DOI 10.1161/01.ATV.0000136649.83297.bf
   Smith N, 2018, RES PRACT THROMB HAE, V2, P800, DOI 10.1002/rth2.12127
   Solomon C, 2015, THROMB HAEMOSTASIS, V113, P759, DOI 10.1160/TH14-06-0514
   Standeven KF, 2007, BLOOD, V110, P902, DOI 10.1182/blood-2007-01-066837
   Standeven KF, 2009, SEMIN THROMB HEMOST, V35, P458, DOI 10.1055/s-0029-1234141
   SUH TT, 1995, GENE DEV, V9, P2020, DOI 10.1101/gad.9.16.2020
   Sumaya W, 2018, EUR HEART J, V39, P1078, DOI 10.1093/eurheartj/ehy013
   TREZZINI C, 1988, BIOCHEM BIOPH RES CO, V156, P477, DOI 10.1016/S0006-291X(88)80866-0
   Undas A, 2011, ARTERIOSCL THROM VAS, V31, pE88, DOI 10.1161/ATVBAHA.111.230631
   Valnickova Z, 1998, J BIOL CHEM, V273, P27220, DOI 10.1074/jbc.273.42.27220
   Veklich Y, 1998, BLOOD, V92, P4721, DOI 10.1182/blood.V92.12.4721.424k13_4721_4729
   Vo AH, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0074682
   Weisel JW, 2007, J THROMB HAEMOST, V5, P116, DOI 10.1111/j.1538-7836.2007.02504.x
   Weisel J. W., 2008, Cardiovascular & Hematological Agents in Medicinal Chemistry, V6, P161, DOI 10.2174/187152508784871963
   Weisel JW, 2013, BLOOD, V121, P1712, DOI 10.1182/blood-2012-09-306639
   Wolberg AS, 2007, BLOOD REV, V21, P131, DOI 10.1016/j.blre.2006.11.001
NR 69
TC 173
Z9 189
U1 6
U2 98
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
EI 2475-0379
J9 RES PRACT THROMB HAE
JI Res. Pract. Thromb. Haemost.
PD APR
PY 2019
VL 3
IS 2
BP 161
EP 172
DI 10.1002/rth2.12191
PG 12
WC Hematology; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Hematology; Cardiovascular System & Cardiology
GA HT6EQ
UT WOS:000464657400007
PM 31011700
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Ottolia, M
   John, S
   Hazan, A
   Goldhaber, JI
AF Ottolia, Michela
   John, Scott
   Hazan, Adina
   Goldhaber, Joshua I.
TI The Cardiac Na<SUP>+</SUP>-Ca<SUP>2+</SUP> Exchanger: From Structure to
   Function
SO COMPREHENSIVE PHYSIOLOGY
LA English
DT Article
ID SODIUM-CALCIUM EXCHANGER; NA+/K+-ATPASE ALPHA(2)-ISOFORM;
   TISSUE-SPECIFIC EXPRESSION; CA2+ BINDING DOMAINS; AMINO-ACID-RESIDUES;
   NA+/CA2+ EXCHANGER; NA/CA EXCHANGE; STEADY-STATE; GUINEA-PIG; MOLECULAR
   DETERMINANTS
AB Ca2+ homeostasis is essential for cell function and survival. As such, the cytosolic Ca2+ concentration is tightly controlled by a wide number of specialized Ca2+ handling proteins. One among them is the Na+-Ca2+ exchanger (NCX), a ubiquitous plasma membrane transporter that exploits the electrochemical gradient of Na+ to drive Ca2+ out of the cell, against its concentration gradient. In this critical role, this secondary transporter guides vital physiological processes such as Ca2+ homeostasis, muscle contraction, bone formation, and memory to name a few.
   Herein, we review the progress made in recent years about the structure of the mammalian NCX and how it relates to function. Particular emphasis will be given to the mammalian cardiac isoform, NCX1.1, due to the extensive studies conducted on this protein. Given the degree of conservation among the eukaryotic exchangers, the information highlighted herein will provide a foundation for our understanding of this transporter family. We will discuss gene structure, alternative splicing, topology, regulatory mechanisms, and NCX's functional role on cardiac physiology. Throughout this article, we will attempt to highlight important milestones in the field and controversial topics where future studies are required. (C) 2022 American Physiological Society.
C1 [Ottolia, Michela] Univ Calif Los Angeles, David Geffen Sch Med, Div Mol Med, Dept Anesthesiol & Perioperat Med, Los Angeles, CA 90095 USA.
   [John, Scott] Univ Calif Los Angeles, Dept Med Cardiol, Los Angeles, CA USA.
   [Hazan, Adina; Goldhaber, Joshua I.] Cedars Sinai Med Ctr, Smidt Heart Inst, Los Angeles, CA 90048 USA.
C3 University of California System; University of California Los Angeles;
   University of California Los Angeles Medical Center; David Geffen School
   of Medicine at UCLA; University of California System; University of
   California Los Angeles; Cedars Sinai Medical Center
RP Ottolia, M (corresponding author), Univ Calif Los Angeles, David Geffen Sch Med, Div Mol Med, Dept Anesthesiol & Perioperat Med, Los Angeles, CA 90095 USA.
EM mottolia@ucla.edu
FU NIH/NHLBI [R01 HL130308, R01 HL152296]; MPI [R01 HL147569]; National
   Heart Lung and Blood Institute [R01HL152296] Funding Source: NIH
   RePORTER
FX This work was supported by the following NIH/NHLBI grants: R01 HL130308
   (M. Ottolia), R01 HL152296 (M. Ottolia) and MPI R01 HL147569 (J. I.
   Goldhaber/M. Ottolia).
CR AdachiAkahane S, 1997, J GEN PHYSIOL, V109, P717, DOI 10.1085/jgp.109.6.717
   Ander BP, 2007, CARDIOVASC RES, V73, P395, DOI 10.1016/j.cardiores.2006.09.013
   Armoundas AA, 2003, CIRC RES, V93, P46, DOI 10.1161/01.RES.0000080932.98903.D8
   Artman Michael, 1995, American Journal of Physiology, V268, pH1714
   Artman Michael, 1992, American Journal of Physiology, V263, pH1506
   Asteggiano C, 2001, EUR J BIOCHEM, V268, P437
   BAKER PF, 1968, BIOCHIM BIOPHYS ACTA, V150, P167, DOI 10.1016/0005-2736(68)90023-0
   BAKER PF, 1969, J PHYSIOL-LONDON, V200, P431, DOI 10.1113/jphysiol.1969.sp008702
   Bano D, 2005, CELL, V120, P275, DOI 10.1016/j.cell.2004.11.049
   Barnes KV, 1997, J BIOL CHEM, V272, P11510, DOI 10.1074/jbc.272.17.11550
   Bartholomaeus I, 2008, J BIOL CHEM, V283, P10978, DOI 10.1074/jbc.M800622200
   Baruscotti M, 2011, P NATL ACAD SCI USA, V108, P1705, DOI 10.1073/pnas.1010122108
   BASSANI RA, 1992, J PHYSIOL-LONDON, V453, P591, DOI 10.1113/jphysiol.1992.sp019246
   Beaugé L, 2002, ANN NY ACAD SCI, V976, P288
   Bers DM, 2002, NATURE, V415, P198, DOI 10.1038/415198a
   Besserer GM, 2007, P NATL ACAD SCI USA, V104, P18467, DOI 10.1073/pnas.0707417104
   Blaustein MP, 1999, PHYSIOL REV, V79, P763, DOI 10.1152/physrev.1999.79.3.763
   Bögeholz N, 2016, J MOL CELL CARDIOL, V101, P106, DOI 10.1016/j.yjmcc.2016.11.004
   Bögeholz N, 2015, CIRC-ARRHYTHMIA ELEC, V8, P1210, DOI 10.1161/CIRCEP.115.002927
   BOERTH SR, 1994, CIRC RES, V74, P354, DOI 10.1161/01.RES.74.2.354
   BOUNTRA C, 1989, J PHYSIOL-LONDON, V418, P163, DOI 10.1113/jphysiol.1989.sp017833
   Boyman L, 2011, J BIOL CHEM, V286, P28811, DOI 10.1074/jbc.M110.214106
   Boyman L, 2009, J BIOL CHEM, V284, P6185, DOI 10.1074/jbc.M809012200
   Brette F, 2006, BIOCHEM BIOPH RES CO, V348, P1163, DOI 10.1016/j.bbrc.2006.07.189
   Breukels V, 2010, PROTEINS, V78, P1813, DOI 10.1002/prot.22695
   BRIDGE JHB, 1990, SCIENCE, V248, P376, DOI 10.1126/science.2158147
   Bucchi A, 2012, FRONT PHYSIOL, V3, DOI 10.3389/fphys.2012.00240
   Bukowska A, 2012, CARDIOVASC THER, V30, pe115, DOI 10.1111/j.1755-5922.2010.00245.x
   Chaptal Vincent, 2007, Channels (Austin), V1, P397
   Cheng GM, 1999, J BIOL CHEM, V274, P12819, DOI 10.1074/jbc.274.18.12819
   Cheung JY, 2007, ANN NY ACAD SCI, V1099, P119, DOI 10.1196/annals.1387.004
   Cho CH, 2000, MOL CELLS, V10, P712
   Chou AC, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0138856
   Cingolani E, 2018, NAT REV CARDIOL, V15, P139, DOI 10.1038/nrcardio.2017.165
   Cook O, 1998, BBA-BIOMEMBRANES, V1371, P40, DOI 10.1016/S0005-2736(97)00272-1
   Cross HR, 1998, CIRC RES, V83, P1215, DOI 10.1161/01.RES.83.12.1215
   Cunha SR, 2007, J BIOL CHEM, V282, P4875, DOI 10.1074/jbc.M607096200
   Dan P, 2007, BIOPHYS J, V93, P2504, DOI 10.1529/biophysj.107.104943
   Despa S, 2003, BIOPHYS J, V85, P3388, DOI 10.1016/S0006-3495(03)74758-4
   Despa S, 2002, CIRCULATION, V105, P2543, DOI 10.1161/01.CIR.0000016701.85760.97
   Despa S, 2012, CARDIOVASC RES, V95, P480, DOI 10.1093/cvr/cvs213
   DIPOLO R, 1979, J GEN PHYSIOL, V73, P91, DOI 10.1085/jgp.73.1.91
   DiPolo R, 2008, PFLUG ARCH EUR J PHY, V456, P623, DOI 10.1007/s00424-007-0430-0
   Dixon RE, 2012, P NATL ACAD SCI USA, V109, P1749, DOI 10.1073/pnas.1116731109
   Doering AE, 1998, J BIOL CHEM, V273, P778, DOI 10.1074/jbc.273.2.778
   DOERING AE, 1993, J PHYSIOL-LONDON, V466, P481
   DOERING AE, 1994, J PHYSIOL-LONDON, V480, P9, DOI 10.1113/jphysiol.1994.sp020336
   Doleschal B, 2015, CARDIOVASC RES, V106, P163, DOI 10.1093/cvr/cvv022
   Dunn J, 2002, J BIOL CHEM, V277, P33957, DOI 10.1074/jbc.M206677200
   DURKIN JT, 1991, ARCH BIOCHEM BIOPHYS, V290, P369, DOI 10.1016/0003-9861(91)90553-U
   Dyck C, 1999, J GEN PHYSIOL, V114, P701, DOI 10.1085/jgp.114.5.701
   Dyck C, 1998, J BIOL CHEM, V273, P12981, DOI 10.1074/jbc.273.21.12981
   Eder P, 2007, CARDIOVASC RES, V73, P111, DOI 10.1016/j.cardiores.2006.10.016
   Eder P, 2005, PFLUG ARCH EUR J PHY, V451, P99, DOI 10.1007/s00424-005-1434-2
   Eisner DA, 2017, CIRC RES, V121, P181, DOI 10.1161/CIRCRESAHA.117.310230
   Faham S, 2008, SCIENCE, V321, P810, DOI 10.1126/science.1160406
   Farhan H, 2006, HANDB EXP PHARM, V175, P233
   FRANK JS, 1992, J CELL BIOL, V117, P337, DOI 10.1083/jcb.117.2.337
   Fuller W, 2016, CHANNELS, V10, P75, DOI 10.1080/19336950.2015.1099329
   FURMAN I, 1995, J BIOL CHEM, V270, P19120, DOI 10.1074/jbc.270.32.19120
   Fuster D, 2008, J GEN PHYSIOL, V132, P465, DOI 10.1085/jgp.200810016
   Gabellini N, 2002, ANN NY ACAD SCI, V976, P282
   Gabellini N, 2002, GENE, V298, P1, DOI 10.1016/S0378-1119(02)00982-4
   Gabellini N, 2003, J NEUROCHEM, V84, P282, DOI 10.1046/j.1471-4159.2003.01511.x
   Gao Z, 2013, CIRC RES, V112, P309, DOI 10.1161/CIRCRESAHA.111.300193
   Garciarena CD, 2013, J MOL CELL CARDIOL, V61, P51, DOI 10.1016/j.yjmcc.2013.04.008
   Gershome C, 2011, AM J PHYSIOL-HEART C, V300, pH300, DOI 10.1152/ajpheart.00798.2010
   Giladi M, 2017, J BIOL CHEM, V292, P12311, DOI 10.1074/jbc.M117.787168
   Giladi M, 2016, INT J MOL SCI, V17, DOI 10.3390/ijms17111949
   Giladi M, 2016, FRONT PHYSIOL, V7, DOI [10.3359/fphys.7016.00030, 10.3389/fphys.2016.00030]
   Giladi M, 2013, J BIOL CHEM, V288, P23141, DOI 10.1074/jbc.M113.471698
   Giladi M, 2013, ADV EXP MED BIOL, V961, P35, DOI 10.1007/978-1-4614-4756-6_4
   Giladi M, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0039985
   Giladi M, 2012, CELL CALCIUM, V51, P478, DOI 10.1016/j.ceca.2012.04.007
   Giladi M, 2010, J BIOL CHEM, V285, P28117, DOI 10.1074/jbc.M110.127001
   Ginsburg KS, 2013, J PHYSIOL-LONDON, V591, P2067, DOI 10.1113/jphysiol.2013.252080
   Ginsburg KS, 2005, J MOL CELL CARDIOL, V39, P972, DOI 10.1016/j.yjmcc.2005.09.005
   Goel M, 2007, AM J PHYSIOL-HEART C, V292, pH874, DOI 10.1152/ajpheart.00785.2006
   Gök C, 2020, CELL REP, V31, DOI 10.1016/j.celrep.2020.107697
   Goldhaber JI, 2013, ADV EXP MED BIOL, V961, P355, DOI 10.1007/978-1-4614-4756-6_30
   Groenke S, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0081633
   Haddock PS, 1999, CIRC RES, V85, P415, DOI 10.1161/01.RES.85.5.415
   Hafver TL, 2016, J BIOL CHEM, V291, P4561, DOI 10.1074/jbc.M115.677898
   Hale CC, 1997, BIOCHEM BIOPH RES CO, V236, P113, DOI 10.1006/bbrc.1997.6912
   Hampton TG, 2000, AM J PHYSIOL-HEART C, V279, pH2846, DOI 10.1152/ajpheart.2000.279.6.H2846
   He Z, 1997, J MEMBRANE BIOL, V156, P149, DOI 10.1007/s002329900197
   He ZP, 2000, AM J PHYSIOL-CELL PH, V278, pC661, DOI 10.1152/ajpcell.2000.278.4.C661
   He ZP, 1998, J GEN PHYSIOL, V111, P857, DOI 10.1085/jgp.111.6.857
   Henderson SA, 2004, CIRC RES, V95, P604, DOI 10.1161/01.RES.0000142316.08250.68
   Herrmann S, 2013, CARDIOVASC RES, V99, P780, DOI 10.1093/cvr/cvt154
   Herz K, 2009, J BIOL CHEM, V284, P6337, DOI 10.1074/jbc.M807720200
   Hilge M, 2006, MOL CELL, V22, P15, DOI 10.1016/j.molcel.2006.03.008
   Hilge M, 2007, ANN NY ACAD SCI, V1099, P7, DOI 10.1196/annals.1387.030
   Hilge M, 2012, J BIOL CHEM, V287, P31641, DOI 10.1074/jbc.R112.353573
   Hilge M, 2009, P NATL ACAD SCI USA, V106, P14333, DOI 10.1073/pnas.0902171106
   Hilgemann DW, 1996, SCIENCE, V273, P956, DOI 10.1126/science.273.5277.956
   Hilgemann DW, 1996, BIOPHYS J, V71, P759, DOI 10.1016/S0006-3495(96)79275-5
   Hilgemann DW, 1998, METHOD ENZYMOL, V293, P267
   HILGEMANN DW, 1992, J GEN PHYSIOL, V100, P905, DOI 10.1085/jgp.100.6.905
   HILGEMANN DW, 1990, NATURE, V344, P242, DOI 10.1038/344242a0
   HILGEMANN DW, 1992, J GEN PHYSIOL, V100, P933, DOI 10.1085/jgp.100.6.933
   HILGEMANN DW, 1992, J PHYSIOL-LONDON, V454, P59, DOI 10.1113/jphysiol.1992.sp019254
   HILGEMANN DW, 1991, ANN NY ACAD SCI, V639, P126, DOI 10.1111/j.1749-6632.1991.tb17296.x
   Hnatowich M, 2012, CELL CALCIUM, V51, P164, DOI 10.1016/j.ceca.2011.12.006
   Hoshi M, 2014, CIRC-CARDIOVASC GENE, V7, P123, DOI 10.1161/CIRCGENETICS.113.000292
   HRYSHKO LV, 1993, BIOCHIM BIOPHYS ACTA, V1151, P35, DOI 10.1016/0005-2736(93)90068-B
   Huang JB, 2005, AM J PHYSIOL-CELL PH, V288, pC195, DOI 10.1152/ajpcell.00183.2004
   Hunte C, 2005, NATURE, V435, P1197, DOI 10.1038/nature03692
   Huser J, 1996, J PHYSIOL-LONDON, V494, P641
   Imahashi K, 2005, CIRC RES, V97, P916, DOI 10.1161/01.RES.0000187456.06162.cb
   Inserte J, 2012, CARDIOVASC RES, V96, P23, DOI 10.1093/cvr/cvs232
   Iwamoto T, 1999, J BIOL CHEM, V274, P23094, DOI 10.1074/jbc.274.33.23094
   Iwamoto T, 2000, J BIOL CHEM, V275, P38571, DOI 10.1074/jbc.M003788200
   IWAMOTO T, 1995, J BIOL CHEM, V270, P8996, DOI 10.1074/jbc.270.15.8996
   Iwamoto T, 1999, FEBS LETT, V446, P264, DOI 10.1016/S0014-5793(99)00218-5
   Iwamoto T, 1996, J BIOL CHEM, V271, P13609, DOI 10.1074/jbc.271.23.13609
   Iwamoto Takahiro, 2007, Cardiovascular & Hematological Disorders - Drug Targets, V7, P188, DOI 10.2174/187152907781745288
   James PF, 1999, MOL CELL, V3, P555, DOI 10.1016/S1097-2765(00)80349-4
   JARDETZK.O, 1966, NATURE, V211, P969, DOI 10.1038/211969a0
   Jayasinghe I, 2009, BIOPHYS J, V97, P2664, DOI 10.1016/j.bpj.2009.08.036
   Jeffs GJ, 2008, EXP NEUROL, V210, P268, DOI 10.1016/j.expneurol.2007.10.013
   Jeffs GJ, 2007, J CLIN NEUROSCI, V14, P507, DOI 10.1016/j.jocn.2006.07.013
   Jeon D, 2008, CELL CALCIUM, V43, P482, DOI 10.1016/j.ceca.2007.08.003
   John S, 2018, J GEN PHYSIOL, V150, P245, DOI 10.1085/jgp.201611693
   John SA, 2013, P NATL ACAD SCI USA, V110, P7500, DOI 10.1073/pnas.1218751110
   John SA, 2011, P NATL ACAD SCI USA, V108, P1699, DOI 10.1073/pnas.1016114108
   Jordan MC, 2010, J CARD FAIL, V16, P786, DOI 10.1016/j.cardfail.2010.03.012
   Jovanovic S, 2000, J AM COLL CARDIOL, V36, P948, DOI 10.1016/S0735-1097(00)00798-1
   Kang K, 2003, BIOCHEMISTRY-US, V42, P4593, DOI 10.1021/bi027276z
   Kang TM, 2004, NATURE, V427, P544, DOI 10.1038/nature02271
   Keller M, 2004, J MEMBRANE BIOL, V198, P159, DOI 10.1007/s00232-004-0668-9
   Khananshvili D, 2017, ADV EXP MED BIOL, V981, P41, DOI 10.1007/978-3-319-55858-5_3
   Kim I, 1998, COMP BIOCHEM PHYS B, V119, P157, DOI 10.1016/S0305-0491(97)00299-X
   Kim I, 1996, ANN NY ACAD SCI, V779, P126, DOI 10.1111/j.1749-6632.1996.tb44779.x
   Kockskämper J, 2001, BIOPHYS J, V81, P2590, DOI 10.1016/S0006-3495(01)75903-6
   KOFUJI P, 1994, J BIOL CHEM, V269, P5145
   Kohajda Z, 2020, FRONT PHARMACOL, V11, DOI 10.3389/fphar.2020.00516
   Koushik SV, 2001, FASEB J, V15, P1209, DOI 10.1096/fj.00-0696fje
   Lakatta EG, 2010, CIRC RES, V106, P659, DOI 10.1161/CIRCRESAHA.109.206078
   Larbig R, 2010, J PHYSIOL-LONDON, V588, P3266, DOI 10.1113/jphysiol.2010.187708
   LEBLANC N, 1990, SCIENCE, V248, P372, DOI 10.1126/science.2158146
   Lee C, 2005, CAN J CARDIOL, V21, P509
   LEE SL, 1994, J BIOL CHEM, V269, P14849
   Lee SY, 2016, FASEB J, V30, P1356, DOI 10.1096/fj.15-282251
   LEVITSKY DO, 1994, J BIOL CHEM, V269, P22847
   Li XF, 1999, J BIOL CHEM, V274, P8153, DOI 10.1074/jbc.274.12.8153
   LI ZP, 1991, J BIOL CHEM, V266, P1014
   LI ZP, 1993, J BIOL CHEM, V268, P11489
   LI ZP, 1994, J BIOL CHEM, V269, P17434
   Liao J, 2016, NAT STRUCT MOL BIOL, V23, P590, DOI 10.1038/nsmb.3230
   Liao J, 2012, SCIENCE, V335, P686, DOI 10.1126/science.1215759
   Lin X, 2006, AM J PHYSIOL-CELL PH, V290, pC601, DOI 10.1152/ajpcell.00452.2005
   Linck B, 1998, AM J PHYSIOL-CELL PH, V274, pC415, DOI 10.1152/ajpcell.1998.274.2.C415
   Lindgren RM, 2005, GENE, V348, P143, DOI 10.1016/j.gene.2005.01.003
   LIPP P, 1994, J PHYSIOL-LONDON, V474, P439, DOI 10.1113/jphysiol.1994.sp020035
   Liu T, 2018, EUR J CELL BIOL, V97, P190, DOI 10.1016/j.ejcb.2018.02.004
   Lytton J., 2007, NA CA2 EXCHANGERS CA
   Lytton J, 2007, BIOCHEM J, V406, P365, DOI 10.1042/BJ20070619
   Maack C, 2005, CIRC RES, V96, P91, DOI 10.1161/01.RES.0000151334.48676.68
   Maltsev Victor A, 2007, Heart Lung Circ, V16, P335, DOI 10.1016/j.hlc.2007.07.005
   Manfra O, 2018, BIOPHYS J, V114, p620A
   Marinelli F, 2014, P NATL ACAD SCI USA, V111, pE5354, DOI 10.1073/pnas.1415751111
   Marshall CR, 2005, PHYSIOL GENOMICS, V21, P161, DOI 10.1152/physiolgenomics.00286.2004
   MATSUOKA S, 1994, J PHYSIOL-LONDON, V476, P443, DOI 10.1113/jphysiol.1994.sp020146
   MATSUOKA S, 1995, J GEN PHYSIOL, V105, P403, DOI 10.1085/jgp.105.3.403
   MATSUOKA S, 1992, J GEN PHYSIOL, V100, P963, DOI 10.1085/jgp.100.6.963
   Matsuoka S, 1997, J GEN PHYSIOL, V109, P273, DOI 10.1085/jgp.109.2.273
   MATSUOKA S, 1993, P NATL ACAD SCI USA, V90, P3870, DOI 10.1073/pnas.90.9.3870
   Matsuoka S, 1996, ANN NY ACAD SCI, V779, P159, DOI 10.1111/j.1749-6632.1996.tb44784.x
   Maxwell K, 1999, AM J PHYSIOL-HEART C, V277, pH2212, DOI 10.1152/ajpheart.1999.277.6.H2212
   MIURA Y, 1989, J GEN PHYSIOL, V93, P1129, DOI 10.1085/jgp.93.6.1129
   Mohler PJ, 2005, PLOS BIOL, V3, P2158, DOI 10.1371/journal.pbio.0030423
   Mohler PJ, 2003, NATURE, V421, P634, DOI 10.1038/nature01335
   Molinaro P, 2008, J NEUROSCI, V28, P1179, DOI 10.1523/JNEUROSCI.4671-07.2008
   Molinaro P, 2020, CELL CALCIUM, V87, DOI 10.1016/j.ceca.2020.102189
   Molinaro P, 2015, MOL THER, V23, P465, DOI 10.1038/mt.2014.231
   Morad M, 2011, AM J PHYSIOL-CELL PH, V300, pC970, DOI 10.1152/ajpcell.00064.2011
   Müller JG, 2002, CIRC RES, V90, P158, DOI 10.1161/hh0202.103231
   NAKASAKI Y, 1993, J BIOCHEM-TOKYO, V114, P528, DOI 10.1093/oxfordjournals.jbchem.a124211
   Neco P, 2010, BIOPHYS J, V99, P755, DOI 10.1016/j.bpj.2010.04.071
   Nicholas SB, 1999, AM J PHYSIOL-HEART C, V277, pH324, DOI 10.1152/ajpheart.1999.277.1.H324
   Nicholas SB, 1998, AM J PHYSIOL-HEART C, V274, pH217, DOI 10.1152/ajpheart.1998.274.1.H217
   Nicoll DA, 2002, ANN NY ACAD SCI, V976, P11
   Nicoll DA, 1999, J BIOL CHEM, V274, P910, DOI 10.1074/jbc.274.2.910
   Nicoll DA, 1996, J BIOL CHEM, V271, P13385, DOI 10.1074/jbc.271.23.13385
   Nicoll DA, 1996, J BIOL CHEM, V271, P24914, DOI 10.1074/jbc.271.40.24914
   NICOLL DA, 1990, SCIENCE, V250, P562, DOI 10.1126/science.1700476
   Nicoll DA, 1996, ANN NY ACAD SCI, V779, P86, DOI 10.1111/j.1749-6632.1996.tb44772.x
   Nicoll DA, 2006, J BIOL CHEM, V281, P21577, DOI 10.1074/jbc.C600117200
   NIGGLI E, 1991, NATURE, V349, P621, DOI 10.1038/349621a0
   On C, 2008, BMC EVOL BIOL, V8, DOI 10.1186/1471-2148-8-127
   Ottolia M, 2005, J BIOL CHEM, V280, P1061, DOI 10.1074/jbc.M411899200
   Ottolia M, 2004, BIOPHYS J, V87, P899, DOI 10.1529/biophysj.104.043471
   Ottolia M, 2001, J BIOL CHEM, V276, P19603, DOI 10.1074/jbc.M101489200
   Ottolia M, 2007, J BIOL CHEM, V282, P3695, DOI 10.1074/jbc.M610425200
   Ottolia M, 2013, J MOL CELL CARDIOL, V61, P28, DOI 10.1016/j.yjmcc.2013.06.001
   Ottolia M, 2010, CHANNELS, V4, P159, DOI 10.4161/chan.4.3.11386
   Ottolia M, 2009, J BIOL CHEM, V284, P32735, DOI 10.1074/jbc.M109.055434
   Perez C, 2011, EMBO REP, V12, P804, DOI 10.1038/embor.2011.102
   PHILIPSON KD, 1982, CIRC RES, V50, P287, DOI 10.1161/01.RES.50.2.287
   PHILIPSON KD, 1984, J BIOL CHEM, V259, P3999
   PHILIPSON KD, 1988, BIOCHIM BIOPHYS ACTA, V945, P298, DOI 10.1016/0005-2736(88)90492-0
   PHILIPSON KD, 1982, J BIOL CHEM, V257, P5111
   PHILIPSON KD, 1985, J BIOL CHEM, V260, P9666
   PHILIPSON KD, 1983, J BIOL CHEM, V258, P5905
   PHILIPSON KD, 1984, J BIOL CHEM, V259, P16
   Plain F, 2017, J BIOL CHEM, V292, P10745, DOI 10.1074/jbc.M116.773945
   Pogwizd SM, 2003, DRUGS, V63, P439, DOI 10.2165/00003495-200363050-00001
   Pogwizd SM, 2004, TRENDS CARDIOVAS MED, V14, P61, DOI 10.1016/j.tcm.2003.12.002
   Pogwizd SM, 1999, CIRC RES, V85, P1009
   Pogwizd SM, 2002, ANN NY ACAD SCI, V976, P454
   PORZIG H, 1993, AM J PHYSIOL, V265, pC748, DOI 10.1152/ajpcell.1993.265.3.C748
   Pott C, 2005, CIRC RES, V97, P1288, DOI 10.1161/01.RES.0000196563.84231.21
   Pott C, 2004, BIOCHEM BIOPH RES CO, V322, P1336, DOI 10.1016/j.bbrc.2004.08.038
   Pott C, 2007, ANN NY ACAD SCI, V1099, P310, DOI 10.1196/annals.1387.019
   Pott C, 2007, ANN NY ACAD SCI, V1099, P270, DOI 10.1196/annals.1387.015
   Pott C, 2007, AM J PHYSIOL-CELL PH, V292, pC968, DOI 10.1152/ajpcell.00177.2006
   Pott C, 2012, BASIC RES CARDIOL, V107, DOI 10.1007/s00395-012-0247-7
   Pott C, 2011, CURR DRUG TARGETS, V12, P737, DOI 10.2174/138945011795378559
   Quednau BD, 2004, PFLUG ARCH EUR J PHY, V447, P543, DOI 10.1007/s00424-003-1065-4
   Quednau Beate D., 1997, American Journal of Physiology, V272, pC1250
   Radwanski PB, 2015, CARDIOVASC RES, V106, P143, DOI 10.1093/cvr/cvu262
   Ramos-Franco J, 2016, CIRC RES, V118, P203, DOI 10.1161/CIRCRESAHA.115.307399
   Ranu HK, 2002, J MOL CELL CARDIOL, V34, P389, DOI 10.1006/jmcc.2001.1521
   REEVES JP, 1984, J BIOL CHEM, V259, P7733
   Reilly L, 2015, FASEB J, V29, P4532, DOI 10.1096/fj.15-276493
   Ren XY, 2008, BIOCHEMISTRY-US, V47, P6081, DOI 10.1021/bi800177t
   Ren XY, 2013, J MOL CELL CARDIOL, V57, P68, DOI 10.1016/j.yjmcc.2013.01.010
   Reuter H, 2004, J PHYSIOL-LONDON, V554, P779, DOI 10.1113/jphysiol.2003.055046
   Reuter H, 2003, CELL CALCIUM, V34, P19, DOI 10.1016/S0143-4160(03)00018-6
   REUTER H, 1968, J PHYSIOL-LONDON, V195, P451, DOI 10.1113/jphysiol.1968.sp008467
   Reuter H, 2002, CIRC RES, V90, P305, DOI 10.1161/hh0302.104562
   Riedel MJ, 2006, EMBO J, V25, P4605, DOI 10.1038/sj.emboj.7601321
   Rimon A, 2007, J BIOL CHEM, V282, P26810, DOI 10.1074/jbc.M704469200
   Robertson JL, 2010, NATURE, V468, P844, DOI 10.1038/nature09556
   Roos KP, 2007, J CARD FAIL, V13, P318, DOI 10.1016/j.cardfail.2007.01.004
   Rosker C, 2004, J BIOL CHEM, V279, P13696, DOI 10.1074/jbc.M308108200
   Ruknudin AM, 2007, ANN NY ACAD SCI, V1099, P103, DOI 10.1196/annals.1387.036
   SAHINTOTH M, 1995, BIOCHEM BIOPH RES CO, V212, P968, DOI 10.1006/bbrc.1995.2064
   Salinas RK, 2011, J BIOL CHEM, V286, P32123, DOI 10.1074/jbc.M111.249268
   Santacruz-Toloza L, 2000, J BIOL CHEM, V275, P182, DOI 10.1074/jbc.275.1.182
   Schäfer C, 2001, CARDIOVASC RES, V51, P241, DOI 10.1016/S0008-6363(01)00282-6
   Schulson MN, 2011, J CELL SCI, V124, P1167, DOI 10.1242/jcs.080929
   Schulze DH, 2003, J BIOL CHEM, V278, P28849, DOI 10.1074/jbc.M300754200
   Schwarz EM, 1997, P NATL ACAD SCI USA, V94, P10249, DOI 10.1073/pnas.94.19.10249
   Scranton K, 2020, BIOPHYS J, V118, p100A
   Scriven DRL, 2000, BIOPHYS J, V79, P2682, DOI 10.1016/S0006-3495(00)76506-4
   Shannon Thomas R., 1994, American Journal of Physiology, V266, pC1350
   Shattock MJ, 2015, J PHYSIOL-LONDON, V593, P1361, DOI 10.1113/jphysiol.2014.282319
   Shen CC, 2007, J PHYSIOL-LONDON, V582, P1011, DOI 10.1113/jphysiol.2007.132720
   SHIEH BH, 1992, GENOMICS, V12, P616, DOI 10.1016/0888-7543(92)90459-6
   Shigekawa M, 2002, ANN NY ACAD SCI, V976, P19
   Shipston MJ, 2011, J BIOL CHEM, V286, P8709, DOI 10.1074/jbc.R110.210005
   Shlosman I, 2018, J GEN PHYSIOL, V150, P51, DOI 10.1085/jgp.201711897
   Shuart NG, 2011, NAT COMMUN, V2, DOI 10.1038/ncomms1466
   Sitte HH, 2004, MOL INTERV, V4, P38, DOI 10.1124/mi.4.1.38
   Skogestad J, 2020, CARDIOVASC RES, V116, P78, DOI 10.1093/cvr/cvz087
   Sokolow S, 2004, J CLIN INVEST, V113, P265, DOI 10.1172/JCI200418688
   Sorimachi H, 2012, CARDIOVASC RES, V96, P11, DOI 10.1093/cvr/cvs157
   Steccanella F, 2020, BIOPHYS J, V118, p100A
   Stieber J, 2003, P NATL ACAD SCI USA, V100, P15235, DOI 10.1073/pnas.2434235100
   Sugishita K, 2001, CIRCULATION, V104, P2101, DOI 10.1161/hc4001.097038
   Swift F, 2008, CARDIOVASC RES, V78, P71, DOI 10.1093/cvr/cvn013
   Swift F, 2007, CARDIOVASC RES, V75, P109, DOI 10.1016/j.cardiores.2007.03.017
   Szerencsei RT, 2013, CHANNELS, V7, P109, DOI 10.4161/chan.23898
   Terracciano CMN, 1998, J PHYSIOL-LONDON, V512, P651, DOI 10.1111/j.1469-7793.1998.651bd.x
   Thomas MJ, 2003, J MOL CELL CARDIOL, V35, P1325, DOI 10.1016/j.yjmcc.2003.08.005
   Tombola F, 2010, NAT STRUCT MOL BIOL, V17, P44, DOI 10.1038/nsmb.1738
   Torrente AG, 2017, J PHYSIOL-LONDON, V595, P3847, DOI 10.1113/JP274249
   Torrente AG, 2015, P NATL ACAD SCI USA, V112, P9769, DOI 10.1073/pnas.1505670112
   Torres NS, 2010, J PHYSIOL-LONDON, V588, P4249, DOI 10.1113/jphysiol.2010.194688
   van Dijk L, 2018, CELL CALCIUM, V76, P10, DOI 10.1016/j.ceca.2018.09.004
   Van Eylen F, 2001, CELL CALCIUM, V30, P191, DOI 10.1054/ceca.2001.0223
   VANDERVUSSE GJ, 1994, ANN NY ACAD SCI, V723, P1
   Vaughan-Jones RD, 2009, J MOL CELL CARDIOL, V46, P318, DOI 10.1016/j.yjmcc.2008.10.024
   VEMURI R, 1988, BIOCHIM BIOPHYS ACTA, V937, P258, DOI 10.1016/0005-2736(88)90248-9
   Waight AB, 2013, NATURE, V499, P107, DOI 10.1038/nature12233
   Wakimoto K, 2000, J BIOL CHEM, V275, P36991, DOI 10.1074/jbc.M004035200
   Wakimoto K, 2003, COMP BIOCHEM PHYS B, V135, P9, DOI 10.1016/S1096-4959(03)00057-5
   Wang JF, 2009, AM J PHYSIOL-HEART C, V297, pH590, DOI 10.1152/ajpheart.00190.2009
   Wanichawan P, 2014, J BIOL CHEM, V289, P33984, DOI 10.1074/jbc.M114.602581
   Wanichawan P, 2011, AM J PHYSIOL-CELL PH, V300, pC989, DOI 10.1152/ajpcell.00196.2010
   Weber CR, 2003, CIRCULATION, V108, P2224, DOI 10.1161/01.CIR.0000095274.72486.94
   Weber CR, 2003, CIRC RES, V92, P950, DOI 10.1161/01.RES.0000071747.61468.7F
   Weber CR, 2002, CIRC RES, V90, P182, DOI 10.1161/hh0202.103940
   Weber CR, 2001, J GEN PHYSIOL, V117, P119, DOI 10.1085/jgp.117.2.119
   Wetzel Glenn T., 1995, American Journal of Physiology, V268, pH1723
   Wu MS, 2013, P NATL ACAD SCI USA, V110, P11367, DOI 10.1073/pnas.1302515110
   Wu MS, 2011, STRUCTURE, V19, P1509, DOI 10.1016/j.str.2011.07.008
   Wu MS, 2010, J BIOL CHEM, V285, P2554, DOI 10.1074/jbc.M109.059162
   Xiao YF, 2004, BIOCHEM BIOPH RES CO, V321, P116, DOI 10.1016/j.bbrc.2004.06.114
   Xie Y, 2008, AM J PHYSIOL-CELL PH, V295, pC388, DOI 10.1152/ajpcell.00178.2008
   Yao AS, 1998, CIRC RES, V82, P657, DOI 10.1161/01.RES.82.6.657
   Yaradanakul A, 2007, J PHYSIOL-LONDON, V582, P991, DOI 10.1113/jphysiol.2007.132712
   Yuan JQ, 2018, BIOCHEMISTRY-US, V57, P5096, DOI 10.1021/acs.biochem.8b00300
   Yue X, 2020, CELL CALCIUM, V87, DOI 10.1016/j.ceca.2020.102167
   Yue X, 2017, J MOL CELL CARDIOL, V108, P50, DOI 10.1016/j.yjmcc.2017.05.008
   Zhang J, 2005, J PHYSIOL-LONDON, V569, P243, DOI 10.1113/jphysiol.2005.091801
   Zhang XQ, 2006, J BIOL CHEM, V281, P7784, DOI 10.1074/jbc.M512092200
   Zhao J, 2009, J BIOL CHEM, V284, P4605, DOI 10.1074/jbc.M804462200
NR 300
TC 25
Z9 27
U1 2
U2 10
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN, NJ 07030 USA
SN 2040-4603
J9 COMPR PHYSIOL
JI Compr. Physiol.
PD JAN
PY 2022
VL 12
IS 1
BP 2681
EP 2717
DI 10.1002/cphy.c200031
PG 37
WC Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Physiology
GA 3L9DD
UT WOS:000835060100002
PM 34964124
DA 2025-04-10
ER

PT J
AU Simionescu-Bankston, A
   Pichavant, C
   Canner, JP
   Apponi, LH
   Wang, YR
   Steeds, C
   Olthoff, JT
   Belanto, JJ
   Ervasti, JM
   Pavlath, GK
AF Simionescu-Bankston, Adriana
   Pichavant, Christophe
   Canner, James P.
   Apponi, Luciano H.
   Wang, Yanru
   Steeds, Craig
   Olthoff, John T.
   Belanto, Joseph J.
   Ervasti, James M.
   Pavlath, Grace K.
TI Creatine kinase B is necessary to limit myoblast fusion during
   myogenesis
SO AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY
LA English
DT Article
DE muscle growth; adenosine triphosphate; myotube; actin; myocyte
ID SKELETAL-MUSCLE DIFFERENTIATION; GTPASE-ACTIVATING PROTEIN; ACTIN
   CYTOSKELETON; CELL-FUSION; MAMMALIAN SEPTIN; BINDING DOMAIN; BETA-ACTIN;
   IN-VITRO; GENE; FAMILY
AB Myoblast fusion is critical for proper muscle growth and regeneration. During myoblast fusion, the localization of some molecules is spatially restricted; however, the exact reason for such localization is unknown. Creatine kinase B (CKB), which replenishes local ATP pools, localizes near the ends of cultured primary mouse myotubes. To gain insights into the function of CKB, we performed a yeast two-hybrid screen to identify CKB-interacting proteins. We identified molecules with a broad diversity of roles, including actin polymerization, intracellular protein trafficking, and alternative splicing, as well as sarcomeric components. In-depth studies of alpha-skeletal actin and alpha-cardiac actin, two predominant muscle actin isoforms, demonstrated their biochemical interaction and partial colocalization with CKB near the ends of myotubes in vitro. In contrast to other cell types, specific knockdown of CKB did not grossly affect actin polymerization in myotubes, suggesting other muscle-specific roles for CKB. Interestingly, knockdown of CKB resulted in significantly increased myoblast fusion and myotube size in vitro, whereas knockdown of creatine kinase M had no effect on these myogenic parameters. Our results suggest that localized CKB plays a key role in myotube formation by limiting myoblast fusion during myogenesis.
C1 [Simionescu-Bankston, Adriana] Emory Univ, Sch Med, Grad Program Biochem Cell & Dev Biol, Atlanta, GA 30322 USA.
   [Simionescu-Bankston, Adriana; Pichavant, Christophe; Canner, James P.; Apponi, Luciano H.; Wang, Yanru; Steeds, Craig; Pavlath, Grace K.] Emory Univ, Sch Med, Dept Pharmacol, Atlanta, GA 30322 USA.
   [Olthoff, John T.; Belanto, Joseph J.; Ervasti, James M.] Univ Minnesota, Dept Biochem Mol Biol & Biophys, Minneapolis, MN USA.
C3 Emory University; Emory University; University of Minnesota System;
   University of Minnesota Twin Cities
RP Pavlath, GK (corresponding author), Emory Univ, Sch Med, Dept Pharmacol, 1510 Clifton Rd, Atlanta, GA 30322 USA.
EM gpavlat@emory.edu
RI Wang, yanru/JAX-5241-2023; Ervasti, James/AAZ-4786-2020; Bankston,
   Adriana/G-4924-2012; Apponi, Luciano/A-4081-2013
OI pichavant, christophe/0000-0003-0150-9346
FU National Institute of Arthritis and Musculoskeletal and Skin Diseases
   [AR-04731408, AR-049899, AR-007612]
FX This work was supported by National Institute of Arthritis and
   Musculoskeletal and Skin Diseases Grants to G. K. Pavlath (AR-04731408),
   J. M. Ervasti (AR-049899), and J. T. Olthoff and J. J. Belanto
   (AR-007612).
CR Abmayr SM, 2012, DEVELOPMENT, V139, P641, DOI 10.1242/dev.068353
   Abramovici H, 2007, CELL MOTIL CYTOSKEL, V64, P549, DOI 10.1002/cm.20204
   BAINS W, 1984, MOL CELL BIOL, V4, P1449, DOI 10.1128/MCB.4.8.1449
   Bartel PL., 1993, Cellular interactions in development: A practical approach
   Bois PRJ, 2003, EMBO J, V22, P1147, DOI 10.1093/emboj/cdg116
   Bondesen BA, 2004, AM J PHYSIOL-CELL PH, V287, pC475, DOI 10.1152/ajpcell.00088.2004
   Bondesen BA, 2007, FASEB J, V21, P3338, DOI 10.1096/fj.06-7070com
   Brzóska E, 2006, DIFFERENTIATION, V74, P105, DOI 10.1111/j.1432-0436.2005.00059.x
   Bürklen TS, 2007, MOL CELL BIOCHEM, V297, P53, DOI 10.1007/s11010-006-9322-4
   CASELLA JF, 1981, NATURE, V293, P302, DOI 10.1038/293302a0
   Castellani L, 2006, J BIOL CHEM, V281, P15249, DOI 10.1074/jbc.M601390200
   Chang EJ, 2008, NAT MED, V14, P966, DOI 10.1038/nm.1860
   CIFUENTESDIAZ C, 1995, MECH DEVELOP, V50, P85, DOI 10.1016/0925-4773(94)00327-J
   Craig R., 2004, Myology, V3, P129
   Diguet N, 2011, J BIOL CHEM, V286, P35007, DOI 10.1074/jbc.M111.252395
   Doherty KR, 2008, J BIOL CHEM, V283, P20252, DOI 10.1074/jbc.M802306200
   Dowling JJ, 2008, BMC CELL BIOL, V9, DOI 10.1186/1471-2121-9-36
   Duan R, 2009, DEV BIOL, V325, P374, DOI 10.1016/j.ydbio.2008.10.035
   Friday BB, 2000, J CELL BIOL, V149, P657, DOI 10.1083/jcb.149.3.657
   Friday BB, 2001, J CELL SCI, V114, P303
   Frost A, 2009, CELL, V137, P191, DOI 10.1016/j.cell.2009.04.010
   Furukawa Y, 2001, BIOCHEM BIOPH RES CO, V284, P643, DOI 10.1006/bbrc.2001.5022
   Gruenbaum-Cohen Y, 2012, P NATL ACAD SCI USA, V109, P11211, DOI 10.1073/pnas.1116065109
   Hall A, 1998, SCIENCE, V279, P509, DOI 10.1126/science.279.5350.509
   He F, 2009, PROTEIN SCI, V18, P80, DOI 10.1002/pro.17
   Henderson DM, 2010, P NATL ACAD SCI USA, V107, P9632, DOI 10.1073/pnas.1001517107
   HOLLENBERG SM, 1995, MOL CELL BIOL, V15, P3813
   Horsley V, 2001, J CELL BIOL, V153, P329, DOI 10.1083/jcb.153.2.329
   Ito H, 2005, ONCOGENE, V24, P7064, DOI 10.1038/sj.onc.1208862
   Jansen KM, 2006, J CELL BIOL, V174, P403, DOI 10.1083/jcb.200601102
   Kashina AS, 2006, TRENDS CELL BIOL, V16, P610, DOI 10.1016/j.tcb.2006.10.001
   Kim S, 2007, DEV CELL, V12, P571, DOI 10.1016/j.devcel.2007.02.019
   Kinoshita M, 2002, DEV CELL, V3, P791, DOI 10.1016/S1534-5807(02)00366-0
   Kinoshita M, 1997, GENE DEV, V11, P1535, DOI 10.1101/gad.11.12.1535
   Kuiper JWP, 2008, PLOS BIOL, V6, P568, DOI 10.1371/journal.pbio.0060051
   Kuiper JWP, 2009, PLOS ONE, V4, DOI 10.1371/journal.pone.0005030
   Lafuste P, 2005, MOL BIOL CELL, V16, P861, DOI 10.1091/mbc.e04-03-0226
   Lee KS, 2008, DIFFERENTIATION, V76, P299, DOI 10.1111/j.1432-0436.2007.00209.x
   Lodish H.F., 2013, Molecular cell biology
   Moon SY, 2003, TRENDS CELL BIOL, V13, P13, DOI 10.1016/S0962-8924(02)00004-1
   Mostowy S, 2012, NAT REV MOL CELL BIO, V13, P183, DOI 10.1038/nrm3284
   Mounier N, 2002, CELL STRESS CHAPERON, V7, P167, DOI 10.1379/1466-1268(2002)007<0167:ACASHS>2.0.CO;2
   Mukai A, 2008, EXP CELL RES, V314, P387, DOI 10.1016/j.yexcr.2007.10.006
   Mukai A, 2009, EXP CELL RES, V315, P3052, DOI 10.1016/j.yexcr.2009.07.010
   NAMBA Y, 1992, J BIOCHEM-TOKYO, V112, P503, DOI 10.1093/oxfordjournals.jbchem.a123929
   Nishiyama T, 2004, J BIOL CHEM, V279, P47311, DOI 10.1074/jbc.M403546200
   Nowak SJ, 2009, J CELL SCI, V122, P3282, DOI 10.1242/jcs.047597
   O'Connor RS, 2008, J PHYSIOL-LONDON, V586, P2841, DOI 10.1113/jphysiol.2008.151027
   O'Connor RS, 2007, J CELL SCI, V120, P149, DOI 10.1242/jcs.03307
   Pavlath GK, 2010, EXP CELL RES, V316, P3067, DOI 10.1016/j.yexcr.2010.05.025
   Peck J, 2002, FEBS LETT, V528, P27, DOI 10.1016/S0014-5793(02)03331-8
   Peckham M, 2008, J MICROSC-OXFORD, V231, P486, DOI 10.1111/j.1365-2818.2008.02061.x
   Perrin BJ, 2013, J NEUROSCI, V33, P8114, DOI 10.1523/JNEUROSCI.0238-13.2013
   Perrin BJ, 2010, CYTOSKELETON, V67, P630, DOI 10.1002/cm.20475
   Prakash SK, 2000, HUM MOL GENET, V9, P477, DOI 10.1093/hmg/9.4.477
   Ramalingam A, 2008, CANCER RES, V68, P1683, DOI 10.1158/0008-5472.CAN-07-6072
   Ren G, 2006, MICROBIOL MOL BIOL R, V70, P37, DOI 10.1128/MMBR.70.1.37-120.2006
   Renema WKJ, 2007, NMR BIOMED, V20, P448, DOI 10.1002/nbm.1117
   Ridley AJ, 2011, CELL, V145, P1012, DOI 10.1016/j.cell.2011.06.010
   Rybakova IN, 2002, MOL BIOL CELL, V13, P1512, DOI 10.1091/mbc.01-09-0446
   SCHAFER BW, 1988, J CELL BIOL, V106, P1161, DOI 10.1083/jcb.106.4.1161
   Schwander M, 2003, DEV CELL, V4, P673, DOI 10.1016/S1534-5807(03)00118-7
   Shin JB, 2007, NEURON, V53, P371, DOI 10.1016/j.neuron.2006.12.021
   Shuster CB, 1996, CELL MOTIL CYTOSKEL, V35, P175
   Simionescu A, 2011, ADV EXP MED BIOL, V713, P113, DOI 10.1007/978-94-007-0763-4_8
   Simionescu-Bankston A, 2013, DEV BIOL, V382, P160, DOI 10.1016/j.ydbio.2013.07.004
   Small JV, 2002, TRENDS CELL BIOL, V12, P112, DOI 10.1016/S0962-8924(01)02237-1
   Squillace RM, 2002, DEV BIOL, V250, P218, DOI 10.1006/dbio.2002.0798
   Städler B, 2010, J MICROSC-OXFORD, V237, P63, DOI 10.1111/j.1365-2818.2009.03302.x
   Stolz M, 1998, J CELL SCI, V111, P1207
   Strating JRPM, 2009, BIOL CELL, V101, P495, DOI 10.1042/BC20080233
   Straube A, 2007, CURR BIOL, V17, P1318, DOI 10.1016/j.cub.2007.06.058
   Teplova M, 2008, NAT STRUCT MOL BIOL, V15, P1343, DOI 10.1038/nsmb.1519
   van den Eijnde SM, 2001, J CELL SCI, V114, P3631
   VANDEKERCKHOVE J, 1986, J BIOL CHEM, V261, P1838
   Vasyutina E, 2009, P NATL ACAD SCI USA, V106, P8935, DOI 10.1073/pnas.0902501106
   Wakelam M., 1985, BIOCHEM J, V15, P1, DOI DOI 10.1042/BJ2280001
   Wang JS, 2005, CELL MOTIL CYTOSKEL, V62, P35, DOI 10.1002/cm.20083
   Weirich CS, 2008, NAT REV MOL CELL BIO, V9, P478, DOI 10.1038/nrm2407
   Wyss M, 2000, PHYSIOL REV, V80, P1107, DOI 10.1152/physrev.2000.80.3.1107
   Yao XB, 1996, J BIOL CHEM, V271, P7224, DOI 10.1074/jbc.271.12.7224
   Zhang J, 2005, FEBS LETT, V579, P559, DOI 10.1016/j.febslet.2004.10.112
   Zhang Z, 2002, INT J BIOCHEM CELL B, V34, P325, DOI 10.1016/S1357-2725(01)00134-0
NR 83
TC 12
Z9 15
U1 0
U2 11
PU AMER PHYSIOLOGICAL SOC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA
SN 0363-6143
EI 1522-1563
J9 AM J PHYSIOL-CELL PH
JI Am. J. Physiol.-Cell Physiol.
PD JUN 1
PY 2015
VL 308
IS 11
BP C919
EP C931
DI 10.1152/ajpcell.00029.2015
PG 13
WC Cell Biology; Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Physiology
GA CK5CO
UT WOS:000356240000007
PM 25810257
OA Green Published
DA 2025-04-10
ER

PT J
AU Duffy, L
   Cappas, E
   Schofield, PR
   Scimone, A
   Karl, T
AF Duffy, Liesl
   Cappas, Emily
   Schofield, Peter R.
   Scimone, Anna
   Karl, Tim
TI Behavioral profile of a heterozygous mutant mouse model for EGF-like
   domain neuregulin 1
SO BEHAVIORAL NEUROSCIENCE
LA English
DT Article
DE EGF-like domain neuregulin 1; mouse model for schizophrenia; motor
   activity; exploration; sensorimotor gating
ID OPEN-FIELD BEHAVIOR; PREPULSE INHIBITION; LOCOMOTOR-ACTIVITY;
   NERVOUS-SYSTEM; CARDIAC DEVELOPMENT; PREFRONTAL CORTEX; KNOCKOUT MICE;
   TEST BATTERY; SCHIZOPHRENIA; RECEPTOR
AB Human genetic studies have demonstrated that the neuregulin 1 gene (NRG1) is involved in the development of schizophrenia. Alternative splicing of NRG1 results in at least 15 distinct isoforms and all contain an extracellular epidermal growth factor (EGF)-like domain, which is sufficient for Nrg1's biological activity. Here, we characterize a heterozygous mutant model for mouse EGF-like domain neuregulin 1 (Nrg1) regarding schizophrenia-related behavioral domains. A comprehensive, multitiered phenotyping strategy was used to investigate locomotion, exploration, anxiety-related behaviors, and sensorimotor gating. Nrg1 mutant mice exhibited a hyper-locomotive phenotype and an improved ability to habituate to a new environment. Extensive analysis of anxiety-related behaviors revealed a wild type-like phenotype in this domain. However, a moderate impairment in sensorimotor gating was found after pharmacological challenge using psychoactive substances. Our study adds to the increasing behavioral data available from a variety of animal models for Nrg1 isoforms. We suggest a standardized and comprehensive behavioral phenotyping approach to distinguish between the different models and to clarify their relevance for schizophrenia research. Future behavioral investigations will focus on the negative and cognitive symptoms of schizophrenia.
C1 [Duffy, Liesl; Cappas, Emily; Karl, Tim] St Vincents Hosp, Garvan Inst Med Res, Neurosci Res Program, Darlinghurst, NSW 2010, Australia.
   [Schofield, Peter R.; Scimone, Anna] Prince Wales Med Res Inst, Schizophrenia Res Inst, Sydney, NSW, Australia.
   [Schofield, Peter R.] Univ New S Wales, Sydney, NSW, Australia.
C3 NSW Health; St Vincents Hospital Sydney; Garvan Institute of Medical
   Research; Schizophrenia Research Institute; Neuroscience Research
   Australia; University of New South Wales Sydney
RP Karl, T (corresponding author), St Vincents Hosp, Garvan Inst Med Res, Neurosci Res Program, 384 Victoria St, Darlinghurst, NSW 2010, Australia.
EM t.karl@garvan.org.au
RI Karl, Tim/E-2088-2011; Schofield, Peter/C-9669-2011
OI Karl, Tim/0000-0001-9904-8482; Schofield, Peter/0000-0003-2967-9662
CR Adriani W, 1998, EXP BRAIN RES, V123, P52, DOI 10.1007/s002210050544
   Bjarnadottir M, 2007, J NEUROSCI, V27, P4519, DOI 10.1523/JNEUROSCI.4314-06.2007
   Boucher AA, 2007, NEUROSCIENCE, V149, P861, DOI 10.1016/j.neuroscience.2007.08.020
   Boucher AA, 2007, PSYCHOPHARMACOLOGY, V192, P325, DOI 10.1007/s00213-007-0721-3
   Britsch S, 1998, GENE DEV, V12, P1825, DOI 10.1101/gad.12.12.1825
   Clark BJ, 2005, BEHAV BRAIN RES, V163, P91, DOI 10.1016/j.bbr.2005.04.007
   Corfas G, 2004, NAT NEUROSCI, V7, P575, DOI 10.1038/nn1258
   COSTALL B, 1989, PHARMACOL BIOCHEM BE, V32, P777, DOI 10.1016/0091-3057(89)90033-6
   Crawley JN, 1997, HORM BEHAV, V31, P197, DOI 10.1006/hbeh.1997.1382
   DEFRIES JC, 1966, SCIENCE, V154, P1577, DOI 10.1126/science.154.3756.1577
   DENENBERG VH, 1969, ANN NY ACAD SCI, V159, P852, DOI 10.1111/j.1749-6632.1969.tb12983.x
   Ellenbroek B.A., 1990, Behav Pharmacol, V1, P469
   Erickson SL, 1997, DEVELOPMENT, V124, P4999
   Falls DL, 2003, EXP CELL RES, V284, P14, DOI 10.1016/S0014-4827(02)00102-7
   Gainetdinov RR, 2001, TRENDS NEUROSCI, V24, P527, DOI 10.1016/S0166-2236(00)01886-5
   GASSMANN M, 1995, NATURE, V378, P390, DOI 10.1038/378390a0
   Gerlai R, 2000, BEHAV BRAIN RES, V109, P219, DOI 10.1016/S0166-4328(99)00175-8
   Geyer MA, 2001, PSYCHOPHARMACOLOGY, V156, P117, DOI 10.1007/s002130100811
   Geyer MA, 1998, Current Protocols in Neuroscience
   Golub MS, 2004, BEHAV BRAIN RES, V153, P159, DOI 10.1016/j.bbr.2003.11.010
   Gu ZL, 2005, J NEUROSCI, V25, P4974, DOI 10.1523/JNEUROSCI.1086-05.2005
   GYERTYAN I, 1995, BEHAV PHARMACOL, V6, P24
   Hahn CG, 2006, NAT MED, V12, P824, DOI 10.1038/nm1418
   Harrison PJ, 2006, BIOL PSYCHIAT, V60, P132, DOI 10.1016/j.biopsych.2005.11.002
   Hascoët M, 2001, PROG NEURO-PSYCHOPH, V25, P141, DOI 10.1016/S0278-5846(00)00151-2
   Hashimoto R, 2004, MOL PSYCHIATR, V9, P299, DOI 10.1038/sj.mp.4001434
   Javitt DC, 2004, SCI AM, V290, P48, DOI 10.1038/scientificamerican0104-48
   Karl T, 2007, GENES BRAIN BEHAV, V6, P677, DOI 10.1111/j.1601-183X.2006.00298.x
   Karl T, 2003, EXP TOXICOL PATHOL, V55, P69, DOI 10.1078/0940-2993-00301
   Kerber G, 2003, J MOL NEUROSCI, V21, P149, DOI 10.1385/JMN:21:2:149
   Kopp C, 2001, BEHAV BRAIN RES, V125, P93, DOI 10.1016/S0166-4328(01)00289-3
   Kramer R, 1996, P NATL ACAD SCI USA, V93, P4833, DOI 10.1073/pnas.93.10.4833
   Law AJ, 2006, P NATL ACAD SCI USA, V103, P6747, DOI 10.1073/pnas.0602002103
   Lee I, 2005, BEHAV NEUROSCI, V119, P145, DOI 10.1037/0735-7044.119.1.145
   Leng A, 2004, BEHAV BRAIN RES, V154, P449, DOI 10.1016/j.bbr.2004.03.012
   Long WW, 2003, DEVELOPMENT, V130, P5257, DOI 10.1242/dev.00715
   MEYER D, 1995, NATURE, V378, P386, DOI 10.1038/378386a0
   Michailov GV, 2004, SCIENCE, V304, P700, DOI 10.1126/science.1095862
   MONTGOMERY KC, 1955, J COMP PHYSIOL PSYCH, V48, P254, DOI 10.1037/h0043788
   Munafò MR, 2006, MOL PSYCHIATR, V11, P539, DOI 10.1038/sj.mp.4001817
   O'Tuathaigh CMP, 2007, NEUROSCIENCE, V147, P18, DOI 10.1016/j.neuroscience.2007.03.051
   O'Tuathaigh CM, 2006, NEUROREPORT, V17, P79, DOI 10.1097/01.wnr.0000192738.31029.0a
   Ozaki M, 1997, NATURE, V390, P691, DOI 10.1038/37795
   PELLOW S, 1985, J NEUROSCI METH, V14, P149, DOI 10.1016/0165-0270(85)90031-7
   Powell CM, 2006, BIOL PSYCHIAT, V59, P1198, DOI 10.1016/j.biopsych.2006.05.008
   Riethmacher D, 1997, NATURE, V389, P725, DOI 10.1038/39593
   Rimer M, 2005, NEUROREPORT, V16, P271, DOI 10.1097/00001756-200502280-00014
   Snodgrass-Belt P, 2005, BRAIN RES, V1038, P171, DOI 10.1016/j.brainres.2005.01.030
   Stefansson H, 2002, AM J HUM GENET, V71, P877, DOI 10.1086/342734
   Steinthorsdottir V, 2004, GENE, V342, P97, DOI 10.1016/j.gene.2004.07.029
   Thuret S, 2004, J NEUROCHEM, V91, P1302, DOI 10.1111/j.1471-4159.2004.02809.x
   van Gaalen MM, 2000, BEHAV BRAIN RES, V115, P95, DOI 10.1016/S0166-4328(00)00240-0
   Walss-Bass C, 2006, BIOL PSYCHIAT, V60, P548, DOI 10.1016/j.biopsych.2006.03.017
   Wang JH, 2003, BEHAV BRAIN RES, V143, P201, DOI 10.1016/S0166-4328(03)00036-6
   Wolpowitz D, 2000, NEURON, V25, P79, DOI 10.1016/S0896-6273(00)80873-9
   Wong AHC, 2003, NEUROSCI BIOBEHAV R, V27, P269, DOI 10.1016/S0149-7634(03)00035-6
   Yurek DM, 2004, BRAIN RES, V1028, P116, DOI 10.1016/j.brainres.2004.08.066
NR 57
TC 47
Z9 61
U1 0
U2 4
PU AMER PSYCHOLOGICAL ASSOC
PI WASHINGTON
PA 750 FIRST ST NE, WASHINGTON, DC 20002-4242 USA
SN 0735-7044
J9 BEHAV NEUROSCI
JI Behav. Neurosci.
PD AUG
PY 2008
VL 122
IS 4
BP 748
EP 759
DI 10.1037/0735-7044.122.4.748
PG 12
WC Behavioral Sciences; Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Behavioral Sciences; Neurosciences & Neurology
GA 332JT
UT WOS:000258080000002
PM 18729627
DA 2025-04-10
ER

PT J
AU Kang, TH
   Bae, KH
   Yu, MJ
   Kim, WK
   Hwang, HR
   Jung, H
   Lee, PY
   Kang, S
   Yoon, TS
   Park, SG
   Ryu, SE
   Lee, SC
AF Kang, Tae Hyuk
   Bae, Kwang-Hee
   Yu, Min-Jung
   Kim, Won-Kon
   Hwang, Hyang-Ran
   Jung, Hyeyun
   Lee, Phil Young
   Kang, Sunghyun
   Yoon, Tae-Sung
   Park, Sung Goo
   Ryu, Seong Eon
   Lee, Sang Chul
TI Phosphoproteomic analysis of neuronal cell death by glutamate-induced
   oxidative stress
SO PROTEOMICS
LA English
DT Article
DE apoptosis; HT22; oxidative stress; phosphoproteome; ROS
ID NEURODEGENERATIVE DISEASES; PROTEOMIC ANALYSIS; MASS-SPECTROMETRY;
   PHOSPHORYLATION; TOXICITY; APOPTOSIS; NUCLEAR; PHOSPHATASES; ACTIVATION;
   MECHANISMS
AB Oxidative stress is one of the major causes of neuronal cell death in disorders such as perinatal hypoxia and ischemia. Protein phosphorylation is the most significant PTM of proteins and plays an important role in stress-induced signal transduction. Thus, the analysis of alternative protein phosphorylation states which occur during oxidative stress-induced cell death could provide valuable information regarding cell death. In this study, a reference phosphoproteome map of the mouse hippocampal cell line HT22 was constructed based on 125 spots that were identified by MALDI-TOF or LC-ESI-Q-TOF-MS analysis. In addition, proteins of HT22 cells at various stages of oxidative stress-induced cell death were separated by 2-DE and alterations in phospho-proteins were detected by Pro-Q Diamond staining. A total of 17 spots showing significant quantitative changes and. seven newly appearing spots were identified after glutamate treatment. Splicing factor 2, peroxiredoxin 2, S100 calcium binding protein All, and purine nucleoside phosphorylase were identified as up- or down-regulated proteins. CDC25A, caspase-8, and cyp51 protein appeared during oxidative stress-induced cell death. The data in this study from phosphoproteomic analysis provide a valuable resource for the understanding of HT22 cell death mechanisms mediated by oxidative stress.
C1 KRIBB, Translat Res Ctr, Taejon 305806, South Korea.
   KRIBB, Syst Proteom Res Ctr, Taejon 305806, South Korea.
C3 Korea Research Institute of Bioscience & Biotechnology (KRIBB); Korea
   Research Institute of Bioscience & Biotechnology (KRIBB)
RP Lee, SC (corresponding author), KRIBB, Translat Res Ctr, 52 Eoeun Dong, Taejon 305806, South Korea.
EM ryuse@kribb.re.kr; lesach@kribb.re.kr
OI Kang, Sunghyun/0000-0003-1542-9750; Bae, Kwang-Hee/0000-0002-5868-2556
CR Alvarado-Kristensson M, 2004, J EXP MED, V199, P449, DOI 10.1084/jem.20031771
   BEAL MF, 1995, ANN NEUROL, V38, P357, DOI 10.1002/ana.410380304
   Beausoleil SA, 2004, P NATL ACAD SCI USA, V101, P12130, DOI 10.1073/pnas.0404720101
   Blagoev B, 2004, NAT BIOTECHNOL, V22, P1139, DOI 10.1038/nbt1005
   Boutros R, 2006, CURR OPIN CELL BIOL, V18, P185, DOI 10.1016/j.ceb.2006.02.003
   Chandra J, 2000, FREE RADICAL BIO MED, V29, P323, DOI 10.1016/S0891-5849(00)00302-6
   Chen ZhaoYuan, 2004, J Biomol Tech, V15, P249
   Dawson VL, 2004, J BIOENERG BIOMEMBR, V36, P287, DOI 10.1023/B:JOBB.0000041755.22613.8d
   Erion MD, 1997, BIOCHEMISTRY-US, V36, P11725, DOI 10.1021/bi961969w
   Ficarro SB, 2002, NAT BIOTECHNOL, V20, P301, DOI 10.1038/nbt0302-301
   Harding HP, 2005, CELL METAB, V2, P361, DOI 10.1016/j.cmet.2005.11.005
   Huber LA, 2003, CIRC RES, V92, P962, DOI 10.1161/01.RES.0000071748.48338.25
   HUNTER T, 1995, CELL, V80, P225, DOI 10.1016/0092-8674(95)90405-0
   Jin M, 2006, PROTEOME SCI, V4, DOI 10.1186/1477-5956-4-16
   Kang DH, 2002, B KOREAN CHEM SOC, V23, P1511
   Kang S, 2007, CELL MOL BIOL LETT, V12, P139, DOI 10.2478/s11658-006-0057-8
   Kho CW, 2006, BIOCHEM BIOPH RES CO, V348, P25, DOI 10.1016/j.bbrc.2006.06.067
   KRLUME DE, 2003, CURR OPIN CHEM BIOL, V7, P64
   Laugesen S, 2006, PHYTOCHEMISTRY, V67, P2208, DOI 10.1016/j.phytochem.2006.07.010
   Lee Y, 2007, PROTEOMICS, V7, P185, DOI 10.1002/pmic.200600644
   Luo Y, 2006, J BIOL CHEM, V281, P16436, DOI 10.1074/jbc.M512430200
   Maher P, 1996, J NEUROSCI, V16, P6394
   Morandell S, 2006, PROTEOMICS, V6, P4047, DOI 10.1002/pmic.200600058
   Nühse TS, 2003, MOL CELL PROTEOMICS, V2, P1234, DOI 10.1074/mcp.T300006-MCP200
   Pettmann B, 1998, NEURON, V20, P633, DOI 10.1016/S0896-6273(00)81004-1
   Raggiaschi R, 2005, BIOSCIENCE REP, V25, P33, DOI 10.1007/s10540-005-2846-0
   Reinders J, 2005, PROTEOMICS, V5, P4052, DOI 10.1002/pmic.200401289
   Rhee SG, 2005, ANTIOXID REDOX SIGN, V7, P619, DOI 10.1089/ars.2005.7.619
   Rössler OG, 2004, J NEUROCHEM, V88, P1240, DOI 10.1046/j.1471-4159.2003.02255.x
   Sakaguchi M, 2004, J CELL BIOL, V164, P979, DOI 10.1083/jcb.200312041
   Sanford JR, 2005, P NATL ACAD SCI USA, V102, P15042, DOI 10.1073/pnas.0507827102
   Simonian NA, 1996, ANNU REV PHARMACOL, V36, P83, DOI 10.1146/annurev.pa.36.040196.000503
   Sohn H, 2006, FASEB J, V20, P1248, DOI 10.1096/fj.05-4911fje
   Stanciu M, 2000, J BIOL CHEM, V275, P12200, DOI 10.1074/jbc.275.16.12200
   Steinberg TH, 2003, PROTEOMICS, V3, P1128, DOI 10.1002/pmic.200300434
   Tan Shirlee, 2001, Current Topics in Medicinal Chemistry, V1, P497, DOI 10.2174/1568026013394741
   Tan SL, 1998, J NEUROCHEM, V71, P95
   Taylor SW, 2003, TRENDS BIOTECHNOL, V21, P82, DOI 10.1016/S0167-7799(02)00037-9
   Velazquez-Dones A, 2005, J BIOL CHEM, V280, P41761, DOI 10.1074/jbc.M504156200
   Zhang YM, 2006, BMC NEUROSCI, V7, DOI 10.1186/1471-2202-7-49
   Zitzler J, 2004, MOL CELL PROTEOMICS, V3, P834, DOI 10.1074/mcp.M400054-MCP200
NR 41
TC 32
Z9 34
U1 0
U2 2
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 1615-9853
EI 1615-9861
J9 PROTEOMICS
JI Proteomics
PD AUG
PY 2007
VL 7
IS 15
BP 2624
EP 2635
DI 10.1002/pmic.200601028
PG 12
WC Biochemical Research Methods; Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 198SK
UT WOS:000248647600014
PM 17610204
DA 2025-04-10
ER

PT J
AU Sather, S
   Kenyon, KD
   Lefkowitz, JB
   Liang, XY
   Varnum, BC
   Henson, PM
   Graham, DK
AF Sather, Susan
   Kenyon, Karla D.
   Lefkowitz, Jerry B.
   Liang, Xiayuan
   Varnum, Brian C.
   Henson, Peter M.
   Graham, Douglas K.
TI A soluble form of the Mer receptor tyrosine kinase inhibits macrophage
   clearance of apoptotic cells and platelet aggregation
SO BLOOD
LA English
DT Article
ID TUMOR-NECROSIS-FACTOR; C-MER; CLEAVAGE SITE; PROTEOLYTIC CLEAVAGE;
   EXPRESSION ANALYSIS; SURFACE PROTEINS; RCS RAT; GENE 6; V-RYK; GAS6
AB Membrane-bound receptors generate soluble ligand-binding domains either by proteolytic cleavage of the extracellular domain or alternative mRNA splicing yielding a secreted protein. Mertk (Mer) is in a receptor tyrosine kinase family with Axl and Tyro-3, and all 3 receptors share the Gas6 ligand. Mer regulates macrophage activation, promotes apoptotic cell engulfment, and supports platelet aggregation and clot stability in vivo. We have found that the membrane-bound Mer protein is cleaved in the extracellular domain via a metalloproteinase. The cleavage results in the production of a soluble Mer protein released in a constitutive manner from cultured cells. Significant amounts of the soluble Mer protein were also detected in human plasma, suggesting its physiologic relevance. Cleavage of Mer was enhanced by treatment with LIPS and PMA and was specifically inhibited by a tumor necrosis factor alpha-converting enzyme metalloproteinase inhibitor. As a decoy receptor for Gas6, soluble Mer prevented Gas6-mediated stimulation of membrane-bound Mer. The inhibition of Gas6 activity by soluble Mer led to defective macrophage-mediated engulfment of apoptotic cells. Furthermore, soluble Mer decreased platelet aggregation in vitro and prevented fatal collagen/epinephrine-induced thromboembolism in mice, suggesting a potential therapeutic use for soluble Mer in the treatment of clotting disorders.
C1 Univ Colorado Denver & Hlth Sci Ctr, Dept Pediat, Aurora, CO 80045 USA.
   Natl Jewish Med & Res Ctr, Dept Pediat, Denver, CO USA.
   Univ Colorado Denver & Hlth Sci Ctr, Dept Pathol, Aurora, CO 80045 USA.
   Amgen Inc, Thousand Oaks, CA 91320 USA.
C3 University of Colorado System; University of Colorado Anschutz Medical
   Campus; National Jewish Health; University of Colorado System;
   University of Colorado Anschutz Medical Campus; Amgen
RP Graham, DK (corresponding author), Univ Colorado Denver & Hlth Sci Ctr, Dept Pediat, Mail Stop 8302,POB 6511, Aurora, CO 80045 USA.
EM doug.graham@uchsc.edu
OI Graham, Douglas/0000-0002-6201-6900
FU NIGMS NIH HHS [GM061031, R01 GM061031] Funding Source: Medline
CR ADERKA D, 1992, J EXP MED, V175, P323, DOI 10.1084/jem.175.2.323
   Angelillo-Scherrer A, 2005, J CLIN INVEST, V115, P237, DOI 10.1172/JCI200522079
   Angelillo-Scherrer A, 2001, NAT MED, V7, P215, DOI 10.1038/84667
   Black RA, 1997, NATURE, V385, P729, DOI 10.1038/385729a0
   Blobel CP, 2005, NAT REV MOL CELL BIO, V6, P32, DOI 10.1038/nrm1548
   Budagian V, 2005, MOL CELL BIOL, V25, P9324, DOI 10.1128/MCB.25.21.9324-9339.2005
   Camenisch TD, 1999, J IMMUNOL, V162, P3498
   Chen CL, 2004, ARTERIOSCL THROM VAS, V24, P1118, DOI 10.1161/01.ATV.0000130662.30537.08
   Chen J, 1997, ONCOGENE, V14, P2033, DOI 10.1038/sj.onc.1201039
   Cohen PL, 2002, J EXP MED, V196, P135, DOI 10.1084/jem.20012094
   Correll PH, 2004, J LEUKOCYTE BIOL, V75, P731, DOI 10.1189/jlb.0703347
   Costa M, 1996, J CELL PHYSIOL, V168, P737, DOI 10.1002/(SICI)1097-4652(199609)168:3<737::AID-JCP27>3.0.CO;2-U
   Cui XL, 2003, J IMMUNOL, V171, P6814, DOI 10.4049/jimmunol.171.12.6814
   D'Cruz PM, 2000, HUM MOL GENET, V9, P645, DOI 10.1093/hmg/9.4.645
   Ek S, 2002, CANCER RES, V62, P4398
   Evans CO, 2001, J CLIN ENDOCR METAB, V86, P3097, DOI 10.1210/jc.86.7.3097
   Gal A, 2000, NAT GENET, V26, P270, DOI 10.1038/81555
   Georgescu MM, 1999, MOL CELL BIOL, V19, P1171
   Graham DK, 2006, CLIN CANCER RES, V12, P2662, DOI 10.1158/1078-0432.CCR-05-2208
   GRAHAM DK, 1994, CELL GROWTH DIFFER, V5, P647
   GRAHAM DK, 1995, ONCOGENE, V10, P2349
   GULTRIDGE KL, 2002, J BIOL CHEM, V277, P24057
   Guo L, 2002, MOL CELL PROTEOMICS, V1, P30, DOI 10.1074/mcp.M100020-MCP200
   Heaney ML, 1996, BLOOD, V87, P847, DOI 10.1182/blood.V87.3.847.bloodjournal873847
   Heaney ML, 1998, J LEUKOCYTE BIOL, V64, P135, DOI 10.1002/jlb.64.2.135
   Hooper NM, 1997, BIOCHEM J, V321, P265, DOI 10.1042/bj3210265
   JIA R, 1992, J VIROL, V66, P5975, DOI 10.1128/JVI.66.10.5975-5987.1992
   JIA R, 1994, J BIOL CHEM, V269, P1839
   Keating AK, 2006, ONCOGENE, V25, P6092, DOI 10.1038/sj.onc.1209633
   Khan J, 1999, P NATL ACAD SCI USA, V96, P13264, DOI 10.1073/pnas.96.23.13264
   Kruse MN, 2004, BIOCHEM J, V378, P383, DOI 10.1042/BJ20031163
   LAI C, 1994, ONCOGENE, V9, P2567
   Lemke G, 2003, CURR OPIN IMMUNOL, V15, P31, DOI 10.1016/S0952-7915(02)00016-X
   LING L, 1995, MOL CELL BIOL, V15, P6582
   LUNDWALL A, 1986, P NATL ACAD SCI USA, V83, P6716, DOI 10.1073/pnas.83.18.6716
   Mark MR, 1996, J BIOL CHEM, V271, P9785, DOI 10.1074/jbc.271.16.9785
   MIGAKI GI, 1995, J EXP MED, V182, P549, DOI 10.1084/jem.182.2.549
   MOHLER KM, 1994, NATURE, V370, P218, DOI 10.1038/370218a0
   MULLBERG J, 1994, J IMMUNOL, V152, P4958
   Mullberg J, 1997, FEBS LETT, V401, P235, DOI 10.1016/S0014-5793(96)01480-9
   Nagata K, 1996, J BIOL CHEM, V271, P30022, DOI 10.1074/jbc.271.47.30022
   Nakano T, 1997, J BIOL CHEM, V272, P29411, DOI 10.1074/jbc.272.47.29411
   OBRYAN JP, 1995, J BIOL CHEM, V270, P551, DOI 10.1074/jbc.270.2.551
   OBRYAN JP, 1991, MOL CELL BIOL, V11, P5016, DOI 10.1128/MCB.11.10.5016
   OHASHI K, 1994, ONCOGENE, V9, P699
   ROSEJOHN S, 1994, BIOCHEM J, V300, P281, DOI 10.1042/bj3000281
   Rovida E, 2001, J IMMUNOL, V166, P1583, DOI 10.4049/jimmunol.166.3.1583
   Scott RS, 2001, NATURE, V411, P207, DOI 10.1038/35075603
   STITT TN, 1995, CELL, V80, P661, DOI 10.1016/0092-8674(95)90520-0
   Tang P, 1996, BIOCHEMISTRY-US, V35, P8226, DOI 10.1021/bi952183l
   Wang XD, 2002, J BIOL CHEM, V277, P50510, DOI 10.1074/jbc.M208738200
   Wu CW, 2002, ANTICANCER RES, V22, P1071
NR 52
TC 267
Z9 316
U1 0
U2 19
PU AMER SOC HEMATOLOGY
PI WASHINGTON
PA 1900 M STREET. NW SUITE 200, WASHINGTON, DC 20036 USA
SN 0006-4971
J9 BLOOD
JI Blood
PD FEB 1
PY 2007
VL 109
IS 3
BP 1026
EP 1033
DI 10.1182/blood-2006-05-021634
PG 8
WC Hematology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Hematology
GA 135CX
UT WOS:000244132800034
PM 17047157
OA Green Published, Bronze
DA 2025-04-10
ER

PT J
AU Melby, JA
   Roberts, DS
   Larson, EJ
   Brown, KA
   Bayne, EF
   Jin, S
   Ge, Y
AF Melby, Jake A.
   Roberts, David S.
   Larson, Eli J.
   Brown, Kyle A.
   Bayne, Elizabeth F.
   Jin, Song
   Ge, Ying
TI Novel Strategies to Address the Challenges in Top-Down Proteomics
SO JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
LA English
DT Article
ID SIZE-EXCLUSION CHROMATOGRAPHY; INTEGRAL MEMBRANE-PROTEINS;
   HYDROPHOBIC-INTERACTION CHROMATOGRAPHY; ELECTRON-CAPTURE DISSOCIATION;
   TANDEM MASS-SPECTROMETRY; PHASE LIQUID-CHROMATOGRAPHY; CARDIAC
   TROPONIN-I; EXTRACELLULAR-MATRIX; INTACT PROTEINS; COMPATIBLE SURFACTANT
AB Top-down mass spectrometry (MS)-based proteomics is a powerful technology for comprehensively characterizing proteoforms to decipher post-translational modifications (PTMs) together with genetic variations and alternative splicing isoforms toward a proteome-wide understanding of protein functions. In the past decade, top-down proteomics has experienced rapid growth benefiting from groundbreaking technological advances, which have begun to reveal the potential of top-down proteomics for understanding basic biological functions, unraveling disease mechanisms, and discovering new biomarkers. However, many challenges remain to be comprehensively addressed. In this Account & Perspective, we discuss the major challenges currently facing the top-down proteomics field, particularly in protein solubility, proteome dynamic range, proteome complexity, data analysis, proteoform-function relationship, and analytical throughput for precision medicine. We specifically review the major technology developments addressing these challenges with an emphasis on our research group's efforts, induding the development of top-down MS-compatible surfactants for protein solubilization, functionalized nanoparticles for the enrichment of low-abundance proteoforms, strategies for multidimensional chromatography separation of proteins, and a new comprehensive user-friendly software package for top-down proteomics. We have also made efforts to connect proteoforms with biological functions and provide our visions on what the future holds for top-down proteomics.
C1 [Melby, Jake A.; Roberts, David S.; Larson, Eli J.; Brown, Kyle A.; Bayne, Elizabeth F.; Jin, Song; Ge, Ying] Univ Wisconsin, Dept Chem, Madison, WI 53706 USA.
   [Brown, Kyle A.] Univ Wisconsin, Dept Surg, Madison, WI 53705 USA.
   [Ge, Ying] Univ Wisconsin, Dept Cell & Regenerat Biol, Madison, WI 53705 USA.
   [Ge, Ying] Univ Wisconsin, Human Prote Program, Madison, WI 53705 USA.
C3 University of Wisconsin System; University of Wisconsin Madison;
   University of Wisconsin System; University of Wisconsin Madison;
   University of Wisconsin System; University of Wisconsin Madison;
   University of Wisconsin System; University of Wisconsin Madison
RP Ge, Y (corresponding author), Univ Wisconsin, Dept Chem, Madison, WI 53706 USA.; Ge, Y (corresponding author), Univ Wisconsin, Dept Cell & Regenerat Biol, Madison, WI 53705 USA.; Ge, Y (corresponding author), Univ Wisconsin, Human Prote Program, Madison, WI 53705 USA.
EM ying.ge@wisc.edu
RI Jin, Song/B-4300-2008; Roberts, David/GQQ-2773-2022
OI Ge, Ying/0000-0001-5211-6812; Jin, Song/0000-0001-8693-7010; Roberts,
   David/0000-0002-0478-4987; Larson, Eli/0000-0002-1354-0722; Melby,
   Jake/0000-0003-1499-9508
FU National Institutes of Health (NIH) [R01 HL096971, R01 HL109810, R01
   GM117058, R01 GM125085, S10 OD018475]; Training Program in Translational
   Cardiovascular Science [T32 HL007936-20, T32 HL007936-19]; American
   Heart Association [832615]; Vascular Surgery Research Training Program
   grant [T32HL110853]; Biemann Medal Award; National Heart Lung and Blood
   Institute [T32HL110853, R01HL109810, R01HL096971] Funding Source: NIH
   RePORTER; National Institute of General Medical Sciences [R01GM125085]
   Funding Source: NIH RePORTER; American Heart Association (AHA) [832615]
   Funding Source: American Heart Association (AHA)
FX We would like to acknowledge the funding from the National Institutes of
   Health (NIH) R01s, HL096971, HL109810, GM117058, GM125085, and S10
   OD018475. J.A.M. would like to acknowledge support from the Training
   Program in Translational Cardiovascular Science, T32 HL007936-20. D.S.R.
   would like to acknowledge support from the American Heart Association
   Predoctoral Fellowship Grant No. 832615/David S. Roberts/2021. K.A.B.
   would like to acknowledge the Training Program in Translational
   Cardiovascular Science, T32 HL007936-19, and the Vascular Surgery
   Research Training Program grant, T32HL110853. Y.G. would like to
   acknowledge all of the current and former group members as well as our
   collaborators who have made significant contributions to the Ge lab's
   development of top-down proteomics which culminated in this Biemann
   Medal Award.
CR Abbatiello SE, 2015, MOL CELL PROTEOMICS, V14, P2357, DOI 10.1074/mcp.M114.047050
   Aebersold R, 2018, NAT CHEM BIOL, V14, P206, DOI [10.1038/NCHEMBIO.2576, 10.1038/nchembio.2576]
   Aebersold R, 2016, NATURE, V537, P347, DOI 10.1038/nature19949
   ALPERT AJ, 1986, J CHROMATOGR, V359, P85, DOI 10.1016/0021-9673(86)80064-4
   Anderson NL, 2002, MOL CELL PROTEOMICS, V1, P845, DOI 10.1074/mcp.R200007-MCP200
   Ansong C, 2013, P NATL ACAD SCI USA, V110, P10153, DOI 10.1073/pnas.1221210110
   Armirotti A, 2010, PROTEOMICS, V10, P3566, DOI 10.1002/pmic.201000245
   Astefanei A, 2017, CHROMATOGRAPHIA, V80, P665, DOI 10.1007/s10337-016-3168-z
   Baghdady YZ, 2019, ANAL CHEM, V91, P11085, DOI 10.1021/acs.analchem.9b01665
   Baker ES, 2015, PROTEOMICS, V15, P2766, DOI 10.1002/pmic.201500048
   Baker M, 2015, NATURE, V521, P274, DOI 10.1038/521274a
   Bantscheff M, 2012, ANAL BIOANAL CHEM, V404, P939, DOI 10.1007/s00216-012-6203-4
   Barrera NP, 2011, ANNU REV BIOCHEM, V80, P247, DOI 10.1146/annurev-biochem-062309-093307
   Bauer A, 2003, EUR J BIOCHEM, V270, P570, DOI 10.1046/j.1432-1033.2003.03428.x
   Bolla JR, 2019, ANNU REV BIOCHEM, V88, P85, DOI 10.1146/annurev-biochem-013118-111508
   Bourgoin-Voillard S, 2014, PROTEOMICS, V14, P1174, DOI 10.1002/pmic.201300433
   Bradbury A, 2015, NATURE, V518, P27, DOI 10.1038/518027a
   Brown KA, 2020, EXPERT REV PROTEOMIC, V17, P719, DOI 10.1080/14789450.2020.1855982
   Brown KA, 2020, ANGEW CHEM INT EDIT, V59, P8406, DOI 10.1002/anie.201915374
   Brown KA, 2019, NAT METHODS, V16, P417, DOI 10.1038/s41592-019-0391-1
   Brunner A.D., 2020, Ultra-high sensitivity mass spectrometry quantifies single
   Cai WX, 2019, CIRC RES, V125, P936, DOI 10.1161/CIRCRESAHA.119.315305
   Cai WX, 2017, ANAL CHEM, V89, P5467, DOI 10.1021/acs.analchem.7b00380
   Cai WX, 2016, EXPERT REV PROTEOMIC, V13, P717, DOI 10.1080/14789450.2016.1209414
   Cai WX, 2016, MOL CELL PROTEOMICS, V15, P703, DOI 10.1074/mcp.O115.054387
   Carel C, 2017, P NATL ACAD SCI USA, V114, P4231, DOI 10.1073/pnas.1617888114
   Carroll J, 2007, P NATL ACAD SCI USA, V104, P14330, DOI 10.1073/pnas.0706817104
   Catherman AD, 2014, BIOCHEM BIOPH RES CO, V445, P683, DOI 10.1016/j.bbrc.2014.02.041
   Catherman AD, 2013, MOL CELL PROTEOMICS, V12, P3465, DOI 10.1074/mcp.M113.030114
   Catherman AD, 2013, ANAL CHEM, V85, P1880, DOI 10.1021/ac3031527
   Cesnik AJ, 2018, J PROTEOME RES, V17, P568, DOI 10.1021/acs.jproteome.7b00685
   Chait BT, 2006, SCIENCE, V314, P65, DOI 10.1126/science.1133987
   Chamot-Rooke J, 2011, SCIENCE, V331, P778, DOI 10.1126/science.1200729
   Chang YH, 2015, J PROTEOME RES, V14, P1587, DOI 10.1021/pr5012679
   Chen BF, 2018, ANAL CHEM, V90, P7135, DOI 10.1021/acs.analchem.8b01865
   Chen BF, 2018, ANAL CHEM, V90, P110, DOI 10.1021/acs.analchem.7b04747
   Chen BF, 2017, CHEM SCI, V8, P4306, DOI 10.1039/c6sc05435h
   Chen BF, 2016, ANAL CHEM, V88, P1885, DOI 10.1021/acs.analchem.5b04285
   Chen R, 2013, WIRES SYST BIOL MED, V5, P73, DOI 10.1002/wsbm.1198
   Chen X, 2013, PROTEOMICS, V13, P2563, DOI 10.1002/pmic.201200594
   Chen YC, 2015, ANAL CHEM, V87, P8399, DOI 10.1021/acs.analchem.5b01745
   Chen Y, 2016, MOL CELL PROTEOMICS, V15, P818, DOI 10.1074/mcp.M114.046441
   Chorev DS, 2018, SCIENCE, V362, P829, DOI 10.1126/science.aau0976
   Compton PD, 2011, ANAL CHEM, V83, P6868, DOI 10.1021/ac2010795
   Cravatt BF, 2007, NATURE, V450, P991, DOI 10.1038/nature06525
   Cui WD, 2011, ANALYST, V136, P3854, DOI 10.1039/c1an15286f
   Dodds JN, 2019, J AM SOC MASS SPECTR, V30, P2185, DOI 10.1007/s13361-019-02288-2
   Dong XT, 2012, J BIOL CHEM, V287, P848, DOI 10.1074/jbc.M111.293258
   Donnelly DP, 2019, NAT METHODS, V16, P587, DOI 10.1038/s41592-019-0457-0
   Doucette AA, 2011, EXPERT REV PROTEOMIC, V8, P787, DOI [10.1586/EPR.11.67, 10.1586/epr.11.67]
   ELLINGTON AD, 1990, NATURE, V346, P818, DOI 10.1038/346818a0
   Eschelbach JW, 2006, ANAL CHEM, V78, P1697, DOI 10.1021/ac0518304
   Fu Q, 2020, JOVE-J VIS EXP, DOI 10.3791/59842
   Fung YME, 2009, J AM CHEM SOC, V131, P9977, DOI 10.1021/ja8087407
   Füssl F, 2020, ANAL CHEM, V92, P5431, DOI 10.1021/acs.analchem.0c00185
   Gajadhar AS, 2014, CURR OPIN BIOTECH, V28, P83, DOI 10.1016/j.copbio.2013.12.009
   Garcia BA, 2007, NAT METHODS, V4, P487, DOI 10.1038/nmeth1052
   García MC, 2005, J CHROMATOGR B, V825, P111, DOI 10.1016/j.jchromb.2005.03.041
   Gargano AFG, 2018, J PROTEOME RES, V17, P3791, DOI 10.1021/acs.jproteome.8b00458
   Gault J, 2020, NAT METHODS, V17, P505, DOI 10.1038/s41592-020-0821-0
   Ge Y, 2003, J AM SOC MASS SPECTR, V14, P253, DOI 10.1016/S1044-0305(02)00913-3
   Ge Y, 2002, J AM CHEM SOC, V124, P672, DOI 10.1021/ja011335z
   Ge Y, 2009, P NATL ACAD SCI USA, V106, P12658, DOI 10.1073/pnas.0813369106
   Gilda JE, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0135392
   Gregorich ZR, 2016, J PROTEOME RES, V15, P2706, DOI 10.1021/acs.jproteome.6b00244
   Gregorich ZR, 2014, PFLUG ARCH EUR J PHY, V466, P1199, DOI 10.1007/s00424-014-1471-9
   Gregorich ZR, 2014, PROTEOMICS, V14, P1195, DOI 10.1002/pmic.201300432
   Guner H, 2014, J AM SOC MASS SPECTR, V25, P464, DOI 10.1007/s13361-013-0789-4
   Han XM, 2006, SCIENCE, V314, P109, DOI 10.1126/science.1128868
   Hayes R, 2014, J CHROMATOGR A, V1357, P36, DOI 10.1016/j.chroma.2014.05.010
   He LD, 2019, CLIN CHEM, V65, P986, DOI 10.1373/clinchem.2018.295766
   Holt M. V., 2021, CURR PROTOC, V1
   Hood L, 2011, NAT REV CLIN ONCOL, V8, P184, DOI 10.1038/nrclinonc.2010.227
   Horn DM, 2000, ANAL CHEM, V72, P4778, DOI 10.1021/ac000494i
   Hwang L, 2015, J AM CHEM SOC, V137, P2432, DOI 10.1021/ja511833y
   Hynes RO, 2009, SCIENCE, V326, P1216, DOI 10.1126/science.1176009
   Janes KA, 2020, SCI SIGNAL, V13, DOI 10.1126/scisignal.aaz8130
   Jeong K, 2020, CELL SYST, V10, P213, DOI 10.1016/j.cels.2020.01.003
   Jin YT, 2017, ANAL CHEM, V89, P4922, DOI 10.1021/acs.analchem.7b00113
   Jooss K, 2021, ELECTROPHORESIS, V42, P1050, DOI 10.1002/elps.202000317
   Karabacak NM, 2009, MOL CELL PROTEOMICS, V8, P846, DOI 10.1074/mcp.M800099-MCP200
   Karczewski KJ, 2018, NAT REV GENET, V19, P299, DOI 10.1038/nrg.2018.4
   Keener JE, 2021, ANAL CHEM, V93, P583, DOI 10.1021/acs.analchem.0c04342
   Kelleher NL, 2014, EXPERT REV PROTEOMIC, V11, P649, DOI 10.1586/14789450.2014.976559
   Kelleher NL, 2004, ANAL CHEM, V76, p196A, DOI 10.1021/ac0415657
   Kelleher NL, 1999, J AM CHEM SOC, V121, P806, DOI 10.1021/ja973655h
   Knott SJ, 2020, ANAL CHEM, V92, P15693, DOI 10.1021/acs.analchem.0c03104
   Kou Q, 2016, BIOINFORMATICS, V32, P3495, DOI 10.1093/bioinformatics/btw398
   Krueger KE, 2006, MOL CELL PROTEOMICS, V5, P1799, DOI 10.1074/mcp.R600009-MCP200
   Laganowsky A, 2013, NAT PROTOC, V8, P639, DOI 10.1038/nprot.2013.024
   LeDuc RD, 2004, NUCLEIC ACIDS RES, V32, pW340, DOI 10.1093/nar/gkh447
   Leney AC, 2017, J AM SOC MASS SPECTR, V28, P5, DOI 10.1007/s13361-016-1545-3
   Li HL, 2018, NAT CHEM, V10, P139, DOI [10.1038/nchem.2908, 10.1038/NCHEM.2908]
   Li YH, 2012, ANAL CHEM, V84, P1617, DOI 10.1021/ac202899p
   Liang Y, 2019, ANAL CHEM, V91, P1743, DOI 10.1021/acs.analchem.8b05817
   Lin ZQ, 2019, MOL CELL PROTEOMICS, V18, P594, DOI 10.1074/mcp.TIR118.001086
   Lindsey ML, 2018, EXPERT REV PROTEOMIC, V15, P105, DOI 10.1080/14789450.2018.1421947
   Liu XW, 2012, MOL CELL PROTEOMICS, V11, DOI 10.1074/mcp.M111.008524
   Lollo B, 2014, PROTEOMICS, V14, P638, DOI 10.1002/pmic.201300187
   LOO JA, 1990, SCIENCE, V248, P201, DOI 10.1126/science.2326633
   LOO RRO, 1994, PROTEIN SCI, V3, P1975, DOI 10.1002/pro.5560031109
   Mack S, 2019, ELECTROPHORESIS, V40, P3084, DOI 10.1002/elps.201900325
   Madian AG, 2013, ANAL CHEM, V85, P737, DOI 10.1021/ac302071k
   Mann M, 2003, NAT BIOTECHNOL, V21, P255, DOI 10.1038/nbt0303-255
   Maron BJ, 2013, LANCET, V381, P242, DOI 10.1016/S0140-6736(12)60397-3
   Marshall AG, 2008, ANNU REV ANAL CHEM, V1, P579, DOI 10.1146/annurev.anchem.1.031207.112945
   Marty MT, 2015, ANAL CHEM, V87, P4370, DOI 10.1021/acs.analchem.5b00140
   Marx V, 2013, NAT METHODS, V10, P829, DOI 10.1038/nmeth.2607
   McCool EN, 2018, ANAL CHEM, V90, P5529, DOI 10.1021/acs.analchem.8b00693
   McIlwain SJ, 2020, J AM SOC MASS SPECTR, V31, P1104, DOI 10.1021/jasms.0c00035
   Mehaffey MR, 2020, ANAL CHEM, V92, P15202, DOI 10.1021/acs.analchem.0c03784
   Melby JA, 2021, J PROTEOME RES, V20, P1424, DOI 10.1021/acs.jproteome.0c00830
   Meng FY, 2001, NAT BIOTECHNOL, V19, P952, DOI 10.1038/nbt1001-952
   Meng FY, 2002, ANAL CHEM, V74, P2923, DOI 10.1021/ac020049i
   MOORE AW, 1995, ANAL CHEM, V67, P3456, DOI 10.1021/ac00115a014
   Mouw JK, 2014, NAT REV MOL CELL BIO, V15, P771, DOI 10.1038/nrm3902
   Muneeruddin K, 2015, ANAL CHEM, V87, P10138, DOI 10.1021/acs.analchem.5b02982
   Naba A, 2012, MOL CELL PROTEOMICS, V11, DOI 10.1074/mcp.M111.014647
   Nedelkov D, 2018, J PROTEOMICS, V175, P27, DOI 10.1016/j.jprot.2017.08.001
   Niu L., 2020, BIORXIV, DOI 10.1101/ 2020.10.16.337592
   Nshanian M, 2019, J AM SOC MASS SPECTR, V30, P16, DOI 10.1007/s13361-018-2027-6
   Ntai I, 2018, P NATL ACAD SCI USA, V115, P4140, DOI 10.1073/pnas.1716122115
   Park J, 2017, NAT METHODS, V14, P909, DOI [10.1038/NMETH.4388, 10.1038/nmeth.4388]
   Peng Y, 2014, MOL CELL PROTEOMICS, V13, P2752, DOI 10.1074/mcp.M114.040675
   Picotti P, 2009, CELL, V138, P795, DOI 10.1016/j.cell.2009.05.051
   Pirok BWJ, 2019, ANAL CHEM, V91, P240, DOI 10.1021/acs.analchem.8b04841
   Polasky DA, 2020, J AM CHEM SOC, V142, P6750, DOI 10.1021/jacs.0c01076
   Queiroz JA, 2001, J BIOTECHNOL, V87, P143, DOI 10.1016/S0168-1656(01)00237-1
   Reid GE, 2002, J MASS SPECTROM, V37, P663, DOI 10.1002/jms.346
   Rifai N, 2006, NAT BIOTECHNOL, V24, P971, DOI 10.1038/nbt1235
   Riley NM, 2017, J PROTEOME RES, V16, P2653, DOI 10.1021/acs.jproteome.7b00249
   Roberts DS, 2019, NANO RES, V12, P1473, DOI 10.1007/s12274-019-2418-4
   Ruotolo BT, 2005, SCIENCE, V310, P1658, DOI 10.1126/science.1120177
   Ryan CM, 2010, MOL CELL PROTEOMICS, V9, P791, DOI 10.1074/mcp.M900516-MCP200
   Saveliev SV, 2013, ANAL CHEM, V85, P907, DOI 10.1021/ac302423t
   Schachner LF, 2021, NAT METHODS, V18, P303, DOI 10.1038/s41592-020-01052-9
   Schaffer LV, 2019, PROTEOMICS, V19, DOI 10.1002/pmic.201800361
   Schmitt ND, 2017, J MASS SPECTROM, V52, P480, DOI 10.1002/jms.3953
   Shaw JB, 2013, J AM CHEM SOC, V135, P12646, DOI 10.1021/ja4029654
   Shen XJ, 2021, INT J MASS SPECTROM, V462, DOI 10.1016/j.ijms.2021.116541
   Shen XJ, 2018, ANAL CHEM, V90, P10095, DOI 10.1021/acs.analchem.8b02725
   Siuti N, 2007, NAT METHODS, V4, P817, DOI 10.1038/NMETH1097
   Skinner OS, 2018, NAT CHEM BIOL, V14, P36, DOI [10.1038/NCHEMBIO.2515, 10.1038/nchembio.2515]
   Skinner OS, 2014, ANAL CHEM, V86, P4627, DOI 10.1021/ac500864w
   Smith JG, 2017, CIRCULATION, V135, P1651, DOI 10.1161/CIRCULATIONAHA.116.025446
   Smith L. M., 2020, HUMAN PROTEOFORM PRO, DOI [10.20944/preprints202010.0368.v1, DOI 10.20944/PREPRINTS202010.0368.V1]
   Smith LM, 2018, SCIENCE, V359, P1106, DOI 10.1126/science.aat1884
   Smith LM, 2013, NAT METHODS, V10, P186, DOI 10.1038/nmeth.2369
   Speers AE, 2007, CHEM REV, V107, P3687, DOI 10.1021/cr068286z
   Stolz A, 2019, ELECTROPHORESIS, V40, P79, DOI 10.1002/elps.201800331
   Sun RX, 2016, ANAL CHEM, V88, P3082, DOI 10.1021/acs.analchem.5b03963
   Takemori A, 2020, J PROTEOME RES, V19, P3779, DOI 10.1021/acs.jproteome.0c00303
   Tiambeng TN, 2020, NAT COMMUN, V11, DOI 10.1038/s41467-020-17643-1
   Toby TK, 2017, AM J TRANSPLANT, V17, P2458, DOI 10.1111/ajt.14359
   Toby TK, 2019, NAT PROTOC, V14, P119, DOI 10.1038/s41596-018-0085-7
   Toby TK, 2016, ANNU REV ANAL CHEM, V9, P499, DOI 10.1146/annurev-anchem-071015-041550
   Tran JC, 2011, NATURE, V480, P254, DOI 10.1038/nature10575
   Tran JC, 2009, ANAL CHEM, V81, P6201, DOI 10.1021/ac900729r
   Tucholski T, 2020, P NATL ACAD SCI USA, V117, P24691, DOI 10.1073/pnas.2006764117
   Tucholski T, 2022, MASS SPECTROM REV, V41, P158, DOI 10.1002/mas.21653
   Tucholski T, 2019, ANAL CHEM, V91, P3835, DOI 10.1021/acs.analchem.8b04082
   TUERK C, 1990, SCIENCE, V249, P505, DOI 10.1126/science.2200121
   Uhlen M, 2015, SCIENCE, V347, DOI 10.1126/science.1260419
   Urner LH, 2020, NAT COMMUN, V11, DOI 10.1038/s41467-020-14424-8
   Valeja SG, 2015, ANAL CHEM, V87, P5363, DOI 10.1021/acs.analchem.5b00657
   van den Broek I, 2020, J PROTEOME RES, V19, P2278, DOI 10.1021/acs.jproteome.9b00854
   Van Eyk JE, 2019, J PROTEOME RES, V18, P1, DOI 10.1021/acs.jproteome.8b00504
   Wang T, 2019, BIOTECHNOL ADV, V37, P28, DOI 10.1016/j.biotechadv.2018.11.001
   Wang YH, 2019, ANAL CHEM, V91, P935, DOI 10.1021/acs.analchem.8b03970
   Wang Z, 2020, ANAL CHEM, V92, P12774, DOI 10.1021/acs.analchem.0c03395
   Wang Z, 2018, INT J MASS SPECTROM, V427, P43, DOI 10.1016/j.ijms.2017.09.001
   Washburn MP, 2001, NAT BIOTECHNOL, V19, P242, DOI 10.1038/85686
   Wei LM, 2018, MOL CELL PROTEOMICS, V17, P148, DOI 10.1074/mcp.RA117.000124
   Whitelegge JP, 1998, PROTEIN SCI, V7, P1423, DOI 10.1002/pro.5560070619
   Whitelegge JP, 2013, ANAL CHEM, V85, P2558, DOI 10.1021/ac303064a
   Wisniewski JR, 2009, NAT METHODS, V6, P359, DOI [10.1038/nmeth.1322, 10.1038/NMETH.1322]
   Wu CC, 2003, NAT BIOTECHNOL, V21, P262, DOI 10.1038/nbt0303-262
   Wu ZJ, 2020, J PROTEOME RES, V19, P3867, DOI 10.1021/acs.jproteome.0c00469
   Xie SN, 2009, EXPERT REV PROTEOMIC, V6, P573, DOI 10.1586/EPR.09.74
   Xiu LC, 2014, ANAL CHEM, V86, P7899, DOI 10.1021/ac501836k
   Yang L, 2011, ADV DRUG DELIVER REV, V63, P1361, DOI 10.1016/j.addr.2011.10.002
   Yu YQ, 2003, ANAL CHEM, V75, P6023, DOI 10.1021/ac0346196
   Zamdborg L, 2007, NUCLEIC ACIDS RES, V35, pW701, DOI 10.1093/nar/gkm371
   Zenaidee MA, 2020, J AM SOC MASS SPECTR, V31, P1896, DOI 10.1021/jasms.0c00160
   Zhang J, 2011, J PROTEOME RES, V10, P4054, DOI 10.1021/pr200258m
   Zhang YY, 2013, CHEM REV, V113, P2343, DOI 10.1021/cr3003533
   Zhang ZR, 2014, ANNU REV ANAL CHEM, V7, P427, DOI 10.1146/annurev-anchem-071213-020216
   Zhou MW, 2020, CHEM SCI, V11, DOI 10.1039/d0sc04392c
   Zinnel NF, 2012, ANAL CHEM, V84, P3390, DOI 10.1021/ac300193s
NR 189
TC 120
Z9 136
U1 13
U2 78
PU AMER CHEMICAL SOC
PI WASHINGTON
PA 1155 16TH ST, NW, WASHINGTON, DC 20036 USA
SN 1044-0305
EI 1879-1123
J9 J AM SOC MASS SPECTR
JI J. Am. Soc. Mass Spectrom.
PD JUN 2
PY 2021
VL 32
IS 6
BP 1278
EP 1294
DI 10.1021/jasms.1c00099
EA MAY 2021
PG 17
WC Biochemical Research Methods; Chemistry, Analytical; Chemistry,
   Physical; Spectroscopy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Chemistry; Spectroscopy
GA WR6XK
UT WOS:000714641000002
PM 33983025
DA 2025-04-10
ER

PT J
AU Baltzinger, M
   Mager-Heckel, AM
   Remy, P
AF Baltzinger, M
   Mager-Heckel, AM
   Remy, P
TI Xl erg:: Expression pattern and overexpression during development
   plead for a role in endothelial cell differentiation
SO DEVELOPMENTAL DYNAMICS
LA English
DT Article
DE Xenopus; ets; angiogenesis; migration
ID ETS TRANSCRIPTION FACTORS; IN-SITU HYBRIDIZATION; XI-FLI GENE;
   XENOPUS-LAEVIS; FAMILY; EMBRYOGENESIS; PROTEINS; PROTOONCOGENES;
   EMBRYOS; FUSION
AB The ets gene family encodes transcription factors related to the proto-oncogene c-ets-l and involved in cell proliferation, differentiation, and oncogenic transformation. We have characterized the Xenopus homologue of the human erg gene, an ets-related-gene, and its expression has been examined throughout early embryonic development. XI erg encodes at least two proteins, resulting from alternative splicing events. The transcripts are restricted to the forming endocardium, the endothelial cells of the blood vessels and to the neural crest-derived mesenchyme cells of the pharyngial arches. When Xl ERG; is expressed ectopically in Xenopus embryos by microinjection of synthetic mRNA, multiple developmental defects are observed. Dorsally injected embryos have their AP axis shortened and present severe defects in eye and somite morphogenesis. Ventrally injected embryos show a posteriorization of the cells having received the message together with ectopic endothelial cell differentiation as revealed by the accumulation of X-msr transcripts. In both cases, accumulation of erythrocytes in structures not connected with the blood circulatory system can be observed. Our data suggest that XI erg may be involved in cell motility and in the development of the circulatory system. (C) 1999 Wiley-Liss, Inc.
C1 CNRS, Div Cellulaire & Dev, UPR 9005, F-67084 Strasbourg, France.
C3 Universites de Strasbourg Etablissements Associes; Universite de
   Strasbourg; Centre National de la Recherche Scientifique (CNRS)
RP Baltzinger, M (corresponding author), CNRS, Div Cellulaire & Dev, UPR 9005, 15 Rue Rene Descartes, F-67084 Strasbourg, France.
CR Bassuk AG, 1997, ADV IMMUNOL, V64, P65, DOI 10.1016/S0065-2776(08)60887-1
   Buttice G, 1996, ONCOGENE, V13, P2297
   Carrère S, 1998, ONCOGENE, V16, P3261, DOI 10.1038/sj.onc.1201868
   Delannoy-Courdent A, 1998, J CELL SCI, V111, P1521
   DELATTRE O, 1992, NATURE, V359, P162, DOI 10.1038/359162a0
   Deramaudt BMJM, 1999, J CELL BIOCHEM, V72, P311, DOI 10.1002/(SICI)1097-4644(19990301)72:3<311::AID-JCB1>3.0.CO;2-G
   Devic E, 1996, MECH DEVELOP, V59, P129, DOI 10.1016/0925-4773(96)00585-0
   DHORDAIN P, 1995, MECH DEVELOP, V50, P17, DOI 10.1016/0925-4773(94)00322-E
   Dittmer J, 1998, BBA-REV CANCER, V1377, pF1, DOI 10.1016/S0304-419X(97)00039-5
   DUFOUR S, 1994, J CELL BIOL, V127, P521, DOI 10.1083/jcb.127.2.521
   DUTERQUECOQUILLAUD M, 1993, ONCOGENE, V8, P1865
   GHYSDAEL J, 1997, ONCOGENES TRANSCRIPT, V1, P29
   GLOOR S, 1995, GENE, V160, P213, DOI 10.1016/0378-1119(95)00226-V
   Gory S, 1998, J BIOL CHEM, V273, P6750, DOI 10.1074/jbc.273.12.6750
   Hadeball B, 1998, MECH DEVELOP, V72, P101, DOI 10.1016/S0925-4773(98)00022-7
   HARLAND RM, 1991, METHOD CELL BIOL, V36, P685
   HART AH, 1995, ONCOGENE, V10, P1423
   KNECHT AK, 1995, DEVELOPMENT, V121, P1927
   KOZAK M, 1991, J BIOL CHEM, V266, P19867
   LEMEUR M, 1981, CELL, V23, P561, DOI 10.1016/0092-8674(81)90152-5
   LEPRINCE D, 1983, NATURE, V306, P395, DOI 10.1038/306395a0
   Meyer D, 1997, INT J DEV BIOL, V41, P607
   Meyer D, 1995, INT J DEV BIOL, V39, P909
   MEYER D, 1993, MECH DEVELOP, V44, P109, DOI 10.1016/0925-4773(93)90061-2
   NIEHRS C, 1994, SCIENCE, V263, P817, DOI 10.1126/science.7905664
   PANAGOPOULOS I, 1994, GENE CHROMOSOME CANC, V11, P256, DOI 10.1002/gcc.2870110408
   PRASAD DDK, 1994, ONCOGENE, V9, P669
   RAO VN, 1987, SCIENCE, V237, P635, DOI 10.1126/science.3299708
   Remy P, 1996, INT J DEV BIOL, V40, P577
   RIVERA RR, 1993, MOL CELL BIOL, V13, P7163, DOI 10.1128/MCB.13.11.7163
   Sharrocks AD, 1997, INT J BIOCHEM CELL B, V29, P1371, DOI 10.1016/S1357-2725(97)00086-1
   STIEGLER P, 1990, NUCLEIC ACIDS RES, V18, P5298, DOI 10.1093/nar/18.17.5298
   STIEGLER P, 1993, MECH DEVELOP, V41, P163, DOI 10.1016/0925-4773(93)90046-Z
   Thomsen GH, 1996, DEVELOPMENT, V122, P2359
   Wasylyk B, 1998, TRENDS BIOCHEM SCI, V23, P213, DOI 10.1016/S0968-0004(98)01211-0
   WASYLYK B, 1993, EUR J BIOCHEM, V211, P7, DOI 10.1111/j.1432-1033.1993.tb19864.x
   WOLFF CM, 1991, CELL GROWTH DIFFER, V2, P447
   ZUCMAN J, 1993, EMBO J, V12, P4481, DOI 10.1002/j.1460-2075.1993.tb06137.x
NR 38
TC 69
Z9 79
U1 0
U2 4
PU WILEY-LISS
PI NEW YORK
PA DIV JOHN WILEY & SONS INC, 605 THIRD AVE, NEW YORK, NY 10158-0012 USA
SN 1058-8388
J9 DEV DYNAM
JI Dev. Dyn.
PD DEC
PY 1999
VL 216
IS 4-5
BP 420
EP 433
DI 10.1002/(SICI)1097-0177(199912)216:4/5<420::AID-DVDY10>3.0.CO;2-C
PG 14
WC Anatomy & Morphology; Developmental Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Anatomy & Morphology; Developmental Biology
GA 264GC
UT WOS:000084171400010
PM 10633861
DA 2025-04-10
ER

PT J
AU Yang, F
   Jiang, XY
   Zhu, YH
   Lee, MY
   Xu, ZR
   Zhang, JL
   Li, Q
   Lin, MY
   Wang, HJ
   Lin, ZM
AF Yang, Fang
   Jiang, Xingyuan
   Zhu, Yuhao
   Lee, Mingyang
   Xu, Zhengren
   Zhang, Jianglin
   Li, Qian
   Lin, Mao-Ying
   Wang, Huijun
   Lin, Zhimiao
TI Biallelic Variants in Lanosterol Synthase (LSS) Cause
   Palmoplantar Keratoderma- Congenital Alopecia Syndrome Type 2
SO JOURNAL OF INVESTIGATIVE DERMATOLOGY
LA English
DT Article
ID MUTATIONS
AB Palmoplantar keratoderma-congenital alopecia syndrome type 2 is an autosomal recessive disorder with an unknown genetic basis. In this study, we identified biallelic variants in the LSS gene in two unrelated palmo-plantar keratoderma-congenital alopecia syndrome type 2 cases (c.3G > A, p.Met1? and c.1025T > G, p.Ile342Ser in patient 1; c.1522G > T, p.Gly508Trp and c.428+42T > A in patient 2) presenting with additional clinical features, including early-onset cataracts, pseudoainhum, and agenesis of the corpus callosum. LSS encodes lanosterol synthase (LSS), which functions in the cholesterol biosynthesis pathway by converting (S)-2,3-oxidosqualene to lanosterol. The c.3G > A variant resulted in an alternative translation initiation at residue Met81, producing an N-terminal truncated protein (LSS-delta N80), as shown by immunoblotting. The c.428+42T > A variant introduced a potential splicing site, leading to a premature stop codon. Ex vivo studies revealed downregulation of LSS in both patients. Remarkably decreased lanosterol levels were found in vitro in three LSS variants, LSS-delta N80, p.Ile342Ser, and p.Gly508Trp, suggesting a loss of enzymatic activity. Transmission electron microscopy and immunofluorescence showed abnormal cornified envelope formation in the stratum corneum of the patients. Taken together, our findings indicate LSS as a causative gene for palmoplantar keratoderma-congenital alopecia syndrome type 2, which emphasizes the importance of the cholesterol synthesis pathway in human skin cornification.
C1 [Yang, Fang; Jiang, Xingyuan; Lee, Mingyang; Lin, Zhimiao] Peking Univ First Hosp, Dept Dermatol, Beijing, Peoples R China.
   [Yang, Fang; Jiang, Xingyuan; Lee, Mingyang] Beijing Key Lab Mol Diag Dermatoses, Beijing, Peoples R China.
   [Yang, Fang; Jiang, Xingyuan; Lee, Mingyang] Natl Clin Res Ctr Skin & Immune Dis, Beijing, Peoples R China.
   [Yang, Fang; Zhang, Jianglin] Jinan Univ, Shenzhen Peoples Hosp, Clin Med Coll 2, Dept Dermatol, Shenzhen, Peoples R China.
   [Yang, Fang; Zhang, Jianglin] Southern Univ Sci & Technol, Affiliated Hosp 1, Shenzhen, Peoples R China.
   [Yang, Fang; Zhang, Jianglin] Natl Clin Res Ctr Skin Dis, Candidate Branch, Shenzhen, Peoples R China.
   [Zhu, Yuhao; Xu, Zhengren] Peking Univ, Sch Pharmaceut Sci, State Key Lab Nat & Biomimet Drugs, Beijing, Peoples R China.
   [Li, Qian] Natl Human Genet Resources Ctr, Natl Res Inst Family Planning, Beijing, Peoples R China.
   [Lin, Mao-Ying; Lin, Zhimiao] Xiamen Chang Gung Hosp, Dept Dermatol, Xiamen, Peoples R China.
   [Wang, Huijun; Lin, Zhimiao] Southern Med Univ, Dermatol Hosp, Guangzhou 510091, Peoples R China.
C3 Peking University; Jinan University; Southern University of Science &
   Technology; Peking University; Southern Medical University - China
RP Lin, ZM (corresponding author), Southern Med Univ, Dermatol Hosp, Guangzhou 510091, Peoples R China.
EM zhimiaolin@bjmu.edu.cn
RI Jiang-lin, Zhang/ABC-3073-2020; Jiang, Xingyuan/JHT-7111-2023
OI ZHU, Yuhao/0000-0003-0192-0290; Jianglin, Zhang/0000-0003-0434-1729;
   Lee, Ming Yang/0000-0003-3135-3928; Wang, Huijun/0000-0001-5414-1472;
   Yang, Fang/0000-0003-4390-677X; Xu, Zhengren/0000-0001-7302-6488; Lin,
   Zhimiao/0000-0001-9323-2035; Jiang, Xingyuan/0000-0002-9891-6353
FU National Natural Science Foundation of China;  [81872515];  [82073423]; 
   [82003327]
FX ACKNOWLEDGMENTS We are thankful to all the participants and their family
   members in this study. This work was supported by the National Natural
   Science Foundation of China (grant numbers 81872515, 82073423, and
   82003327) .
CR Atzmony L, 2020, J AM ACAD DERMATOL, V82, P123, DOI 10.1016/j.jaad.2019.08.043
   Besnard T, 2019, GENET MED, V21, P2025, DOI 10.1038/s41436-019-0445-x
   Caengprasath N, 2021, J TRANSL MED, V19, DOI 10.1186/s12967-021-02779-5
   Castori M, 2016, CLIN EXP DERMATOL, V41, P632, DOI 10.1111/ced.12857
   Chen XD, 2017, J PEDIATR ENDOCR MET, V30, P1231, DOI 10.1515/jpem-2017-0101
   Clements SE, 2010, BRIT J DERMATOL, V163, P624, DOI 10.1111/j.1365-2133.2010.09859.x
   Hua SY, 2021, J DERMATOL, V48, P408, DOI 10.1111/1346-8138.15697
   Huff MW, 2005, TRENDS PHARMACOL SCI, V26, P335, DOI 10.1016/j.tips.2005.05.004
   Lamari F, 2013, J INHERIT METAB DIS, V36, P411, DOI 10.1007/s10545-012-9509-7
   Li FC, 2019, J DERMATOL, V46, pE393, DOI 10.1111/1346-8138.15010
   Lin ZM, 2012, AM J HUM GENET, V90, P558, DOI 10.1016/j.ajhg.2012.02.006
   Murata M, 2021, J DERMATOL, V48, P392, DOI 10.1111/1346-8138.15679
   Paller AS, 2011, J INVEST DERMATOL, V131, P2242, DOI 10.1038/jid.2011.189
   Petrof G, 2012, BRIT J DERMATOL, V166, P36, DOI 10.1111/j.1365-2133.2011.10640.x
   Romano MT, 2018, AM J HUM GENET, V103, P777, DOI 10.1016/j.ajhg.2018.09.011
   Thoma R, 2004, NATURE, V432, P118, DOI 10.1038/nature02993
   Wada Y, 2020, PLOS GENET, V16, DOI 10.1371/journal.pgen.1008628
   WALLIS C, 1989, AM J MED GENET, V32, P500, DOI 10.1002/ajmg.1320320415
   Wang HJ, 2020, AM J HUM GENET, V107, P34, DOI 10.1016/j.ajhg.2020.05.006
   Wang HJ, 2015, HUM MOL GENET, V24, P243, DOI 10.1093/hmg/ddu442
   Zhao L, 2015, NATURE, V523, P607, DOI 10.1038/nature14650
NR 21
TC 13
Z9 13
U1 0
U2 11
PU ELSEVIER SCIENCE INC
PI NEW YORK
PA STE 800, 230 PARK AVE, NEW YORK, NY 10169 USA
SN 0022-202X
EI 1523-1747
J9 J INVEST DERMATOL
JI J. Invest. Dermatol.
PD OCT
PY 2022
VL 142
IS 10
BP 2687
EP +
DI 10.1016/j.jid.2022.03.023
EA SEP 2022
PG 10
WC Dermatology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Dermatology
GA 5A2LG
UT WOS:000862722900001
PM 35413293
OA Bronze
DA 2025-04-10
ER

PT J
AU Bonne, G
   Di Barletta, MR
   Varnous, S
   Bécane, HM
   Hammouda, EH
   Merlini, L
   Muntoni, F
   Greenberg, CR
   Gary, F
   Urtizberea, JA
   Duboc, D
   Fardeau, M
   Toniolo, D
   Schwartz, K
AF Bonne, G
   Di Barletta, MR
   Varnous, S
   Bécane, HM
   Hammouda, EH
   Merlini, L
   Muntoni, F
   Greenberg, CR
   Gary, F
   Urtizberea, JA
   Duboc, D
   Fardeau, M
   Toniolo, D
   Schwartz, K
TI Mutations in the gene encoding lamin A/C cause autosomal dominant
   Emery-Dreifuss muscular dystrophy
SO NATURE GENETICS
LA English
DT Article
ID INTERMEDIATE FILAMENT PROTEINS; CHROMATIN BINDING-SITE;
   NUCLEAR-ENVELOPE; IDENTIFICATION; MEMBRANE; DOMAIN; CDNA;
   CARDIOMYOPATHY; ORGANIZATION; LOCALIZATION
AB Emery-Dreifuss muscular dystrophy (EDMD) is characterized by early contractures of elbows and Achilles tendons, slowly progressive muscle wasting and weakness, and a cardiomyopathy with conduction blocks which is life-threatening(1). Two modes of inheritance exist, X-linked (OMIM 310300) and autosomal dominant (EDMD-AD; OMIM 181350). EDMD-AD is clinically identical to the X-linked forms of the disease(2-4). Mutations in EMD, the gene encoding emerin, are responsible for the X-linked form(5,6). We have mapped the locus for EDMD-AD to an 8-cM interval on chromosome 1q11-q23 in a large French pedigree, and found that the EMD phenotype in four other small families was potentially linked to this locus. This region contains the lamin A/C gene (LMNA), a candidate gene encoding two proteins of the nuclear lamina, lamins A and C, produced by alternative splicing(7,8). We identified four mutations in LMNA that co-segregate with the disease phenotype in the five families: one nonsense mutation and three missense mutations. These results are the first identification of mutations in a component of the nuclear lamina as a cause of inherited muscle disorder. Together with mutations in EMD (refs 5,6), they underscore the potential importance of the nuclear envelope components in the pathogenesis of neuromuscular disorders.
C1 Grp Hosp Pitie Salpetriere, INSERM UR153, F-75651 Paris 13, France.
   Grp Hosp Pitie Salpetriere, Inst Myol, F-75651 Paris 13, France.
   CNR, IGBE CNR, Ist Genet Biochim & Evoluz, I-27100 Pavia, Italy.
   Ist Ortoped Rizzoli, Neuromuscular Lab, I-40136 Bologna, Italy.
   Univ London Imperial Coll Sci Technol & Med, Hammersmith Hosp, Dept Paediat, London W12 0NN, England.
   Ctr Hlth Sci, Winnipeg, MB, Canada.
   Genethon, F-91002 Evry, France.
   Hop Cochin, Serv Cardiol, F-75014 Paris, France.
C3 Assistance Publique Hopitaux Paris (APHP); Hopital Universitaire
   Pitie-Salpetriere - APHP; Sorbonne Universite; Institut National de la
   Sante et de la Recherche Medicale (Inserm); Assistance Publique Hopitaux
   Paris (APHP); Hopital Universitaire Pitie-Salpetriere - APHP; Sorbonne
   Universite; Consiglio Nazionale delle Ricerche (CNR); IRCCS Istituto
   Ortopedico Rizzoli; Imperial College London; Assistance Publique
   Hopitaux Paris (APHP); Universite Paris Cite; Hopital Universitaire
   Cochin - APHP
RP Grp Hosp Pitie Salpetriere, INSERM UR153, Batiment Babinski,47 Bld de Hop, F-75651 Paris 13, France.
EM gbonne@myologie.infobiogen.fr; mroumane@myologie.infobiogen.fr
RI Toniolo, Daniela/AAE-2969-2019; Merlini, Luciano/N-6478-2019; Bonne,
   Gisele/G-3121-2013; MERLINI, LUCIANO/O-2944-2013
OI Bonne, Gisele/0000-0002-2516-3258; MERLINI, LUCIANO/0000-0002-1108-1198
FU Telethon [E.0297] Funding Source: Medline
CR BIONE S, 1994, NAT GENET, V8, P323, DOI 10.1038/ng1294-323
   BUSHBY KMD, 1995, NEUROMUSCULAR DISORD, V5, P337, DOI 10.1016/0960-8966(95)00005-8
   Carrier L, 1997, CIRC RES, V80, P427, DOI 10.1161/01.res.0000435859.24609.b3
   Cartegni L, 1997, HUM MOL GENET, V6, P2257, DOI 10.1093/hmg/6.13.2257
   Dib C, 1996, NATURE, V380, P152, DOI 10.1038/380152a0
   EMERY AEH, 1989, J MED GENET, V26, P637, DOI 10.1136/jmg.26.10.637
   FENICHEL GM, 1982, NEUROLOGY, V32, P1399, DOI 10.1212/WNL.32.12.1399
   FISHER DZ, 1986, P NATL ACAD SCI USA, V83, P6450, DOI 10.1073/pnas.83.17.6450
   FURUKAWA K, 1995, EMBO J, V14, P1626, DOI 10.1002/j.1460-2075.1995.tb07151.x
   GLASS CA, 1993, EMBO J, V12, P4413, DOI 10.1002/j.1460-2075.1993.tb06126.x
   GUILLY MN, 1990, EXP CELL RES, V189, P145, DOI 10.1016/0014-4827(90)90267-E
   GUILLY MN, 1987, EMBO J, V6, P3795, DOI 10.1002/j.1460-2075.1987.tb02715.x
   HOGER TH, 1991, EXP CELL RES, V197, P280, DOI 10.1016/0014-4827(91)90434-V
   LIN F, 1993, J BIOL CHEM, V268, P16321
   MARTIN L, 1995, J BIOL CHEM, V270, P8822, DOI 10.1074/jbc.270.15.8822
   MCKEON FD, 1986, NATURE, V319, P463, DOI 10.1038/319463a0
   MILLER RG, 1985, NEUROLOGY, V35, P1230, DOI 10.1212/WNL.35.8.1230
   Nagano A, 1996, NAT GENET, V12, P254, DOI 10.1038/ng0396-254
   ROBER RA, 1990, J CELL SCI, V95, P587
   SPEER MC, 1992, AM J HUM GENET, V50, P1211
   Squarzoni S, 1998, NEUROMUSCULAR DISORD, V8, P338, DOI 10.1016/S0960-8966(98)00031-5
   TANIURA H, 1995, J CELL BIOL, V131, P33, DOI 10.1083/jcb.131.1.33
   Van Der Kooi A. J., 1996, Annals of Neurology, V39, P636, DOI 10.1002/ana.410390513
   vanderKooi AJ, 1997, AM J HUM GENET, V60, P891
   Vicart P, 1998, NAT GENET, V20, P92, DOI 10.1038/1765
   WORMAN HJ, 1990, J CELL BIOL, V111, P1535, DOI 10.1083/jcb.111.4.1535
   Wydner KL, 1996, GENOMICS, V32, P474, DOI 10.1006/geno.1996.0146
   Yates JRW, 1997, NEUROMUSCULAR DISORD, V7, P67, DOI 10.1016/S0960-8966(96)00403-8
NR 28
TC 1022
Z9 1147
U1 1
U2 40
PU NATURE PUBLISHING GROUP
PI NEW YORK
PA 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA
SN 1061-4036
EI 1546-1718
J9 NAT GENET
JI Nature Genet.
PD MAR
PY 1999
VL 21
IS 3
BP 285
EP 288
DI 10.1038/6799
PG 4
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA 173JR
UT WOS:000078977900021
PM 10080180
DA 2025-04-10
ER

PT J
AU Kawahara, Y
   Kwak, S
AF Kawahara, Y
   Kwak, S
TI Excitotoxicity and ALS: What is unique about the AMPA receptors
   expressed on spinal motor neurons?
SO AMYOTROPHIC LATERAL SCLEROSIS AND OTHER MOTOR NEURON DISORDERS
LA English
DT Review
DE ALS; AMPA receptor; excitotoxicity; RNA editing
ID AMYOTROPHIC-LATERAL-SCLEROSIS; CU/ZN-SUPEROXIDE-DISMUTASE; GLUR2
   MESSENGER-RNA; SELECTIVE MOTONEURON VULNERABILITY; TRANSIENT FOREBRAIN
   ISCHEMIA; HIPPOCAMPAL CA1 NEURONS; TRANSGENIC MOUSE MODEL; LOW RELATIVE
   ABUNDANCE; KINASE-C-ALPHA; Q/R SITE
AB It has been repeatedly reported that spinal motor neurons are selectively vulnerable to AMPA receptor-mediated excitotoxicity. Therefore, identifying the uniqueness of AMPA receptors that are expressed on motor neurons, especially in individuals affected with sporadic amyotrophic lateral sclerosis (ALS) is essential for elucidating the etiology of this disorder. The mechanism that initiates motor neuronal death appears to be an exaggerated influx of Ca2+ through AMPA receptors. The determinants that affect this Ca2+ influx are Ca2+ permeability, which is regulated by the presence of the GluR2 subunit and by RNA editing at the Q/R site of GluR2; channel desensitization, which is regulated by alternative splicing at the flip/ flop site and by RNA editing at the R/G site of GluR subunits; and receptor density on the cell surface, which is controlled by many factors including regulatory proteins, direct phosphorylation and RNA editing at the Q/R site. This review focuses on recent progress on the molecular dynamics of AMPA receptors and discusses the pathophysiology of selective motor neuron death mediated by AMPA receptors in individuals affected with sporadic ALS.
C1 Wistar Inst Anat & Biol, Philadelphia, PA 19104 USA.
   Univ Tokyo, Grad Sch Med, Dept Neurol, Tokyo, Japan.
C3 The Wistar Institute; University of Tokyo
RP Kawahara, Y (corresponding author), Wistar Inst Anat & Biol, 3601 Spruce St, Philadelphia, PA 19104 USA.
EM ykawahara@wistar.org
RI Kawahara, Yukio/AEA-7686-2022
CR Ahmad-Annuar A, 2003, AMYOTROPH LATERAL SC, V4, P150, DOI 10.1080/14660820310011737
   AKBARIAN S, 1995, BRAIN RES, V699, P297, DOI 10.1016/0006-8993(95)00922-D
   ALLAOUA H, 1992, BRAIN RES, V579, P169, DOI 10.1016/0006-8993(92)90758-2
   Anzai T, 2003, NEUROSCI RES, V46, P41, DOI 10.1016/S0168-0102(03)00023-3
   BALLERINI L, 1995, EUR J NEUROSCI, V7, P1229, DOI 10.1111/j.1460-9568.1995.tb01113.x
   Bar-Peled O, 1999, NEUROREPORT, V10, P855, DOI 10.1097/00001756-199903170-00034
   Brorson JR, 2004, J NEUROSCI, V24, P3461, DOI 10.1523/JNEUROSCI.5023-03.2004
   Brorson JR, 1999, J NEUROSCI, V19, P9149
   BRORSON JR, 1995, J NEUROSCI, V15, P4515
   BRUSA R, 1995, SCIENCE, V270, P1677, DOI 10.1126/science.270.5242.1677
   BURNASHEV N, 1992, NEURON, V8, P189, DOI 10.1016/0896-6273(92)90120-3
   BURNASHEV N, 1992, SCIENCE, V256, P1566, DOI 10.1126/science.1317970
   BURNASHEV N, 1995, J PHYSIOL-LONDON, V485, P403, DOI 10.1113/jphysiol.1995.sp020738
   Carlson NG, 2000, NEUROBIOL AGING, V21, P599, DOI 10.1016/S0197-4580(00)00127-5
   Carriedo SG, 1996, J NEUROSCI, V16, P4069
   Carriedo SG, 2000, J NEUROSCI, V20, P240, DOI 10.1523/JNEUROSCI.20-01-00240.2000
   CARRIEDO SG, 1995, NEUROREPORT, V6, P945, DOI 10.1097/00001756-199504190-00030
   Carvalho AL, 1999, J NEUROSCI, V19, P4748
   Chen L, 2000, NATURE, V408, P936, DOI 10.1038/35050030
   Chen YZ, 2004, AM J HUM GENET, V74, P1128, DOI 10.1086/421054
   CHOI DW, 1992, J NEUROBIOL, V23, P1261, DOI 10.1002/neu.480230915
   Coleman SK, 2003, J NEUROSCI, V23, P798
   COURATIER P, 1993, LANCET, V341, P265, DOI 10.1016/0140-6736(93)92615-Z
   Dai WM, 2001, BRIT J PHARMACOL, V132, P1859, DOI 10.1038/sj.bjp.0703993
   Dev KK, 1999, NEUROPHARMACOLOGY, V38, P635, DOI 10.1016/S0028-3908(98)00230-5
   Dong HL, 1997, NATURE, V386, P279, DOI 10.1038/386279a0
   Dong HL, 1999, ANN NY ACAD SCI, V868, P535, DOI 10.1111/j.1749-6632.1999.tb11323.x
   Esteban JA, 2003, NAT NEUROSCI, V6, P136, DOI 10.1038/nn997
   Feldmeyer D, 1999, NAT NEUROSCI, V2, P57, DOI 10.1038/4561
   FRIEDMAN LK, 1994, J NEUROSCI, V14, P2697
   FURUYAMA T, 1993, MOL BRAIN RES, V18, P141, DOI 10.1016/0169-328X(93)90183-P
   GALLO V, 1992, J NEUROSCI, V12, P1010
   Garry EM, 2003, MOL CELL NEUROSCI, V24, P10, DOI 10.1016/S1044-7431(03)00134-9
   GEIGER JRP, 1995, NEURON, V15, P193, DOI 10.1016/0896-6273(95)90076-4
   Gorter JA, 1997, J NEUROSCI, V17, P6179
   Greger IH, 2003, NEURON, V40, P763, DOI 10.1016/S0896-6273(03)00668-8
   Greger IH, 2002, NEURON, V34, P759, DOI 10.1016/S0896-6273(02)00693-1
   Greig A, 2000, J NEUROCHEM, V74, P179, DOI 10.1046/j.1471-4159.2000.0740179.x
   Grigorenko EV, 1998, NEUROREPORT, V9, P2219, DOI 10.1097/00001756-199807130-00013
   Grossman SD, 1999, J NEUROSCI, V19, P5711, DOI 10.1523/JNEUROSCI.19-14-05711.1999
   Hadano S, 2001, NAT GENET, V29, P166, DOI 10.1038/ng1001-166
   Hafezparast M, 2003, SCIENCE, V300, P808, DOI 10.1126/science.1083129
   Hayashi Y, 2000, SCIENCE, V287, P2262, DOI 10.1126/science.287.5461.2262
   Heath PR, 2002, NEUROREPORT, V13, P1753, DOI 10.1097/00001756-200210070-00012
   Higuchi M, 2000, NATURE, V406, P78, DOI 10.1038/35017558
   Hirata A, 1997, BRAIN RES, V771, P37, DOI 10.1016/S0006-8993(97)00709-9
   HOLLMANN M, 1991, SCIENCE, V252, P851, DOI 10.1126/science.1709304
   HUGON J, 1989, NEUROSCI LETT, V104, P258, DOI 10.1016/0304-3940(89)90585-5
   HUME RI, 1991, SCIENCE, V253, P1028, DOI 10.1126/science.1653450
   Iihara K, 2001, J NEUROSCI, V21, P2224, DOI 10.1523/JNEUROSCI.21-07-02224.2001
   Ikonomidou C, 1996, J NEUROPATH EXP NEUR, V55, P211, DOI 10.1097/00005072-199602000-00010
   Inglis FM, 2002, J NEUROSCI, V22, P8042
   Jackson M, 1997, ANN NEUROL, V42, P803, DOI 10.1002/ana.410420518
   JAKOWEC MW, 1995, NEUROSCIENCE, V67, P893, DOI 10.1016/0306-4522(95)00026-F
   Jia ZP, 1996, NEURON, V17, P945, DOI 10.1016/S0896-6273(00)80225-1
   JONAS P, 1994, NEURON, V12, P1281, DOI 10.1016/0896-6273(94)90444-8
   Kamphuis W, 1995, Brain Res Mol Brain Res, V29, P35
   KAMPHUIS W, 1995, NEUROREPORT, V6, P1133, DOI 10.1097/00001756-199505300-00015
   Kask K, 1998, P NATL ACAD SCI USA, V95, P13777, DOI 10.1073/pnas.95.23.13777
   Kawahara Y, 2004, NATURE, V427, P801, DOI 10.1038/427801a
   Kawahara Y, 2004, DEV BRAIN RES, V148, P151, DOI 10.1016/j.devbrainres.2003.11.008
   Kawahara Y, 2004, MOL BRAIN RES, V127, P150, DOI 10.1016/j.molbrainres.2004.05.020
   Kawahara Y, 2003, EUR J NEUROSCI, V18, P23, DOI 10.1046/j.1460-9568.2003.02718.x
   Kawahara Y, 2003, J NEUROCHEM, V85, P680, DOI 10.1046/j.1471-4159.2003.01703.x
   KIM U, 1994, J BIOL CHEM, V269, P13480
   KOH DS, 1995, J PHYSIOL-LONDON, V486, P305, DOI 10.1113/jphysiol.1995.sp020813
   KOHLER M, 1994, J BIOL CHEM, V269, P17367
   Kolleker A, 2003, NEURON, V40, P1199, DOI 10.1016/S0896-6273(03)00722-0
   Kortenbruck G, 2001, NEUROBIOL DIS, V8, P459, DOI 10.1006/nbdi.2001.0394
   Kuner T, 2001, J NEUROSCI, V21, P4162, DOI 10.1523/JNEUROSCI.21-12-04162.2001
   Kwak S, 2005, J MOL MED, V83, P110, DOI 10.1007/s00109-004-0599-z
   Lambolez B, 1996, P NATL ACAD SCI USA, V93, P1797, DOI 10.1073/pnas.93.5.1797
   LAMBOLEZ B, 1992, NEURON, V9, P247, DOI 10.1016/0896-6273(92)90164-9
   Lambrechts D, 2003, NAT GENET, V34, P383, DOI 10.1038/ng1211
   LaMonte BH, 2002, NEURON, V34, P715, DOI 10.1016/S0896-6273(02)00696-7
   Laslo P, 2001, EXP NEUROL, V169, P461, DOI 10.1006/exnr.2001.7653
   Leonard AS, 1998, J BIOL CHEM, V273, P19518, DOI 10.1074/jbc.273.31.19518
   Liu SH, 2004, NEURON, V43, P43, DOI 10.1016/j.neuron.2004.06.017
   LOMELI H, 1994, SCIENCE, V266, P1709, DOI 10.1126/science.7992055
   Lu YM, 1996, J NEUROSCI, V16, P5457
   Lüthi A, 1999, NEURON, V24, P389, DOI 10.1016/S0896-6273(00)80852-1
   Malinow R, 2002, ANNU REV NEUROSCI, V25, P103, DOI 10.1146/annurev.neuro.25.112701.142758
   Melcher T, 1996, NATURE, V379, P460, DOI 10.1038/379460a0
   Meng YH, 2003, NEURON, V39, P163, DOI 10.1016/S0896-6273(03)00368-4
   Mennini T, 2002, J NEUROSCI RES, V70, P553, DOI 10.1002/jnr.10420
   Morrison BM, 1998, J COMP NEUROL, V395, P523
   MOSBACHER J, 1994, SCIENCE, V266, P1059, DOI 10.1126/science.7973663
   Münch C, 2004, NEUROLOGY, V63, P724, DOI 10.1212/01.WNL.0000134608.83927.B1
   Nagy GG, 2004, J NEUROSCI, V24, P5766, DOI 10.1523/JNEUROSCI.1237-04.2004
   NAKAMURA R, 1994, BRAIN RES, V654, P279, DOI 10.1016/0006-8993(94)90490-1
   Nishimura AL, 2004, AM J HUM GENET, V75, P822, DOI 10.1086/425287
   Noel J, 1999, NEURON, V23, P365, DOI 10.1016/S0896-6273(00)80786-2
   NUTT SL, 1994, NEUROREPORT, V5, P1679, DOI 10.1097/00001756-199408150-00034
   O'Brien R, 2002, J NEUROSCI, V22, P4487, DOI 10.1523/JNEUROSCI.22-11-04487.2002
   Oosthuyse B, 2001, NAT GENET, V28, P131, DOI 10.1038/88842
   Osten P, 2000, NEURON, V27, P313, DOI 10.1016/S0896-6273(00)00039-8
   Osten P, 1998, NEURON, V21, P99, DOI 10.1016/S0896-6273(00)80518-8
   PASCHEN W, 1995, J NEUROSCI METH, V56, P21, DOI 10.1016/0165-0270(94)00085-U
   Paschen W, 1996, J CEREBR BLOOD F MET, V16, P548, DOI 10.1097/00004647-199607000-00004
   PASCHEN W, 1994, J NEUROCHEM, V63, P1596, DOI 10.1046/j.1471-4159.1994.63051596.x
   Passafaro M, 2003, NATURE, V424, P677, DOI 10.1038/nature01781
   Passafaro M, 2001, NAT NEUROSCI, V4, P917, DOI 10.1038/nn0901-917
   PellegriniGiampietro DE, 1997, TRENDS NEUROSCI, V20, P464, DOI 10.1016/S0166-2236(97)01100-4
   PELLEGRINIGIAMPIETRO DE, 1992, P NATL ACAD SCI USA, V89, P10499, DOI 10.1073/pnas.89.21.10499
   PELLEGRINIGIAMPIETRO DE, 1994, J NEUROSCI, V14, P1576
   PELLEGRINIGIAMPIETRO DE, 1994, J NEUROCHEM, V62, P1067
   Perez JL, 2001, J NEUROSCI, V21, P5417, DOI 10.1523/JNEUROSCI.21-15-05417.2001
   Pieri M, 2003, NEUROSCIENCE, V122, P47, DOI 10.1016/j.neuroscience.2003.07.003
   POLLARD H, 1993, NEUROSCIENCE, V57, P545, DOI 10.1016/0306-4522(93)90004-Y
   Puls I, 2003, NAT GENET, V33, P455, DOI 10.1038/ng1123
   Rembach A, 2004, J NEUROSCI RES, V77, P573, DOI 10.1002/jnr.20191
   ROSEN DR, 1993, NATURE, V362, P59, DOI 10.1038/362059a0
   ROTHSTEIN JD, 1993, P NATL ACAD SCI USA, V90, P6591, DOI 10.1073/pnas.90.14.6591
   ROTHSTEIN JD, 1990, ANN NEUROL, V28, P18, DOI 10.1002/ana.410280106
   Roy J, 1998, J NEUROSCI, V18, P9673
   Sans N, 2003, J NEUROSCI, V23, P9367
   Schnell E, 2002, P NATL ACAD SCI USA, V99, P13902, DOI 10.1073/pnas.172511199
   Seeburg PH, 2001, BRAIN RES, V907, P233, DOI 10.1016/S0006-8993(01)02445-3
   Shaw PJ, 1999, NEUROREPORT, V10, P261, DOI 10.1097/00001756-199902050-00011
   Shen L, 2000, J NEUROSCI, V20, P7932
   Shi SH, 2001, CELL, V105, P331, DOI 10.1016/S0092-8674(01)00321-X
   SOMMER B, 1991, CELL, V67, P11, DOI 10.1016/0092-8674(91)90568-J
   SOMMER B, 1990, SCIENCE, V249, P1580, DOI 10.1126/science.1699275
   Song I, 1998, NEURON, V21, P393, DOI 10.1016/S0896-6273(00)80548-6
   Spalloni A, 2004, NEUROBIOL DIS, V15, P340, DOI 10.1016/j.nbd.2003.11.012
   SUN H, AMYOTROPH LATERAL S2, V5, P90
   Suzuki Takeshi, 2003, Nihon Yakurigaku Zasshi, V122, P515, DOI 10.1254/fpj.122.515
   Takuma H, 1999, ANN NEUROL, V46, P806, DOI 10.1002/1531-8249(199912)46:6<806::AID-ANA2>3.0.CO;2-S
   Tateno M, 2004, HUM MOL GENET, V13, P2183, DOI 10.1093/hmg/ddh246
   TOLLE TR, 1993, J NEUROSCI, V13, P5009, DOI 10.1523/JNEUROSCI.13-12-05009.1993
   Tomita S, 2004, SCIENCE, V303, P1508, DOI 10.1126/science.1090262
   Tomiyama M, 2002, SYNAPSE, V45, P245, DOI 10.1002/syn.10098
   TOMIYAMA M, NEUROSCIENCE, P901
   Tsuzuki K, 2001, J NEUROCHEM, V77, P1650, DOI 10.1046/j.1471-4159.2001.00388.x
   Van Damme P, 2003, J NEUROSCI, V23, P4942
   Van Damme P, 2002, J NEUROPHYSIOL, V88, P1279, DOI 10.1152/jn.2002.88.3.1279
   Van den Bosch L, 2002, EXP NEUROL, V174, P150, DOI 10.1006/exnr.2001.7858
   Van Den Bosch L, 2000, J NEUROL SCI, V180, P29, DOI 10.1016/S0022-510X(00)00414-7
   Van den Bosch L, 2000, BRAIN RES BULL, V53, P383, DOI 10.1016/S0361-9230(00)00371-3
   Vandenberghe W, 2000, J NEUROSCI, V20, P7158
   Vandenberghe W, 2000, J NEUROSCI, V20, P123, DOI 10.1523/JNEUROSCI.20-01-00123.2000
   VERDOORN TA, 1991, SCIENCE, V252, P1715, DOI 10.1126/science.1710829
   Virgo L, 1996, NEUROREPORT, V7, P2507, DOI 10.1097/00001756-199611040-00021
   Vollmar W, 2004, NEUROBIOL DIS, V15, P371, DOI 10.1016/j.nbd.2003.11.006
   Wang Q, 2000, SCIENCE, V290, P1765, DOI 10.1126/science.290.5497.1765
   Wenthold RJ, 1996, J NEUROSCI, V16, P1982
   Williams TL, 1997, ANN NEUROL, V42, P200, DOI 10.1002/ana.410420211
   WO ZG, 1995, TRENDS NEUROSCI, V18, P161
   Yang Y, 2001, NAT GENET, V29, P160, DOI 10.1038/ng1001-160
   Zhu JJ, 2000, NAT NEUROSCI, V3, P1098, DOI 10.1038/80614
   ZORUMSKI CF, 1990, NEURON, V5, P61, DOI 10.1016/0896-6273(90)90033-C
NR 151
TC 50
Z9 60
U1 0
U2 6
PU TAYLOR & FRANCIS AS
PI OSLO
PA PO BOX 12 POSTHUSET, NO-0051 OSLO, NORWAY
SN 1466-0822
J9 AMYOTROPH LATERAL SC
JI Amyotroph. Lateral. Scler. Mot. Neuron Disord.
PD SEP
PY 2005
VL 6
IS 3
BP 131
EP 144
DI 10.1080/14660820510037872
PG 14
WC Clinical Neurology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA 966RG
UT WOS:000232038000001
PM 16183555
DA 2025-04-10
ER

PT J
AU Kallijärvi, J
   Hämäläinen, RH
   Karlberg, N
   Sainio, K
   Lehesjoki, AE
AF Kallijarvi, Jukka
   Hamalainen, Riikka H.
   Karlberg, Niklas
   Sainio, Kirsi
   Lehesjoki, Anna-Elina
TI Tissue expression of the mulibrey nanism-associated Trim37 protein in
   embryonic and adult mouse tissues
SO HISTOCHEMISTRY AND CELL BIOLOGY
LA English
DT Article
DE TRIM37; mulibrey nanism; ubiquitin ligase
ID AUTOSOMAL RECESSIVE SYNDROME; COILED-COIL PROTEIN; RING-FINGER PROTEIN;
   FAMILY; AMPLIFICATION; DISEASE
AB Mutations in the TRIM37 gene underlie mulibrey nanism (muscle-liver-brain-eye nanism), a rare monogenic developmental disorder characterized by severe growth failure, characteristic dysmorphic features, cardiopathy, failure of sexual maturation, and metabolic syndrome. The TRIM37 protein, a member of the tripartite motif subfamily of RING finger proteins, is highly conserved between human and mouse. High evolutionary conservation is seen also at the gene level. We here show that the mouse Trim37 gene presents several alternative splice variants, including a testis-specific transcript with an additional 3' exon. By Northern blot analysis the highest level of Trim37 mRNA was detected in testis and brain. In embryonic tissues, the Trim37 protein was detected in epithelia, including ducts of the developing pancreas, epithelium of the midgut and nasal epithelium. In adult mouse tissues, Trim37 immunoreactivity was detected in the central and peripheral nervous systems, including enteric ganglia, retina, and the adrenal medulla. Moreover, specific cellular populations in the adenohypophysis, pancreatic islets, intestine and gonads showed intense Trim37 staining. Both nuclear and granular cytoplasmic staining patterns were observed. These findings are in agreement with the clinical manifestations of mulibrey nanism and provide a basis for the future analysis of Trim37 knock-out mice.
C1 Univ Helsinki, Folkhalsan Inst Genet, Dept Med Genet, FIN-00014 Helsinki, Finland.
   Univ Helsinki, Ctr Neurosci, Biomedicum Helsinki, FIN-00014 Helsinki, Finland.
   Univ Helsinki, Hosp Children & Adolescents, Biomedicum Helsinki, FIN-00014 Helsinki, Finland.
   Univ Helsinki, Inst Biomed, FIN-00014 Helsinki, Finland.
C3 University of Helsinki; University of Helsinki; University of Helsinki;
   University of Helsinki
RP Lehesjoki, AE (corresponding author), Univ Helsinki, Folkhalsan Inst Genet, Dept Med Genet, POB 63, FIN-00014 Helsinki, Finland.
EM anna-elina.lehesjoki@helsinki.fi
RI Kallijarvi, Jukka/AAV-5091-2021; Lehesjoki, Anna-Elina/JPK-4409-2023;
   Martikainen, Riikka/AAR-8397-2020
OI Lehesjoki, Anna-Elina/0000-0003-4014-3113; Kallijarvi,
   Jukka/0000-0003-3773-7025
CR ADAMS JC, 1992, J HISTOCHEM CYTOCHEM, V40, P1457, DOI 10.1177/40.10.1527370
   Avela K, 2000, NAT GENET, V25, P298, DOI 10.1038/77053
   HAMALAINEN R, IN PRESS GENE
   Hamalainen Riikka H, 2004, Hum Mutat, V23, P522, DOI 10.1002/humu.9233
   Jagiello P, 2003, HUM MUTAT, V21, P630, DOI 10.1002/humu.10220
   Kallijärvi J, 2005, EXP CELL RES, V308, P146, DOI 10.1016/j.yexcr.2005.04.001
   Kallijärvi J, 2002, AM J HUM GENET, V70, P1215, DOI 10.1086/340256
   Karlberg N, 2005, DIABETES, V54, P3577, DOI 10.2337/diabetes.54.12.3577
   Karlberg N, 2004, J MED GENET, V41, P92, DOI 10.1136/jmg.2003.014118
   Lehesjoki AE, 2001, MECH DEVELOP, V108, P221, DOI 10.1016/S0925-4773(01)00491-9
   Lipsanen-Nyman M, 2003, CIRCULATION, V107, P2810, DOI 10.1161/01.CIR.0000070949.76608.E2
   Nardacci R, 2004, J HISTOCHEM CYTOCHEM, V52, P423, DOI 10.1177/002215540405200401
   O'Connor DT, 2005, J CLIN ENDOCR METAB, V90, P5414, DOI 10.1210/jc.2005-0408
   PERHEENTUPA J, 1973, LANCET, V2, P351, DOI 10.1016/S0140-6736(73)93193-0
   Schad A, 2003, J HISTOCHEM CYTOCHEM, V51, P751, DOI 10.1177/002215540305100606
   TARKKANEN A, 1982, ACTA OPHTHALMOL, V60, P628
   Zapata JM, 2001, J BIOL CHEM, V276, P24242, DOI 10.1074/jbc.M100354200
NR 17
TC 17
Z9 18
U1 0
U2 1
PU SPRINGER
PI NEW YORK
PA 233 SPRING STREET, NEW YORK, NY 10013 USA
SN 0948-6143
J9 HISTOCHEM CELL BIOL
JI Histochem. Cell Biol.
PD SEP
PY 2006
VL 126
IS 3
BP 325
EP 334
DI 10.1007/s00418-006-0162-9
PG 10
WC Cell Biology; Microscopy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Microscopy
GA 074UF
UT WOS:000239836600004
PM 16514549
DA 2025-04-10
ER

PT J
AU Nakamura, K
   Kennedy, MA
   Baldán, A
   Bojanic, DD
   Lyons, K
   Edwards, PA
AF Nakamura, K
   Kennedy, MA
   Baldán, A
   Bojanic, DD
   Lyons, K
   Edwards, PA
TI Expression and regulation of multiple murine ATP-binding cassette
   transporter G1 mRNAs/isoforms that stimulate cellular cholesterol efflux
   to high density lipoprotein
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID DROSOPHILA-WHITE GENE; FARNESOID-X RECEPTOR; ABC-TRANSPORTER;
   DIETARY-CHOLESTEROL; TANGIER-DISEASE; LOADED MACROPHAGES; ACTIVATED
   RECEPTOR; MOLECULAR-CLONING; NUCLEAR RECEPTOR; MESSENGER-RNA
AB The murine Abcg1 gene is reported to consist of 15 exons that encode a single mRNA ( herein referred to as Abcg1-a) and protein. We now demonstrate that (i) the murine gene contains two additional coding exons downstream of exon 1, (ii) transcription involves the use of multiple promoters, and (iii) the RNA undergoes alternative splicing reactions. As a result, three mRNAs are expressed that encode three putative protein isoforms that differ at their amino terminus. ABCG1 transcripts are induced in vivo in multiple tissues in response to the liver X receptor ligand T0901317. Identification and characterization of four liver X receptor response elements in the intron downstream of exon 2 provides a mechanism by which this induction occurs. Importantly, cholesterol efflux to high density lipoprotein was stimulated following transfection of Hek293 cells with plasmids encoding individual ABCG1 isoforms. In situ hybridization studies in embryonic day 11.5-15.5 mouse embryos revealed strong expression of ABCG1 transcripts in the olfactory epithelium, hind brain, eye, and dorsal root ganglia. The relatively high levels of expression in neuronal tissues and the eye suggest that ABCG1-dependent cholesterol efflux may be critical for normal neuronal function in addition to its role in macrophages.
C1 Univ Calif Los Angeles, Dept Med & Biol Chem, Los Angeles, CA 90095 USA.
   Univ Calif Los Angeles, Dept Mol & Cell Biol, Los Angeles, CA 90095 USA.
   Univ Calif Los Angeles, Inst Mol Biol, Los Angeles, CA 90095 USA.
C3 University of California System; University of California Los Angeles;
   University of California System; University of California Los Angeles;
   University of California System; University of California Los Angeles
RP Univ Calif Los Angeles, Dept Biol Chem, CHS 33-257,10833 Le Conte Ave, Los Angeles, CA 90095 USA.
EM pedwards@mednet.ucla.edu
RI Kennedy, Michael/M-2578-2019
FU NHLBI NIH HHS [HL30568, HL68445] Funding Source: Medline
CR Allikmets R, 1996, HUM MOL GENET, V5, P1649, DOI 10.1093/hmg/5.10.1649
   AMBUDKAR SV, 1998, ABC TRANSPORTERS BIO, V292, P101
   Anisfeld AM, 2003, J BIOL CHEM, V278, P20420, DOI 10.1074/jbc.M302505200
   Annilo T, 2001, CYTOGENET CELL GENET, V94, P196, DOI 10.1159/000048816
   Berge KE, 2000, SCIENCE, V290, P1771, DOI 10.1126/science.290.5497.1771
   Bodzioch M, 1999, NAT GENET, V22, P347, DOI 10.1038/11914
   BOEHM MF, 1994, J MED CHEM, V37, P2930, DOI 10.1021/jm00044a014
   BREATHNACH R, 1981, ANNU REV BIOCHEM, V50, P349, DOI 10.1146/annurev.bi.50.070181.002025
   Brooks-Wilson A, 1999, NAT GENET, V22, P336, DOI 10.1038/11905
   Campbell JL, 2001, J NEUROBIOL, V49, P339, DOI 10.1002/neu.10009
   Chen HM, 1996, AM J HUM GENET, V59, P66
   Childs S, 1994, Important Adv Oncol, P21
   Croop JM, 1997, GENE, V185, P77, DOI 10.1016/S0378-1119(96)00633-6
   Dean M, 2001, J LIPID RES, V42, P1007
   Dean M, 2001, GENOME RES, V11, P1156, DOI 10.1101/gr.GR-1649R
   DREESEN TD, 1988, MOL CELL BIOL, V8, P5206, DOI 10.1128/MCB.8.12.5206
   HIGGINS CF, 1992, ANNU REV CELL BIOL, V8, P67, DOI 10.1146/annurev.cellbio.8.1.67
   Hoekstra M, 2003, J BIOL CHEM, V278, P25448, DOI 10.1074/jbc.M301189200
   Hogan B, 1994, Manipulating the mouse embryo. Cold spring harbor lab
   Kast HR, 2002, J BIOL CHEM, V277, P2908, DOI 10.1074/jbc.M109326200
   Kennedy MA, 2001, J BIOL CHEM, V276, P39438, DOI 10.1074/jbc.M105863200
   Klein I, 1999, BBA-BIOMEMBRANES, V1461, P237, DOI 10.1016/S0005-2736(99)00161-3
   Klucken J, 2000, P NATL ACAD SCI USA, V97, P817, DOI 10.1073/pnas.97.2.817
   KRITHARIDES L, 1995, ARTERIOSCL THROM VAS, V15, P276, DOI 10.1161/01.ATV.15.2.276
   Laffitte BA, 2000, J BIOL CHEM, V275, P10638, DOI 10.1074/jbc.275.14.10638
   Laffitte BA, 2001, P NATL ACAD SCI USA, V98, P507, DOI 10.1073/pnas.021488798
   Langmann T, 2000, BBA-GENE STRUCT EXPR, V1494, P175, DOI 10.1016/S0167-4781(00)00215-3
   Langmann T, 1999, BIOCHEM BIOPH RES CO, V257, P29, DOI 10.1006/bbrc.1999.0406
   Lee MH, 2001, NAT GENET, V27, P79, DOI 10.1038/83799
   Lorkowski S, 2001, BIOCHEM BIOPH RES CO, V280, P121, DOI 10.1006/bbrc.2000.4089
   Luciani MF, 1996, EMBO J, V15, P226, DOI 10.1002/j.1460-2075.1996.tb00353.x
   Mackenzie SM, 2000, GENETICA, V108, P239, DOI 10.1023/A:1004115718597
   Mak PA, 2002, J BIOL CHEM, V277, P31900, DOI 10.1074/jbc.M202993200
   Oldfield S, 2002, BBA-MOL CELL RES, V1591, P175, DOI 10.1016/S0167-4889(02)00269-0
   Oram JF, 2001, J LIPID RES, V42, P1173
   PEPLING M, 1990, NUCLEIC ACIDS RES, V18, P1633, DOI 10.1093/nar/18.6.1633
   Repa JJ, 2002, J BIOL CHEM, V277, P18793, DOI 10.1074/jbc.M109927200
   Rust S, 1999, NAT GENET, V22, P352, DOI 10.1038/11921
   Sánchez-Fernández R, 2001, J BIOL CHEM, V276, P30231, DOI 10.1074/jbc.M103104200
   Savary S, 1996, MAMM GENOME, V7, P673, DOI 10.1007/s003359900203
   Schmitz G, 2001, CURR OPIN LIPIDOL, V12, P129, DOI 10.1097/00041433-200104000-00006
   SELDEN RF, 1986, MOL CELL BIOL, V6, P3173, DOI 10.1128/MCB.6.9.3173
   Tangirala RK, 2002, P NATL ACAD SCI USA, V99, P11896, DOI 10.1073/pnas.182199799
   TEARLE RG, 1989, GENETICS, V122, P595
   Venkateswaran A, 2000, J BIOL CHEM, V275, P14700, DOI 10.1074/jbc.275.19.14700
   Venkateswaran A, 2000, P NATL ACAD SCI USA, V97, P12097, DOI 10.1073/pnas.200367697
   Wang N, 2004, P NATL ACAD SCI USA, V101, P9774, DOI 10.1073/pnas.0403506101
   Wellington CL, 2002, LAB INVEST, V82, P273, DOI 10.1038/labinvest.3780421
   Whitney KD, 2002, MOL ENDOCRINOL, V16, P1378, DOI 10.1210/me.16.6.1378
   WILLY PJ, 1995, GENE DEV, V9, P1033, DOI 10.1101/gad.9.9.1033
   Yu LQ, 2002, P NATL ACAD SCI USA, V99, P16237, DOI 10.1073/pnas.252582399
   Yu LQ, 2003, J BIOL CHEM, V278, P15565, DOI 10.1074/jbc.M301311200
   Yu LQ, 2002, J CLIN INVEST, V110, P671, DOI [10.1172/JCI200216001, 10.1172/JCI0216001]
   Zhang YQ, 2003, J BIOL CHEM, V278, P104, DOI 10.1074/jbc.M209505200
NR 54
TC 138
Z9 166
U1 0
U2 2
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
SN 0021-9258
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD OCT 29
PY 2004
VL 279
IS 44
BP 45980
EP 45989
DI 10.1074/jbc.M408652200
PG 10
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 865IC
UT WOS:000224694900083
PM 15319426
OA hybrid
DA 2025-04-10
ER

PT J
AU Chuvpilo, S
   Avots, A
   Berberich-Siebelt, F
   Glöckner, J
   Fischer, C
   Kerstan, A
   Escher, C
   Inashkina, E
   Hlubek, F
   Jankevics, E
   Brabletz, T
   Serfling, E
AF Chuvpilo, S
   Avots, A
   Berberich-Siebelt, F
   Glöckner, J
   Fischer, C
   Kerstan, A
   Escher, C
   Inashkina, E
   Hlubek, F
   Jankevics, E
   Brabletz, T
   Serfling, E
TI Multiple NF-ATc isoforms with individual transcriptional properties are
   synthesized in T lymphocytes
SO JOURNAL OF IMMUNOLOGY
LA English
DT Article
ID INTERLEUKIN-5 GENE PROMOTER; DNA-BINDING DOMAIN; NUCLEAR FACTOR; CELL
   ACTIVATION; DEFICIENT MICE; CYCLOSPORINE-A; EXPRESSION; FAMILY;
   PROTEINS; RECEPTOR
AB The transcription factor NF-ATc that controls gene expression in T lymphocytes and embryonic cardiac cells is expressed in three prominent isoforms, This is due to alternative splice/polyadenylation event that lead to the predominant synthesis of two long isoforms in naive T cells and a shorter NF-ATc isoform in effector T cells. Whereas the previously described isoform NF-ATc/A contains a relatively short C terminus, the longer isoforms, B and Ci span extra C-terminal peptides,of 128 and 246 aa, respectively. We show here that in addition to the strong N-terminal trans-activation domain, TAD-A, which is common to all three NF-ATc-isoforms, NF-ATc/C contains a second trans-activation domain, TAD-B, in its C-terminal peptide, Various stimuli of T cells that induce the activity of TAD-A also enhance the activity of TAD-B, but, unlike TAD-A, TAD-B remains unphosphorylated by protein from 12-O-tetradecanoyl, 12-phorbol 13-acetate-stimulated T cells, The shorter C-terminal peptide of isoform NF-ATc/B exerts a suppressive transcriptional effect. These-properties of NF-ATc/B and -C might be of importance for gene regulation in naive T lymphocytes in which NF-ATc/B and -C are predominantly synthesized.
C1 Univ Wurzburg, Inst Pathol, Dept Mol Pathol, D-97080 Wurzburg, Germany.
   Univ Erlangen Nurnberg, Inst Pathol, D-8520 Erlangen, Germany.
   Latvian State Univ, Biomed Res & Study Ctr, LV-1063 Riga, Latvia.
C3 University of Wurzburg; University of Erlangen Nuremberg; University of
   Latvia; Latvian Biomedical Research & Study Centre
RP Serfling, E (corresponding author), Univ Wurzburg, Inst Pathol, Dept Mol Pathol, Josef Schneider Str 2, D-97080 Wurzburg, Germany.
RI Serfling, Edgar/X-7212-2019; Chuvpilo, Sergey/AAD-3144-2019; Inashkina,
   Inna/AAH-9955-2021; Brunner, née Escher, Cornelia/ISV-0665-2023;
   Brunner, Cornelia/H-8893-2018
OI Inashkina, Inna/0000-0002-7560-797X; Brunner,
   Cornelia/0000-0002-6456-5508
CR Aramburu J, 1998, MOL CELL, V1, P627, DOI 10.1016/S1097-2765(00)80063-5
   BANIAHMAD A, 1992, EMBO J, V11, P1015, DOI 10.1002/j.1460-2075.1992.tb05140.x
   Chuvpilo S, 1999, IMMUNITY, V10, P261, DOI 10.1016/S1074-7613(00)80026-6
   CHUVPILO S, 1993, NUCLEIC ACIDS RES, V21, P5694, DOI 10.1093/nar/21.24.5694
   de la Pompa JL, 1998, NATURE, V392, P182, DOI 10.1038/32419
   EHLERS S, 1991, J EXP MED, V173, P25, DOI 10.1084/jem.173.1.25
   FIERING S, 1990, GENE DEV, V4, P1823, DOI 10.1101/gad.4.10.1823
   GRUARTGOUILLEUX V, 1995, EUR J IMMUNOL, V25, P1431, DOI 10.1002/eji.1830250544
   Hodge MR, 1996, IMMUNITY, V4, P397, DOI 10.1016/S1074-7613(00)80253-8
   HOEY T, 1995, IMMUNITY, V2, P461, DOI 10.1016/1074-7613(95)90027-6
   Imamura R, 1998, J IMMUNOL, V161, P3455
   JAIN JN, 1995, J BIOL CHEM, V270, P4138, DOI 10.1074/jbc.270.8.4138
   Kel A, 1999, J MOL BIOL, V288, P353, DOI 10.1006/jmbi.1999.2684
   Kiani A, 1997, IMMUNITY, V7, P849, DOI 10.1016/S1074-7613(00)80403-3
   Klemm JD, 1997, CURR BIOL, V7, P638, DOI 10.1016/S0960-9822(06)00290-9
   LEE HJ, 1995, J BIOL CHEM, V270, P17541, DOI 10.1074/jbc.270.29.17196
   Luo C, 1996, J EXP MED, V184, P141, DOI 10.1084/jem.184.1.141
   Luo C, 1996, MOL CELL BIOL, V16, P3955
   Lyakh L, 1997, MOL CELL BIOL, V17, P2475, DOI 10.1128/MCB.17.5.2475
   Mages HW, 1998, MOL CELL BIOL, V18, P7157, DOI 10.1128/MCB.18.12.7157
   NEUMANN M, 1991, EMBO J, V14
   NORTHROP JP, 1994, NATURE, V369, P497, DOI 10.1038/369497a0
   Park JC, 1996, J BIOL CHEM, V271, P20914, DOI 10.1074/jbc.271.34.20914
   RANDAK C, 1990, EMBO J, V9, P2529, DOI 10.1002/j.1460-2075.1990.tb07433.x
   Ranger AM, 1998, IMMUNITY, V9, P627, DOI 10.1016/S1074-7613(00)80660-3
   Ranger AM, 1998, NATURE, V392, P186, DOI 10.1038/32426
   Rao A, 1997, ANNU REV IMMUNOL, V15, P707, DOI 10.1146/annurev.immunol.15.1.707
   ROONEY JW, 1995, MOL CELL BIOL, V15, P6299
   SCHMITZ ML, 1994, BIOTECHNIQUES, V17, P714
   SCHREIBER E, 1988, EMBO J, V7, P4221, DOI 10.1002/j.1460-2075.1988.tb03319.x
   Schuh K, 1998, EUR J IMMUNOL, V28, P2456, DOI 10.1002/(SICI)1521-4141(199808)28:08<2456::AID-IMMU2456>3.0.CO;2-9
   SHAW JP, 1988, SCIENCE, V241, P202, DOI 10.1126/science.3260404
   TRIEZENBERG SJ, 1995, CURR OPIN GENET DEV, V5, P190, DOI 10.1016/0959-437X(95)80007-7
   Wolfe SA, 1997, NATURE, V385, P172, DOI 10.1038/385172a0
   Xanthoudakis S, 1996, SCIENCE, V272, P892, DOI 10.1126/science.272.5263.892
   Yoshida H, 1998, IMMUNITY, V8, P115, DOI 10.1016/S1074-7613(00)80464-1
NR 36
TC 76
Z9 82
U1 0
U2 1
PU AMER ASSOC IMMUNOLOGISTS
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA
SN 0022-1767
J9 J IMMUNOL
JI J. Immunol.
PD JUN 15
PY 1999
VL 162
IS 12
BP 7294
EP 7301
PG 8
WC Immunology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Immunology
GA 205BT
UT WOS:000080802000047
PM 10358178
DA 2025-04-10
ER

PT J
AU Bahri, SM
   Chia, W
   Yang, XH
AF Bahri, SM
   Chia, W
   Yang, XH
TI Characterization and mutant analysis of the Drosophila
   sema 5C gene
SO DEVELOPMENTAL DYNAMICS
LA English
DT Article
DE semaphorin domain; thrombospondin repeats; mesoderm; muscle attachment;
   fat body; Drosophila
ID GROWTH CONE GUIDANCE; I REPEATS; EXTRACELLULAR-MATRIX; HEPARIN-BINDING;
   SEMAPHORIN-III; THROMBOSPONDIN; PROTEIN; FAMILY; TRANSMEMBRANE;
   EXPRESSION
AB Class V semaphorins are transmembrane glycoproteins characterised by the presence of thrombospondin type I (Tsp) repeats linked to their extracellular semaphorin domain. Sema 5C is the only class V semaphorin found in Drosophila. Dsema 5C RNA is maternally provided and its embryonic expression is prominent in the mesoderm and muscle attachment sites. Here, we show that DSema 5C exists in two protein isoforms as a result of alternative splicing and that both protein and RNA have similar expression patterns. Using a combination of various molecular markers, we show that the DSema 5C protein becomes enriched in mesodermal cells that would normally give rise to fat body and visceral structures. In late embryos, DSema 5C is expressed in segment boundary cells that would constitute subsets of muscle attachment sites. Both RNA and protein are excluded from the somatic precursors and the mature muscles. The expression data suggest DSema 5C localised to the epidermal component of muscle attachment sites. Mutations in Dsema 5C were isolated from a P-element excision screen and by blotting analysis. The Dsema 5C mutants are homozygous viable and show no obvious embryonic phenotypes, suggesting that the maternal and zygotic components of Dsema 5C are not essential for fly development. (C) 2001 Wiley-Liss, Inc.
C1 Inst Mol & Cell Biol, Singapore 117609, Singapore.
C3 Agency for Science Technology & Research (A*STAR); A*STAR - Institute of
   Molecular & Cell Biology (IMCB)
RP Inst Mol & Cell Biol, 30 Med Dr, Singapore 117609, Singapore.
EM mcbsb@imcb.nus.edu.sg
CR ADAMS J, 1993, CURR BIOL, V3, P188, DOI 10.1016/0960-9822(93)90270-X
   Adams JC, 2000, DEV DYNAM, V218, P280
   Adams RH, 1996, MECH DEVELOP, V57, P33, DOI 10.1016/0925-4773(96)00525-4
   ASCH AS, 1993, SCIENCE, V262, P1436, DOI 10.1126/science.7504322
   Ashburner M, 1989, DROSOPHILA LAB HDB
   Behar O, 1996, NATURE, V383, P525, DOI 10.1038/383525a0
   BORK P, 1993, FEBS LETT, V327, P125, DOI 10.1016/0014-5793(93)80155-N
   Borkowski OMD, 1995, DEVELOPMENT, V121, P4183
   BROWN NH, 1988, J MOL BIOL, V203, P425, DOI 10.1016/0022-2836(88)90010-1
   Bunch TA, 1998, DEVELOPMENT, V125, P1679
   Campos-Ortega J.A., 1985, EMBRYONIC DEV DROSOP
   DEFREITAS MF, 1995, NEURON, V15, P333, DOI 10.1016/0896-6273(95)90038-1
   FOGERTY FJ, 1994, DEVELOPMENT, V120, P1747
   GEORGE EL, 1993, DEVELOPMENT, V119, P1079
   GUO NH, 1992, P NATL ACAD SCI USA, V89, P3040, DOI 10.1073/pnas.89.7.3040
   HENCHCLIFFE C, 1993, DEVELOPMENT, V118, P325
   HSU S, 1988, NEUROSCI LETT, V85, P169
   Khare N, 2000, MECH DEVELOP, V91, P393, DOI 10.1016/S0925-4773(99)00297-X
   KIEHART DP, 1986, J CELL BIOL, V103, P1517, DOI 10.1083/jcb.103.4.1517
   Kolodkin AL, 1997, CELL, V90, P753, DOI 10.1016/S0092-8674(00)80535-8
   KOLODKIN AL, 1992, NEURON, V9, P831, DOI 10.1016/0896-6273(92)90237-8
   Kolodkin AL, 1997, NEURON, V19, P1159, DOI 10.1016/S0896-6273(00)80408-0
   KOLODKIN AL, 1993, CELL, V75, P1389, DOI 10.1016/0092-8674(93)90625-Z
   LI WX, 1993, J BIOL CHEM, V268, P16179
   LUO YL, 1993, CELL, V75, P217, DOI 10.1016/0092-8674(93)80064-L
   Nakamura F, 2000, J NEUROBIOL, V44, P219, DOI 10.1002/1097-4695(200008)44:2<219::AID-NEU11>3.0.CO;2-W
   NGUYEN HT, 1994, P NATL ACAD SCI USA, V91, P7520, DOI 10.1073/pnas.91.16.7520
   Nose A, 1998, DEVELOPMENT, V125, P215
   PRATER CA, 1991, J CELL BIOL, V112, P1031, DOI 10.1083/jcb.112.5.1031
   Riechmann V, 1998, DEVELOPMENT, V125, P713
   ROBERTSON HM, 1988, GENETICS, V118, P461
   Rohm B, 2000, MECH DEVELOP, V93, P95, DOI 10.1016/S0925-4773(00)00269-0
   Roy PJ, 2000, DEVELOPMENT, V127, P755
   Russell DW., 2001, Molecular Cloning: ALaboratory Manual, V1
   SAGA Y, 1992, GENE DEV, V6, P1821, DOI 10.1101/gad.6.10.1821
   Simmons AD, 1998, BIOCHEM BIOPH RES CO, V242, P685, DOI 10.1006/bbrc.1997.8027
   Takahashi T, 1999, CELL, V99, P59, DOI 10.1016/S0092-8674(00)80062-8
   Tamagnone L, 1999, CELL, V99, P71, DOI 10.1016/S0092-8674(00)80063-X
   Tamagnone L, 2000, TRENDS CELL BIOL, V10, P377, DOI 10.1016/S0962-8924(00)01816-X
   TAMKUN JW, 1992, CELL, V68, P561, DOI 10.1016/0092-8674(92)90191-E
   Tear G, 1996, NEURON, V16, P501, DOI 10.1016/S0896-6273(00)80070-7
   TOLSMA SS, 1993, J CELL BIOL, V122, P497, DOI 10.1083/jcb.122.2.497
   TUSZYNSKI GP, 1993, J CELL BIOL, V120, P513, DOI 10.1083/jcb.120.2.513
   Umemiya T, 1997, DEV BIOL, V186, P165, DOI 10.1006/dbio.1997.8591
   VOGEL T, 1993, J CELL BIOCHEM, V53, P74, DOI 10.1002/jcb.240530109
   VOLK T, 1994, DEVELOPMENT, V120, P59
   Winberg ML, 1998, CELL, V95, P903, DOI 10.1016/S0092-8674(00)81715-8
   YARNITZKY T, 1995, DEV BIOL, V169, P609, DOI 10.1006/dbio.1995.1173
   Yu HH, 1998, NEURON, V20, P207, DOI 10.1016/S0896-6273(00)80450-X
NR 49
TC 21
Z9 28
U1 0
U2 0
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 1058-8388
EI 1097-0177
J9 DEV DYNAM
JI Dev. Dyn.
PD JUL
PY 2001
VL 221
IS 3
BP 322
EP 330
DI 10.1002/dvdy.1142
PG 9
WC Anatomy & Morphology; Developmental Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Anatomy & Morphology; Developmental Biology
GA 447LW
UT WOS:000169575700007
PM 11458392
DA 2025-04-10
ER

PT J
AU Fujino, H
   Srinivasan, D
   Pierce, KL
   Regan, JW
AF Fujino, H
   Srinivasan, D
   Pierce, KL
   Regan, JW
TI Differential regulation of prostaglandin F2α receptor
   isoforms by protein kinase C
SO MOLECULAR PHARMACOLOGY
LA English
DT Article
ID THROMBOXANE RECEPTOR; DESENSITIZATION; PHOSPHORYLATION; SENSITIVITY;
   CLONING
AB Prostaglandin F-2 alpha receptors (FP) are G protein-coupled receptors that bind prostaglandin F-2 alpha (PGF(2 alpha)), resulting in the activation of an inositol phosphate (IP) second messenger pathway. Alternative mRNA splicing generates two FP receptor isoforms. These isoforms, designated FPA and FPB, are otherwise identical except for their carboxyl termini. FPB is essentially a truncated version of FPA that lacks the 46 carboxyl-terminal amino acids, including four putative protein kinase C (PKC) phosphorylation sites. Until now, functional differences between these FP receptor isoforms have not been identified. We now report that pretreatment with the PKC inhibitor bisindolylmaleimide I enhanced PGF(2 alpha)-stimulated IP accumulation in transfected cells stably expressing the FPA isoform but not in cells stably expressing the FPB isoform. Whole-cell phosphorylation experiments showed a strong agonist-dependent phosphorylation of the FPA isoform but little or no phosphorylation of the FPB. Pretreatment of cells with bisindolylmaleimide I decreased PGF(2 alpha)-stimulated phosphorylation of the FPA isoform consistent with a PKC-dependent phosphorylation. In vitro phosphorylation of an FPA carboxyl-terminal fusion protein by recombinant PKC alpha showed that the carboxyl terminus of the FPA is a substrate for PKC. These results suggest that PKC-dependent phosphorylation is responsible for differential regulation of second messenger signaling by FP prostanoid receptor isoforms.
C1 Univ Arizona, Coll Pharm, Dept Pharmacol & Toxicol, Tucson, AZ 85721 USA.
   Duke Univ, Med Ctr, Howard Hughes Med Inst, Durham, NC 27710 USA.
C3 University of Arizona; Howard Hughes Medical Institute; Duke University
RP Regan, JW (corresponding author), Univ Arizona, Coll Pharm, Dept Pharmacol & Toxicol, 1703 E Mabel St,Box 210207, Tucson, AZ 85721 USA.
FU NEI NIH HHS [EY11291] Funding Source: Medline
CR Ali H, 1997, J BIOL CHEM, V272, P11706, DOI 10.1074/jbc.272.18.11706
   Anthony TL, 1998, INVEST OPHTH VIS SCI, V39, P315
   Freedman NJ, 1996, RECENT PROG HORM RES, V51, P319
   GRAVES PE, 1995, ENDOCRINOLOGY, V136, P3430, DOI 10.1210/en.136.8.3430
   Habib A, 1997, J BIOL CHEM, V272, P7191, DOI 10.1074/jbc.272.11.7191
   Hirata T, 1996, J CLIN INVEST, V97, P949, DOI 10.1172/JCI118518
   NEGISHI M, 1993, J BIOL CHEM, V268, P9517
   Parent JL, 1999, J BIOL CHEM, V274, P8941, DOI 10.1074/jbc.274.13.8941
   Pierce KL, 1997, J BIOL CHEM, V272, P883, DOI 10.1074/jbc.272.2.883
   Pierce KL, 1998, LIFE SCI, V62, P1479, DOI 10.1016/S0024-3205(98)00093-9
   RYU SH, 1990, J BIOL CHEM, V265, P17941
   Smyth EM, 1998, J BIOL CHEM, V273, P23258, DOI 10.1074/jbc.273.36.23258
   Spurney RF, 1998, J BIOL CHEM, V273, P28496, DOI 10.1074/jbc.273.43.28496
NR 13
TC 36
Z9 46
U1 0
U2 0
PU AMER SOC PHARMACOLOGY EXPERIMENTAL THERAPEUTICS
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3998 USA
SN 0026-895X
J9 MOL PHARMACOL
JI Mol. Pharmacol.
PD FEB
PY 2000
VL 57
IS 2
BP 353
EP 358
PG 6
WC Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Pharmacology & Pharmacy
GA 280BC
UT WOS:000085081300016
PM 10648645
DA 2025-04-10
ER

PT J
AU Tsuchida, S
   Kagi, A
   Takahashi, T
AF Tsuchida, Shuichi
   Kagi, Akiko
   Takahashi, Toshikazu
TI Characterization of cDNA and genomic sequences encoding a canine
   chemokine receptor, CXCR4 and its ligand CXCL12
SO VETERINARY IMMUNOLOGY AND IMMUNOPATHOLOGY
LA English
DT Article
DE cDNA cloning; CXCR4; CXCL 12; dog
ID MOLECULAR-CLONING; BORDER COLLIES; 7-TRANSMEMBRANE; CELLS;
   MICROENVIRONMENT; LYMPHOPOIESIS; MYELOKATHEXIS; MYELOPOIESIS;
   NEUTROPENIA; MIGRATION
AB The interaction of chemokine receptor CXCR4 and its functional ligand CXCL12 plays a key role in bone marrow hematopoiesis, neuronal and cardiovascular development, and organization of the immune system. Despite the importance of the CXCL12-CXCR4 axis for regulating hematopoiesis, information on the canine CXCR4 and CXCL12 genes is insufficient. In this present study, we identified the canine counterparts of the CXCR4 and CXCL12 cDNAs and genes. The amino acid sequence encoding canine CXCR4 showed the structural characteristics of seven transmembrane domain G protein-coupled receptors and high homology with those of humans and other animals. Two isoforms, CXCL12 alpha and CXCL12 beta, were identified in dogs, as described in human and other animals. The gene structures for canine CXCR4 and CXCL12 were similar to those of other animals. The canine CXCL12 gene structure indicated that the transcripts of the isoforms arose from alternative mRNA splicing. A single nucleotide polymorphism (SNP) with synonymous substitution was observed in the exon of the canine CXCL12 gene. mRNAs encoding canine CXCR4 and CXCL 12 were expressed widely and constitutively. Molecular homology and constitutive expression of CXCR4 and CXCL12 mRNAs in canine normal tissues suggests critical roles in hematopoiesis and trafficking of leukocytes, as shown in other animals. (c) 2007 Elsevier B.V. All rights reserved.
C1 Nippon Vet & Life Sci Univ, Lab Comparat Cellular Biol, Musashino, Tokyo 1808602, Japan.
   Takahashi Anim Hosp, Family Anim Hosp, Kanagawa 2420001, Japan.
C3 Nippon Veterinary & Life Science University
RP Tsuchida, S (corresponding author), Nippon Vet & Life Sci Univ, Lab Comparat Cellular Biol, 1-7-1 Kyonan Cho, Musashino, Tokyo 1808602, Japan.
EM tsuchida@nvlu.ac.jp
CR Allan FJ, 1996, NEW ZEAL VET J, V44, P67, DOI 10.1080/00480169.1996.35937
   Broxmeyer HE, 2005, J EXP MED, V201, P1307, DOI 10.1084/jem.20041385
   Burger JA, 2006, BLOOD, V107, P1761, DOI 10.1182/blood-2005-08-3182
   Ceradini DJ, 2004, NAT MED, V10, P858, DOI 10.1038/nm1075
   Doitsidou M, 2002, CELL, V111, P647, DOI 10.1016/S0092-8674(02)01135-2
   FEDERSPPIEL B, 1993, GENOMICS, V16, P707, DOI 10.1006/geno.1993.1251
   Feng Y, 1996, SCIENCE, V272, P872, DOI 10.1126/science.272.5263.872
   Hernandez PA, 2003, NAT GENET, V34, P70, DOI 10.1038/ng1149
   Knaut H, 2003, NATURE, V421, P279, DOI 10.1038/nature01338
   LOETSCHER M, 1994, J BIOL CHEM, V269, P232
   Ma Q, 1999, IMMUNITY, V10, P463, DOI 10.1016/S1074-7613(00)80046-1
   Ma Q, 1998, P NATL ACAD SCI USA, V95, P9448, DOI 10.1073/pnas.95.16.9448
   Müller A, 2001, NATURE, V410, P50, DOI 10.1038/35065016
   Nagasawa T, 1996, P NATL ACAD SCI USA, V93, P14726, DOI 10.1073/pnas.93.25.14726
   Nagasawa T, 1996, NATURE, V382, P635, DOI 10.1038/382635a0
   OREGAN S, 1977, AM J DIS CHILD, V131, P655, DOI 10.1001/archpedi.1977.02120190049011
   Pablos JL, 1999, AM J PATHOL, V155, P1577, DOI 10.1016/S0002-9440(10)65474-0
   Shearman JR, 2006, ANIM GENET, V37, P89, DOI 10.1111/j.1365-2052.2005.01413.x
   TASHIRO K, 1993, SCIENCE, V261, P600, DOI 10.1126/science.8342023
   Zlotnik A, 2000, IMMUNITY, V12, P121, DOI 10.1016/S1074-7613(00)80165-X
   ZUELZER WW, 1964, NEW ENGL J MED, V270, P699, DOI 10.1056/NEJM196404022701402
NR 21
TC 7
Z9 7
U1 0
U2 3
PU ELSEVIER SCIENCE BV
PI AMSTERDAM
PA PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
SN 0165-2427
J9 VET IMMUNOL IMMUNOP
JI Vet. Immunol. Immunopathol.
PD APR 15
PY 2007
VL 116
IS 3-4
BP 219
EP 225
DI 10.1016/j.vetimm.2007.01.008
PG 7
WC Immunology; Veterinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Immunology; Veterinary Sciences
GA 158NG
UT WOS:000245797600011
PM 17316828
DA 2025-04-10
ER

PT J
AU Griffioen, PH
   de Jonge, R
   van Zelst, BD
   Brouns, RM
   Lindemans, J
AF Griffioen, PH
   de Jonge, R
   van Zelst, BD
   Brouns, RM
   Lindemans, J
TI Detection and allele-frequencies of the 833T&gt;C, 844ins68 and a novel
   mutation in the cystathionine β-synthase gene
SO CLINICA CHIMICA ACTA
LA English
DT Article
DE cystathionine beta-synthase; 833T > C; 844ins68; homocysteine;
   cardiovascular disease
ID HOMOCYSTINURIA; PREVALENCE
AB Background: The most common 833T > C/844ins68 in cis double mutation in the cystathionine beta-synthase (CBS) gene probably is non-pathogenic because the 68-bp insertion eliminates the 833T > C mutation due to alternative splicing. However, allele frequency and effects of the isolated 833T > C mutation are unclear.
   Method: DNA was isolated from 500 volunteers and used directly for PCR-RFLP of CBS gene exon-8. A new primer design was developed to create annealing sites upstream and downstream of exon-8 for forward and reverse primers, respectively. The design was made to exclude sequence homology of the forward primer with the insert fragment and to introduce an internal Bsr1 digestion site.
   Results: A new 9276G > A mutation was found in intron 8. Because of this mutation, an extra Bsr1 digestion site is created in intron 8. In Caucasian volunteers, the following allele frequencies were found: 833T > C=0.2%, 833T > C/844ins68=10.2%, and 9276G > A=0.2%.
   Conclusion: The developed PCR-RFLP method is able to detect the 833T > C mutation, the 833T > C/844ins68 polymorphism as well as a new 9276G > A mutation in intron 8. Further study should explore the effect of the isolated 9276G > A mutation. (c) 2004 Elsevier B.V. All rights reserved.
C1 Univ Med Ctr Rotterdam, Erasmus MC, Dept Clin Chem, NL-3000 CA Rotterdam, Netherlands.
C3 Erasmus University Rotterdam; Erasmus MC
RP Univ Med Ctr Rotterdam, Erasmus MC, Dept Clin Chem, POB 2040, NL-3000 CA Rotterdam, Netherlands.
EM p.griffioen@erasmusmc.nl
CR Gaustadnes M, 1999, NEW ENGL J MED, V340, P1513, DOI 10.1056/NEJM199905133401915
   Kraus JP, 1998, GENOMICS, V52, P312, DOI 10.1006/geno.1998.5437
   KRAUS JP, 1998, EUR J PEDIATR, V157, P50
   Linnebank M, 2001, THROMB HAEMOSTASIS, V85, P986, DOI 10.1055/s-0037-1615951
   SEBASTIO G, 1995, AM J HUM GENET, V56, P1324
   Tsai MY, 2000, ATHEROSCLEROSIS, V149, P131, DOI 10.1016/S0021-9150(99)00297-X
   Tsai MY, 1996, AM J HUM GENET, V59, P1262
NR 7
TC 15
Z9 16
U1 0
U2 0
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
SN 0009-8981
EI 1873-3492
J9 CLIN CHIM ACTA
JI Clin. Chim. Acta
PD APR
PY 2005
VL 354
IS 1-2
BP 191
EP 194
DI 10.1016/j.cccn.2004.11.019
PG 4
WC Medical Laboratory Technology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Medical Laboratory Technology
GA 911LQ
UT WOS:000228004400022
PM 15748616
DA 2025-04-10
ER

PT J
AU Claus, P
   Döring, F
   Gringel, S
   Müller-Ostermeyer, F
   Fuhlrott, J
   Kraft, T
   Grothe, C
AF Claus, P
   Döring, F
   Gringel, S
   Müller-Ostermeyer, F
   Fuhlrott, J
   Kraft, T
   Grothe, C
TI Differential intranuclear localization of fibroblast growth factor-2
   isoforms and specific interaction with the survival of motoneuron
   protein
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID SPINAL MUSCULAR-ATROPHY; DISEASE GENE-PRODUCT; MOLECULAR-WEIGHT;
   NUCLEAR-LOCALIZATION; FACTOR-II; CARDIAC MYOCYTES; IN-VITRO;
   ENDOTHELIAL-CELLS; OVER-EXPRESSION; FGF RECEPTOR-1
AB Fibroblast growth factor 2 (FGF-2) is an important modulator of cell growth and differentiation and a neurotrophic factor. FGF-2 occurs in isoforms, at a low molecular weight of 18,000 and at least two high molecular weight forms (21,000 and 23,000), representing alternative translation products from a single mRNA. In addition to its role as an extracellular ligand, FGF-2 localizes to the nuclei of cells. Here we show differential localization of the 18- and 23-kDa isoforms in the nuclei of rat Schwann cells. Whereas the 18-kDa isoform was found in the nucleoli, nucleoplasm, and Cajal bodies, the 23-kDa isoform localized in a punctuate pattern and associates with mitotic chromosomes suggesting different functional roles of the isoforms. Moreover, we show here that the 23-kDa FGF-2 isoform co-immunoprecipitates specifically with the survival of motor neuron protein (SMN). SMN is an assembly and recycling factor of the splicing machinery and locates to the cytoplasm, the nucleoplasm, and nuclear gems, where it co-localizes with 23-kDa FGF-2. Patients with spinal muscular atrophy suffer from fatal degeneration of motoneurons because of mutations and deletions of the gene for the SMN protein.
C1 Hannover Med Sch, Dept Neuroanat, D-30625 Hannover, Germany.
   Hannover Med Sch, Dept Mol & Cell Physiol, D-30625 Hannover, Germany.
C3 Hannover Medical School; Hannover Medical School
RP Claus, P (corresponding author), Hannover Med Sch, Dept Neuroanat, OE 4140,Carl Neuberg Str 1, D-30625 Hannover, Germany.
RI Fuhlrott, Jutta/KDN-6061-2024; Döring, Frank/E-9483-2010; Claus,
   Peter/A-7978-2008
OI Claus, Peter/0000-0003-3824-9445
CR AMALRIC F, 1994, BIOCHEM PHARMACOL, V47, P111, DOI 10.1016/0006-2952(94)90443-X
   Arese M, 1999, MOL BIOL CELL, V10, P1429, DOI 10.1091/mbc.10.5.1429
   BOUCHE G, 1987, P NATL ACAD SCI USA, V84, P6770, DOI 10.1073/pnas.84.19.6770
   BURGESS WH, 1991, CELL REGUL, V2, P87, DOI 10.1091/mbc.2.2.87
   BURWEN SJ, 1987, TRENDS BIOCHEM SCI, V12, P159, DOI 10.1016/0968-0004(87)90074-0
   Choi JK, 2000, MOL VIS, V6, P222
   CLAUS P, 1994, J BIOL CHEM, V269, P33042
   CohenJonathan E, 1997, CANCER RES, V57, P1364
   COLLINS T, 1987, NATURE, V328, P621, DOI 10.1038/328621a0
   Dundr M, 2001, BIOCHEM J, V356, P297, DOI 10.1042/0264-6021:3560297
   Escaffit F, 2000, INT J CANCER, V85, P555, DOI 10.1002/(SICI)1097-0215(20000215)85:4<555::AID-IJC18>3.0.CO;2-H
   ESTIVAL A, 1993, CANCER RES, V53, P1182
   Florkiewicz RZ, 1991, GROWTH FACTORS, V4, P265, DOI 10.3109/08977199109043912
   Friesen WJ, 2001, MOL CELL, V7, P1111, DOI 10.1016/S1097-2765(01)00244-1
   Gall JG, 2000, ANNU REV CELL DEV BI, V16, P273, DOI 10.1146/annurev.cellbio.16.1.273
   Gangwani L, 2001, NAT CELL BIOL, V3, P376, DOI 10.1038/35070059
   GROTHE C, 1992, J NEUROSCI RES, V32, P317, DOI 10.1002/jnr.490320304
   Grothe C, 2000, NEUROSCIENCE, V100, P73, DOI 10.1016/S0306-4522(00)00247-5
   Grothe C, 1998, MOL BRAIN RES, V57, P97, DOI 10.1016/S0169-328X(98)00076-X
   Grothe C, 1996, INT J DEV BIOL, V40, P403
   Gualandris A, 1999, J CELL PHYSIOL, V181, P273, DOI 10.1002/(SICI)1097-4652(199911)181:2<273::AID-JCP9>3.0.CO;2-#
   Hebert MD, 2000, MOL BIOL CELL, V11, P4159, DOI 10.1091/mbc.11.12.4159
   Huber K, 1997, J COMP NEUROL, V382, P189
   IMAMURA T, 1990, SCIENCE, V249, P1567, DOI 10.1126/science.1699274
   Isaac C, 1998, J CELL BIOL, V142, P319, DOI 10.1083/jcb.142.2.319
   Jans DA, 1998, BIOESSAYS, V20, P400, DOI 10.1002/(SICI)1521-1878(199805)20:5<400::AID-BIES7>3.0.CO;2-R
   KIEFER P, 1994, EMBO J, V13, P4126, DOI 10.1002/j.1460-2075.1994.tb06730.x
   Klein S, 2000, J BIOL CHEM, V275, P3150, DOI 10.1074/jbc.275.5.3150
   Lennon G, 1996, GENOMICS, V33, P151, DOI 10.1006/geno.1996.0177
   Lin SY, 2001, NAT CELL BIOL, V3, P802, DOI 10.1038/ncb0901-802
   Liu Q, 1997, CELL, V90, P1013, DOI 10.1016/S0092-8674(00)80367-0
   Liu Q, 1996, EMBO J, V15, P3555, DOI 10.1002/j.1460-2075.1996.tb00725.x
   Lorson CL, 1998, NAT GENET, V19, P63, DOI 10.1038/ng0598-63
   Meisinger C, 1996, J BIOL CHEM, V271, P16520, DOI 10.1074/jbc.271.28.16520
   MOROIANU J, 1994, BIOCHEMISTRY-US, V33, P12535, DOI 10.1021/bi00208a001
   Müller-Ostermeyer F, 2001, GROWTH FACTORS, V19, P175
   Ornitz DM, 1996, J BIOL CHEM, V271, P15292, DOI 10.1074/jbc.271.25.15292
   Pasumarthi KBS, 1996, CIRC RES, V78, P126, DOI 10.1161/01.RES.78.1.126
   PASUMARTHI KBS, 1994, J MOL CELL CARDIOL, V26, P1045, DOI 10.1006/jmcc.1994.1125
   Pederson T, 1998, J CELL BIOL, V143, P279, DOI 10.1083/jcb.143.2.279
   Pellizzoni L, 1998, CELL, V95, P615, DOI 10.1016/S0092-8674(00)81632-3
   Pellizzoni L, 2001, CURR BIOL, V11, P1079, DOI 10.1016/S0960-9822(01)00316-5
   Peng H, 2001, MOL BIOL CELL, V12, P449, DOI 10.1091/mbc.12.2.449
   Pintucci G, 1996, MOL BIOL CELL, V7, P1249, DOI 10.1091/mbc.7.8.1249
   QUARTO N, 1991, J CELL PHYSIOL, V147, P311, DOI 10.1002/jcp.1041470217
   Reimers K, 2001, MOL CELL BIOL, V21, P4996, DOI 10.1128/MCB.21.15.4996-5007.2001
   Sendtner M, 2001, CURR OPIN NEUROL, V14, P629, DOI 10.1097/00019052-200110000-00012
   Sleeman JE, 1999, CURR BIOL, V9, P1065, DOI 10.1016/S0960-9822(99)80475-8
   Stachowiak EK, 1997, ONCOGENE, V14, P2201, DOI 10.1038/sj.onc.1201057
   Stachowiak MK, 1996, MOL BRAIN RES, V38, P161, DOI 10.1016/0169-328X(96)00010-1
   STACHOWIAK MK, 1994, J CELL BIOL, V127, P203, DOI 10.1083/jcb.127.1.203
   Sun CP, 2001, J CELL PHYSIOL, V186, P457, DOI 10.1002/1097-4652(2000)9999:999<000::AID-JCP1044>3.0.CO;2-2
   TENNEKOON GI, 1987, J CELL BIOL, V105, P2315, DOI 10.1083/jcb.105.5.2315
   Terns MP, 2001, CURR BIOL, V11, pR862, DOI 10.1016/S0960-9822(01)00517-6
   Van den Berghe L, 2000, MOL ENDOCRINOL, V14, P1709, DOI 10.1210/me.14.11.1709
   ZHAN X, 1992, BIOCHEM BIOPH RES CO, V188, P982, DOI 10.1016/0006-291X(92)91328-N
NR 56
TC 95
Z9 110
U1 0
U2 3
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
SN 0021-9258
J9 J BIOL CHEM
JI J. Biol. Chem.
PD JAN 3
PY 2003
VL 278
IS 1
BP 479
EP 485
DI 10.1074/jbc.M206056200
PG 7
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 632ZX
UT WOS:000180255700063
PM 12397076
OA hybrid
DA 2025-04-10
ER

PT J
AU Kiang, KMY
   Leung, GKK
AF Kiang, Karrie Mei-Yee
   Leung, Gilberto Ka-Kit
TI A Review on Adducin from Functional to Pathological Mechanisms: Future
   Direction in Cancer
SO BIOMED RESEARCH INTERNATIONAL
LA English
DT Review
ID PROTEIN-KINASE-C; GENOME-WIDE ASSOCIATION; HUMAN ALPHA-ADDUCIN;
   ERYTHROCYTE-MEMBRANE SKELETON; CALMODULIN-BINDING DOMAIN;
   POLYCYSTIC-KIDNEY-DISEASE; SPECTRIN-ACTIN COMPLEXES; CELL-CYCLE
   PROGRESSION; LOW-RENIN HYPERTENSION; MARCKS-RELATED DOMAIN
AB Adducin (ADD) is a family of membrane skeleton proteins including ADD1, ADD2, and ADD3 that are encoded by distinct genes on different chromosomes. Adducin is primarily responsible for the assembly of spectrin-actin network that provides physical support to the plasma membrane and mediates signal transduction in various cellular physiological processes upon regulation by protein kinase C-dependent and calcium/calmodulin-dependent pathways. Abnormal phosphorylation, genetic variations, and alternative splicing of adducin may contribute to alterations in cellular functions involved in pathogenic processes. These alterations are associated with a wide range of diseases including cancer. This paper begins with a discussion on how adducin partakes in the structural formation of membrane skeleton, its regulation, and related functional characteristics, followed by a review on the pathogenesis of hypertension, biliary atresia, and cancer with respect to increased disease susceptibility mediated by adducin polymorphism and/or dysregulation. Given the functional diversity of adducin in different cellular compartments, we aim to provide a knowledge base whereby its pathophysiological roles can be better understood. More importantly, we aim to provide novel insights that may be of significance in turning the adducin model to clinical application.
C1 [Kiang, Karrie Mei-Yee; Leung, Gilberto Ka-Kit] Univ Hong Kong, Queen Mary Hosp, Li Ka Shing Fac Med, Dept Surg, Pok Fu Lam, Hong Kong, Peoples R China.
C3 University of Hong Kong
RP Leung, GKK (corresponding author), Univ Hong Kong, Queen Mary Hosp, Li Ka Shing Fac Med, Dept Surg, Pok Fu Lam, Hong Kong, Peoples R China.
EM gilberto@hku.hk
RI Kiang, Karrie/ABI-2656-2020; Leung, Gilberto Ka Kit/C-4337-2009
OI Leung, Gilberto Ka Kit/0000-0003-3147-3057
CR Abdi KM, 2008, MOL BIOL CELL, V19, P536, DOI 10.1091/mbc.E07-08-0818
   ADEREM A, 1992, CELL, V71, P713, DOI 10.1016/0092-8674(92)90546-O
   Alam S, 2000, J HUM HYPERTENS, V14, P199, DOI 10.1038/sj.jhh.1000944
   Assoian RK, 1997, J CELL BIOL, V136, P1, DOI 10.1083/jcb.136.1.1
   Baines AJ, 2010, PROTOPLASMA, V244, P99, DOI 10.1007/s00709-010-0181-1
   Barkalow KL, 2003, J CELL BIOL, V161, P557, DOI 10.1083/jcb.200211122
   BEAVEN GH, 1985, EUR J CELL BIOL, V36, P299
   Beeks E, 2004, HYPERTENSION, V44, P419, DOI 10.1161/01.HYP.0000141410.72537.fd
   Beeks E, 2001, AM J HYPERTENS, V14, P1185, DOI 10.1016/S0895-7061(01)02216-6
   BENNETT V, 1979, J BIOL CHEM, V254, P2533
   BENNETT V, 1980, J BIOL CHEM, V255, P6424
   BENNETT V, 1979, NATURE, V280, P468, DOI 10.1038/280468a0
   BENNETT V, 1993, ANNU REV CELL BIOL, V9, P27, DOI 10.1146/annurev.cb.09.110193.000331
   BENNETT V, 1988, J BIOL CHEM, V263, P5860
   Bianchi G, 2000, AM J HYPERTENS, V13, P739, DOI 10.1016/S0895-7061(00)00241-7
   BIANCHI G, 1994, P NATL ACAD SCI USA, V91, P3999, DOI 10.1073/pnas.91.9.3999
   Bianchi G, 1997, CURR OPIN NEPHROL HY, V6, P167, DOI 10.1097/00041552-199703000-00010
   BLACKSHEAR PJ, 1993, J BIOL CHEM, V268, P1501
   Blake JA, 2017, NUCLEIC ACIDS RES, V45, pD723, DOI 10.1093/nar/gkw1040
   Bohmer RM, 1996, MOL BIOL CELL, V7, P101
   BOURGUIGNON LYW, 1985, J CELL BIOL, V101, P477, DOI 10.1083/jcb.101.2.477
   BYERS TJ, 1985, P NATL ACAD SCI USA, V82, P6153, DOI 10.1073/pnas.82.18.6153
   Calhoun DA, 2008, CIRCULATION, V117, pE510, DOI 10.1161/CIRCULATIONAHA.108.189141
   Castejon AM, 2003, AM J HYPERTENS, V16, P1018, DOI 10.1016/j.amjhyper.2003.07.022
   Chan PC, 2014, J CELL BIOL, V204, P19, DOI 10.1083/jcb.201306083
   CHAPLINE C, 1993, J BIOL CHEM, V268, P6858
   Chen CL, 2007, J CELL SCI, V120, P1157, DOI 10.1242/jcs.03408
   Chen CL, 2011, TRAFFIC, V12, P1327, DOI 10.1111/j.1600-0854.2011.01245.x
   Cheng G, 2013, J HEPATOL, V59, P1285, DOI 10.1016/j.jhep.2013.07.021
   Cho YS, 2009, NAT GENET, V41, P527, DOI 10.1038/ng.357
   Ciechanowicz A, 2001, KIDNEY BLOOD PRESS R, V24, P201, DOI 10.1159/000054228
   Citterio L, 1999, BIOCHEM BIOPH RES CO, V266, P110, DOI 10.1006/bbrc.1999.1769
   Clark CJ, 2000, HYPERTENSION, V36, P990, DOI 10.1161/01.HYP.36.6.990
   Cusi D, 1997, LANCET, V349, P1353, DOI 10.1016/S0140-6736(97)01029-5
   DERICK LH, 1992, EUR J CELL BIOL, V57, P317
   Dimke H, 2011, J AM SOC NEPHROL, V22, P508, DOI 10.1681/ASN.2010060606
   Doaei S, 2014, ARYA ATHEROSCLER, V10, P169
   DONG LQ, 1995, J BIOL CHEM, V270, P25534, DOI 10.1074/jbc.270.43.25534
   Dou Xiang-feng, 2004, Zhonghua Yi Xue Za Zhi, V84, P186
   DRENCKHAHN D, 1985, SCIENCE, V230, P1287, DOI 10.1126/science.2933809
   Dutertre M, 2010, CANCER RES, V70, P896, DOI 10.1158/0008-5472.CAN-09-2703
   Efendiev R, 2004, CIRC RES, V95, P1100, DOI 10.1161/01.RES.0000149570.20845.89
   Fan F, 2017, AM J PHYSIOL-RENAL, V312, pF971, DOI 10.1152/ajprenal.00529.2016
   Ferrandi M, 1999, AM J PHYSIOL-HEART C, V277, pH1338, DOI 10.1152/ajpheart.1999.277.4.H1338
   Fischler B, 2002, J PEDIATR-US, V141, P217, DOI 10.1067/mpd.2002.126001
   Fowler L, 1998, CELL GROWTH DIFFER, V9, P177
   Fowler L, 1998, CELL GROWTH DIFFER, V9, P405
   FOWLER V, 1980, J CELL BIOL, V85, P361, DOI 10.1083/jcb.85.2.361
   Fukata Y, 1999, J CELL BIOL, V145, P347, DOI 10.1083/jcb.145.2.347
   GARDNER K, 1987, NATURE, V328, P359, DOI 10.1038/328359a0
   GARDNER K, 1986, J BIOL CHEM, V261, P1339
   Gilligan DM, 1999, P NATL ACAD SCI USA, V96, P10717, DOI 10.1073/pnas.96.19.10717
   Gilligan DM, 2002, BLOOD, V99, P2418, DOI 10.1182/blood.V99.7.2418
   Glorioso N, 2002, HYPERTENSION, V39, P357, DOI 10.1161/hy0202.103065
   Grant FD, 2002, HYPERTENSION, V39, P191, DOI 10.1161/hy0202.104273
   Györffy B, 2006, INT J CANCER, V118, P1699, DOI 10.1002/ijc.21570
   Hadziselimovic N, 2014, CELL, V156, P1153, DOI 10.1016/j.cell.2014.01.054
   HALL JE, 1986, J HYPERTENS, V4, pS57
   HANSEN LK, 1994, MOL BIOL CELL, V5, P967, DOI 10.1091/mbc.5.9.967
   He X, 2003, J HUM HYPERTENS, V17, P69, DOI 10.1038/sj.jhh.1001495
   He X, 2001, CLIN EXP HYPERTENS, V23, P579, DOI 10.1081/CEH-100106828
   Huang HT, 2000, CANCER RES, V60, P6868
   Huang S, 2002, EXP CELL RES, V275, P255, DOI 10.1006/excr.2002.5504
   Huang S, 1998, MOL BIOL CELL, V9, P3179, DOI 10.1091/mbc.9.11.3179
   HUGHES CA, 1995, J BIOL CHEM, V270, P18990, DOI 10.1074/jbc.270.32.18990
   Iwai N, 1997, LANCET, V350, P369, DOI 10.1016/S0140-6736(05)63430-7
   IWIG M, 1995, EUR J CELL BIOL, V67, P145
   Jen J, 2016, ONCOGENE, V35, P2357, DOI 10.1038/onc.2015.296
   JOSHI R, 1990, J BIOL CHEM, V265, P13130
   JOSHI R, 1991, J CELL BIOL, V115, P665, DOI 10.1083/jcb.115.3.665
   Ju ZY, 2003, J HYPERTENS, V21, P1861, DOI 10.1097/00004872-200310000-00013
   KAISER HW, 1989, J CELL BIOL, V109, P557, DOI 10.1083/jcb.109.2.557
   Kamitani A, 1998, HYPERTENSION, V32, P138, DOI 10.1161/01.HYP.32.1.138
   Khan AA, 2008, J BIOL CHEM, V283, P14600, DOI 10.1074/jbc.M707818200
   Kiley SC, 1999, ONCOGENE, V18, P6748, DOI 10.1038/sj.onc.1203101
   KIM JY, 1994, BIOPHYS J, V67, P227, DOI 10.1016/S0006-3495(94)80473-4
   Kimura K, 1998, J BIOL CHEM, V273, P5542, DOI 10.1074/jbc.273.10.5542
   Krieger C, 2016, FRONT CELL NEUROSCI, V10, DOI 10.3389/fncel.2016.00011
   Kruer MC, 2013, ANN NEUROL, V74, P805, DOI 10.1002/ana.23971
   Kugelmann D, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0126213
   Kuhlman PA, 1996, J BIOL CHEM, V271, P7986, DOI 10.1074/jbc.271.14.7986
   Lahortiga I, 2003, CANCER RES, V63, P3079
   Lam DH, 2001, LEUKEMIA, V15, P1689, DOI 10.1038/sj.leu.2402269
   Langer W, 2010, BMC GENOMICS, V11, DOI 10.1186/1471-2164-11-676
   Lechuga S., 2017, FASEB J, P31
   Leite SC, 2016, CELL REP, V15, P490, DOI 10.1016/j.celrep.2016.03.047
   LEVINE J, 1983, P NATL ACAD SCI-BIOL, V80, P191, DOI 10.1073/pnas.80.1.191
   Levy D, 2009, NAT GENET, V41, P677, DOI 10.1038/ng.384
   Li J, 2017, J MATERN-FETAL NEO M, V30, P1882, DOI 10.1080/14767058.2016.1228102
   Li XL, 1998, J BIOL CHEM, V273, P19329, DOI 10.1074/jbc.273.30.19329
   Liao XY, 2015, MED SCI MONITOR, V21, P1634, DOI 10.12659/MSM.893191
   LING E, 1986, J BIOL CHEM, V261, P13875
   Liu CM, 2017, J BIOMED SCI, V24, DOI 10.1186/s12929-017-0333-0
   Lou H, 2013, J MOL NEUROSCI, V49, P1, DOI 10.1007/s12031-012-9827-0
   Ma PC, 2007, BRIT J CANCER, V97, P368, DOI 10.1038/sj.bjc.6603884
   Mammoto A, 2004, J BIOL CHEM, V279, P26323, DOI 10.1074/jbc.M402725200
   Manunta P, 1998, KIDNEY INT, V53, P1471, DOI 10.1046/j.1523-1755.1998.00931.x
   Manunta P, 1999, HYPERTENSION, V33, P694, DOI 10.1161/01.HYP.33.2.694
   Manunta P, 2008, HYPERTENSION, V52, P366, DOI 10.1161/HYPERTENSIONAHA.108.113977
   Mariani L, 2001, J NEURO-ONCOL, V53, P161, DOI 10.1023/A:1012253317934
   Matou-Nasri S, 2009, INT J ONCOL, V35, P761, DOI 10.3892/ijo_00000389
   Matsuoka Y, 1998, J CELL BIOL, V142, P485, DOI 10.1083/jcb.142.2.485
   Matsuoka Y, 1996, J BIOL CHEM, V271, P25157, DOI 10.1074/jbc.271.41.25157
   Matsuoka Y, 2000, CELL MOL LIFE SCI, V57, P884, DOI 10.1007/PL00000731
   MCLAUGHLIN S, 1995, TRENDS BIOCHEM SCI, V20, P272, DOI 10.1016/S0968-0004(00)89042-8
   Melander O, 2000, J HUM HYPERTENS, V14, P43, DOI 10.1038/sj.jhh.1000942
   Merta M, 2003, KIDNEY BLOOD PRESS R, V26, P42, DOI 10.1159/000069768
   MISCHE SM, 1987, J CELL BIOL, V105, P2837, DOI 10.1083/jcb.105.6.2837
   Misra UK, 2012, NEUROL SCI, V33, P1071, DOI 10.1007/s10072-011-0903-y
   Mitchison TJ, 1996, CELL, V84, P371, DOI 10.1016/S0092-8674(00)81281-7
   Morrison AC, 2002, HYPERTENSION, V39, P1053, DOI 10.1161/01.HYP.0000019128.94483.3A
   Morrison AC, 2001, STROKE, V32, P822, DOI 10.1161/01.STR.32.4.822
   Mulatero P, 2002, J CLIN ENDOCR METAB, V87, P3337, DOI 10.1210/jc.87.7.3337
   Nakamura T, 1999, BLOOD, V94, P741, DOI 10.1182/blood.V94.2.741.414k04_741_747
   Narita I, 2003, HYPERTENSION, V42, P304, DOI 10.1161/01.HYP.0000085193.25617.78
   Naydenov NG, 2010, MOL BIOL CELL, V21, P3506, DOI 10.1091/mbc.E10-03-0259
   NEHLS V, 1991, BLOOD, V78, P1692
   NELSON WJ, 1983, P NATL ACAD SCI-BIOL, V80, P1626, DOI 10.1073/pnas.80.6.1626
   Newton-Cheh C, 2009, NAT GENET, V41, P666, DOI 10.1038/ng.361
   Nicod J, 2002, KIDNEY INT, V61, P1270, DOI 10.1046/j.1523-1755.2002.00275.x
   Ningappa M, 2015, WIRES SYST BIOL MED, V7, P267, DOI 10.1002/wsbm.1303
   Niu TH, 1999, HYPERTENSION, V33, P1332, DOI 10.1161/01.HYP.33.6.1332
   OHANIAN V, 1984, BIOCHEMISTRY-US, V23, P4416, DOI 10.1021/bi00314a027
   Org E, 2009, HUM MOL GENET, V18, P2288, DOI 10.1093/hmg/ddp135
   Pariser H, 2005, P NATL ACAD SCI USA, V102, P12407, DOI 10.1073/pnas.0505901102
   PERRIN D, 1987, NATURE, V326, P498, DOI 10.1038/326498a0
   Persu A, 2003, NEPHROL DIAL TRANSPL, V18, P2032, DOI 10.1093/ndt/gfg292
   PINDER JC, 1975, NATURE, V258, P765, DOI 10.1038/258765a0
   PINDER JC, 1984, FEBS LETT, V169, P161, DOI 10.1016/0014-5793(84)80310-5
   Poon MW, 2015, ANTICANCER RES, V35, P6487
   Porro F, 2010, GENES BRAIN BEHAV, V9, P84, DOI 10.1111/j.1601-183X.2009.00537.x
   Psaty BM, 2000, J HUM HYPERTENS, V14, P95, DOI 10.1038/sj.jhh.1000943
   Psaty BM, 2002, JAMA-J AM MED ASSOC, V287, P1680, DOI 10.1001/jama.287.13.1680
   Qu YL, 2016, CELL MOL BIOL, V62, P62, DOI 10.14715/cmb/2016.62.13.11
   Ramirez GA, 2015, RHEUMATOL INT, V35, P1975, DOI 10.1007/s00296-015-3298-x
   Ramu P, 2010, Indian J Hum Genet, V16, P8, DOI 10.4103/0971-6866.64938
   Rani SB, 2013, NEURO-ONCOLOGY, V15, P1302, DOI 10.1093/neuonc/not090
   REID ME, 1990, BLOOD, V75, P2229
   Reshetnikova G, 2000, EXP CELL RES, V259, P35, DOI 10.1006/excr.2000.4966
   Robledo RF, 2008, BLOOD, V112, P4298, DOI 10.1182/blood-2008-05-156000
   Sahr KE, 2009, AM J HEMATOL, V84, P354, DOI 10.1002/ajh.21427
   SALARDI S, 1988, J HYPERTENS, V6, pS196, DOI 10.1097/00004872-198812040-00058
   SCARAMUZZINO DA, 1993, P NATL ACAD SCI USA, V90, P3398, DOI 10.1073/pnas.90.8.3398
   SEIDEL B, 1995, BRAIN RES, V700, P13, DOI 10.1016/0006-8993(95)00962-P
   Seidlerová J, 2009, J HUM HYPERTENS, V23, P55, DOI 10.1038/jhh.2008.113
   Senderowicz AM, 2003, CANCER CHEMOTH PHARM, V52, pS61, DOI 10.1007/s00280-003-0624-x
   Shen N, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0121485
   Shi YN, 2013, INT J NANOMED, V8, P1, DOI 10.2147/IJN.S38648
   Shioji K, 2004, HYPERTENS RES, V27, P31, DOI 10.1291/hypres.27.31
   Staessen JA, 2001, J HYPERTENS, V19, P1349, DOI 10.1097/00004872-200108000-00002
   Sugimoto K, 2002, J HYPERTENS, V20, P1779, DOI 10.1097/00004872-200209000-00022
   Tamaki S, 1998, HYPERTENS RES-CLIN E, V21, P29, DOI 10.1291/hypres.21.29
   Tang V, 2016, J PEDIATR GASTR NUTR, V63, P524, DOI 10.1097/MPG.0000000000001375
   TAYLOR KA, 1994, BIOPHYS J, V67, P1976, DOI 10.1016/S0006-3495(94)80680-0
   Tikhonoff V, 2003, AM J HYPERTENS, V16, P840, DOI 10.1016/S0895-7061(03)00975-0
   Tikhonoff V, 2003, BLOOD PRESS MONIT, V8, P151, DOI 10.1097/00126097-200308000-00004
   TILNEY LG, 1975, J CELL BIOL, V66, P508, DOI 10.1083/jcb.66.3.508
   Tobin MD, 2004, EUR HEART J, V25, P459, DOI 10.1016/j.ehj.2003.11.014
   Tripodi G, 2004, BIOCHEM BIOPH RES CO, V324, P562, DOI 10.1016/j.bbrc.2004.09.079
   Tripodi G, 1997, BIOCHEM BIOPH RES CO, V237, P685, DOI 10.1006/bbrc.1997.7173
   Tripodi G, 1996, J CLIN INVEST, V97, P2815, DOI 10.1172/JCI118737
   Tsai EA, 2014, HUM GENET, V133, P235, DOI 10.1007/s00439-013-1368-2
   Turner ST, 2003, AM J HYPERTENS, V16, P834, DOI 10.1016/S0895-7061(03)01011-2
   TYLER JM, 1980, J BIOL CHEM, V255, P7034
   UNGEWICKELL E, 1979, NATURE, V280, P811, DOI 10.1038/280811a0
   van den Boom J, 2003, AM J PATHOL, V163, P1033, DOI 10.1016/S0002-9440(10)63463-3
   van Rijn MJE, 2006, STROKE, V37, P2930, DOI 10.1161/01.STR.0000248760.67039.2b
   Walters DK, 2008, ANTICANCER RES, V28, P673
   Wang JG, 2003, J HYPERTENS, V21, P1475, DOI 10.1097/00004872-200308000-00010
   Wang JG, 2002, KIDNEY INT, V62, P2152, DOI 10.1046/j.1523-1755.2002.00691.x
   Wang Meng-han, 2013, Zhonghua Zhong Liu Za Zhi, V35, P311, DOI 10.3760/cma.j.issn.0253-3766.2013.04.016
   WASEEM A, 1990, J CELL SCI, V96, P93
   Winnicki M, 2002, J HYPERTENS, V20, P1771, DOI 10.1097/00004872-200209000-00021
   Workman RF, 1998, J BIOL CHEM, V273, P6171, DOI 10.1074/jbc.273.11.6171
   Xu K, 2013, SCIENCE, V339, P452, DOI 10.1126/science.1232251
   Yamagishi K, 2004, AM J HYPERTENS, V17, P385, DOI 10.1016/j.amjhyper.2003.12.018
   Ye YQ, 2017, PLOS ONE, V12, DOI 10.1371/journal.pone.0180896
   YU J, 1973, Journal of Supramolecular Structure, V1, P233, DOI 10.1002/jss.400010308
   Zeng SD, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0107977
   Zhang LN, 2013, BIOMED RES INT, V2013, DOI 10.1155/2013/451094
   Zhu DL, 2002, CHINESE MED J-PEKING, V115, P654
   Zoccali C, 2000, NEPHROL DIAL TRANSPL, V15, P69, DOI 10.1093/ndt/15.suppl_6.69
NR 182
TC 30
Z9 32
U1 0
U2 7
PU HINDAWI LTD
PI LONDON
PA ADAM HOUSE, 3RD FLR, 1 FITZROY SQ, LONDON, W1T 5HF, ENGLAND
SN 2314-6133
EI 2314-6141
J9 BIOMED RES INT
JI Biomed Res. Int.
PY 2018
VL 2018
AR 3465929
DI 10.1155/2018/3465929
PG 14
WC Biotechnology & Applied Microbiology; Medicine, Research & Experimental
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biotechnology & Applied Microbiology; Research & Experimental Medicine
GA GG0BA
UT WOS:000432341700001
PM 29862265
OA hybrid, Green Submitted, Green Published
DA 2025-04-10
ER

PT J
AU McDaniel, JS
   Babu, RAS
   Navarro, MM
   LeBaron, RG
AF McDaniel, Jennifer S.
   Babu, Ramya Akula Suresh
   Navarro, Mary M.
   LeBaron, Richard G.
TI Transcriptional regulation of proteoglycan 4 by 17β-estradiol in
   immortalized baboon temporomandibular joint disc cells
SO EUROPEAN JOURNAL OF ORAL SCIENCES
LA English
DT Article
DE alternative splicing; proteoglycan 4; temporomandibular joint;
   extracellular matrix; estrogen
ID BOUNDARY LUBRICANT; ESTROGEN-RECEPTORS; GENE; HORMONES; PERICARDITIS;
   EXPRESSION; MUTATIONS; PROTEIN; FORCES; CACP
AB Temporomandibular joint disorders (TMDs) affect a significant portion of the population of the USA, with the majority of those seeking treatment being women of childbearing age. Owing to this striking sexual dimorphism it has been postulated that sex hormones play a role in the maintenance of normal temporomandibular joint (TMJ) function. Proteoglycan 4 (PRG4) is a secreted lubricating molecule required for maintaining low frictional levels within articular joints; however, its role in the TMJ is not well characterized. In this study we describe the development of immortalized baboon cells isolated from specific regions of the TMJ disc and their use in the investigation of PRG4 expression and localization patterns in the TMJ. We identified conserved estrogen response elements within the 5 ' flanking region of the PRG4 gene of several species, and found that treatment of baboon TMJ disc cells with estrogen led to reduced PRG4 promoter activity and reduced expression of PRG4 mRNA in vitro. The observed negative regulation of PRG4 by estrogen could lead to increased friction and degradation of joint components over time. This study, for the first time, provides evidence of the regulatory potential of estrogen on PRG4 gene expression and suggests a novel etiology for the gender disparity observed among TMD patients.
C1 [McDaniel, Jennifer S.; Babu, Ramya Akula Suresh; Navarro, Mary M.; LeBaron, Richard G.] Univ Texas San Antonio, San Antonio, TX 78249 USA.
C3 University of Texas System; University of Texas at San Antonio (UTSA)
RP McDaniel, JS (corresponding author), Univ Texas San Antonio, One UTSA Circle, San Antonio, TX 78249 USA.
EM s.jennifer@sbcglobal.net
RI Lebaron, Richard/K-4722-2013
FU Oral and Maxillofacial Surgery Foundation;  [5G12RR013646-12]
FX We would like to thank the Oral and Maxillofacial Surgery Foundation for
   their support of this project. We would also like to thank the Research
   Center in Minority Institution Advanced Imaging Core at the University
   of Texas at San Antonio, supported by grant #5G12RR013646-12, for their
   assistance with the confocal microscopy data acquisition.
CR ABUBAKER AO, 1993, J ORAL MAXIL SURG, V51, P1096
   Abubaker AO, 1996, J ORAL MAXIL SURG, V54, P721, DOI 10.1016/S0278-2391(96)90690-4
   Alazami AM, 2006, HUM MUTAT, V27, DOI 10.1002/humu.9399
   AUFDEMORTE TB, 1986, ORAL SURG ORAL MED O, V61, P307, DOI 10.1016/0030-4220(86)90407-X
   BOYD RL, 1990, AM J ORTHOD DENTOFAC, V97, P472, DOI 10.1016/S0889-5406(05)80027-7
   CAVAILLES V, 1993, P NATL ACAD SCI USA, V90, P203, DOI 10.1073/pnas.90.1.203
   Coles JM, 2010, ARTHRITIS RHEUM-US, V62, P1666, DOI 10.1002/art.27436
   Condon J, 2002, BIOL REPROD, V67, P506, DOI 10.1095/biolreprod67.2.506
   Detamore MS, 2006, J ORAL MAXIL SURG, V64, P243, DOI 10.1016/j.joms.2005.10.009
   Detamore MS, 2003, TISSUE ENG, V9, P1065, DOI 10.1089/10763270360727991
   Frasor J, 2003, ENDOCRINOLOGY, V144, P4562, DOI 10.1210/en.2003-0567
   Gargett CE, 2000, HUM REPROD, V15, P293, DOI 10.1093/humrep/15.2.293
   Grabe N., 2002, SILICO BIOL, V2, P1
   Herring S. W., 2003, Journal of Musculoskeletal & Neuronal Interactions, V3, P391
   JAY GD, 1992, CONNECT TISSUE RES, V28, P71, DOI 10.3109/03008209209014228
   Landi N, 2004, Minerva Stomatol, V53, P651
   Larkin MA, 2007, BIOINFORMATICS, V23, P2947, DOI 10.1093/bioinformatics/btm404
   Leonandi R, 2012, ARCH ORAL BIOL, V57, P614, DOI 10.1016/j.archoralbio.2011.12.004
   Leonardi R, 2012, ACTA HISTOCHEM, V114, P1, DOI 10.1016/j.acthis.2010.11.011
   LeResche L, 1997, PAIN, V69, P153, DOI 10.1016/S0304-3959(96)03230-7
   Marcelino J, 1999, NAT GENET, V23, P319, DOI 10.1038/15496
   McDaniel JS, 2010, THESIS U TEXAS SAN A
   MILAM SB, 1987, ORAL SURG ORAL MED O, V64, P527, DOI 10.1016/0030-4220(87)90025-9
   Nanci A., 2007, TENCATES ORAL HISTOL, P358
   Nitzan DW, 2003, CELLS TISSUES ORGANS, V174, P6, DOI 10.1159/000070570
   Nitzan DW, 2002, INT J ORAL MAX SURG, V31, P94, DOI 10.1054/ijom.2001.0153
   Nugent GE, 2006, ARTHRITIS RHEUM-US, V54, P1888, DOI 10.1002/art.21831
   Nugent-Derfus GE, 2007, OSTEOARTHR CARTILAGE, V15, P566, DOI 10.1016/j.joca.2006.10.015
   Rhee DK, 2005, J BIOL CHEM, V280, P31325, DOI 10.1074/jbc.M505401200
   Rhee DK, 2005, J CLIN INVEST, V115, P622, DOI 10.1172/JCI200522263
   Ruan MZC, 2013, SCI TRANSL MED, V5, DOI 10.1126/scitranslmed.3005409
   Schaefer DB, 2004, BIORHEOLOGY, V41, P503
   Schmidt TA, 2013, JAMA OPHTHALMOL, V131, P766, DOI 10.1001/jamaophthalmol.2013.2385
   SHULL JD, 1987, J STEROID BIOCHEM, V26, P451, DOI 10.1016/0022-4731(87)90055-0
   SWANN DA, 1972, J BIOL CHEM, V247, P8069
   SWANN DA, 1981, J BIOL CHEM, V256, P5921
   VERMA UN, 1995, J RHEUMATOL, V22, P2349
   Wang DY, 2004, MOL ENDOCRINOL, V18, P402, DOI 10.1210/me.2003-0202
   Warren MP, 2001, CELLS TISSUES ORGANS, V169, P187, DOI 10.1159/000047881
   Wimmer MA, 2009, J BIOMECH, V42, P424, DOI 10.1016/j.jbiomech.2008.12.003
   Wingender E, 1996, NUCLEIC ACIDS RES, V24, P238, DOI 10.1093/nar/24.1.238
   Yasuoka T, 2000, J ORAL MAXIL SURG, V58, P189, DOI 10.1016/S0278-2391(00)90337-9
   Zappone B, 2008, LANGMUIR, V24, P1495, DOI 10.1021/la702383n
NR 43
TC 8
Z9 8
U1 0
U2 6
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0909-8836
EI 1600-0722
J9 EUR J ORAL SCI
JI Eur. J. Oral Sci.
PD APR
PY 2014
VL 122
IS 2
BP 100
EP 108
DI 10.1111/eos.12119
PG 9
WC Dentistry, Oral Surgery & Medicine
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Dentistry, Oral Surgery & Medicine
GA AC5VM
UT WOS:000332589100002
PM 24621258
OA Bronze, Green Accepted
DA 2025-04-10
ER

PT J
AU Ki, CS
   Hong, JS
   Jeong, GY
   Ahn, KJ
   Choi, KM
   Kim, DK
   Kim, JW
AF Ki, CS
   Hong, JS
   Jeong, GY
   Ahn, KJ
   Choi, KM
   Kim, DK
   Kim, JW
TI Identification of lamin A/C (LMNA) gene mutations in Korean
   patients with autosomal dominant Emery-Dreifuss muscular dystrophy and
   limb-girdle muscular dystrophy 1B
SO JOURNAL OF HUMAN GENETICS
LA English
DT Article
DE lamin A/C; LMNA; autosomal dominant emery-dreifuss muscular dystrophy;
   EDMD2; limb-girdle muscular dystrophy 1B; LGMDlB
AB Mutations in the LMNA gene encoding lamins A and C by alternative splicing have been found to cause at least four different kinds of genetic disorders: autosomal dominant Emery-Dreifuss muscular dystrophy (EDMD2; MIM 181350) limb-girdle muscular dystrophy type 1B (LGMD1B; MIM 159001); dilated cardiomyopathy type 1A (CMD1A; MIM 115200) and familial partial lipodystrophy (FPLD; MIM 151660). Recently, we have studied two Korean patients with atrioventricular conduction defects. They had variable extents of muscular dystrophy; one patient was diagnosed with EDMD2 and the other with LGMD1B. We performed a mutation analysis of the LMNA gene by direct sequencing and found two different missense mutations: R249Q and R377L, in the EDMD2 and LGMD1B patient, respectively. The R249Q mutation is located within the central rod domain of the LMNA gene, and has been described in at least five unrelated sporadic EDMD2 patients. On the other hand, the R377L mutation. also located within the rod domain, is a novel mutation, although a histidine substitution instead of leucine (R377H) has been reported previously in an LGMD1B patient. To our knowledge, this is the first report of LMNA gene mutations in Korean patients with EDMD2 and LGMD1B.
C1 Sungkyunkwan Univ, Sch Med, Samsung Med Ctr, Dept Clin Pathol,Kanagnam Ku, Seoul 135710, South Korea.
   Sungkyunkwan Univ, Sch Med, Dept Internal Med, Seoul, South Korea.
   Seoul Med Sci Inst, Seoul Clin Labs, Dept Clin Pathol, Seoul, South Korea.
   Han Il Gen Hosp, Dept Internal Med, Seoul, South Korea.
C3 Sungkyunkwan University (SKKU); Samsung Medical Center; Sungkyunkwan
   University (SKKU)
RP Sungkyunkwan Univ, Sch Med, Samsung Med Ctr, Dept Clin Pathol,Kanagnam Ku, 50 Ilwon Dong, Seoul 135710, South Korea.
EM culture@med.skku.ac.kr
RI Kim, Duk/F-4613-2014; Ki, Chang-Seok/G-7559-2014
OI Kim, Duk-Kyung/0000-0002-2348-8948; Ki, Chang-Seok/0000-0001-7679-8731
CR Bonne G, 2000, ANN NEUROL, V48, P170, DOI 10.1002/1531-8249(200008)48:2<170::AID-ANA6>3.0.CO;2-J
   Bonne G, 1999, NAT GENET, V21, P285, DOI 10.1038/6799
   Brown CA, 2001, AM J MED GENET, V102, P359, DOI 10.1002/ajmg.1463
   di Barletta MR, 2000, AM J HUM GENET, V66, P1407, DOI 10.1086/302869
   Emery AEH, 2000, NEUROMUSCULAR DISORD, V10, P228, DOI 10.1016/S0960-8966(00)00105-X
   Fatkin D, 1999, NEW ENGL J MED, V341, P1715, DOI 10.1056/NEJM199912023412302
   Genschel J, 2000, HUM MUTAT, V16, P451, DOI 10.1002/1098-1004(200012)16:6<451::AID-HUMU1>3.3.CO;2-0
   HEALD R, 1990, CELL, V61, P579, DOI 10.1016/0092-8674(90)90470-Y
   Kitaguchi T, 2001, NEUROMUSCULAR DISORD, V11, P542, DOI 10.1016/S0960-8966(01)00207-3
   Muchir A, 2000, HUM MOL GENET, V9, P1453, DOI 10.1093/hmg/9.9.1453
   Nagano A, 2000, CURR OPIN NEUROL, V13, P533, DOI 10.1097/00019052-200010000-00005
   Shackleton S, 2000, NAT GENET, V24, P153, DOI 10.1038/72807
   Stuurman N, 1998, J STRUCT BIOL, V122, P42, DOI 10.1006/jsbi.1998.3987
   Van Der Kooi A. J., 1996, Annals of Neurology, V39, P636, DOI 10.1002/ana.410390513
NR 14
TC 31
Z9 34
U1 0
U2 4
PU NATURE PUBLISHING GROUP
PI NEW YORK
PA 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA
SN 1434-5161
EI 1435-232X
J9 J HUM GENET
JI J. Hum. Genet.
PY 2002
VL 47
IS 5
BP 225
EP 228
DI 10.1007/s100380200029
PG 4
WC Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Genetics & Heredity
GA 555EV
UT WOS:000175781900002
PM 12032588
OA Bronze
DA 2025-04-10
ER

PT J
AU Uapinyoying, P
   Goecks, J
   Knoblach, SM
   Panchapakesan, K
   Bonnemann, CG
   Partridge, TA
   Jaiswal, JK
   Hoffman, EP
AF Uapinyoying, Prech
   Goecks, Jeremy
   Knoblach, Susan M.
   Panchapakesan, Karuna
   Bonnemann, Carsten G.
   Partridge, Terence A.
   Jaiswal, Jyoti K.
   Hoffman, Eric P.
TI A long-read RNA-seq approach to identify novel transcripts of very large
   genes
SO GENOME RESEARCH
LA English
DT Article
ID N-RAP; SKELETAL-MUSCLE; GENOMIC ORGANIZATION; NEBULIN FAMILY; MOUSE
   NEBULIN; LIM PROTEIN; TITIN; EXPRESSION; LOCALIZATION; SEQUENCE
AB RNA-seq is widely used for studying gene expression, but commonly used sequencing platforms produce short reads that only span up to two exon junctions per read. This makes it difficult to accurately determine the composition and phasing of exons within transcripts. Although long-read sequencing improves this issue, it is not amenable to precise quantitation, which limits its utility for differential expression studies. We used long-read isoform sequencing combined with a novel analysis approach to compare alternative splicing of large, repetitive structural genes in muscles. Analysis of muscle structural genes that produce medium (Nrap: 5 kb), large (Neb: 22 kb), and very large (Ttn: 106 kb) transcripts in cardiac muscle, and fast and slow skeletal muscles identified unannotated exons for each of these ubiquitous muscle genes. This also identified differential exon usage and phasing for these genes between the different muscle types. By mapping the in-phase transcript structures to known annotations, we also identified and quantified previously unannotated transcripts. Results were confirmed by endpoint PCR and Sanger sequencing, which revealed muscle-type-specific differential expression of these novel transcripts. The improved transcript identification and quantification shown by our approach removes previous impediments to studies aimed at quantitative differential expression of ultralong transcripts.
C1 [Uapinyoying, Prech; Knoblach, Susan M.; Panchapakesan, Karuna; Bonnemann, Carsten G.; Partridge, Terence A.; Jaiswal, Jyoti K.; Hoffman, Eric P.] Childrens Natl Hlth Syst, Childrens Res Inst, Ctr Genet Med Res, Washington, DC 20010 USA.
   [Uapinyoying, Prech; Knoblach, Susan M.; Partridge, Terence A.; Jaiswal, Jyoti K.] George Washington Univ, Sch Med & Hlth Sci, Dept Genom & Precis Med, Washington, DC 20052 USA.
   [Uapinyoying, Prech; Bonnemann, Carsten G.] NINDS, Neuromuscular & Neurogenet Disorders Childhood Se, NIH, Bldg 36,Rm 4D04, Bethesda, MD 20892 USA.
   [Goecks, Jeremy] Oregon Hlth & Sci Univ, Computat Biol Program, Portland, OR 97239 USA.
   [Hoffman, Eric P.] Binghamton Univ, Sch Pharm & Pharmaceut Sci, Dept Pharmaceut Sci, Binghamton, NY 13902 USA.
C3 Children's National Health System; George Washington University;
   National Institutes of Health (NIH) - USA; NIH National Institute of
   Neurological Disorders & Stroke (NINDS); Oregon Health & Science
   University; State University of New York (SUNY) System; Binghamton
   University, SUNY
RP Uapinyoying, P (corresponding author), Childrens Natl Hlth Syst, Childrens Res Inst, Ctr Genet Med Res, Washington, DC 20010 USA.; Uapinyoying, P (corresponding author), George Washington Univ, Sch Med & Hlth Sci, Dept Genom & Precis Med, Washington, DC 20052 USA.; Uapinyoying, P (corresponding author), NINDS, Neuromuscular & Neurogenet Disorders Childhood Se, NIH, Bldg 36,Rm 4D04, Bethesda, MD 20892 USA.
EM prech.uapinyoying@nih.gov
RI Jaiswal, Jyoti/ABI-1666-2020; Hoffman, Eric/KYP-6390-2024; Jaiswal,
   Jyoti/M-5891-2013
OI Jaiswal, Jyoti/0000-0002-5992-5185; Hoffman, Eric/0000-0001-6470-5139;
   Goecks, Jeremy/0000-0002-4583-5226; Uapinyoying,
   Prech/0000-0003-1950-4164; Partridge, Terence/0000-0003-0203-758X
FU National Institutes of Health, District of Columbia Intellectual and
   Developmental Disabilities Research Center Award (DC-IDDRC) program
   [1U54HD090257]; National Institutes of Health [R01NS029525, T32AR056993]
FX We thank Adam K.L. Wong, Keith Crandall, and the Colonial One HPC team
   at GeorgeWashington University for providing technical support and
   computational resources for the project; Hiroki Morizono for
   bioinformatics lessons and insight; Linda Werling for academic and
   motivational support; Heather Locovare for helping us optimize the
   Iso-Seq bench protocol; and Jaakko Saparanta for corrections regarding
   Ttn exon 312. We thank past and present members of the Eric Hoffman
   laboratory and the Genetic Medicine department at Children's National
   Hospital for helpful discussions. This project was supported by award
   number 1U54HD090257 from the National Institutes of Health, District of
   Columbia Intellectual and Developmental Disabilities Research Center
   Award (DC-IDDRC) program. Its contents are solely the responsibility of
   the authors and do not necessarily represent the official views of the
   District of Columbia Intellectual and Developmental Disabilities
   Research Center or the National Institutes of Health. Additional support
   was provided by the National Institutes of Health award numbers
   R01NS029525 (NINDS) and T32AR056993 (NIAMS).
CR Anders S, 2015, BIOINFORMATICS, V31, P166, DOI 10.1093/bioinformatics/btu638
   Anders S, 2012, GENOME RES, V22, P2008, DOI 10.1101/gr.133744.111
   [Anonymous], 2010, J BIOMED BIOTECHNOL, DOI 10.1155/2010/753675
   Bang ML, 2015, CIRC J, V79, P2081, DOI 10.1253/circj.CJ-15-0854
   Bang ML, 2001, CIRC RES, V89, P1065, DOI 10.1161/hh2301.100981
   Bolger AM, 2014, BIOINFORMATICS, V30, P2114, DOI 10.1093/bioinformatics/btu170
   Buck D, 2010, J STRUCT BIOL, V170, P325, DOI 10.1016/j.jsb.2010.02.014
   Carrol SL, 2000, CELL MOTIL CYTOSKEL, V47, P63, DOI 10.1002/1097-0169(200009)47:1<63::AID-CM6>3.0.CO;2-M
   Carroll S, 2004, J CELL SCI, V117, P105, DOI 10.1242/jcs.00847
   Carroll SL, 2001, J CELL SCI, V114, P4229
   Castle JC, 2008, NAT GENET, V40, P1416, DOI 10.1038/ng.264
   Charton K, 2015, HUM MOL GENET, V24, P3718, DOI 10.1093/hmg/ddv116
   Cock PJA, 2009, BIOINFORMATICS, V25, P1422, DOI 10.1093/bioinformatics/btp163
   Dhume A, 2006, CELL MOTIL CYTOSKEL, V63, P493, DOI 10.1002/cm.20141
   Dobin A, 2013, BIOINFORMATICS, V29, P15, DOI 10.1093/bioinformatics/bts635
   Donner K, 2004, EUR J HUM GENET, V12, P744, DOI 10.1038/sj.ejhg.5201242
   Donner K, 2006, GENOMICS, V88, P489, DOI 10.1016/j.ygeno.2006.06.008
   Frankish A, 2019, NUCLEIC ACIDS RES, V47, pD766, DOI 10.1093/nar/gky955
   Garg A, 2014, J CLIN INVEST, V124, P3529, DOI 10.1172/JCI74994
   Gautel M, 1996, J CELL SCI, V109, P2747
   Gordon SP, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0132628
   Herrera AH, 2000, CELL MOTIL CYTOSKEL, V45, P211, DOI 10.1002/(SICI)1097-0169(200003)45:3<211::AID-CM4>3.0.CO;2-Y
   Joseph C, 2001, BIOCHEMISTRY-US, V40, P4957, DOI 10.1021/bi002739r
   Kinbara K, 1997, ARCH BIOCHEM BIOPHYS, V342, P99, DOI 10.1006/abbi.1997.0108
   Kolmerer B, 1996, J MOL BIOL, V256, P556, DOI 10.1006/jmbi.1996.0108
   LABEIT S, 1991, FEBS LETT, V282, P313, DOI 10.1016/0014-5793(91)80503-U
   LABEIT S, 1995, J MOL BIOL, V248, P308, DOI 10.1016/S0022-2836(95)80052-2
   Laddach A, 2017, BIOINFORMATICS, V33, P3482, DOI 10.1093/bioinformatics/btx424
   Lam LT, 2018, SCI REP-UK, V8, DOI 10.1038/s41598-018-33281-6
   Li YF, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0136653
   Linke WA, 2018, ANNU REV PHYSIOL, V80, P389, DOI 10.1146/annurev-physiol-021317-121234
   Lu SJ, 2008, CELL MOTIL CYTOSKEL, V65, P945, DOI 10.1002/cm.20317
   Luo G, 1997, CELL MOTIL CYTOSKEL, V38, P75
   McElhinny AS, 2005, J CELL BIOL, V170, P947, DOI 10.1083/jcb.200502158
   Mohiddin SA, 2003, CELL MOTIL CYTOSKEL, V55, P200, DOI 10.1002/cm.10123
   NADALGINARD B, 1991, ADV ENZYME REGUL, V31, P261, DOI 10.1016/0065-2571(91)90017-G
   Nam DK, 2002, P NATL ACAD SCI USA, V99, P6152, DOI 10.1073/pnas.092140899
   Nilsen TW, 2010, NATURE, V463, P457, DOI 10.1038/nature08909
   Opitz CA, 2004, CIRC RES, V94, P967, DOI 10.1161/01.RES.0000124301.48193.E1
   Pappas CT, 2011, TRENDS CELL BIOL, V21, P29, DOI 10.1016/j.tcb.2010.09.005
   Politou AS, 2002, J MOL BIOL, V316, P305, DOI 10.1006/jmbi.2001.5312
   Rief M, 1997, SCIENCE, V276, P1109, DOI 10.1126/science.276.5315.1109
   Roberts AM, 2015, SCI TRANSL MED, V7, DOI 10.1126/scitranslmed.3010134
   ROWE RWD, 1973, J CELL BIOL, V57, P261, DOI 10.1083/jcb.57.2.261
   Savarese M, 2018, SKELET MUSCLE, V8, DOI 10.1186/s13395-018-0156-z
   Singh RK, 2018, CELL REP, V24, P197, DOI 10.1016/j.celrep.2018.06.017
   Steijger T, 2013, NAT METHODS, V10, P1177, DOI [10.1038/NMETH.2714, 10.1038/nmeth.2714]
   Thorvaldsdóttir H, 2013, BRIEF BIOINFORM, V14, P178, DOI 10.1093/bib/bbs017
   Trapnell C, 2010, NAT BIOTECHNOL, V28, P511, DOI 10.1038/nbt.1621
   Treangen TJ, 2012, NAT REV GENET, V13, P36, DOI 10.1038/nrg3117
   Wang B, 2016, NAT COMMUN, V7, DOI 10.1038/ncomms11708
   Wang ET, 2008, NATURE, V456, P470, DOI 10.1038/nature07509
   WANG K, 1988, J CELL BIOL, V107, P2199, DOI 10.1083/jcb.107.6.2199
   Weirather Jason L, 2017, F1000Res, V6, P100, DOI 10.12688/f1000research.10571.1
   Witt CC, 2006, EMBO J, V25, P3843, DOI 10.1038/sj.emboj.7601242
   Xin JW, 2016, GENOME BIOL, V17, DOI 10.1186/s13059-016-0953-9
   Yang XP, 2016, CELL, V164, P805, DOI 10.1016/j.cell.2016.01.029
   Zacharchenko T, 2015, BIOCHEM SOC T, V43, P850, DOI 10.1042/BST20150084
   Zhang RQ, 2001, BIOCHEMISTRY-US, V40, P14898, DOI 10.1021/bi0107445
NR 59
TC 26
Z9 28
U1 2
U2 6
PU COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
PI COLD SPRING HARBOR
PA 1 BUNGTOWN RD, COLD SPRING HARBOR, NY 11724 USA
SN 1088-9051
EI 1549-5469
J9 GENOME RES
JI Genome Res.
PD JUN
PY 2020
VL 30
IS 6
BP 885
EP 897
DI 10.1101/gr.259903.119
PG 13
WC Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology;
   Genetics & Heredity
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology;
   Genetics & Heredity
GA MT3WV
UT WOS:000554899700008
PM 32660935
OA hybrid, Green Published, Green Submitted
DA 2025-04-10
ER

PT J
AU Aracil-Sanus, E
   Mendieta-Azcona, C
   Cuesta-Gimeno, C
   Chinchilla-Molina, A
AF Aracil-Sanus, E
   Mendieta-Azcona, C
   Cuesta-Gimeno, C
   Chinchilla-Molina, A
TI Infragenicular bypass graft for limb salvage using
   polytetrafluoroethylene and distal vein cuff as the first alternative in
   patients without ipsilateral greater saphenous vein
SO ANNALS OF VASCULAR SURGERY
LA English
DT Article
ID LOWER-EXTREMITY ISCHEMIA; PROSPECTIVE RANDOMIZED-TRIAL;
   ARTERIOVENOUS-FISTULA; PROSTHETIC BYPASS; INFRAINGUINAL BYPASS;
   INTERPOSITION CUFFS; TIBIAL BYPASS; SPLICED VEIN; PATENCY; ANASTOMOSIS
AB The objectives of this study were to evaluate the results of polytetrafluoroethylene infragenicular bypass grafts with a distal interposition vein cuff in patients with critical limb ischemia in the 14 absence of ipsilateral greater saphenous vein. From January 1997 to June 2002, 58 consecutive below-knee bypass grafts with PTFE and distal interposition vein cuff were performed in 57 patients with a median age of 70.8 years. The distal anastomosis was located at the infragenicular popliteal artery in 18 cases and at tibial vessels in 40. Primary patency, secondary patency, and limb salvage were analyzed using the Kaplan-Meier method. During a median follow-up of 14.4 months (range, 1-50) 26 cases of graft occlusion and 19 major amputations were registered. The primary and secondary patency rates at 12, 24, and 36 months were 57%, 54%, and 47% and 61%, 58%, and 50%, respectively. Limb salvage rates reached 69%, 69%, and 59% at 12, 24, and 36 months. When below-knee revasculanzation is required in patients with limb-threatening ischemia, in the absence ipsilateral greater saphenous vein, PTFE grafts with a distal vein cuff are a reasonable substitute with acceptable long-term patency and limb salvage rates.
C1 Hosp Ramon y Cajal, Div Vasc Surg, Madrid 28033, Spain.
C3 Hospital Universitario Ramon y Cajal
RP Hosp Ramon y Cajal, Div Vasc Surg, Ctra Colmenar Km 9,1, Madrid 28033, Spain.
EM earacil@mundofree.com
CR Ascer E, 1996, J VASC SURG, V24, P134, DOI 10.1016/S0741-5214(96)70154-4
   BERGAN J, 1982, SURGERY, V90, P100
   Calligaro KD, 1997, J VASC SURG, V26, P919, DOI 10.1016/S0741-5214(97)70003-X
   CHANG BB, 1995, J VASC SURG, V21, P403, DOI 10.1016/S0741-5214(95)70282-2
   Chew DKW, 2002, J VASC SURG, V35, P1085, DOI 10.1067/mva.2002.124628
   Dardik H, 1996, J VASC SURG, V24, P240, DOI 10.1016/S0741-5214(96)70099-X
   Faries PL, 2000, J VASC SURG, V31, P50, DOI 10.1016/S0741-5214(00)70067-X
   FICHELLE JM, 1995, ANN VASC SURG, V9, P187, DOI 10.1007/BF02139662
   Fisher RK, 2001, EUR J VASC ENDOVASC, V21, P251, DOI 10.1053/ejvs.2000.1273
   Hamsho A, 1999, EUR J VASC ENDOVASC, V17, P197, DOI 10.1053/ejvs.1998.0671
   HOBSON RW, 1985, J VASC SURG, V2, P174, DOI 10.1067/mva.1985.avs0020174
   HOBSON RW, 1980, ARCH SURG-CHICAGO, V115, P833
   Holzenbein TJ, 1996, J VASC SURG, V23, P130, DOI 10.1016/S0741-5214(05)80043-6
   How TV, 2000, J VASC SURG, V31, P1008, DOI 10.1067/mva.2000.105961
   Jakobsen HL, 1998, EUR J VASC ENDOVASC, V15, P327, DOI 10.1016/S1078-5884(98)80036-1
   Kansal N, 1999, ANN VASC SURG, V13, P386, DOI 10.1007/s100169900273
   Kissin M, 2000, J VASC SURG, V31, P69, DOI 10.1016/S0741-5214(00)70069-3
   Kreienberg PB, 2002, J VASC SURG, V35, P299, DOI 10.1067/mva.2002.121208
   Kreienberg PB, 2000, J VASC SURG, V31, P696, DOI 10.1067/mva.2000.104597
   Kunlin J., 1949, ARCH MAL COEUR VAISS, V42, P371
   MILLER JH, 1984, AUST NZ J SURG, V54, P283, DOI 10.1111/j.1445-2197.1984.tb05318.x
   Neville RF, 1997, AM J SURG, V174, P173, DOI 10.1016/S0002-9610(97)00091-3
   Neville RF, 2001, J VASC SURG, V33, P266, DOI 10.1067/mva.2001.113131
   NORBERTO JJ, 1995, J VASC SURG, V21, P558, DOI 10.1016/S0741-5214(95)70187-7
   ODONNELL TF, 1984, J VASC SURG, V1, P136
   Parsons RE, 1996, J VASC SURG, V23, P347, DOI 10.1016/S0741-5214(96)70280-X
   Piorko D, 2001, EUR J VASC ENDOVASC, V21, P461, DOI 10.1053/ejvs.2001.1353
   RAPTIS S, 1995, BRIT J SURG, V82, P487, DOI 10.1002/bjs.1800820419
   RUTHERFORD RB, 1986, J VASC SURG, V4, P80
   SCHWEIGER H, 1993, J VASC SURG, V18, P867, DOI 10.1016/0741-5214(93)90343-K
   SIEGMAN FA, 1979, SURG GYNECOL OBSTET, V148, P930
   Stonebridge PA, 1997, J VASC SURG, V26, P543, DOI 10.1016/S0741-5214(97)70051-X
   SUGGS WD, 1988, ANN SURG, V207, P717, DOI 10.1097/00000658-198806000-00011
   Tarry WC, 1998, J VASC SURG, V27, P1039, DOI 10.1016/S0741-5214(98)70007-2
   TAYLOR LM, 1987, AM J SURG, V153, P505, DOI 10.1016/0002-9610(87)90803-8
   TAYLOR LM, 1990, J VASC SURG, V11, P193, DOI 10.1067/mva.1990.17235
   TAYLOR RS, 1992, BRIT J SURG, V79, P348
   TYRRELL MR, 1991, BRIT J SURG, V78, P1016, DOI 10.1002/bjs.1800780840
   VEITH FJ, 1980, SURGERY, V87, P581
   VEITH FJ, 1986, J VASC SURG, V3, P104
   Wijesinghe LD, 1998, EUR J VASC ENDOVASC, V15, P449, DOI 10.1016/S1078-5884(98)80209-8
   WIJESINGHE LD, 1997, EUR J VASC ENDOVASC, V14, P240
NR 42
TC 15
Z9 20
U1 0
U2 0
PU ELSEVIER SCIENCE INC
PI NEW YORK
PA 360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA
SN 0890-5096
EI 1615-5947
J9 ANN VASC SURG
JI Ann. Vasc. Surg.
PD MAY
PY 2005
VL 19
IS 3
BP 379
EP 385
DI 10.1007/s10016-004-0130-6
PG 7
WC Surgery; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Surgery; Cardiovascular System & Cardiology
GA 928RI
UT WOS:000229289000013
PM 15864479
DA 2025-04-10
ER

PT J
AU Schumertl, T
   Lokau, J
   Rose-John, S
   Garbers, C
AF Schumertl, Tim
   Lokau, Juliane
   Rose-John, Stefan
   Garbers, Christoph
TI Function and proteolytic generation of the soluble interleukin-6
   receptor in health and disease
SO BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
LA English
DT Review
DE Interleukin-6; Interleukin-6 receptor; gp130; Proteolysis; ADAM17
ID SIGNAL TRANSDUCER GP130; CORONARY-HEART-DISEASE; NECROSIS-FACTOR-ALPHA;
   IL-6 RECEPTOR; MESSENGER-RNA; GLYCOPROTEIN 130; T-CELL; CYTOKINE
   RECEPTOR; EPITHELIAL-CELLS; COMMON VARIANT
AB The pleiotropic cytokine interleukin-6 (IL-6) is involved in numerous physiological and pathophysiological functions that include development, immune cell differentiation, inflammation and cancer. IL-6 can signal via the membrane-bound IL-6 receptor (IL-6R, classic signaling) or via soluble forms of the IL-6R (sIL-6R, trans-signaling). Both modes of signaling induce the formation of a homodimer of the signal transducing beta-receptor glycoprotein 130 (gp130) and the activation of several intracellular signaling cascades, e.g. the Jak/STAT pathway. Intriguingly, only IL-6 trans-signaling is required for the pro-inflammatory properties of IL-6, while regenerative and anti-inflammatory functions are mediated via classic signaling. The sIL-6R is generated by different molecular mechanisms, including alternative mRNA splicing, proteolysis of the membrane-bound IL-6R and the release of extracellular vesicles. In this review, we give an in-depth overview on these molecular mechanisms with a special emphasize on IL-6R cleavage by the metalloprotease ADAM17 and other proteases. We discuss the biological functions of the sIL-6R and highlight attempts to selectively block IL-6 trans-signaling in pre-clinical animal models as well as in clinical studies in patients with inflammatory bowel disease.
C1 [Schumertl, Tim; Lokau, Juliane; Garbers, Christoph] Otto von Guericke Univ, Dept Pathol, Med Fac, Magdeburg, Germany.
   [Rose-John, Stefan] Univ Kiel, Inst Biochem, D-24118 Kiel, Germany.
C3 Otto von Guericke University; University of Kiel
RP Garbers, C (corresponding author), Otto von Guericke Univ, Dept Pathol, Med Fac, Magdeburg, Germany.
EM christoph.garbers@med.ovgu.de
RI Rose-John, Stefan/A-7998-2010; Garbers, Christoph/D-9932-2015
OI Garbers, Christoph/0000-0003-4939-6950
FU Deutsche Forschungsgemeinschaft (DFG, German Research Foundation)
   [125440785 - SFB 877]
FX This study was supported by the Deutsche Forschungsgemeinschaft (DFG,
   German Research Foundation) - Projektnummer 125440785 - SFB 877
   (projects A14).
CR Aparicio-Siegmund S, 2019, AM J PHYSIOL-ENDOC M, V317, pE411, DOI 10.1152/ajpendo.00166.2019
   Arnold P, 2020, CELLS-BASEL, V9, DOI 10.3390/cells9051307
   Arnold P, 2017, SCI REP-UK, V7, DOI 10.1038/srep44053
   Atreya R, 2000, NAT MED, V6, P583, DOI 10.1038/75068
   Bank U, 1999, J INTERF CYTOK RES, V19, P1277, DOI 10.1089/107999099312957
   Baran P, 2018, J BIOL CHEM, V293, P6762, DOI 10.1074/jbc.RA117.001163
   Baran P, 2013, J BIOL CHEM, V288, P14756, DOI 10.1074/jbc.M113.466169
   Barkhausen T, 2011, CRIT CARE MED, V39, P1407, DOI 10.1097/CCM.0b013e318211ff56
   Benrick A, 2008, REGUL PEPTIDES, V146, P189, DOI 10.1016/j.regpep.2007.09.031
   Black RA, 1997, NATURE, V385, P729, DOI 10.1038/385729a0
   Boulanger MJ, 2003, SCIENCE, V300, P2101, DOI 10.1126/science.1083901
   Briso EM, 2008, J IMMUNOL, V180, P7102, DOI 10.4049/jimmunol.180.11.7102
   Briukhovetska D, 2021, NAT REV CANCER, V21, P481, DOI 10.1038/s41568-021-00363-z
   Campbell IL, 2014, J NEUROSCI, V34, P2503, DOI 10.1523/JNEUROSCI.2830-13.2014
   Campochiaro C, 2020, EUR J INTERN MED, V76, P43, DOI 10.1016/j.ejim.2020.05.021
   Chalaris A, 2007, BLOOD, V110, P1748, DOI 10.1182/blood-2007-01-067918
   Chen B., 2021, J CROHNS COLITIS, V15, P041
   Chen G, 2020, J CLIN INVEST, V130, P2620, DOI 10.1172/JCI137244
   Chilimuri S, 2021, J CLIN PHARM THER, V46, P440, DOI 10.1111/jcpt.13303
   Cichy J, 1997, J IMMUNOL, V159, P5648
   de Almeida AR, 2020, IMMUNOBIOLOGY, V225, DOI 10.1016/j.imbio.2020.151964
   Dela Cruz CS, 2004, J EXP MED, V199, P503, DOI 10.1084/jem.20031205
   Diamant M, 1997, FEBS LETT, V412, P379, DOI 10.1016/S0014-5793(97)00750-3
   Dimitrov S, 2006, FASEB J, V20, P2174, DOI 10.1096/fj.06-5754fje
   Düsterhöft S, 2019, PATHOL RES PRACT, V215, DOI 10.1016/j.prp.2019.04.002
   Eimer J, 2021, J INTERN MED, V289, P434, DOI 10.1111/joim.13162
   Eulenfeld R, 2012, EUR J CELL BIOL, V91, P486, DOI 10.1016/j.ejcb.2011.09.010
   Ferreira RC, 2013, PLOS GENET, V9, DOI 10.1371/journal.pgen.1003444
   Flynn CM, 2021, J BIOL CHEM, V296, DOI 10.1016/j.jbc.2021.100434
   Flynn CM, 2020, SCI REP-UK, V10, DOI 10.1038/s41598-020-77884-4
   Flynn CM, 2019, SCI REP-UK, V9, DOI 10.1038/s41598-019-43617-5
   Franchimont N, 2005, ARTHRITIS RHEUM, V52, P84, DOI 10.1002/art.20727
   Galicia JC, 2004, GENES IMMUN, V5, P513, DOI 10.1038/sj.gene.6364120
   Garbers C, 2021, LANCET RHEUMATOL, V3, pE96
   Garbers C, 2020, ECLINICALMEDICINE, V22, DOI 10.1016/j.eclinm.2020.100340
   Garbers C, 2018, NAT REV DRUG DISCOV, V17, P395, DOI 10.1038/nrd.2018.45
   Garbers C, 2014, BBA-MOL BASIS DIS, V1842, P1485, DOI 10.1016/j.bbadis.2014.05.018
   Garbers C, 2012, CYTOKINE GROWTH F R, V23, P85, DOI 10.1016/j.cytogfr.2012.04.001
   Garbers C, 2011, J BIOL CHEM, V286, P42959, DOI 10.1074/jbc.M111.295758
   Garbers C, 2011, J BIOL CHEM, V286, P14804, DOI 10.1074/jbc.M111.229393
   George MJ, 2021, JACC-BASIC TRANSL SC, V6, P431, DOI 10.1016/j.jacbts.2021.01.013
   Giraldez MD, 2021, NAT REV GASTRO HEPAT, V18, P787, DOI 10.1038/s41575-021-00473-x
   Goth CK, 2015, P NATL ACAD SCI USA, V112, P14623, DOI 10.1073/pnas.1511175112
   Grivennikov S, 2009, CANCER CELL, V15, P103, DOI 10.1016/j.ccr.2009.01.001
   Groth E, 2016, BBA-MOL CELL RES, V1863, P2795, DOI 10.1016/j.bbamcr.2016.09.002
   Guaraldi G, 2020, LANCET RHEUMATOL, V2, pE474, DOI 10.1016/S2665-9913(20)30173-9
   Haddick PCG, 2017, J ALZHEIMERS DIS, V56, P1037, DOI 10.3233/JAD-160524
   Harrison SC, 2013, EUR HEART J, V34, P3707, DOI 10.1093/eurheartj/ehs354
   Heink S, 2017, NAT IMMUNOL, V18, P74, DOI 10.1038/ni.3632
   HIBI M, 1990, CELL, V63, P1149, DOI 10.1016/0092-8674(90)90411-7
   Hoge J, 2013, J IMMUNOL, V190, P703, DOI 10.4049/jimmunol.1201044
   Holub MC, 2002, IMMUNOL LETT, V82, P79, DOI 10.1016/S0165-2478(02)00022-6
   Holub MC, 1999, IMMUNOL LETT, V68, P121
   Horby PW, 2021, LANCET, V397, P1637, DOI 10.1016/S0140-6736(21)00676-0
   HORIUCHI S, 1994, EUR J IMMUNOL, V24, P1945, DOI 10.1002/eji.1830240837
   Horiuchi S, 1998, IMMUNOLOGY, V95, P360, DOI 10.1046/j.1365-2567.1998.00622.x
   Hunter CA, 2015, NAT IMMUNOL, V16, P448, DOI 10.1038/ni.3153
   Ichiki Tomoko, 2007, J Cardiol, V50, P101
   Johnson N, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-07556-3
   Jones SA, 1999, J EXP MED, V189, P599, DOI 10.1084/jem.189.3.599
   Jones SA, 1998, EUR J IMMUNOL, V28, P3514, DOI 10.1002/(SICI)1521-4141(199811)28:11<3514::AID-IMMU3514>3.0.CO;2-T
   Jones SA, 2011, J CLIN INVEST, V121, P3375, DOI 10.1172/JCI57158
   Jostock T, 2001, EUR J BIOCHEM, V268, P160, DOI 10.1046/j.1432-1327.2001.01867.x
   Kewan T, 2020, ECLINICALMEDICINE, V24, DOI 10.1016/j.eclinm.2020.100418
   Kinugawa T, 2012, INT HEART J, V53, P182, DOI 10.1536/ihj.53.182
   Koch L, 2021, FASEB J, V35, DOI 10.1096/fj.202002087R
   KOPF M, 1994, NATURE, V368, P339, DOI 10.1038/368339a0
   Korotaeva AA, 2018, BIOMARKERS, V23, P527, DOI 10.1080/1354750X.2018.1458151
   Lacroix M, 2015, J BIOL CHEM, V290, P26943, DOI 10.1074/jbc.M115.682138
   Lang VR, 2012, RHEUMATOLOGY, V51, P852, DOI 10.1093/rheumatology/ker223
   Leggate M, 2010, CELL STRESS CHAPERON, V15, P827, DOI 10.1007/s12192-010-0192-z
   Levine SJ, 2008, J BIOL CHEM, V283, P14177, DOI 10.1074/jbc.R700052200
   Li M, 2018, GENE, V676, P101, DOI 10.1016/j.gene.2018.07.018
   Lin M, 2006, BIOCHEM J, V398, P577, DOI 10.1042/BJ20060544
   Lokau J, 2020, CYTOKINE GROWTH F R, V55, P94, DOI 10.1016/j.cytogfr.2020.04.003
   Lokau J, 2020, METABOLISM, V109, DOI 10.1016/j.metabol.2020.154281
   Lokau J, 2020, PLOS ONE, V15, DOI 10.1371/journal.pone.0232612
   Lokau J, 2016, CELL REP, V14, P1761, DOI 10.1016/j.celrep.2016.01.053
   LUST JA, 1992, CYTOKINE, V4, P96, DOI 10.1016/1043-4666(92)90043-Q
   MACKIEWICZ A, 1992, J IMMUNOL, V149, P2021
   Magro Giuseppe, 2020, Cytokine X, V2, P100029, DOI 10.1016/j.cytox.2020.100029
   Martens AS, 2000, J CELL SCI, V113, P3593
   Matsumoto S, 2010, J IMMUNOL, V184, P1543, DOI 10.4049/jimmunol.0801217
   Matthews V, 2003, J BIOL CHEM, V278, P38829, DOI 10.1074/jbc.M210584200
   Mehta P, 2020, LANCET, V395, P1033, DOI 10.1016/S0140-6736(20)30628-0
   MITSUYAMA K, 1991, DIGESTION, V50, P104, DOI 10.1159/000200747
   Monhasery N, 2016, CELL REP, V16, P1067, DOI 10.1016/j.celrep.2016.06.062
   Moss ML, 1997, NATURE, V385, P733, DOI 10.1038/385733a0
   MULLBERG J, 1994, J IMMUNOL, V152, P4958
   MULLBERG J, 1993, EUR J IMMUNOL, V23, P473, DOI 10.1002/eji.1830230226
   MULLBERG J, 1995, J IMMUNOL, V155, P5198
   MULLBERG J, 1993, FEBS LETT, V332, P174, DOI 10.1016/0014-5793(93)80507-Q
   MULLBERG J, 1992, BIOCHEM BIOPH RES CO, V189, P794, DOI 10.1016/0006-291X(92)92272-Y
   MullerNewen G, 1996, EUR J BIOCHEM, V236, P837, DOI 10.1111/j.1432-1033.1996.00837.x
   NARAZAKI M, 1993, BLOOD, V82, P1120, DOI 10.1182/blood.V82.4.1120.bloodjournal8241120
   Narazaki M, 2017, EXPERT REV CLIN IMMU, V13, P535, DOI 10.1080/1744666X.2017.1295850
   Nikolaus S, 2018, INT J COLORECTAL DIS, V33, P927, DOI 10.1007/s00384-018-3069-8
   Nitz R, 2015, BIOCHIMIE, V119, P175, DOI 10.1016/j.biochi.2015.11.005
   Nowell MA, 2009, J IMMUNOL, V182, P613, DOI 10.4049/jimmunol.182.1.613
   Oh JW, 1996, CYTOKINE, V8, P401, DOI 10.1006/cyto.1996.0055
   Padro CJ, 2013, J IMMUNOL, V191, P5383, DOI 10.4049/jimmunol.1301019
   Paige E, 2019, CIRC-GENOM PRECIS ME, V12, DOI 10.1161/CIRCGEN.118.002413
   PAREKH RB, 1992, EUR J BIOCHEM, V203, P135, DOI 10.1111/j.1432-1033.1992.tb19838.x
   Parisinos CA, 2018, GASTROENTEROLOGY, V155, P303, DOI 10.1053/j.gastro.2018.05.022
   Rafiq S, 2007, GENES IMMUN, V8, P552, DOI 10.1038/sj.gene.6364414
   Lamas JR, 2013, CYTOKINE, V61, P720, DOI 10.1016/j.cyto.2012.12.025
   Reif A, 2021, ANGEW CHEM INT EDIT, V60, P13380, DOI 10.1002/anie.202101496
   Riethmueller S, 2017, PLOS BIOL, V15, DOI 10.1371/journal.pbio.2000080
   Riethmueller S, 2016, SCI REP-UK, V6, DOI 10.1038/srep25550
   Rogers M. Bowman, 2021, WHAT BACE HITS NEW S
   ROSEJOHN S, 1994, BIOCHEM J, V300, P281, DOI 10.1042/bj3000281
   Säily M, 1998, CYTOKINE, V10, P860, DOI 10.1016/S1043-4666(98)90003-5
   Salas A, 2020, NAT REV GASTRO HEPAT, V17, P323, DOI 10.1038/s41575-020-0273-0
   Sarwar N, 2012, LANCET, V379, P1205, DOI 10.1016/S0140-6736(11)61931-4
   Scheller J, 2005, BIOCHEM BIOPH RES CO, V326, P724, DOI 10.1016/j.bbrc.2004.11.098
   Scheller J, 2012, LANCET, V380, P338, DOI 10.1016/S0140-6736(12)61246-X
   Schmidt S, 2018, J EXP MED, V215, P1205, DOI 10.1084/jem.20171696
   Schreiber S, 2021, GASTROENTEROLOGY, V160, P2354, DOI 10.1053/j.gastro.2021.02.062
   Schumacher N, 2019, CANCERS, V11, DOI 10.3390/cancers11111736
   Schumacher N, 2015, J BIOL CHEM, V290, P26059, DOI 10.1074/jbc.M115.649509
   SHARKEY AM, 1995, BIOL REPROD, V53, P974, DOI 10.1095/biolreprod53.4.974
   Skiniotis G, 2005, NAT STRUCT MOL BIOL, V12, P545, DOI 10.1038/nsmb941
   Sommer J, 2014, J BIOL CHEM, V289, P22140, DOI 10.1074/jbc.M114.560938
   STAHL N, 1994, SCIENCE, V263, P92, DOI 10.1126/science.8272873
   STAHL N, 1995, SCIENCE, V267, P1349, DOI 10.1126/science.7871433
   Starr R, 1997, NATURE, V387, P917, DOI 10.1038/43206
   Stephens OW, 2012, BLOOD, V119, P503, DOI 10.1182/blood-2011-07-367052
   Stone JH, 2017, NEW ENGL J MED, V377, P317, DOI 10.1056/NEJMoa1613849
   Stuhlmann-Laeisz C, 2006, MOL BIOL CELL, V17, P2986, DOI 10.1091/mbc.E05-12-1129
   Swerdlow DI, 2012, LANCET, V379, P1214, DOI 10.1016/S0140-6736(12)60110-X
   TAGA T, 1989, CELL, V58, P573, DOI 10.1016/0092-8674(89)90438-8
   Tanaka M, 2000, J CLIN INVEST, V106, P137, DOI 10.1172/JCI7479
   Tanaka T, 2014, SEMIN IMMUNOL, V26, P88, DOI 10.1016/j.smim.2014.01.009
   Taniguchi K, 2015, NATURE, V519, P57, DOI 10.1038/nature14228
   Thabard W, 1999, CLIN CANCER RES, V5, P2693
   Tucher J, 2014, J PROTEOME RES, V13, P2205, DOI 10.1021/pr401135u
   Villarino AV, 2017, NAT IMMUNOL, V18, P374, DOI 10.1038/ni.3691
   Wilkinson AN, 2018, J IMMUNOL, V200, P3547, DOI 10.4049/jimmunol.1701191
   Wolf J, 2016, J BIOL CHEM, V291, P16186, DOI 10.1074/jbc.M116.718551
   Wolf J, 2016, BIOCHEM BIOPH RES CO, V470, P870, DOI 10.1016/j.bbrc.2016.01.127
   Wolf J, 2014, CYTOKINE, V70, P11, DOI 10.1016/j.cyto.2014.05.024
   Wonnerth A, 2014, METABOLISM, V63, P647, DOI 10.1016/j.metabol.2014.02.005
   Xu XL, 2020, P NATL ACAD SCI USA, V117, P10970, DOI 10.1073/pnas.2005615117
   Yan I, 2016, J LEUKOCYTE BIOL, V99, P749, DOI 10.1189/jlb.3A0515-207R
   Yousif AS, 2021, IMMUNITY, V54, P235, DOI 10.1016/j.immuni.2020.12.001
   Zhang JG, 1998, J BIOL CHEM, V273, P10798, DOI 10.1074/jbc.273.17.10798
   Ziegler L, 2019, CARDIOVASC RES, V115, P213, DOI 10.1093/cvr/cvy191
NR 147
TC 41
Z9 42
U1 5
U2 20
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
SN 0167-4889
EI 1879-2596
J9 BBA-MOL CELL RES
JI Biochim. Biophys. Acta-Mol. Cell Res.
PD JAN
PY 2022
VL 1869
IS 1
AR 119143
DI 10.1016/j.bbamcr.2021.119143
EA OCT 2021
PG 10
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA WL0TB
UT WOS:000710127600009
PM 34626681
OA Bronze
DA 2025-04-10
ER

PT J
AU Hirata, T
   Ushikubi, F
   Kakizuka, A
   Okuma, M
   Narumiya, S
AF Hirata, T
   Ushikubi, F
   Kakizuka, A
   Okuma, M
   Narumiya, S
TI Two thromboxane A(2) receptor isoforms in human platelets - Opposite
   coupling to adenylyl cyclase with different sensitivity to Arg(60) to
   Leu mutation
SO JOURNAL OF CLINICAL INVESTIGATION
LA English
DT Article
DE G-proteins; phospholipase C; phospholipases A; platelet activation;
   alternative splicing
ID DEFECTIVE SIGNAL TRANSDUCTION; TERMINAL DOMAINS; 2 ISOFORMS; BINDING;
   H-2-RECEPTOR; ACTIVATION; EXPRESSION; DISTINCT; RADIOLIGAND; CDNA
AB Thromboxane A(2) (TXA(2)) receptor is a key molecule in hemostasis as its abnormality leads to bleeding disorders. Two isoforms of the human TXA(2) receptor have been cloned; one from placenta and the other from endothelium, here referred to as TXR alpha and TXR beta, respectively. These isoforms differ only in their carboxyl-terminal tails. We report that both isoforms are present in human platelets. The two isoforms expressed in cultured cells show similar ligand binding characteristics and phospholipase C (PLC) activation but oppositely regulate adenylyl cyclase activity; TXR alpha activates adenylyl cyclase, while TXR beta inhibits it. The Arg(60) to Leu mutant of TXR alpha, which has been shown to impair PLC activation (Hirata, T., A. Kakizuka, F. Ushikubi, I. Fuse, M. Okuma, and S. Narumiya. 1994. J. Clin. Invest. 94: 1662-1667), also impairs adenylyl cyclase stimulation, whereas that of TXR beta retains its activity to inhibit adenylyl cyclase. These findings suggest that the pathway linked to adenylyl cyclase inhibition might be involved in some of the TXA(2)-induced platelet responses such as shape change and phospholipase A(2) activation which remain unaffected in the patients with this mutation.
C1 KYOTO UNIV,FAC MED,DEPT PHARMACOL,SAKYO KU,KYOTO 60601,JAPAN.
   KYOTO UNIV,FAC MED,DEPT INTERNAL MED,DIV 1,SAKYO KU,KYOTO 60601,JAPAN.
C3 Kyoto University; Kyoto University
OI Hirata, Takako/0000-0002-1740-6168
CR BERRIDGE MJ, 1983, BIOCHEM J, V212, P473, DOI 10.1042/bj2120473
   BRASS LF, 1987, J CLIN INVEST, V79, P1269, DOI 10.1172/JCI112947
   CHARO IF, 1994, P NATL ACAD SCI USA, V91, P2752, DOI 10.1073/pnas.91.7.2752
   CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
   DORN GW, 1989, J CLIN INVEST, V84, P1883, DOI 10.1172/JCI114375
   DORN GW, 1991, AM J PHYSIOL, V260, pH327, DOI 10.1152/ajpheart.1991.260.2.H327
   FONG TM, 1992, MOL PHARMACOL, V41, P24
   FUSE I, 1993, BLOOD, V81, P994
   GIROS B, 1989, NATURE, V342, P923, DOI 10.1038/342923a0
   GRAHAM FL, 1973, VIROLOGY, V52, P456, DOI 10.1016/0042-6822(73)90341-3
   HALUSHKA PV, 1989, ANN REV PHARM TOXICO, V10, P213
   HANASAKI K, 1988, THROMB RES, V50, P365, DOI 10.1016/0049-3848(88)90266-6
   HEDBERG A, 1988, J PHARMACOL EXP THER, V245, P786
   HIRATA M, 1991, NATURE, V349, P617, DOI 10.1038/349617a0
   HIRATA T, 1994, J CLIN INVEST, V94, P1662, DOI 10.1172/JCI117510
   ISHIKAWA Y, 1991, THROMB RES, V64, P667, DOI 10.1016/0049-3848(91)90067-7
   JOHNSON GJ, 1988, CIRC RES, V62, P494, DOI 10.1161/01.RES.62.3.494
   KAKIZUKA A, 1991, CELL, V66, P663, DOI 10.1016/0092-8674(91)90112-C
   KROLL MH, 1989, BLOOD, V74, P181
   LIN LL, 1993, CELL, V72, P269, DOI 10.1016/0092-8674(93)90666-E
   MIZUSHIMA S, 1990, NUCLEIC ACIDS RES, V18, P5322, DOI 10.1093/nar/18.17.5322
   MONSMA FJ, 1989, NATURE, V342, P926, DOI 10.1038/342926a0
   MORINELLI TA, 1994, J BIOL CHEM, V269, P5693
   MORINELLI TA, 1987, AM J PHYSIOL, V253, pH135
   NAKANO T, 1987, J BIOCHEM, V101, P1169, DOI 10.1093/oxfordjournals.jbchem.a121981
   NAMBA T, 1993, NATURE, V365, P166, DOI 10.1038/365166a0
   NEGISHI M, 1993, J BIOL CHEM, V268, P9517
   NUSING RM, 1993, J BIOL CHEM, V268, P25253
   RAYCHOWDHURY MK, 1995, J BIOL CHEM, V270, P7011, DOI 10.1074/jbc.270.12.7011
   RAYCHOWDHURY MK, 1994, J BIOL CHEM, V269, P19256
   SAMUELSSON B, 1978, ANNU REV BIOCHEM, V47, P997, DOI 10.1146/annurev.bi.47.070178.005025
   SHENKER A, 1991, J BIOL CHEM, V266, P9309
   SUGIMOTO Y, 1993, J BIOL CHEM, V268, P2712
   TAKAHARA K, 1990, J BIOL CHEM, V265, P6836
   TOSO RD, 1989, EMBO J, V8, P4025
   UMESONO K, 1991, CELL, V65, P1255, DOI 10.1016/0092-8674(91)90020-Y
   USHIKUBI F, 1989, J BIOL CHEM, V264, P16496
   USHIKUBI F, 1987, THROMB HAEMOSTASIS, V57, P158
   USHIKUBI F, 1994, MOL PHARMACOL, V46, P808
   VANDENPLAS S, 1984, J MED GENET, V21, P164, DOI 10.1136/jmg.21.3.164
   YOKOTA Y, 1989, J BIOL CHEM, V264, P17649
NR 41
TC 239
Z9 265
U1 0
U2 4
PU ROCKEFELLER UNIV PRESS
PI NEW YORK
PA 222 E 70TH STREET, NEW YORK, NY 10021
SN 0021-9738
J9 J CLIN INVEST
JI J. Clin. Invest.
PD FEB 15
PY 1996
VL 97
IS 4
BP 949
EP 956
DI 10.1172/JCI118518
PG 8
WC Medicine, Research & Experimental
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Research & Experimental Medicine
GA UD037
UT WOS:A1996UD03700011
PM 8613548
OA Green Published
DA 2025-04-10
ER

PT J
AU Zha, ZY
   Han, XR
   Smith, MD
   Lei, QY
   Guan, KL
   Xiong, Y
AF Zha, Zhengyu
   Han, Xiao-Ran
   Smith, Matthew D.
   Lei, Qun-Ying
   Guan, Kun-Liang
   Xiong, Yue
TI Hypertension-associated C825T polymorphism impairs the function of Gβ3
   to target GRK2 ubiquitination
SO CELL DISCOVERY
LA English
DT Article
ID BETA-3 SUBUNIT VARIANT; 825T ALLELE; PROTEINS; LIGASE; GENE; OBESITY
AB Population-based and case-control studies in different ethnicities have linked a polymorphism, C825T, in exon 10 of GNB3 gene to hypertension and several additional diseases. The 825T allele is associated with alternative splicing and results in a shortened G beta 3 protein, referred to as G beta 3s, which loses 41 amino acids encompassing one WD40 repeat domain. The mechanism of how G beta 3 C825T polymorphism is associated with hypertension has remained unclear, but an impairment of its canonical function in G-protein-coupled receptor signaling has been ruled out. Here, we report that G beta 3, like other G beta proteins, binds to DDB1 and assembles a DDB1-CUL4A-ROC1 E3 ubiquitin ligase (CRL4A(G beta 3)) to target GRK2 ubiquitination. The loss of the 41 amino-acid residues disrupts the G beta 3-DDB1 binding and impairs the function of G beta 3s to ubiquitinate GRK2. GRK2 ubiquitination levels were decreased and protein levels were accumulated in the blood samples of G beta 3 825T allele carriers. Deletion of Cul4a in mice resulted in systolic pressure increased and weakened heart function in male mice that can be partially rescued by the deletion of one Grk2 allele. These results reveal a mechanism explaining the link between G beta 3 C825T polymorphism and hypertension.
C1 [Zha, Zhengyu; Han, Xiao-Ran; Lei, Qun-Ying; Guan, Kun-Liang; Xiong, Yue] Fudan Univ, Shanghai Med Coll, Key Lab Mol Med, Minist Educ, Shanghai, Peoples R China.
   [Zha, Zhengyu; Han, Xiao-Ran; Lei, Qun-Ying; Guan, Kun-Liang; Xiong, Yue] Fudan Univ, Shanghai Med Coll, Dept Biochem & Mol Biol, Shanghai, Peoples R China.
   [Zha, Zhengyu; Han, Xiao-Ran; Guan, Kun-Liang; Xiong, Yue] Fudan Univ, Inst Biomed Sci, Mol & Cell Biol Lab, Shanghai, Peoples R China.
   [Zha, Zhengyu; Han, Xiao-Ran] Fudan Univ, Sch Life Sci, Shanghai, Peoples R China.
   [Zha, Zhengyu; Smith, Matthew D.; Xiong, Yue] Univ North Carolina Chapel Hill, Lineberger Comprehens Canc Ctr, Dept Biochem & Biophys, Chapel Hill, NC 27599 USA.
   [Guan, Kun-Liang] Univ Calif San Diego, Dept Pharmacol, La Jolla, CA 92093 USA.
   [Guan, Kun-Liang] Univ Calif San Diego, Moores Canc Ctr, La Jolla, CA 92093 USA.
C3 Fudan University; Fudan University; Fudan University; Fudan University;
   University of North Carolina; University of North Carolina Chapel Hill;
   University of North Carolina School of Medicine; University of
   California System; University of California San Diego; University of
   California System; University of California San Diego
RP Lei, QY; Guan, KL; Xiong, Y (corresponding author), Fudan Univ, Shanghai Med Coll, Key Lab Mol Med, Minist Educ, Shanghai, Peoples R China.; Lei, QY; Guan, KL; Xiong, Y (corresponding author), Fudan Univ, Shanghai Med Coll, Dept Biochem & Mol Biol, Shanghai, Peoples R China.; Guan, KL; Xiong, Y (corresponding author), Fudan Univ, Inst Biomed Sci, Mol & Cell Biol Lab, Shanghai, Peoples R China.; Xiong, Y (corresponding author), Univ North Carolina Chapel Hill, Lineberger Comprehens Canc Ctr, Dept Biochem & Biophys, Chapel Hill, NC 27599 USA.; Guan, KL (corresponding author), Univ Calif San Diego, Dept Pharmacol, La Jolla, CA 92093 USA.; Guan, KL (corresponding author), Univ Calif San Diego, Moores Canc Ctr, La Jolla, CA 92093 USA.
EM qlei@fudan.edu.cn; kuguan@ucsd.edu; yxiong@email.unc.edu
RI Han, Xiaoran/LCD-8335-2024; Guan, Kun-Liang/ADK-7088-2022; Lei,
   Qun-Ying/J-1390-2017
FU Chinese Ministry of Sciences and Technology 973 [2015CB910401]; NSFC
   [81430057, 81225016, 31271454]; Shanghai Key basic research program
   [12JC1401100]; Shanghai Outstanding Academic Leader [13XD1400600]; Youth
   Science and Technology Leading Talent by MOST; NIH [EY022611, CA132809,
   GM067113]
FX We thank the members of the Fudan MCB and Xiong laboratories for
   discussions throughout this study, Brenda Temple of UNC RL Juliano
   Structural Bioinformatics Core facility for the molecular modeling, Bev
   Koller, Howard Rockman, Dennis Abraham, Kathleen Caron and John Sondek
   for discussions, and Cam Patterson for discussion and critical reading
   of the paper. This work was supported by Chinese Ministry of Sciences
   and Technology 973 (grant number 2015CB910401), NSFC (grant numbers
   81430057, 81225016 and 31271454), Shanghai Key basic research program
   (12JC1401100), Shanghai Outstanding Academic Leader (grant number
   13XD1400600) and the Youth Science and Technology Leading Talent by MOST
   to QYL, NIH grants EY022611 and CA132809 (to K-LG), and GM067113 (to
   YX).
CR Angers S, 2006, NATURE, V443, P590, DOI 10.1038/nature05175
   Benjafield AV, 1998, HYPERTENSION, V32, P1094, DOI 10.1161/01.HYP.32.6.1094
   Dobrev D, 2000, CIRCULATION, V102, P692, DOI 10.1161/01.CIR.102.6.692
   Dupré DJ, 2009, ANNU REV PHARMACOL, V49, P31, DOI 10.1146/annurev-pharmtox-061008-103038
   Faruqi M, 2012, NAT REV DRUG DISCOV, V11, DOI 10.1038/nrd3874
   Gurevich EV, 2012, PHARMACOL THERAPEUT, V133, P40, DOI 10.1016/j.pharmthera.2011.08.001
   He YZJ, 2006, GENE DEV, V20, P2949, DOI 10.1101/gad.1483206
   Higa LA, 2006, NAT CELL BIOL, V8, P1277, DOI 10.1038/ncb1490
   Hu J, 2004, NAT CELL BIOL, V6, P1003, DOI 10.1038/ncb1172
   Jiang BC, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0037070
   Jin JP, 2006, MOL CELL, V23, P709, DOI 10.1016/j.molcel.2006.08.010
   Kato N, 1998, HYPERTENSION, V32, P935, DOI 10.1161/01.HYP.32.5.935
   Klenke S, 2011, PHARMACOGENET GENOM, V21, P594, DOI 10.1097/FPC.0b013e3283491153
   Leftowitz RJ, 2005, SCIENCE, V308, P512, DOI 10.1126/science.1109237
   Liu SL, 2005, NAT MED, V11, P952, DOI 10.1038/nm1289
   Lodowski DT, 2003, SCIENCE, V300, P1256, DOI 10.1126/science.1082348
   Mayor Federico Jr., 2011, Archives of Physiology and Biochemistry, V117, P125, DOI 10.3109/13813455.2011.584693
   Rockman HA, 2002, NATURE, V415, P206, DOI 10.1038/415206a
   Schunkert H, 1998, HYPERTENSION, V32, P510, DOI 10.1161/01.HYP.32.3.510
   Semplicini A, 2015, HIGH BLOOD PRESS CAR, V22, P225, DOI 10.1007/s40292-015-0093-4
   Siderovski DP, 2009, WILEY ENCY CHEM BIOL
   Siffert W, 1999, J AM SOC NEPHROL, V10, P1921
   Siffert W, 1998, NAT GENET, V18, P45, DOI 10.1038/ng0198-45
   Stevens RC, 2013, NAT REV DRUG DISCOV, V12, P25, DOI 10.1038/nrd3859
   Whalen EJ, 2007, CELL, V129, P511, DOI 10.1016/j.cell.2007.02.046
   Yu XC, 2005, AM J PHYSIOL-HEART C, V289, pH1960, DOI 10.1152/ajpheart.00328.2005
   Zha ZY, 2015, MOL CELL, V58, P794, DOI 10.1016/j.molcel.2015.04.017
NR 27
TC 14
Z9 13
U1 0
U2 1
PU NATURE PUBLISHING GROUP
PI LONDON
PA MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
EI 2056-5968
J9 CELL DISCOV
JI Cell Discov.
PD APR 26
PY 2016
VL 2
AR 16005
DI 10.1038/celldisc.2016.5
PG 8
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA FM2CU
UT WOS:000414792600001
PM 27462452
OA Green Published, Green Submitted, gold
DA 2025-04-10
ER

PT J
AU Petiti, J
   Lo Iacono, M
   Rosso, V
   Andreani, G
   Jovanovski, A
   Podestà, M
   Lame, D
   De Gobbi, M
   Fava, C
   Saglio, G
   Frassoni, F
   Cilloni, D
AF Petiti, Jessica
   Lo Iacono, Marco
   Rosso, Valentina
   Andreani, Giacomo
   Jovanovski, Aleksandar
   Podesta, Marina
   Lame, Dorela
   De Gobbi, Marco
   Fava, Carmen
   Saglio, Giuseppe
   Frassoni, Francesco
   Cilloni, Daniela
TI Bcl-xL represents a therapeutic target in Philadelphia negative
   myeloproliferative neoplasms
SO JOURNAL OF CELLULAR AND MOLECULAR MEDICINE
LA English
DT Article
DE ABT-737; Bcl-xL; myeloproliferative neoplasms; therapeutic target
ID APOPTOSIS; EXPRESSION; RESISTANCE; CANCER; RUXOLITINIB; ACTIVATION;
   INHIBITOR; MECHANISMS; ABT-737; CELLS
AB Myeloproliferative neoplasms are divided into essential thrombocythemia (ET), polycythemia vera (PV) and primary myelofibrosis (PMF). Although ruxolitinib was proven to be effective in reducing symptoms, patients rarely achieve complete molecular remission. Therefore, it is relevant to identify new therapeutic targets to improve the clinical outcome of patients. Bcl-xL protein, the long isoform encoded by alternative splicing of theBcl-xgene, acts as an anti-apoptotic regulator. Our study investigated the role of Bcl-xL as a marker of severity of MPN and the possibility to target Bcl-xL in patients. 129 MPN patients and 21 healthy patients were enrolled in the study. We analysedBcl-xLexpression in leucocytes and in enriched CD34+ and CD235a+ cells. Furthermore, ABT-737, a Bcl-xL inhibitor, was tested in HEL cells and in leucocytes from MPN patients. Bcl-xL was found progressively over-expressed in cells from ET, PV and PMF patients, independently by JAK2 mutational status. Moreover, our data indicated that the combination of ABT-737 and ruxolitinib resulted in a significantly higher apoptotic rate than the individual drug. Our study suggests that Bcl-xL plays an important role in MPN independently from JAK2 V617F mutation. Furthermore, data demonstrate that targeting simultaneously JAK2 and Bcl-xL might represent an interesting new approach.
C1 [Petiti, Jessica; Lo Iacono, Marco; Rosso, Valentina; Andreani, Giacomo; Jovanovski, Aleksandar; Lame, Dorela; De Gobbi, Marco; Fava, Carmen; Saglio, Giuseppe; Frassoni, Francesco; Cilloni, Daniela] Univ Turin, Dept Clin & Biol Sci, Reg Gonzole 10, I-10043 Turin, Italy.
   [Podesta, Marina] Inst G Gaslini, Dept Pediat Hematooncol, Genoa, Italy.
   [Podesta, Marina] Inst G Gaslini, Stem Cell & Cellular Therapy Lab, Genoa, Italy.
C3 University of Turin; University of Genoa; IRCCS Istituto Giannina
   Gaslini; University of Genoa; IRCCS Istituto Giannina Gaslini
RP Petiti, J (corresponding author), Univ Turin, Dept Clin & Biol Sci, Reg Gonzole 10, I-10043 Turin, Italy.
EM jessica.petiti@unito.it
RI Andreani, Giacomo/AAO-8897-2020; fava, carmen/J-9494-2018; Saglio,
   Giuseppe/G-8976-2013; De Gobbi, Marco/E-8136-2013; Petiti,
   Jessica/AAF-8023-2020; LO IACONO, MARCO/L-5453-2016; Jovanovski,
   Aleksandar/ABC-9195-2020; Podesta, Marina/K-3875-2016
OI LO IACONO, MARCO/0000-0002-3936-4472; Petiti,
   Jessica/0000-0001-8640-2462; Andreani, Giacomo/0000-0003-4877-3929;
   Jovanovski, Aleksandar/0000-0001-8221-3357; Podesta,
   Marina/0000-0002-6755-613X
FU Associazione Italiana per la Ricerca sul Cancro [10005]; AIRC [10005]
FX Associazione Italiana per la Ricerca sul Cancro, Grant/Award Number:
   10005; AIRC, Grant/Award Number: 10005
CR Adams JM, 2018, CELL DEATH DIFFER, V25, P27, DOI 10.1038/cdd.2017.161
   Balligand T, 2016, LEUKEMIA, V30, P1775, DOI 10.1038/leu.2016.47
   Borrás C, 2020, INT J MOL SCI, V21, DOI 10.3390/ijms21020418
   Campbell PJ, 2006, NEW ENGL J MED, V355, P2452, DOI 10.1056/NEJMra063728
   Campo E, 2011, BLOOD, V117, P5019, DOI 10.1182/blood-2011-01-293050
   Cerquozzi S, 2015, BLOOD CANCER J, V5, DOI 10.1038/bcj.2015.95
   Chauhan D, 2005, MOL CANCER THER, V4, P686, DOI 10.1158/1535-7163.MCT-04-0338
   Grillot DAM, 1997, J IMMUNOL, V158, P4750
   Kirito K, 2002, J BIOL CHEM, V277, P8329, DOI 10.1074/jbc.M109824200
   Klampfl T, 2013, NEW ENGL J MED, V369, P2379, DOI 10.1056/NEJMoa1311347
   Konopleva M, 2006, CANCER CELL, V10, P375, DOI 10.1016/j.ccr.2006.10.006
   KORSMEYER SJ, 1995, TRENDS GENET, V11, P101, DOI 10.1016/S0168-9525(00)89010-1
   Kralovics R, 2005, NEW ENGL J MED, V352, P1779, DOI 10.1056/NEJMoa051113
   Kreipe H., 2011, J HEMATOP, V4, P61, DOI [10.1007/s12308-011-0096-6, DOI 10.1007/S12308-011-0096-6, 10.1182/blood-2013-03-487694]
   Lim SN, 2013, BLOOD RES, V48, P178, DOI 10.5045/br.2013.48.3.178
   Lin KL, 2010, TOXICON, V55, P1263, DOI 10.1016/j.toxicon.2010.01.017
   Lo Iacono M, 2015, INT J CANCER, V136, P2598, DOI 10.1002/ijc.29302
   Mazzacurati L, 2015, ONCOTARGET, V6, P40141, DOI 10.18632/oncotarget.5653
   McConkey DJ, 1996, CANCER RES, V56, P5594
   Oltersdorf T, 2005, NATURE, V435, P677, DOI 10.1038/nature03579
   Opferman JT, 2018, CELL DEATH DIFFER, V25, P37, DOI 10.1038/cdd.2017.170
   Petiti J, 2020, J CLIN MED, V9, DOI 10.3390/jcm9051457
   Petiti J, 2019, J CELL MOL MED, V23, P4349, DOI 10.1111/jcmm.14326
   Pikman Y, 2006, PLOS MED, V3, P1140, DOI 10.1371/journal.pmed.0030270
   Rosso V, 2019, J CLIN MED, V8, DOI 10.3390/jcm8070972
   Silva M, 1998, NEW ENGL J MED, V338, P564, DOI 10.1056/NEJM199802263380902
   Spivak JL, 2004, SEMIN HEMATOL, V41, P1, DOI 10.1053/j.seminhematol.2004.02.011
   Tognon R, 2012, J HEMATOL ONCOL, V5, DOI 10.1186/1756-8722-5-2
   Tu YP, 1998, CANCER RES, V58, P256
   Tvorogov D, 2018, SCI ADV, V4, DOI 10.1126/sciadv.aat3834
   Vannucchi AM, 2015, NEW ENGL J MED, V372, P426, DOI 10.1056/NEJMoa1409002
   Vaux DL, 2008, CELL DEATH DIFFER, V15, P807, DOI 10.1038/cdd.2008.31
   Verstovsek S, 2017, J HEMATOL ONCOL, V10, DOI 10.1186/s13045-017-0417-z
   Verstovsek S, 2012, NEW ENGL J MED, V366, P799, DOI 10.1056/NEJMoa1110557
   Waibel M, 2013, CELL REP, V5, P1047, DOI 10.1016/j.celrep.2013.10.038
   Yogarajah M, 2017, MAYO CLIN PROC, V92, P1118, DOI 10.1016/j.mayocp.2017.05.010
   Zapata JM, 1998, BREAST CANCER RES TR, V47, P129, DOI 10.1023/A:1005940832123
   Zeuner A, 2009, BLOOD, V113, P1522, DOI 10.1182/blood-2008-03-143321
NR 38
TC 22
Z9 24
U1 0
U2 4
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 1582-1838
EI 1582-4934
J9 J CELL MOL MED
JI J. Cell. Mol. Med.
PD SEP
PY 2020
VL 24
IS 18
BP 10978
EP 10986
DI 10.1111/jcmm.15730
EA AUG 2020
PG 9
WC Cell Biology; Medicine, Research & Experimental
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology; Research & Experimental Medicine
GA NT8EF
UT WOS:000559395100001
PM 32790151
OA Green Published
DA 2025-04-10
ER

PT J
AU Sartori, MT
   Saggiorato, G
   Pellati, D
   Casonato, A
   Spiezia, L
   Pontara, E
   Gavasso, S
   Girolami, A
AF Sartori, MT
   Saggiorato, G
   Pellati, D
   Casonato, A
   Spiezia, L
   Pontara, E
   Gavasso, S
   Girolami, A
TI Contraceptive pills induce an improvement in congenital
   hypoplasminogenemia in two unrelated patients with ligneous
   conjunctivitis
SO THROMBOSIS AND HAEMOSTASIS
LA English
DT Article
DE plasminogen deficiency; ligneous conjunctivitis; oral contraceptives;
   plasminogen gene mutations; von Willebrand's disease
ID TISSUE PLASMINOGEN-ACTIVATOR; VENOUS THROMBOEMBOLISM; T-PA; DEFICIENCY;
   GENE; MUTATIONS; PREGNANCY; THERAPY; DISEASE; DEFECT
AB Severe type I plasminogen deficiency is the underlying cause of ligneous conjunctivitis, a rare disease characterized by wood-like pseudomembranes developing on the ocular and extraocular mucosa. Two unrelated female patients with ligneous conjunctivitis and moderate hypoplasminogenemia are described. Being of fertile age, they were treated with oral contraceptives, which determined a marked increase in plasminogen levels. Moreover, a palpebral pseudomembrane stopped growing in one patient and disappeared completely in the other while on the estroprogestinic treatment. In patient n. 2, who also suffered from von Willebrand's disease, prior Cushing's disease induced an increase in both von Willebrand factor and plasminogen levels, which dropped after curative hypophysectomy. Genetic plasminogen study showed a 19Lys>Glu mutation in a heterozygous state in the first proposita and in a homozygous state in the second proband. In addition, both index patients were homozygous for a new intron F-14T>G mutation, which was found to reduce the acceptor splicing site prediction score.
   In conclusion, oral contraceptive therapy may improve plasminogen deficiency and deserves attention as an alternative therapeutic approach in selected cases of ligneous conjunctivitis with low, but not absent, plasminogen synthesis.
C1 Univ Padua, Dept Med & Surg Sci, Sch Med, Chair Internal Med 2, I-35128 Padua, Italy.
C3 University of Padua
RP Univ Padua, Dept Med & Surg Sci, Sch Med, Chair Internal Med 2, Via Osped Civile 105, I-35128 Padua, Italy.
EM mtsart@unipd.it
OI Spiezia, Luca/0000-0003-4339-8525; Pontara, Elena/0000-0003-2003-7081
CR AZUMA H, 1993, BLOOD, V82, P475
   CASONATO A, 1985, AM J CLIN PATHOL, V84, P107, DOI 10.1093/ajcp/84.1.107
   CASONATO A, 1992, BLOOD COAGUL FIBRIN, V3, P149, DOI 10.1097/00001721-199204000-00003
   COHEN SR, 1990, ANN OTO RHINOL LARYN, V99, P509, DOI 10.1177/000348949009900702
   DECLERCK PJ, 1988, BLOOD, V71, P220
   ERIKSSON E, 1988, THROMB RES, V50, P91, DOI 10.1016/0049-3848(88)90177-6
   Friederich PW, 1996, ANN INTERN MED, V125, P955, DOI 10.7326/0003-4819-125-12-199612150-00003
   GIROLAMI A, 1970, BRIT J HAEMATOL, V19, P179, DOI 10.1111/j.1365-2141.1970.tb01615.x
   HOLVOET P, 1985, THROMB HAEMOSTASIS, V54, P684
   LAURELL CB, 1966, ANAL BIOCHEM, V15, P45, DOI 10.1016/0003-2697(66)90246-6
   MANABE S, 1985, THROMB RES, V39, P333, DOI 10.1016/0049-3848(85)90229-4
   MANNUCCI PM, 1986, BRIT J HAEMATOL, V63, P753, DOI 10.1111/j.1365-2141.1986.tb07559.x
   Mateo J, 1997, THROMB HAEMOSTASIS, V77, P444
   Mingers AM, 1999, APMIS, V107, P62, DOI 10.1111/j.1699-0463.1999.tb01527.x
   MINGERS AM, 1995, 25 HAM S 1994, P96
   NUSSGENS Z, 1993, OPHTHALMIC PAED GEN, V14, P137, DOI 10.3109/13816819309087630
   PARUNOVIC A, 1993, VESTN OFTALMOL, V109, P30
   PATRASSI GM, 1985, THROMB HAEMOSTASIS, V54, P518
   PETERSEN TE, 1990, J BIOL CHEM, V265, P6104
   Ramsby ML, 2000, INFLAMMATION, V24, P45, DOI 10.1023/A:1006988025799
   Sartori MT, 1999, CLIN APPL THROMB-HEM, V5, P277, DOI 10.1177/107602969900500412
   Sartori MT, 2000, CLIN APPL THROMB-HEM, V6, P36, DOI 10.1177/107602960000600106
   Schott D, 1998, NEW ENGL J MED, V339, P1679, DOI 10.1056/NEJM199812033392305
   Schuster V, 1997, BLOOD, V90, P958, DOI 10.1182/blood.V90.3.958.958_958_966
   Schuster V, 2001, THROMB HAEMOSTASIS, V85, P1004
   Schuster V, 1999, BLOOD, V93, P3457, DOI 10.1182/blood.V93.10.3457.410k03_3457_3466
   SCHWARTZ GS, 1995, AM J OPHTHALMOL, V120, P253, DOI 10.1016/S0002-9394(14)72619-4
   SCURRY J, 1993, J REPROD MED, V38, P407
   SHIGEKIYO T, 1992, THROMB HAEMOSTASIS, V68, P233
   Simioni P, 1996, THROMB HAEMOSTASIS, V75, P422
   SORIA J, 1976, PATHOL BIOL, V24, P725
   TAIT RC, 1992, THROMB HAEMOSTASIS, V68, P506
   Watts P, 2002, AM J OPHTHALMOL, V133, P451, DOI 10.1016/S0002-9394(01)01433-7
   WRIGHT JG, 1988, BRIT J HAEMATOL, V69, P253, DOI 10.1111/j.1365-2141.1988.tb07630.x
NR 34
TC 34
Z9 35
U1 0
U2 2
PU GEORG THIEME VERLAG KG
PI STUTTGART
PA RUDIGERSTR 14, D-70469 STUTTGART, GERMANY
SN 0340-6245
EI 2567-689X
J9 THROMB HAEMOSTASIS
JI Thromb. Haemost.
PD JUL
PY 2003
VL 90
IS 1
BP 86
EP 91
PG 6
WC Hematology; Peripheral Vascular Disease
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Hematology; Cardiovascular System & Cardiology
GA 710MC
UT WOS:000184683100013
PM 12876630
DA 2025-04-10
ER

PT J
AU Vawter, MP
   Usen, N
   Thatcher, L
   Ladenheim, B
   Zhang, PS
   VanderPutten, DM
   Conant, K
   Herman, MM
   van Kammen, DP
   Sedvall, G
   Garver, DL
   Freed, WJ
AF Vawter, MP
   Usen, N
   Thatcher, L
   Ladenheim, B
   Zhang, PS
   VanderPutten, DM
   Conant, K
   Herman, MM
   van Kammen, DP
   Sedvall, G
   Garver, DL
   Freed, WJ
TI Characterization of human cleaved N-CAM and association with
   schizophrenia
SO EXPERIMENTAL NEUROLOGY
LA English
DT Article
DE synaptosome; MALDI-TOF; protein sequence; ventricular enlargement;
   protease; N-CAM; cell adhesion molecule; cell recognition molecule;
   schizophrenia; proteolysis
ID CELL-ADHESION MOLECULE; TISSUE-PLASMINOGEN ACTIVATOR; SERINE-PROTEASE
   INHIBITOR; RECOGNITION MOLECULES; SYNAPTIC PLASTICITY; BIPOLAR DISORDER;
   NERVOUS-SYSTEM; EXPRESSION; NCAM; HIPPOCAMPUS
AB The neural cell adhesion molecule (N-CAM) is a cell recognition molecule involved in cellular migration, synaptic plasticity, and CNS development. A 105- to 115-kDa isoform. of N-CAM (cleaved N-CAM or cN-CAM) is increased in schizophrenia in hippocampus, prefrontal cortex, and CSF. We purified and partially characterized cN-CAM, a putative novel isoform, and confirmed that the first 9 amino acids were identical to exon 1 of N-CAM, without the signal sequence. Analysis of trypsin-digested cN-CAM fragments by matrix-assisted laser desorption ionization on a time-of-flight mass spectrometer (MALDI-TOF) yielded peptides that could be identified as being derived from the first 548 amino acid residues of the expected N-CAM amino acid sequence. Immunological identification with four specific N-CAM antisera directed toward cytoplasmic, secreted, variable alternative spliced exon, or GPI epitopes failed to indicate other known splice variants. Neuraminidase treatment of cN-CAM produced a minor alteration resulting in a faster migrating immunoreactive band, indicating partial glycosylation of cN-CAM. Membranous particles from cytosolic brain extract containing cN-CAM were obtained by ultracentrifugation; however, CSF contained few such particles. cN-CAM and synaptophysin were colocalized on these particles. Both cN-CAM and N-CAM 180 were present in synaptosomal preparations of human brain. Following incubation of synaptosomes or brain tissue without protease inhibitors, N-CAM 180 was degraded and cN-CAM was increased. A cN-CAM-like band was present in human fetal neuronal cultures, but not in fetal astrocyte cultures. Thus, cN-CAM represents a protease- and neuraminidase-susceptible fragment possibly derived by proteolytic cleavage of N-CAM 180. An enlargement in ventricular volume in a group of adult patients with schizophrenia over a 2-year interval was found to be correlated with CSF cN-CAM levels as measured at the time of the initial MRI scan (r=0.53, P=0.01). cN-CAM is associated with ventricular enlargement; thus, the release of N-CAM fragments may be part of the pathogenic mechanism of schizophrenia in vulnerable brain regions such as the hippocampus and prefrontal cortex. Alternatively, the increases in cN-CAM in schizophrenia may be a reflection of a more general abnormality in the regulation of proteolysis or of extracellular matrix stability. (C) 2001 Academic Press.
C1 NIDA, Dev & Plast Sect, Cellular Neurobiol Res Branch, Baltimore, MD 21224 USA.
   DirectGene, Annapolis, MD 21401 USA.
   Johns Hopkins Univ, Dept Neurol, Baltimore, MD 21287 USA.
   NIMH, Clin Brain Disorders Branch, IRP, Bethesda, MD 20892 USA.
   RW Johnson Pharmaceut Res Inst, Raritan, NJ 08869 USA.
   Karolinska Hosp & Inst, Dept Clin Neurosci, Psychiat Sect, S-17176 Stockholm, Sweden.
   Univ Louisville, Sch Med, Dept Psychiat & Behav Sci, Louisville, KY 40222 USA.
   Univ Calif Irvine, Irvine, CA 92697 USA.
C3 National Institutes of Health (NIH) - USA; NIH National Institute on
   Drug Abuse (NIDA); Johns Hopkins University; National Institutes of
   Health (NIH) - USA; NIH National Institute of Mental Health (NIMH);
   Johnson & Johnson; Johnson & Johnson USA; Karolinska Institutet;
   Karolinska University Hospital; University of Louisville; University of
   California System; University of California Irvine
RP NIDA, Dev & Plast Sect, Cellular Neurobiol Res Branch, 550 Nathan Shock Dr, Baltimore, MD 21224 USA.
EM wfreed@intra.nida.nih.gov
RI conant, katherine/JLL-5328-2023
CR BARBEAU D, 1995, P NATL ACAD SCI USA, V92, P2785, DOI 10.1073/pnas.92.7.2785
   Berger P, 1999, MOL CELL NEUROSCI, V14, P455, DOI 10.1006/mcne.1999.0804
   BREESE CR, 1995, BRAIN RES, V674, P82, DOI 10.1016/0006-8993(94)01384-T
   Cadet JL, 2001, SYNAPSE, V41, P40, DOI 10.1002/syn.1058
   Conant K, 1998, P NATL ACAD SCI USA, V95, P3117, DOI 10.1073/pnas.95.6.3117
   CONRAD AJ, 1987, SCHIZOPHRENIA BULL, V13, P577, DOI 10.1093/schbul/13.4.577
   Davis RL, 1999, NATURE, V401, P376, DOI 10.1038/43894
   ELDER GA, 1988, DEV BRAIN RES, V42, P146, DOI 10.1016/0165-3806(88)90211-8
   Endo A, 1998, NEUROSCI LETT, V246, P37, DOI 10.1016/S0304-3940(98)00204-3
   Endo A, 1999, NEUROSCI RES, V33, P1, DOI 10.1016/S0168-0102(98)00105-9
   Fernandez J, 1998, ELECTROPHORESIS, V19, P1036, DOI 10.1002/elps.1150190619
   GALLAGHER HC, 1999, SOC NEUR ABSTR, V25, P1973
   Garver DL, 2000, SCHIZOPHR RES, V44, P11, DOI 10.1016/S0920-9964(00)00015-3
   Gualandris A, 1996, J NEUROSCI, V16, P2220
   Harrison PJ, 1999, BRAIN, V122, P593, DOI 10.1093/brain/122.4.593
   HEMPERLY JJ, 1986, P NATL ACAD SCI USA, V83, P3037, DOI 10.1073/pnas.83.9.3037
   HOCHSTRASSER DF, 1988, ANAL BIOCHEM, V173, P424, DOI 10.1016/0003-2697(88)90209-6
   Hoffman KB, 1998, BRAIN RES, V811, P152, DOI 10.1016/S0006-8993(98)00907-X
   Hoffman KB, 1998, BRAIN RES, V811, P29, DOI 10.1016/S0006-8993(98)00906-8
   Honer WG, 1997, NEUROSCIENCE, V78, P99, DOI 10.1016/S0306-4522(96)00489-7
   Krueger SR, 1997, J NEUROSCI, V17, P8984
   LYONS F, 1988, BIOL PSYCHIAT, V23, P769, DOI 10.1016/0006-3223(88)90065-0
   MAYFORD M, 1992, SCIENCE, V256, P638, DOI 10.1126/science.1585176
   McCarley RW, 1999, BIOL PSYCHIAT, V45, P1099, DOI 10.1016/S0006-3223(99)00018-9
   MCCLAIN DA, 1982, P NATL ACAD SCI-BIOL, V79, P6380, DOI 10.1073/pnas.79.20.6380
   Murphy KJ, 1996, J NEUROCHEM, V67, P1268
   Nair TR, 1997, PSYCHIAT RES-NEUROIM, V74, P141, DOI 10.1016/S0925-4927(97)00013-9
   Osterwalder T, 1996, EMBO J, V15, P2944, DOI 10.1002/j.1460-2075.1996.tb00657.x
   PERSOHN E, 1989, J COMP NEUROL, V288, P92, DOI 10.1002/cne.902880108
   Phillips G. R., 1999, Society for Neuroscience Abstracts, V25, P2006
   Plioplys A V, 1990, J Neuropsychiatry Clin Neurosci, V2, P413
   Poltorak M, 1997, BRAIN RES, V751, P152, DOI 10.1016/S0006-8993(97)00023-1
   POLTORAK M, 1995, EXP NEUROL, V131, P266, DOI 10.1016/0014-4886(95)90048-9
   Rabinowitz JE, 1996, P NATL ACAD SCI USA, V93, P6421, DOI 10.1073/pnas.93.13.6421
   Ronn LCB, 2000, INT J DEV NEUROSCI, V18, P193, DOI 10.1016/S0736-5748(99)00088-X
   Ronn LCB, 1998, EXP GERONTOL, V33, P853, DOI 10.1016/S0531-5565(98)00040-0
   Rose SPR, 1996, J PHYSIOLOGY-PARIS, V90, P387, DOI 10.1016/S0928-4257(97)87926-0
   SHEPPARD A, 1991, BIOCHIM BIOPHYS ACTA, V1076, P156, DOI 10.1016/0167-4838(91)90234-Q
   Tanaka H, 2000, NEURON, V25, P93, DOI 10.1016/S0896-6273(00)80874-0
   van Kammen DP, 1998, BIOL PSYCHIAT, V43, P680, DOI 10.1016/S0006-3223(97)00324-7
   Vawter MP, 1998, EXP NEUROL, V154, P1, DOI 10.1006/exnr.1998.6889
   Vawter MP, 1998, EXP NEUROL, V149, P424, DOI 10.1006/exnr.1997.6721
   Vawter MP, 1998, SCHIZOPHR RES, V34, P123, DOI 10.1016/S0920-9964(98)00103-0
   Vawter MP, 2000, EUR J PHARMACOL, V405, P385, DOI 10.1016/S0014-2999(00)00568-9
   Vawter MP, 1999, MOL PSYCHIATR, V4, P467, DOI 10.1038/sj.mp.4000547
   Vawter MP, 2001, BRAIN RES BULL, V55, P641, DOI 10.1016/S0361-9230(01)00522-6
   WALSH FS, 1992, COLD SPRING HARB SYM, V57, P431, DOI 10.1101/SQB.1992.057.01.048
   Wood GK, 1998, NEUROREPORT, V9, P461, DOI 10.1097/00001756-199802160-00019
   Wright IC, 2000, AM J PSYCHIAT, V157, P16, DOI 10.1176/ajp.157.1.16
NR 49
TC 65
Z9 72
U1 0
U2 7
PU ACADEMIC PRESS INC ELSEVIER SCIENCE
PI SAN DIEGO
PA 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0014-4886
EI 1090-2430
J9 EXP NEUROL
JI Exp. Neurol.
PD NOV
PY 2001
VL 172
IS 1
BP 29
EP 46
DI 10.1006/exnr.2001.7790
PG 18
WC Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Neurosciences & Neurology
GA 491BH
UT WOS:000172087800003
PM 11681838
DA 2025-04-10
ER

PT J
AU Dijk, F
   Kraal-Muller, E
   Kamphuis, W
AF Dijk, F
   Kraal-Muller, E
   Kamphuis, W
TI Ischemia-induced changes of AMPA-type glutamate receptor subunit
   expression pattern in the rat retina: A real-time quantitative PCR study
SO INVESTIGATIVE OPHTHALMOLOGY & VISUAL SCIENCE
LA English
DT Article
ID POLYMERASE-CHAIN-REACTION; MESSENGER-RNA; GANGLION-CELLS; BETA-ACTIN;
   GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; HYPOXANTHINE
   PHOSPHORIBOSYLTRANSFERASE; DIFFERENTIAL EXPRESSION; HIPPOCAMPAL CA1;
   AMACRINE CELLS; BIPOLAR CELLS
AB PURPOSE. To investigate whether the previously observed decrease in immunoreactivity of the alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type glutamate receptor subunits GluR1, -2, -3, and -4 after ischemia-reperfusion in the rat retina is associated with changes at the mRNA expression level. Furthermore, to study possible changes in the ratios of alternative splice variants of GluR2 and -4 and possible changes in the subunit composition of the receptor complex after ischemia-reperfusion. The ischemia-induced changes were related to expression levels of immediate early genes, c-fos and c-jun, and to expression levels of different cell-type-specific transcripts.
   METHODS. A 60-minute ischemic event was induced unilaterally in the rat eye by cannulating the anterior chamber and raising the intraocular pressure. Reperfusion was allowed to occur for 2 hours up to 28 days. Total RNA was isolated from the retinas and transcript levels were assessed by real-time quantitative PCR (qPCR).
   RESULTS. A differential decrease was observed in the expression levels of all AMPA-type GluR subunits 2 hours after ischemia-reperfusion, with a significant downregulation of GluR2 and -3 transcript levels. At the long-term (72 hours- 4 weeks), expression levels for all four subunits were decreased by approximately 64%. No changes were observed, either in the expression ratio of GluR2 and -4 splice variants, or in the relative expression of the different subunits. Immediate early genes c-fos and c-jun were transiently upregulated. Expression levels of the ganglion-cell-specific transcripts Thy-1 and neurofilament and of the All-amacrine-specific transcript parvalbumin decreased after ischemia-reperfusion, whereas the ON bipolar cell transcripts mGluR6 and PKCalpha did not show ischemia-induced changes.
   CONCLUSIONS. Shortly after ischemia-reperfusion immunolabeling of GluR1, -2/3, and -4 is strongly decreased, whereas the corresponding mRNA levels are not affected, indicating degradation at the protein level. In contrast, the GluR2 mRNA level is reduced, whereas immunostaining is not yet affected, suggesting that the GluR2 protein is relatively stable under post-ischemia conditions. The long-term decrease in mRNA levels of all AMPA-type GluR subunits suggests that ischemia affects a main component of the excitatory retinal neurotransmission. It remains to be investigated whether these changes contribute to the subsequent neurodegeneration.
C1 NORI KNAW, Glaucoma Res Grp, Grad Sch Neurosci Amsterdam, NL-1105 BA Amsterdam, Netherlands.
C3 Royal Netherlands Academy of Arts & Sciences; Netherlands Institute for
   Neuroscience (NIN-KNAW); University of Amsterdam
RP NORI KNAW, Glaucoma Res Grp, Grad Sch Neurosci Amsterdam, Meibergdreef 47, NL-1105 BA Amsterdam, Netherlands.
EM f.dijk@ioi.knaw.nl
RI Dijk, Frederike/C-1627-2008
OI Dijk, Frederike/0000-0003-3970-6601
CR Alsbo CW, 2000, NEUROREPORT, V11, P311, DOI 10.1097/00001756-200002070-00018
   Braithwaite SP, 2002, P NATL ACAD SCI USA, V99, P7096, DOI 10.1073/pnas.102156099
   Brandstätter JH, 1998, VISION RES, V38, P1385, DOI 10.1016/S0042-6989(97)00176-4
   Bustin SA, 2000, J MOL ENDOCRINOL, V25, P169, DOI 10.1677/jme.0.0250169
   Casini G, 1998, DEV BRAIN RES, V111, P107, DOI 10.1016/S0165-3806(98)00127-8
   Chidlow G, 2003, BRAIN RES, V963, P298, DOI 10.1016/S0006-8993(02)04052-0
   Dev KK, 1999, NEUROPHARMACOLOGY, V38, P635, DOI 10.1016/S0028-3908(98)00230-5
   DIJK F, IN PRESS BRAIN RES
   Dingledine R, 1999, PHARMACOL REV, V51, P7
   Dong HL, 1997, NATURE, V386, P279, DOI 10.1038/386279a0
   Dong HL, 1999, J NEUROSCI, V19, P6930, DOI 10.1523/JNEUROSCI.19-16-06930.1999
   Ehlers MD, 2000, NEURON, V28, P511, DOI 10.1016/S0896-6273(00)00129-X
   EULER T, 1995, J COMP NEUROL, V361, P461, DOI 10.1002/cne.903610310
   Foss DL, 1998, ANIM BIOTECHNOL, V9, P67, DOI 10.1080/10495399809525893
   FRANK L, 1995, ACTA NEUROL SCAND, V92, P337
   Freeman WM, 1999, BIOTECHNIQUES, V26, P112, DOI 10.2144/99261rv01
   GALLO V, 1992, J NEUROSCI, V12, P1010
   GEIGER JRP, 1995, NEURON, V15, P193, DOI 10.1016/0896-6273(95)90076-4
   Ginham R, 2001, NEUROSCI LETT, V302, P113, DOI 10.1016/S0304-3940(01)01687-1
   Gorter JA, 1997, J NEUROSCI, V17, P6179
   Grooms SY, 2000, P NATL ACAD SCI USA, V97, P3631, DOI 10.1073/pnas.050586497
   Ham J, 2000, BIOCHEM PHARMACOL, V60, P1015, DOI 10.1016/S0006-2952(00)00372-5
   HAMASSAKIBRITTO DE, 1993, J NEUROSCI, V13, P1888
   Horii A, 2002, BRAIN RES PROTOC, V9, P77, DOI 10.1016/S1385-299X(01)00139-8
   HUGHES TE, 1992, VISUAL NEUROSCI, V8, P49, DOI 10.1017/S0952523800006489
   Katai N, 1999, INVEST OPHTH VIS SCI, V40, P2697
   KOHLER M, 1994, J BIOL CHEM, V269, P17367
   Kondo M, 1997, J NEUROSCI, V17, P1570
   Kuroiwa S, 1998, INVEST OPHTH VIS SCI, V39, P610
   Kurokawa T, 1999, INVEST OPHTH VIS SCI, V40, P3006
   Lam TT, 1999, INVEST OPHTH VIS SCI, V40, P967
   Lee JC, 1998, BRAIN RES PROTOC, V3, P142, DOI 10.1016/S1385-299X(98)00035-X
   Leuschner WD, 1999, J BIOL CHEM, V274, P16907, DOI 10.1074/jbc.274.24.16907
   Lu XY, 2000, BRAIN RES, V863, P143, DOI 10.1016/S0006-8993(00)02112-0
   Lu XY, 2001, J NEUROCHEM, V77, P1553, DOI 10.1046/j.1471-4159.2001.00359.x
   MASSEY SC, 1990, J NEUROPHYSIOL, V63, P16, DOI 10.1152/jn.1990.63.1.16
   Meijerink J, 2001, J MOL DIAGN, V3, P55, DOI 10.1016/S1525-1578(10)60652-6
   Michaelis EK, 1998, PROG NEUROBIOL, V54, P369, DOI 10.1016/S0301-0082(97)00055-5
   Moe TK, 2001, CURR EYE RES, V23, P44, DOI 10.1076/ceyr.23.1.44.5420
   Nash MS, 1999, INVEST OPHTH VIS SCI, V40, P1293
   Oguro K, 1999, J NEUROSCI, V19, P9218
   Osborne NN, 1996, NEUROCHEM INT, V29, P263, DOI 10.1016/0197-0186(96)00005-8
   Osborne NN, 1999, EXP EYE RES, V69, P331, DOI 10.1006/exer.1999.0706
   OSBORNE NN, 1995, INVEST OPHTH VIS SCI, V36, P1692
   Osborne NN, 2002, INVEST OPHTH VIS SCI, V43, P1456
   Osborne NN, 1999, SURV OPHTHALMOL, V43, pS102, DOI 10.1016/S0039-6257(99)00044-2
   OSBORNE NN, 1997, VASCULAR RISK FACTOR, P139
   PellegriniGiampietro DE, 1997, TRENDS NEUROSCI, V20, P464, DOI 10.1016/S0166-2236(97)01100-4
   PENG YW, 1995, NEUROSCIENCE, V66, P483, DOI 10.1016/0306-4522(94)00569-Q
   Pfaffl MW, 2002, NUCLEIC ACIDS RES, V30, DOI 10.1093/nar/30.9.e36
   Pfaffl MW, 2001, NUCLEIC ACIDS RES, V29, DOI 10.1093/nar/29.9.e45
   Reme CE, 1998, PROG RETIN EYE RES, V17, P443, DOI 10.1016/S1350-9462(98)00009-3
   SMEYNE RJ, 1993, NATURE, V363, P166, DOI 10.1038/363166a0
   Song I, 2002, TRENDS NEUROSCI, V25, P578, DOI 10.1016/S0166-2236(02)02270-1
   Srivastava S, 1998, NEURON, V21, P581, DOI 10.1016/S0896-6273(00)80568-1
   TAKAHASHI K, 1992, ARCH OPHTHALMOL-CHIC, V110, P862, DOI 10.1001/archopht.1992.01080180134041
   Takeda M, 2000, INVEST OPHTH VIS SCI, V41, P2412
   Tanaka H, 2000, BRAIN RES, V886, P190, DOI 10.1016/S0006-8993(00)02951-6
   Thoreson WB, 1999, PROG RETIN EYE RES, V18, P765, DOI 10.1016/S1350-9462(98)00031-7
   Vandesompele J, 2002, GENOME BIOL, V3, DOI 10.1186/gb-2002-3-7-research0034
   Vardi N, 2000, J COMP NEUROL, V423, P402, DOI 10.1002/1096-9861(20000731)423:3<402::AID-CNE4>3.0.CO;2-E
   WASSLE H, 1991, PHYSIOL REV, V71, P447, DOI 10.1152/physrev.1991.71.2.447
   WASSLE H, 1993, J COMP NEUROL, V332, P407
   Zhong H, 1999, BIOCHEM BIOPH RES CO, V259, P523, DOI 10.1006/bbrc.1999.0815
NR 64
TC 48
Z9 53
U1 0
U2 1
PU ASSOC RESEARCH VISION OPHTHALMOLOGY INC
PI ROCKVILLE
PA 12300 TWINBROOK PARKWAY, ROCKVILLE, MD 20852-1606 USA
SN 0146-0404
EI 1552-5783
J9 INVEST OPHTH VIS SCI
JI Invest. Ophthalmol. Vis. Sci.
PD JAN
PY 2004
VL 45
IS 1
BP 330
EP 341
DI 10.1167/iovs.03-0285
PG 12
WC Ophthalmology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Ophthalmology
GA 761AF
UT WOS:000187875600047
PM 14691192
DA 2025-04-10
ER

PT J
AU Kobayashi, Y
   Katanosaka, Y
   Iwata, Y
   Matsuoka, M
   Shigekawa, M
   Wakabayashi, S
AF Kobayashi, Yuko
   Katanosaka, Yuki
   Iwata, Yuko
   Matsuoka, Masayuki
   Shigekawa, Munekazu
   Wakabayashi, Shigeo
TI Identification and characterization of GSRP-56, a novel Golgi-localized
   spectrin repeat-containing protein
SO EXPERIMENTAL CELL RESEARCH
LA English
DT Article
DE Syne-1; Nesprin-1; spectrin repeat; Golgi apparatus; subcellular
   localization
ID NUCLEAR-MEMBRANE; NEUROMUSCULAR-JUNCTION; MEMBER SYNE-1; COMPLEX;
   CHANNEL; MUSCLE; ASSOCIATION; APPARATUS; MAKAP; TRANSLOCATION
AB Spectrin repeat (SR)-containing proteins are important for regulation of integrity of biomembranes, not only the plasma membrane but also those of intracellular organelles, such as the Golgi nucleus, endo/lysosomes, and synaptic vesicles. We identified a novel SR-containing protein, named GSRP-56 (Golgi-localized SR-containing protein-56), by a yeast two-hybrid method, using a member of the transient receptor potential channel family, TRPV2, as bait. GSRP-56 is an isoform. derived from a giant SR-containing protein, Syne-1 (synaptic nuclear envelope protein-1, also referred to as Nesprin-1 or Enaptin), predicted to be produced by alternative splicing. Immunological analysis demonstrated that this isoform is a 56-kDa protein, which is localized predominantly in the Golgi apparatus in cardiomyocytes and C2C12 myoblasts/myotubes, and we found that two SR domains were required both for Golgi targeting and for interaction with TRPV2. Interestingly, overexpression of GSRP-56 resulted in a morphological change in the Golgi structure, characterized by its enlargement of cis-Golgi marker antibody-staining area, which would result partly from fragmentation of Golgi membranes. Our findings indicate that GSRP-56 is a novel, particularly small Golgi-localized member of the spectrin family, which possibly play a role in maintenance of the Golgi structure. (c) 2006 Elsevier Inc. All rights reserved.
C1 Senri Kinran Univ, Dept Human Life Sci, Suita, Osaka 5650873, Japan.
   Natl Cardiovasc Ctr, Res Inst, Dept Mol Physiol, Suita, Osaka 5658565, Japan.
C3 National Cerebral & Cardiovascular Center - Japan
RP Kobayashi, Y (corresponding author), Senri Kinran Univ, Dept Human Life Sci, Suita, Osaka 5650873, Japan.
EM yu-kobayashi@kinran.ac.jp; wak@ri.ncvc.go.jp
CR Apel ED, 2000, J BIOL CHEM, V275, P31986, DOI 10.1074/jbc.M004775200
   Barnhill JC, 2004, J CELL BIOCHEM, V91, P808, DOI 10.1002/jcb.10775
   Beck KA, 1996, AM J PHYSIOL-CELL PH, V270, pC1263, DOI 10.1152/ajpcell.1996.270.5.C1263
   Beck KA, 2005, BBA-MOL CELL RES, V1744, P374, DOI 10.1016/j.bbamcr.2005.04.008
   Beck KA, 1998, BBA-MOL CELL RES, V1404, P153, DOI 10.1016/S0167-4889(98)00054-8
   BECK KA, 1994, J CELL BIOL, V127, P707, DOI 10.1083/jcb.127.3.707
   Beck KA, 1997, J CELL SCI, V110, P1239
   Bennett V, 2001, PHYSIOL REV, V81, P1353, DOI 10.1152/physrev.2001.81.3.1353
   Boels K, 2001, J CELL SCI, V114, P3599
   Cottrell JR, 2004, NEURON, V44, P677, DOI 10.1016/S0896-6273(04)00688-9
   De Matteis MA, 2000, J CELL SCI, V113, P2331
   Devarajan P, 1996, J CELL BIOL, V133, P819, DOI 10.1083/jcb.133.4.819
   Djinovic-Carugo K, 2002, FEBS LETT, V513, P119, DOI 10.1016/S0014-5793(01)03304-X
   Fan J, 2004, J CELL SCI, V117, P619, DOI 10.1242/jcs.00892
   Godi A, 1998, P NATL ACAD SCI USA, V95, P8607, DOI 10.1073/pnas.95.15.8607
   Gough LL, 2004, BBA-MOL CELL RES, V1693, P29, DOI 10.1016/j.bbamcr.2004.04.004
   Gough LL, 2003, MOL BIOL CELL, V14, P2410, DOI 10.1091/mbc.E02-07-0446
   Grady RM, 2005, P NATL ACAD SCI USA, V102, P4359, DOI 10.1073/pnas.0500711102
   Iwata Y, 2003, J CELL BIOL, V161, P957, DOI 10.1083/jcb.200301101
   IWATA Y, 1993, FEBS LETT, V329, P227, DOI 10.1016/0014-5793(93)80227-L
   Kanzaki M, 1999, NAT CELL BIOL, V1, P165, DOI 10.1038/11086
   Kapiloff MS, 1999, J CELL SCI, V112, P2725
   Kapiloff MS, 2001, J CELL SCI, V114, P3167
   Katanosaka Y, 2005, J BIOL CHEM, V280, P5764, DOI 10.1074/jbc.M410240200
   KENNEDY SP, 1994, J BIOL CHEM, V269, P11400
   Kent WJ, 2002, GENOME RES, V12, P656, DOI [10.1101/gr.229202. Article published online before March 2002, 10.1101/gr.229202]
   KRONEBUSCH PJ, 1987, J CELL SCI, V88, P25
   LOMBARDO CR, 1994, J BIOL CHEM, V269, P29212
   Lu ZM, 2001, MOL BIOL CELL, V12, P795, DOI 10.1091/mbc.12.4.795
   Mislow JMK, 2002, FEBS LETT, V525, P135, DOI 10.1016/S0014-5793(02)03105-8
   Mislow JMK, 2002, J CELL SCI, V115, P61
   Padmakumar VC, 2004, EXP CELL RES, V295, P330, DOI 10.1016/j.yexcr.2004.01.014
   Pare GC, 2005, EXP CELL RES, V303, P388, DOI 10.1016/j.yexcr.2004.10.009
   Pascual J, 1997, BIOESSAYS, V19, P811, DOI 10.1002/bies.950190911
   Schultz J, 1998, P NATL ACAD SCI USA, V95, P5857, DOI 10.1073/pnas.95.11.5857
   Stokes AJ, 2005, J CELL BIOCHEM, V94, P669, DOI 10.1002/jcb.20331
   Strausberg RL, 2002, P NATL ACAD SCI USA, V99, P16899, DOI 10.1073/pnas.242603899
   TASSIN AM, 1985, J CELL BIOL, V101, P630, DOI 10.1083/jcb.101.2.630
   YAN Y, 1993, SCIENCE, V262, P2027, DOI 10.1126/science.8266097
   Zhang QP, 2001, J CELL SCI, V114, P4485
NR 40
TC 23
Z9 30
U1 0
U2 6
PU ELSEVIER INC
PI SAN DIEGO
PA 525 B STREET, STE 1900, SAN DIEGO, CA 92101-4495 USA
SN 0014-4827
EI 1090-2422
J9 EXP CELL RES
JI Exp. Cell Res.
PD OCT 1
PY 2006
VL 312
IS 16
BP 3152
EP 3164
DI 10.1016/j.yexcr.2006.06.026
PG 13
WC Oncology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Oncology; Cell Biology
GA 085EV
UT WOS:000240587200016
PM 16875688
DA 2025-04-10
ER

PT J
AU Blumenstein, Y
   Kanevsky, N
   Sahar, G
   Barzilai, R
   Ivanina, T
   Dascal, N
AF Blumenstein, Y
   Kanevsky, N
   Sahar, G
   Barzilai, R
   Ivanina, T
   Dascal, N
TI A novel long N-terminal isoform of human L-type Ca<SUP>2+</SUP> channel
   is up-regulated by protein kinase C
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID SENSITIVE CALCIUM-CHANNEL; ALPHA(1C) SUBUNIT; XENOPUS OOCYTES;
   FUNCTIONAL EXPRESSION; SPLICE VARIANTS; MODULATION; PHOSPHORYLATION;
   INHIBITION; CURRENTS; CLONING
AB Human L-type voltage-dependent Ca2+ channels (alpha(1C), or Ca(v)1.2) are up-regulated by protein kinase C (PKC) in native tissues, but in heterologous systems this modulation is absent. In rat and rabbit, alpha(1C) has two N-terminal (NT) isoforms, long and short, with variable initial segments of 46 and 16 amino acids, respectively. The initial 46 amino acids of the long-NT alpha(1c) are crucial for PKC regulation. However, only a short-NT human a1c is known. We assumed that a Iong-NT isoform of human a,c may exist. By homology screening of human genomic DNA, we identified a stretch (termed exon 1a) highly homologous to rabbit long-NT, separated from the next known exon of alpha(1c) (exon lb, which encodes the alternative, short-NT) by an similar to80 kb-long intron. The predicted 46-amino acid protein sequence is highly homologous to rabbit long-NT. Reverse transcriptase PCR showed the presence of exon la transcript in human cardiac RNA. Expression of human long(.)NT alpha(1c) in Xenopus oocytes produced Ca2+ channel enhanced by a PKC activator, whereas the short-NT alpha(1c) was inhibited. The long-NT isoform may be the Ca2+ channel enhanced by PKC-activating transmitters in human tissues.
C1 Rabin Med Ctr, IL-49100 Petah Tiqwa, Israel.
   Tel Aviv Univ, Sackler Fac Med, Dept Physiol & Pharmacol, IL-69978 Tel Aviv, Israel.
C3 Rabin Medical Center; Tel Aviv University; Sackler Faculty of Medicine
RP Dascal, N (corresponding author), Tel Aviv Univ, Sackler Fac Med, Dept Physiol & Pharmacol, IL-69978 Tel Aviv, Israel.
RI Dascal, Nathan/O-3915-2015
OI Dascal, Nathan/0000-0002-5397-4146
CR BIEL M, 1990, FEBS LETT, V269, P409, DOI 10.1016/0014-5793(90)81205-3
   Boixel C, 2000, AM J PHYSIOL-HEART C, V278, pH670, DOI 10.1152/ajpheart.2000.278.2.H670
   BOURINET E, 1992, PFLUG ARCH EUR J PHY, V421, P247, DOI 10.1007/BF00374834
   Bouron A, 1995, FEBS LETT, V377, P159, DOI 10.1016/0014-5793(95)01327-X
   Catterall WA, 2000, ANNU REV CELL DEV BI, V16, P521, DOI 10.1146/annurev.cellbio.16.1.521
   Dascal N., 1992, METHOD MOL BIOL, V13, P205
   Ertel EA, 2000, NEURON, V25, P533, DOI 10.1016/S0896-6273(00)81057-0
   Fearon IM, 2000, CIRC RES, V87, P537, DOI 10.1161/01.RES.87.7.537
   Finkbeiner S, 1998, J NEUROBIOL, V37, P171, DOI 10.1002/(SICI)1097-4695(199810)37:1<171::AID-NEU13>3.0.CO;2-H
   Hernández ME, 1999, NEUROENDOCRINOLOGY, V70, P31, DOI 10.1159/000054457
   Kamp TJ, 2000, CIRC RES, V87, P1095, DOI 10.1161/01.RES.87.12.1095
   Klockner U, 1997, AM J PHYSIOL-HEART C, V272, pH1372, DOI 10.1152/ajpheart.1997.272.3.H1372
   KOCH WJ, 1990, J BIOL CHEM, V265, P17786
   LACERDA AE, 1988, NATURE, V335, P249, DOI 10.1038/335249a0
   Love JA, 1998, AM J PHYSIOL-GASTR L, V274, pG397, DOI 10.1152/ajpgi.1998.274.2.G397
   McHugh D, 2000, P NATL ACAD SCI USA, V97, P12334, DOI 10.1073/pnas.210384297
   MIKAMI A, 1989, NATURE, V340, P230, DOI 10.1038/340230a0
   PEREZREYES E, 1992, J BIOL CHEM, V267, P1792
   REEVE HL, 1995, PFLUG ARCH EUR J PHY, V429, P729, DOI 10.1007/BF00373996
   REUTER H, 1983, NATURE, V301, P569, DOI 10.1038/301569a0
   Savignac M, 2001, FASEB J, V15, P1577, DOI 10.1096/fj.00-0733fje
   SCHUHMANN K, 1994, FEBS LETT, V341, P208, DOI 10.1016/0014-5793(94)80458-3
   Sharon D, 1997, J GEN PHYSIOL, V109, P477, DOI 10.1085/jgp.109.4.477
   Shistik E, 1999, J BIOL CHEM, V274, P31145, DOI 10.1074/jbc.274.44.31145
   Shistik E, 1998, J BIOL CHEM, V273, P17901, DOI 10.1074/jbc.273.28.17901
   SINGER D, 1991, SCIENCE, V253, P1553, DOI 10.1126/science.1716787
   SINGERLAHAT D, 1992, FEBS LETT, V306, P113, DOI 10.1016/0014-5793(92)80980-U
   SNUTCH TP, 1991, NEURON, V7, P45, DOI 10.1016/0896-6273(91)90073-9
   SOLDATOV NM, 1995, J BIOL CHEM, V270, P10540, DOI 10.1074/jbc.270.18.10540
   SOLDATOV NM, 1994, GENOMICS, V22, P77, DOI 10.1006/geno.1994.1347
   Soldatov NM, 1997, J BIOL CHEM, V272, P3560, DOI 10.1074/jbc.272.6.3560
   TSENG GN, 1991, AM J PHYSIOL, V261, pH364, DOI 10.1152/ajpheart.1991.261.2.H364
   Wang XT, 2000, AM J PATHOL, V157, P1549, DOI 10.1016/S0002-9440(10)64792-X
   Yang YB, 2000, J MOL CELL CARDIOL, V32, P973, DOI 10.1006/jmcc.2000.1138
   Zühlke RD, 1998, FEBS LETT, V427, P220, DOI 10.1016/S0014-5793(98)00425-6
NR 35
TC 41
Z9 46
U1 0
U2 1
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
SN 0021-9258
J9 J BIOL CHEM
JI J. Biol. Chem.
PD FEB 1
PY 2002
VL 277
IS 5
BP 3419
EP 3423
DI 10.1074/jbc.C100642200
PG 5
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 518VF
UT WOS:000173688000049
PM 11741969
OA hybrid
DA 2025-04-10
ER

PT J
AU Pierzchlinska, A
   Slawek, J
   Kwasniak-Butowska, M
   Malinowski, D
   Komaniecka, N
   Mak, M
   Czerkawska, A
   Kukowka, A
   Bialecka, M
AF Pierzchlinska, Anna
   Slawek, Jaroslaw
   Kwasniak-Butowska, Magdalena
   Malinowski, Damian
   Komaniecka, Nina
   Mak, Monika
   Czerkawska, Anna
   Kukowka, Arnold
   Bialecka, Monika
TI Genetic Polymorphisms in the HMGCR Gene and Associations with
   Cognitive Decline in Parkinson's Disease Patients
SO INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
LA English
DT Article
DE Parkinson's disease; HMGCR; dementia; cognitive decline; genetic
   polymorphisms; lipids
ID ALZHEIMERS-DISEASE; CHOLESTEROL LEVELS; STATIN THERAPY; LIPID-LEVELS;
   DEMENTIA; PATHOLOGY; REDUCTASE; RISK; PREDICTORS; ONSET
AB Parkinson's disease (PD) is a common neurodegenerative disease characterized by motor and non-motor symptoms including cognitive impairment and dementia. The etiopathogenesis of PD, as well as its protective and susceptibility factors, are still elusive. 3-Hydroxy-3-methyglutaryl coenzyme A reductase (HMGCR) is an enzyme regulating cholesterol synthesis. Single-nucleotide polymorphisms (SNPs) in the gene coding HMGCR have recently been correlated with the risk of Alzheimer's disease. Alternative splicing of exon 13 of the HMGCR transcript and its strongly associated HMGCR haplotype 7 (H7: rs17244841, rs3846662, rs17238540) may downregulate protein activity and cholesterol synthesis, with lower low-density lipoprotein cholesterol (LDL) levels associated with PD that may affect cognitive abilities. We genotyped three SNPs in the H7 HMGCR gene in 306 PD patients divided into three groups-without cognitive decline, with mild cognitive impairment (MCI), and with PD dementia-and in 242 healthy participants. A correlation between the rs17238540 genotype and PD susceptibility as well as a minor association between rs3846662 and cognitive status in PD patients was observed; however, the two-sided analysis of these groups did not reveal any significance. We observed a statistically significant elevated high-density lipoprotein cholesterol (HDL) plasma level in the minor allele carriers of rs17238540 and rs17244841 among PD patients. This study should be replicated in a larger population.
C1 [Pierzchlinska, Anna; Malinowski, Damian; Czerkawska, Anna; Kukowka, Arnold; Bialecka, Monika] Pomeranian Med Univ, Dept Pharmacokinet & Therapeut Drug Monitoring, PL-70111 Szczecin, Poland.
   [Pierzchlinska, Anna] Univ Cologne, Inst Zool, Dept Anim Physiol, D-50923 Cologne, Germany.
   [Slawek, Jaroslaw; Kwasniak-Butowska, Magdalena] Med Univ Gdansk, Fac Hlth Sci, Dept Neurol Psychiat Nursing, PL-80211 Gdansk, Poland.
   [Slawek, Jaroslaw; Kwasniak-Butowska, Magdalena] St Adalbert Hosp, Dept Neurol, PL-61144 Gdansk, Poland.
   [Komaniecka, Nina] Pomeranian Med Univ, Dept Expt & Clin Pharmacol, PL-70111 Szczecin, Poland.
   [Mak, Monika] Pomeranian Med Univ, Dept Hlth Psychol, Szczecin, Poland.
C3 Pomeranian Medical University; University of Cologne; Fahrenheit
   Universities; Medical University Gdansk; Pomeranian Medical University;
   Pomeranian Medical University
RP Malinowski, D (corresponding author), Pomeranian Med Univ, Dept Pharmacokinet & Therapeut Drug Monitoring, PL-70111 Szczecin, Poland.
EM pierzchlinska@gmail.com; jaroslaw.slawek@gumed.edu.pl;
   magda.kwasniak@gmail.com; damian.malinowski@pum.edu.pl;
   nina.komaniecka@pum.edu.pl; monika.mak@pum.edu.pl;
   ania.czerkawska@wp.pl; arnold.kukowka@gmail.com; monika-bialecka@post.pl
RI Malinowski, Damian/M-1455-2014; Mak, Monika/I-8736-2014; Białecka,
   Monika/A-9341-2015; Pierzchlinska, Anna/H-2266-2017
OI Kukowka, Arnold/0000-0001-5374-7827; Pierzchlinska,
   Anna/0000-0002-1606-7918; Malinowski, Damian/0000-0001-8393-9627
FU institutional grants of the Department of Pharmacokinetics and
   Therapeutic Drug Monitoring, Pomeranian Medical University, Szczecin,
   Poland; Pomeranian Medical University, Szczecin, Poland
FX This research was funded by institutional grants of the Department of
   Pharmacokinetics and Therapeutic Drug Monitoring, Pomeranian Medical
   University, Szczecin, Poland. No external funding was received.
CR Aarsland D, 2003, ARCH NEUROL-CHICAGO, V60, P387, DOI 10.1001/archneur.60.3.387
   Aarsland D, 2010, J NEUROL SCI, V289, P18, DOI 10.1016/j.jns.2009.08.034
   Alecu I, 2019, FRONT NEUROSCI-SWITZ, V13, DOI 10.3389/fnins.2019.00328
   Anang JBM, 2014, NEUROLOGY, V83, P1253, DOI 10.1212/WNL.0000000000000842
   Benn M, 2017, BMJ-BRIT MED J, V357, DOI 10.1136/bmj.j1648
   Björkhem I, 2004, ARTERIOSCL THROM VAS, V24, P806, DOI 10.1161/01.ATV.0000120374.59826.1b
   Burkhardt R, 2008, ARTERIOSCL THROM VAS, V28, P2078, DOI 10.1161/ATVBAHA.108.172288
   Cano-Corres R, 2018, J CLIN LAB ANAL, V32, DOI 10.1002/jcla.22566
   Chang XL, 2016, ONCOTARGET, V7, P22746, DOI 10.18632/oncotarget.8176
   Chasman DI, 2004, JAMA-J AM MED ASSOC, V291, P2821, DOI 10.1001/jama.291.23.2821
   Chen YC, 2009, LIPIDS, V44, P733, DOI 10.1007/s11745-009-3314-6
   Choe CU, 2021, PARKINSONISM RELAT D, V85, P5, DOI 10.1016/j.parkreldis.2021.02.007
   Donnelly LA, 2008, PHARMACOGENET GENOM, V18, P1021, DOI 10.1097/FPC.0b013e3283106071
   Emre M, 2007, MOVEMENT DISORD, V22, P1689, DOI 10.1002/mds.21507
   Freitas RN, 2010, EUR J CARDIOV PREV R, V17, P89, DOI 10.1097/HJR.0b013e328330be77
   Freitas RN, 2009, J AM SOC HYPERTENS, V3, P238, DOI 10.1016/j.jash.2009.05.001
   Hu G, 2008, NEUROLOGY, V70, P1972, DOI 10.1212/01.wnl.0000312511.62699.a8
   Huang CQ, 2009, DEMENT GERIATR COGN, V27, P111, DOI 10.1159/000194660
   Huang XM, 2007, MOVEMENT DISORD, V22, P377, DOI 10.1002/mds.21290
   HUGHES AJ, 1992, J NEUROL NEUROSUR PS, V55, P181, DOI 10.1136/jnnp.55.3.181
   Hurh K, 2022, SCI REP-UK, V12, DOI 10.1038/s41598-022-25180-8
   Jellinger KA, 2003, ACTA NEUROPATHOL, V106, P191, DOI 10.1007/s00401-003-0725-y
   Kalia LV, 2015, JAMA NEUROL, V72, P100, DOI 10.1001/jamaneurol.2014.2704
   Kushniarevich A, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0135820
   Leduc V, 2015, MOL PSYCHIATR, V20, P867, DOI 10.1038/mp.2014.81
   Leduc V, 2016, PHARMACOGENET GENOM, V26, P1, DOI 10.1097/FPC.0000000000000178
   Litvan I, 2011, MOVEMENT DISORD, V26, P1814, DOI 10.1002/mds.23823
   Medina MW, 2010, DISCOV MED, V9, P495
   Medina MW, 2008, CIRCULATION, V118, P355, DOI 10.1161/CIRCULATIONAHA.108.773267
   Paul R, 2015, NEUROCHEM INT, V90, P125, DOI 10.1016/j.neuint.2015.07.025
   Peng ZY, 2018, PARKINSONISM RELAT D, V55, P68, DOI 10.1016/j.parkreldis.2018.05.013
   Pierzchlinska A, 2021, MOL BIOL REP, V48, P5541, DOI 10.1007/s11033-021-06569-6
   Pierzchlinska A, 2018, NEUROL NEUROCHIR POL, V52, P477, DOI 10.1016/j.pjnns.2018.04.003
   Rizwan M, 2021, PAK J PHARM SCI, V34, P1577, DOI 10.36721/PJPS.2021.34.4.SUP.1577-1583.1
   Saravi SSS, 2017, METAB BRAIN DIS, V32, P949, DOI 10.1007/s11011-017-0021-5
   Shahmoradian SH, 2019, NAT NEUROSCI, V22, P1099, DOI 10.1038/s41593-019-0423-2
   Siokas V, 2021, NEUROSCI LETT, V748, DOI 10.1016/j.neulet.2021.135709
   Wright SM, 2019, NEUROBIOL AGING, V84, DOI 10.1016/j.neurobiolaging.2019.03.004
   Yan JQ, 2019, MEDICINE, V98, DOI 10.1097/MD.0000000000014852
   Yang ZJ, 2022, NEUROSCI LETT, V784, DOI 10.1016/j.neulet.2022.136734
   Zhu KD, 2014, PARKINSONISM RELAT D, V20, P980, DOI 10.1016/j.parkreldis.2014.06.006
NR 41
TC 0
Z9 0
U1 0
U2 1
PU MDPI
PI BASEL
PA ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
SN 1661-6596
EI 1422-0067
J9 INT J MOL SCI
JI Int. J. Mol. Sci.
PD AUG
PY 2024
VL 25
IS 16
AR 8964
DI 10.3390/ijms25168964
PG 11
WC Biochemistry & Molecular Biology; Chemistry, Multidisciplinary
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Chemistry
GA F0T5Q
UT WOS:001307031700001
PM 39201649
OA gold, Green Published
DA 2025-04-10
ER

PT J
AU Doherty, R
   MacLeod, BL
   Nelson, MM
   Ibrahim, MMH
   Borges, BC
   Jaradat, NW
   Finneran, MC
   Giger, RJ
   Corfas, G
AF Doherty, Robert
   MacLeod, Brenna L.
   Nelson, Megan M.
   Ibrahim, Mostafa M. H.
   Borges, Beatriz C.
   Jaradat, Nada W.
   Finneran, Matthew C.
   Giger, Roman J.
   Corfas, Gabriel
TI Identification of in vivo roles of ErbB4-JMa and its direct nuclear
   signaling using a novel isoform-specific knock out mouse
SO SCIENTIFIC REPORTS
LA English
DT Article
ID ALPHA-CONVERTING ENZYME; CARDIAC DEVELOPMENT; MICE LACKING; CLEAVAGE;
   NEUREGULIN-1; DEFECTS; ERBB-4; PROLIFERATION; INTERNEURONS; MUTATIONS
AB Like all receptor tyrosine kinases (RTKs), ErbB4 signals through a canonical signaling involving phosphorylation cascades. However, ErbB4 can also signal through a non-canonical mechanism whereby the intracellular domain is released into the cytoplasm by regulated intramembrane proteolysis (RIP) and translocates to the nucleus where it regulates transcription. These different signaling mechanisms depend on the generation of alternative spliced isoforms, a RIP cleavable ErbB4-JMa and an uncleavable ErbB4-JMb. Non-canonical signaling by ErbB4-JMa has been implicated in the regulation of brain, heart, mammary gland, lung, and immune cell development. However, most studies on non-canonical ErbB4 signaling have been performed in vitro due to the lack of an adequate mouse model. We created an ErbB4-JMa specific knock out mouse and demonstrate that RIP-dependent, non-canonical signaling by ErbB4-JMa is required for the regulation of GFAP expression during cortical development. We also show that ErbB4-JMa signaling is not required for the development of the heart, mammary glands, sensory ganglia. Furthermore, we identify genes whose expression during cortical development is regulated by ErbB4, and show that the expression of three of them, CRYM and DBi, depend on ErbB4-JMa whereas WDFY1 relies on ErbB4-JMb. Thus, we provide the first animal model to directly study the roles of ErbB4-JMa and non-canonical ErbB4 signaling in vivo.
C1 [Doherty, Robert; MacLeod, Brenna L.; Nelson, Megan M.; Ibrahim, Mostafa M. H.; Borges, Beatriz C.; Jaradat, Nada W.; Corfas, Gabriel] Univ Michigan, Kresge Hearing Res Inst, Dept Otolaryngol Head & Neck Surg, Med Sch, Med Sci 1 Bldg,Rm 5428,1150 West Med Ctr Dr, Ann Arbor, MI 48109 USA.
   [Doherty, Robert; Nelson, Megan M.; Finneran, Matthew C.; Giger, Roman J.] Univ Michigan, Neurosci Grad Program, Med Sch, Ann Arbor, MI 48109 USA.
   [Finneran, Matthew C.; Giger, Roman J.] Univ Michigan, Dept Cell & Dev Biol, Med Sch, Ann Arbor, MI 48109 USA.
C3 University of Michigan System; University of Michigan; University of
   Michigan System; University of Michigan; University of Michigan System;
   University of Michigan
RP Corfas, G (corresponding author), Univ Michigan, Kresge Hearing Res Inst, Dept Otolaryngol Head & Neck Surg, Med Sch, Med Sci 1 Bldg,Rm 5428,1150 West Med Ctr Dr, Ann Arbor, MI 48109 USA.
EM corfas@med.umich.edu
RI Giger, Roman/JCE-2303-2023
OI Finneran, Matthew/0000-0002-6742-206X; Giger, Roman/0000-0002-2926-3336;
   Doherty, Robert/0000-0001-9307-7995
FU  [R21NS108783]
FX This study was supported in part by R21NS108783 (G.C.). We thank Michael
   Hayes for his help managing the mouse colony.
CR Alfonso J, 2012, CELL STEM CELL, V10, P76, DOI 10.1016/j.stem.2011.11.011
   Ali Zafar, 2011, Indian J Hum Genet, V17, P65, DOI 10.4103/0971-6866.86178
   Almenar-Queralt A, 2013, J BIOL CHEM, V288, P35222, DOI 10.1074/jbc.M113.513705
   Anton ES, 2004, NAT NEUROSCI, V7, P1319, DOI 10.1038/nn1345
   Arribere JA, 2018, ELIFE, V7, DOI 10.7554/eLife.33292
   Chai H, 2017, NEURON, V95, P531, DOI 10.1016/j.neuron.2017.06.029
   Cheng QC, 2003, J BIOL CHEM, V278, P38421, DOI 10.1074/jbc.M302111200
   del Pino I, 2013, NEURON, V79, P1152, DOI 10.1016/j.neuron.2013.07.010
   Dumitru I, 2017, NEURON, V94, P125, DOI 10.1016/j.neuron.2017.03.003
   Elenius K, 1997, J BIOL CHEM, V272, P26761, DOI 10.1074/jbc.272.42.26761
   Flames N, 2004, NEURON, V44, P251, DOI 10.1016/j.neuron.2004.09.028
   GASSMANN M, 1995, NATURE, V378, P390, DOI 10.1038/378390a0
   Geng HY, 2017, J NEUROSCI, V37, P7450, DOI 10.1523/JNEUROSCI.3948-16.2017
   Golding JP, 2000, NAT CELL BIOL, V2, P103, DOI 10.1038/35000058
   Goth CK, 2015, P NATL ACAD SCI USA, V112, P14623, DOI 10.1073/pnas.1511175112
   Guan YF, 2015, NEUROSCIENCE, V307, P151, DOI 10.1016/j.neuroscience.2015.08.047
   Hoeing K, 2011, BBA-MOL CELL RES, V1813, P480, DOI 10.1016/j.bbamcr.2010.12.017
   Horiuchi Keisuke, 2013, Keio Journal of Medicine, V62, P29, DOI 10.2302/kjm.2012-0003-RE
   Iwamoto R, 2017, J CELL SCI, V130, P1321, DOI 10.1242/jcs.196618
   Kinney Christian J, 2021, Endocr Regul, V55, P89, DOI 10.2478/enr-2021-0011
   Krämer A, 2014, BIOINFORMATICS, V30, P523, DOI 10.1093/bioinformatics/btt703
   Lemmon MA, 2010, CELL, V141, P1117, DOI 10.1016/j.cell.2010.06.011
   Li B, 2007, NEURON, V54, P583, DOI 10.1016/j.neuron.2007.03.028
   Li H, 2012, NEURAL DEV, V7, DOI 10.1186/1749-8104-7-10
   Liu W, 2010, BBA-MOL CELL RES, V1803, P832, DOI 10.1016/j.bbamcr.2010.03.003
   López-Bendito G, 2006, CELL, V125, P127, DOI 10.1016/j.cell.2006.01.042
   McDonell LM, 2015, HUM MOL GENET, V24, pR60, DOI 10.1093/hmg/ddv254
   Mei L, 2008, NAT REV NEUROSCI, V9, P437, DOI 10.1038/nrn2392
   Mei L, 2014, NEURON, V83, P27, DOI 10.1016/j.neuron.2014.06.007
   Merilahti JAM, 2019, ONCOGENE, V38, P151, DOI 10.1038/s41388-018-0465-z
   Merilahti JAM, 2017, MOL BIOL CELL, V28, P3123, DOI 10.1091/mbc.E17-04-0261
   Mitchell RM, 2013, P NATL ACAD SCI USA, V110, P19603, DOI 10.1073/pnas.1312791110
   Mitsui S, 2009, EUR J NEUROSCI, V30, P2368, DOI 10.1111/j.1460-9568.2009.07029.x
   Molinari F, 2002, SCIENCE, V298, P1779, DOI 10.1126/science.1076521
   Müller T, 2018, EMBO J, V37, DOI 10.15252/embj.201798858
   Muraoka-Cook RS, 2008, J MAMMARY GLAND BIOL, V13, P235, DOI 10.1007/s10911-008-9080-x
   Muraoka-Cook RS, 2005, BREAST CANCER RES, V7, pS32, DOI 10.1186/bcr1124
   Ni CY, 2001, SCIENCE, V294, P2179, DOI 10.1126/science.1065412
   Pitcher GM, 2008, NEUROREPORT, V19, P139, DOI 10.1097/WNR.0b013e3282f3da10
   Rio C, 2000, J BIOL CHEM, V275, P10379, DOI 10.1074/jbc.275.14.10379
   Sardi SP, 2006, CELL, V127, P185, DOI 10.1016/j.cell.2006.07.037
   Schlessinger J, 2006, CELL, V127, P45, DOI 10.1016/j.cell.2006.09.013
   Shen J, 1997, CELL, V89, P629, DOI 10.1016/S0092-8674(00)80244-5
   Shi W, 2003, DEV BIOL, V261, P371, DOI 10.1016/S0012-1606(03)00315-4
   Skirzewski M, 2018, MOL PSYCHIATR, V23, P2227, DOI 10.1038/mp.2017.132
   Song SM, 2013, CSH PERSPECT BIOL, V5, DOI 10.1101/cshperspect.a009001
   Soto-Faguás CM, 2021, ACTA NEUROPATHOL COM, V9, DOI 10.1186/s40478-021-01259-7
   Takahashi Y, 2013, AM J HUM GENET, V93, P900, DOI 10.1016/j.ajhg.2013.09.008
   Tian J, 2017, MOL NEUROBIOL, V54, P3976, DOI 10.1007/s12035-016-9956-5
   Tidcombe H, 2003, P NATL ACAD SCI USA, V100, P8281, DOI 10.1073/pnas.1436402100
   Vecchi M, 1996, J BIOL CHEM, V271, P18989, DOI 10.1074/jbc.271.31.18989
   Yin DM, 2013, J NEUROSCI, V33, P19295, DOI 10.1523/JNEUROSCI.2090-13.2013
   Zhang H, 2017, NEUROBIOL DIS, V106, P171, DOI 10.1016/j.nbd.2017.07.001
   Zhou WL, 2000, J BIOL CHEM, V275, P34737, DOI 10.1074/jbc.M003756200
NR 54
TC 1
Z9 1
U1 0
U2 2
PU NATURE PORTFOLIO
PI BERLIN
PA HEIDELBERGER PLATZ 3, BERLIN, 14197, GERMANY
SN 2045-2322
J9 SCI REP-UK
JI Sci Rep
PD OCT 14
PY 2022
VL 12
IS 1
AR 17267
DI 10.1038/s41598-022-21598-2
PG 16
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA 5U0RL
UT WOS:000876261700035
PM 36241655
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Markó, L
   Paragh, G
   Ugocsai, P
   Boettcher, A
   Vogt, T
   Schling, P
   Balogh, A
   Tarabin, V
   Orsó, E
   Wikonkál, N
   Mandl, J
   Remenyik, E
   Schmitz, G
AF Marko, Lorant
   Paragh, Gyoergy
   Ugocsai, Peter
   Boettcher, Alfred
   Vogt, Thomas
   Schling, Petra
   Balogh, Attila
   Tarabin, Victoria
   Orso, Evelyn
   Wikonkal, Norbert
   Mandl, Jozsef
   Remenyik, Eva
   Schmitz, Gerd
TI Keratinocyte ATP binding cassette transporter expression is regulated by
   ultraviolet light
SO JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY
LA English
DT Article
DE Keratinocyte; Lipid transport; ABC transporter; UVB; Epidermal barrier
ID CULTURED HUMAN KERATINOCYTES; UVB-INDUCED ALTERATIONS; STRATUM-CORNEUM
   LIPIDS; PERMEABILITY BARRIER; ABC TRANSPORTERS; SKIN BARRIER; HARLEQUIN
   ICHTHYOSIS; LAMELLAR GRANULES; IRRADIATION; GENE
AB Many ATP binding cassette (ABC) transporters are important regulators of lipid homeostasis and have been implicated in keratinocyte lipid transport. Ultraviolet (UV) light exposure is a known epidermal stressor, which amongst other effects causes lipid alterations and defective lamellar body biogenesis. To elucidate the background of these lipid changes we studied the effect of UVB light on ABC transporter expression. The effect of UVB treatment on the levels of 47 known human ABC transporter mRNAs was analyzed in normal human epidermal keratinocytes. Immunoblots and promoter assays were carried out for ABCA1 and ABCG1. The mRNA levels of cholesterol transport regulators ABCA1 and ABCG1 were markedly downregulated by UVB, parallel to the lamellar ichthyosis related glucosylceramide transporter ABCA12 and the suspected sphingosine-1-phosphate and cholesterol sulfate transporter ABCC1. The long but not the short alternative splice variant of the ABCF2 was found to be markedly upregulated rapidly after UVB irradiation. Immunoblot confirmed ABCA1 and ABCG1 protein downregulation, and luciferase assays showed suppression of their promoters by UVB. These proteins mostly transport lipids, which account for the integrity of the epidermal barrier; therefore our findings on the UVB regulation of ABC transporters may explain the appearance of barrier dysfunction after UVB exposure. (C) 2012 Elsevier B.V. All rights reserved.
C1 [Marko, Lorant; Paragh, Gyoergy; Ugocsai, Peter; Boettcher, Alfred; Schling, Petra; Balogh, Attila; Tarabin, Victoria; Orso, Evelyn; Schmitz, Gerd] Univ Regensburg, Inst Clin Chem & Lab Med, D-93053 Regensburg, Germany.
   [Marko, Lorant; Balogh, Attila; Remenyik, Eva] Univ Debrecen, Dept Dermatol & Venereol, H-4012 Debrecen, Hungary.
   [Paragh, Gyoergy; Wikonkal, Norbert] Semmelweis Univ, Dept Dermatol, H-1085 Budapest, Hungary.
   [Mandl, Jozsef] Semmelweis Univ, Dept Med Chem, H-1085 Budapest, Hungary.
   [Vogt, Thomas] Univ Regensburg, Dept Dermatol, D-93053 Regensburg, Germany.
C3 University of Regensburg; University of Debrecen; Semmelweis University;
   Semmelweis University; University of Regensburg
RP Schmitz, G (corresponding author), Univ Regensburg, Inst Clin Chem & Lab Med, Franz Josef Strauss Allee 11, D-93053 Regensburg, Germany.
EM gerd.schmitz@klinik.uni-regensburg.de
OI Schmitz, Gerd/0000-0002-1325-1007; Mandl, Jozsef/0009-0003-9163-1325
FU SFB Transregio-13 Project; Fraunhofer Project Group Regensburg;
   Evonik-Goldschmidt GmbH; EU
FX The authors are grateful to Harry Islinger, Manfred Haas and Birgit
   Wilhelm for their excellent technical help. We also grateful to Norbert
   E. Fusenig for providing us the HaCaT immortalized human keratinocyte
   cell line. This work was supported by grants from the SFB Transregio-13
   Project, the Fraunhofer Project Group Regensburg, the Evonik-Goldschmidt
   GmbH and the 7th Framework Program of the EU-funded "LipidomicNet"
   (Lipid droplets as dynamic organelles of fat deposition and release:
   translational research towards human) proposal number.
CR ABE T, 1979, CHEM PHARM BULL, V27, P458
   Akiyama M, 2005, J CLIN INVEST, V115, P1777, DOI 10.1172/JCI24834
   Akiyama M, 2008, EXP DERMATOL, V17, P373, DOI 10.1111/j.1600-0625.2007.00691.x
   Akiyama M, 2011, DERM-ENDOCRINOL, V3, P107, DOI 10.4161/derm.3.2.15136
   Bakos E, 2007, PFLUG ARCH EUR J PHY, V453, P621, DOI 10.1007/s00424-006-0160-8
   Baldán A, 2006, CURR OPIN LIPIDOL, V17, P227, DOI 10.1097/01.mol.0000226113.89812.bb
   Balogh A, 2008, J PHOTOCH PHOTOBIO B, V93, P133, DOI 10.1016/j.jphotobiol.2008.07.010
   Bebes A, 2012, ARCH DERMATOL RES, V304, P57, DOI 10.1007/s00403-011-1174-4
   Bebes A, 2011, J PHOTOCH PHOTOBIO B, V105, P162, DOI 10.1016/j.jphotobiol.2011.08.007
   Berton TR, 2005, ONCOGENE, V24, P2449, DOI 10.1038/sj.onc.1208462
   Braff MH, 2005, J INVEST DERMATOL, V124, P394, DOI 10.1111/j.0022-202X.2004.23443.x
   Brash DE, 1997, TRENDS GENET, V13, P410, DOI 10.1016/S0168-9525(97)01246-8
   Canguilhem B, 2005, J BIOL CHEM, V280, P43257, DOI 10.1074/jbc.M508650200
   Cao C, 2009, J CELL PHYSIOL, V220, P277, DOI 10.1002/jcp.21780
   Dean M, 2001, GENOME RES, V11, P1156, DOI 10.1101/gr.GR-1649R
   Dumitriu IE, 2004, CELL DEATH DIFFER, V11, P314, DOI 10.1038/sj.cdd.4401348
   Duval C, 2001, PIGM CELL RES, V14, P348, DOI 10.1034/j.1600-0749.2001.140506.x
   Elias PM, 2004, J INVEST DERMATOL, V122, P314, DOI 10.1046/j.1523-1747.2003.22258.x
   Fears TR, 2002, CANCER RES, V62, P3992
   Feingold KR, 2007, J LIPID RES, V48, P2531, DOI 10.1194/jlr.R700013-JLR200
   Feingold KR, 2009, J LIPID RES, V50, pS417, DOI 10.1194/jlr.R800039-JLR200
   FUCHS E, 1990, J CELL BIOL, V111, P2807, DOI 10.1083/jcb.111.6.2807
   Gambichler T, 2005, J AM ACAD DERMATOL, V52, P660, DOI 10.1016/j.jaad.2004.08.047
   GRUBAUER G, 1989, J LIPID RES, V30, P89
   Hamanaka S, 2005, BRIT J DERMATOL, V152, P426, DOI 10.1111/J.1365-2133.2004.06333.X
   Haratake A, 1997, J INVEST DERMATOL, V108, P769, DOI 10.1111/1523-1747.ep12292163
   Helmerl S, 2007, MELANOMA RES, V17, P265, DOI 10.1097/CMR.0b013e3282a7e0b9
   Herget M, 2007, PFLUG ARCH EUR J PHY, V453, P591, DOI 10.1007/s00424-006-0083-4
   Holleran WM, 1997, PHOTODERMATOL PHOTO, V13, P117, DOI 10.1111/j.1600-0781.1997.tb00214.x
   Hovnanian A, 2005, J CLIN INVEST, V115, P1708, DOI 10.1172/JCI25736
   Hu Z, 2000, J BIOL CHEM, V275, P2979, DOI 10.1074/jbc.275.4.2979
   Ibuki Y, 2001, PHOTOCHEM PHOTOBIOL, V73, P513, DOI 10.1562/0031-8655(2001)073<0513:UIIEIP>2.0.CO;2
   Ishida-Yamamoto A, 2004, J INVEST DERMATOL, V122, P1137, DOI 10.1111/j.0022-202X.2004.22515.x
   Jessup W, 2006, CURR OPIN LIPIDOL, V17, P247, DOI 10.1097/01.mol.0000226116.35555.eb
   Jiang SJ, 2007, EXP DERMATOL, V16, P985, DOI 10.1111/j.1600-0625.2007.00619.x
   Jiang SJ, 2006, J DERMATOL SCI, V44, P29, DOI 10.1016/j.jdermsci.2006.05.012
   Jiang YJ, 2008, J INVEST DERMATOL, V128, P104, DOI 10.1038/sj.jid.5700944
   Kennedy MA, 2001, J BIOL CHEM, V276, P39438, DOI 10.1074/jbc.M105863200
   Kennedy MA, 2005, CELL METAB, V1, P121, DOI 10.1016/j.cmet.2005.01.002
   Kielar D, 2003, J INVEST DERMATOL, V121, P465, DOI 10.1046/j.1523-1747.2003.12404.x
   Kolly C, 2005, J INVEST DERMATOL, V124, P1014, DOI 10.1111/j.0022-202X.2005.23655.x
   Langmann T, 2000, BBA-GENE STRUCT EXPR, V1494, P175, DOI 10.1016/S0167-4781(00)00215-3
   Langmann T, 2003, CLIN CHEM, V49, P230, DOI 10.1373/49.2.230
   Lewis GF, 2005, CIRC RES, V96, P1221, DOI 10.1161/01.RES.0000170946.56981.5c
   Li Q, 2005, PHARM RES-DORDR, V22, P842, DOI 10.1007/s11095-005-4576-1
   Madison KC, 2003, J INVEST DERMATOL, V121, P231, DOI 10.1046/j.1523-1747.2003.12359.x
   Madson JG, 2007, MOL CARCINOGEN, V46, P624, DOI 10.1002/mc.20335
   MAN MQ, 1993, J INVEST DERMATOL, V101, P185, DOI 10.1111/1523-1747.ep12363729
   Meguro S, 1999, PHOTOCHEM PHOTOBIOL, V69, P317, DOI 10.1562/0031-8655(1999)069<0317:CAIUIS>2.3.CO;2
   Meguro S, 2000, ARCH DERMATOL RES, V292, P463, DOI 10.1007/s004030000160
   MING ME, 1994, J INVEST DERMATOL, V103, P780, DOI 10.1111/1523-1747.ep12413024
   Mitra P, 2006, P NATL ACAD SCI USA, V103, P16394, DOI 10.1073/pnas.0603734103
   Miyake A, 2008, DEV GROWTH DIFFER, V50, P703, DOI 10.1111/j.1440-169X.2008.01068.x
   Nishimura S, 2008, BRIT J CANCER, V99, P1651, DOI 10.1038/sj.bjc.6604734
   Ogawa Y, 2006, ANTICANCER RES, V26, P1809
   Oji V, 2010, J AM ACAD DERMATOL, V63, P607, DOI 10.1016/j.jaad.2009.11.020
   Proksch E, 2008, EXP DERMATOL, V17, P1063, DOI 10.1111/j.1600-0625.2008.00786.x
   Sakai K, 2007, EXP DERMATOL, V16, P920, DOI 10.1111/j.1600-0625.2007.00614.x
   Sasaki H, 2005, PHOTODERMATOL PHOTO, V21, P9, DOI 10.1111/j.1600-0781.2005.00117.x
   Schmitz G, 2005, BBA-MOL CELL BIOL L, V1735, P1, DOI 10.1016/j.bbalip.2005.04.004
   Schmitz G, 2001, FRONT BIOSCI, V6, pD505, DOI 10.2741/Schmitz
   Schmuth M, 2008, J LIPID RES, V49, P499, DOI 10.1194/jlr.R800001-JLR200
   SCHURER NY, 1991, ADV LIPID RES, V24, P27
   Takagi Y, 2004, J INVEST DERMATOL, V123, P1102, DOI 10.1111/j.0022-202X.2004.23491.x
   Wenzel JJ, 2007, FRONT BIOSCI-LANDMRK, V12, P3177, DOI 10.2741/2305
   Wunderlich L, 2008, EXP DERMATOL, V17, P335, DOI 10.1111/j.1600-0625.2007.00640.x
   Yamanaka Y, 2007, AM J PATHOL, V171, P43, DOI 10.2353/ajpath.2007.061207
   Zhang WG, 2001, P NATL ACAD SCI USA, V98, P13948, DOI 10.1073/pnas.241353198
   Zuo Y, 2008, J BIOL CHEM, V283, P36624, DOI 10.1074/jbc.M807377200
   Zutz A, 2009, BBA-BIOENERGETICS, V1787, P681, DOI 10.1016/j.bbabio.2009.02.009
NR 70
TC 10
Z9 10
U1 0
U2 13
PU ELSEVIER SCIENCE SA
PI LAUSANNE
PA PO BOX 564, 1001 LAUSANNE, SWITZERLAND
SN 1011-1344
J9 J PHOTOCH PHOTOBIO B
JI J. Photochem. Photobiol. B-Biol.
PD NOV 5
PY 2012
VL 116
BP 79
EP 88
DI 10.1016/j.jphotobiol.2012.06.007
PG 10
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA 022VD
UT WOS:000309991000011
PM 22982209
DA 2025-04-10
ER

PT J
AU Lundquist, P
   Lundgren, T
   Gritli-Linde, A
   Linde, A
AF Lundquist, P
   Lundgren, T
   Gritli-Linde, A
   Linde, A
TI Na<SUP>+</SUP>/Ca<SUP>2+</SUP> exchanger isoforms of rat odontoblasts
   and osteoblasts
SO CALCIFIED TISSUE INTERNATIONAL
LA English
DT Article
DE odontoblasts; osteoblasts; sodium-calcium exchanger; alternative
   splicing; mineralization
ID CARDIAC NA+-CA2+ EXCHANGER; SODIUM-CALCIUM EXCHANGE; FUNCTIONAL
   EXPRESSION; INCISOR ODONTOBLASTS; PLASMA-MEMBRANE; CELLS; CLONING;
   DENTINOGENESIS; NIFEDIPINE; TRANSPORT
AB In odontoblasts as well as osteoblasts, a number of mechanisms for the inflow and extrusion of Ca2+ have been demonstrated. The entrance of Ca2+ ions into odontoblasts occurs mainly through voltage-gated calcium channels. Extrusion of Ca2+ is found to be an ATP-dependent process and, in addition, Na+/Ca2+-antiports exist, which are provoked by extracellular Na+. The aim of this study was to identify the Na+/Ca2+-antiport isoforms expressed in dentinogenically active rat incisor odontoblasts and to make a comparison with different osteoblastic cells. Using RT-PCR and RNAse protection assay, we demonstrated the expression of three different isoforms, NaCa 3, 7, and 10, of the NCX1-encoded antiport in odontoblasts and osteoblastic cells. When incubated in the presence of Na+, dissected rat incisor odontoblasts as well as the osteoblastic cells extruded Ca2+ ions, as detected by chlorotetracycline and Fura-2 fluorometry, thus supporting a physiological role for the detected isoform expression. Odontoblasts and rat calvarial osteoblasts, as well as osteoblast-like cell lines UMR106.01 and Saos-2, were shown to exhibit identical phenotypes of Na+/Ca2+-antiport isoform expression, different from the expression patterns of other tissues. The significance of this specific expression pattern is unknown, but there is a possibility that it is in some way related to the unique demands on these cell types to produce mineralized connective tissue.
C1 Univ Gothenburg, Dept Oral Biochem, SE-40530 Gothenburg, Sweden.
C3 University of Gothenburg
RP Univ Gothenburg, Dept Oral Biochem, Box 450, SE-40530 Gothenburg, Sweden.
OI Lundgren, Ted/0000-0002-1985-2524
CR ANTKIEWICZMICHALUK L, 1994, EUR J PHARMACOL, V254, P9, DOI 10.1016/0014-2999(94)90363-8
   Bishop M A, 1992, Proc Finn Dent Soc, V88 Suppl 1, P331
   BISHOP MA, 1992, J ANAT, V181, P29
   CHIN TK, 1993, CIRC RES, V72, P497, DOI 10.1161/01.RES.72.3.497
   DURIEZ J, 1993, CALCIFIED TISSUE INT, V52, P120, DOI 10.1007/BF00308320
   GABELLINI N, 1995, J BIOL CHEM, V270, P6917, DOI 10.1074/jbc.270.12.6917
   GRANSTROM G, 1981, CALCIFIED TISSUE INT, V33, P125, DOI 10.1007/BF02409424
   GRAY C, 1992, J BONE MINER RES, V7, P41
   GRYNKIEWICZ G, 1985, J BIOL CHEM, V260, P3440
   HARA Y, 1995, BRIT J PHARMACOL, V116, P2750, DOI 10.1111/j.1476-5381.1995.tb17237.x
   HOHLING HJ, 1984, DENTIN DENTINOGENESI, V2, P1
   JY W, 1984, CIRC RES, V55, P595, DOI 10.1161/01.RES.55.5.595
   KOFUJI P, 1994, J BIOL CHEM, V269, P5145
   KOFUJI P, 1992, AM J PHYSIOL, V263, pC1241, DOI 10.1152/ajpcell.1992.263.6.C1241
   LEE SL, 1994, J BIOL CHEM, V269, P14849
   Levitsky DO, 1996, MOL CELL BIOCHEM, V161, P27, DOI 10.1007/BF00240027
   LI ZP, 1993, J BIOL CHEM, V268, P11489
   LI ZP, 1994, J BIOL CHEM, V269, P17434
   LINDE A, 1972, ARCH ORAL BIOL, V17, P1209, DOI 10.1016/0003-9969(72)90091-X
   LINDE A, 1995, INT J DEV BIOL, V39, P213
   LOO TW, 1994, AM J PHYSIOL, V267, pF70, DOI 10.1152/ajprenal.1994.267.1.F70
   LUNDGREN T, 1992, CALCIFIED TISSUE INT, V50, P134, DOI 10.1007/BF00298790
   LUNDGREN T, 1988, J ORAL PATHOL MED, V17, P560, DOI 10.1111/j.1600-0714.1988.tb01334.x
   Lundgren T, 1997, CALCIFIED TISSUE INT, V60, P79, DOI 10.1007/s002239900189
   LUNDGREN T, 1992, BONE MINER, V19, P31, DOI 10.1016/0169-6009(92)90842-2
   LYU RM, 1991, J MEMBRANE BIOL, V124, P73, DOI 10.1007/BF01871366
   Matsuoka S, 1997, J GEN PHYSIOL, V109, P273, DOI 10.1085/jgp.109.2.273
   MATSUOKA S, 1993, P NATL ACAD SCI USA, V90, P3870, DOI 10.1073/pnas.90.9.3870
   MORAN D, 1983, J EXP ZOOL, V226, P475, DOI 10.1002/jez.1402260319
   Nicoll DA, 1996, J BIOL CHEM, V271, P24914, DOI 10.1074/jbc.271.40.24914
   NICOLL DA, 1990, SCIENCE, V250, P562, DOI 10.1126/science.1700476
   Quednau BD, 1997, AM J PHYSIOL-CELL PH, V272, pC1250, DOI 10.1152/ajpcell.1997.272.4.C1250
   Stains JP, 1998, J BONE MINER RES, V13, P1862, DOI 10.1359/jbmr.1998.13.12.1862
   Thomas A.P., 1991, CELLULAR CALCIUM, P1
   Wada Y, 1998, BONE, V22, P479, DOI 10.1016/S8756-3282(98)00039-8
   WHITE JR, 1983, ANAL BIOCHEM, V132, P1, DOI 10.1016/0003-2697(83)90417-7
   White KE, 1996, J BONE MINER RES, V11, P1666
NR 37
TC 17
Z9 20
U1 0
U2 3
PU SPRINGER
PI NEW YORK
PA 233 SPRING ST, NEW YORK, NY 10013 USA
SN 0171-967X
EI 1432-0827
J9 CALCIFIED TISSUE INT
JI Calcif. Tissue Int.
PD JUL
PY 2000
VL 67
IS 1
BP 60
EP 67
DI 10.1007/s00223001098
PG 8
WC Endocrinology & Metabolism
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism
GA 330LC
UT WOS:000087962700012
PM 10908415
DA 2025-04-10
ER

PT J
AU Wang, JX
   Zhao, WL
   Liu, H
   He, HW
   Shao, RG
AF Wang, Junxia
   Zhao, Wuli
   Liu, Hong
   He, Hongwei
   Shao, Rongguang
TI Myofibrillogenesis regulator 1 (MR-1): a potential therapeutic target
   for cancer and PNKD
SO JOURNAL OF DRUG TARGETING
LA English
DT Review
DE Myofibrillogenesis regulator 1; PNKD; cancer; proliferation; migration;
   differentiation
ID NON-KINESIGENIC DYSKINESIA; ANGIOTENSIN-II; SIGNALING PATHWAY;
   POOR-PROGNOSIS; HYPERTROPHY; PROLIFERATION; MIGRATION; CELLS;
   EXPRESSION; PROTEIN
AB Human myofibrillogenesis regulator 1 (MR-1) is a functional gene also known as paroxysmal nonkinesigenic dyskinesia (PNKD). It is localised on human chromosome 2q35 and three different isomers, MR-1L, MR-1M and MR-1S, are formed by alternative splicing. MR-1S promotes cardiac hypertrophy and is closely related to cancer. MR-1S is overexpressed in haematologic and solid malignancies, such as hepatoma, breast cancer and chronic myelogenous leukaemia. MR-1S causes disordered cell differentiation, initiates malignant transformation and accelerates metastasis. MR-1S directly phosphorylates and activates the MEK-ERK-RSK pathway to accelerate cancer growth and facilitates metastasis by activating the MLC2-FAK-AKT pathway. Silencing MR-1 inhibits cancer cell proliferation and metastasis. MR-1S causes disordered cell differentiation, initiates malignant transformation and accelerates metastasis. MR-1 interacts with eukaryotic translation initiation factors and MRIP-1, which contains Ras GTPase, PH and zinc-containing ArfGap domains, as well as three ankyrin repeats. Mutations in the N-terminal region of MR-1L and MR-1S are the main causes of PNKD (a hereditary disease characterised by paroxysmal dystonic choreoathetosis) and targeting the mutated protein could provide symptomatic relief. These findings provide compelling evidence that MR-1 might be a diagnostic marker and therapeutic target for solid tumours, myelogenous leukaemia and PNKD.
C1 Peking Union Med Coll, Inst Med Biotechnol, Lab Oncol, Minist Hlth,Key Lab Antibiot Bioengn, Beijing, Peoples R China.
   Chinese Acad Med Sci, Beijing, Peoples R China.
C3 Chinese Academy of Medical Sciences - Peking Union Medical College;
   Peking Union Medical College; Chinese Academy of Medical Sciences -
   Peking Union Medical College
RP Zhao, WL (corresponding author), Chinese Acad Med Sci, Key Lab Antibiot Bioengn, Minist Hlth, Lab Oncol,Inst Med Biotechnol, 1 Tiantan Xili, Beijing 100050, Peoples R China.; Shao, RG (corresponding author), Chinese Acad Med Sci, Inst Med Biotechnol, 1 Tiantan Xili, Beijing 100050, Peoples R China.
EM zwl21146@hotmail.com; rgshao@163.com
CR Bruno MK, 2007, NEUROLOGY, V68, P1782, DOI 10.1212/01.wnl.0000262029.91552.e0
   Calabretta B, 2004, BLOOD, V103, P4010, DOI 10.1182/blood-2003-12-4111
   Clemens MJ, 2000, CELL DEATH DIFFER, V7, P603, DOI 10.1038/sj.cdd.4400695
   Dai WJ, 2010, AM J PHYSIOL-HEART C, V299, pH1468, DOI 10.1152/ajpheart.00582.2009
   Dai WJ, 2010, BIOCHEM BIOPH RES CO, V391, P1573, DOI 10.1016/j.bbrc.2009.12.130
   Epstein JA, 2005, CIRCULATION, V112, P592, DOI 10.1161/CIRCULATIONAHA.104.479857
   Frey N, 2004, CIRCULATION, V109, P1580, DOI 10.1161/01.CIR.0000120390.68287.BB
   Gao M, 2017, ONCOL REP, V38, P2507, DOI 10.3892/or.2017.5915
   Ghezzi D, 2009, HUM MOL GENET, V18, P1058, DOI 10.1093/hmg/ddn441
   Gong YY, 2014, FEBS LETT, V588, P2903, DOI 10.1016/j.febslet.2014.07.018
   Guo J, 2012, WORLD J GASTROENTERO, V18, P5434, DOI 10.3748/wjg.v18.i38.5434
   Hochhaus A, 2008, ANN ONCOL, V19, P63, DOI 10.1093/annonc/mdn091
   Ichihara S, 2001, CIRCULATION, V104, P346, DOI 10.1161/01.CIR.104.3.346
   Lee HY, 2004, HUM MOL GENET, V13, P3161, DOI 10.1093/hmg/ddh330
   Li HL, 2007, HYPERTENSION, V49, P1399, DOI 10.1161/HYPERTENSIONAHA.106.085399
   Li TB, 2004, ACTA BIOCH BIOPH SIN, V36, P412, DOI 10.1093/abbs/36.6.412
   Liu XH, 2006, AM J PHYSIOL-HEART C, V290, pH279, DOI 10.1152/ajpheart.00247.2005
   Lu Ren-quan, 2012, Zhonghua Zhong Liu Za Zhi, V34, P176, DOI 10.3760/cma.j.issn.0253-3766.2012.03.004
   Lu RQ, 2011, BMC CANCER, V11, DOI 10.1186/1471-2407-11-270
   MCWHIRTER JR, 1993, MOL CELL BIOL, V13, P7587, DOI 10.1128/MCB.13.12.7587
   Nagao M, 1986, IARC Sci Publ, P283
   Owen JD, 1999, MOL CELL BIOL, V19, P4806
   Qiu WW, 2017, GENE, V633, P35, DOI 10.1016/j.gene.2017.08.024
   Ren KH, 2008, J BIOL CHEM, V283, P35598, DOI 10.1074/jbc.M802253200
   Sattler Martin, 1997, Cytokine and Growth Factor Reviews, V8, P63, DOI 10.1016/S1359-6101(96)00047-0
   Shen YG, 2011, HUM MOL GENET, V20, P2322, DOI 10.1093/hmg/ddr125
   Shimojima K, 2012, BRAIN DEV-JPN, V34, P230, DOI 10.1016/j.braindev.2011.04.014
   Sonoda Y, 1999, J BIOL CHEM, V274, P10566, DOI 10.1074/jbc.274.15.10566
   Wang CW, 2015, INT J CLIN EXP PATHO, V8, P14818
   WILSON AK, 1992, CANCER METAST REV, V11, P79, DOI 10.1007/BF00047605
   Zhao CY, 2013, TUMOR BIOL, V34, P2983, DOI 10.1007/s13277-013-0862-4
   Zhao W, 2013, BLOOD CANCER J, V3, DOI 10.1038/bcj.2013.5
   Zhao WL, 2013, CHINESE SCI BULL, V58, P3007, DOI 10.1007/s11434-013-5933-9
   Zolfaghari N, 2017, REPROD SCI, V24, P1438, DOI 10.1177/1933719116689596
NR 34
TC 9
Z9 12
U1 0
U2 3
PU TAYLOR & FRANCIS LTD
PI ABINGDON
PA 2-4 PARK SQUARE, MILTON PARK, ABINGDON OR14 4RN, OXON, ENGLAND
SN 1061-186X
EI 1029-2330
J9 J DRUG TARGET
JI J. Drug Target.
PY 2018
VL 26
IS 8
BP 643
EP 648
DI 10.1080/1061186X.2017.1401077
PG 6
WC Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Pharmacology & Pharmacy
GA GL2RO
UT WOS:000436972100003
PM 29103325
DA 2025-04-10
ER

PT J
AU Coers, J
   Ranft, C
   Skoda, RC
AF Coers, J
   Ranft, C
   Skoda, RC
TI A truncated isoform of c-Mpl with an essential C-terminal peptide
   targets the full-length receptor for degradation
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID COLONY-STIMULATING FACTOR; SOLUBLE CYTOKINE RECEPTORS;
   MOLECULAR-CLONING; ERYTHROPOIETIN RECEPTOR; TRANSGENIC MICE;
   ALPHA-SUBUNIT; EGF RECEPTOR; CELL-GROWTH; HALF-LIFE; PROTEIN
AB Thrombopoietin and its cognate receptor c-Mpl are the primary regulators of megakaryopoiesis and platelet production. They also play an important role in the maintenance of hematopoietic stem cells. Here, we have analyzed the function of a truncated Mpl receptor isoform (Mpl-tr), which results from alternative splicing. The mpl-tr variant is the only alternate mpl isoform conserved between mouse and humans, suggesting a relevant function in regulating Mpl signaling. Despite the presence of a signal peptide and the lack of a transmembrane domain, Mpl-tr is retained intracellularly. Our results provide evidence that Mpl-tr exerts a dominant-negative effect on thrombopoietin-dependent cell proliferation and survival. We demonstrate that this inhibitory effect is due to down-regulation of the full-length Mpl protein. The C terminus of Mpl-tr, consisting of 30 amino acids of unique sequence, is essential for the suppression of thrombopoietin-dependent proliferation and Mpl protein down-regulation. Cathepsin inhibitor-1 (CATI-1), an inhibitor of cathepsin-like cysteine proteases, counteracts the effect of Mpl-tr on Mpl protein expression, suggesting that Mpl-tr targets Mpl for lysosomal degradation. Together, these data suggest a new paradigm for the regulation of cytokine receptor expression and function through a proteolytic process directed by a truncated isoform of the same receptor.
C1 Univ Basel Hosp, Dept Res Expt Hematol, CH-4031 Basel, Switzerland.
C3 University of Basel
RP Univ Basel Hosp, Dept Res Expt Hematol, Hebelstr 20, CH-4031 Basel, Switzerland.
EM radek.skoda@unibas.ch
RI Coers, Jorn/LRT-1826-2024
OI Coers, Jorn/0000-0001-8707-4608
CR ADERKA D, 1992, J EXP MED, V175, P323, DOI 10.1084/jem.175.2.323
   AREND WP, 1994, J IMMUNOL, V153, P4766
   ARMSTRONG J, 1990, J CELL SCI, V95, P191
   Ashman LK, 1999, INT J BIOCHEM CELL B, V31, P1037, DOI 10.1016/S1357-2725(99)00076-X
   BASU A, 1989, MOL CELL BIOL, V9, P671, DOI 10.1128/MCB.9.2.671
   Bormann P, 1999, MOL CELL NEUROSCI, V13, P167, DOI 10.1006/mcne.1999.0742
   BROWN CB, 1995, BLOOD, V85, P1488, DOI 10.1182/blood.V85.6.1488.bloodjournal8561488
   CHANG A, 1995, J CELL BIOL, V128, P39, DOI 10.1083/jcb.128.1.39
   DALEY GQ, 1990, SCIENCE, V247, P824, DOI 10.1126/science.2406902
   EVAN GI, 1985, MOL CELL BIOL, V5, P3610, DOI 10.1128/MCB.5.12.3610
   FERNANDEZBOTRAN R, 1991, FASEB J, V5, P2567, DOI 10.1096/fasebj.5.11.1868981
   Ghilardi N, 2002, J BIOL CHEM, V277, P16831, DOI 10.1074/jbc.M201140200
   GURISH MF, 1992, J EXP MED, V175, P1003, DOI 10.1084/jem.175.4.1003
   HAYASHIDA K, 1990, P NATL ACAD SCI USA, V87, P9655, DOI 10.1073/pnas.87.24.9655
   Heaney ML, 1996, BLOOD, V87, P847, DOI 10.1182/blood.V87.3.847.bloodjournal873847
   Heaney ML, 1998, J LEUKOCYTE BIOL, V64, P135, DOI 10.1002/jlb.64.2.135
   HEANEY ML, 1995, P NATL ACAD SCI USA, V92, P2365, DOI 10.1073/pnas.92.6.2365
   Hofmann F, 1996, GENE DEV, V10, P2949, DOI 10.1101/gad.10.23.2949
   IHLE JN, 1995, NATURE, V377, P591, DOI 10.1038/377591a0
   Jones SA, 2001, FASEB J, V15, P43, DOI 10.1096/fj.99-1003rev
   Kaushansky K, 2002, ONCOGENE, V21, P3359, DOI 10.1038/sj.onc.1205323
   KOMATSU N, 1991, CANCER RES, V51, P341
   Kralovics R, 2003, BLOOD, V102, P1869, DOI 10.1182/blood-2003-03-0744
   Li JZ, 2000, CYTOKINE, V12, P835, DOI 10.1006/cyto.1999.0654
   Liu XD, 2000, ANAL BIOCHEM, V280, P20, DOI 10.1006/abio.2000.4478
   Livnah O, 1999, SCIENCE, V283, P987, DOI 10.1126/science.283.5404.987
   Longva KE, 2002, J CELL BIOL, V156, P843, DOI 10.1083/jcb.200106056
   MIGNOTTE V, 1994, GENOMICS, V20, P5, DOI 10.1006/geno.1994.1120
   Morishita E, 1996, BLOOD, V88, P465, DOI 10.1182/blood.V88.2.465.bloodjournal882465
   Nakamura Y, 1998, EXP HEMATOL, V26, P1105
   Ogata A, 1997, J IMMUNOL, V159, P2212
   PALACIOS R, 1985, CELL, V41, P727, DOI 10.1016/S0092-8674(85)80053-2
   Peters M, 1996, J EXP MED, V183, P1399, DOI 10.1084/jem.183.4.1399
   Roberts GC, 2002, CURR OPIN CHEM BIOL, V6, P375, DOI 10.1016/S1367-5931(02)00320-4
   Sabath DF, 2002, BBA-GENE STRUCT EXPR, V1574, P383, DOI 10.1016/S0167-4781(01)00357-8
   SKODA RC, 1993, EMBO J, V12, P2645, DOI 10.1002/j.1460-2075.1993.tb05925.x
   Slater NJ, 2003, BRIT J HAEMATOL, V122, P150, DOI 10.1046/j.1365-2141.2003.04383.x
   Stoffel R, 1996, BLOOD, V87, P567, DOI 10.1182/blood.V87.2.567.bloodjournal872567
   Tavernier J, 2000, BLOOD, V95, P1600, DOI 10.1182/blood.V95.5.1600.005k22_1600_1607
   TAVERNIER J, 1992, P NATL ACAD SCI USA, V89, P7041, DOI 10.1073/pnas.89.15.7041
   TSURUOKA N, 1993, ARCH BIOCHEM BIOPHYS, V307, P133, DOI 10.1006/abbi.1993.1571
   Vanslyke JK, 2000, MOL BIOL CELL, V11, P1933, DOI 10.1091/mbc.11.6.1933
   VELDHUIS JD, 1993, J CLIN INVEST, V91, P629, DOI 10.1172/JCI116243
   VIGON I, 1993, ONCOGENE, V8, P2607
   VIGON I, 1992, P NATL ACAD SCI USA, V89, P5640, DOI 10.1073/pnas.89.12.5640
   Wagner K, 2001, BLOOD, V98, P2689, DOI 10.1182/blood.V98.9.2689
   Wolins N, 1997, J CELL BIOL, V139, P1735, DOI 10.1083/jcb.139.7.1735
   Yu AX, 2001, J BIOL CHEM, V276, P381, DOI 10.1074/jbc.M007991200
NR 48
TC 16
Z9 20
U1 0
U2 4
PU AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
SN 0021-9258
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD AUG 27
PY 2004
VL 279
IS 35
BP 36397
EP 36404
DI 10.1074/jbc.M401386200
PG 8
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 848FS
UT WOS:000223453600030
PM 15210714
OA hybrid
DA 2025-04-10
ER

PT J
AU Kandoi, G
   Dickerson, JA
AF Kandoi, Gaurav
   Dickerson, Julie A.
TI Tissue-specific mouse mRNA isoform networks
SO SCIENTIFIC REPORTS
LA English
DT Article
ID CORONARY-HEART-DISEASE; HUMAN TRANSCRIPTOME; R PACKAGE; VITAMIN-E;
   EXPRESSION; ACID; COMPLEXITY; INHIBITION; RISK
AB Alternative Splicing produces multiple mRNA isoforms of genes which have important diverse roles such as regulation of gene expression, human heritable diseases, and response to environmental stresses. However, little has been done to assign functions at the mRNA isoform level. Functional networks, where the interactions are quantified by their probability of being involved in the same biological process are typically generated at the gene level. We use a diverse array of tissue-specific RNA-seq datasets and sequence information to train random forest models that predict the functional networks. Since there is no mRNA isoform-level gold standard, we use single isoform genes co-annotated to Gene Ontology biological process annotations, Kyoto Encyclopedia of Genes and Genomes pathways, BioCyc pathways and protein-protein interactions as functionally related (positive pair). To generate the nonfunctional pairs (negative pair), we use the Gene Ontology annotations tagged with "NOT" qualifier. We describe 17 Tissue-spEcific mrNa iSoform functIOnal Networks (TENSION) following a leave-one-tissue-out strategy in addition to an organism level reference functional network for mouse. We validate our predictions by comparing its performance with previous methods, randomized positive and negative class labels, updated Gene Ontology annotations, and by literature evidence. We demonstrate the ability of our networks to reveal tissue-specific functional differences of the isoforms of the same genes. All scripts and data from TENSION are available at: https://doi.org/10.25380/iastate.c.4275191.
C1 [Kandoi, Gaurav; Dickerson, Julie A.] Iowa State Univ, Bioinformat & Computat Biol Program, Ames, IA 50011 USA.
   [Kandoi, Gaurav; Dickerson, Julie A.] Iowa State Univ, Dept Elect & Comp Engn, Ames, IA 50011 USA.
C3 Iowa State University; Iowa State University
RP Dickerson, JA (corresponding author), Iowa State Univ, Bioinformat & Computat Biol Program, Ames, IA 50011 USA.; Dickerson, JA (corresponding author), Iowa State Univ, Dept Elect & Comp Engn, Ames, IA 50011 USA.
EM julied@iastate.edu
RI Kandoi, Gaurav/U-5245-2019
OI Kandoi, Gaurav/0000-0003-0559-9481; Dickerson, Julie
   A/0000-0003-4973-5641
FU National Science Foundation [IOS-1062546, ACI-1548562]
FX This material is based upon work supported by the National Science
   Foundation under Grant IOS-1062546. Any opinions, findings, and
   conclusions or recommendations expressed in this material are those of
   the author(s) and do not necessarily reflect the views of the National
   Science Foundation. This work used the Extreme Science and Engineering
   Discovery Environment (XSEDE), which is supported by National Science
   Foundation grant number ACI-1548562. This work used the XSEDE Comet
   cluster at San Diego Supercomputer Center (SDSC) through allocation
   TG-BIO170049. We would like to thank Dr. Mahidhar Tatineni and Dr.
   Martin Kandes from SDSC User Services group for providing technical
   support at Comet cluster. We also thank Megan O'Donnell and Levi Baber
   for setting up the data repository at DataShare: Iowa State University's
   Open Research Data Repository. We would also like to thank Dr. Yuanfang
   Guan and Dr. Hongdong Li for providing some data and the code for the
   comparison with Bayesian network-based MIL method.
CR Alonso-López D, 2016, NUCLEIC ACIDS RES, V44, pW529, DOI 10.1093/nar/gkw363
   [Anonymous], INT J MOL SCI
   BENJAMINI Y, 1995, J R STAT SOC B, V57, P289, DOI 10.1111/j.2517-6161.1995.tb02031.x
   Berthier CC, 2009, DIABETES, V58, P469, DOI 10.2337/db08-1328
   Breiman L., 2001, MACH LEARN, V45, P5, DOI 10.1023/A:1010933404324
   Brosius FC, 2015, CURR OPIN NEPHROL HY, V24, P88, DOI 10.1097/MNH.0000000000000079
   Buljan M, 2012, MOL CELL, V46, P871, DOI 10.1016/j.molcel.2012.05.039
   Calderone A, 2013, NAT METHODS, V10, P690, DOI 10.1038/nmeth.2561
   Chatr-aryamontri A, 2017, NUCLEIC ACIDS RES, V45, pD369, DOI 10.1093/nar/gkw1102
   Chen KF, 2012, BRIEF FUNCT GENOMICS, V11, P405, DOI 10.1093/bfgp/els038
   Chou KC, 2001, PROTEINS, V43, P246, DOI 10.1002/prot.1035
   Chuang PY, 2010, KIDNEY INT, V78, P231, DOI 10.1038/ki.2010.158
   Della Torre S, 2014, NAT REV ENDOCRINOL, V10, P13, DOI 10.1038/nrendo.2013.203
   Della Torre S, 2011, CELL METAB, V13, P205, DOI 10.1016/j.cmet.2011.01.002
   Dickerson J.A., 2019, Tissue-spEcific mrNa iSoform functIOnal Networks (TENSION) Collection, DOI [DOI 10.25380/IASTATE.C.4275191, 10.25380/iastate.c.4275191]
   Dobin A, 2013, BIOINFORMATICS, V29, P15, DOI 10.1093/bioinformatics/bts635
   Eksi R, 2013, PLOS COMPUT BIOL, V9, DOI 10.1371/journal.pcbi.1003314
   Ellis JD, 2012, MOL CELL, V46, P884, DOI 10.1016/j.molcel.2012.05.037
   Fontana R, 2016, NUTRIENTS, V8, DOI 10.3390/nu8020087
   García L, 2000, J ENDOCRINOL, V166, P381, DOI 10.1677/joe.0.1660381
   Kandoi G, 2015, FRONT PHYSIOL, V6, DOI 10.3389/fphys.2015.00366
   Kelemen O, 2013, GENE, V514, P1, DOI 10.1016/j.gene.2012.07.083
   Kohavi R., 1995, IJCAI-95. Proceedings of the Fourteenth International Joint Conference on Artificial Intelligence, P1137
   Kotlyar M, 2016, NUCLEIC ACIDS RES, V44, pD536, DOI 10.1093/nar/gkv1115
   Li B, 2017, SCI REP-UK, V7, DOI 10.1038/s41598-017-04520-z
   Li HD, 2015, J PROTEOME RES, V14, P3484, DOI 10.1021/acs.jproteome.5b00494
   Li HD, 2014, TRENDS GENET, V30, P340, DOI 10.1016/j.tig.2014.05.005
   Li HN, 2016, J CIV STRUCT HEALTH, V6, P3, DOI 10.1007/s13349-015-0108-9
   Li WY, 2014, NUCLEIC ACIDS RES, V42, DOI 10.1093/nar/gkt1362
   Liu RL, 2014, BMC BIOINFORMATICS, V15, DOI 10.1186/1471-2105-15-286
   Luo TJ, 2017, KDD'17: PROCEEDINGS OF THE 23RD ACM SIGKDD INTERNATIONAL CONFERENCE ON KNOWLEDGE DISCOVERY AND DATA MINING, P345, DOI 10.1145/3097983.3097984
   Marquez Y, 2012, GENOME RES, V22, P1184, DOI 10.1101/gr.134106.111
   MICHAEL SD, 1979, ARTHRITIS RHEUM, V22, P1241, DOI 10.1002/art.1780221111
   MORAN PAP, 1950, BIOMETRIKA, V37, P17, DOI 10.2307/2332142
   Nepusz T., 2006, INTERJ COMPLEX SYST, V1695, P1, DOI DOI 10.1234/EXAMPLE-DOI-5678
   Nezami Behtash Ghazi, 2010, Curr Gastroenterol Rep, V12, P358, DOI 10.1007/s11894-010-0129-9
   Oikonomopoulou K, 2012, SEMIN IMMUNOPATHOL, V34, P151, DOI 10.1007/s00281-011-0280-x
   Orchard S, 2014, NUCLEIC ACIDS RES, V42, pD358, DOI 10.1093/nar/gkt1115
   Pan Q, 2004, MOL CELL, V16, P929, DOI 10.1016/j.molcel.2004.12.004
   Pan Q, 2008, NAT GENET, V40, P1413, DOI 10.1038/ng.259
   Panwar B, 2016, J PROTEOME RES, V15, P1747, DOI 10.1021/acs.jproteome.5b00883
   Pedregosa F, 2011, J MACH LEARN RES, V12, P2825
   Pertea M, 2016, NAT PROTOC, V11, P1650, DOI 10.1038/nprot.2016.095
   R Core Team, 2017, R: A language and environment for statistical computing
   Radhakrishnan VM, 2015, J BIOL CHEM, V290, P8964, DOI 10.1074/jbc.M114.616516
   Raj B, 2015, NEURON, V87, P14, DOI 10.1016/j.neuron.2015.05.004
   Rao M, 2016, NAT REV GASTRO HEPAT, V13, DOI 10.1038/nrgastro.2016.107
   Resch A, 2004, J PROTEOME RES, V3, P76, DOI 10.1021/pr034064v
   Rimm EB, 1998, JAMA-J AM MED ASSOC, V279, P359, DOI 10.1001/jama.279.5.359
   RIMM EB, 1993, NEW ENGL J MED, V328, P1450, DOI 10.1056/NEJM199305203282004
   Said HM, 2006, CURR OPIN GASTROEN, V22, P140, DOI 10.1097/01.mog.0000203870.22706.52
   Schnyder G, 2002, JAMA-J AM MED ASSOC, V288, P973, DOI 10.1001/jama.288.8.973
   Shen JW, 2007, P NATL ACAD SCI USA, V104, P4337, DOI 10.1073/pnas.0607879104
   Söllner JF, 2017, SCI DATA, V4, DOI 10.1038/sdata.2017.185
   Stephens NG, 1996, LANCET, V347, P781, DOI 10.1016/S0140-6736(96)90866-1
   Sun Y, 2018, BMC PLANT BIOL, V18, DOI 10.1186/s12870-017-1217-x
   Suzuki H, 2011, PLOS ONE, V6, DOI 10.1371/journal.pone.0016880
   Towns J, 2014, COMPUT SCI ENG, V16, P62, DOI 10.1109/MCSE.2014.80
   Tseng YT, 2015, BMC GENOMICS, V16, DOI 10.1186/1471-2164-16-S2-S10
   Uhlen M, 2015, SCIENCE, V347, DOI 10.1126/science.1260419
   Vitulo N, 2014, BMC PLANT BIOL, V14, DOI 10.1186/1471-2229-14-99
   Wang JZ, 2007, BIOINFORMATICS, V23, P1274, DOI 10.1093/bioinformatics/btm087
   Wei B, 2016, GENE, V582, P1, DOI 10.1016/j.gene.2016.01.006
   Wood JD, 2016, DIGEST DIS SCI, V61, P1803, DOI 10.1007/s10620-016-4183-5
   Wu P, 2018, DNA RES, V25, P265, DOI 10.1093/dnares/dsx055
   Xiao N, 2015, BIOINFORMATICS, V31, P1857, DOI 10.1093/bioinformatics/btv042
   Xu Q, 2002, NUCLEIC ACIDS RES, V30, P3754, DOI 10.1093/nar/gkf492
   Yang NS, 2008, NEPHROL DIAL TRANSPL, V23, P91, DOI 10.1093/ndt/gfm509
   Yu GC, 2016, MOL BIOSYST, V12, P477, DOI 10.1039/c5mb00663e
   Yu GC, 2012, OMICS, V16, P284, DOI 10.1089/omi.2011.0118
   Yura K, 2006, GENE, V380, P63, DOI 10.1016/j.gene.2006.05.015
   Zhu M., 2016, rDNAse: Generating Various Numerical Representation Schemes of DNA Sequences
   Zittermann A, 2003, J AM COLL CARDIOL, V41, P105, DOI 10.1016/S0735-1097(02)02624-4
NR 73
TC 10
Z9 12
U1 0
U2 7
PU NATURE PORTFOLIO
PI BERLIN
PA HEIDELBERGER PLATZ 3, BERLIN, 14197, GERMANY
SN 2045-2322
J9 SCI REP-UK
JI Sci Rep
PD SEP 27
PY 2019
VL 9
AR 13949
DI 10.1038/s41598-019-50119-x
PG 24
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA JB0DW
UT WOS:000488222500001
PM 31562339
OA gold, Green Published, Green Submitted
DA 2025-04-10
ER

PT J
AU Hsieh, CM
   Fukumoto, S
   Layne, MD
   Maemura, K
   Charles, H
   Patel, A
   Perrella, MA
   Lee, ME
AF Hsieh, CM
   Fukumoto, S
   Layne, MD
   Maemura, K
   Charles, H
   Patel, A
   Perrella, MA
   Lee, ME
TI Striated muscle preferentially expressed genes α and β are two
   serine/threonine protein kinases derived from the same gene as the
   aortic preferentially expressed gene-1
SO JOURNAL OF BIOLOGICAL CHEMISTRY
LA English
DT Article
ID LIGHT-CHAIN KINASE; SMOOTH-MUSCLE; TRANSCRIPTION FACTORS; TELOKIN;
   DOMAIN; ADULT; INDUCTION; SEQUENCES; ISOFORMS; FAMILY
AB Aortic preferentially expressed gene (APEG)-1 is a 1.4-kilobase pair (kb) mRNA expressed in vascular smooth muscle cells and is down-regulated by vascular injury. An APEG-1 5'-end cDNA probe identified three additional isoforms. The 9-kb striated preferentially expressed gene (SPEG)alpha and the 11-kb SPEG beta were found in skeletal muscle and heart. The 4-kb brain preferentially expressed gene was detected in the brain and aorta. We report here cloning of the Il-kb SPEG beta cDNA SPEG beta encodes a 355-kDa protein that contains two serine/threonine kinase domains and is homologous to proteins of the myosin light chain kinase family. At least one Kinase domain is active and capable of autophosphorylation. In the genome, all four isoforms share the middle three of the five exons of APEG-1, and they differ from each other by using different 5'- and S'-ends and alternative splicing. We show that the expression of SPEG alpha and SPEG beta is developmentally regulated in the striated muscle during C2C12 myoblast to myotube differentiation in vitro and cardiomyocyte maturation in vivo. This developmental regulation suggests that both SPEG alpha and SPEG beta can serve as sensitive markers for striated muscle differentiation and that they may be important for adult striated muscle function.
C1 Brigham & Womens Hosp, Div Cardiovasc, Program Dev Cardiovasc Biol, Boston, MA 02115 USA.
   Brigham & Womens Hosp, Pulm & Crit Care Div, Boston, MA 02115 USA.
   Harvard Univ, Sch Med, Dept Med, Boston, MA 02115 USA.
C3 Harvard University; Harvard University Medical Affiliates; Brigham &
   Women's Hospital; Harvard University; Harvard University Medical
   Affiliates; Brigham & Women's Hospital; Harvard University; Harvard
   Medical School
RP Brigham & Womens Hosp, Div Cardiovasc, Program Dev Cardiovasc Biol, 75 Francis St, Boston, MA 02115 USA.
EM mperrella@rics.bwh.harvard.edu
OI Layne, Matthew/0000-0003-0007-4870
CR ANDERSON PAW, 1995, CIRC RES, V76, P681, DOI 10.1161/01.RES.76.4.681
   Bateman A, 2004, NUCLEIC ACIDS RES, V32, pD138, DOI [10.1093/nar/gkr1065, 10.1093/nar/gkp985, 10.1093/nar/gkh121]
   BREATHNACH R, 1981, ANNU REV BIOCHEM, V50, P349, DOI 10.1146/annurev.bi.50.070181.002025
   Chin MT, 2000, J BIOL CHEM, V275, P6381, DOI 10.1074/jbc.275.9.6381
   Chin MT, 1999, J MOL CELL CARDIOL, V31, P2199, DOI 10.1006/jmcc.1999.1054
   CLAYCOMB WC, 1992, TRENDS CARDIOVAS MED, V2, P231, DOI 10.1016/1050-1738(92)90030-V
   Corpet F, 2000, NUCLEIC ACIDS RES, V28, P267, DOI 10.1093/nar/28.1.267
   EPSTEIN HF, 1991, SCIENCE, V251, P1039, DOI 10.1126/science.1998120
   ERICKSONVIITANEN S, 1987, METHOD ENZYMOL, V139, P455
   Franke TF, 1997, SCIENCE, V275, P665, DOI 10.1126/science.275.5300.665
   GALLAGHER PJ, 1991, J BIOL CHEM, V266, P23945
   Gittenberger-de Groot AC, 1999, ARTERIOSCL THROM VAS, V19, P1589
   HANKS SK, 1991, METHOD ENZYMOL, V200, P38
   HANKS SK, 1988, SCIENCE, V241, P42, DOI 10.1126/science.3291115
   Hofmann K, 1999, NUCLEIC ACIDS RES, V27, P215, DOI 10.1093/nar/27.1.215
   HOLDEN HM, 1992, J MOL BIOL, V227, P840, DOI 10.1016/0022-2836(92)90226-A
   Hsieh CM, 1999, J BIOL CHEM, V274, P14344, DOI 10.1074/jbc.274.20.14344
   Hsieh CM, 1996, J BIOL CHEM, V271, P17354, DOI 10.1074/jbc.271.29.17354
   IZUMO S, 1988, P NATL ACAD SCI USA, V85, P339, DOI 10.1073/pnas.85.2.339
   KEMP BE, 1994, PROTEIN KINASES, P30
   Maruyama K, 1997, FASEB J, V11, P341, DOI 10.1096/fasebj.11.5.9141500
   Mende U, 1998, P NATL ACAD SCI USA, V95, P13893, DOI 10.1073/pnas.95.23.13893
   Molkentin JD, 1996, CURR OPIN GENET DEV, V6, P445, DOI 10.1016/S0959-437X(96)80066-9
   Nagase T, 2000, DNA RES, V7, P65, DOI 10.1093/dnares/7.1.65
   NAUMANN K, 1994, DIFFERENTIATION, V55, P203, DOI 10.1046/j.1432-0436.1994.5530203.x
   Nieznanski K, 1997, BIOCHEM J, V322, P65, DOI 10.1042/bj3220065
   Ota S, 2000, J BIOL CHEM, V275, P414, DOI 10.1074/jbc.275.1.414
   OWENS GK, 1995, PHYSIOL REV, V75, P487
   PARKER TG, 1991, ANNU REV PHYSIOL, V53, P179
   ROSS R, 1993, NATURE, V362, P801, DOI 10.1038/362801a0
   RUDNICKI MA, 1995, BIOESSAYS, V17, P203, DOI 10.1002/bies.950170306
   Rumyantsev P P, 1977, Int Rev Cytol, V51, P186
   Sanjo H, 1998, J BIOL CHEM, V273, P29066, DOI 10.1074/jbc.273.44.29066
   Schiaffino S, 1996, PHYSIOL REV, V76, P371, DOI 10.1152/physrev.1996.76.2.371
   SCHWARTZ K, 1986, CIRC RES, V59, P551, DOI 10.1161/01.RES.59.5.551
   Wu XQ, 1998, J BIOL CHEM, V273, P11362, DOI 10.1074/jbc.273.18.11362
   YOSHIZUMI M, 1995, J CLIN INVEST, V95, P2275, DOI 10.1172/JCI117918
NR 37
TC 55
Z9 65
U1 0
U2 4
PU ELSEVIER
PI AMSTERDAM
PA RADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
EI 1083-351X
J9 J BIOL CHEM
JI J. Biol. Chem.
PD NOV 24
PY 2000
VL 275
IS 47
BP 36966
EP 36973
DI 10.1074/jbc.M006028200
PG 8
WC Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA 378GY
UT WOS:000165577700073
PM 10973969
OA hybrid
DA 2025-04-10
ER

PT J
AU McLean, J
   Liu, HN
   Miletic, D
   Weng, YC
   Rogaeva, E
   Zinman, L
   Kriz, J
   Robertson, J
AF McLean, Jesse
   Liu, Hsueh-Ning
   Miletic, Denise
   Weng, Yuan Cheng
   Rogaeva, Ekaterina
   Zinman, Lorne
   Kriz, Jasna
   Robertson, Janice
TI Distinct biochemical signatures characterize peripherin isoform
   expression in both traumatic neuronal injury and motor neuron disease
SO JOURNAL OF NEUROCHEMISTRY
LA English
DT Article
DE alternative splicing; amyotrophic lateral sclerosis; inclusion;
   intermediate filament; sciatic crush; stroke
ID AMYOTROPHIC-LATERAL-SCLEROSIS; INTERMEDIATE-FILAMENT PROTEIN;
   NEUROFILAMENT HEAVY GENE; TRANSGENIC MOUSE MODEL; SUPEROXIDE-DISMUTASE;
   NERVOUS-SYSTEM; FAMILIAL ALS; DIFFERENTIAL EXPRESSION;
   CEREBRAL-ISCHEMIA; B-LYMPHOCYTES
AB Peripherin is a type Ill intermediate filament protein that is up-regulated during neuronal injury and is a major component of pathological inclusions found within degenerating motor neurons of patients with amyotrophic lateral sclerosis (ALS). The relationship between these inclusions and their protein constituents remains largely unknown. We have previously shown that peripherin expression is characterized by tissue-specific, intra-isoform associations that contribute to filament structure; changes to the normal isoform expression pattern is associated with malformed filaments and intracellular inclusions. Here, we profile peripherin isoform expression and ratio changes in traumatic neuronal injury, transgenic mouse models of motor neuron disease, and ALS. Extensive western blot analyses of Triton X-100 soluble and insoluble fractions of neuronal tissue from these conditions revealed significant changes in peripherin isoform content which could be differentiated by electrophoretic banding patterns to produce distinct peripherin biochemical signatures. Significantly, we found that the pattern of peripherin expression in ALS most closely approximates that of peripherin over-expressing mice, but differs with regard to inter-individual variations in isoform-specific expression. Overall, these results provide important insights into complex post-transcriptional processes that may underlie a continuum between peripherin-mediated neuronal repair and its role in the pathogenesis of motor neuron disease.
C1 [McLean, Jesse; Liu, Hsueh-Ning; Miletic, Denise; Rogaeva, Ekaterina; Robertson, Janice] Univ Toronto, Ctr Res Neurodegenerat Dis, Toronto, ON M5S 3H2, Canada.
   [McLean, Jesse; Robertson, Janice] Univ Toronto, Dept Lab Med & Pathol, Toronto, ON, Canada.
   [Weng, Yuan Cheng; Kriz, Jasna] Univ Laval, Dept Anat & Physiol, Ctr Rech, CHU Laval, Quebec City, PQ G1K 7P4, Canada.
   [Zinman, Lorne] Sunnybrook Hlth Sci Ctr, ALS Neuromuscular Clin, Toronto, ON M4N 3M5, Canada.
C3 University of Toronto; University of Toronto; Laval University; Laval
   University Hospital; University of Toronto; Sunnybrook Health Science
   Center; Sunnybrook Research Institute
RP Robertson, J (corresponding author), Univ Toronto, Ctr Res Neurodegenerat Dis, 6 Queens Pk Crescent W, Toronto, ON M5S 3H2, Canada.
EM jan.robertson@utoronto.ca
OI Kriz, Jasna/0000-0002-1811-7456
FU R&D/Health Research Foundation; Canadian Institutes of Health Research;
   ALS Society of Canada; American ALS Association; UK Motor Neurone
   Disease Association; Muscular Dystrophy Association; Natural Sciences
   and Engineering Research Council of Canada
FX The authors wish to thank Dr. Kate Banks (University of Toronto.
   Toronto, ON, Canada) for surgical demonstrations. JR is a Canada
   Research Chair in the Molecular Mechanisms of ALS. JK is the recipient
   of the Career Award from the R&D/Health Research Foundation. This work
   was supported by grants from the Canadian Institutes of Health Research
   (to J.R. and J.K.), the ALS Society of Canada, the American ALS
   Association, the UK Motor Neurone Disease Association, the Muscular
   Dystrophy Association (to J.R.), and the Natural Sciences and
   Engineering Research Council of Canada (to J.M.).
CR ALETTA JM, 1989, J BIOL CHEM, V264, P4619
   Alexianu ME, 2001, NEUROLOGY, V57, P1282, DOI 10.1212/WNL.57.7.1282
   AlvarezGago T, 1996, HISTOPATHOLOGY, V28, P349, DOI 10.1046/j.1365-2559.1996.d01-434.x
   Anthony K, 2010, BRAIN RES, V1338, P67, DOI 10.1016/j.brainres.2010.03.008
   Athlan ES, 1997, J NEUROSCI RES, V47, P300
   BAUDOIN C, 1993, CANCER RES, V53, P1175
   Beaulieu JM, 2002, BRAIN RES, V946, P153, DOI 10.1016/S0006-8993(02)02830-5
   Beaulieu JM, 1999, BIOCHEM CELL BIOL, V77, P41, DOI 10.1139/bcb-77-1-41
   Beaulieu JM, 1999, J CELL BIOL, V147, P531, DOI 10.1083/jcb.147.3.531
   Belayev L, 1999, BRAIN RES, V833, P181, DOI 10.1016/S0006-8993(99)01528-0
   BERGERON C, 1994, J NEUROPATH EXP NEUR, V53, P221, DOI 10.1097/00005072-199405000-00002
   BOITARD C, 1992, P NATL ACAD SCI USA, V89, P172, DOI 10.1073/pnas.89.1.172
   BRODY BA, 1989, J NEUROSCI, V9, P2391
   Brooks BR, 2000, AMYOTROPH LATERAL SC, V1, P293, DOI 10.1080/146608200300079536
   Bruijn LI, 1997, NEURON, V18, P327, DOI 10.1016/S0896-6273(00)80272-X
   Buée L, 1999, BRAIN PATHOL, V9, P681
   Cairns NJ, 2007, ACTA NEUROPATHOL, V114, P5, DOI 10.1007/s00401-007-0237-2
   Carrillo J, 2008, MOL IMMUNOL, V45, P3152, DOI 10.1016/j.molimm.2008.03.003
   CHADAN S, 1994, J NEUROCHEM, V62, P1894
   COLLARD JF, 1995, NATURE, V375, P61, DOI 10.1038/375061a0
   CORBO M, 1992, J NEUROPATH EXP NEUR, V51, P531, DOI 10.1097/00005072-199209000-00008
   Corrado L, 2011, NEUROBIOL AGING, V32, DOI 10.1016/j.neurobiolaging.2010.02.011
   COTE F, 1993, CELL, V73, P35, DOI 10.1016/0092-8674(93)90158-M
   CUI CQ, 1995, J CELL SCI, V108, P3279
   EAKER EY, 1994, GASTROENTEROLOGY, V107, P666, DOI 10.1016/0016-5085(94)90113-9
   Elder GA, 1999, J CELL BIOL, V146, P181
   Elliott JL, 2001, MOL BRAIN RES, V95, P172, DOI 10.1016/S0169-328X(01)00242-X
   ESCURAT M, 1990, J NEUROSCI, V10, P764
   FOLEY J, 1994, LAB INVEST, V71, P193
   Ganns D, 2006, HISTOL HISTOPATHOL, V21, P41, DOI 10.14670/HH-21.41
   Goldman RD, 2008, CURR OPIN CELL BIOL, V20, P28, DOI 10.1016/j.ceb.2007.11.003
   Gros-Louis F, 2004, J BIOL CHEM, V279, P45951, DOI 10.1074/jbc.M408139200
   GURNEY ME, 1994, SCIENCE, V264, P1772, DOI 10.1126/science.8209258
   Hall ED, 1998, GLIA, V23, P249, DOI 10.1002/(SICI)1098-1136(199807)23:3<249::AID-GLIA7>3.0.CO;2-#
   He CZ, 2004, J NEUROL SCI, V217, P47, DOI 10.1016/j.jns.2003.08.016
   Hensley K, 2003, NEUROBIOL DIS, V14, P74, DOI 10.1016/S0969-9961(03)00087-1
   Herrmann H, 2007, NAT REV MOL CELL BIO, V8, P562, DOI 10.1038/nrm2197
   Ho CL, 1996, CANCER METAST REV, V15, P483, DOI 10.1007/BF00054014
   HUC C, 1989, BIOCHEM BIOPH RES CO, V160, P772, DOI 10.1016/0006-291X(89)92500-X
   Kanitakis J, 1998, EUR J DERMATOL, V8, P339
   KAWAMATA T, 1992, AM J PATHOL, V140, P691
   Konishi H, 2007, J BIOL CHEM, V282, P23491, DOI 10.1074/jbc.M611703200
   Kriz J, 2000, EXP NEUROL, V163, P414, DOI 10.1006/exnr.2000.7378
   Lalancette-Hébert M, 2007, J NEUROSCI, V27, P2596, DOI 10.1523/JNEUROSCI.5360-06.2007
   LAMPSON LA, 1990, ANN NEUROL, V28, P365, DOI 10.1002/ana.410280311
   Landon F, 2000, BIOL CELL, V92, P397, DOI 10.1016/S0248-4900(00)01099-6
   Larivière RC, 2003, NEUROBIOL DIS, V13, P158, DOI 10.1016/S0969-9961(03)00036-6
   Lee VMY, 2001, ANNU REV NEUROSCI, V24, P1121, DOI 10.1146/annurev.neuro.24.1.1121
   Leung CL, 2004, BRAIN PATHOL, V14, P290, DOI 10.1111/j.1750-3639.2004.tb00066.x
   McLean J, 2008, J NEUROCHEM, V104, P1663, DOI 10.1111/j.1471-4159.2007.05198.x
   MIGHELI A, 1993, LAB INVEST, V68, P185
   OBLINGER MM, 1989, J NEUROSCI, V9, P3766
   PARYSEK LM, 1988, J NEUROSCI, V8, P555
   PARYSEK LM, 1991, J NEUROSCI RES, V30, P80, DOI 10.1002/jnr.490300110
   PEDERSEN WA, 1993, INT J CANCER, V53, P463, DOI 10.1002/ijc.2910530319
   Prasad S, 1999, INT J ONCOL, V14, P563
   Prieto VG, 1997, J CUTAN PATHOL, V24, P145, DOI 10.1111/j.1600-0560.1997.tb01568.x
   Puertas MC, 2007, J IMMUNOL, V178, P6533, DOI 10.4049/jimmunol.178.10.6533
   RhrichHaddout F, 1997, NEUROREPORT, V8, P3313, DOI 10.1097/00001756-199710200-00024
   Robertson J, 2003, J CELL BIOL, V160, P939, DOI 10.1083/jcb.200205027
   ROSEN DR, 1993, NATURE, V362, P59, DOI 10.1038/362059a0
   ROTHSTEIN JD, 1995, ANN NEUROL, V38, P73, DOI 10.1002/ana.410380114
   SARRIA AJ, 1990, J CELL BIOL, V111, P553, DOI 10.1083/jcb.111.2.553
   Saxena S, 2007, PROG NEUROBIOL, V83, P174, DOI 10.1016/j.pneurobio.2007.07.007
   Schiffer D, 1996, J NEUROL SCI, V139, P27, DOI 10.1016/0022-510X(96)00073-1
   Schweitzer SC, 2001, J CELL SCI, V114, P1079
   Steinert PM, 1999, J BIOL CHEM, V274, P9881, DOI 10.1074/jbc.274.14.9881
   Szabolcs MJ, 1996, PEDIATR PATHOL LAB M, V16, P51, DOI 10.1080/107710496175877
   Tedeschi G, 2007, NEUROCHEM RES, V32, P433, DOI 10.1007/s11064-006-9244-2
   Terao E, 2000, NEUROSCIENCE, V101, P679, DOI 10.1016/S0306-4522(00)00423-1
   TROY CM, 1990, BRAIN RES, V529, P232, DOI 10.1016/0006-8993(90)90832-V
   Vargas ME, 2007, ANNU REV NEUROSCI, V30, P153, DOI 10.1146/annurev.neuro.30.051606.094354
   Wang J, 2002, NEUROBIOL DIS, V10, P128, DOI 10.1006/nbdi.2002.0498
   Weng YC, 2007, EXP NEUROL, V204, P433, DOI 10.1016/j.expneurol.2006.12.003
   WONG J, 1990, J NEUROSCI RES, V27, P332, DOI 10.1002/jnr.490270312
   Wong NKY, 2000, J NEUROPATH EXP NEUR, V59, P972, DOI 10.1093/jnen/59.11.972
   WONG PC, 1995, NEURON, V14, P1105, DOI 10.1016/0896-6273(95)90259-7
   Xiao S, 2008, J NEUROSCI, V28, P1833, DOI 10.1523/JNEUROSCI.3222-07.2008
   Xiao SX, 2006, BBA-MOL BASIS DIS, V1762, P1001, DOI 10.1016/j.bbadis.2006.09.003
   XU ZS, 1993, CELL, V73, P23, DOI 10.1016/0092-8674(93)90157-L
   Yoshihara T, 2002, J NEUROCHEM, V80, P158, DOI 10.1046/j.0022-3042.2001.00683.x
   Zhu QZ, 1997, EXP NEUROL, V148, P299, DOI 10.1006/exnr.1997.6654
   Zinman L, 2009, NEUROLOGY, V72, P1153, DOI 10.1212/01.wnl.0000345363.65799.35
NR 83
TC 17
Z9 20
U1 0
U2 5
PU WILEY-BLACKWELL
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0022-3042
EI 1471-4159
J9 J NEUROCHEM
JI J. Neurochem.
PD AUG
PY 2010
VL 114
IS 4
BP 1177
EP 1192
DI 10.1111/j.1471-4159.2010.06846.x
PG 16
WC Biochemistry & Molecular Biology; Neurosciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Neurosciences & Neurology
GA 636EC
UT WOS:000280710100022
PM 20533992
OA Bronze
DA 2025-04-10
ER

PT J
AU Liu, HH
   Irving, HR
   Coupar, IM
AF Liu, HH
   Irving, HR
   Coupar, IM
TI Expression patterns of 5-HT7 receptor isoforms in the rat
   digestive tract
SO LIFE SCIENCES
LA English
DT Article
DE 5-hydroxytryptamine(7) (5-HT7) receptor; serotonin; isoform; jejunum;
   rat digestive tract; thalamus; alternative splicing
ID ESOPHAGEAL SMOOTH-MUSCLE; GUINEA-PIG ILEUM; SEROTONIN RECEPTOR;
   5-HYDROXYTRYPTAMINE RECEPTOR; MOLECULAR-CLONING; PHARMACOLOGICAL
   CHARACTERIZATION; MEDIATING CONTRACTION; LONGITUDINAL MUSCLE;
   ADENYLATE-CYCLASE; CORONARY-ARTERY
AB In this study, we determined the expression patterns of the 5-HT7 receptor isoforms at the mRNA level in the rat jejunum and other regions of the rat digestive tract using reverse transcriptase-PCR. In control studies using the rat thalamus, we detected all three known isoforms of the rat 5-HT7 receptor, 5-HT7(a), 5-HT7(b) and 5-HT7(c). In addition, we also detected in the thalamus a new PCR product that we provisionally name 5-HT7(c), All four isoforms of the 5-HT7 receptor were present throughout the rat digestive tract. However, the spatial distribution and levels of expression of the different isoforms varied between regions of the rat digestive tract. All three known isoforms and the provisional isoform were found in the jejunum, ileum, stomach fundus, oesophagus and colon. The level of expression of the isoforms varied with all four being most consistently found in the ileum. The 5-HT7(a) receptor isoform was predominantly expressed in the rat digestive tissue and 5-HT7(b), 5-HT7(c) and 5-HT7(e) were only sometimes expressed but always accompanying the receptor isoform. 5-HT7(a). (C) 2001 Elsevier Science Inc. All rights reserved.
C1 Monash Univ, Victorian Coll Pharm, Dept Pharmaceut Biol & Pharmacol, Parkville, Vic 3052, Australia.
C3 Monash University
RP Coupar, IM (corresponding author), Monash Univ, Victorian Coll Pharm, Dept Pharmaceut Biol & Pharmacol, Parkville, Vic 3052, Australia.
RI Irving, Helen/B-4425-2019
OI Irving, Helen/0000-0002-1514-0909
CR Albuquerque FC, 1998, J SURG RES, V77, P137, DOI 10.1006/jsre.1998.5361
   Amemiya N, 1996, EUR J PHARMACOL, V318, P403, DOI 10.1016/S0014-2999(96)00777-7
   Arcuni JC, 2000, J SURG RES, V91, P118, DOI 10.1006/jsre.2000.5915
   BARD JA, 1993, J BIOL CHEM, V268, P23422
   BAXTER GS, 1991, N-S ARCH PHARMACOL, V343, P439
   BAXTER GS, 1994, BRIT J PHARMACOL, V112, P323, DOI 10.1111/j.1476-5381.1994.tb13072.x
   BEUBLER E, 1993, EUR J PHARM-ENVIRON, V248, P157, DOI 10.1016/0926-6917(93)90038-R
   Briejer MR, 1997, NEUROGASTROENT MOTIL, V9, P231, DOI 10.1046/j.1365-2982.1997.d01-62.x
   Budhoo MR, 1996, EUR J PHARMACOL, V298, P137, DOI 10.1016/0014-2999(95)00752-0
   CARTER D, 1995, EUR J PHARMACOL, V280, P243, DOI 10.1016/0014-2999(95)00195-Q
   COHEN ML, 1994, GEN PHARMACOL, V25, P1143, DOI 10.1016/0306-3623(94)90130-9
   Cushing DJ, 1996, J PHARMACOL EXP THER, V277, P1560
   Eglen RM, 1997, TRENDS PHARMACOL SCI, V18, P104, DOI 10.1016/S0165-6147(97)01043-2
   FENIUK W, 1983, EUR J PHARMACOL, V96, P71, DOI 10.1016/0014-2999(83)90530-7
   Gelal A, 1998, GEN PHARMACOL, V30, P343, DOI 10.1016/S0306-3623(97)00096-7
   Haga K, 1995, OBES RES, V3, pS801, DOI 10.1002/j.1550-8528.1995.tb00503.x
   HANSEN MB, 1994, J SURG RES, V56, P277, DOI 10.1006/jsre.1994.1044
   Hardcastle J, 1998, J PHARM PHARMACOL, V50, P539, DOI 10.1111/j.2042-7158.1998.tb06196.x
   Heidmann DEA, 1997, J NEUROCHEM, V68, P1372
   Hemedah M, 1999, BRIT J PHARMACOL, V126, P179, DOI 10.1038/sj.bjp.0702293
   HEMEDAH M, 2000, P AUSTR SOC CLIN EXP, V7, P145
   HOYER D, 1994, PHARMACOL REV, V46, P157
   KALKMAN HO, 1986, EUR J PHARMACOL, V129, P139, DOI 10.1016/0014-2999(86)90345-6
   Kiso T, 1997, EUR J PHARMACOL, V320, P187, DOI 10.1016/S0014-2999(96)00893-X
   Kitazawa T, 1998, BRIT J PHARMACOL, V123, P173, DOI 10.1038/sj.bjp.0701583
   LOVENBERG TW, 1993, NEURON, V11, P449, DOI 10.1016/0896-6273(93)90149-L
   McLean PG, 1998, GEN PHARMACOL, V30, P227, DOI 10.1016/S0306-3623(97)00095-5
   McLean PG, 1996, EUR J PHARMACOL, V312, P215, DOI 10.1016/0014-2999(96)00456-6
   Morecroft I, 1998, BRIT J PHARMACOL, V125, P69, DOI 10.1038/sj.bjp.0702055
   Nagakura Y, 1997, J PHARMACOL EXP THER, V281, P284
   OHIA SE, 1992, GEN PHARMACOL, V23, P649, DOI 10.1016/0306-3623(92)90143-8
   PLASSAT JL, 1993, MOL PHARMACOL, V44, P229
   RUAT M, 1993, P NATL ACAD SCI USA, V90, P8547, DOI 10.1073/pnas.90.18.8547
   SHEN Y, 1993, J BIOL CHEM, V268, P18200
   Stam NJ, 1997, FEBS LETT, V413, P489, DOI 10.1016/S0014-5793(97)00964-2
   SUMNER MJ, 1989, BRIT J PHARMACOL, V97, P292, DOI 10.1111/j.1476-5381.1989.tb11953.x
   Terron JA, 1996, BRIT J PHARMACOL, V118, P1421, DOI 10.1111/j.1476-5381.1996.tb15555.x
   TSOU AP, 1994, J NEUROCHEM, V63, P456
   Tuladhar BR, 1996, BRIT J PHARMACOL, V119, P303, DOI 10.1111/j.1476-5381.1996.tb15986.x
NR 39
TC 27
Z9 32
U1 0
U2 3
PU PERGAMON-ELSEVIER SCIENCE LTD
PI OXFORD
PA THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND
SN 0024-3205
J9 LIFE SCI
JI Life Sci.
PD OCT 12
PY 2001
VL 69
IS 21
BP 2467
EP 2475
DI 10.1016/S0024-3205(01)01318-2
PG 9
WC Medicine, Research & Experimental; Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Research & Experimental Medicine; Pharmacology & Pharmacy
GA 483EP
UT WOS:000171621000002
PM 11693255
DA 2025-04-10
ER

PT J
AU Lim, YH
   Yoon, G
   Ryu, Y
   Jeong, D
   Song, JHY
   Kim, YS
   Ahn, Y
   Kook, H
   Kim, YK
AF Lim, Yeong-Hwan
   Yoon, Gwangho
   Ryu, Yeongseo
   Jeong, Dahee
   Song, Juhyun
   Kim, Yong Sook
   Ahn, Youngkeun
   Kook, Hyun
   Kim, Young-Kook
TI Human lncRNA SUGCT-AS1 Regulates the Proinflammatory Response of
   Macrophage
SO INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
LA English
DT Article
DE long non-coding RNAs; SUGCT-AS1; hnRNPU; MALT1; macrophage; vascular
   smooth muscle cells; inflammation
ID NF-KAPPA-B; CARDIOVASCULAR-DISEASE; ATHEROSCLEROSIS; TRANSLOCATION;
   SURVIVAL; NUCLEAR; RNAS
AB Macrophages are the major primary immune cells that mediate the inflammatory response. In this process, long non-coding RNAs (lncRNAs) play an important, yet largely unknown role. Therefore, utilizing several publicly available RNA sequencing datasets, we predicted and selected lncRNAs that are differentially expressed in M1 or M2 macrophages and involved in the inflammatory response. We identified SUGCT-AS1, which is a human macrophage-specific lncRNA whose expression is increased upon M1 macrophage stimulation. Conditioned media of SUGCT-AS1-depleted M1 macrophages induced an inflammatory phenotype of vascular smooth muscle cells, which included increased expression of inflammatory genes (IL1B and IL6), decreased contractile marker proteins (ACTA2 and SM22a), and increased cell migration. Depletion of SUGCT-AS1 promoted the expression and secretion of proinflammatory cytokines, such as TNF, IL1B, and IL6, in M1 macrophages, and transcriptomic analysis showed that SUGCT-AS1 has functions related to inflammatory responses and cytokines. Furthermore, we found that SUGCT-AS1 directly binds to hnRNPU and regulates its nuclear-cytoplasmic translocation. This translocation of hnRNPU altered the proportion of the MALT1 isoforms by regulating the alternative splicing of MALT1, a mediator of NF-?B signaling. Overall, our findings suggest that lncRNAs can be used for future studies on macrophage regulation. Moreover, they establish the SUGCT-AS1/hnRNPU/MALT1 axis, which is a novel inflammatory regulatory mechanism in macrophages.
C1 [Lim, Yeong-Hwan; Kim, Yong Sook; Ahn, Youngkeun; Kook, Hyun; Kim, Young-Kook] Chonnam Natl Univ, Med Sch, Basic Res Lab Vasc Remodeling, Hwasun 58128, South Korea.
   [Lim, Yeong-Hwan; Ryu, Yeongseo; Jeong, Dahee; Kim, Young-Kook] Chonnam Natl Univ, Med Sch, Dept Biochem, Hwasun 58128, South Korea.
   [Lim, Yeong-Hwan; Ryu, Yeongseo; Jeong, Dahee; Song, Juhyun; Kook, Hyun; Kim, Young-Kook] Chonnam Natl Univ, Biomed Sci Grad Program BMSGP, Hwasun 58128, South Korea.
   [Yoon, Gwangho] Korea Natl Inst Hlth, Dept Chron Dis Convergence Res, Div Brain Dis Res, Cheongju 28159, South Korea.
   [Song, Juhyun] Chonnam Natl Univ, Med Sch, Dept Anat, Hwasun 58128, South Korea.
   [Kim, Yong Sook; Ahn, Youngkeun] Chonnam Natl Univ Hosp, Cell Regenerat Res Ctr, Gwangju 61469, South Korea.
   [Kim, Yong Sook] Chonnam Natl Univ Hosp, Biomed Res Inst, Gwangju 61469, South Korea.
   [Ahn, Youngkeun] Chonnam Natl Univ, Med Sch, Dept Cardiol, Gwangju 61469, South Korea.
   [Kook, Hyun] Chonnam Natl Univ, Med Sch, Dept Pharmacol, Hwasun 58128, South Korea.
C3 Chonnam National University; Chonnam National University; Chonnam
   National University; Korea Disease Control & Prevention Agency (KDCA);
   Korea National Institute of Health (KNIH); Chonnam National University;
   Chonnam National University; Chonnam National University Hospital;
   Chonnam National University; Chonnam National University Hospital;
   Chonnam National University; Chonnam National University
RP Kim, YK (corresponding author), Chonnam Natl Univ, Med Sch, Basic Res Lab Vasc Remodeling, Hwasun 58128, South Korea.; Kim, YK (corresponding author), Chonnam Natl Univ, Med Sch, Dept Biochem, Hwasun 58128, South Korea.; Kim, YK (corresponding author), Chonnam Natl Univ, Biomed Sci Grad Program BMSGP, Hwasun 58128, South Korea.
EM ykk@jnu.ac.kr
RI Kim, Young-Kook/AAE-8306-2020; Kook, Hyun/AAR-5405-2021
OI Kim, Young-Kook/0000-0001-6434-2235; Lim, Yeong-Hwan/0000-0001-7390-4826
FU Basic Science Research Program [NRF-2021R1A2B5B02001501,
   2022R1A4A2000767, 2021R1A6A3A13044540, 2022R1I1A1A01070056]; Bio &
   Medical Technology Development Program of the National Research
   Foundation of Korea - Korean government (MSIT) [NRF-2022M3A9E4017151]
FX This study was supported by grants from the Basic Science Research
   Program (NRF-2021R1A2B5B02001501, 2022R1A4A2000767, 2021R1A6A3A13044540,
   and 2022R1I1A1A01070056) and the Bio & Medical Technology Development
   Program (NRF-2022M3A9E4017151) of the National Research Foundation of
   Korea funded by the Korean government (MSIT). The funders had no role in
   the study design, data collection, data analysis, decision to publish,
   or preparation of the manuscript.
CR Barrett TJ, 2020, ARTERIOSCL THROM VAS, V40, P20, DOI 10.1161/ATVBAHA.119.312802
   Basatemur GL, 2019, NAT REV CARDIOL, V16, P727, DOI [10.1038/s41569-019-0227-9, 10.1161/CIRCRESAHA.115.306361]
   Beermann J, 2016, PHYSIOL REV, V96, P1297, DOI 10.1152/physrev.00041.2015
   Bolger AM, 2014, BIOINFORMATICS, V30, P2114, DOI 10.1093/bioinformatics/btu170
   Chen YS, 2021, J CARDIOVASC TRANSL, V14, P857, DOI 10.1007/s12265-021-10108-w
   Chinetti-Gbaguidi G, 2015, NAT REV CARDIOL, V12, P10, DOI 10.1038/nrcardio.2014.173
   Creamer KM, 2021, MOL CELL, V81, P3509, DOI 10.1016/j.molcel.2021.07.004
   Cui M, 2021, NAT COMMUN, V12, DOI 10.1038/s41467-021-25653-w
   Delekta PC, 2010, J BIOL CHEM, V285, P41432, DOI 10.1074/jbc.M110.158949
   Dobin A, 2013, BIOINFORMATICS, V29, P15, DOI 10.1093/bioinformatics/bts635
   Fasolo F, 2019, CARDIOVASC RES, V115, P1732, DOI 10.1093/cvr/cvz203
   Frankish A, 2023, NUCLEIC ACIDS RES, V51, pD942, DOI 10.1093/nar/gkac1071
   Gimbrone MA, 2016, CIRC RES, V118, P620, DOI 10.1161/CIRCRESAHA.115.306301
   Gomez I, 2020, NAT COMMUN, V11, DOI 10.1038/s41467-019-14043-y
   Gunawan F, 2020, CIRC RES, V126, P968, DOI 10.1161/CIRCRESAHA.119.315992
   Gurvich OL, 2020, SCI REP-UK, V10, DOI 10.1038/s41598-020-70967-2
   Halaby MJ, 2019, SCI IMMUNOL, V4, DOI 10.1126/sciimmunol.aax8189
   Hao XY, 2022, AM J TRANSL RES, V14, P5363
   Herman AB, 2022, MOL CELL, V82, P2252, DOI 10.1016/j.molcel.2022.05.027
   Jones AN, 2022, SCI ADV, V8, DOI 10.1126/sciadv.abp9153
   Jones WK, 2005, CARDIOVASC TOXICOL, V5, P183, DOI 10.1385/CT:5:2:183
   Kutukculer N, 2021, J ALLERGY CLIN IMMUN, V147, P775, DOI 10.1016/j.jaci.2020.07.034
   Lee TL, 2021, THERANOSTICS, V11, P3131, DOI 10.7150/thno.52677
   Li T, 2021, J INFLAMM RES, V14, P4245, DOI 10.2147/JIR.S327152
   Liang HH, 2020, MOL THER-ONCOLYTICS, V16, P53, DOI 10.1016/j.omto.2019.12.002
   Lim YH, 2020, MOL THER-NUCL ACIDS, V22, P209, DOI 10.1016/j.omtn.2020.08.032
   Maarouf M, 2019, CELL MICROBIOL, V21, DOI 10.1111/cmi.13036
   Mahmoud AD, 2019, CIRC RES, V125, P535, DOI 10.1161/CIRCRESAHA.119.314876
   Meininger I, 2016, NAT COMMUN, V7, DOI 10.1038/ncomms11292
   Nazari-Jahantigh M, 2012, J CLIN INVEST, V122, P4190, DOI 10.1172/JCI61716
   Park Sung Ho, 2021, J Lipid Atheroscler, V10, P251, DOI 10.12997/jla.2021.10.3.251
   Park Sungmi, 2019, J Lipid Atheroscler, V8, P15, DOI 10.12997/jla.2019.8.1.15
   Riddell A, 2020, CARDIOVASC RES, V116, P1410, DOI 10.1093/cvr/cvaa034
   Robinson JT, 2023, BIOINFORMATICS, V39, DOI 10.1093/bioinformatics/btac830
   Roth S, 2017, EXP CELL RES, V350, P210, DOI 10.1016/j.yexcr.2016.11.023
   Roux BT, 2017, FRONT IMMUNOL, V8, DOI 10.3389/fimmu.2017.01038
   Rua R, 2015, J LEUKOCYTE BIOL, V98, P319, DOI 10.1189/jlb.4RI0115-006RR
   Simion V, 2020, NAT COMMUN, V11, DOI 10.1038/s41467-020-19664-2
   Simion V, 2020, JCI INSIGHT, V5, DOI 10.1172/jci.insight.140627
   Simmonds Rachel E, 2019, Wellcome Open Res, V4, P43, DOI 10.12688/wellcomeopenres.15065.1
   Siomi MC, 1997, J CELL BIOL, V138, P1181, DOI 10.1083/jcb.138.6.1181
   Song Juhyun, 2020, J Lipid Atheroscler, V9, P449, DOI 10.12997/jla.2020.9.3.449
   Sun CB, 2020, ARTERIOSCL THROM VAS, V40, P1464, DOI 10.1161/ATVBAHA.119.313749
   Tang XJ, 2018, CURR PROTEIN PEPT SC, V19, P172, DOI 10.2174/1389203718666171009111835
   Tedgui A, 2006, PHYSIOL REV, V86, P515, DOI 10.1152/physrev.00024.2005
   Thorp E, 2009, CELL METAB, V9, P474, DOI 10.1016/j.cmet.2009.03.003
   Trapnell C, 2012, NAT PROTOC, V7, P562, DOI 10.1038/nprot.2012.016
   Vargova K, 2011, BLOOD, V117, P3816, DOI 10.1182/blood-2010-05-285064
   Veseli BE, 2017, EUR J PHARMACOL, V816, P3, DOI 10.1016/j.ejphar.2017.05.010
   Wang P, 2014, SCIENCE, V344, P310, DOI 10.1126/science.1251456
   Yao RW, 2019, NAT CELL BIOL, V21, P542, DOI 10.1038/s41556-019-0311-8
   Yao Z, 2010, ONCOGENE, V29, P1821, DOI 10.1038/onc.2009.473
   Ye JQ, 2015, P NATL ACAD SCI USA, V112, pE3020, DOI 10.1073/pnas.1508461112
   Zhang HR, 2017, J AM HEART ASSOC, V6, DOI 10.1161/JAHA.117.007431
   Zhang HR, 2015, CIRC RES, V117, P17, DOI 10.1161/CIRCRESAHA.117.305860
   Zhang X, 2019, ATHEROSCLEROSIS, V281, P180, DOI 10.1016/j.atherosclerosis.2018.09.040
   Zhao W, 2012, J IMMUNOL, V188, P3179, DOI 10.4049/jimmunol.1101175
NR 57
TC 4
Z9 4
U1 1
U2 5
PU MDPI
PI BASEL
PA MDPI AG, Grosspeteranlage 5, CH-4052 BASEL, SWITZERLAND
SN 1661-6596
EI 1422-0067
J9 INT J MOL SCI
JI Int. J. Mol. Sci.
PD SEP
PY 2023
VL 24
IS 17
AR 13315
DI 10.3390/ijms241713315
PG 22
WC Biochemistry & Molecular Biology; Chemistry, Multidisciplinary
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Chemistry
GA S3GU9
UT WOS:001070095500001
PM 37686120
OA Green Published, gold
DA 2025-04-10
ER

PT J
AU Yuan, CC
   Ma, WK
   Schemmel, P
   Cheng, YS
   Liu, JM
   Tsaprailis, G
   Feldman, S
   Southgate, AA
   Irving, TC
AF Yuan, Chen-Ching
   Ma, Weikang
   Schemmel, Peter
   Cheng, Yu-Shu
   Liu, Jiangmin
   Tsaprailis, George
   Feldman, Samuel
   Southgate, Agnes Ayme
   Irving, Thomas C.
TI Elastic proteins in the flight muscle of Manduca sexta
SO ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
LA English
DT Article
DE Insect flight muscle; Passive tension; Elastic proteins
ID TEMPERATURE-GRADIENTS; MYOFIBRILLAR PROTEIN; ASYNCHRONOUS MUSCLE;
   STATISTICAL-MODEL; TITIN ISOFORMS; CARDIAC-MUSCLE; PEVK DOMAIN;
   PROJECTIN; TANDEM; IDENTIFICATIONS
AB The flight muscles (DLK) of the Hawkmoth, Manduca sexta are synchronous, requiring a neural spike for each contraction. Stress/strain curves of skinned DLM1, showed hysteresis indicating the presence of titin-like elastic proteins. Projectin and kettin are titin-like proteins previously identified in Lethocerus and Drosophila flight muscles. Analysis of Manduca muscles with 1% SDS-agarose gels and western blots showed two bands near 1 MDa that cross-reacted with antibodies to Drosophila projectin. Antibodies to Drosophila kettin cross-reacted to bands at similar to 500 and similar to 700 kDa, but also to bands at similar to 1.6 and similar to 2.1 MDa, that had not been previously observed in insect flight muscles. Mass spectrometry identified the 2.1 MDa protein as a product of the Sallimus (sis) gene. Analysis of the gene sequence showed that all 4 putative Sallimus and kettin isoforms could be explained as products of alternative splicing of the single sls gene. Both projectin and sallimus isoforms were expressed to higher levels in ventrally located DLM1 subunits, primarily responsible for active work production, as compared to dorsally located subunits, which may act as damped springs. The different expression levels of the 2 projectin isoforms and 4 sallimus/kettin isoforms may be adaptations to the specific requirements of individual muscle subunits. (C) 2015 Elsevier Inc. All rights reserved.
C1 [Yuan, Chen-Ching; Ma, Weikang; Schemmel, Peter; Cheng, Yu-Shu; Liu, Jiangmin; Irving, Thomas C.] IIT, Dept Biol & Chem Sci, Chicago, IL 60616 USA.
   [Tsaprailis, George] Univ Arizona, Ctr Toxicol, Tucson, AZ USA.
   [Feldman, Samuel; Southgate, Agnes Ayme] Coll Charleston, Dept Biol, Charleston, SC 29401 USA.
C3 Illinois Institute of Technology; University of Arizona; College of
   Charleston
RP Irving, TC (corresponding author), IIT, Dept Biol & Chem Sci, 3101 S Dearborn St, Chicago, IL 60616 USA.
EM irving@iit.edu
RI Ma, Weikang/AAA-4847-2021
OI Ma, Weikang/0000-0001-9535-7114; Tsaprailis, George/0000-0003-1239-2358
FU NSF [IOS-1022058]; NIEHS [ES06694]; NIH/NCI [CA023074]; BIO5 Institute
   of the University of Arizona; NIH/NCRR [1S10 RR028868-01]; College of
   Charleston
FX We would like to thank Prof. T. Daniel (U. Washington) for providing
   Manduca sexta samples. Research was supported by NSF IOS-1022058
   (Irving). Mass spectrometry and proteomics data were acquired by the
   Arizona Proteomics Consortium supported by NIEHS grant ES06694 to the
   SWEHSC, NIH/NCI grant CA023074 to the AZCC and by the BIO5 Institute of
   the University of Arizona. The Thermo Fisher LTQ OrbitrapVelos mass
   spectrometer was provided by grant 1S10 RR028868-01 from NIH/NCRR. AAS
   and SF were supported by the College of Charleston.
CR ALTSCHUL SF, 1990, J MOL BIOL, V215, P403, DOI 10.1016/S0022-2836(05)80360-2
   Andon NL, 2002, PROTEOMICS, V2, P1156, DOI 10.1002/1615-9861(200209)2:9<1156::AID-PROT1156>3.0.CO;2-4
   Ayme-Southgate A, 2011, INSECT MOL BIOL, V20, P347, DOI 10.1111/j.1365-2583.2011.01069.x
   Ayme-Southgate A., 2012, J PROTEOMICS GENOME, V1, P21
   Ayme-Southgatea AJ, 2013, J INSECT SCI, V13, DOI 10.1673/031.013.8801
   Ayme-Southgate A, 2005, J MUSCLE RES CELL M, V26, P467, DOI 10.1007/s10974-005-9031-8
   Ayme-Southgate AJ, 2008, J MOL EVOL, V67, P653, DOI 10.1007/s00239-008-9177-2
   AYMESOUTHGATE A, 1995, J CELL BIOL, V128, P393, DOI 10.1083/jcb.128.3.393
   Bullard B, 2006, P NATL ACAD SCI USA, V103, P4451, DOI 10.1073/pnas.0509016103
   Bullard B, 2002, J MUSCLE RES CELL M, V23, P435, DOI 10.1023/A:1023454305437
   Bullard B., 2006, NATURES VERSATILE EN, P177
   Bullard B, 2005, J MUSCLE RES CELL M, V26, P479, DOI 10.1007/s10974-005-9032-7
   Burkart C, 2007, J MOL BIOL, V367, P953, DOI 10.1016/j.jmb.2007.01.059
   Cazorla O, 2000, CIRC RES, V86, P59, DOI 10.1161/01.RES.86.1.59
   Craig R, 2004, BIOINFORMATICS, V20, P1466, DOI 10.1093/bioinformatics/bth092
   Dudley R., 2000, The biomechanics of insect flight: form, function, evolution
   Gautel M, 1996, FEBS LETT, V385, P11, DOI 10.1016/0014-5793(96)00338-9
   George NT, 2013, SCIENCE, V340, P1217, DOI 10.1126/science.1229573
   George NT, 2012, J EXP BIOL, V215, P471, DOI 10.1242/jeb.062901
   George NT, 2011, J EXP BIOL, V214, P894, DOI 10.1242/jeb.047969
   Granzier H, 2002, J PHYSIOL-LONDON, V541, P335, DOI 10.1113/jphysiol.2001.014381
   GRANZIER HL, 1995, BIOPHYS J, V68, P1027, DOI 10.1016/S0006-3495(95)80278-X
   Granzier HL, 2005, ADV PROTEIN CHEM, V71, P89, DOI 10.1016/S0065-3233(04)71003-7
   HOROWITS R, 1992, BIOPHYS J, V61, P392, DOI 10.1016/S0006-3495(92)81845-3
   HUANG XQ, 1991, ADV APPL MATH, V12, P337, DOI 10.1016/0196-8858(91)90017-D
   Josephson RK, 2000, J EXP BIOL, V203, P2713
   Junier T, 2000, BIOINFORMATICS, V16, P178, DOI 10.1093/bioinformatics/16.2.178
   Keller A, 2002, ANAL CHEM, V74, P5383, DOI 10.1021/ac025747h
   Kreisköther N, 2006, J MUSCLE RES CELL M, V27, P93, DOI 10.1007/s10974-006-9060-y
   Kulke M, 2001, J CELL BIOL, V154, P1045, DOI 10.1083/jcb.200104016
   Linke WA, 1999, J CELL BIOL, V146, P631, DOI 10.1083/jcb.146.3.631
   Linke WA, 1996, J MOL BIOL, V261, P62, DOI 10.1006/jmbi.1996.0441
   Machado C, 2000, J CELL BIOL, V151, P639, DOI 10.1083/jcb.151.3.639
   NAVE R, 1990, J CELL SCI, V95, P535
   Nedrud J, 2011, BIOPHYS J, V101, P1385, DOI 10.1016/j.bpj.2011.06.054
   Nesvizhskii AI, 2003, ANAL CHEM, V75, P4646, DOI 10.1021/ac0341261
   Perz-Edwards RJ, 2011, P NATL ACAD SCI USA, V108, P120, DOI 10.1073/pnas.1014599107
   PRINGLE JWS, 1978, PROC R SOC SER B-BIO, V201, P107, DOI 10.1098/rspb.1978.0035
   Qian WJ, 2005, J PROTEOME RES, V4, P53, DOI 10.1021/pr0498638
   Roberts RJ, 2013, GENOME BIOL, V14, DOI [10.1186/gb-2013-14-7-405, 10.1186/gb-2013-14-6-405]
   Shevchenko A, 1996, ANAL CHEM, V68, P850, DOI 10.1021/ac950914h
   SIEGMAN MJ, 1976, SCIENCE, V191, P383, DOI 10.1126/science.128819
   Southgate R, 2001, J MOL BIOL, V313, P1035, DOI 10.1006/jmbi.2001.5115
   STEVENSON RD, 1990, J EXP BIOL, V149, P61
   Thompson JD, 1997, NUCLEIC ACIDS RES, V25, P4876, DOI 10.1093/nar/25.24.4876
   Trombitas K, 1998, J STRUCT BIOL, V122, P188, DOI 10.1006/jsbi.1998.3984
   Trombitás K, 2000, ADV EXP MED BIOL, V481, P1
   Tu MS, 2004, J EXP BIOL, V207, P2455, DOI 10.1242/jeb.01039
   Warren CM, 2003, ELECTROPHORESIS, V24, P1695, DOI 10.1002/elps.200305392
   Weitkamp B, 1998, J BIOL CHEM, V273, P19802, DOI 10.1074/jbc.273.31.19802
NR 50
TC 9
Z9 12
U1 0
U2 6
PU ELSEVIER SCIENCE INC
PI NEW YORK
PA STE 800, 230 PARK AVE, NEW YORK, NY 10169 USA
SN 0003-9861
EI 1096-0384
J9 ARCH BIOCHEM BIOPHYS
JI Arch. Biochem. Biophys.
PD FEB 15
PY 2015
VL 568
BP 16
EP 27
DI 10.1016/j.abb.2014.12.033
PG 12
WC Biochemistry & Molecular Biology; Biophysics
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Biophysics
GA CC7GN
UT WOS:000350535800003
PM 25602701
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Toullec, JY
   Serrano, L
   Lopez, P
   Soyez, D
   Spanings-Pierrot, C
AF Toullec, Jean-Yves
   Serrano, Laetitia
   Lopez, Philippe
   Soyez, Daniel
   Spanings-Pierrot, Celine
TI The crustacean hyperglycemic hormones from an euryhaline crab
   Pachygrapsus marmoratus and a fresh water crab Potamon
   ibericum:: Eyestalk and pericardial isoforms
SO PEPTIDES
LA English
DT Article
DE crustacean hyperglycemic hormone; X-organ; pericardial organ; brachyura;
   heterotremata; alternative splicing
ID AMINO-ACID-SEQUENCE; TRANSPORT PEPTIDE ITP; SINUS GLAND; SPINY LOBSTER;
   ION-TRANSPORT; MOLECULAR-CLONING; MEXICAN CRAYFISH; SHORE CRAB; CHH;
   NEUROPEPTIDE
AB The structures of crustacean hyperglycemic hormones (CHH) were investigated in two crabs, the coastal euryhaline crab Pachygrapsus marmoratus(1) and the fresh water crab Potamon ibericum.(2) The neuropeptide mRNAs were extracted from pericardial and X-organs (PO and XO), and the sequences of the cDNA encoding the hormones' precursors were determined. The X-organ preprohormones are composed of 29 and 28 amino acid signal peptides in P. marmoratus and P. ibericum respectively, followed by 43 and 41 amino acid crustacean hyperglycemic hormone precursor related peptide (CPRP) flanking the 72 amino acid crustacean hyperglycemic hormones. A similar organization is reported for pericardial. preprohormones with identical sequences for the signal peptide, the CPRP and the N-terminal sequences of CHH (1-40), but remaining sequences (41-72 and 41-71) differing considerably. In P. marmoratus two CHH cDNAs were characterized from XO and evidences were obtained for the existence of at least two forms in the PO. From our results and by comparison with other known sequences, a consensus pattern for crab pericardial CHH could be pointed out. Analysis of the data presented in this article using phylogenetic methods reveals that the two crab species studied are much closer than previously predicted. (c) 2005 Elsevier Inc. All rights reserved.
C1 Univ Paris 06, CNRS, FRE 2852, Grp Biogenese Peptides Isomeres, F-75252 Paris 05, France.
   Univ Montpellier 2, CNRS, UMR 5171, Lab Genome Populat Interact Adaptat,Equipe Adapta, F-34095 Montpellier, France.
   Univ Paris 06, CNRS, UMR 7138, Equipe Modelisat Dynam Syst Integres, F-75005 Paris, France.
C3 Sorbonne Universite; Centre National de la Recherche Scientifique
   (CNRS); Centre National de la Recherche Scientifique (CNRS); Universite
   de Montpellier; Centre National de la Recherche Scientifique (CNRS);
   CNRS - National Institute for Biology (INSB); Museum National d'Histoire
   Naturelle (MNHN); Sorbonne Universite
RP Toullec, JY (corresponding author), Univ Paris 06, CNRS, FRE 2852, Grp Biogenese Peptides Isomeres, 7 Quai St Bernard, F-75252 Paris 05, France.
EM jean-yves.toullec@upmc.fr
CR Abramowitz AA, 1944, BIOL BULL-US, V86, P1, DOI 10.2307/1537946
   Ahyong ST, 2004, RAFFLES B ZOOL, V52, P673
   Altschul SF, 1997, NUCLEIC ACIDS RES, V25, P3389, DOI 10.1093/nar/25.17.3389
   AUDSLEY N, 1992, J EXP BIOL, V173, P261
   Bulau P, 2003, PEPTIDES, V24, P1871, DOI 10.1016/j.peptides.2003.10.002
   CHARMANTIERDAURES M, 1994, GEN COMP ENDOCR, V94, P281, DOI 10.1006/gcen.1994.1085
   Chen SH, 2004, MAR BIOTECHNOL, V6, P83, DOI 10.1007/s10126-003-0014-8
   Chung JS, 1998, REGUL PEPTIDES, V77, P17, DOI 10.1016/S0167-0115(98)00024-X
   Chung JS, 1999, P NATL ACAD SCI USA, V96, P13103, DOI 10.1073/pnas.96.23.13103
   DEKLEIJN DPV, 1994, EUR J BIOCHEM, V224, P623, DOI 10.1111/j.1432-1033.1994.00623.x
   DEKLEIJN DPV, 1994, BIOCHIM BIOPHYS ACTA, V1260, P62
   DESAINTLAURENT M, 1980, CR ACAD SCI D NAT, V290, P1320
   Dircksen H, 2001, BIOCHEM J, V356, P159, DOI 10.1042/0264-6021:3560159
   DIRCKSEN H, 2000, ZOOLOGY S3, V103, P81
   Endo H, 2000, INSECT BIOCHEM MOLEC, V30, P355, DOI 10.1016/S0965-1748(99)00129-0
   GUINOT D, 1977, CR ACAD SCI D NAT, V285, P1049
   Huberman A, 1995, AQUACULTURE, V135, P149, DOI 10.1016/0044-8486(95)01010-6
   HUBERMAN A, 1993, PEPTIDES, V14, P7, DOI 10.1016/0196-9781(93)90004-Z
   JAROS PP, 1982, CELL TISSUE RES, V227, P555
   KEGEL G, 1991, PEPTIDES, V12, P909, DOI 10.1016/0196-9781(91)90036-O
   KEGEL G, 1989, FEBS LETT, V255, P10, DOI 10.1016/0014-5793(89)81051-8
   Keller R., 1999, Recent Developments in Comparative Endocrinology and Neurobiology, P209
   KOZAK M, 1987, NUCLEIC ACIDS RES, V15, P8125, DOI 10.1093/nar/15.20.8125
   Lacombe C, 1999, NEUROPEPTIDES, V33, P71, DOI 10.1054/npep.1999.0016
   Liu L, 1996, ARCH INSECT BIOCHEM, V32, P375, DOI 10.1002/(SICI)1520-6327(1996)32:3/4<375::AID-ARCH10>3.3.CO;2-0
   Liu Lei, 1997, Invertebrate Neuroscience, V3, P199, DOI 10.1007/BF02480375
   Macins A, 1999, ARCH INSECT BIOCHEM, V40, P107, DOI 10.1002/(SICI)1520-6327(1999)40:2<107::AID-ARCH5>3.0.CO;2-B
   Marco HG, 1998, BIOCHEM BIOPH RES CO, V248, P578, DOI 10.1006/bbrc.1998.9025
   Marco HG, 2000, PEPTIDES, V21, P19, DOI 10.1016/S0196-9781(99)00171-0
   Marco HG, 2003, PEPTIDES, V24, P845, DOI 10.1016/S0196-9781(03)00168-2
   MARTIN G, 1993, EUR J BIOCHEM, V211, P601, DOI 10.1111/j.1432-1033.1993.tb17587.x
   Meredith J, 1996, J EXP BIOL, V199, P1053
   Mettulio R, 2004, PEPTIDES, V25, P1899, DOI 10.1016/j.peptides.2004.06.013
   Serrano L, 2003, J EXP BIOL, V206, P979, DOI 10.1242/jeb.00178
   Shapiro JA, 2005, BIOL REV, V80, P227, DOI 10.1017/S1464793104006657
   SHAW G, 1986, CELL, V46, P659, DOI 10.1016/0092-8674(86)90341-7
   Soyez D, 1998, NEUROSCIENCE, V82, P935
   Soyez D, 2003, RE ADV MAR BIOTECHNO, V10, P279
   SOYEZ D, 1994, J BIOL CHEM, V269, P18295
   Spanings-Pierrot C, 2000, GEN COMP ENDOCR, V119, P340, DOI 10.1006/gcen.2000.7527
   Spanings-Pierrot Celine, 2005, Bulletin of the Mount Desert Island Biological Laboratory, V44, P67
   Toullec JY, 2002, PEPTIDES, V23, P31, DOI 10.1016/S0196-9781(01)00576-9
   Udomkit A, 2000, J EXP MAR BIOL ECOL, V244, P145, DOI 10.1016/S0022-0981(99)00134-3
   Von Sternberg R, 2001, CRUSTACEANA, V74, P321, DOI 10.1163/156854001300104417
   VONHEIJNE G, 1986, NUCLEIC ACIDS RES, V14, P4683, DOI 10.1093/nar/14.11.4683
   Webster S. G., 1998, Recent advances in arthropod endocrinology., P33
NR 46
TC 25
Z9 32
U1 2
U2 4
PU ELSEVIER SCIENCE INC
PI NEW YORK
PA STE 800, 230 PARK AVE, NEW YORK, NY 10169 USA
SN 0196-9781
EI 1873-5169
J9 PEPTIDES
JI Peptides
PD JUN
PY 2006
VL 27
IS 6
BP 1269
EP 1280
DI 10.1016/j.peptides.2005.12.001
PG 12
WC Biochemistry & Molecular Biology; Endocrinology & Metabolism;
   Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Endocrinology & Metabolism;
   Pharmacology & Pharmacy
GA 055MU
UT WOS:000238455600014
PM 16413086
DA 2025-04-10
ER

PT J
AU de Jesus, J
   Imane, Z
   Senée, V
   Romero, S
   Guillausseau, PJ
   Balafrej, A
   Julier, C
AF de Jesus, J.
   Imane, Z.
   Senee, V.
   Romero, S.
   Guillausseau, P. -J.
   Balafrej, A.
   Julier, C.
TI SLC29A3 mutation in a patient with syndromic diabetes with
   features of pigmented hypertrichotic dermatosis with insulin-dependent
   diabetes, H syndrome and Faisalabad histiocytosis
SO DIABETES & METABOLISM
LA English
DT Article
DE Diabetes; Syndrome; Monogenic; Genetics; Diagnosis
ID LYMPHADENOPATHY; GENE
AB Aims. - Atypical forms of diabetes may be caused by monogenic mutations in key genes controlling beta-cell development, survival and function. This report describes an insulin-dependent diabetes patient with a syndromic presentation in whom a homozygous SLC29A3 mutation was identified.
   Methods. - SLC29A3 was selected as the candidate gene based on the patient's clinical manifestations, and all exons and flanking regions in the patient's genomic DNA were sequenced.
   Results. - A homozygous splice mutation (c.300+IG>C) resulting in a frameshift and truncated protein (p.N101LfsX34) was identified. The patient had insulin-dependent diabetes, congenital deafness, short stature, hyperpigmented patches on the skin, dysmorphic features, cardiomegaly, arthrogryposis, hepatosplenomegaly, anaemia with erythroblastopenia, and an inflammatory syndrome with fever and arthritis; she also presented with a fibrotic mediastinal mass. These clinical features overlapped with pigmented hypertrichosis with insulin-dependent diabetes (PHID), H syndrome, Faisalabad histiocytosis and sinus histiocytosis with massive lymphadenopathy (SHML), all of which are also caused by SLC29A3 mutations.
   Conclusion. - This is the most severe case reported of SLC29A3 mutations with cumulative features of all these syndromes. This extreme severity coincides with the most N-terminal location of the truncation mutation, thereby affecting all alternative transcripts of the gene. This case report extends the clinical variability of homozygous SLC29A3 mutations that result in a spectrum of multisystemic manifestations. (C) 2013 Elsevier Masson SAS. All rights reserved.
C1 [de Jesus, J.; Senee, V.; Romero, S.; Guillausseau, P. -J.; Julier, C.] Med Fac Paris 7, INSERM, UMR S958, F-75010 Paris, France.
   [de Jesus, J.; Senee, V.; Romero, S.; Guillausseau, P. -J.; Julier, C.] Univ Paris 07, Paris, France.
   [Imane, Z.; Balafrej, A.] Children Hosp, Rabat, Morocco.
   [Guillausseau, P. -J.] Lariboisiere Hosp, AP HP, Dept Internal Med B, Paris, France.
C3 Universite Paris Cite; Institut National de la Sante et de la Recherche
   Medicale (Inserm); Universite Paris Cite; Mohammed V University in
   Rabat; Ibn sina University Hospital Center of Rabat; Assistance Publique
   Hopitaux Paris (APHP); Universite Paris Cite; Hopital Universitaire
   Lariboisiere-Fernand-Widal - APHP
RP Julier, C (corresponding author), Med Fac Paris 7, INSERM, UMR S958, Site Villemin,10,Ave Verdun, F-75010 Paris, France.
EM cecile.julier@inserm.fr
RI senee, valerie/M-9854-2017; JULIER, Cecile/M-9824-2017
OI senee, valerie/0000-0001-7012-3944; JULIER, Cecile/0000-0002-1538-0240
FU Agence Nationale de la Recherche (National Research Agency); Assistance
   Publique-Hopitaux de Paris (Public Hospital System of Paris)
FX We thank the patient and her family for agreeing to participate in this
   study. We are grateful to Professors Malihy, Lamalmi and Alhamany for
   performing the histopathological study of the skin lesion. We thank
   Professor Damien Sene for his critical review of the manuscript and
   interesting discussions. The study was supported by a grant from the
   Agence Nationale de la Recherche (National Research Agency) to C.J. We
   also thank the Assistance Publique-Hopitaux de Paris (Public Hospital
   System of Paris) for their support.
CR Bolze A, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0029708
   Campeau PM, 2012, HUM MOL GENET, V21, P4904, DOI 10.1093/hmg/dds326
   Cliffe ST, 2009, HUM MOL GENET, V18, P2257, DOI 10.1093/hmg/ddp161
   Elbarbary NS, 2012, PEDIAT DIABETES
   Govindarajan R, 2009, AM J PHYSIOL-GASTR L, V296, pG910, DOI 10.1152/ajpgi.90672.2008
   Holm P, 2001, AM J HUM GENET, V69, P1301
   Jonard L, 2012, EUR J MED GENET, V55, P56, DOI 10.1016/j.ejmg.2011.06.009
   Karges B, 2012, NAT REV ENDOCRINOL, V8, P201, DOI 10.1038/nrendo.2011.204
   Kismet E, 2005, PEDIATR INT, V47, P473, DOI 10.1111/j.1442-200x.2005.02096.x
   Molho-Pessach V, 2008, J AM ACAD DERMATOL, V59, P79, DOI 10.1016/j.jaad.2008.03.021
   Morgan NV, 2010, PLOS GENET, V6, DOI 10.1371/journal.pgen.1000833
   Moynihan LM, 1998, AM J HUM GENET, V62, P1123, DOI 10.1086/301824
   Prendiville J, 2007, PEDIATR DERMATOL, V24, P101, DOI 10.1111/j.1525-1470.2007.00352.x
   Priya TP, 2010, BRIT J DERMATOL, V162, P1132, DOI 10.1111/j.1365-2133.2010.09653.x
   Rossbach HC, 2006, PEDIATR BLOOD CANCER, V47, P629, DOI 10.1002/pbc.20605
NR 15
TC 25
Z9 26
U1 1
U2 6
PU MASSON EDITEUR
PI MOULINEAUX CEDEX 9
PA 21 STREET CAMILLE DESMOULINS, ISSY, 92789 MOULINEAUX CEDEX 9, FRANCE
SN 1262-3636
EI 1878-1780
J9 DIABETES METAB
JI Diabetes Metab.
PD MAY
PY 2013
VL 39
IS 3
BP 281
EP 285
DI 10.1016/j.diabet.2013.03.007
PG 5
WC Endocrinology & Metabolism
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Endocrinology & Metabolism
GA 177XP
UT WOS:000321409000013
PM 23623699
DA 2025-04-10
ER

PT J
AU Yoon, S
   Gariepy, CE
   Yanagisawa, M
   Zuccarello, M
   Rapoport, RM
AF Yoon, SeongHun
   Gariepy, Cheryl E.
   Yanagisawa, Masashi
   Zuccarello, Mario
   Rapoport, Robert M.
TI Functional ETA-ETB Receptor Cross-talk in Basilar
   Artery In Situ From ETB Receptor Deficient Rats
SO JOURNAL OF CARDIOVASCULAR PHARMACOLOGY
LA English
DT Article
DE endothelin receptor antagonist; spotting lethal rat; in situ;
   constriction; basilar artery; endothelin receptor; cross-talk
ID PULMONARY-HYPERTENSION; ENDOTHELIN-1; INTERNALIZATION; CONTRACTION; ET-1
AB The role of endothelin (ET)(A)-ETB receptor cross-talk in limiting the ETA receptor antagonist inhibition of ET-1 constriction is revealed by the partial or complete dependency of the ETA receptor antagonist inhibition on functional removal of the ETB receptor. Although functional removal of the ETB receptor is generally accomplished with ETB receptor antagonist, a novel approach using rats containing a naturally occurring deletion mutation in the ETB receptor [rescued "spotting lethal" (sl) rats; ETBsl/sl] demonstrated increased ETA receptor antagonist inhibition of ET-1 constriction in vena cava. We investigated whether this deletion mutation was also sufficient to remove the ETB receptor dependency of the ETA receptor antagonist inhibition of ET-1 constriction in the basilar artery. Consistent with previous reports, ET-1 plasma levels were elevated in ETBsl/sl as compared with ETB+/+ rats. ETB receptor antagonist failed to relax the ET-1 constricted basilar artery from ETB+/+ and ETBsl/sl rats. Relaxation to combined ETA and ETB receptor antagonist was greater than relaxation to ETA receptor antagonist in the basilar artery from ETB+/+ and, unexpectedly, ETBsl/sl rats. These findings confirm the presence of ETA-ETB receptor cross-talk in the basilar artery. We speculate that mutant ETB receptor expression produced by alternative splicing may be sufficient to allow cross-talk.
C1 [Yoon, SeongHun] Rutgers State Univ, New Jersey Med Sch, Dept Cell Biol & Mol Med, Newark, NJ 07102 USA.
   [Gariepy, Cheryl E.] Ohio State Univ, Dept Pediat Gastroenterol, Columbus, OH 43210 USA.
   [Gariepy, Cheryl E.] Nationwide Childrens Hosp, Columbus, OH USA.
   [Yanagisawa, Masashi] Univ Tsukuba, Int Inst Integrat Sleep Med WPI IIIS, Tsukuba, Ibaraki, Japan.
   [Zuccarello, Mario] Univ Cincinnati, Coll Med, Dept Neurosurg, Inst Neurosci, Cincinnati, OH 45267 USA.
   [Rapoport, Robert M.] Univ Cincinnati, Coll Med, Dept Pharmacol & Cell Biophys, POB 670575, Cincinnati, OH 45267 USA.
C3 Rutgers University System; Rutgers University Newark; Rutgers University
   New Brunswick; Rutgers University Biomedical & Health Sciences;
   University System of Ohio; Ohio State University; University System of
   Ohio; Ohio State University; Nationwide Childrens Hospital; University
   of Tsukuba; University System of Ohio; University of Cincinnati;
   University System of Ohio; University of Cincinnati
RP Rapoport, RM (corresponding author), Univ Cincinnati, Coll Med, Dept Pharmacol & Cell Biophys, POB 670575, Cincinnati, OH 45267 USA.
EM robert.rapoport@uc.edu
RI Gariepy, Cheryl/AAQ-3441-2021
FU Office of Research and Development, Medical Research Service, Department
   of Veterans Affairs; Mayfield Educational Fund, Department of
   Neurosurgery, University of Cincinnati, Cincinnati, Ohio; World Premier
   International Research Center Initiative from MEXT, Japan
FX Supported by grants from the Office of Research and Development, Medical
   Research Service, Department of Veterans Affairs and the Mayfield
   Educational Fund, Department of Neurosurgery, University of Cincinnati,
   Cincinnati, Ohio (R.M.R. and M.Z.) and the World Premier International
   Research Center Initiative from MEXT, Japan (M.Y.). M. Yanagisawa is a
   former investigator of the Howard Hughes Medical Institute.
CR Evans NJ, 2008, CAN J PHYSIOL PHARM, V86, P526, DOI 10.1139/Y08-050
   FUKURODA T, 1994, BIOCHEM BIOPH RES CO, V199, P1461, DOI 10.1006/bbrc.1994.1395
   Gariepy CE, 2000, J CLIN INVEST, V105, P925, DOI 10.1172/JCI8609
   Gariepy CE, 1998, J CLIN INVEST, V102, P1092, DOI 10.1172/JCI3702
   Gregan B, 2004, J BIOL CHEM, V279, P27679, DOI 10.1074/jbc.M403601200
   Iglarz M, 2015, J CARDIOVASC PHARM, V66, P332, DOI 10.1097/FJC.0000000000000283
   Ivy DD, 2002, AM J PHYSIOL-LUNG C, V282, pL703, DOI 10.1152/ajplung.00272.2001
   Ivy DD, 2001, AM J PHYSIOL-LUNG C, V280, pL1040, DOI 10.1152/ajplung.2001.280.5.L1040
   Li WG, 2011, NEUROL RES, V33, P185, DOI 10.1179/016164111X12881719352417
   Mazzuca MQ, 2012, BIOCHEM PHARMACOL, V84, P147, DOI 10.1016/j.bcp.2012.03.020
   Pearl JM, 2004, ANN THORAC SURG, V77, P994, DOI 10.1016/j.athoracsur.2003.09.067
   Perry MG, 2001, AM J PHYSIOL-HEART C, V281, pH2680, DOI 10.1152/ajpheart.2001.281.6.H2680
   Pollock DM, 2000, J CARDIOVASC PHARM, V36, pS82, DOI 10.1097/00005344-200036051-00027
   Rapoport RM, 2012, J CARDIOVASC PHARM, V60, P483, DOI 10.1097/FJC.0b013e31826f32c1
   Rapoport RM, 2011, J PHARM PHARMACOL, V63, P1373, DOI 10.1111/j.2042-7158.2011.01334.x
   Sandoval YHG, 2014, CURR VASC PHARMACOL, V12, P202, DOI 10.2174/1570161112666140226122054
   Sauvageau S, 2006, EXP BIOL MED, V231, P840
   Taylor TA, 2003, HYPERTENSION, V41, P657, DOI 10.1161/01.HYP.0000048193.85814.78
   Thakali K, 2008, VASC PHARMACOL, V49, P6, DOI 10.1016/j.vph.2008.03.005
   Yoon S, 2012, N-S ARCH PHARMACOL, V385, P437, DOI 10.1007/s00210-012-0725-3
NR 20
TC 3
Z9 3
U1 0
U2 6
PU LIPPINCOTT WILLIAMS & WILKINS
PI PHILADELPHIA
PA TWO COMMERCE SQ, 2001 MARKET ST, PHILADELPHIA, PA 19103 USA
SN 0160-2446
EI 1533-4023
J9 J CARDIOVASC PHARM
JI J. Cardiovasc. Pharmacol.
PD MAR
PY 2016
VL 67
IS 3
BP 212
EP 217
DI 10.1097/FJC.0000000000000335
PG 6
WC Cardiac & Cardiovascular Systems; Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cardiovascular System & Cardiology; Pharmacology & Pharmacy
GA DG9OP
UT WOS:000372413600003
PM 26528589
DA 2025-04-10
ER

PT J
AU Liu, ZY
   Ho, LD
   Bonning, B
AF Liu, Zhiyan
   Ho, Linda
   Bonning, Bryony
TI Localization of a Drosophila melanogaster homolog of the putative
   juvenile hormone esterase binding protein of Manduca sexta
SO INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY
LA English
DT Article
DE Drosophila melanogaster; juvenile hormone esterase binding protein; P29;
   Manduca sexta; mitochondria
ID RECOMBINANT PROTEINS; HELIOTHIS-VIRESCENS; PERICARDIAL CELLS; TOBACCO
   HORNWORM; GENE-EXPRESSION; INSECT CELLS; IMPORT; MITOCHONDRIA; GENOME;
   TIM44
AB A putative juvenile hormone esterase (JHE) binding protein, P29, was isolated from the tobacco hornworm Manduca sexta [J. Biol. Chem. 275(3), 1802-1806]. A homolog of P29 was identified in Drosophila melanogaster by sequence alignment. This gene, CG3776 was cloned, recombinant DmP29 expressed in Escheriscia coli and two anti-DmP29 antisera raised. In vitro binding of the P29 homolog to Drosophila JHE was confirmed. P29 mRNA and an immunoreactive protein of 25 kDa were detected in Drosophila larvae, pupae and adults. The predicted size of the protein is 30 kDa. Drosophila P29 is predicted to localize to mitochondria (MitoProt; 93%, probability) and has a 6kDa N-terminal targeting sequence. Subcellular organelle fractionation and confocal microscopy of Drosophila S2 cells confirmed that the immunoreactive 25 kDa protein is present in mitochondria but not in the cytosol. Expression of P29 without the predicted N-terminal targeting sequence in High Five (TM) cells showed that the N-terminal targeting sequence is shorter than predicted, and that a second, internal mitochondrial targeting signal is also present. An immunoreactive protein of 50 kDa in the hemolymph does not result from alternative splicing of CG3776 but may result from dimerization of P29. The function of P29 in mitochondria and the possible interaction with JHE are discussed. (c) 2006 Elsevier Ltd. All rights reserved.
C1 Iowa State Univ, Dept Entomol, Ames, IA 50011 USA.
   Iowa State Univ, Interdept Program Genet, Ames, IA 50011 USA.
C3 Iowa State University; Iowa State University
RP Bonning, B (corresponding author), Iowa State Univ, Dept Entomol, Ames, IA 50011 USA.
EM bbonning@iastate.edu
CR Adams MD, 2000, SCIENCE, V287, P2185, DOI 10.1126/science.287.5461.2185
   Bassham DC, 1998, PLANT PHYSIOL, V117, P407, DOI 10.1104/pp.117.2.407
   Bonning BC, 1997, P NATL ACAD SCI USA, V94, P6007, DOI 10.1073/pnas.94.12.6007
   BONNING BC, 1992, INSECT BIOCHEM MOLEC, V22, P453, DOI 10.1016/0965-1748(92)90141-Z
   BOOTH TF, 1992, TISSUE CELL, V24, P267, DOI 10.1016/0040-8166(92)90100-L
   Campbell PM, 2001, INSECT BIOCHEM MOLEC, V31, P513, DOI 10.1016/S0965-1748(01)00035-2
   Campbell PM, 1998, INSECT BIOCHEM MOLEC, V28, P501, DOI 10.1016/S0965-1748(98)00037-X
   CAMPBELL PM, 1992, INSECT BIOCHEM MOLEC, V22, P665, DOI 10.1016/0965-1748(92)90045-G
   Chacinska A, 2002, TRENDS CELL BIOL, V12, P299, DOI 10.1016/S0962-8924(02)02310-3
   COTTON C, 1991, EXPERIENTIA, V47, P705
   ELDRIDGE R, 1992, APPL ENVIRON MICROB, V58, P1583, DOI 10.1128/AEM.58.5.1583-1591.1992
   Farkas R, 2001, BIOCHEM CELL BIOL, V79, P755, DOI 10.1139/bcb-79-6-755
   Farrell P, 2004, PROTEIN EXPRES PURIF, V36, P177, DOI 10.1016/j.pep.2004.03.010
   Farrell PJ, 1998, BIOTECHNOL BIOENG, V60, P656, DOI 10.1002/(SICI)1097-0290(19981220)60:6<656::AID-BIT2>3.0.CO;2-9
   Ghebrehiwet B, 2001, IMMUNOL REV, V180, P65, DOI 10.1034/j.1600-065X.2001.1800106.x
   Giot L, 2003, SCIENCE, V302, P1727, DOI 10.1126/science.1090289
   HALARNKAR PP, 1988, INSECT BIOCHEM, V16, P455
   Hammock B., 1990, P49
   HAMMOCK BD, 1985, COMPREHENSIVE INSECT, V7, P431
   Harlow ED, 1988, ANTIBODIES LAB MANUA
   ICHINOSE R, 1992, PESTIC BIOCHEM PHYS, V42, P13, DOI 10.1016/0048-3575(92)90069-C
   ICHINOSE R, 1992, INSECT BIOCHEM MOLEC, V22, P893, DOI 10.1016/0965-1748(92)90116-V
   Matsuoka T, 2005, DIABETES, V54, P2882, DOI 10.2337/diabetes.54.10.2882
   MITSUI T, 1979, INSECT BIOCHEM, V9, P637, DOI 10.1016/0020-1790(79)90103-3
   Moro F, 2002, J BIOL CHEM, V277, P6874, DOI 10.1074/jbc.M107935200
   Rehling P, 2003, J MOL BIOL, V326, P639, DOI 10.1016/S0022-2836(02)01440-7
   SCHNEIDER I, 1972, J EMBRYOL EXP MORPH, V27, P353
   Shanmugavelu M, 2000, J BIOL CHEM, V275, P1802, DOI 10.1074/jbc.275.3.1802
   STEPIEN G, 1988, INSECT BIOCHEM, V18, P313, DOI 10.1016/0020-1790(88)90096-0
   Stolc V, 2004, SCIENCE, V306, P655, DOI 10.1126/science.1101312
   Taylor AB, 2001, STRUCTURE, V9, P615, DOI 10.1016/S0969-2126(01)00621-9
   VINCE RK, 1977, INSECT BIOCHEM, V7, P115, DOI 10.1016/0020-1790(77)90003-8
   Weiss C, 1999, P NATL ACAD SCI USA, V96, P8890, DOI 10.1073/pnas.96.16.8890
   WICKHAM TJ, 1992, BIOTECHNOL PROGR, V8, P391, DOI 10.1021/bp00017a003
   Wiedemann N, 2004, J BIOL CHEM, V279, P14473, DOI 10.1074/jbc.R400003200
   WROBLEWSKI VJ, 1990, ARCH BIOCHEM BIOPHYS, V278, P461, DOI 10.1016/0003-9861(90)90285-7
NR 36
TC 10
Z9 13
U1 0
U2 3
PU PERGAMON-ELSEVIER SCIENCE LTD
PI OXFORD
PA THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND
SN 0965-1748
J9 INSECT BIOCHEM MOLEC
JI Insect Biochem. Mol. Biol.
PD FEB
PY 2007
VL 37
IS 2
BP 155
EP 163
DI 10.1016/j.ibmb.2006.11.003
PG 9
WC Biochemistry & Molecular Biology; Entomology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Entomology
GA 136QR
UT WOS:000244239700006
PM 17244544
DA 2025-04-10
ER

PT J
AU Bikis, C
   Moris, D
   Vasileiou, I
   Patsouris, E
   Theocharis, S
AF Bikis, Christos
   Moris, Demetrios
   Vasileiou, Ioanna
   Patsouris, Eustratios
   Theocharis, Stamatios
TI FAK/Src family of kinases: protective or aggravating factor for ischemia
   reperfusion injury in nervous system?
SO EXPERT OPINION ON THERAPEUTIC TARGETS
LA English
DT Review
DE focal adhesion kinase; ischemia-reperfusion injury; nervous system; Src
ID FOCAL ADHESION KINASE; TRANSIENT CEREBRAL-ISCHEMIA; RECEPTOR SUBUNIT 2A;
   INCREASED TYROSINE PHOSPHORYLATION; OXYGEN-GLUCOSE DEPRIVATION;
   ENDOTHELIAL GROWTH-FACTOR; ACTIVATED PROTEIN-KINASE; GATED
   CALCIUM-CHANNELS; D-ASPARTATE RECEPTOR; BRAIN ISCHEMIA
AB Introduction: The focal adhesion kinase (FAK) and the Src families of kinases are subfamilies of the non-receptor protein tyrosine kinases. FAK activity is regulated by gene amplification, alternative splicing and phosporylation/dephosphorylation. FAK/Src complex has been found to participate through various pathways in neuronal models of ischemia-reperfusion injury (IRI) with conflicting results. The aim of the present review is to summarize the currently available data on this subject.
   Areas covered: The MEDLINE/PubMed database was searched for publications with the medical subject heading IRI and FAK and/or Src, nervous system. We restricted our search till 2014. We identified 93 articles that were available in English as abstracts or/and full-text articles that were deemed appropriate for our review.
   Expert opinion: FAK has been found to have a beneficial preconditioning effect on IRI through activation via the protein kinase C (PKC) pathway by anesthetic agents. Of great importance are the interactions between FAK/Src and VEGF that has been already detected as a protective mean for IRI. The effect of VEGF administration might depend on dose as well as on time of administration. A Ca2+/calmodulin-dependent protein kinase II or PKC inhibitors seem to have protective effects on IRI by inhibiting ion channels activation.
C1 [Bikis, Christos; Moris, Demetrios; Vasileiou, Ioanna; Patsouris, Eustratios; Theocharis, Stamatios] Univ Athens, Athens 11474, Greece.
C3 National & Kapodistrian University of Athens
RP Moris, D (corresponding author), Univ Athens, Anastasiou Gennadiou 56, Athens 11474, Greece.
EM dimmoris@yahoo.com
RI Theocharis, Serafeim/ABC-9663-2021
OI Moris, Dimitrios/0000-0002-5276-0699
CR Ali DW, 2001, CURR OPIN NEUROBIOL, V11, P336, DOI 10.1016/S0959-4388(00)00216-6
   Armendariz BG, 2014, EUR J NEUROSCI
   Arundine M, 2004, CELL MOL LIFE SCI, V61, P657, DOI 10.1007/s00018-003-3319-x
   Ben-Mahdi MH, 2000, ANTIOXID REDOX SIGN, V2, P789, DOI 10.1089/ars.2000.2.4-789
   Bisht B, 2008, J PHYSIOL-LONDON, V586, P3825, DOI 10.1113/jphysiol.2008.157107
   Bradbury P, 2014, J BIOL CHEM, V289, P24792, DOI 10.1074/jbc.M113.544106
   Brown MT, 1996, BBA-REV CANCER, V1287, P121, DOI 10.1016/0304-419X(96)00003-0
   Burnett CA, 2005, BIOORGAN MED CHEM, V13, P3763, DOI 10.1016/j.bmc.2005.03.024
   Carragher NO, 2001, J BIOL CHEM, V276, P4270, DOI 10.1074/jbc.M008972200
   CHAN PH, 1994, BRAIN PATHOL, V4, P59
   Chatzizacharias NA, 2008, TOXICOLOGY, V245, P1, DOI 10.1016/j.tox.2007.12.003
   Chen M, 2003, NEUROSCI LETT, V339, P29, DOI 10.1016/S0304-3940(02)01439-8
   Cheung HH, 2000, J CEREBR BLOOD F MET, V20, P505, DOI 10.1097/00004647-200003000-00009
   Corvol JC, 2005, J BIOL CHEM, V280, P660, DOI 10.1074/jbc.M411312200
   Dahmani S, 2005, ANESTHESIOLOGY, V103, P969, DOI 10.1097/00000542-200511000-00011
   Dahmani S, 2004, ANESTHESIOLOGY, V101, P344, DOI 10.1097/00000542-200408000-00015
   Dahmani S, 2004, BRIT J ANAESTH, V93, P270, DOI 10.1093/bja/aeh188
   Dalton GD, 2013, CELL SIGNAL, V25, P1665, DOI 10.1016/j.cellsig.2013.03.020
   Deramaudt TB, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0092059
   Derkinderen P, 1996, SCIENCE, V273, P1719, DOI 10.1126/science.273.5282.1719
   Eliceiri BP, 1999, MOL CELL, V4, P915, DOI 10.1016/S1097-2765(00)80221-X
   Fang XQ, 2014, PLOS ONE, V9, DOI 10.1371/journal.pone.0107134
   Fujimoto S, 2004, NEUROSCI RES, V50, P179, DOI 10.1016/j.neures.2004.06.013
   Girault JA, 1999, TRENDS NEUROSCI, V22, P257, DOI 10.1016/S0166-2236(98)01358-7
   Guo J, 2004, NEUROSCI LETT, V355, P177, DOI 10.1016/j.neulet.2003.10.076
   Gupta A, 2012, BBA-MOL BASIS DIS, V1822, P1030, DOI 10.1016/j.bbadis.2012.02.011
   Han HY, 2013, PLOS ONE, V8, DOI 10.1371/journal.pone.0064839
   Hayashi T, 1998, J CEREBR BLOOD F MET, V18, P887, DOI 10.1097/00004647-199808000-00009
   Hou XY, 2003, BRAIN RES, V979, P43, DOI 10.1016/S0006-8993(03)02845-2
   Hou XY, 2002, BRAIN RES, V955, P123, DOI 10.1016/S0006-8993(02)03376-0
   Hu BR, 1998, J NEUROSCI, V18, P625
   Huang YQ, 2001, NEURON, V29, P485, DOI 10.1016/S0896-6273(01)00220-3
   Igishi T, 1999, J BIOL CHEM, V274, P30738, DOI 10.1074/jbc.274.43.30738
   Jaeschke H, 2002, HEPATOLOGY, V36, P761, DOI 10.1053/jhep.2002.36038
   Kandilis AN, 2014, EXPERT OPIN INV DRUG, V23, P67, DOI 10.1517/13543784.2013.840287
   King WG, 1997, MOL CELL BIOL, V17, P4406, DOI 10.1128/MCB.17.8.4406
   KINOUCHI H, 1991, P NATL ACAD SCI USA, V88, P11158, DOI 10.1073/pnas.88.24.11158
   Kratimenos P, 2014, EXPERT OPIN THER TAR, V18, P1395, DOI 10.1517/14728222.2014.952280
   Kumai Y, 2007, J CEREBR BLOOD F MET, V27, P1152, DOI 10.1038/sj.jcbfm.9600420
   KUMAR S, 1992, BIOCHEM BIOPH RES CO, V185, P1155, DOI 10.1016/0006-291X(92)91747-E
   Lambeth JD, 2004, NAT REV IMMUNOL, V4, P181, DOI 10.1038/nri1312
   Law SF, 1996, MOL CELL BIOL, V16, P3327
   Lee BY, 2014, PHARMACOL THERAPEUT, pS0163
   Lesay A, 2001, NEUROREPORT, V12, P2111, DOI 10.1097/00001756-200107200-00014
   Levkau B, 1998, J EXP MED, V187, P579, DOI 10.1084/jem.187.4.579
   Lin EH, 2004, EXP CELL RES, V293, P1, DOI 10.1016/j.yexcr.2003.09.008
   LITTAUER A, 1992, AM J PHYSIOL, V262, pG1015, DOI 10.1152/ajpgi.1992.262.6.G1015
   Liu Y, 2005, NEUROSCI LETT, V379, P55, DOI 10.1016/j.neulet.2004.12.054
   Liu Y, 2003, NEUROSCI LETT, V348, P127, DOI 10.1016/S0304-3940(03)00618-9
   Liu Y, 2003, BRAIN RES, V972, P142, DOI 10.1016/S0006-8993(03)02519-8
   Liu Y, 2001, BRAIN RES, V909, P51, DOI 10.1016/S0006-8993(01)02619-1
   Ma J, 2004, NEUROSCI RES, V49, P357, DOI 10.1016/j.neures.2004.04.004
   Masson-Gadais B, 2003, CELL STRESS CHAPERON, V8, P37, DOI 10.1379/1466-1268(2003)8<37:IVRFVA>2.0.CO;2
   MCCORD JM, 1985, NEW ENGL J MED, V312, P159
   Neumar RW, 2001, EXP NEUROL, V170, P27, DOI 10.1006/exnr.2001.7708
   Nicodemo AA, 2010, MOL BRAIN, V3, DOI 10.1186/1756-6606-3-4
   Nisato Riccardo E., 2003, Angiogenesis, V6, P105, DOI 10.1023/B:AGEN.0000011801.98187.f2
   Paul R, 2001, NAT MED, V7, P222, DOI 10.1038/84675
   Pei L, 2000, ACTA PHARMACOL SIN, V21, P715
   Qu H, 2014, J BIOL CHEM, V289, P31001, DOI 10.1074/jbc.M114.580811
   Ribeiro A, 2013, NEUROSCIENCE, V248, P67, DOI 10.1016/j.neuroscience.2013.05.057
   Richardson A, 1996, NATURE, V380, P538, DOI 10.1038/380538a0
   Sasaki T, 2005, STROKE, V36, P2457, DOI 10.1161/01.STR.0000185672.10390.30
   Scheele C, 2007, FASEB J, V21, P3653, DOI 10.1096/fj.07-8520com
   Schlaepfer DD, 1998, MOL CELL BIOL, V18, P2571, DOI 10.1128/MCB.18.5.2571
   Schlaepfer DD, 1998, TRENDS CELL BIOL, V8, P151, DOI 10.1016/S0962-8924(97)01172-0
   Schoch HJ, 2002, BRAIN, V125, P2549, DOI 10.1093/brain/awf257
   Schwock J, 2010, EXPERT OPIN THER TAR, V14, P77, DOI 10.1517/14728220903460340
   Shani V, 2009, J MOL NEUROSCI, V37, P50, DOI 10.1007/s12031-008-9113-3
   Sharma BK, 1998, METAB BRAIN DIS, V13, P1, DOI 10.1023/A:1020670610512
   Shimamura N, 2006, STROKE, V37, P1902, DOI 10.1161/01.STR.0000226991.27540.f2
   Sigaut S, 2009, ANESTH ANALG, V108, P601, DOI 10.1213/ane.0b013e31818e2018
   Tachibana K, 1997, J BIOL CHEM, V272, P29083, DOI 10.1074/jbc.272.46.29083
   Tamura M, 1999, J BIOL CHEM, V274, P20693, DOI 10.1074/jbc.274.29.20693
   Tang KQ, 1999, BIOCHEM BIOPH RES CO, V264, P127, DOI 10.1006/bbrc.1999.1496
   Tang LJ, 2012, MOL CELL BIOCHEM, V365, P363, DOI 10.1007/s11010-012-1280-4
   Tian DH, 2000, J NEUROSCI, V20, P6478, DOI 10.1523/JNEUROSCI.20-17-06478.2000
   Toledo-Pereyra LH, 2008, J INVEST SURG, V21, P215, DOI 10.1080/08941930802130149
   van Bruggen N, 1999, J CLIN INVEST, V104, P1613, DOI 10.1172/JCI8218
   Wang YM, 2005, BRAIN, V128, P52, DOI 10.1093/brain/awh325
   White BC, 2000, J NEUROL SCI, V179, P1, DOI 10.1016/S0022-510X(00)00386-5
   Xu J, 2008, J BIOL CHEM, V283, P29355, DOI 10.1074/jbc.M800393200
   Xu WQ, 1997, NATURE, V385, P595, DOI 10.1038/385595a0
   Yang S, 2004, P W PHARMACOL SOC, P54
   Zablocka B, 1998, BRAIN RES, V779, P254, DOI 10.1016/S0006-8993(97)00906-2
   ZACHARY I, 1992, CELL, V71, P891, DOI 10.1016/0092-8674(92)90385-P
   Zalewska T, 2005, INT J DEV NEUROSCI, V23, P657, DOI 10.1016/j.ijdevneu.2005.05.010
   Zalewska T, 2005, BRAIN RES, V1042, P214, DOI 10.1016/j.brainres.2005.02.025
   Zalewska T, 2003, BRAIN RES, V977, P62, DOI 10.1016/S0006-8993(03)02742-2
   Zhan RZ, 2001, J CEREBR BLOOD F MET, V21, P529, DOI 10.1097/00004647-200105000-00007
   Zhou D, 2002, FEBS LETT, V525, P164, DOI 10.1016/S0014-5793(02)03091-0
   Ziemka-Nalecz M, 2003, NEUROCHEM INT, V42, P205, DOI 10.1016/S0197-0186(02)00096-7
   Ziemka-Nalecz M, 2007, NEUROCHEM INT, V51, P405, DOI 10.1016/j.neuint.2007.04.008
NR 93
TC 4
Z9 4
U1 0
U2 34
PU TAYLOR & FRANCIS LTD
PI ABINGDON
PA 4 PARK SQUARE, MILTON PARK, ABINGDON OX14 4RN, OXON, ENGLAND
SN 1472-8222
EI 1744-7631
J9 EXPERT OPIN THER TAR
JI Expert Opin. Ther. Targets
PD APR
PY 2015
VL 19
IS 4
BP 539
EP 549
DI 10.1517/14728222.2014.990374
PG 11
WC Pharmacology & Pharmacy
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Pharmacology & Pharmacy
GA CD5PH
UT WOS:000351139800010
PM 25474489
DA 2025-04-10
ER

PT J
AU Shah, MY
   Vasanthakumar, A
   Barnes, NY
   Figueroa, ME
   Kamp, A
   Hendrick, C
   Ostler, KR
   Davis, EM
   Lin, S
   Anastasi, J
   Le Beau, MM
   Moskowitz, IP
   Melnick, A
   Pytel, P
   Godley, LA
AF Shah, Mrinal Y.
   Vasanthakumar, Aparna
   Barnes, Natalie Y.
   Figueroa, Maria E.
   Kamp, Anna
   Hendrick, Christopher
   Ostler, Kelly R.
   Davis, Elizabeth M.
   Lin, Shang
   Anastasi, John
   Le Beau, Michelle M.
   Moskowitz, Ivan P.
   Melnick, Ari
   Pytel, Peter
   Godley, Lucy A.
TI DNMT3B7, a Truncated DNMT3B Isoform Expressed in Human Tumors, Disrupts
   Embryonic Development and Accelerates Lymphomagenesis
SO CANCER RESEARCH
LA English
DT Article
ID ALTERNATIVE SPLICING MARKERS; CELL LUNG-CANCER; DNA METHYLATION;
   MAMMALIAN DEVELOPMENT; DELTA-DNMT3B VARIANTS; TRANSGENIC MICE; ICF
   SYNDROME; IN-VIVO; METHYLTRANSFERASES; HYPOMETHYLATION
AB Epigenetic changes are among the most common alterations observed in cancer cells, yet the mechanism by which cancer cells acquire and maintain abnormal DNA methylation patterns is not understood. Cancer cells have an altered distribution of DNA methylation and express aberrant DNA methyltransferase 3B transcripts, which encode truncated proteins, some of which lack the COOH-terminal catalytic domain. To test if a truncated DNMT3B isoform disrupts DNA methylation in vivo, we constructed two lines of transgenic mice expressing DNMT3B7, a truncated DNMT3B isoform commonly found in cancer cells. DNMT3B7 transgenic mice exhibit altered embryonic development, including lymphopenia, craniofacial abnormalities, and cardiac defects, similar to Dnmt3b-deficient animals, but rarely develop cancer. However, when DNMT3B7 transgenic mice are bred with E mu-Myc transgenic mice, which model aggressive B-cell lymphoma, DNMT3B7 expression increases the frequency of mediastinal lymphomas in E mu-Myc animals. E mu-Myc/DNMT3B7 mediastinal lymphomas have more chromosomal rearrangements, increased global DNA methylation levels, and more locus-specific perturbations in DNA methylation patterns compared with E mu-Myc lymphomas. These data represent the first in vivo modeling of cancer-associated DNA methylation changes and suggest that truncated DNMT3B isoforms contribute to the redistribution of DNA methylation characterizing virtually every human tumor. Cancer Res; 70(14); 5840-50. (C)2010 AACR.
C1 [Shah, Mrinal Y.; Vasanthakumar, Aparna; Barnes, Natalie Y.; Hendrick, Christopher; Ostler, Kelly R.; Davis, Elizabeth M.; Le Beau, Michelle M.; Godley, Lucy A.] Univ Chicago, Hematol Oncol Sect, Dept Med, Chicago, IL 60637 USA.
   [Kamp, Anna; Moskowitz, Ivan P.] Univ Chicago, Inst Mol Pediat Sci, Dept Pediat, Chicago, IL 60637 USA.
   [Lin, Shang] Univ Chicago, Biostat Core Facil, Chicago, IL 60637 USA.
   [Lin, Shang; Le Beau, Michelle M.; Godley, Lucy A.] Univ Chicago, Ctr Comprehens Canc, Chicago, IL 60637 USA.
   [Anastasi, John; Moskowitz, Ivan P.; Pytel, Peter] Univ Chicago, Dept Pathol, Chicago, IL 60637 USA.
   [Figueroa, Maria E.; Melnick, Ari] Weill Cornell Med Coll, Dept Hematol Oncol, New York, NY USA.
C3 University of Chicago; University of Chicago; University of Chicago;
   University of Chicago; Robert H. Lurie Comprehensive Cancer Center;
   University of Chicago; Cornell University; Weill Cornell Medicine
RP Godley, LA (corresponding author), Univ Chicago, Hematol Oncol Sect, Dept Med, 5841 S Maryland Ave,MC2115, Chicago, IL 60637 USA.
EM lgodley@medicine.bsd.uchicago.edu
RI Figueroa, Maria/AAE-8662-2019; SchneiderKamp, Anna/KHX-9828-2024
OI Figueroa, Maria Eugenia/0000-0003-4887-4981; Moskowitz,
   Ivan/0000-0003-0014-4963; Young, Natalie/0000-0002-3263-4847
FU Pharmion; NIH/National Cancer Institute [R01 CA129831]; American Cancer
   Society [08-02]; Kimmel Scholars Program; Leukemia & Lymphoma Society
   Specialized Center of Research [7410-07]
FX L.A. Godley: commercial research grant, Pharmion. The other authors
   disclosed no potential conflicts of interest.NIH/National Cancer
   Institute R01 grant CA129831, American Cancer Society grant 08-02,
   Kimmel Scholars Program (L. A. Godley), and Leukemia & Lymphoma Society
   Specialized Center of Research grant 7410-07 (M. M. Le Beau).
CR ADAMS JM, 1985, NATURE, V318, P533, DOI 10.1038/318533a0
   [Anonymous], 2009, R LANG ENV STAT COMP
   Bernstein BE, 2007, CELL, V128, P669, DOI 10.1016/j.cell.2007.01.033
   Bestor TH, 2000, HUM MOL GENET, V9, P2395, DOI 10.1093/hmg/9.16.2395
   Brenner C, 2005, EMBO J, V24, P336, DOI 10.1038/sj.emboj.7600509
   Bröske AM, 2009, NAT GENET, V41, P1207, DOI 10.1038/ng.463
   Chen ZX, 2005, J CELL BIOCHEM, V95, P902, DOI 10.1002/jcb.20447
   Corcoran LM, 1999, J IMMUNOL METHODS, V228, P131, DOI 10.1016/S0022-1759(99)00094-0
   Dang CV, 2006, SEMIN CANCER BIOL, V16, P253, DOI 10.1016/j.semcancer.2006.07.014
   Fackenthal JD, 2008, DIS MODEL MECH, V1, P37, DOI 10.1242/dmm.000331
   Fan T, 2008, EPIGENETICS-US, V3, P134, DOI 10.4161/epi.3.3.6252
   Figueroa ME, 2010, CANCER CELL, V17, P13, DOI 10.1016/j.ccr.2009.11.020
   Figueroa ME, 2009, BLOOD, V114, P3448, DOI 10.1182/blood-2009-01-200519
   Figueroa Maria E., 2009, V538, P395, DOI 10.1007/978-1-59745-418-6_20
   FRITH CH, 1990, LAB ANIM SCI, V40, P418
   Gaudet F, 2003, SCIENCE, V300, P489, DOI 10.1126/science.1083558
   Gopalakrishnan S, 2009, MOL CANCER RES, V7, P1622, DOI 10.1158/1541-7786.MCR-09-0018
   Goto Y, 2009, CANCER RES, V69, P9073, DOI 10.1158/0008-5472.CAN-09-1595
   Hagleitner MM, 2008, J MED GENET, V45, P93, DOI 10.1136/jmg.2007.053397
   HARRIS AW, 1988, J EXP MED, V167, P353, DOI 10.1084/jem.167.2.353
   Hata K, 2002, DEVELOPMENT, V129, P1983
   Helmrich A, 2005, ONCOGENE, V24, P4174, DOI 10.1038/sj.onc.1208600
   Howard G, 2008, ONCOGENE, V27, P404, DOI 10.1038/sj.onc.1210631
   Huang YW, 2009, CANCER RES, V69, P9038, DOI 10.1158/0008-5472.CAN-09-1499
   Irizarry RA, 2009, NAT GENET, V41, P178, DOI 10.1038/ng.298
   Jia D, 2007, NATURE, V449, P248, DOI 10.1038/nature06146
   Jones PA, 2007, CELL, V128, P683, DOI 10.1016/j.cell.2007.01.029
   Kelly TLJ, 2003, J ANDROL, V24, P822
   Khulan B, 2006, GENOME RES, V16, P1046, DOI 10.1101/gr.5273806
   Klinck R, 2008, CANCER RES, V68, P657, DOI 10.1158/0008-5472.CAN-07-2580
   Le Beau MM, 2002, BLOOD, V99, P2985, DOI 10.1182/blood.V99.8.2985
   LI E, 1992, CELL, V69, P915, DOI 10.1016/0092-8674(92)90611-F
   Li E, 2002, NAT REV GENET, V3, P662, DOI 10.1038/nrg887
   *NCBI, GEN EXPR OMN REP
   Okano M, 1999, CELL, V99, P247, DOI 10.1016/S0092-8674(00)81656-6
   Ostler K, 2007, ONCOGENE, V26, P5553, DOI 10.1038/sj.onc.1210351
   Song LG, 2005, ANAL CHEM, V77, P504, DOI 10.1021/ac0489420
   Stumpel DJPM, 2009, BLOOD, V114, P5490, DOI 10.1182/blood-2009-06-227660
   Ueda Y, 2006, DEVELOPMENT, V133, P1183, DOI 10.1242/dev.02293
   Venables JP, 2008, CANCER RES, V68, P9525, DOI 10.1158/0008-5472.CAN-08-1769
   Wang J, 2007, CANCER RES, V67, P10647, DOI 10.1158/0008-5472.CAN-07-1337
   Wang J, 2006, CANCER RES, V66, P8361, DOI 10.1158/0008-5472.CAN-06-2031
   Wang L, 2006, INT J ONCOL, V29, P201
NR 43
TC 54
Z9 65
U1 0
U2 1
PU AMER ASSOC CANCER RESEARCH
PI PHILADELPHIA
PA 615 CHESTNUT ST, 17TH FLOOR, PHILADELPHIA, PA 19106-4404 USA
SN 0008-5472
EI 1538-7445
J9 CANCER RES
JI Cancer Res.
PD JUL 15
PY 2010
VL 70
IS 14
BP 5840
EP 5850
DI 10.1158/0008-5472.CAN-10-0847
PG 11
WC Oncology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Oncology
GA 626GV
UT WOS:000279955300020
PM 20587527
OA Green Accepted, Green Submitted, Bronze
DA 2025-04-10
ER

PT J
AU Semba, RD
   Zhang, PB
   Zhu, M
   Fabbri, E
   Gonzalez-Freire, M
   Moaddel, R
   Geng-Spyropoulos, M
   Ferrucci, L
AF Semba, Richard D.
   Zhang, Pingbo
   Zhu, Min
   Fabbri, Elisa
   Gonzalez-Freire, Marta
   Moaddel, Ruin
   Geng-Spyropoulos, Minghui
   Ferrucci, Luigi
TI A targeted proteomic assay for the measurement of plasma proteoforms
   related to human aging phenotypes
SO PROTEOMICS
LA English
DT Article
DE Aging; Eotaxin; Follistatin; Growth/differentiation factor 8; Growth
   /differentiation factor 11; Oxytocin; WFIKKN1; WFIKKN2
ID SKELETAL-MUSCLE; CARDIOVASCULAR-DISEASE; SERUM CONCENTRATIONS;
   MASS-SPECTROMETRY; LATENT MYOSTATIN; LC-MS/MS; FOLLISTATIN; OXYTOCIN;
   GROWTH; BINDING
AB Circulating polypeptides and proteins have been implicated in reversing or accelerating aging phenotypes, including growth/differentiation factor 8 (GDF8), GDF11, eotaxin, and oxytocin. These proteoforms, which are defined as the protein products arising from a single gene due to alternative splicing and PTMs, have been challenging to study. Both GDF8 and GDF11 have known antagonists such as follistatin (FST), and WAP, Kazal, immunoglobulin, Kunitz, and NTR domain-containing proteins 1 and 2 (WFIKKN1, WFIKKN2). We developed a novel multiplexed SRM assay using LC-MS/MS to measure five proteins related to GDF8 and GDF11 signaling, and in addition, eotaxin, and oxytocin. Eighteen peptides consisting of 54 transitions were monitored and validated in pooled human plasma. In 24 adults, the mean (SD) concentrations (ng/mL) were as follows: GDF8 propeptide, 11.0 (2.4); GDF8 mature protein, 25.7 (8.0); GDF11 propeptide, 21.3 (10.9); GDF11 mature protein, 16.5 (12.4); FST, 29.8 (7.1); FST cleavage form FST303, 96.4 (69.2); WFIKKN1, 38.3 (8.3); WFIKKN2, 32.2 (10.5); oxytocin, 1.9 (0.9); and eotaxin, 2.3 (0.5). This novel multiplexed SRM assay should facilitate the study of the relationships of these proteoforms with major aging phenotypes.
C1 [Semba, Richard D.; Zhang, Pingbo; Geng-Spyropoulos, Minghui] Johns Hopkins Univ, Sch Med, Wilmer Eye Inst, Smith Bldg M015,400 N Broadway, Baltimore, MD 21287 USA.
   [Zhu, Min; Fabbri, Elisa; Gonzalez-Freire, Marta; Moaddel, Ruin; Ferrucci, Luigi] NIA, NIH, Baltimore, MD 21224 USA.
C3 Johns Hopkins University; Johns Hopkins Medicine; National Institutes of
   Health (NIH) - USA; NIH National Institute on Aging (NIA)
RP Semba, RD (corresponding author), Johns Hopkins Univ, Sch Med, Wilmer Eye Inst, Smith Bldg M015,400 N Broadway, Baltimore, MD 21287 USA.
EM rdsemba@jhmi.edu
RI Gonzalez-Freire, Marta/ABG-1197-2020; Moaddel, Ruin/AAE-3378-2020;
   Ferrucci, Luigi/AED-9724-2022
OI Moaddel, Ruin/0000-0002-6812-0127; Ferrucci, Luigi/0000-0002-6273-1613;
   FABBRI, ELISA/0000-0002-1017-7892; Gonzalez-Freire,
   Marta/0000-0001-9741-2826
FU National Institutes of Health [R56 AG052973, R01 EY024596, R01
   AG027012]; Intramural Research Program of the National Institute on
   Aging
FX This work was supported by the National Institutes of Health grants R56
   AG052973, R01 EY024596, R01 AG027012, and the Intramural Research
   Program of the National Institute on Aging.
CR [Anonymous], 2016, QUANTIKINE ELISA GDF
   Bergen HR, 2015, SKELET MUSCLE, V5, DOI 10.1186/s13395-015-0047-5
   Billhult A, 2009, AUTON NEUROSCI-BASIC, V150, P111, DOI 10.1016/j.autneu.2009.03.010
   Brandtzaeg OK, 2016, SCI REP-UK, V6, DOI 10.1038/srep31693
   Ceglarek U, 2013, PROTEOM CLIN APPL, V7, P794, DOI 10.1002/prca.201300034
   Crown SE, 2006, J BIOL CHEM, V281, P25438, DOI 10.1074/jbc.M601518200
   Crump MP, 1998, J BIOL CHEM, V273, P22471, DOI 10.1074/jbc.273.35.22471
   Domanski D, 2012, PROTEOMICS, V12, P1222, DOI 10.1002/pmic.201100568
   Egerman MA, 2015, CELL METAB, V22, P164, DOI 10.1016/j.cmet.2015.05.010
   Elabd C, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms5082
   Farrah T, 2011, MOL CELL PROTEOMICS, V10, DOI 10.1074/mcp.M110.006353
   Furihata T, 2016, INT J CARDIOL, V220, P483, DOI 10.1016/j.ijcard.2016.06.231
   Goldman M, 2008, SCHIZOPHR RES, V98, P247, DOI 10.1016/j.schres.2007.09.019
   Green LA, 2001, BIOL PSYCHIAT, V50, P609, DOI 10.1016/S0006-3223(01)01139-8
   Hansen J, 2013, DIABETES-METAB RES, V29, P463, DOI 10.1002/dmrr.2415
   Hill JJ, 2002, J BIOL CHEM, V277, P40735, DOI 10.1074/jbc.M206379200
   Hill JJ, 2003, MOL ENDOCRINOL, V17, P1144, DOI 10.1210/me.2002-0366
   Ho DM, 2010, MECH DEVELOP, V127, P485, DOI 10.1016/j.mod.2010.08.004
   Hofmann M, 2015, EXP GERONTOL, V64, P35, DOI 10.1016/j.exger.2015.02.008
   Holt-Lunstad J, 2008, PSYCHOSOM MED, V70, P976, DOI 10.1097/PSY.0b013e318187aef7
   Hughes RD, 2003, EUR J GASTROEN HEPAT, V15, P127, DOI 10.1097/00042737-200302000-00004
   Kondás K, 2008, J BIOL CHEM, V283, P23677, DOI 10.1074/jbc.M803025200
   Kuzyk Michael A, 2013, Methods Mol Biol, V1023, P53, DOI 10.1007/978-1-4614-7209-4_4
   Lee SJ, 2001, P NATL ACAD SCI USA, V98, P9306, DOI 10.1073/pnas.151270098
   Liebler DC, 2013, BIOCHEMISTRY-US, V52, P3797, DOI 10.1021/bi400110b
   McPherron Alexandra C., 2010, Immunology Endocrine & Metabolic Agents in Medicinal Chemistry, V10, P217
   Palandra J, 2016, PROTEOM CLIN APPL, V10, P597, DOI 10.1002/prca.201500112
   Panizzutti B, 2015, J AFFECT DISORDERS, V182, P64, DOI 10.1016/j.jad.2014.12.010
   Peiris HN, 2014, J PROTEOME RES, V13, P3802, DOI 10.1021/pr5004642
   Ratkevicius A, 2011, J GERONTOL A-BIOL, V66, P620, DOI 10.1093/gerona/glr025
   Saremi A, 2010, MOL CELL ENDOCRINOL, V317, P25, DOI 10.1016/j.mce.2009.12.019
   Schafer MJ, 2016, CELL METAB, V23, P1207, DOI 10.1016/j.cmet.2016.05.023
   Schneyer AL, 2008, ENDOCRINOLOGY, V149, P4589, DOI 10.1210/en.2008-0259
   SHIMASAKI S, 1988, P NATL ACAD SCI USA, V85, P4218, DOI 10.1073/pnas.85.12.4218
   Shurin GV, 2007, CYTOKINE, V39, P123, DOI 10.1016/j.cyto.2007.06.006
   Sinha M, 2014, SCIENCE, V344, P649, DOI 10.1126/science.1251152
   Smith LM, 2013, NAT METHODS, V10, P186, DOI 10.1038/nmeth.2369
   SUGINO K, 1993, J BIOL CHEM, V268, P15579
   Szeto A, 2011, PSYCHOSOM MED, V73, P393, DOI 10.1097/PSY.0b013e31821df0c2
   Szláma G, 2013, FEBS J, V280, P3822, DOI 10.1111/febs.12377
   Thies RS, 2001, GROWTH FACTORS, V18, P251
   Villeda SA, 2011, NATURE, V477, P90, DOI 10.1038/nature10357
   Weisman O, 2013, PSYCHONEUROENDOCRINO, V38, P694, DOI 10.1016/j.psyneuen.2012.08.011
   Wintgens KF, 2012, CLIN CHIM ACTA, V413, P1288, DOI 10.1016/j.cca.2012.04.023
   Wolfman NM, 2003, P NATL ACAD SCI USA, V100, P15842, DOI 10.1073/pnas.2534946100
   Yano S, 2015, PLOS ONE, V10, DOI 10.1371/journal.pone.0141035
   Zak PJ, 2005, HORM BEHAV, V48, P522, DOI 10.1016/j.yhbeh.2005.07.009
   Zhu M., 2017, Proteomics, V17
NR 48
TC 14
Z9 14
U1 0
U2 10
PU WILEY
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 1615-9853
EI 1615-9861
J9 PROTEOMICS
JI Proteomics
PD AUG
PY 2017
VL 17
IS 15-16
AR 1600232
DI 10.1002/pmic.201600232
PG 12
WC Biochemical Research Methods; Biochemistry & Molecular Biology
WE Science Citation Index Expanded (SCI-EXPANDED); Social Science Citation Index (SSCI)
SC Biochemistry & Molecular Biology
GA FE3WJ
UT WOS:000408146100001
PM 28508553
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Salmerón, C
   Harter, TS
   Kwan, GT
   Roa, JN
   Blair, SD
   Rummer, JL
   Shiels, HA
   Goss, GG
   Wilson, RW
   Tresguerres, M
AF Salmeron, Cristina
   Harter, Till S.
   Kwan, Garfield T.
   Roa, Jinae N.
   Blair, Salvatore D.
   Rummer, Jodie L.
   Shiels, Holly A.
   Goss, Greg G.
   Wilson, Rod W.
   Tresguerres, Martin
TI Molecular and biochemical characterization of the bicarbonate-sensing
   soluble adenylyl cyclase from a bony fish, the rainbow trout
   Oncorhynchus mykiss
SO INTERFACE FOCUS
LA English
DT Article
DE cAMP; CO2; Golgi; microdomain; pH sensing; sAC
ID CELLULAR MECHANISMS; GILL; TRANSMEMBRANE; EXPRESSION; DEFINES; ATPASE;
   SECRETION; TRANSPORT; EVOLUTION; ISOFORMS
AB Soluble adenylyl cyclase (sAC) is a HCO3--stimulated enzyme that produces the ubiquitous signalling molecule cAMP, and deemed an evolutionarily conserved acid-base sensor. However, its presence is not yet confirmed in bony fishes, the most abundant and diverse of vertebrates. Here, we identified sAC genes in various cartilaginous, ray-finned and lobe-finned fish species. Next, we focused on rainbow trout sAC (rtsAC) and identified 20 potential alternative spliced mRNAs coding for protein isoforms ranging in size from 28 to 186 kDa. Biochemical and kinetic analyses on purified recombinant rtsAC protein determined stimulation by HCO3- at physiologically relevant levels for fish internal fluids (EC50 similar to 7 mM). rtsAC activity was sensitive to KH7, LRE1, and DIDS (established inhibitors of sAC from other organisms), and insensitive to forskolin and 2,5-dideoxyadenosine (modulators of transmembrane adenylyl cyclases). Western blot and immunocytochemistry revealed high rtsAC expression in gill ion-transporting cells, hepatocytes, red blood cells, myocytes and cardiomyocytes. Analyses in the cell line RTgill-W1 suggested that some of the longer rtsAC isoforms may be preferentially localized in the nucleus, the Golgi apparatus and podosomes. These results indicate that sAC is poised to mediate multiple acid-base homeostatic responses in bony fishes, and provide cues about potential novel functions in mammals.
C1 [Salmeron, Cristina; Harter, Till S.; Kwan, Garfield T.; Roa, Jinae N.; Tresguerres, Martin] Univ Calif San Diego, Scripps Inst Oceanog, La Jolla, CA 92093 USA.
   [Salmeron, Cristina] Univ Calif San Diego, Dept Pharmacol, San Diego, CA 92103 USA.
   [Blair, Salvatore D.; Goss, Greg G.] Univ Alberta, Dept Biol Sci, Edmonton, AB, Canada.
   [Blair, Salvatore D.] Winthrop Univ, Dept Biol, Rock Hill, SC 29733 USA.
   [Rummer, Jodie L.] James Cook Univ, Australian Res Council, Ctr Excellence Coral Reef Studies, Townsville, Qld, Australia.
   [Shiels, Holly A.] Univ Manchester, Fac Biol Med & Hlth, Div Cardiovasc Sci, Manchester, Lancs, England.
   [Wilson, Rod W.] Univ Exeter, Dept Biosci, Exeter, Devon, England.
C3 University of California System; University of California San Diego;
   Scripps Institution of Oceanography; University of California System;
   University of California San Diego; University of Alberta; James Cook
   University; University of Manchester; University of Exeter
RP Tresguerres, M (corresponding author), Univ Calif San Diego, Scripps Inst Oceanog, La Jolla, CA 92093 USA.
EM mtresguerres@ucsd.edu
RI Goss, Greg/A-2646-2014; Salmeron, Cristina/CAG-8357-2022; Rummer,
   Jodie/A-6524-2015; Tresguerres, Martin/J-8628-2012
OI Kwan, Garfield/0000-0001-9183-2731; Tresguerres,
   Martin/0000-0002-7090-9266; Salmeron, Cristina/0000-0003-2259-3807;
   Shiels, Holly Alice/0000-0001-5223-5205
FU National Science Foundation (USA) [NSF IOS 1354181, 1754994];
   Biotechnology and Biological Sciences Research Council (UK) [BBSRC
   BB/N013344/1]; UCSD Chancellor's Research Excellence Scholarship (CRES);
   Company of Biologists Travel grant [JEBTF-161115]; Division Of
   Integrative Organismal Systems; Direct For Biological Sciences [1754994]
   Funding Source: National Science Foundation; BBSRC [BB/N013344/1]
   Funding Source: UKRI
FX This work was supported by grants from the National Science Foundation
   (USA) to M.T. (NSF IOS 1354181 and 1754994) and from the Biotechnology
   and Biological Sciences Research Council (UK) to R.W.W. (BBSRC
   BB/N013344/1), a UCSD Chancellor's Research Excellence Scholarship
   (CRES) to M.T. and C.S., a Company of Biologists Travel grant to C.S.
   (JEBTF-161115).
CR Barott KL, 2017, P ROY SOC B-BIOL SCI, V284, DOI 10.1098/rspb.2017.1769
   Bitterman JL, 2013, J PHARMACOL EXP THER, V347, P589, DOI 10.1124/jpet.113.208496
   BOLS NC, 1994, J FISH DIS, V17, P601, DOI 10.1111/j.1365-2761.1994.tb00258.x
   BRAUN T, 1991, METHOD ENZYMOL, V195, P130
   BRAUN T, 1975, P NATL ACAD SCI USA, V72, P1097, DOI 10.1073/pnas.72.3.1097
   Buck J, 1999, P NATL ACAD SCI USA, V96, P79, DOI 10.1073/pnas.96.1.79
   Buck J, 2014, BBA-MOL BASIS DIS, V1842, P2533, DOI 10.1016/j.bbadis.2014.09.009
   CAMERON JN, 1972, J EXP BIOL, V57, P673
   Carvalho ESM, 2012, J COMP PHYSIOL B, V182, P1069, DOI 10.1007/s00360-012-0685-4
   Chaloupka JA, 2006, MOL REPROD DEV, V73, P361, DOI 10.1002/mrd.20409
   Chen J, 2013, BRAIN RES, V1518, P1, DOI 10.1016/j.brainres.2013.04.027
   Chen X, 2014, AM J RESP CELL MOL, V51, P750, DOI 10.1165/rcmb.2013-0542OC
   Chen YQ, 2000, SCIENCE, V289, P625, DOI 10.1126/science.289.5479.625
   Dereeper A, 2008, NUCLEIC ACIDS RES, V36, pW465, DOI 10.1093/nar/gkn180
   Espejo MS, 2020, PFLUG ARCH EUR J PHY, V472, P103, DOI 10.1007/s00424-019-02331-x
   Farrell J, 2008, PLOS ONE, V3, DOI 10.1371/journal.pone.0003251
   Fischer M, 2019, TOXICOL SCI, V169, P353, DOI 10.1093/toxsci/kfz057
   Furimsky M, 2000, J EXP BIOL, V203, P2201
   Galvez F, 2002, AM J PHYSIOL-REG I, V282, pR658, DOI 10.1152/ajpregu.00342.2001
   Geng WD, 2005, AM J PHYSIOL-CELL PH, V288, pC1305, DOI 10.1152/ajpcell.00584.2004
   Geng WD, 2009, J CELL PHYSIOL, V220, P332, DOI 10.1002/jcp.21767
   Gong F, 2010, AM J PHYSIOL-RENAL, V298, pF1162, DOI 10.1152/ajprenal.00645.2009
   Hailey DW, 2012, PLOS GENET, V8, DOI 10.1371/journal.pgen.1002971
   Hallows KR, 2009, J BIOL CHEM, V284, P5774, DOI 10.1074/jbc.M805501200
   Han H, 2005, J EXP MED, V202, P353, DOI 10.1084/jem.20050778
   Heisler N., 1988, P215
   Hess KC, 2005, DEV CELL, V9, P249, DOI 10.1016/j.devcel.2005.06.007
   Jagadeshwaran U, 2010, J EXP BIOL, V213, P295, DOI 10.1242/jeb.037549
   Jaiswal BS, 2001, J BIOL CHEM, V276, P31698, DOI 10.1074/jbc.M011698200
   Kleinboelting S, 2014, P NATL ACAD SCI USA, V111, P3727, DOI 10.1073/pnas.1322778111
   Kwan GT, 2020, J COMP PHYSIOL B, V190, P419, DOI 10.1007/s00360-020-01276-3
   Ladilov Y, 2014, BBA-MOL BASIS DIS, V1842, P2646, DOI 10.1016/j.bbadis.2014.06.034
   Larsen EH, 2014, COMPR PHYSIOL, V4, P405, DOI 10.1002/cphy.c130004
   Lee LEJ, 2009, IN VITRO CELL DEV-AN, V45, P127, DOI 10.1007/s11626-008-9173-2
   Linder JU, 2003, CELL SIGNAL, V15, P1081, DOI 10.1016/S0898-6568(03)00130-X
   Litvin TN, 2003, J BIOL CHEM, V278, P15922, DOI 10.1074/jbc.M212475200
   Magro CM, 2012, ARCH PATHOL LAB MED, V136, P1558, DOI 10.5858/arpa.2011-0617-OA
   Middelhaufe S, 2012, BIOSCIENCE REP, V32, P491, DOI 10.1042/BSR20120051
   NIKINMAA M, 1984, J EXP BIOL, V113, P215
   Nomura M, 2005, GENE, V353, P231, DOI 10.1016/j.gene.2005.04.034
   Nomura M, 2006, CELL MOTIL CYTOSKEL, V63, P582, DOI 10.1002/cm.20147
   Parks SK, 2007, AM J PHYSIOL-CELL PH, V292, pC935, DOI 10.1152/ajpcell.00604.2005
   Paunescu TG, 2008, AM J PHYSIOL-RENAL, V294, pF130, DOI 10.1152/ajprenal.00406.2007
   Ramos LS, 2008, J GEN PHYSIOL, V132, P329, DOI 10.1085/jgp.200810044
   Ramos-Espiritu L, 2016, NAT CHEM BIOL, V12, P838, DOI [10.1038/NCHEMBIO.2151, 10.1038/nchembio.2151]
   Roa JN, 2017, PHYSIOL REP, V5, DOI 10.14814/phy2.13090
   Roa JN, 2016, AM J PHYSIOL-CELL PH, V311, pC340, DOI 10.1152/ajpcell.00089.2016
   Roa JN, 2014, COMP BIOCHEM PHYS A, V174, P29, DOI 10.1016/j.cbpa.2014.04.003
   Roelofs J, 2002, MOL BIOL EVOL, V19, P2239, DOI 10.1093/oxfordjournals.molbev.a004047
   Schirmer I, 2018, PLOS ONE, V13, DOI 10.1371/journal.pone.0192322
   Schmid A, 2007, J GEN PHYSIOL, V130, P99, DOI 10.1085/jgp.200709784
   Schnell S, 2016, NAT PROTOC, V11, P490, DOI 10.1038/nprot.2016.029
   Shiba K, 2014, INT J MOL SCI, V15, P13192, DOI 10.3390/ijms150813192
   Shiels HA, 2014, PHYSIOLOGY, V29, P456, DOI 10.1152/physiol.00015.2014
   Sinclair ML, 2000, MOL REPROD DEV, V56, P6, DOI 10.1002/(SICI)1098-2795(200005)56:1<6::AID-MRD2>3.0.CO;2-M
   Steegborn C, 2014, BBA-MOL BASIS DIS, V1842, P2535, DOI 10.1016/j.bbadis.2014.08.012
   Strazzabosco M, 2009, HEPATOLOGY, V50, P244, DOI 10.1002/hep.22926
   Sun Xing Cai, 2004, BMC Physiol, V4, P8, DOI 10.1186/1472-6793-4-8
   Tambutte E, 1996, J EXP BIOL, V199, P1029
   Tresguerres M, 2008, AM J PHYSIOL-REG I, V294, pR1033, DOI 10.1152/ajpregu.00516.2007
   Tresguerres M, 2019, FISH PHYSIOL, V37, P33, DOI 10.1016/bs.fp.2019.07.001
   Tresguerres M, 2020, J EXP ZOOL PART A, V333, P449, DOI 10.1002/jez.2367
   Tresguerres M, 2018, METHOD ENZYMOL, V605, P525, DOI 10.1016/bs.mie.2018.02.022
   Tresguerres M, 2014, BBA-MOL BASIS DIS, V1842, P2629, DOI 10.1016/j.bbadis.2014.06.021
   Tresguerres M, 2014, J EXP BIOL, V217, P663, DOI 10.1242/jeb.086157
   Tresguerres M, 2011, KIDNEY INT, V79, P1277, DOI 10.1038/ki.2011.95
   Tresguerres M, 2010, AM J PHYSIOL-REG I, V299, pR62, DOI 10.1152/ajpregu.00761.2009
   Tresguerres M, 2010, P NATL ACAD SCI USA, V107, P442, DOI 10.1073/pnas.0911790107
   Vacquier VD, 2014, BBA-MOL BASIS DIS, V1842, P2621, DOI 10.1016/j.bbadis.2014.07.011
   von Schalburg KR, 2018, HISTOCHEM CELL BIOL, V149, P75, DOI 10.1007/s00418-017-1611-3
   Watson RL, 2015, J EXP MED, V212, P1021, DOI 10.1084/jem.20150354
   Wilson CM, 2016, J EXP BIOL, V219, P3227, DOI 10.1242/jeb.138198
   Wilson JM, 2013, J EXP BIOL, V216, P623, DOI 10.1242/jeb.074401
   Zippin JH, 2004, J CELL BIOL, V164, P527, DOI 10.1083/jcb.200311119
   Zippin JH, 2002, FASEB J, V16, P82, DOI 10.1096/fj.02-0598fje
   Zippin JH, 2013, J BIOL CHEM, V288, P33283, DOI 10.1074/jbc.M113.510073
   Zippin JH, 2010, J INVEST DERMATOL, V130, P1279, DOI 10.1038/jid.2009.440
NR 77
TC 7
Z9 7
U1 1
U2 8
PU ROYAL SOC
PI LONDON
PA 6-9 CARLTON HOUSE TERRACE, LONDON SW1Y 5AG, ENGLAND
SN 2042-8898
EI 2042-8901
J9 INTERFACE FOCUS
JI Interface Focus
PD APR 6
PY 2021
VL 11
IS 2
AR 20200026
DI 10.1098/rsfs.2020.0026
PG 12
WC Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Life Sciences & Biomedicine - Other Topics
GA SA2RB
UT WOS:000649146500002
PM 33633829
OA Green Published, Bronze
DA 2025-04-10
ER

PT J
AU Duhachek-Muggy, S
   Li, H
   Qi, Y
   Zolkiewska, A
AF Duhachek-Muggy, Sara
   Li, Hui
   Qi, Yue
   Zolkiewska, Anna
TI Alternative mRNA Splicing Generates Two Distinct ADAM12 Prodomain
   Variants
SO PLOS ONE
LA English
DT Article
ID EPIDERMAL-GROWTH-FACTOR; MELTRIN-ALPHA; BREAST-CANCER; TUMOR
   PROGRESSION; SECRETED FORM; REGULATED EXPRESSION; CARDIAC-HYPERTROPHY;
   CELL-PROLIFERATION; DISINTEGRIN ADAM12; MOLECULAR SWITCH
AB Human ADAM12, transcript variant 1 (later on referred to as Var-1b), present in publicly available databases contains the sequence 59-GTAATTCTG-3' at the nucleotide positions 340-348 of the coding region, at the 3' end of exon 4. The translation product of this variant, ADAM12-Lb, includes the three amino acid motif (VIL116)-V-114 in the prodomain. This motif is not conserved in ADAM12 from different species and is not present in other human ADAMs. Currently, it is not clear whether a shorter variant, Var-1a, encoding the protein version without the (VIL116)-V-114 motif, ADAM12-La, is expressed in human. In this work, we have established that human mammary epithelial cells and breast cancer cells express both Var-1a and Var-1b transcripts. Importantly, the proteolytic processing and intracellular trafficking of the corresponding ADAM12-La and ADAM12-Lb proteins are different. While ADAM12-La is cleaved and trafficked to the cell surface in a manner similar to ADAM12 in other species, ADAM12-Lb is retained in the ER and is not proteolytically processed. Furthermore, the relative abundance of ADAM12-La and ADAM12-Lb proteins detected in several breast cancer cell lines varies significantly. We conclude that the canonical form of transmembrane ADAM12 is represented by Var-1a/ ADAM12-La, rather than Var-1b/ADAM12-Lb currently featured in major sequence databases.
C1 [Duhachek-Muggy, Sara; Li, Hui; Qi, Yue; Zolkiewska, Anna] Kansas State Univ, Dept Biochem & Mol Biophys, Manhattan, KS 66506 USA.
C3 Kansas State University
RP Zolkiewska, A (corresponding author), Kansas State Univ, Dept Biochem & Mol Biophys, Manhattan, KS 66506 USA.
EM zolkiea@ksu.edu
RI qi, yue/KLE-0386-2024; LI, HUI/G-1227-2011
OI Li, Hui/0000-0002-4114-8349
FU National Institutes of Health [R15CA151065, R01CA172222]; Innovative
   Research Award from Terry C. Johnson Center for Basic Cancer Research at
   KSU
FX This work was supported by National Institutes of Health grants
   R15CA151065 and R01CA172222, and Innovative Research Award from Terry C.
   Johnson Center for Basic Cancer Research at KSU. This is contribution
   13-393-J from Kansas Agricultural Experiment Station. The funders had no
   role in study design, data collection and analysis, decision to publish,
   or preparation of the manuscript.
CR Asakura M, 2002, NAT MED, V8, P35, DOI 10.1038/nm0102-35
   Atfi A, 2007, J CELL BIOL, V178, P201, DOI 10.1083/jcb.200612046
   Barnabas N, 2013, INT J BREAST CANCER, V2013, DOI 10.1155/2013/872743
   Bertucci F, 2006, CANCER RES, V66, P4636, DOI 10.1158/0008-5472.CAN-06-0031
   Bornemann A, 2000, J MUSCLE RES CELL M, V21, P475, DOI 10.1023/A:1005657607591
   Brodsky JL, 2012, CELL, V151, P1163, DOI 10.1016/j.cell.2012.11.012
   Capasso R, 2012, PLOS ONE, V7, DOI 10.1371/journal.pone.0031388
   Carmel I, 2004, RNA, V10, P828, DOI 10.1261/rna.5196404
   Clark HF, 2003, GENOME RES, V13, P2265, DOI 10.1101/gr.1293003
   Díaz B, 2013, J CELL BIOL, V201, P279, DOI 10.1083/jcb.201209151
   Dulauroy S, 2012, NAT MED, V18, P1262, DOI 10.1038/nm.2848
   Dyczynska E, 2007, J BIOL CHEM, V282, P436, DOI 10.1074/jbc.M605451200
   Edwards DR, 2008, MOL ASPECTS MED, V29, P258, DOI 10.1016/j.mam.2008.08.001
   Fröhlich C, 2006, CLIN CANCER RES, V12, P7359, DOI 10.1158/1078-0432.CCR-06-1066
   Fröhlich C, 2013, BIOCHEM J, V452, P97, DOI 10.1042/BJ20121558
   Georges S, 2013, EUR J CANCER, V49, P2253, DOI 10.1016/j.ejca.2013.02.020
   Gilpin BJ, 1998, J BIOL CHEM, V273, P157, DOI 10.1074/jbc.273.1.157
   Gödde NJ, 2007, GENE, V403, P80, DOI 10.1016/j.gene.2007.07.033
   Gonzales PE, 2004, J BIOL CHEM, V279, P31638, DOI 10.1074/jbc.M401311200
   Harsha A, 2008, J MOL MED, V86, P961, DOI 10.1007/s00109-008-0353-z
   Hiller M, 2006, AM J HUM GENET, V78, P291, DOI 10.1086/500151
   Hiller M, 2008, TRENDS GENET, V24, P246, DOI 10.1016/j.tig.2008.03.003
   Horiuchi K, 2007, MOL BIOL CELL, V18, P176, DOI 10.1091/mbc.E06-01-0014
   Hotoda N, 2002, BIOCHEM BIOPH RES CO, V293, P800, DOI 10.1016/S0006-291X(02)00302-9
   Howard L, 2000, BIOCHEM J, V348, P21, DOI 10.1042/0264-6021:3480021
   Iba K, 1999, AM J PATHOL, V154, P1489, DOI 10.1016/S0002-9440(10)65403-X
   Ieguchi K, 2013, ONCOGENE, DOI [10.1038/onc.2013.180, DOI 10.1038/0NC.2013.180]
   Kleino I, 2007, BMC MOL BIOL, V8, DOI 10.1186/1471-2199-8-90
   Kleino I, 2009, J CELL BIOCHEM, V108, P877, DOI 10.1002/jcb.22317
   Kodama T, 2004, AM J PATHOL, V165, P1743, DOI 10.1016/S0002-9440(10)63429-3
   Kurisaki T, 1998, MECH DEVELOP, V73, P211, DOI 10.1016/S0925-4773(98)00043-4
   Kurisaki T, 2003, MOL CELL BIOL, V23, P55, DOI 10.1128/MCB.23.1.55-61.2003
   Kurisaki T, 2002, FEBS LETT, V532, P419, DOI 10.1016/S0014-5793(02)03732-8
   Kveiborg M, 2005, CANCER RES, V65, P4754, DOI 10.1158/0008-5472.CAN-05-0262
   Kveiborg M, 2008, INT J BIOCHEM CELL B, V40, P1685, DOI 10.1016/j.biocel.2008.01.025
   Le Pabic H, 2003, HEPATOLOGY, V37, P1056, DOI 10.1053/jhep.2003.50205
   Lendeckel U, 2005, J CANCER RES CLIN, V131, P41, DOI 10.1007/s00432-004-0619-y
   Li H, 2013, BREAST CANCER RES TR, V139, P691, DOI 10.1007/s10549-013-2602-2
   Li H, 2012, BREAST CANCER RES TR, V135, P759, DOI 10.1007/s10549-012-2220-4
   Mazzocca A, 2005, CANCER RES, V65, P4728, DOI 10.1158/0008-5472.CAN-04-4449
   Miller FR, 2000, J NATL CANCER I, V92, P1185, DOI 10.1093/jnci/92.14.1185A
   Mino N, 2009, J SURG ONCOL, V100, P267, DOI 10.1002/jso.21313
   Mitsui Y, 2006, CANCER RES, V66, P9913, DOI 10.1158/0008-5472.CAN-06-0377
   Ohlig S, 2011, DEV CELL, V20, P764, DOI 10.1016/j.devcel.2011.05.010
   Ortiz RM, 2004, GENE CHROMOSOME CANC, V41, P366, DOI 10.1002/gcc.20102
   Peduto L, 2006, ONCOGENE, V25, P5462, DOI 10.1038/sj.onc.1209536
   Powell RM, 2004, AM J RESP CELL MOL, V31, P13, DOI 10.1165/rcmb.2003-0330OC
   Prat A, 2010, BREAST CANCER RES, V12, DOI 10.1186/bcr2635
   Rao VH, 2012, ONCOGENE, V31, P2888, DOI 10.1038/onc.2011.460
   Rawlings ND, 2008, NUCLEIC ACIDS RES, V36, pD320, DOI 10.1093/nar/gkm954
   Roberts CM, 1999, J BIOL CHEM, V274, P29251, DOI 10.1074/jbc.274.41.29251
   Sagane K, 2005, BMC NEUROSCI, V6, DOI 10.1186/1471-2202-6-33
   Scheller J, 2011, TRENDS IMMUNOL, V32, P380, DOI 10.1016/j.it.2011.05.005
   Skubitz KM, 2004, J LAB CLIN MED, V143, P89, DOI 10.1016/j.lab.2003.10.002
   Sorensen HP, 2008, J BIOL CHEM, V283, P31920, DOI 10.1074/jbc.M804113200
   Stautz D, 2012, TRAFFIC, V13, P1532, DOI 10.1111/j.1600-0854.2012.01405.x
   Turashvili G, 2007, BMC CANCER, V7, DOI 10.1186/1471-2407-7-55
   Uehara E, 2012, INT J ONCOL, V40, P1414, DOI 10.3892/ijo.2012.1339
   VANWART HE, 1990, P NATL ACAD SCI USA, V87, P5578, DOI 10.1073/pnas.87.14.5578
   Wang X, 2009, CIRCULATION, V119, P2480, DOI 10.1161/CIRCULATIONAHA.108.835488
   Wang ZF, 2008, RNA, V14, P802, DOI 10.1261/rna.876308
   Weber S, 2012, DEVELOPMENT, V139, P3693, DOI 10.1242/dev.076398
   Gomis-Rüth FX, 2009, J BIOL CHEM, V284, P15353, DOI 10.1074/jbc.R800069200
   Xu SW, 2007, MATRIX BIOL, V26, P625, DOI 10.1016/j.matbio.2007.06.003
NR 64
TC 8
Z9 8
U1 0
U2 8
PU PUBLIC LIBRARY SCIENCE
PI SAN FRANCISCO
PA 1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA
SN 1932-6203
J9 PLOS ONE
JI PLoS One
PD OCT 7
PY 2013
VL 8
IS 10
AR e75730
DI 10.1371/journal.pone.0075730
PG 11
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA 232NS
UT WOS:000325501300040
PM 24116070
OA gold, Green Published, Green Submitted
DA 2025-04-10
ER

PT J
AU Tokue, SI
   Sasaki, M
   Nakahata, N
AF Tokue, Shin-ichi
   Sasaki, Masako
   Nakahata, Norimichi
TI Thromboxane A2-induced signal transduction is negatively
   regulated by KIAA1005 that directly interacts with thromboxane
   A2 receptor
SO PROSTAGLANDINS & OTHER LIPID MEDIATORS
LA English
DT Article
DE Thromboxane A(2); Thromboxa ne A(2) receptor; TP alpha; TP beta;
   KIAA1005
ID HUMAN ASTROCYTOMA-CELLS; ACTIVATED PROTEIN-KINASE; CYTOSOLIC
   PHOSPHOLIPASE A(2); PARATHYROID-HORMONE RECEPTOR; HUMAN PLATELETS;
   JOUBERT-SYNDROME; BINDING PROTEIN; COOH TERMINUS; C2 DOMAINS; ISOFORMS
AB Thromboxane A(2) (TXA(2)), a potent inducer of platelet aggregation and smooth muscle contraction, exerts its action through TXA2 receptor (TP). There are two alternative splicing variants of TP, TP alpha and TP beta. To clarify the signal transduction of TP pathway, we searched for putative TP binding proteins using a yeast two-hybrid system with the C-terminal region of TP alpha or TP beta as bait. We found KIAA1005 as a novel interacting protein of the TP alpha and TP beta C-terminal region (TP interacting protein, TPIP). KIAA1005/TPIP was co-immunoprecipitated with TP alpha or TP beta in HEK293 cells expressing myc-KIAA1005/TPIP and FLAG-TP isoforms. Expression analysis showed a ubiquitous expression pattern of KIAA1005/TPIP mRNA, including prominent expression in the thymus. Furthermore, TP-mediated phosphoinositide hydrolysis, phosphorylation of extracellular signal-regulated kinase (ERK) 1/2 and interleukin-6 production were reduced by the expression of KIAA1005/TPIP. The expression of KIAA1005/TPIP decreased cell-surface TP alpha and TP beta levels. Thus, we show for the first time that KIAA1005/TPIP is a novel TP interacting protein that regulates TP-mediated signal transduction negatively. (C) 2009 Elsevier Inc. All rights reserved.
C1 [Tokue, Shin-ichi; Sasaki, Masako; Nakahata, Norimichi] Tohoku Univ, Dept Cellular Signaling, Grad Sch Pharmaceut Sci, Aoba Ku, Sendai, Miyagi 9808578, Japan.
   [Tokue, Shin-ichi; Sasaki, Masako; Nakahata, Norimichi] Tohoku Univ, 21st Century COE Program, CRESCENDO, Sendai, Miyagi 9808578, Japan.
C3 Tohoku University; Tohoku University
RP Nakahata, N (corresponding author), Tohoku Univ, Dept Cellular Signaling, Grad Sch Pharmaceut Sci, Aoba Ku, Aoba 6-3, Sendai, Miyagi 9808578, Japan.
EM nakahata@mail.pharm.tohoku.ac.jp
FU Japan Society for the Promotion of Science [19659011]; Ministry of
   Education, Culture, Sports, Science and Technology [18058002, 20054002];
   Tohoku University; Grants-in-Aid for Scientific Research [18058002,
   20054002] Funding Source: KAKEN
FX This work was supported in part by a Grant-in-Aid for Scientific
   Research from the Japan Society for the Promotion of Science (No.
   19659011 to N.N.), from the Ministry of Education, Culture, Sports,
   Science and Technology (Nos. 18058002 and 20054002 to N.N.) and from
   Tohoku University 21st Century COE Program CRESCENDO (to S.T. and N.N.).
CR Arora KK, 1998, J BIOL CHEM, V273, P25581, DOI 10.1074/jbc.273.40.25581
   Arts HH, 2007, NAT GENET, V39, P882, DOI 10.1038/ng2069
   Ashton AW, 2004, CIRC RES, V95, P372, DOI 10.1161/01.RES.0000138300.41642.15
   Corbin JA, 2007, BIOCHEMISTRY-US, V46, P4322, DOI 10.1021/bi062140c
   Delous M, 2007, NAT GENET, V39, P875, DOI 10.1038/ng2039
   Deretic D, 2005, P NATL ACAD SCI USA, V102, P3301, DOI 10.1073/pnas.0500095102
   Djellas Y, 1999, J BIOL CHEM, V274, P14325, DOI 10.1074/jbc.274.20.14325
   Evans JH, 2004, MOL BIOL CELL, V15, P371, DOI 10.1091/mbc.e03-05-0338
   Ferguson SSG, 2001, PHARMACOL REV, V53, P1
   GLOVER S, 1995, J BIOL CHEM, V270, P15359, DOI 10.1074/jbc.270.25.15359
   Habib A, 1997, J BIOL CHEM, V272, P7191, DOI 10.1074/jbc.272.11.7191
   Halushka PV, 2000, PROSTAG OTH LIPID M, V60, P175, DOI 10.1016/S0090-6980(99)00062-3
   Hamelin E, 2005, J BIOL CHEM, V280, P36195, DOI 10.1074/jbc.M503438200
   HIRATA M, 1991, NATURE, V349, P617, DOI 10.1038/349617a0
   Hirata T, 1996, J CLIN INVEST, V97, P949, DOI 10.1172/JCI118518
   Honma S, 1998, PROSTAG OTH LIPID M, V55, P159, DOI 10.1016/S0090-6980(98)00017-3
   Honma S, 2006, EUR J PHARMACOL, V545, P100, DOI 10.1016/j.ejphar.2006.06.062
   Hurley JH, 2006, BBA-MOL CELL BIOL L, V1761, P805, DOI 10.1016/j.bbalip.2006.02.020
   Kobayashi H, 2000, J NEUROCHEM, V74, P2167, DOI 10.1046/j.1471-4159.2000.0742167.x
   Liedtke CM, 2003, AM J PHYSIOL-CELL PH, V284, pC487, DOI 10.1152/ajpcell.00357.2002
   Lupas AN, 2005, ADV PROTEIN CHEM, V70, P37, DOI 10.1016/S0065-3233(04)70003-0
   Luttrell LM, 2002, J CELL SCI, V115, P455
   Miggin SM, 2001, BBA-MOL CELL RES, V1539, P147, DOI 10.1016/S0167-4889(01)00103-3
   Miyosawa K, 2006, BIOL PHARM BULL, V29, P719, DOI 10.1248/bpb.29.719
   NAKAHATA N, 1995, RES COMMUN MOL PATH, V87, P243
   NAKAHATA N, 1989, EUR J PHARMACOL, V162, P407, DOI 10.1016/0014-2999(89)90331-2
   Nakahata N, 2008, PHARMACOL THERAPEUT, V118, P18, DOI 10.1016/j.pharmthera.2008.01.001
   Nalefski EA, 1996, PROTEIN SCI, V5, P2375, DOI 10.1002/pro.5560051201
   NUSING RM, 1993, J BIOL CHEM, V268, P25253
   Obara Y, 2005, MOL PHARMACOL, V68, P670, DOI 10.1124/mol.105.012922
   ODOWD BF, 1988, J BIOL CHEM, V263, P15985
   OFFERMANNS S, 1994, P NATL ACAD SCI USA, V91, P504, DOI 10.1073/pnas.91.2.504
   Ohkubo S, 1996, PROSTAGLANDINS, V52, P403, DOI 10.1016/S0090-6980(96)00105-0
   Parent JL, 2001, J BIOL CHEM, V276, P7079, DOI 10.1074/jbc.M009375200
   Parent JL, 1999, J BIOL CHEM, V274, P8941, DOI 10.1074/jbc.274.13.8941
   RAYCHOWDHURY MK, 1994, J BIOL CHEM, V269, P19256
   Saito M, 2005, BIOCHEM J, V392, P75, DOI 10.1042/BJ20050618
   Sakai K, 1996, J PHARMACOL EXP THER, V276, P829
   Sasaki M, 2006, J PHARMACOL SCI, V100, P263, DOI 10.1254/jphs.FP0050839
   Sasaki M, 2007, PROSTAG OTH LIPID M, V83, P237, DOI 10.1016/j.prostaglandins.2006.12.001
   Sheetz MP, 1999, EUR J BIOCHEM, V262, P19, DOI 10.1046/j.1432-1327.1999.00340.x
   Shen RF, 1998, J BIOMED SCI, V5, P153, DOI 10.1159/000025327
   SHENKER A, 1991, J BIOL CHEM, V266, P9309
   Stahelin RV, 2003, J BIOL CHEM, V278, P12452, DOI 10.1074/jbc.M212864200
   Sugai M, 2003, BIOCHEM BIOPH RES CO, V311, P24, DOI 10.1016/j.bbrc.2003.09.157
   Tazawa H, 2003, BBA-GEN SUBJECTS, V1620, P32, DOI 10.1016/S0304-4165(02)00503-2
   Verdaguer N, 1999, EMBO J, V18, P6329, DOI 10.1093/emboj/18.22.6329
   Vezza R, 1999, J BIOL CHEM, V274, P12774, DOI 10.1074/jbc.274.18.12774
   Yukawa M, 1997, CIRC RES, V80, P551, DOI 10.1161/01.RES.80.4.551
NR 49
TC 6
Z9 11
U1 0
U2 0
PU ELSEVIER SCIENCE INC
PI NEW YORK
PA 360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA
SN 1098-8823
EI 2212-196X
J9 PROSTAG OTH LIPID M
JI Prostaglandins Other Lipid Mediat.
PD JUN
PY 2009
VL 89
IS 1-2
BP 8
EP 15
DI 10.1016/j.prostaglandins.2009.02.001
PG 8
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA 464SW
UT WOS:000267528000002
PM 19464661
DA 2025-04-10
ER

PT J
AU Montonen, O
   Aho, M
   Uitto, J
   Aho, S
AF Montonen, O
   Aho, M
   Uitto, J
   Aho, S
TI Tissue distribution and cell type-specific expression of p120ctn
   isoforms
SO JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY
LA English
DT Article
DE p120ctn isoforms; epithelia; cell-cell adhesion
ID TYROSINE KINASE SUBSTRATE; HUMAN P120(CTN) CATENIN; E-CADHERIN; PROTEIN;
   BINDS; DEPHOSPHORYLATES; IDENTIFICATION; COMPLEXES; ADHESION; DOMAIN
AB Cadherin-based molecular complexes play a major role in cell-cell adhesion. At the adherens junctions the intracellular domain of cadherins specifically interacts with P-catenin and p120ctn, members of the Armadillo repeat protein family. Differential splicing and utilization of the alternative translation initiation codons lead to many p120ctn isoforms. Two major p120ctn isoforms are expressed in mouse tissues. In this study we used indirect immunofluorescence to demonstrate significant tissue specificity in expression of the p120ctn isoforms. The short isoform is abundant at cell-cell adhesion junctions in epidermis, palatal, and tongue epithelia, in the ducts of excretory glands, bronchiolar epithelium, and in mucosal epithelia of esophagus, forestomach, and small intestine. In contrast, the long isoform, containing an amino terminus highly conserved within the p120ctn subfamily, is expressed at vascular-endothelial cell junctions in blood vessels, at cell-cell junctions in the serosal epithelium lining the internal organs, in choroid plexus of brain, in the pigment epithelium of retina, and in structures such as the outer limiting membrane of retina and intercalated discs of cardiomyocytes. The tissue- and cell type-specific expression of p120ctn isoforms suggests a role for the long p120ctn isoform in cell structures responsible for stable tissue integrity, compared to the role of the short isoform in cell-cell adhesion in the external epithelia with rapid turnover.
C1 Thomas Jefferson Univ, Jefferson Med Coll, Dept Dermatol & Cutaneous Biol, Philadelphia, PA 19107 USA.
C3 Thomas Jefferson University
RP Aho, S (corresponding author), Thomas Jefferson Univ, Jefferson Med Coll, Dept Dermatol & Cutaneous Biol, 233 S 10th St,Suite 450 BLSB, Philadelphia, PA 19107 USA.
CR Aho S, 1999, J CELL BIOCHEM, V73, P390, DOI 10.1002/(SICI)1097-4644(19990601)73:3<390::AID-JCB10>3.0.CO;2-1
   Anastasiadis PZ, 2000, NAT CELL BIOL, V2, P637, DOI 10.1038/35023588
   Daniel JM, 1999, MOL CELL BIOL, V19, P3614
   DANIEL JM, 1995, MOL CELL BIOL, V15, P4819
   Golenhofen N, 2000, HISTOCHEM CELL BIOL, V114, P147
   Keilhack H, 2000, J BIOL CHEM, V275, P26376, DOI 10.1074/jbc.M001315200
   Keirsebilck A, 1998, GENOMICS, V50, P129, DOI 10.1006/geno.1998.5325
   KIM L, 1995, MOL CELL BIOL, V15, P4553
   Mo YY, 1996, CANCER RES, V56, P2633
   Noren NK, 2000, J CELL BIOL, V150, P567, DOI 10.1083/jcb.150.3.567
   Ohkubo T, 1999, J BIOL CHEM, V274, P21409, DOI 10.1074/jbc.274.30.21409
   REYNOLDS AB, 1989, MOL CELL BIOL, V9, P629, DOI 10.1128/MCB.9.2.629
   REYNOLDS AB, 1994, MOL CELL BIOL, V14, P8333, DOI 10.1128/MCB.14.12.8333
   REYNOLDS AB, 1992, ONCOGENE, V7, P2439
   REYNOLDS JF, 1996, ECOL STU AN, V120, P3
   SHIBAMOTO S, 1995, J CELL BIOL, V128, P949, DOI 10.1083/jcb.128.5.949
   STADDON JM, 1995, J CELL BIOL, V130, P369, DOI 10.1083/jcb.130.2.369
   Thoreson MA, 2000, J CELL BIOL, V148, P189, DOI 10.1083/jcb.148.1.189
   Wu J, 1998, HYBRIDOMA, V17, P175, DOI 10.1089/hyb.1998.17.175
   Yap AS, 1998, J CELL BIOL, V141, P779, DOI 10.1083/jcb.141.3.779
   Zondag GCM, 2000, J BIOL CHEM, V275, P11264, DOI 10.1074/jbc.275.15.11264
NR 21
TC 36
Z9 41
U1 0
U2 1
PU HISTOCHEMICAL SOC INC
PI SEATTLE
PA UNIV WASHINGTON, DEPT BIOSTRUCTURE, BOX 357420, SEATTLE, WA 98195 USA
SN 0022-1554
J9 J HISTOCHEM CYTOCHEM
JI J. Histochem. Cytochem.
PD DEC
PY 2001
VL 49
IS 12
BP 1487
EP 1495
DI 10.1177/002215540104901202
PG 9
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA 509TT
UT WOS:000173166300002
PM 11724896
OA Bronze
DA 2025-04-10
ER

PT J
AU Brown, KA
   Melby, JA
   Roberts, DS
   Ge, Y
AF Brown, Kyle A.
   Melby, Jake A.
   Roberts, David S.
   Ge, Ying
TI Top-down proteomics: challenges, innovations, and applications in basic
   and clinical research
SO EXPERT REVIEW OF PROTEOMICS
LA English
DT Review
DE Top-down Proteomics; Mass Spectrometry; Post-translational
   Modifications; Proteoforms; Heart Diseases
ID ELECTRON-TRANSFER DISSOCIATION; CARDIAC TROPONIN-I;
   SPECTROMETRY-COMPATIBLE SURFACTANT; ION-EXCHANGE CHROMATOGRAPHY; NATIVE
   MASS-SPECTROMETRY; MEMBRANE-PROTEINS; LIQUID-CHROMATOGRAPHY; ONLINE
   DETECTION; INTACT PROTEINS; IDENTIFICATION
AB Introduction- A better understanding of the underlying molecular mechanism of diseases is critical for developing more effective diagnostic tools and therapeutics toward precision medicine. However, many challenges remain to unravel the complex nature of diseases.
   Areas covered- Changes in protein isoform expression and post-translation modifications (PTMs) have gained recognition for their role in underlying disease mechanisms. Top-down mass spectrometry (MS)-based proteomics is increasingly recognized as an important method for the comprehensive characterization of proteoforms that arise from alternative splicing events and/or PTMs for basic and clinical research. Here, we review the challenges, technological innovations, and recent studies that utilize top-down proteomics to elucidate changes in the proteome with an emphasis on its use to study heart diseases.
   Expert opinion- Proteoform-resolved information can substantially contribute to the understanding of the molecular mechanisms underlying various diseases and for the identification of novel proteoform targets for better therapeutic development . Despite the challenges of sequencing intact proteins, top-down proteomics has enabled a wealth of information regarding protein isoform switching and changes in PTMs. Continuous developments in sample preparation, intact protein separation, and instrumentation for top-down MS have broadened its capabilities to characterize proteoforms from a range of samples on an increasingly global scale.
C1 [Brown, Kyle A.; Melby, Jake A.; Roberts, David S.; Ge, Ying] Univ Wisconsin, Dept Chem, 1101 Univ Ave, Madison, WI 53706 USA.
   [Ge, Ying] Univ Wisconsin, Dept Cell & Regenerat Biol, Madison, WI 53706 USA.
   [Ge, Ying] Univ Wisconsin, Dept Chem, Human Prote Program, 1101 Univ Ave, Madison, WI 53706 USA.
C3 University of Wisconsin System; University of Wisconsin Madison;
   University of Wisconsin System; University of Wisconsin Madison;
   University of Wisconsin System; University of Wisconsin Madison
RP Ge, Y (corresponding author), Univ Wisconsin, Dept Cell & Regenerat Biol, Madison, WI 53706 USA.; Brown, KA (corresponding author), WIMR II 8546,1111 Highland Ave, Madison, WI 53705 USA.
EM kbrown33@wisc.edu; ying.ge@wisc.edu
RI ; Roberts, David/GQQ-2773-2022
OI Ge, Ying/0000-0001-5211-6812; Roberts, David/0000-0002-0478-4987; Melby,
   Jake/0000-0003-1499-9508
FU U.S. Foundation for the National Institutes of Health [R01 HL096971, R01
   GM117058, GM125085, HL109810]; Cardiovascular Research Center Training
   Program in Translational Cardiovascular Science [T32 HL007936-19, T32
   HL007936-20]; Vascular Surgery Research Training Program [T32HL110853]
FX This paper was supported by the U.S. Foundation for the National
   Institutes of Health: R01 HL096971, R01 GM117058, GM125085, and HL109810
   (to Y. Ge). K.A. Brown would like to acknowledge Cardiovascular Research
   Center Training Program in Translational Cardiovascular Science, T32
   HL007936-19 and Vascular Surgery Research Training Program grant
   T32HL110853. J.A. Melby would like to thank Cardiovascular Research
   Center Training Program in Translational Cardiovascular Science, T32
   HL007936-20.
CR Aebersold R, 2003, NATURE, V422, P198, DOI 10.1038/nature01511
   Aebersold R, 2018, NAT CHEM BIOL, V14, P206, DOI [10.1038/NCHEMBIO.2576, 10.1038/nchembio.2576]
   Anderson NL, 2002, MOL CELL PROTEOMICS, V1, P845, DOI 10.1074/mcp.R200007-MCP200
   Azad NS, 2006, MOL CELL PROTEOMICS, V5, P1819, DOI 10.1074/mcp.R600008-MCP200
   Baghdady YZ, 2019, ANAL CHEM, V91, P11085, DOI 10.1021/acs.analchem.9b01665
   Baker M, 2015, NATURE, V521, P274, DOI 10.1038/521274a
   Barrera NP, 2011, ANNU REV BIOCHEM, V80, P247, DOI 10.1146/annurev-biochem-062309-093307
   Blackwell AE, 2011, ANAL CHEM, V83, P2862, DOI 10.1021/ac200452b
   Bolla JR, 2019, ANNU REV BIOCHEM, V88, P85, DOI 10.1146/annurev-biochem-013118-111508
   Bradbury A, 2015, NATURE, V518, P27, DOI 10.1038/518027a
   Brown KA, 2020, ANGEW CHEM, V132
   Brown KA, 2019, NAT METHODS, V16, P417, DOI 10.1038/s41592-019-0391-1
   Brunner AM, 2015, ANAL CHEM, V87, P4152, DOI 10.1021/acs.analchem.5b00162
   Cai WX, 2019, CIRC RES, V125, P936, DOI 10.1161/CIRCRESAHA.119.315305
   Cai WX, 2017, ANAL CHEM, V89, P5467, DOI 10.1021/acs.analchem.7b00380
   Cai WX, 2016, EXPERT REV PROTEOMIC, V13, P717, DOI 10.1080/14789450.2016.1209414
   Carroll J, 2006, P NATL ACAD SCI USA, V103, P16170, DOI 10.1073/pnas.0607719103
   Catherman AD, 2013, MOL CELL PROTEOMICS, V12, P3465, DOI 10.1074/mcp.M113.030114
   Cesnik AJ, 2018, J PROTEOME RES, V17, P568, DOI 10.1021/acs.jproteome.7b00685
   Chen B, 2018, ANAL CHEM, V90
   Chen BF, 2018, ANAL CHEM, V90, P110, DOI 10.1021/acs.analchem.7b04747
   Chen BF, 2017, CHEM SCI, V8, P4306, DOI 10.1039/c6sc05435h
   Chen BF, 2016, ANAL CHEM, V88, P1885, DOI 10.1021/acs.analchem.5b04285
   Chen IY, 2016, NAT REV CARDIOL, V13, DOI 10.1038/nrcardio.2016.130
   Chen YC, 2015, ANAL CHEM, V87, P8399, DOI 10.1021/acs.analchem.5b01745
   Chorev DS, 2018, SCIENCE, V362, P829, DOI 10.1126/science.aau0976
   Cleland TP, 2017, J PROTEOME RES, V16, P2072, DOI 10.1021/acs.jproteome.7b00043
   Compton PD, 2011, ANAL CHEM, V83, P6868, DOI 10.1021/ac2010795
   Crittenden CM, 2020, J AM SOC MASS SPECTR, V31, P1140, DOI 10.1021/jasms.0c00066
   Dautant A, 2018, FRONT PHYSIOL, V9, DOI 10.3389/fphys.2018.00329
   de Tombe PP, 2000, ANN BIOMED ENG, V28, P991, DOI 10.1114/1.1312189
   Dong XT, 2012, J BIOL CHEM, V287, P848, DOI 10.1074/jbc.M111.293258
   Donnelly DP, 2019, NAT METHODS, V16, P587, DOI 10.1038/s41592-019-0457-0
   Doucette AA, 2014, J PROTEOME RES, V13, P6001, DOI 10.1021/pr500864a
   Durbin KR, 2016, J PROTEOME RES, V15, P976, DOI 10.1021/acs.jproteome.5b00997
   ENG JK, 1994, J AM SOC MASS SPECTR, V5, P976, DOI 10.1016/1044-0305(94)80016-2
   FENN JB, 1989, SCIENCE, V246, P64, DOI 10.1126/science.2675315
   Fert-Bober J, 2018, CIRC RES, V122, P1221, DOI 10.1161/CIRCRESAHA.118.310966
   Fornelli L, 2017, J PROTEOME RES, V16, P609, DOI 10.1021/acs.jproteome.6b00698
   Fort KL, 2018, ANALYST, V143, P100, DOI 10.1039/c7an01629h
   Frank AM, 2008, J PROTEOME RES, V7, P113, DOI 10.1021/pr070361e
   Gargano AFG, 2018, J PROTEOME RES, V17, P3791, DOI 10.1021/acs.jproteome.8b00458
   Gargano AFG, 2018, ANAL CHEM, V90, P6601, DOI 10.1021/acs.analchem.8b00382
   Gault J, 2020, NAT METHODS, V17, P505, DOI 10.1038/s41592-020-0821-0
   Ge Y, 2009, P NATL ACAD SCI USA, V106, P12658, DOI 10.1073/pnas.0813369106
   Gomes FP, 2020, ANAL CHEM, V92, P2979, DOI 10.1021/acs.analchem.9b03856
   Gomes FP, 2019, MASS SPECTROM REV, V38, P445, DOI 10.1002/mas.21599
   Gregorich ZR, 2014, PROTEOMICS, V14, P1195, DOI 10.1002/pmic.201300432
   Greisch JF, 2019, CHEM SCI, V10, P7163, DOI 10.1039/c9sc01857c
   Harper CC, 2019, ANAL CHEM, V91, P7458, DOI 10.1021/acs.analchem.9b01669
   He JY, 2018, P NATL ACAD SCI USA, V115, P2988, DOI 10.1073/pnas.1722086115
   He LD, 2019, CLIN CHEM, V65, P986, DOI 10.1373/clinchem.2018.295766
   Hebert AS, 2014, MOL CELL PROTEOMICS, V13, P339, DOI 10.1074/mcp.M113.034769
   Horn DM, 2000, J AM SOC MASS SPECTR, V11, P320, DOI 10.1016/S1044-0305(99)00157-9
   Huguet R, 2019, ANAL CHEM, V91, P15732, DOI 10.1021/acs.analchem.9b03925
   Hwang L, 2015, J AM CHEM SOC, V137, P2432, DOI 10.1021/ja511833y
   Janes KA, 2020, SCI SIGNAL, V13, DOI 10.1126/scisignal.aaz8130
   Jeong K, 2020, CELL SYST, V10, P213, DOI 10.1016/j.cels.2020.01.003
   Ji CX, 2019, ANAL CHEM, V91, P7032, DOI 10.1021/acs.analchem.9b01662
   Jin YT, 2019, MABS-AUSTIN, V11, P106, DOI 10.1080/19420862.2018.1525253
   Kachuk C, 2018, J PROTEOMICS, V175, P75, DOI 10.1016/j.jprot.2017.03.002
   Kafader JO, 2020, J PROTEOME RES, V19, P1346, DOI 10.1021/acs.jproteome.9b00797
   Kafader JO, 2020, J AM SOC MASS SPECTR, V31, P574, DOI 10.1021/jasms.9b00040
   Kafader JO, 2020, NAT METHODS, V17, P391, DOI 10.1038/s41592-020-0764-5
   Kafader JO, 2019, J AM SOC MASS SPECTR, V30, P2200, DOI 10.1007/s13361-019-02309-0
   Karabacak NM, 2009, MOL CELL PROTEOMICS, V8, P846, DOI 10.1074/mcp.M800099-MCP200
   Katrukha AG, 1997, CLIN CHEM, V43, P1379
   Kellie JF, 2021, J AM SOC MASS SPECTR, V32, P1886, DOI 10.1021/jasms.0c00270
   Kocurek KI, 2017, J AM SOC MASS SPECTR, V28, P2066, DOI 10.1007/s13361-017-1718-8
   Kou Q, 2016, BIOINFORMATICS, V32, P3495, DOI 10.1093/bioinformatics/btw398
   La Vecchia L, 2000, J HEART LUNG TRANSPL, V19, P644, DOI 10.1016/S1053-2498(00)00120-0
   Labugger R, 2000, CIRCULATION, V102, P1221, DOI 10.1161/01.CIR.102.11.1221
   Laganowsky A, 2013, NAT PROTOC, V8, P639, DOI 10.1038/nprot.2013.024
   Larson EJ, 2020, ANAL CHEM, V92, P15096, DOI 10.1021/acs.analchem.0c03152
   LeDuc R. D., 2004, NUCLEIC ACIDS RES S2, V32, pW340
   Lee SH, 2020, NAT COMMUN, V11, DOI 10.1038/s41467-019-14143-9
   Leney AC, 2017, J AM SOC MASS SPECTR, V28, P5, DOI 10.1007/s13361-016-1545-3
   Lermyte F, 2019, J AM SOC MASS SPECTR, V30, P1149, DOI 10.1007/s13361-019-02201-x
   Li WJ, 2020, ANAL CHEM, V92, P6839, DOI 10.1021/acs.analchem.9b05739
   Lin ZQ, 2018, J AM SOC MASS SPECTR, V29, P1284, DOI 10.1007/s13361-018-1925-y
   Liu XW, 2013, J PROTEOME RES, V12, P5830, DOI 10.1021/pr400849y
   Liu XW, 2010, MOL CELL PROTEOMICS, V9, P2772, DOI 10.1074/mcp.M110.002766
   LOO RRO, 1994, PROTEIN SCI, V3, P1975, DOI 10.1002/pro.5560031109
   Lubeckyj RA, 2017, ANAL CHEM, V89, P12059, DOI 10.1021/acs.analchem.7b02532
   Macias LA, 2020, ANAL CHEM, V92, P227, DOI 10.1021/acs.analchem.9b04859
   MacLennan DH, 2003, NAT REV MOL CELL BIO, V4, P566, DOI 10.1038/nrm1151
   Makarov A, 2009, J AM SOC MASS SPECTR, V20, P1486, DOI 10.1016/j.jasms.2009.03.024
   Mamyrin BA, 2001, INT J MASS SPECTROM, V206, P251, DOI 10.1016/S1387-3806(00)00392-4
   Maron BJ, 2018, NEW ENGL J MED, V379, P655, DOI 10.1056/NEJMra1710575
   Marty MT, 2015, ANAL CHEM, V87, P4370, DOI 10.1021/acs.analchem.5b00140
   McCool EN, 2018, ANAL CHEM, V90, P5529, DOI 10.1021/acs.analchem.8b00693
   McIlwain SJ, 2020, J AM SOC MASS SPECTR, V31, P1104, DOI 10.1021/jasms.0c00035
   Melby JA, 2020, J PROTEOME RES, V19, P446, DOI 10.1021/acs.jproteome.9b00623
   Mikhailov VA, 2017, INT J MASS SPECTROM, V420, P43, DOI 10.1016/j.ijms.2016.09.011
   Muneeruddin K, 2017, ANALYST, V142, P336, DOI 10.1039/c6an02041k
   Muneeruddin K, 2015, ANAL CHEM, V87, P10138, DOI 10.1021/acs.analchem.5b02982
   Ntai I, 2018, P NATL ACAD SCI USA, V115, P4140, DOI 10.1073/pnas.1716122115
   Park J, 2017, NAT METHODS, V14, P909, DOI [10.1038/NMETH.4388, 10.1038/nmeth.4388]
   Peng Y, 2014, MOL CELL PROTEOMICS, V13, P2752, DOI 10.1074/mcp.M114.040675
   Petricoin EF, 2002, LANCET, V359, P572, DOI 10.1016/S0140-6736(02)07746-2
   Reading E, 2015, ANGEW CHEM INT EDIT, V54, P4577, DOI 10.1002/anie.201411622
   Regnier FE, 2018, ANAL CHEM, V90, P361, DOI 10.1021/acs.analchem.7b05007
   Riley NM, 2018, J AM SOC MASS SPECTR, V29, P140, DOI 10.1007/s13361-017-1808-7
   Riley NM, 2018, ANAL CHEM, V90, P40, DOI 10.1021/acs.analchem.7b04810
   Riley NM, 2017, J PROTEOME RES, V16, P2653, DOI 10.1021/acs.jproteome.7b00249
   Roberts DS, 2019, NANO RES, V12, P1473, DOI 10.1007/s12274-019-2418-4
   Rose RJ, 2012, NAT METHODS, V9, P1084, DOI [10.1038/NMETH.2208, 10.1038/nmeth.2208]
   Saveliev SV, 2013, ANAL CHEM, V85, P907, DOI 10.1021/ac302423t
   Sawyer WS, 2020, P NATL ACAD SCI USA, V117, P9851, DOI 10.1073/pnas.1917383117
   Schaffer LV, 2019, PROTEOMICS, V19, DOI 10.1002/pmic.201800361
   SENKO MW, 1995, J AM SOC MASS SPECTR, V6, P229, DOI 10.1016/1044-0305(95)00017-8
   Shaw JB, 2020, ANAL CHEM, V92, P766, DOI 10.1021/acs.analchem.9b03129
   Shaw JB, 2013, ANAL CHEM, V85, P8313, DOI 10.1021/ac401634b
   Shaw JB, 2013, J AM CHEM SOC, V135, P12646, DOI 10.1021/ja4029654
   Shen XJ, 2018, ANAL CHEM, V90, P10095, DOI 10.1021/acs.analchem.8b02725
   Shen YF, 2017, J CHROMATOGR A, V1498, P99, DOI 10.1016/j.chroma.2017.01.008
   Simone P, 2016, J SEP SCI, V39, P264, DOI 10.1002/jssc.201500844
   Skinner OS, 2018, NAT CHEM BIOL, V14, P36, DOI [10.1038/NCHEMBIO.2515, 10.1038/nchembio.2515]
   Smith LM, 2018, SCIENCE, V359, P1106, DOI 10.1126/science.aat1884
   Smith LM, 2013, NAT METHODS, V10, P186, DOI 10.1038/nmeth.2369
   Soetkamp D, 2017, EXPERT REV PROTEOMIC, V14, P973, DOI 10.1080/14789450.2017.1387054
   Speers AE, 2007, CHEM REV, V107, P3687, DOI 10.1021/cr068286z
   Sun RX, 2016, ANAL CHEM, V88, P3082, DOI 10.1021/acs.analchem.5b03963
   Susa AC, 2017, ANAL CHEM, V89, P3116, DOI 10.1021/acs.analchem.6b04897
   Syka JEP, 2004, P NATL ACAD SCI USA, V101, P9528, DOI 10.1073/pnas.0402700101
   Takemori A, 2020, J PROTEOME RES, V19, P3779, DOI 10.1021/acs.jproteome.0c00303
   Thingholm TE, 2006, NAT PROTOC, V1, P1929, DOI 10.1038/nprot.2006.185
   Thompson LV, 2009, EXP GERONTOL, V44, P106, DOI 10.1016/j.exger.2008.05.003
   Tiambeng TN, 2020, NAT COMMUN, V11, DOI 10.1038/s41467-020-17643-1
   Toby TK, 2019, NAT PROTOC, V14, P119, DOI 10.1038/s41596-018-0085-7
   Toby TK, 2016, ANNU REV ANAL CHEM, V9, P499, DOI 10.1146/annurev-anchem-071015-041550
   Tran JC, 2011, NATURE, V480, P254, DOI 10.1038/nature10575
   Tucholski T, 2020, P NATL ACAD SCI USA, V117, P24691, DOI 10.1073/pnas.2006764117
   Uhlen M, 2015, SCIENCE, V347, DOI 10.1126/science.1260419
   Urner LH, 2020, NAT COMMUN, V11, DOI 10.1038/s41467-020-14424-8
   Valeja SG, 2011, ANAL CHEM, V83, P8391, DOI 10.1021/ac202429c
   VanAernum ZL, 2020, NAT PROTOC, V15, P1132, DOI 10.1038/s41596-019-0281-0
   Villén J, 2008, NAT PROTOC, V3, P1630, DOI 10.1038/nprot.2008.150
   Wang YJ, 2020, ANAL CHEM, V92, P11007, DOI 10.1021/acs.analchem.9b05623
   Washburn MP, 2001, NAT BIOTECHNOL, V19, P242, DOI 10.1038/85686
   Wei LM, 2018, MOL CELL PROTEOMICS, V17, P148, DOI 10.1074/mcp.RA117.000124
   Wongkongkathep P, 2018, J AM SOC MASS SPECTR, V29, P1870, DOI 10.1007/s13361-018-2002-2
   Wörner TP, 2020, NAT METHODS, V17, P395, DOI 10.1038/s41592-020-0770-7
   Wu HY, 2015, J PROTEOME RES, V14, P3039, DOI 10.1021/pr501195t
   Wu ZJ, 2020, J PROTEOME RES, V19, P3867, DOI 10.1021/acs.jproteome.0c00469
   Wu ZJ, 2019, J AM SOC MASS SPECTR, V30, P2561, DOI 10.1007/s13361-019-02341-0
   Yang B, 2011, SER INF MANAGE SCI, V10, P6
   Yates JR, 2009, ANNU REV BIOMED ENG, V11, P49, DOI 10.1146/annurev-bioeng-061008-124934
   Yen HY, 2018, NATURE, V559, P424, DOI 10.1038/s41586-018-0325-6
   Yotti R, 2019, ANNU REV GENOM HUM G, V20, P129, DOI 10.1146/annurev-genom-083118-015306
   Yu DH, 2019, J AM SOC MASS SPECTR, V30, P2502, DOI 10.1007/s13361-019-02315-2
   Yu YQ, 2003, ANAL CHEM, V75, P6023, DOI 10.1021/ac0346196
   Yuan ZF, 2012, PROTEOMICS, V12, P226, DOI 10.1002/pmic.201100081
   Zenaidee MA, 2020, J AM SOC MASS SPECTR, V31, P1896, DOI 10.1021/jasms.0c00160
   Zhang H, 2003, NAT BIOTECHNOL, V21, P660, DOI 10.1038/nbt827
   Zhang H, 2011, CIRC-CARDIOVASC GENE, V4, P711, DOI 10.1161/CIRCGENETICS.110.957829
   Zhang YY, 2013, CHEM REV, V113, P2343, DOI 10.1021/cr3003533
   Zhou MW, 2020, CHEM SCI, V11, DOI 10.1039/d0sc04392c
   Zhu Y, 2018, NAT COMMUN, V9, DOI 10.1038/s41467-018-03367-w
   Zubarev RA, 1998, J AM CHEM SOC, V120, P3265, DOI 10.1021/ja973478k
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SN 1478-9450
EI 1744-8387
J9 EXPERT REV PROTEOMIC
JI Expert Rev. Proteomics
PD OCT 2
PY 2020
VL 17
IS 10
BP 719
EP 733
DI 10.1080/14789450.2020.1855982
EA DEC 2020
PG 15
WC Biochemical Research Methods
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology
GA QB9NX
UT WOS:000599689100001
PM 33232185
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Xie, X
   Zhu, DF
   Yang, JF
   Qiu, XE
   Cui, XY
   Tang, J
AF Xie, Xi
   Zhu, Dongfa
   Yang, Jifen
   Qiu, Xier
   Cui, Xiaoyu
   Tang, Jie
TI Molecular Cloning of Two Structure Variants of Crustacean Hyperglycemic
   Hormone (CHH) from the Swimming Crab (Portunus trituberculatus),
   and Their Gene Expression During Molting and Ovarian Development
SO ZOOLOGICAL SCIENCE
LA English
DT Article
DE crustacean hyperglycemic hormone; Portunus trituberculatus; cloning;
   gene expression; molting; ovarian development
ID CRAYFISH PROCAMBARUS-CLARKII; AMINO-ACID-SEQUENCE; INHIBITING HORMONE;
   SHORE CRAB; KURUMA PRAWN; BLUE-CRAB; CARBOHYDRATE-METABOLISM;
   PERICARDIAL ORGAN; AMERICAN CRAYFISH; CARCINUS-MAENAS
AB Two full-length cDNA (Pt-CHH1 and Pt-CHH2) sequences encoding crustacean hyperglycemic hormone (CHH) were cloned from tissues of the swimming crab (Portunus trituberculatus) using RACE. Pt-CHH1 was cloned from eyestalk, whereas Pt-CHH2 was cloned from thoracic ganglia. Sequence and structure analyses of Pt-CHH1 and Pt-CHH2 suggest that they may be generated from alternative splicing. Tissue distribution showed that transcript of Pt-CHH1 was only detected in eyestalk, while transcript of Pt-CHH2 was observed in several extra-eyestalk tissues. The transcript levels of Pt-CHH1 and Pt-CHH2 during molting and ovarian development were determined using qPCR. In molting process, level of Pt-CHH1 in eyestalk increased from stage A (postmolt), and to significant higher at stage C (intermolt), then decreased during premolt (D-0-D-4). In ovarian development, level of Pt-CHH1 in eyestalk decreased from previtellogenic stage (II), and to significant lower at mature stage (IV). The expression patterns of Pt-CHH2 in thoracic ganglia and Y-organ were distinct from that of Pt-CHH1 in eyestalk. The combined results suggest that Pt-CHH1 may be involved in inhibition of molting and ovarian development, whereas Pt-CHH2 may have other physiological functions.
C1 [Xie, Xi; Zhu, Dongfa; Yang, Jifen; Qiu, Xier; Cui, Xiaoyu; Tang, Jie] Ningbo Univ, Sch Marine Sci, Ningbo 315211, Zhejiang, Peoples R China.
C3 Ningbo University
RP Zhu, DF (corresponding author), Ningbo Univ, Sch Marine Sci, Ningbo 315211, Zhejiang, Peoples R China.
EM zhudongfa@nbu.edu.cn
FU National Science Foundation of China [41376152, 40976098]; Zhejiang
   Provincial National Science Foundation [LY13C190006]; K.C. Wong Magna
   Fund at Ningbo University
FX This research was funded by grants from the National Science Foundation
   of China (Nos. 41376152, 40976098), the Zhejiang Provincial National
   Science Foundation (No. LY13C190006) and the K.C. Wong Magna Fund at
   Ningbo University.
CR Abramowitz AA, 1944, BIOL BULL-US, V86, P1, DOI 10.2307/1537946
   Böcking D, 2002, CRUSTACEAN NERVOUS SYSTEM, P84
   Chang ES, 2011, CHEMICAL COMMUNICATION IN CRUSTACEANS, P413, DOI 10.1007/978-0-387-77101-4_21
   Chang ES, 1998, GEN COMP ENDOCR, V111, P359, DOI 10.1006/gcen.1998.7120
   CHANG ES, 1990, BIOCHEM BIOPH RES CO, V171, P818, DOI 10.1016/0006-291X(90)91219-I
   Choi CY, 2006, GEN COMP ENDOCR, V148, P383, DOI 10.1016/j.ygcen.2006.03.003
   Chung JS, 2008, ARCH INSECT BIOCHEM, V68, P171, DOI 10.1002/arch.20247
   Chung JS, 2008, FEBS J, V275, P693, DOI 10.1111/j.1742-4658.2007.06231.x
   Chung JS, 2005, ENDOCRINOLOGY, V146, P5545, DOI 10.1210/en.2005-0859
   Chung JS, 2003, EUR J BIOCHEM, V270, P3280, DOI 10.1046/j.1432-1033.2003.03720.x
   Chung JS, 1999, P NATL ACAD SCI USA, V96, P13103, DOI 10.1073/pnas.96.23.13103
   De Kleijn DPV, 1998, INVERTEBR REPROD DEV, V33, P263, DOI 10.1080/07924259.1998.9652637
   de Kleijn DPV, 1998, J ENDOCRINOL, V156, P291, DOI 10.1677/joe.0.1560291
   DeKleijn DPV, 1995, COMP BIOCHEM PHYS B, V112, P573, DOI 10.1016/0305-0491(95)00126-3
   Dircksen H, 2001, BIOCHEM J, V356, P159, DOI 10.1042/0264-6021:3560159
   Katayama H, 2003, J BIOL CHEM, V278, P9620, DOI 10.1074/jbc.M212962200
   KEGEL G, 1989, FEBS LETT, V255, P10, DOI 10.1016/0014-5793(89)81051-8
   KELLER R, 1992, EXPERIENTIA, V48, P439, DOI 10.1007/BF01928162
   Khayat M, 1998, GEN COMP ENDOCR, V110, P307, DOI 10.1006/gcen.1998.7078
   Kung PC, 2013, GEN COMP ENDOCR, V186, P80, DOI 10.1016/j.ygcen.2013.03.010
   Lacombe C, 1999, NEUROPEPTIDES, V33, P71, DOI 10.1054/npep.1999.0016
   Lee KJ, 2007, GEN COMP ENDOCR, V154, P174, DOI 10.1016/j.ygcen.2007.05.019
   Liu MQ, 2014, PEPTIDES, V53, P115, DOI 10.1016/j.peptides.2013.07.030
   Livak KJ, 2001, METHODS, V25, P402, DOI 10.1006/meth.2001.1262
   Nagai C, 2011, GEN COMP ENDOCR, V172, P293, DOI 10.1016/j.ygcen.2011.03.019
   Nakatsuji T, 2004, GEN COMP ENDOCR, V135, P358, DOI 10.1016/j.ygcen.2003.11.001
   Nakatsuji T, 2000, ZOOL SCI, V17, P1129, DOI 10.2108/zsj.17.1129
   Santos EA, 1997, PHYSIOL ZOOL, V70, P415, DOI 10.1086/515846
   SANTOS EA, 1993, COMP BIOCHEM PHYS A, V106, P405, DOI 10.1016/0300-9629(93)90234-U
   Serrano L, 2003, J EXP BIOL, V206, P979, DOI 10.1242/jeb.00178
   Shen Jie Shen Jie, 2011, Journal of Fisheries of China, V35, P1481
   SOYEZ D, 1994, J BIOL CHEM, V269, P18295
   Spanings-Pierrot C, 2000, GEN COMP ENDOCR, V119, P340, DOI 10.1006/gcen.2000.7527
   Stewart MJ, 2013, COMP BIOCHEM PHYS A, V164, P276, DOI 10.1016/j.cbpa.2012.10.029
   Tsai KW, 2008, GEN COMP ENDOCR, V159, P16, DOI 10.1016/j.ygcen.2008.07.014
   Tsutsui N, 2005, GEN COMP ENDOCR, V144, P232, DOI 10.1016/j.ygcen.2005.06.001
   Wang ChunJian Wang ChunJian, 2013, Acta Hydrobiologica Sinica, V37, P22
   WEBSTER SG, 1993, P ROY SOC B-BIOL SCI, V251, P53, DOI 10.1098/rspb.1993.0008
   WEBSTER SG, 1986, J COMP PHYSIOL B, V156, P617, DOI 10.1007/BF00692738
   Webster SG, 2012, GEN COMP ENDOCR, V175, P217, DOI 10.1016/j.ygcen.2011.11.035
   Wu HJ, 2012, ZOOL STUD, V51, P288
   Yao Gui-gui, 2007, Zoological Research, V28, P423
   Zheng JY, 2010, GEN COMP ENDOCR, V169, P174, DOI 10.1016/j.ygcen.2010.07.013
NR 43
TC 11
Z9 13
U1 0
U2 35
PU ZOOLOGICAL SOC JAPAN
PI TOKYO
PA HONGO MT BUILDING 4F, HONGO 7-2-2, BUNKYO-KU, TOKYO, 113-0033, JAPAN
SN 0289-0003
J9 ZOOL SCI
JI Zool. Sci.
PD DEC
PY 2014
VL 31
IS 12
BP 802
EP 809
DI 10.2108/zs140053
PG 8
WC Zoology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Zoology
GA AW3CW
UT WOS:000346164100004
PM 25483792
DA 2025-04-10
ER

PT J
AU Missale, C
   Nash, SR
   Robinson, SW
   Jaber, M
   Caron, MG
AF Missale, C
   Nash, SR
   Robinson, SW
   Jaber, M
   Caron, MG
TI Dopamine receptors: From structure to function
SO PHYSIOLOGICAL REVIEWS
LA English
DT Review
ID SPONTANEOUSLY HYPERTENSIVE RATS; EPIDERMAL GROWTH-FACTOR;
   PROTEIN-KINASE-C; NA-K-ATPASE; SITE-DIRECTED MUTAGENESIS;
   ANTERIOR-PITUITARY-CELLS; MESSENGER-RNA LEVELS; HAMSTER OVARY CELLS;
   INDUCED ALDOSTERONE SECRETION; NUCLEOTIDE-BINDING-PROTEINS
AB The diverse physiological actions of dopamine are mediated by at least live distinct G protein-coupled receptor subtypes. Two D-1-like receptor subtypes (D-1 and D-5) couple to the G protein G(s) and activate adenylyl cyclase. The other receptor subtypes belong to the D-2-like subfamily (D-2, D-3, and D-4) and are prototypic of G protein-coupled receptors that inhibit adenylyl cyclase and activate K+ channels. The genes for the D-1 and D-5 receptors a-e intronless, but pseudogenes of the D-5 exist. The D-2 and D-3 receptors vary in Certain tissues and species as a result of alternative splicing, and the human D-4 receptor gene exhibits extensive polymorphic variation. Ln the central nervous system, dopamine receptors are widely expressed because they are involved in the control of locomotion, cognition, emotion, and affect as well as neuroendocrine secretion. Ln the periphery, dopamine receptors are present more prominently in kidney, vasculature, and pituitary, where they affect mainly sodium homeostasis, vascular tone, and hormone secretion. Numerous genetic linkage analysis studies have failed so far to reveal unequivocal evidence for the involvement of one of these receptors in the etiology of various central nervous system disorders. However, targeted deletion of several of these dopamine receptor genes in mice should provide valuable information about their physiological functions.
C1 Duke Univ, Med Ctr, Dept Cell Biol, Howard Hughes Med Inst Labs, Durham, NC 27710 USA.
   Duke Univ, Med Ctr, Dept Med, Howard Hughes Med Inst Labs, Durham, NC 27710 USA.
C3 Duke University; Duke University
RP Duke Univ, Med Ctr, Dept Cell Biol, Howard Hughes Med Inst Labs, Durham, NC 27710 USA.
RI JABER, Mohamed/IQW-5358-2023
OI Jaber, Mohamed/0000-0003-2536-1913
CR ALBERT PR, 1990, J BIOL CHEM, V265, P2098
   ALEXANDER RW, 1974, J CLIN INVEST, V54, P194, DOI 10.1172/JCI107743
   AMENTA F, 1990, J PHARMACOL EXP THER, V253, P246
   AMENTA F, 1990, AM J HYPERTENS, V3, pS34, DOI 10.1093/ajh/3.6.34S
   AMENTA F, 1990, J AUTON PHARMACOL, V10, P373, DOI 10.1111/j.1474-8673.1990.tb00037.x
   AMENTA F, 1994, EUR J ENDOCRINOL, V131, P91, DOI 10.1530/eje.0.1310091
   ANDERSEN PH, 1990, TRENDS PHARMACOL SCI, V11, P231, DOI 10.1016/0165-6147(90)90249-8
   ANDREJAK M, 1986, CLIN PHARMACOL THER, V40, P610, DOI 10.1038/clpt.1986.234
   ANTONIPILLAI I, 1989, HYPERTENSION, V13, P463, DOI 10.1161/01.HYP.13.5.463
   AOKI K, 1989, CLIN EXP HYPERTENS A, V11, P403, DOI 10.3109/10641968909045447
   ARIANO MA, 1992, NEUROSCI LETT, V144, P215, DOI 10.1016/0304-3940(92)90753-T
   ARNSTEN AFT, 1995, J NEUROSCI, V15, P3429
   ARNT J, 1992, EUR J PHARMACOL, V213, P259, DOI 10.1016/0014-2999(92)90690-6
   ARTALEJO CR, 1990, NATURE, V348, P239, DOI 10.1038/348239a0
   BAERTSCHI AJ, 1992, MOL ENDOCRINOL, V6, P2257, DOI 10.1210/me.6.12.2257
   BAINES AD, 1992, AM J PHYSIOL, V262, pF566, DOI 10.1152/ajprenal.1992.262.4.F566
   BAINES AD, 1986, AM J PHYSIOL, V250, pF674, DOI 10.1152/ajprenal.1986.250.4.F674
   BALK JH, 1995, NATURE, V377, P424
   BALL SG, 1977, CLIN SCI MOL MED, V52, pP20
   BATES MD, 1991, AM J PHYSIOL, V260, pF937, DOI 10.1152/ajprenal.1991.260.6.F937
   BECK FWJ, 1984, CLIN RES, V32, pA18
   BECK KD, 1993, NEUROSCIENCE, V52, P855, DOI 10.1016/0306-4522(93)90534-M
   BELL C, 1978, J NEUROCHEM, V31, P77, DOI 10.1111/j.1471-4159.1978.tb12435.x
   BELLOREUSS E, 1982, AM J PHYSIOL, V242, pF634, DOI 10.1152/ajprenal.1982.242.6.F634
   BENINGER RJ, 1989, NEUROSCI BIOBEHAV R, V13, P113, DOI 10.1016/S0149-7634(89)80019-3
   BENJONATHAN N, 1985, ENDOCR REV, V6, P564, DOI 10.1210/edrv-6-4-564
   Bergson C, 1995, J NEUROSCI, V15, P7821
   BERGSON C, 1995, P NATL ACAD SCI USA, V92, P3468, DOI 10.1073/pnas.92.8.3468
   BERNARD V, 1991, NEUROSCIENCE, V45, P117, DOI 10.1016/0306-4522(91)90108-Z
   BERTORELLO A, 1988, AM J PHYSIOL, V254, pF795, DOI 10.1152/ajprenal.1988.254.6.F795
   BERTORELLO A, 1990, AM J PHYSIOL, V259, pF924, DOI 10.1152/ajprenal.1990.259.6.F924
   BERTORELLO A, 1989, AM J PHYSIOL, V256, pF370, DOI 10.1152/ajprenal.1989.256.2.F370
   BERTORELLO AM, 1990, NATURE, V347, P386, DOI 10.1038/347386a0
   BERTORELLO AM, 1991, P NATL ACAD SCI USA, V88, P11359, DOI 10.1073/pnas.88.24.11359
   BIGORNIA L, 1990, J PHARMACOL EXP THER, V252, P586
   BIGORNIA L, 1988, J NEUROCHEM, V51, P999, DOI 10.1111/j.1471-4159.1988.tb03060.x
   BIRKHAUSER M, 1979, ACTA ENDOCRINOL-COP, V91, P294, DOI 10.1530/acta.0.0910294
   BOUTHENET ML, 1991, BRAIN RES, V564, P203, DOI 10.1016/0006-8993(91)91456-B
   BOWYER JF, 1989, J PHARMACOL EXP THER, V248, P514
   BRADLEY T, 1986, P SOC EXP BIOL MED, V181, P492
   BREESE GR, 1987, J PHARMACOL EXP THER, V240, P167
   BRENE S, 1990, EXP BRAIN RES, V83, P96
   BRYSON SE, 1990, EUR J PHARMACOL, V183, P746, DOI 10.1016/0014-2999(90)92547-V
   BRYSON SE, 1992, EUR J PHARM-MOLEC PH, V225, P1, DOI 10.1016/0922-4106(92)90031-P
   BUCKLAND PR, 1992, PSYCHOPHARMACOLOGY, V106, P479, DOI 10.1007/BF02244818
   BUGHI S, 1994, J CLIN ENDOCR METAB, V78, P1079, DOI 10.1210/jc.78.5.1079
   BUNZOW JR, 1988, NATURE, V336, P783, DOI 10.1038/336783a0
   CACHERO S, 1992, RENAL PHYSIOL BIOCH, V15, P83
   CADET JL, 1992, MOL BRAIN RES, V12, P59, DOI 10.1016/0169-328X(92)90068-M
   CADNAPAPHORNCHAI P, 1977, AM J PHYSIOL, V232, pF524, DOI 10.1152/ajprenal.1977.232.6.F524
   CAINE SB, 1993, SCIENCE, V260, P1814, DOI 10.1126/science.8099761
   CANONICO PL, 1983, ENDOCRINOLOGY, V113, P7, DOI 10.1210/endo-113-1-7
   CAREY RM, 1984, J CLIN INVEST, V74, P2198, DOI 10.1172/JCI111646
   CAREY RM, 1986, HYPERTENSION, V8, P399, DOI 10.1161/01.HYP.8.5.399
   CAREY RM, 1979, J CLIN INVEST, V63, P727, DOI 10.1172/JCI109356
   CAREY RM, 1980, J CLIN INVEST, V66, P10, DOI 10.1172/JCI109822
   CAREY RM, 1982, J CLIN ENDOCR METAB, V54, P463, DOI 10.1210/jcem-54-2-463
   CAREY RM, 1981, J CLIN ENDOCR METAB, V52, P903, DOI 10.1210/jcem-52-5-903
   CARON MG, 1978, J BIOL CHEM, V253, P2244
   CARTERRUSSEL HR, 1995, SOC NEUR ABSTR, V559, P11
   CASPER D, 1994, J NEUROCHEM, V62, P2166
   CASPER D, 1995, J NEUROCHEM, V65, P1016
   CASS WA, 1991, J NEUROCHEM, V57, P147, DOI 10.1111/j.1471-4159.1991.tb02109.x
   CASTELLANO MA, 1993, MOL PHARMACOL, V44, P649
   CASTELLETTI L, 1989, J PHYSIOL-LONDON, V410, P251, DOI 10.1113/jphysiol.1989.sp017531
   CASTRO SW, 1993, J NEUROCHEM, V60, P372, DOI 10.1111/j.1471-4159.1993.tb05863.x
   CENI MA, 1992, EUR J NEUROSCI, V4, P376
   CHATZIANTONIOU C, 1995, P NATL ACAD SCI USA, V92, P2924, DOI 10.1073/pnas.92.7.2924
   CHEN CJ, 1993, N-S ARCH PHARMACOL, V347, P289, DOI 10.1007/BF00167447
   CHEN CJ, 1993, HYPERTENSION, V21, P364, DOI 10.1161/01.HYP.21.3.364
   CHEN CJ, 1991, J PHARMACOL EXP THER, V256, P486
   CHEN CJ, 1992, HYPERTENSION, V19, P102, DOI 10.1161/01.HYP.19.1.102
   CHEN CJ, 1991, CLIN EXP HYPERTENS A, V13, P1117, DOI 10.3109/10641969109042117
   CHIO CL, 1994, J BIOL CHEM, V269, P11813
   CHIO CL, 1994, MOL PHARMACOL, V45, P51
   CHOI WS, 1995, MOL BRAIN RES, V31, P86
   CHUNG FZ, 1988, J BIOL CHEM, V263, P4052
   CIVELLI O, 1993, ANNU REV PHARMACOL, V33, P281, DOI 10.1146/annurev.pharmtox.33.1.281
   CLARK D, 1987, SYNAPSE, V1, P347, DOI 10.1002/syn.890010408
   COHEN AI, 1992, P NATL ACAD SCI USA, V89, P12093, DOI 10.1073/pnas.89.24.12093
   COHEN AI, 1993, AM J PHYSIOL, V264, pF61
   COOK CCH, 1994, J ROY SOC MED, V87, P400
   COON H, 1993, AM J HUM GENET, V52, P327
   COTE TE, 1982, NEUROENDOCRINOLOGY, V35, P217, DOI 10.1159/000123384
   COX BA, 1992, J NEUROCHEM, V59, P627, DOI 10.1111/j.1471-4159.1992.tb09416.x
   CROCQ MA, 1992, J MED GENET, V29, P858, DOI 10.1136/jmg.29.12.858
   CUCHE JL, 1976, J CLIN INVEST, V58, P71, DOI 10.1172/JCI108461
   CUCHE JL, 1972, CLIN SCI, V43, P381
   CUNNAH D, 1991, CLIN ENDOCRINOL, V34, P231, DOI 10.1111/j.1365-2265.1991.tb00299.x
   CURRAN EJ, 1995, J COMP NEUROL, V361, P57, DOI 10.1002/cne.903610106
   DALTOSO R, 1989, EMBO J, V8, P4025, DOI 10.1002/j.1460-2075.1989.tb08585.x
   DALY SA, 1992, NEUROCHEM INT, V20, pS135
   DALY SA, 1993, NEUROPHARMACOLOGY, V32, P509, DOI 10.1016/0028-3908(93)90177-5
   DALY SA, 1993, PSYCHOPHARMACOLOGY, V113, P45, DOI 10.1007/BF02244332
   DEARRY A, 1990, NATURE, V347, P72, DOI 10.1038/347072a0
   DEBRUYN A, 1994, AM J PSYCHIAT, V151, P102
   DEBSKASLIZIEN A, 1994, J AM SOC NEPHROL, V5, P1125
   DEBSKASLIZIEN A, 1994, AM J PHYSIOL, V266, pF858, DOI 10.1152/ajprenal.1994.266.6.F858
   DECAMILLI P, 1979, NATURE, V278, P252, DOI 10.1038/278252a0
   DEFEO ML, 1987, CLIN EXP HYPERTENS A, V9, P2049, DOI 10.3109/10641968709159074
   DEMCHYSHYN LL, 1995, J BIOL CHEM, V270, P4005, DOI 10.1074/jbc.270.8.4005
   DEUTCH AY, 1992, MOL CELL NEUROSCI, V3, P332, DOI 10.1016/1044-7431(92)90030-6
   DEUTCH AY, 1991, SCHIZOPHR RES, V4, P121, DOI 10.1016/0920-9964(91)90030-U
   DHANASEKARAN N, 1994, J BIOL CHEM, V269, P11802
   DIAZ J, 1994, EUR J NEUROSCI, V6, P1384, DOI 10.1111/j.1460-9568.1994.tb00329.x
   DIAZ J, 1995, NEUROSCIENCE, V65, P731, DOI 10.1016/0306-4522(94)00527-C
   DIBONA GF, 1990, AM J HYPERTENS, V3, pS64, DOI 10.1093/ajh/3.6.64S
   DICHIARA G, 1995, DRUG ALCOHOL DEPEN, V38, P95, DOI 10.1016/0376-8716(95)01118-I
   DIMARZO V, 1993, J NEUROSCI, V13, P4846
   DINERSTEIN RJ, 1979, SCIENCE, V205, P497, DOI 10.1126/science.451614
   DOHLMAN HG, 1987, BIOCHEMISTRY-US, V26, P2657, DOI 10.1021/bi00384a001
   DOHLMAN HG, 1990, BIOCHEMISTRY-US, V29, P2335, DOI 10.1021/bi00461a018
   DOWNES RP, 1993, EUR J PHARMACOL, V234, P135, DOI 10.1016/0014-2999(93)90718-W
   DRAGO J, 1994, P NATL ACAD SCI USA, V91, P12564, DOI 10.1073/pnas.91.26.12564
   DRAKE CR, 1984, METABOLISM, V33, P696, DOI 10.1016/0026-0495(84)90207-5
   DREHER JK, 1989, BRAIN RES, V487, P267, DOI 10.1016/0006-8993(89)90831-7
   EDWARDS RM, 1985, AM J PHYSIOL, V248, pF183, DOI 10.1152/ajprenal.1985.248.2.F183
   EDWARDS RM, 1986, EUR J PHARMACOL, V126, P167, DOI 10.1016/0014-2999(86)90756-9
   EINHORN LC, 1991, J NEUROSCI, V11, P3727
   ELSHOLTZ HP, 1991, J BIOL CHEM, V266, P22919
   ENJALBERT A, 1983, MOL PHARMACOL, V23, P576
   ENJALBERT A, 1990, J BIOL CHEM, V265, P18816
   FELDER CC, 1989, KIDNEY INT, V36, P183, DOI 10.1038/ki.1989.178
   FELDER CC, 1991, P NATL ACAD SCI USA, V88, P6477, DOI 10.1073/pnas.88.15.6477
   FELDER CC, 1989, J BIOL CHEM, V264, P8739
   FELDER CC, 1989, J PHARMACOL EXP THER, V248, P171
   FELDER CC, 1993, AM J PHYSIOL, V264, pF1032, DOI 10.1152/ajprenal.1993.264.6.F1032
   FELDER CC, 1990, AM J PHYSIOL, V259, pF297, DOI 10.1152/ajprenal.1990.259.2.F297
   FELDER RA, 1984, AM J PHYSIOL, V246, pF557, DOI 10.1152/ajprenal.1984.246.5.F557
   FELDER RA, 1993, AM J PHYSIOL, V264, pR726, DOI 10.1152/ajpregu.1993.264.4.R726
   FELDER RA, 1990, AM J HYPERTENS, V3, pS96, DOI 10.1093/ajh/3.6.96S
   FELDER RA, 1988, AM J PHYSIOL, V255, pF970, DOI 10.1152/ajprenal.1988.255.5.F970
   FELDER RA, 1989, AM J PHYSIOL, V257, pF315, DOI 10.1152/ajprenal.1989.257.3.F315
   FELDER RA, 1990, HYPERTENSION, V15, P560, DOI 10.1161/01.HYP.15.6.560
   FELIX R, 1995, ENDOCRINOLOGY, V136, P939, DOI 10.1210/en.136.3.939
   FERRARI G, 1991, J NEUROSCI RES, V30, P493, DOI 10.1002/jnr.490300306
   FISHBURN CS, 1993, J BIOL CHEM, V268, P5872
   FLORIO T, 1992, J BIOL CHEM, V267, P24169
   FOUCART S, 1988, CLIN EXP PHARMACOL P, V15, P601, DOI 10.1111/j.1440-1681.1988.tb01119.x
   FRAIL DE, 1993, MOL PHARMACOL, V44, P1113
   FRANKLIN KBJ, 1983, PHARMACOL BIOCHEM BE, V18, P747, DOI 10.1016/0091-3057(83)90018-7
   FRASER CM, 1989, J BIOL CHEM, V264, P9266
   FREDERICKSON ED, 1985, AM J PHYSIOL, V249, pF236, DOI 10.1152/ajprenal.1985.249.2.F236
   FREEDMAN SB, 1994, J PHARMACOL EXP THER, V268, P417
   Fremeau R.J., 1991, P NATL ACAD SCI US, V91, P12564
   GALLOPAYET N, 1991, MOL CELL ENDOCRINOL, V81, P11, DOI 10.1016/0303-7207(91)90200-C
   GANZ MB, 1990, J BIOL CHEM, V265, P8989
   GAO DQ, 1994, AM J PHYSIOL, V266, pF646, DOI 10.1152/ajprenal.1994.266.4.F646
   GARDETTE R, 1994, NEUROENDOCRINOLOGY, V59, P10, DOI 10.1159/000126632
   GARG LC, 1985, AM J PHYSIOL, V249, pF863, DOI 10.1152/ajprenal.1985.249.6.F863
   GELERNTER J, 1993, AM J PSYCHIAT, V150, P449
   GERFEN CR, 1990, SCIENCE, V250, P1429, DOI 10.1126/science.2147780
   GERFEN CR, 1992, TRENDS NEUROSCI, V15, P133, DOI 10.1016/0166-2236(92)90355-C
   GERLACH J, 1985, BRIT J PSYCHIAT, V147, P283, DOI 10.1192/bjp.147.3.283
   GERSHANIK O, 1983, NEUROLOGY, V33, P1489, DOI 10.1212/WNL.33.11.1489
   GESEK FA, 1991, AM J PHYSIOL, V261, pF526, DOI 10.1152/ajprenal.1991.261.3.F526
   GESEK FA, 1990, AM J PHYSIOL, V258, pF514, DOI 10.1152/ajprenal.1990.258.3.F514
   GEYER MA, 1976, BRAIN RES, V106, P257, DOI 10.1016/0006-8993(76)91024-6
   GINGRICH JA, 1993, ANNU REV NEUROSCI, V16, P299, DOI 10.1146/annurev.ne.16.030193.001503
   GIROS B, 1991, BIOCHEM BIOPH RES CO, V176, P1584, DOI 10.1016/0006-291X(91)90469-N
   GIROS B, 1989, NATURE, V342, P923, DOI 10.1038/342923a0
   Giros B, 1996, NATURE, V379, P606, DOI 10.1038/379606a0
   GLAHN RP, 1993, AM J PHYSIOL, V264, pF618, DOI 10.1152/ajprenal.1993.264.4.F618
   GOLDBERG LI, 1963, NEW ENGL J MED, V269, P1060, DOI 10.1056/NEJM196311142692003
   GOLDBERG LI, 1985, CIRCULATION, V72, P245, DOI 10.1161/01.CIR.72.2.245
   GOLDBERG LI, 1978, ANNU REV PHARMACOL, V18, P57, DOI 10.1146/annurev.pa.18.040178.000421
   Goldman D, 1993, Recent Dev Alcohol, V11, P231
   GRANDY DK, 1989, P NATL ACAD SCI USA, V86, P9762, DOI 10.1073/pnas.86.24.9762
   GRANDY DK, 1991, P NATL ACAD SCI USA, V88, P9175, DOI 10.1073/pnas.88.20.9175
   GRANDY DK, 1989, AM J HUM GENET, V45, P778
   GRAYBIEL AM, 1990, P NATL ACAD SCI USA, V87, P6912, DOI 10.1073/pnas.87.17.6912
   GREIF GJ, 1995, J NEUROSCI, V15, P4533
   GRENADER A, 1991, AM J PHYSIOL, V260, pF906, DOI 10.1152/ajprenal.1991.260.6.F906
   GRENADER AC, 1995, AM J PHYSIOL-RENAL, V268, pF423, DOI 10.1152/ajprenal.1995.268.3.F423
   GUIRAMAND J, 1995, J BIOL CHEM, V270, P7354, DOI 10.1074/jbc.270.13.7354
   GURICH RW, 1994, AM J PHYSIOL-RENAL, V267, pF1069, DOI 10.1152/ajprenal.1994.267.6.F1069
   HANSELL P, 1991, KIDNEY INT, V39, P253, DOI 10.1038/ki.1991.30
   HANSON G, 1981, NEUROPHARMACOLOGY, V20, P541, DOI 10.1016/0028-3908(81)90206-9
   HANSON GR, 1987, EUR J PHARMACOL, V144, P245, DOI 10.1016/0014-2999(87)90527-9
   HARVEY JN, 1984, CLIN SCI, V67, P83, DOI 10.1042/cs0670083
   HEBERT RL, 1991, J CLIN INVEST, V87, P1992, DOI 10.1172/JCI115227
   HEGDE SS, 1989, J PHARMACOL EXP THER, V251, P1237
   HEGDE SS, 1990, AM J HYPERTENS, V3, pS78, DOI 10.1093/ajh/3.6.78S
   HEGDE SS, 1989, HYPERTENSION, V13, P828, DOI 10.1161/01.HYP.13.6.828
   HEGDE SS, 1991, CLIN EXP HYPERTENS A, V13, P357, DOI 10.3109/10641969109045056
   HEGDE SS, 1992, CLIN EXP HYPERTENS A, V14, P1169, DOI 10.3109/10641969209038199
   HERSCH SM, 1995, J NEUROSCI, V15, P5222
   HERVE D, 1993, J NEUROSCI, V13, P2237, DOI 10.1523/jneurosci.13-05-02237.1993
   HIBERT MF, 1993, TRENDS PHARMACOL SCI, V14, P7, DOI 10.1016/0165-6147(93)90106-T
   HIBERT MF, 1991, MOL PHARMACOL, V40, P8
   HOLLENBERG NK, 1974, J CLIN INVEST, V54, P34, DOI 10.1172/JCI107748
   HOLLIS CM, 1992, BIOCHEM PHARMACOL, V43, P1947, DOI 10.1016/0006-2952(92)90637-X
   HOPE B, 1992, P NATL ACAD SCI USA, V89, P5764, DOI 10.1073/pnas.89.13.5764
   HORIUCHI A, 1993, MOL PHARMACOL, V43, P281
   HORIUCHI A, 1992, AM J PHYSIOL, V263, pF1105, DOI 10.1152/ajprenal.1992.263.6.F1105
   HORSTMAN DA, 1990, J BIOL CHEM, V265, P21590
   HUANG Q, 1992, P NATL ACAD SCI USA, V89, P11988, DOI 10.1073/pnas.89.24.11988
   HUBBARD PC, 1995, J MOL ENDOCRINOL, V14, P139, DOI 10.1677/jme.0.0140139
   HUGHES A, 1989, BIOCHEM PHARMACOL, V38, P781, DOI 10.1016/0006-2952(89)90231-1
   HUGHES A, 1989, BIOCHEM SOC T, V17, P918, DOI 10.1042/bst0170918
   HUGHES AD, 1987, J HYPERTENS, V5, P337, DOI 10.1097/00004872-198706000-00012
   HUGHES JM, 1986, J HYPERTENS, V4, pS106
   HUNTLEY GW, 1992, MOL BRAIN RES, V15, P181, DOI 10.1016/0169-328X(92)90107-M
   HUO T, 1991, P NATL ACAD SCI USA, V88, P3170, DOI 10.1073/pnas.88.8.3170
   HUO T, 1989, AM J PHYSIOL, V257, pF414, DOI 10.1152/ajprenal.1989.257.3.F414
   HUO TH, 1991, AM J PHYSIOL, V261, pF647, DOI 10.1152/ajprenal.1991.261.4.F647
   HUO TL, 1991, AM J PHYSIOL, V261, pF655, DOI 10.1152/ajprenal.1991.261.4.F655
   Iimura O, 1987, Agents Actions Suppl, V22, P247
   IIMURA O, 1990, J AUTON PHARMACOL, V10, pS73
   INGRAHAM HA, 1990, ANNU REV PHYSIOL, V52, P773
   ISAAC J, 1992, J AM SOC NEPHROL, V2, P1601
   ISRAEL JM, 1987, J PHYSIOL-LONDON, V390, P1, DOI 10.1113/jphysiol.1987.sp016682
   JABER M, 1995, MOL BRAIN RES, V32, P156, DOI 10.1016/0169-328X(95)00064-Y
   JABER M, 1995, NEUROSCIENCE, V65, P1041, DOI 10.1016/0306-4522(94)00537-F
   JABER M, 1992, MOL BRAIN RES, V15, P189, DOI 10.1016/0169-328X(92)90108-N
   JABER M, 1994, MOL BRAIN RES, V23, P14, DOI 10.1016/0169-328X(94)90206-2
   JACKSON DM, 1994, PHARMACOL THERAPEUT, V64, P291, DOI 10.1016/0163-7258(94)90041-8
   JADHAV AL, 1992, CLIN EXP HYPERTENS A, V14, P653, DOI 10.3109/10641969209036213
   JADHAV AL, 1991, CLIN EXP HYPERTENS A, V13, P1371, DOI 10.3109/10641969109048799
   JENSEN S, 1992, HUM HERED, V42, P269, DOI 10.1159/000154081
   JOSE PA, 1993, PEDIATR NEPHROL, V7, P859, DOI 10.1007/BF01213374
   JOSE PA, 1992, J AM SOC NEPHROL, V2, P1265
   KANE JM, 1994, BRIT J PSYCHIAT, V165, P22, DOI 10.1192/S0007125000293173
   KANEDA Y, 1983, MINER ELECTROL METAB, V9, P147
   KANTERMAN RY, 1991, MOL PHARMACOL, V39, P364
   KEBABIAN JW, 1979, NATURE, V277, P93, DOI 10.1038/277093a0
   KEEFE KA, 1995, NEUROSCIENCE, V66, P903, DOI 10.1016/0306-4522(95)00024-D
   KELSOE JR, 1993, NEUROPSYCHOPHARMACOL, V9, P293, DOI 10.1038/npp.1993.65
   KIMURA K, 1995, J NEUROCHEM, V64, P2118
   KIMURA K, 1995, J BIOL CHEM, V270, P14672, DOI 10.1074/jbc.270.24.14672
   KINOSHITA S, 1989, J CLIN INVEST, V84, P1849, DOI 10.1172/JCI114371
   KITAI ST, 1993, ADV NEUROL, V60, P40
   KJELSBERG MA, 1992, J BIOL CHEM, V267, P1430
   KORNETSKY C, 1981, BRAIN RES, V209, P496, DOI 10.1016/0006-8993(81)90177-3
   Koshikawa N, 1994, Rev Neurosci, V5, P331
   KOYAMA S, 1985, JPN J PHARMACOL, V38, P25, DOI 10.1254/jjp.38.25
   KRISHNA GG, 1985, J LAB CLIN MED, V105, P214
   KUCHEL O, 1989, CLIN EXP HYPERTENS A, V11, P217, DOI 10.3109/10641968909045426
   KUCHEL O, 1987, CLIN EXP HYPERTEN S1, V11, P217
   KUKSTAS LA, 1991, ENDOCRINOLOGY, V129, P1101, DOI 10.1210/endo-129-2-1101
   KURTZ A, 1988, J CARDIOVASC PHARM, V12, P658, DOI 10.1097/00005344-198812000-00006
   LAHOSTE GJ, 1993, P NATL ACAD SCI USA, V90, P7451, DOI 10.1073/pnas.90.16.7451
   LAITINEN JT, 1993, J NEUROCHEM, V61, P1461, DOI 10.1111/j.1471-4159.1993.tb13641.x
   LAJINESS ME, 1993, J PHARMACOL EXP THER, V267, P1573
   LANDWEHRMEYER B, 1993, EUR J NEUROSCI, V5, P145, DOI 10.1111/j.1460-9568.1993.tb00480.x
   LANDWEHRMEYER B, 1993, MOL BRAIN RES, V18, P187, DOI 10.1016/0169-328X(93)90188-U
   LEE MR, 1990, J AUTON PHARMACOL, V10, pS103, DOI 10.1111/j.1474-8673.1990.tb00235.x
   LEE MR, 1993, CLIN SCI, V84, P357, DOI 10.1042/cs0840357
   LEE MR, 1982, CLIN SCI, V62, P439, DOI 10.1042/cs0620439
   LEFKOWITZ RJ, 1993, TRENDS PHARMACOL SCI, V14, P303, DOI 10.1016/0165-6147(93)90048-O
   LEIER CV, 1978, CIRCULATION, V58, P466, DOI 10.1161/01.CIR.58.3.466
   LEMOAL M, 1991, PHYSIOL REV, V71, P155, DOI 10.1152/physrev.1991.71.1.155
   LeMoine C, 1996, NEUROSCIENCE, V73, P131, DOI 10.1016/0306-4522(96)00029-2
   LEMOINE C, 1990, P NATL ACAD SCI USA, V87, P230, DOI 10.1073/pnas.87.1.230
   LEMOINE C, 1995, J COMP NEUROL, V355, P418, DOI 10.1002/cne.903550308
   LEMOINE C, 1991, P NATL ACAD SCI USA, V88, P4205, DOI 10.1073/pnas.88.10.4205
   LESTER J, 1993, BRAIN RES, V621, P106, DOI 10.1016/0006-8993(93)90303-5
   LEVESQUE D, 1992, P NATL ACAD SCI USA, V89, P8155, DOI 10.1073/pnas.89.17.8155
   LEVESQUE D, 1995, P NATL ACAD SCI USA, V92, P1719, DOI 10.1073/pnas.92.5.1719
   LEVEY AI, 1993, P NATL ACAD SCI USA, V90, P8861, DOI 10.1073/pnas.90.19.8861
   LEVIN ED, 1995, ANN NY ACAD SCI, V757, P245, DOI 10.1111/j.1749-6632.1995.tb17481.x
   LEW AM, 1995, J BIOL CHEM, V270, P7156, DOI 10.1074/jbc.270.13.7156
   LIN CW, 1995, MOL PHARMACOL, V47, P131
   LIU LX, 1994, SYNAPSE, V17, P230, DOI 10.1002/syn.890170404
   LIU YF, 1992, MOL ENDOCRINOL, V6, P1815, DOI 10.1210/me.6.11.1815
   LIU YF, 1992, J NEUROCHEM, V59, P2311
   LIU YF, 1994, J BIOL CHEM, V269, P13880
   LLEDO PM, 1992, NEURON, V8, P455, DOI 10.1016/0896-6273(92)90273-G
   LLEDO PM, 1990, ENDOCRINOLOGY, V127, P990, DOI 10.1210/endo-127-3-990
   LLEDO PM, 1990, NEUROENDOCRINOLOGY, V52, P545, DOI 10.1159/000125650
   LOMBARDI C, 1988, EUR J CLIN PHARMACOL, V35, P323, DOI 10.1007/BF00558273
   LYON RA, 1987, J NEUROCHEM, V48, P631, DOI 10.1111/j.1471-4159.1987.tb04139.x
   MACCIARDI F, 1994, ARCH GEN PSYCHIAT, V51, P288
   MACKENZIE RG, 1994, EUR J PHARM-MOLEC PH, V266, P79, DOI 10.1016/0922-4106(94)90212-7
   MAHAN LC, 1990, P NATL ACAD SCI USA, V87, P2196, DOI 10.1073/pnas.87.6.2196
   MALCHOFF CD, 1986, J CLIN ENDOCR METAB, V63, P197, DOI 10.1210/jcem-63-1-197
   MALDONADO R, 1993, PHARMACOL BIOCHEM BE, V45, P239, DOI 10.1016/0091-3057(93)90112-7
   MALMBERG A, 1993, MOL PHARMACOL, V43, P749
   MANDEL LJ, 1985, ANNU REV PHYSIOL, V47, P85
   MANNELLI M, 1988, J CLIN ENDOCR METAB, V66, P626, DOI 10.1210/jcem-66-3-626
   MANNELLI M, 1984, J CLIN ENDOCR METAB, V59, P74, DOI 10.1210/jcem-59-1-74
   MANSOUR A, 1992, EUR J PHARM-MOLEC PH, V227, P205, DOI 10.1016/0922-4106(92)90129-J
   MARTRES MP, 1992, J NEUROCHEM, V58, P673, DOI 10.1111/j.1471-4159.1992.tb09770.x
   MASSRY SG, 1973, ARCH INTERN MED, V131, P828, DOI 10.1001/archinte.131.6.828
   MATSUMOTO M, 1995, MOL BRAIN RES, V29, P157, DOI 10.1016/0169-328X(94)00245-A
   MATTHYSSE S, 1974, J PSYCHIAT RES, V11, P107, DOI 10.1016/0022-3956(74)90081-8
   MCALLISTER G, 1995, J RECEPT SIGNAL TR R, V15, P267, DOI 10.3109/10799899509045220
   MCDONALD RH, 1964, J CLIN INVEST, V43, P1116, DOI 10.1172/JCI104996
   MCDONALD WM, 1984, MOL CELL ENDOCRINOL, V36, P201, DOI 10.1016/0303-7207(84)90037-6
   MCHALE M, 1994, FEBS LETT, V345, P147, DOI 10.1016/0014-5793(94)00423-4
   MCNAY JL, 1965, CIRC RES, V16, P510, DOI 10.1161/01.RES.16.6.510
   MEADORWOODRUFF JH, 1992, NEUROSCI LETT, V145, P209, DOI 10.1016/0304-3940(92)90024-2
   MEADORWOODRUFF JH, 1989, P NATL ACAD SCI USA, V86, P7625, DOI 10.1073/pnas.86.19.7625
   MEISTER B, 1989, P NATL ACAD SCI USA, V86, P8068, DOI 10.1073/pnas.86.20.8068
   MEISTER B, 1991, ACTA PHYSIOL SCAND, V143, P447, DOI 10.1111/j.1748-1716.1991.tb09258.x
   MELTZER HY, 1991, SCHIZOPHRENIA BULL, V17, P263, DOI 10.1093/schbul/17.2.263
   MELTZER HY, 1989, PSYCHOPHARMACOLOGY, V99, pS18, DOI 10.1007/BF00442554
   MEMO M, 1986, J NEUROCHEM, V47, P1689, DOI 10.1111/j.1471-4159.1986.tb13075.x
   MEMO M, 1986, J NEURAL TRANSM, P19
   MEYER MB, 1967, J PHARMACOL EXP THER, V156, P186
   MEYER ME, 1993, PHARMACOL BIOCHEM BE, V46, P269, DOI 10.1016/0091-3057(93)90352-T
   MISSALE C, 1991, ENDOCRINOLOGY, V128, P13, DOI 10.1210/endo-128-1-13
   MISSALE C, 1993, P NATL ACAD SCI USA, V90, P7961, DOI 10.1073/pnas.90.17.7961
   MISSALE C, 1995, ENDOCRINOLOGY, V136, P1205, DOI 10.1210/en.136.3.1205
   MISSALE C, 1989, J CARDIOVASC PHARM, V14, pS29, DOI 10.1097/00005344-198906148-00004
   MISSALE C, 1991, J BIOL CHEM, V266, P23392
   MISSALE C, 1986, ENDOCRINOLOGY, V119, P2227, DOI 10.1210/endo-119-5-2227
   MISSALE C, 1994, ENDOCRINOLOGY, V135, P290, DOI 10.1210/en.135.1.290
   MISSALE C, 1988, J PHARMACOL EXP THER, V246, P1137
   MISSALE C, 1988, J CARDIOVASC PHARM, V11, P643, DOI 10.1097/00005344-198806000-00003
   MISSALE C, 1995, BRIT J CANCER, V72, P1397, DOI 10.1038/bjc.1995.520
   MOISES HW, 1991, ARCH GEN PSYCHIAT, V48, P643
   MONSMA FJ, 1989, NATURE, V342, P926, DOI 10.1038/342926a0
   MONSMA FJ, 1990, P NATL ACAD SCI USA, V87, P6723, DOI 10.1073/pnas.87.17.6723
   MONSMA FJ, 1990, J NEUROCHEM, V54, P1200, DOI 10.1111/j.1471-4159.1990.tb01949.x
   MONTASTRUC JL, 1989, FUND CLIN PHARMACOL, V3, P665, DOI 10.1111/j.1472-8206.1989.tb00467.x
   MONTMAYEUR JP, 1991, P NATL ACAD SCI USA, V88, P3135, DOI 10.1073/pnas.88.8.3135
   MONTMAYEUR JP, 1993, MOL ENDOCRINOL, V7, P161, DOI 10.1210/me.7.2.161
   Mrzljak L, 1996, NATURE, V381, P245, DOI 10.1038/381245a0
   MUNEMURA M, 1980, ENDOCRINOLOGY, V107, P1676, DOI 10.1210/endo-107-6-1676
   MUTO S, 1985, EUR J PHARMACOL, V114, P393, DOI 10.1016/0014-2999(85)90386-3
   NAKAJIMA T, 1980, JPN J PHARMACOL, V30, P891, DOI 10.1254/jjp.30.891
   NAKAJIMA T, 1989, BRAIN RES, V501, P307, DOI 10.1016/0006-8993(89)90647-1
   NANKO S, 1993, LANCET, V341, P689, DOI 10.1016/0140-6736(93)90456-Q
   NANKO S, 1994, AM J MED GENET, V54, P264, DOI 10.1002/ajmg.1320540315
   NASH SR, 1993, MOL PHARMACOL, V44, P918
   NATHANS J, 1983, CELL, V34, P807, DOI 10.1016/0092-8674(83)90537-8
   NEVE KA, 1991, MOL PHARMACOL, V39, P733
   NEVE KA, 1992, J BIOL CHEM, V267, P25748
   NGUYEN TV, 1992, P NATL ACAD SCI USA, V89, P4270, DOI 10.1073/pnas.89.10.4270
   NISHI A, 1993, HYPERTENSION, V21, P767, DOI 10.1161/01.HYP.21.6.767
   NISHI A, 1992, ACTA PHYSIOL SCAND, V144, P263, DOI 10.1111/j.1748-1716.1992.tb09295.x
   NORMAND E, 1987, NEUROSCI LETT, V83, P232, DOI 10.1016/0304-3940(87)90091-7
   NOTH RH, 1980, J CLIN ENDOCR METAB, V51, P64, DOI 10.1210/jcem-51-1-64
   OATES NS, 1979, CLIN SCI, V56, P261, DOI 10.1042/cs0560261
   OCONNELL DP, 1995, AM J PHYSIOL-RENAL, V268, pF1185, DOI 10.1152/ajprenal.1995.268.6.F1185
   ODOWD BF, 1993, J NEUROCHEM, V60, P804, DOI 10.1111/j.1471-4159.1993.tb03224.x
   ODOWD BF, 1989, J BIOL CHEM, V264, P7564
   OHBU K, 1995, AM J PHYSIOL-REG I, V268, pR231, DOI 10.1152/ajpregu.1995.268.1.R231
   OHBU K, 1991, AM J PHYSIOL, V261, pF890, DOI 10.1152/ajprenal.1991.261.5.F890
   OHBU K, 1993, AM J PHYSIOL, V264, pF274, DOI 10.1152/ajprenal.1993.264.2.F274
   OLSEN NV, 1990, CLIN SCI, V78, P503, DOI 10.1042/cs0780503
   OMALLEY KL, 1992, NEW BIOL, V4, P137
   ONALI P, 1981, P NATL ACAD SCI-BIOL, V78, P6531, DOI 10.1073/pnas.78.10.6531
   ONALI P, 1985, MOL PHARMACOL, V28, P138
   OSIPENKO ON, 1994, ENDOCRINOLOGY, V134, P511, DOI 10.1210/en.134.1.511
   OVCHINNIKOV YA, 1988, FEBS LETT, V230, P1, DOI 10.1016/0014-5793(88)80628-8
   PACKARD MG, 1991, BEHAV NEUROSCI, V105, P295, DOI 10.1037/0735-7044.105.2.295
   Parsons LH, 1996, J NEUROCHEM, V67, P1078
   PAUL ML, 1992, J NEUROSCI, V12, P3729, DOI 10.1523/jneurosci.12-10-03729.1992
   PEDERSEN UB, 1994, EUR J PHARM-MOLEC PH, V267, P85, DOI 10.1016/0922-4106(94)90228-3
   PELLEGRINI I, 1989, J CLIN ENDOCR METAB, V69, P500, DOI 10.1210/jcem-69-3-500
   PENDLETON RG, 1976, ARCH INT PHARMACOD T, V222, P94
   PHILLIPS GD, 1994, PSYCHOPHARMACOLOGY, V114, P477, DOI 10.1007/BF02249339
   PILON C, 1994, EUR J PHARM-MOLEC PH, V268, P129, DOI 10.1016/0922-4106(94)90182-1
   PIOMELLI D, 1991, NATURE, V353, P164, DOI 10.1038/353164a0
   PIZZI M, 1990, Molecular Neuropharmacology, V1, P37
   PORTER ID, 1992, J ENDOCRINOL, V133, P275, DOI 10.1677/joe.0.1330275
   PORTER TE, 1994, ENDOCRINOLOGY, V134, P164, DOI 10.1210/en.134.1.164
   POTENZA MN, 1994, J NEUROSCI, V14, P1463, DOI 10.1523/JNEUROSCI.14-03-01463.1994
   PROBST WC, 1992, DNA CELL BIOL, V11, P1, DOI 10.1089/dna.1992.11.1
   PUPILLI C, 1994, J CLIN ENDOCR METAB, V79, P56, DOI 10.1210/jc.79.1.56
   RAGSDALE NV, 1990, HYPERTENSION, V15, P914, DOI 10.1161/01.HYP.15.6.914
   RAJFER SI, 1990, CIRCULATION, V82, P97
   RAMSEY NF, 1992, PHARMACOL TOXICOL, V71, P81, DOI 10.1111/j.1600-0773.1992.tb00525.x
   RAPPAPORT MS, 1993, BRAIN RES, V616, P242, DOI 10.1016/0006-8993(93)90215-9
   Ravindranathan A., 1994, Psychiatric Genetics, V4, P77, DOI 10.1097/00041444-199422000-00002
   REYNOLDS GP, 1989, BRIT J PSYCHIAT, V155, P305, DOI 10.1192/bjp.155.3.305
   RICCI A, 1991, N-S ARCH PHARMACOL, V344, P259, DOI 10.1007/BF00167228
   RICCI A, 1991, J AUTON PHARMACOL, V11, P121, DOI 10.1111/j.1474-8673.1991.tb00251.x
   RIVET JM, 1994, EUR J PHARMACOL, V265, P175, DOI 10.1016/0014-2999(94)90429-4
   ROBERTSON GS, 1995, NEUROSCIENCE, V64, P1019, DOI 10.1016/0306-4522(94)00426-6
   ROBERTSON GS, 1992, NEUROSCIENCE, V46, P315, DOI 10.1016/0306-4522(92)90054-6
   ROBERTSON GS, 1992, NEUROSCIENCE, V49, P285, DOI 10.1016/0306-4522(92)90096-K
   ROBERTSON HA, 1992, TRENDS NEUROSCI, V15, P201, DOI 10.1016/0166-2236(92)90034-6
   ROBERTSON HA, 1992, BIOCHEM CELL BIOL, V70, P729, DOI 10.1139/o92-112
   ROBINSON SW, 1994, MOL PHARMACOL, V46, P352
   Robinson SW, 1996, J NEUROCHEM, V67, P212
   RODRIGUES PD, 1990, P NATL ACAD SCI USA, V87, P9693, DOI 10.1073/pnas.87.24.9693
   RUBINSTEIN JE, 1990, BIOCHEM PHARMACOL, V39, P1965, DOI 10.1016/0006-2952(90)90616-S
   RUMP LC, 1993, KIDNEY INT, V43, P197, DOI 10.1038/ki.1993.32
   Sacktor B, 1982, MEMBRANES TRANSPORT, P197
   SAITO I, 1986, J HYPERTENS, V4, P57, DOI 10.1097/00004872-198602000-00009
   SAITO I, 1994, CLIN EXP HYPERTENS, V16, P29, DOI 10.3109/10641969409068582
   SAKAMOTO T, 1994, CLIN EXP HYPERTENS, V16, P197, DOI 10.3109/10641969409067949
   SAMAMA P, 1993, J BIOL CHEM, V268, P4625
   SATOH T, 1993, J CLIN INVEST, V91, P409, DOI 10.1172/JCI116215
   SATOH T, 1992, J CLIN INVEST, V89, P1496, DOI 10.1172/JCI115740
   SATOH T, 1993, AM J PHYSIOL, V265, pF399, DOI 10.1152/ajprenal.1993.265.3.F399
   SAWAGUCHI T, 1991, SCIENCE, V251, P947, DOI 10.1126/science.1825731
   SAWAGUCHI T, 1994, J NEUROPHYSIOL, V71, P515, DOI 10.1152/jn.1994.71.2.515
   SCHINELLI S, 1994, J NEUROCHEM, V62, P944
   SCHOORS DF, 1991, AM J HYPERTENS, V4, P494, DOI 10.1093/ajh/4.6.494
   SCHULTZ W, 1993, J NEUROSCI, V13, P900
   SEABROOK GR, 1994, BRIT J PHARMACOL, V112, P728, DOI 10.1111/j.1476-5381.1994.tb13138.x
   SEABROOK GR, 1994, BRIT J PHARMACOL, V111, P1061, DOI 10.1111/j.1476-5381.1994.tb14852.x
   SEABROOK GR, 1994, BRIT J PHARMACOL, V111, P391, DOI 10.1111/j.1476-5381.1994.tb14746.x
   SEEMAN P, 1995, J NEUROCHEM, V64, P1413
   SEEMAN P, 1993, NATURE, V365, P441, DOI 10.1038/365441a0
   SEEMAN P, 1992, NEUROPSYCHOPHARMACOL, V7, P261
   SEEMAN P, 1994, TRENDS PHARMACOL SCI, V15, P264, DOI 10.1016/0165-6147(94)90323-9
   SEEMAN P, 1990, CLIN NEUROPHARMAC S2, V13, P124
   SELF DW, 1992, PHARMACOL TOXICOL, V70, P87, DOI 10.1111/j.1600-0773.1992.tb00435.x
   Self DW, 1996, SCIENCE, V271, P1586, DOI 10.1126/science.271.5255.1586
   SENOGLES SE, 1994, ENDOCRINOLOGY, V134, P783, DOI 10.1210/en.134.2.783
   SENOGLES SE, 1994, J BIOL CHEM, V269, P23120
   SHAHEDI M, 1995, PFLUG ARCH EUR J PHY, V429, P832, DOI 10.1007/BF00374808
   SHIKUMA R, 1986, LIFE SCI, V38, P915, DOI 10.1016/0024-3205(86)90259-6
   SHINAMOTO K, 1994, AM J MED SCI S1, V307, pS70
   SHULTZ PJ, 1987, AM J PHYSIOL, V253, pH358, DOI 10.1152/ajpheart.1987.253.2.H358
   Sidenberg D. G., 1994, Psychiatric Genetics, V4, P95, DOI 10.1097/00041444-199422000-00006
   SIDHU A, 1991, J NEUROCHEM, V57, P1445, DOI 10.1111/j.1471-4159.1991.tb08312.x
   SIDHU A, 1992, J CLIN INVEST, V89, P789, DOI 10.1172/JCI115657
   SIDHU A, 1990, AM J HYPERTENS, V3, pS37, DOI 10.1093/ajh/3.6.37S
   SIGMUNDSON HK, 1994, CAN J PSYCHIAT, V39, pS70
   SIMMONDS SH, 1985, NEUROSCI LETT, V60, P267, DOI 10.1016/0304-3940(85)90588-9
   SMILEY JF, 1994, P NATL ACAD SCI USA, V91, P5720, DOI 10.1073/pnas.91.12.5720
   SNYDER LA, 1991, BIOCHEM BIOPH RES CO, V180, P1031, DOI 10.1016/S0006-291X(05)81169-6
   SOARESDASILVA P, 1994, NEWS PHYSIOL SCI, V9, P128
   SOKOLOFF P, 1990, NATURE, V347, P146, DOI 10.1038/347146a0
   SOKOLOFF P, 1995, TRENDS PHARMACOL SCI, V16, P270, DOI 10.1016/S0165-6147(00)89044-6
   SOWERS JR, 1980, ENDOCRINOLOGY, V107, P937, DOI 10.1210/endo-107-4-937
   SOWERS JR, 1981, J CLIN ENDOCR METAB, V52, P1078, DOI 10.1210/jcem-52-6-1078
   Spano P F, 1978, Adv Biochem Psychopharmacol, V19, P155
   STACK J, 1991, J PHYSIOL-LONDON, V439, P37, DOI 10.1113/jphysiol.1991.sp018655
   STRADER CD, 1988, J BIOL CHEM, V263, P10267
   STRADER CD, 1989, J BIOL CHEM, V264, P13572
   STUDER L, 1995, EUR J NEUROSCI, V7, P223, DOI 10.1111/j.1460-9568.1995.tb01058.x
   SU Y, 1993, ARCH GEN PSYCHIAT, V50, P205
   SUGAMORI KS, 1994, P NATL ACAD SCI USA, V91, P10536, DOI 10.1073/pnas.91.22.10536
   SUNAHARA RK, 1991, NATURE, V350, P614, DOI 10.1038/350614a0
   SURMEIER DJ, 1995, NEURON, V14, P385, DOI 10.1016/0896-6273(95)90294-5
   SURMEIER DJ, 1992, P NATL ACAD SCI USA, V89, P10178, DOI 10.1073/pnas.89.21.10178
   SVENSSON K, 1994, EUR J PHARMACOL, V263, P235, DOI 10.1016/0014-2999(94)90718-8
   SWARZENSKI BC, 1994, P NATL ACAD SCI USA, V91, P649, DOI 10.1073/pnas.91.2.649
   TAKEMOTO F, 1992, PFLUG ARCH EUR J PHY, V421, P302, DOI 10.1007/BF00374216
   TAKEMOTO F, 1991, PFLUG ARCH EUR J PHY, V419, P243, DOI 10.1007/BF00371102
   TANG L, 1994, J PHARMACOL EXP THER, V268, P495
   TANG L, 1994, J PHARMACOL EXP THER, V270, P475
   TIBERI M, 1994, J BIOL CHEM, V269, P27925
   TIBERI M, 1991, P NATL ACAD SCI USA, V88, P7491, DOI 10.1073/pnas.88.17.7491
   TOMIC M, 1993, BIOCHEM BIOPH RES CO, V191, P1020, DOI 10.1006/bbrc.1993.1319
   TRUMPPKALLMEYER S, 1992, J MED CHEM, V35, P3448, DOI 10.1021/jm00097a002
   UNDIE AS, 1990, J PHARMACOL EXP THER, V253, P987
   UNDIE AS, 1994, J NEUROCHEM, V62, P2045
   VACHVANICHSANONG P, 1995, AM J PHYSIOL-RENAL, V268, pF1009, DOI 10.1152/ajprenal.1995.268.6.F1009
   VALENTIJN JA, 1993, ANN NY ACAD SCI, V680, P211, DOI 10.1111/j.1749-6632.1993.tb19686.x
   VALLAR L, 1990, J BIOL CHEM, V265, P10320
   VANMUISWINKEL FL, 1993, J NEUROCHEM, V60, P83
   VANTOL HHM, 1992, NATURE, V358, P149
   VANTOL HHM, 1991, NATURE, V350, P610, DOI 10.1038/350610a0
   VERNIER P, 1995, TRENDS PHARMACOL SCI, V16, P375, DOI 10.1016/S0165-6147(00)89078-1
   VIZI ES, 1993, J ENDOCRINOL, V139, P213, DOI 10.1677/joe.0.1390213
   VOSS JW, 1992, CELL, V70, P527, DOI 10.1016/0092-8674(92)90422-9
   Waddington J L, 1987, Rev Neurosci, V1, P157, DOI 10.1515/REVNEURO.1987.1.3-4.157
   Waddington J L, 1989, J Psychopharmacol, V3, P54, DOI 10.1177/026988118900300202
   WADDINGTON JL, 1989, PHARMACOL THERAPEUT, V43, P1, DOI 10.1016/0163-7258(89)90046-6
   WANG CD, 1991, MOL PHARMACOL, V40, P168
   Wang HY, 1995, MOL PHARMACOL, V48, P988
   WATERS N, 1994, J NEURAL TRANSM-GEN, V98, P39, DOI 10.1007/BF01277593
   WATERS N, 1993, J NEURAL TRANSM-GEN, V94, P11, DOI 10.1007/BF01244979
   WEBB RL, 1986, LIFE SCI, V38, P2319, DOI 10.1016/0024-3205(86)90639-9
   WEINER DM, 1991, P NATL ACAD SCI USA, V88, P1859, DOI 10.1073/pnas.88.5.1859
   WEINSHANK RL, 1991, J BIOL CHEM, V266, P22427
   WHITE NM, 1991, BEHAV NEURAL BIOL, V55, P255, DOI 10.1016/0163-1047(91)90609-T
   WHITE NM, 1993, BEHAV NEURAL BIOL, V59, P230, DOI 10.1016/0163-1047(93)90998-W
   WHITFIELD L, 1980, J CLIN ENDOCR METAB, V51, P724, DOI 10.1210/jcem-51-4-724
   WILLIAMS PJ, 1990, J NEUROSCI, V10, P757
   WILLIAMS PJ, 1989, NEUROSCIENCE, V31, P673, DOI 10.1016/0306-4522(89)90432-6
   WISE RA, 1989, ANNU REV PSYCHOL, V40, P191, DOI 10.1146/annurev.ps.40.020189.001203
   XU M, 1994, CELL, V79, P945, DOI 10.1016/0092-8674(94)90026-4
   XU M, 1994, CELL, V79, P729, DOI 10.1016/0092-8674(94)90557-6
   YAMAGUCHI I, 1993, AM J PHYSIOL, V264, pF280, DOI 10.1152/ajprenal.1993.264.2.F280
   Yoshimura M, 1987, Agents Actions Suppl, V22, P93
   YOSHIMURA M, 1987, CLIN EXP HYPERTENS A, V9, P1141, DOI 10.3109/10641968709160039
   YOSHIMURA M, 1990, J AUTONOMIC PHARM S, V10, pS62
   Yu PY, 1996, J BIOL CHEM, V271, P19503, DOI 10.1074/jbc.271.32.19503
   YUN CHC, 1995, AM J PHYSIOL-GASTR L, V269, pG1, DOI 10.1152/ajpgi.1995.269.1.G1
   ZHANG LJ, 1994, MOL PHARMACOL, V45, P878
   ZHOU QY, 1990, NATURE, V347, P76, DOI 10.1038/347076a0
   ZIMLICHMAN R, 1988, CLIN SCI, V75, P515, DOI 10.1042/cs0750515
NR 481
TC 2749
Z9 3275
U1 7
U2 405
PU AMER PHYSIOLOGICAL SOC
PI BETHESDA
PA 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA
SN 0031-9333
EI 1522-1210
J9 PHYSIOL REV
JI Physiol. Rev.
PD JAN
PY 1998
VL 78
IS 1
BP 189
EP 225
DI 10.1152/physrev.1998.78.1.189
PG 37
WC Physiology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Physiology
GA YT659
UT WOS:000071629200007
PM 9457173
DA 2025-04-10
ER

PT J
AU Liu, Y
   Semina, EV
AF Liu, Yi
   Semina, Elena V.
TI pitx2 Deficiency Results in Abnormal Ocular and Craniofacial
   Development in Zebrafish
SO PLOS ONE
LA English
DT Article
ID AXENFELD-RIEGER-SYNDROME; LEFT-RIGHT ASYMMETRY; FETAL VASCULATURE PFV;
   NEURAL CREST SURVIVAL; HOMEOBOX GENE PITX2; RETINAL VASCULATURE; HYALOID
   VASCULATURE; TOOTH MORPHOGENESIS; CELL-DEATH; EXPRESSION
AB Human PITX2 mutations are associated with Axenfeld-Rieger syndrome, an autosomal-dominant developmental disorder that involves ocular anterior segment defects, dental hypoplasia, craniofacial dysmorphism and umbilical abnormalities. Characterization of the PITX2 pathway and identification of the mechanisms underlying the anomalies associated with PITX2 deficiency is important for better understanding of normal development and disease; studies of pitx2 function in animal models can facilitate these analyses. A knockdown of pitx2 in zebrafish was generated using a morpholino that targeted all known alternative transcripts of the pitx2 gene; morphant embryos generated with the pitx2(ex4/5) splicing-blocking oligomer produced abnormal transcripts predicted to encode truncated pitx2 proteins lacking the third (recognition) helix of the DNA-binding homeodomain. The morphological phenotype of pitx2(ex4/5) morphants included small head and eyes, jaw abnormalities and pericardial edema; lethality was observed at similar to 6-8-dpf. Cartilage staining revealed a reduction in size and an abnormal shape/position of the elements of the mandibular and hyoid pharyngeal arches; the ceratobranchial arches were also decreased in size. Histological and marker analyses of the misshapen eyes of the pitx2(ex4/5) morphants identified anterior segment dysgenesis and disordered hyaloid vasculature. In summary, we demonstrate that pitx2 is essential for proper eye and craniofacial development in zebrafish and, therefore, that PITX2/pitx2 function is conserved in vertebrates.
C1 [Liu, Yi; Semina, Elena V.] Med Coll Wisconsin, Dept Pediat, Milwaukee, WI 53226 USA.
   [Liu, Yi; Semina, Elena V.] Med Coll Wisconsin, Childrens Res Inst, Milwaukee, WI 53226 USA.
   [Liu, Yi; Semina, Elena V.] Childrens Hosp Wisconsin, Milwaukee, WI 53201 USA.
   [Semina, Elena V.] Med Coll Wisconsin, Dept Cell Biol Neurobiol & Anat, Milwaukee, WI 53226 USA.
C3 Medical College of Wisconsin; Medical College of Wisconsin; Children's
   Hospital of Wisconsin; Medical College of Wisconsin
RP Liu, Y (corresponding author), Shandong Acad Med Sci, Shandong Med Biotechnol Ctr, Jinan, Peoples R China.
EM esemina@mcw.edu
FU National Institutes of Health [EY015518]; National Eye Institute
   [R01EY015518] Funding Source: NIH RePORTER
FX This work was supported by the National Institutes of Health award
   EY015518 (EVS). The funders had no role in study design, data collection
   and analysis, decision to publish, or preparation of the manuscript.
CR Alvarez Y, 2007, BMC DEV BIOL, V7, DOI 10.1186/1471-213X-7-114
   Arikawa A, 2010, EYE, V24, P391, DOI 10.1038/eye.2009.114
   Bamforth SD, 2004, NAT GENET, V36, P1189, DOI 10.1038/ng1446
   Barrallo-Gimeno A, 2004, DEVELOPMENT, V131, P1463, DOI 10.1242/dev.01033
   Bisgrove BW, 2000, DEVELOPMENT, V127, P3567
   Bredrup C, 2008, AM J OPHTHALMOL, V146, P602, DOI 10.1016/j.ajo.2008.05.039
   Campione M, 1999, DEVELOPMENT, V126, P1225
   Campione M, 2001, DEV BIOL, V231, P252, DOI 10.1006/dbio.2000.0133
   Chang B, 2001, BMC GENET, V2, DOI 10.1186/1471-2156-2-18
   Chen JY, 2001, BIOCHEM BIOPH RES CO, V285, P105, DOI 10.1006/bbrc.2001.5099
   Chen Y, 2008, DEVELOPMENT, V135, P2939, DOI 10.1242/dev.021097
   Christiaen L, 2005, DEV BIOL, V277, P557, DOI 10.1016/j.ydbio.2004.10.008
   Cox CJ, 2002, J BIOL CHEM, V277, P25001, DOI 10.1074/jbc.M201737200
   Dahlman JM, 2005, MOL VIS, V11, P88
   Dhingra S, 2006, BRIT J OPHTHALMOL, V90, P1324, DOI 10.1136/bjo.2005.088625
   Edwards MM, 2010, J BIOL CHEM, V285, P7697, DOI 10.1074/jbc.M109.069575
   Ekker SC, 2008, ZEBRAFISH, V5, P121, DOI 10.1089/zeb.2008.9988
   Espinoza HM, 2002, HUM MOL GENET, V11, P743, DOI 10.1093/hmg/11.7.743
   Essner JJ, 2000, DEVELOPMENT, V127, P1081
   Evans AL, 2005, HUM MOL GENET, V14, P3347, DOI 10.1093/hmg/ddi365
   Gage PJ, 2008, DEV BIOL, V317, P310, DOI 10.1016/j.ydbio.2008.02.030
   Gage PJ, 1999, DEVELOPMENT, V126, P4643
   Goldberg MF, 1997, AM J OPHTHALMOL, V124, P587, DOI 10.1016/S0002-9394(14)70899-2
   HADDAD R, 1978, SURV OPHTHALMOL, V23, P123, DOI 10.1016/0039-6257(78)90091-7
   Hjalt Tord A., 2005, Expert Reviews in Molecular Medicine, V7, P1, DOI 10.1017/S1462399405010082
   Ishimaru Y, 2008, DEVELOPMENT, V135, P677, DOI 10.1242/dev.012856
   Ito M, 1999, ANAT EMBRYOL, V200, P403, DOI 10.1007/s004290050289
   KIMMEL CB, 1995, DEV DYNAM, V203, P253, DOI 10.1002/aja.1002030302
   Kitamura K, 1999, DEVELOPMENT, V126, P5749
   Kleinjan DA, 2008, PLOS GENET, V4, DOI 10.1371/journal.pgen.0040029
   Kraus P, 2006, AM J MED GENET A, V140A, P1366, DOI 10.1002/ajmg.a.31252
   Lawson ND, 2002, DEV BIOL, V248, P307, DOI 10.1006/dbio.2002.0711
   Lieschke GJ, 2007, NAT REV GENET, V8, P353, DOI 10.1038/nrg2091
   Lin CR, 1999, NATURE, V401, P279, DOI 10.1038/45803
   Lister JA, 2006, DEV BIOL, V290, P92, DOI 10.1016/j.ydbio.2005.11.014
   Liu CQ, 2008, DEVELOPMENT, V135, P3567, DOI 10.1242/dev.028076
   Liu W, 2003, DEVELOPMENT, V130, P6375, DOI 10.1242/dev.00849
   Lobov IB, 2005, NATURE, V437, P417, DOI 10.1038/nature03928
   Lu MF, 1999, NATURE, V401, P276, DOI 10.1038/45797
   Martin DM, 2004, DEV BIOL, V267, P93, DOI 10.1016/j.ydbio.2003.10.035
   Nelms BL, 2010, TRANSCRIPTIONAL CONT, P227
   Piotrowski T, 1996, DEVELOPMENT, V123, P345
   Richter M, 1998, INVEST OPHTH VIS SCI, V39, P2450
   Robitaille JM, 2009, OPHTHALMIC GENET, V30, P23, DOI 10.1080/13816810802464312
   Robu ME, 2007, PLOS GENET, V3, P787, DOI 10.1371/journal.pgen.0030078
   Rutland CS, 2007, MOL VIS, V13, P47
   Ryan AK, 1998, NATURE, V394, P545, DOI 10.1038/29004
   Schweickert A, 2000, MECH DEVELOP, V90, P41, DOI 10.1016/S0925-4773(99)00227-0
   Semina EV, 2006, DEV BIOL, V299, P63, DOI 10.1016/j.ydbio.2006.07.005
   Semina EV, 1996, NAT GENET, V14, P392, DOI 10.1038/ng1296-392
   Shi XH, 2005, MECH DEVELOP, V122, P513, DOI 10.1016/j.mod.2004.11.012
   Silbert, 2000, Clin Eye Vis Care, V12, P131, DOI 10.1016/S0953-4431(00)00054-0
   Sperber SM, 2008, DEV BIOL, V314, P59, DOI 10.1016/j.ydbio.2007.11.005
   Toro R, 2004, J BIOL CHEM, V279, P52087, DOI 10.1074/jbc.M404802200
   Tümer Z, 2009, EUR J HUM GENET, V17, P1527, DOI 10.1038/ejhg.2009.93
   Volkmann BA, 2011, INVEST OPHTH VIS SCI, V52, P1450, DOI 10.1167/iovs.10-6060
   Yoshikawa S, 2007, DEV DYNAM, V236, P1929, DOI 10.1002/dvdy.21197
   Yu XY, 2001, DEVELOPMENT, V128, P1005
   Zhang JM, 2008, INVEST OPHTH VIS SCI, V49, P5561, DOI 10.1167/iovs.08-2226
   Zhao XPC, 2006, INVEST OPHTH VIS SCI, V47, P4341, DOI 10.1167/iovs.05-1611
   Zhu MD, 2000, EXP EYE RES, V70, P767, DOI 10.1006/exer.2000.0844
   Zilinski CA, 2005, GENESIS, V41, P33, DOI 10.1002/gene.20094
NR 62
TC 33
Z9 45
U1 0
U2 12
PU PUBLIC LIBRARY SCIENCE
PI SAN FRANCISCO
PA 185 BERRY ST, STE 1300, SAN FRANCISCO, CA 94107 USA
SN 1932-6203
J9 PLOS ONE
JI PLoS One
PD JAN 27
PY 2012
VL 7
IS 1
AR e30896
DI 10.1371/journal.pone.0030896
PG 9
WC Multidisciplinary Sciences
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Science & Technology - Other Topics
GA 911GB
UT WOS:000301704200043
PM 22303467
OA Green Published, gold, Green Submitted
DA 2025-04-10
ER

PT J
AU Sakurai, T
   Uruno, T
   Sugiura, Y
   Tatsuguchi, T
   Yamamura, K
   Ushijima, M
   Hattori, Y
   Kukimoto-Niino, M
   Mishima-Tsumagari, C
   Watanabe, M
   Suematsu, M
   Fukui, Y
AF Sakurai, Tetsuya
   Uruno, Takehito
   Sugiura, Yuki
   Tatsuguchi, Takaaki
   Yamamura, Kazuhiko
   Ushijima, Miho
   Hattori, Yuko
   Kukimoto-Niino, Mutsuko
   Mishima-Tsumagari, Chiemi
   Watanabe, Mayuki
   Suematsu, Makoto
   Fukui, Yoshinori
TI Cholesterol sulfate is a DOCK2 inhibitor that mediates tissue-specific
   immune evasion in the eye
SO SCIENCE SIGNALING
LA English
DT Article
ID HUMAN EPIDERMAL-KERATINOCYTES; HYDROXYSTEROID SULFOTRANSFERASE;
   LYMPHOCYTE MIGRATION; LIPID-METABOLISM; PROTEIN DOCK2; RAC ACTIVATOR;
   IN-VIVO; EXPRESSION; PRIVILEGE; CELLS
AB Although immune responses are essential to protect the body from infection, they can also harm tissues. Certain tissues and organs, including the eye, constitute specialized microenvironments that locally inhibit immune reactivity. Dedicator of cytokinesis protein 2 (DOCK2) is a Rac-specific guanine nucleotide exchange factor (GEF) that is predominantly found in hematopoietic cells. DOCK2 plays a key role in immune surveillance because it is essential for the activation and migration of leukocytes. DOCK2 mutations cause severe immunodeficiency in humans. We found that DOCK2-mediated Rac activation and leukocyte migration were effectively inhibited by cholesterol sulfate (CS), but not by cholesterol or other sulfated steroids. CS bound to the catalytic domain of DOCK2 and suppressed its GEF activity. Mass spectrometric quantification revealed that CS was most abundantly produced in the Harderian gland, which provides the lipids that form the oily layer of the tear film. Sulfation of cholesterol is mediated by the sulfotransferases SULT2B1b and, to a lesser extent, SULT2B1a, which are produced from the same gene through alternative splicing. By genetically inactivating Sult2b1, we showed that the lack of CS in mice augmented ultraviolet-and antigen-induced ocular surface inflammation, which was suppressed by administration of eye drops containing CS. Thus, CS is a naturally occurring DOCK2 inhibitor and contributes to the generation of the immunosuppressive microenvironment in the eye.
C1 [Sakurai, Tetsuya; Uruno, Takehito; Tatsuguchi, Takaaki; Yamamura, Kazuhiko; Ushijima, Miho; Watanabe, Mayuki; Fukui, Yoshinori] Kyushu Univ, Med Inst Bioregulat, Dept Immunobiol & Neurosci, Div Immunogenet, Fukuoka, Fukuoka 8128582, Japan.
   [Uruno, Takehito; Fukui, Yoshinori] Kyushu Univ, Res Ctr Adv Immunol, Fukuoka, Fukuoka 8128582, Japan.
   [Sugiura, Yuki; Hattori, Yuko; Suematsu, Makoto] Keio Univ, Sch Med, Dept Biochem, Tokyo 1608582, Japan.
   [Sugiura, Yuki] Japan Sci & Technol Agcy, Precursory Res Embryon Sci & Technol, Tokyo 1020075, Japan.
   [Kukimoto-Niino, Mutsuko; Mishima-Tsumagari, Chiemi] RIKEN, Ctr Life Sci Technol, Yokohama, Kanagawa 2300045, Japan.
   [Yamamura, Kazuhiko] Kyushu Univ, Grad Sch Med Sci, Dept Dermatol, Fukuoka, Fukuoka 8128582, Japan.
   [Ushijima, Miho] Kyushu Univ, Grad Sch Med Sci, Dept Urol, Fukuoka, Fukuoka 8128582, Japan.
   [Watanabe, Mayuki] Japan Agcy Med Res & Dev, Tokyo 1000004, Japan.
C3 Kyushu University; Kyushu University; Keio University; Japan Science &
   Technology Agency (JST); RIKEN; Kyushu University; Kyushu University
RP Fukui, Y (corresponding author), Kyushu Univ, Med Inst Bioregulat, Dept Immunobiol & Neurosci, Div Immunogenet, Fukuoka, Fukuoka 8128582, Japan.; Fukui, Y (corresponding author), Kyushu Univ, Res Ctr Adv Immunol, Fukuoka, Fukuoka 8128582, Japan.
EM fukui@bioreg.kyushu-u.ac.jp
RI Watanabe, Mitsuru/AAN-6269-2020; Suematsu, Makoto/O-5762-2018; Uruno,
   Takehito/AAF-7998-2019; Suematsu, Makoto/I-8135-2013; Kukimoto-Niino,
   Mutsuko/C-6704-2017
OI Fukui, Yoshinori/0000-0003-2335-8745; Suematsu,
   Makoto/0000-0002-7165-6336; Uruno, Takehito/0000-0002-2812-9645;
   Kukimoto-Niino, Mutsuko/0000-0002-4178-1611; Sugiura,
   Yuki/0000-0002-6983-8958
FU Japan Agency for Medical Research and Development (AMED)
   [JP18gm0010001]; Ministry of Education, Culture, Sports, Science and
   Technology of Japan; Japan Society for the Promotion of Science; Japan
   Science and Technology Agency
FX This research was supported by the Leading Advanced Projects for Medical
   Innovation from Japan Agency for Medical Research and Development (AMED)
   to Y. F. (JP18gm0010001); Grants-in-Aid for Scientific Research from the
   Ministry of Education, Culture, Sports, Science and Technology (to Y.
   F.) of Japan; and the Japan Society for the Promotion of Science (to Y.
   F.). Mass spectrometry infrastructure in this study was partly supported
   by ERATO Suematsu Gas Biology (to M. S.) from Japan Science and
   Technology Agency.
CR Aleksandrov DA, 2006, FEBS J, V273, P548, DOI 10.1111/J.1742-4658.2005.05087.X
   Bronte V, 2005, NAT REV IMMUNOL, V5, P641, DOI 10.1038/nri1668
   Bunting M, 1999, GENE DEV, V13, P1524, DOI 10.1101/gad.13.12.1524
   Cornett DS, 2008, ANAL CHEM, V80, P5648, DOI 10.1021/ac800617s
   Côté JF, 2002, J CELL SCI, V115, P4901, DOI 10.1242/jcs.00219
   Dobbs K, 2015, NEW ENGL J MED, V372, P2409, DOI 10.1056/NEJMoa1413462
   Dong B, 2009, P NATL ACAD SCI USA, V106, P18831, DOI 10.1073/pnas.0909731106
   Falany CN, 2006, J STEROID BIOCHEM, V102, P214, DOI 10.1016/j.jsbmb.2006.09.011
   Falany CN, 2013, DRUG METAB REV, V45, P388, DOI 10.3109/03602532.2013.835609
   Ferguson TA, 2006, IMMUNOL REV, V213, P228, DOI 10.1111/j.1600-065X.2006.00430.x
   Forrester JV, 2008, MUCOSAL IMMUNOL, V1, P372, DOI 10.1038/mi.2008.27
   Fuda H, 2002, J BIOL CHEM, V277, P36161, DOI 10.1074/jbc.M207165200
   Fuda H, 2007, J LIPID RES, V48, P1343, DOI 10.1194/jlr.M700018-JLR200
   Fukui Y, 2001, NATURE, V412, P826, DOI 10.1038/35090591
   Hanyu O, 2012, BIOCHEM BIOPH RES CO, V428, P99, DOI 10.1016/j.bbrc.2012.10.013
   Higashi Y, 2004, J INVEST DERMATOL, V122, P1207, DOI 10.1111/j.0022-202X.2004.22416.x
   Javitt NB, 2001, ENDOCRINOLOGY, V142, P2978, DOI 10.1210/en.142.7.2978
   JETTEN AM, 1989, J INVEST DERMATOL, V92, P203, DOI 10.1111/1523-1747.ep12276731
   Jiang HS, 2005, J EXP MED, V202, P1121, DOI 10.1084/jem.20050911
   Joyce JA, 2015, SCIENCE, V348, P74, DOI 10.1126/science.aaa6204
   Kitaichi N, 2008, EXP EYE RES, V86, P929, DOI 10.1016/j.exer.2008.03.009
   Kolaczkowska E, 2013, NAT REV IMMUNOL, V13, P159, DOI 10.1038/nri3399
   Kulkarni K, 2011, J BIOL CHEM, V286, P25341, DOI 10.1074/jbc.M111.236455
   Kunisaki Y, 2006, J CELL BIOL, V174, P647, DOI 10.1083/jcb.200602142
   Lam SM, 2014, J LIPID RES, V55, P289, DOI 10.1194/jlr.M044826
   LANGLAIS J, 1981, P NATL ACAD SCI-BIOL, V78, P7266, DOI 10.1073/pnas.78.12.7266
   Li DQ, 2011, J ALLERGY CLIN IMMUN, V128, P1318, DOI 10.1016/j.jaci.2011.06.041
   Li XB, 2007, J LIPID RES, V48, P2587, DOI 10.1194/jlr.M700301-JLR200
   Lund EG, 1998, J BIOL CHEM, V273, P34316, DOI 10.1074/jbc.273.51.34316
   Mellor AL, 2004, NAT REV IMMUNOL, V4, P762, DOI 10.1038/nri1457
   Mellor AL, 2008, NAT REV IMMUNOL, V8, P74, DOI 10.1038/nri2233
   Meloche CA, 2001, J STEROID BIOCHEM, V77, P261, DOI 10.1016/S0960-0760(01)00064-4
   Merten M, 2001, CIRCULATION, V103, P2032
   Mueller JW, 2015, ENDOCR REV, V36, P526, DOI 10.1210/er.2015-1036
   Münz C, 2009, NAT REV IMMUNOL, V9, P246, DOI 10.1038/nri2527
   Niederkorn JY, 2006, NAT IMMUNOL, V7, P354, DOI 10.1038/ni1328
   Nishikimi A, 2012, CHEM BIOL, V19, P488, DOI 10.1016/j.chembiol.2012.03.008
   Okazaki T, 2006, TRENDS IMMUNOL, V27, P195, DOI 10.1016/j.it.2006.02.001
   PAYNE AP, 1994, J ANAT, V185, P1
   Reif K, 2002, TRENDS CELL BIOL, V12, P368, DOI 10.1016/S0962-8924(02)02330-9
   RILEY MV, 1990, CURR EYE RES, V9, P677, DOI 10.3109/02713689008999583
   Sakai Y, 2013, BLOOD, V122, P386, DOI 10.1182/blood-2012-12-475897
   Sanui T, 2003, IMMUNITY, V19, P119, DOI 10.1016/S1074-7613(03)00169-9
   Shao YC, 2017, MOL VIS, V23, P219
   Shimada M, 2008, XENOBIOTICA, V38, P1487, DOI 10.1080/00498250802488593
   SHIMADA T, 1985, THROMB RES, V38, P21, DOI 10.1016/0049-3848(85)90004-0
   Shimizu C, 2003, ENDOCRINOLOGY, V144, P1186, DOI 10.1210/en.2002-221011
   Strott CA, 2003, J LIPID RES, V44, P1268, DOI 10.1194/jlr.R300005-JLR200
   Sugiura Y, 2016, SCI REP-UK, V6, DOI 10.1038/srep32361
   Tajiri H, 2017, CELL REP, V19, P969, DOI 10.1016/j.celrep.2017.04.016
   Wang F, 2016, NAT IMMUNOL, V17, P844, DOI 10.1038/ni.3462
   Watanabe M, 2014, J IMMUNOL, V193, P5660, DOI 10.4049/jimmunol.1400885
   Xu LY, 2010, LIPIDS, V45, P821, DOI 10.1007/s11745-010-3451-y
   Yamamoto T, 2014, NAT COMMUN, V5, DOI 10.1038/ncomms4480
   Yamamura K, 2017, NAT COMMUN, V8, DOI 10.1038/ncomms13946
NR 55
TC 31
Z9 31
U1 0
U2 16
PU AMER ASSOC ADVANCEMENT SCIENCE
PI WASHINGTON
PA 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA
SN 1945-0877
EI 1937-9145
J9 SCI SIGNAL
JI Sci. Signal.
PD JUL 31
PY 2018
VL 11
IS 541
AR eaao4874
DI 10.1126/scisignal.aao4874
PG 11
WC Biochemistry & Molecular Biology; Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Biochemistry & Molecular Biology; Cell Biology
GA GO8QH
UT WOS:000440357000003
PM 30065028
DA 2025-04-10
ER

PT J
AU Motsch, I
   Kaluarachchi, M
   Emerson, LJ
   Brown, CA
   Brown, SC
   Dabauvalle, MC
   Ellis, JA
AF Motsch, I
   Kaluarachchi, M
   Emerson, LJ
   Brown, CA
   Brown, SC
   Dabauvalle, MC
   Ellis, JA
TI Lamins A and C are differentially dysfunctional in autosomal dominant
   Emery-Dreifuss muscular dystrophy
SO EUROPEAN JOURNAL OF CELL BIOLOGY
LA English
DT Article
DE nuclear lamins; emerin; EDMD
ID HUTCHINSON-GILFORD PROGERIA; FAMILIAL PARTIAL LIPODYSTROPHY;
   NUCLEAR-ENVELOPE; CELL-CYCLE; A/C GENE; MANDIBULOACRAL DYSPLASIA;
   DILATED CARDIOMYOPATHY; LMNA MUTATIONS; ROD DOMAIN; PROTEINS
AB Mutations in the LMNA gene, which encodes nuclear lamins A and C by alternative splicing, can give rise to Emery-Dreifuss muscular dystrophy. The mechanism by which lamins A and C separately contribute to this molecular phenotype is unknown. To address this question we examined ten LMNA mutations exogenously expressed as lamins A and C in COS-7 cells. Eight of the mutations when expressed in lamin A, exhibited a range of nuclear mislocalisation patterns. However, two mutations (T150P and delQ355) almost completely relocated exogenous lamin A from the nuclear envelope to the cytoplasm, disrupted nuclear envelope reassembly following cell division and altered the protein composition of the mid-body. In contrast, exogenously expressed DsRed2-tagged mutant lamin C constructs were only inserted into the nuclear lamina if co-expressed with any EGFP-tagged lamin A construct, except with one carrying the T150P mutation. The T150P, R527P and L530P mutations reduced the ability of lamin A, but not lamin C from binding to emerin. These data identify specific functional roles for the emerin-lamin C- and emerin-lamin A-containing protein complexes and is the first report to suggest that the A-type lamin mutations may be differentially dysfunctional for the same LMNA mutation. (c) 2005 Elsevier GmbH. All rights reserved.
C1 Kings Coll London, Randall Div Cell & Mol Biophys, London SE1 1UL, England.
   Univ London Imperial Coll Sci Technol & Med, Dept Paediat, Dubowitz Neuromuscular Unit, London, England.
   Univ Wurzburg, Dept Cell & Dev Biol, Wurzburg, Germany.
C3 University of London; King's College London; Imperial College London;
   University of Wurzburg
RP Kings Coll London, Randall Div Cell & Mol Biophys, New Hunts House,Guys Campus, London SE1 1UL, England.
EM juliet.ellis@kcl.ac.uk
OI Brown, Sue/0000-0001-8112-933X
CR Barbie DA, 2004, MOL CELL BIOL, V24, P595, DOI 10.1128/MCB.24.2.595-607.2004
   Bechert K, 2003, EXP CELL RES, V286, P75, DOI 10.1016/S0014-4827(03)00104-6
   BENAVENTE R, 1986, J CELL BIOL, V103, P1847, DOI 10.1083/jcb.103.5.1847
   BIONE S, 1994, NAT GENET, V8, P323, DOI 10.1038/ng1294-323
   Bonne G, 1999, NAT GENET, V21, P285, DOI 10.1038/6799
   Cao HN, 2003, J HUM GENET, V48, P271, DOI 10.1007/s10038-003-0025-3
   Capanni C, 2003, EXP CELL RES, V291, P122, DOI 10.1016/S0014-4827(03)00395-1
   Chen LS, 2003, LANCET, V362, P440, DOI 10.1016/S0140-6736(03)14069-X
   Clements L, 2000, BIOCHEM BIOPH RES CO, V267, P709, DOI 10.1006/bbrc.1999.2023
   Cohen M, 2001, TRENDS BIOCHEM SCI, V26, P41, DOI 10.1016/S0968-0004(00)01727-8
   DABAUVALLE MC, 1982, P NATL ACAD SCI-BIOL, V79, P5302, DOI 10.1073/pnas.79.17.5302
   Dabauvalle MC, 1999, EUR J CELL BIOL, V78, P749, DOI 10.1016/S0171-9335(99)80043-0
   De Sandre-Giovannoli A, 2003, SCIENCE, V300, P2055, DOI 10.1126/science.1084125
   Ellis JA, 1998, J CELL SCI, V111, P781
   EMERY AEH, 1989, J MED GENET, V26, P637, DOI 10.1136/jmg.26.10.637
   Eriksson M, 2003, NATURE, V423, P293, DOI 10.1038/nature01629
   Fairley EAL, 2002, J CELL SCI, V115, P341
   Fairley EAL, 1999, J CELL SCI, V112, P2571
   Fatkin D, 1999, NEW ENGL J MED, V341, P1715, DOI 10.1056/NEJM199912023412302
   Felice KJ, 2000, NEUROLOGY, V55, P275, DOI 10.1212/WNL.55.2.275
   Goldman RD, 2002, GENE DEV, V16, P533, DOI 10.1101/gad.960502
   HAAS M, 1993, EUR J CELL BIOL, V62, P237
   HOGER TH, 1991, EUR J CELL BIOL, V54, P150
   Holt I, 2003, J CELL SCI, V116, P3027, DOI 10.1242/jcs.00599
   HORTON H, 1992, EUR J CELL BIOL, V57, P172
   Hutchison CJ, 2001, J CELL SCI, V114, P9
   Krimm I, 2002, STRUCTURE, V10, P811, DOI 10.1016/S0969-2126(02)00777-3
   LEUKEL M, 1995, EUR J CELL BIOL, V68, P133
   Manilal S, 1999, HUM MOL GENET, V8, P353, DOI 10.1093/hmg/8.2.353
   Markiewicz E, 2002, J STRUCT BIOL, V140, P241, DOI 10.1016/S1047-8477(02)00573-7
   Mounkes L, 2003, CURR OPIN GENET DEV, V13, P223, DOI 10.1016/S0959-437X(03)00058-3
   Mounkes LC, 2003, NATURE, V423, P298, DOI 10.1038/nature01631
   Novelli G, 2002, AM J HUM GENET, V71, P426, DOI 10.1086/341908
   Östlund C, 2001, J CELL SCI, V114, P4435
   Pugh GE, 1997, J CELL SCI, V110, P2483
   Raharjo WH, 2001, J CELL SCI, V114, P4447
   Reichart B, 2004, BMC CELL BIOL, V5, DOI 10.1186/1471-2121-5-12
   Sabatelli P, 2001, MUSCLE NERVE, V24, P826, DOI 10.1002/mus.1076
   Sakaki M, 2001, J BIOCHEM-TOKYO, V129, P321, DOI 10.1093/oxfordjournals.jbchem.a002860
   Sewry CA, 2001, NEUROPATH APPL NEURO, V27, P281, DOI 10.1046/j.0305-1846.2001.00323.x
   Simha V, 2003, J CLIN ENDOCR METAB, V88, P2821, DOI 10.1210/jc.2002-021575
   Skop AR, 2004, SCIENCE, V305, P61, DOI 10.1126/science.1097931
   Talim B, 2003, NEUROMUSCULAR DISORD, V13, P660
   Vaughan OA, 2001, J CELL SCI, V114, P2577
   Vigouroux C, 2001, J CELL SCI, V114, P4459
   Zastrow MS, 2004, J CELL SCI, V117, P979, DOI 10.1242/jcs.01102
NR 46
TC 18
Z9 22
U1 1
U2 1
PU ELSEVIER GMBH
PI MUNICH
PA HACKERBRUCKE 6, 80335 MUNICH, GERMANY
SN 0171-9335
EI 1618-1298
J9 EUR J CELL BIOL
JI Eur. J. Cell Biol.
PD SEP
PY 2005
VL 84
IS 9
BP 765
EP 781
DI 10.1016/j.ejcb.2005.04.004
PG 17
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA 971RD
UT WOS:000232400800003
PM 16218190
DA 2025-04-10
ER

PT J
AU Jin, YT
   Peng, Y
   Lin, ZQ
   Chen, YC
   Wei, LM
   Hacker, TA
   Larsson, L
   Ge, Y
AF Jin, Yutong
   Peng, Ying
   Lin, Ziqing
   Chen, Yi-Chen
   Wei, Liming
   Hacker, Timothy A.
   Larsson, Lars
   Ge, Ying
TI Comprehensive analysis of tropomyosin isoforms in skeletal muscles by
   top-down proteomics
SO JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
LA English
DT Article
DE Tropomyosin; Skeletal muscle; Isoform; Post-translational modification;
   Top-down mass spectrometry
ID RESOLUTION MASS-SPECTROMETRY; CARDIAC TROPONIN-I; ALPHA-TROPOMYOSIN;
   PROTEIN-PHOSPHORYLATION; LIQUID-CHROMATOGRAPHY; ACTIN CYTOSKELETON;
   MYOPATHY MUTATIONS; MEMBRANE-PROTEIN; FIBER TYPES; RAT HEARTS
AB Mammalian skeletal muscles are heterogeneous in nature and are capable of performing various functions. Tropomyosin (Tpm) is a major component of the thin filament in skeletal muscles and plays an important role in controlling muscle contraction and relaxation. Tpm is known to consist of multiple isoforms resulting from different encoding genes and alternative splicing, along with post-translational modifications. However, a systematic characterization of Tpm isoforms in skeletal muscles is still lacking. Therefore, we employed top-down mass spectrometry (MS) to identify and characterize Tpm isoforms present in different skeletal muscles from multiple species, including swine, rat, and human. Our study revealed that Tpm1.1 and Tpm2.2 are the two major Tpm isoforms in swine and rat skeletal muscles, whereas Tpm1.1, Tpm2.2, and Tpm3.12 are present in human skeletal muscles. Tandem MS was utilized to identify the sequences of the major Tpm isoforms. Furthermore, quantitative analysis revealed muscle-type specific differences in the abundance of un-modified and modified Tpm isoforms in rat and human skeletal muscles. This study represents the first systematic investigation of Tpm isoforms in skeletal muscles, which not only demonstrates the capabilities of top-down MS for the comprehensive characterization of skeletal myofilament proteins but also provides the basis for further studies on these Tpm isoforms in muscle-related diseases.
C1 [Jin, Yutong; Chen, Yi-Chen; Ge, Ying] Univ Wisconsin, Dept Chem, 1101 Univ Ave, Madison, WI 53706 USA.
   [Peng, Ying; Lin, Ziqing; Wei, Liming; Ge, Ying] Univ Wisconsin, Dept Cell & Regenerat Biol, 1111 Highland Ave, Madison, WI 53705 USA.
   [Peng, Ying; Lin, Ziqing; Ge, Ying] Univ Wisconsin, Human Prote Program, 1111 Highland Ave, Madison, WI 53705 USA.
   [Wei, Liming] Fudan Univ, Inst Biomed Sci, Shanghai 200032, Peoples R China.
   [Hacker, Timothy A.] Univ Wisconsin, Dept Med, Sch Med & Publ Hlth, 1111 Highland Ave, Madison, WI 53705 USA.
   [Larsson, Lars] Karolinska Inst, Dept Physiol & Pharmacol, Dept Clin Neurosci, Clin Neurophysiol Sect, S-17177 Stockholm, Sweden.
C3 University of Wisconsin System; University of Wisconsin Madison;
   University of Wisconsin System; University of Wisconsin Madison;
   University of Wisconsin System; University of Wisconsin Madison; Fudan
   University; University of Wisconsin System; University of Wisconsin
   Madison; Karolinska Institutet
RP Ge, Y (corresponding author), Univ Wisconsin, Dept Chem, 1101 Univ Ave, Madison, WI 53706 USA.; Ge, Y (corresponding author), Univ Wisconsin, Dept Cell & Regenerat Biol, 1111 Highland Ave, Madison, WI 53705 USA.; Ge, Y (corresponding author), Univ Wisconsin, Human Prote Program, 1111 Highland Ave, Madison, WI 53705 USA.
EM ying.ge@wisc.edu
RI Larsson, Lars/AAY-1347-2021
OI Larsson, Lars/0000-0003-3722-035X; Jin, Yutong/0000-0002-0504-8279
FU NIH [R01HL096971, R01HL109810]; Swedish Foundation for International
   Cooperation in Research and Higher Education (STINT); Swedish Research
   Council [8651]
FX We would like to thank Huseyin Guner for the help of data analysis. We
   also thank Wenxuan Cai, Deyang Yu and Zachery Gregorich for their help
   and suggestions during the manuscript preparation. Financial support was
   kindly provided by NIH R01HL096971 and R01HL109810 (to YG), the Swedish
   Foundation for International Cooperation in Research and Higher
   Education (STINT) (to LL and YG), and the Swedish Research Council
   (8651) (to LL). We also would like to thank the Wisconsin Partnership
   Program for the establishment of UW Human Proteomics Program Mass
   Spectrometry Facility.
CR Arrell DK, 2001, CIRC RES, V89, P480, DOI 10.1161/hh1801.097240
   Ayaz-Guner S, 2009, BIOCHEMISTRY-US, V48, P8161, DOI 10.1021/bi900739f
   BAILEY K, 1948, BIOCHEM J, V43, P271, DOI 10.1042/bj0430271
   Bottinelli R, 2000, PROG BIOPHYS MOL BIO, V73, P195, DOI 10.1016/S0079-6107(00)00006-7
   Brown JH, 2001, P NATL ACAD SCI USA, V98, P8496, DOI 10.1073/pnas.131219198
   Canton M, 2004, AM J PHYSIOL-HEART C, V286, pH870, DOI 10.1152/ajpheart.00714.2003
   CARRARO U, 1981, FEBS LETT, V128, P233, DOI 10.1016/0014-5793(81)80088-9
   Chait BT, 2006, SCIENCE, V314, P65, DOI 10.1126/science.1133987
   Chen YC, 2015, ANAL CHEM, V87, P8399, DOI 10.1021/acs.analchem.5b01745
   Clarke NF, 2009, NEUROMUSCULAR DISORD, V19, P348, DOI 10.1016/j.nmd.2009.03.003
   CUMMINS P, 1974, BIOCHEM J, V141, P43, DOI 10.1042/bj1410043
   Denz CR, 2004, BIOCHEM BIOPH RES CO, V320, P1291, DOI 10.1016/j.bbrc.2004.06.084
   DHOOT GK, 1979, NATURE, V278, P714, DOI 10.1038/278714a0
   Dong XT, 2012, J BIOL CHEM, V287, P848, DOI 10.1074/jbc.M111.293258
   DRIESSEN HPC, 1985, CRIT REV BIOCHEM MOL, V18, P281, DOI 10.3109/10409238509086784
   El-Mezgueldi M, 2014, BIOPHYS J, V106, p350A, DOI 10.1016/j.bpj.2013.11.1991
   Eliuk S, 2015, ANNU REV ANAL CHEM, V8, P61, DOI 10.1146/annurev-anchem-071114-040325
   Ge Y, 2009, P NATL ACAD SCI USA, V106, P12658, DOI 10.1073/pnas.0813369106
   Geeves MA, 2015, J MUSCLE RES CELL M, V36, P147, DOI 10.1007/s10974-014-9389-6
   Greenfield NJ, 1998, BIOCHEMISTRY-US, V37, P7834, DOI 10.1021/bi973167m
   Guner H, 2014, J AM SOC MASS SPECTR, V25, P464, DOI 10.1007/s13361-013-0789-4
   Gunning P, 2008, PHYSIOL REV, V88, P1, DOI 10.1152/physrev.00001.2007
   Gunning PW, 2005, TRENDS CELL BIOL, V15, P333, DOI 10.1016/j.tcb.2005.04.007
   HEELEY DH, 1983, FEBS LETT, V152, P282, DOI 10.1016/0014-5793(83)80396-2
   Hendrickson CL, 2015, J AM SOC MASS SPECTR, V26, P1626, DOI 10.1007/s13361-015-1182-2
   HITCHCOCK SE, 1973, J MOL BIOL, V80, P825, DOI 10.1016/0022-2836(73)90212-X
   HITCHCOCKDEGREGORI SE, 1987, J BIOL CHEM, V262, P9730
   Holden DD, 2016, ANAL CHEM, V88, P1008, DOI 10.1021/acs.analchem.5b03911
   Horn DM, 2000, J AM SOC MASS SPECTR, V11, P320, DOI 10.1016/S1044-0305(99)00157-9
   Huang TY, 2010, PROTEOMICS, V10, P3577, DOI 10.1002/pmic.201000187
   Janco M, 2013, J MUSCLE RES CELL M, V34, P177, DOI 10.1007/s10974-013-9353-x
   JIN JP, 1988, J BIOL CHEM, V263, P7309
   JOHNSON MA, 1973, J NEUROL SCI, V18, P111, DOI 10.1016/0022-510X(73)90023-3
   Kee AJ, 2008, ADV EXP MED BIOL, V644, P143
   KLITGAARD H, 1990, ACTA PHYSIOL SCAND, V140, P41, DOI 10.1111/j.1748-1716.1990.tb08974.x
   Kostyukevich YI, 2012, J AM SOC MASS SPECTR, V23, P2198, DOI 10.1007/s13361-012-0480-1
   LEESMILLER JP, 1991, BIOESSAYS, V13, P429, DOI 10.1002/bies.950130902
   Marston SB, 2003, CIRC RES, V93, P1170, DOI 10.1161/01.RES.0000105088.06696.17
   Marston SB, 2013, J MUSCLE RES CELL M, V34, P189, DOI 10.1007/s10974-013-9347-8
   Memo M, 2013, J MUSCLE RES CELL M, V34, P165, DOI 10.1007/s10974-013-9344-y
   Neverova I, 2002, PROTEOMICS, V2, P22, DOI 10.1002/1615-9861(200201)2:1<22::AID-PROT22>3.0.CO;2-L
   Palmiter KA, 1996, J BIOL CHEM, V271, P11611, DOI 10.1074/jbc.271.20.11611
   Peng Y, 2014, MOL CELL PROTEOMICS, V13, P2752, DOI 10.1074/mcp.M114.040675
   Peng Y, 2013, J MUSCLE RES CELL M, V34, P199, DOI 10.1007/s10974-013-9352-y
   Peng Y, 2013, J PROTEOME RES, V12, P187, DOI 10.1021/pr301054n
   Peng Y, 2012, ANAL CHEM, V84, P3339, DOI 10.1021/ac300083y
   Perry SV, 2001, J MUSCLE RES CELL M, V22, P5, DOI 10.1023/A:1010303732441
   PITTENGER MF, 1994, CURR OPIN CELL BIOL, V6, P96, DOI 10.1016/0955-0674(94)90122-8
   Rajan S, 2010, CIRCULATION, V121, P410, DOI 10.1161/CIRCULATIONAHA.109.889725
   ROMEROHERRERA AE, 1982, MUSCLE NERVE, V5, P713, DOI 10.1002/mus.880050908
   Scellini B, 2015, J MUSCLE RES CELL M, V36, P11, DOI 10.1007/s10974-014-9394-9
   Schevzov G, 2005, J HISTOCHEM CYTOCHEM, V53, P557, DOI 10.1369/jhc.4A6505.2005
   Schiaffino S, 2011, PHYSIOL REV, V91, P1447, DOI 10.1152/physrev.00031.2010
   Scott W, 2001, PHYS THER, V81, P1810, DOI 10.1093/ptj/81.11.1810
   SENKO MW, 1994, ANAL CHEM, V66, P2801, DOI 10.1021/ac00090a003
   Smith LM, 2013, NAT METHODS, V10, P186, DOI 10.1038/nmeth.2369
   Tajsharghi H, 2012, NEUROMUSCULAR DISORD, V22, P923, DOI 10.1016/j.nmd.2012.05.018
   Thangaraj B, 2010, PROTEOMICS, V10, P3644, DOI 10.1002/pmic.201000190
   Wang J, 2008, CELL MOTIL CYTOSKEL, V65, P379, DOI 10.1002/cm.20267
   Whitelegge JP, 2002, MOL CELL PROTEOMICS, V1, P816, DOI 10.1074/mcp.M200045-MCP200
   WIECZOREK DF, 1988, MOL CELL BIOL, V8, P679, DOI 10.1128/MCB.8.2.679
   Xian F, 2012, ANAL CHEM, V84, P708, DOI 10.1021/ac203191t
   Zabrouskov V, 2008, MOL CELL PROTEOMICS, V7, P1838, DOI 10.1074/mcp.M700524-MCP200
   Zubarev RA, 2000, ANAL CHEM, V72, P563, DOI 10.1021/ac990811p
NR 64
TC 28
Z9 33
U1 0
U2 22
PU SPRINGER
PI DORDRECHT
PA VAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDS
SN 0142-4319
EI 1573-2657
J9 J MUSCLE RES CELL M
JI J. Muscle Res. Cell Motil.
PD APR
PY 2016
VL 37
IS 1-2
BP 41
EP 52
DI 10.1007/s10974-016-9443-7
PG 12
WC Cell Biology
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Cell Biology
GA DL0JV
UT WOS:000375319600005
PM 27090236
OA Green Accepted
DA 2025-04-10
ER

PT J
AU Shu, MG
   Guo, XT
   Zhen, HN
   Han, Y
   Chen, FL
   Li, LW
   Guo, SZ
AF Shu, Mao-Guo
   Guo, Xiao-Tong
   Zhen, Hai-Ning
   Han, Yan
   Chen, Fu-Lin
   Li, Li-Wen
   Guo, Shu-Zhong
TI Enhancing skin flap survival by a cell-permeable wild-type survivin
SO MEDICAL HYPOTHESES
LA English
DT Article
ID ENDOTHELIAL GROWTH-FACTOR; TUMOR ANGIOGENESIS; APOPTOSIS PROTEIN;
   GASTRIC-CANCER; GENE-THERAPY; EXPRESSION; PREFABRICATION; PROLIFERATION;
   SUPPRESSION; INHIBITION
AB Skin grafts, including skin flaps, are widely used in plastic and reconstructive surgery to cover wounds and tissue defects resulting from mechanic or burn injury. Ischemic necrosis is the main complication in skin graft surgery due to inefficient revascularization. Though the surgical delay procedure has been proved to be the only effective technique to prevent skin flap ischemic necrosis by mechanism of inducing adaption to hypoxia, but it is time consuming, costly, and having high risk of infection due to repeated surgery. Recent research demonstrated that, in addition to protecting cells against apoptosis, the expression of survivin correlates with intratumoral microvessel density in several different types of tumors and survivin could upregulate several proangiogenic factors, including VEGF, Egr-1 and Siah-1. Moreover, Survivin Delta Ex3, one of the survivin alternative splice variants, is necessary for activating the small GTPase Rac1 during endothelial tube formation and required for in vivo endothelial cell invasion. Therefore, we postulate that intracellular delivery of survivin or Survivin Delta Ex3 by fusion with protein transduction domain would enhance skin flap survival through accelerating revascularization by both inhibiting the apoptosis of microvascular endothelial cells and promoting skin flap angiogenesis. If the hypothesis was proved to be practical, the fusion proteins would be widely used in plastic and reconstructive surgry to prevent skin flap from ischemic necrosis in the future. (C) 2007 Elsevier Ltd. All rights reserved.
C1 Fourth Mil Med Univ, Xijing Hosp, Inst Plast Surg, Xian 710032, Peoples R China.
   Fourth Mil Med Univ, Xijing Hosp, Ctr Clin Oncol, Xian 710032, Peoples R China.
   Fourth Mil Med Univ, Xijing Hosp, Inst Neurosurg, Xian 710032, Peoples R China.
   NW Univ Xian, Coll Life Sci, Dept Biosci, Xian 710069, Peoples R China.
C3 Air Force Medical University; Air Force Medical University; Air Force
   Medical University; Northwest University Xi'an
RP Li, LW (corresponding author), Fourth Mil Med Univ, Xijing Hosp, Inst Plast Surg, No 17 Changle Western Rd, Xian 710032, Peoples R China.
EM liven@fmmu.edu.cn; shuz-hong@fmmu.edu.cn
RI 陈, 福林/IWU-3209-2023
CR Blanc-Brude OP, 2002, NAT MED, V8, P987, DOI 10.1038/nm750
   Caldas H, 2007, BLOOD, V109, P1479, DOI 10.1182/blood-2006-02-003749
   Capla JM, 2006, PLAST RECONSTR SURG, V117, P836, DOI 10.1097/01.prs.0000201459.91559.7f
   Coma S, 2004, OLIGONUCLEOTIDES, V14, P100, DOI 10.1089/1545457041526290
   Dohi T, 2006, EMBO REP, V7, P438, DOI 10.1038/sj.embor.7400640
   Du Pasquier D, 2006, DIFFERENTIATION, V74, P244, DOI 10.1111/j.1432-0436.2006.00073.x
   Fujihara Y, 2005, BRIT J PLAST SURG, V58, P511, DOI 10.1016/j.bjps.2004.12.028
   Goteri G, 2005, ANTICANCER RES, V25, P4313
   Gurunluoglu R, 2005, MICROSURG, V25, P433, DOI 10.1002/micr.20142
   Kawasaki H, 2001, CANCER, V91, P2026, DOI 10.1002/1097-0142(20010601)91:11<2026::AID-CNCR1228>3.0.CO;2-E
   Lee GH, 2006, EUR J GASTROEN HEPAT, V18, P957, DOI 10.1097/01.meg.0000230086.83792.56
   Li FZ, 2006, AM J PATHOL, V169, P1, DOI 10.2353/ajpath.2006.060121
   Li QX, 2006, CANCER BIOL THER, V5, P860, DOI 10.4161/cbt.5.7.2893
   Liu PY, 2005, J RECONSTR MICROSURG, V21, P273, DOI 10.1055/s-2005-871755
   Mäe M, 2006, CURR OPIN PHARMACOL, V6, P509, DOI 10.1016/j.coph.2006.04.004
   Richter GT, 2006, ARCH OTOLARYNGOL, V132, P637, DOI 10.1001/archotol.132.6.637
   Sah NK, 2006, CANCER LETT, V244, P164, DOI 10.1016/j.canlet.2006.03.007
   Tran J, 1999, BIOCHEM BIOPH RES CO, V264, P781, DOI 10.1006/bbrc.1999.1589
   Tu SP, 2005, GASTROENTEROLOGY, V128, P361, DOI 10.1053/j.gastro.2004.11.058
   Tu SP, 2003, CANCER RES, V63, P7724
   Wang GJ, 2005, ARTERIOSCL THROM VAS, V25, P2081, DOI 10.1161/01.ATV.0000183885.66153.8a
   Xiang R, 2005, CANCER RES, V65, P553
   You RI, 2006, CANCER RES, V66, P3051, DOI 10.1158/0008-5472.CAN-05-2479
   Zhang F, 2006, ANN PLAS SURG, V56, P670, DOI 10.1097/01.sap.0000203998.37851.57
   Zhen HN, 2005, CANCER-AM CANCER SOC, V104, P2775, DOI 10.1002/cncr.21490
NR 25
TC 4
Z9 5
U1 0
U2 2
PU CHURCHILL LIVINGSTONE
PI EDINBURGH
PA JOURNAL PRODUCTION DEPT, ROBERT STEVENSON HOUSE, 1-3 BAXTERS PLACE,
   LEITH WALK, EDINBURGH EH1 3AF, MIDLOTHIAN, SCOTLAND
SN 0306-9877
EI 1532-2777
J9 MED HYPOTHESES
JI Med. Hypotheses
PY 2007
VL 69
IS 4
BP 888
EP 891
DI 10.1016/j.mehy.2006.11.055
PG 4
WC Medicine, Research & Experimental
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Research & Experimental Medicine
GA 210TH
UT WOS:000249478000032
PM 17376603
DA 2025-04-10
ER

PT J
AU Lahat, N
   Bitterman, H
   Weiss-Cerem, L
   Rahat, MA
AF Lahat, Nitza
   Bitterman, Haim
   Weiss-Cerem, Lea
   Rahat, Michal A.
TI Hypoxia increases membranal and secreted HLA-DR in endothelial cells,
   rendering them T-cell activators
SO TRANSPLANT INTERNATIONAL
LA English
DT Article
DE endothelial cells; graft rejection; human inflammation; low oxygen
   tension
ID CLASS-II MOLECULES; COMPLEX CLASS-II; IN-VIVO; INJURY; EXPRESSION;
   MONOCYTES; ANTIGENS; TRANSPLANTATION; ALLOANTIBODY; TRAFFICKING
AB Transplantation involves preoperative ischemic periods that contribute to endothelial cell (EC) dysfunction and T-cell activation, leading to graft rejection. As hypoxia is a major constituent of ischemia, we evaluated its effect on the ability of ECs to express HLA-DR, which is required for presentation of antigens to T cells, and by itself serves as an important target for allogeneic T cells. Primary human umbilical vein ECs (HUVEC) and the human endothelial cell line EaHy926 were incubated in normoxia or hypoxia (PO2 < 0.3%). Hypoxia increased the membranal expression (by 4-6 fold, P < 0.01) and secretion (by sixfold, P < 0.05) of HLA-DR protein, without influencing the accumulation of its mRNA. Alternative splicing, attenuated trafficking, or shedding from the plasma membrane were not observed, but the lysosomal inhibitor bafilomycin A1 reduced HLA-DR secretion. Hypoxia-induced endothelial HLA-DR elevated and diminished the secretion of IL-2 and IL-10, respectively, from co-cultured allogeneic CD4(+) T cells in a HLA-DR-dependent manner, as demonstrated by the use of monoclonal anti-HLA-DR. Our results indicate a yet not fully understood post-translational mechanism(s), which elevate both membranal and soluble HLA-DR expression. This elevation is involved in allogeneic T-cell activation, highlighting the pivotal role of ECs in ischemia/hypoxia-associated injury and graft rejection.
C1 [Lahat, Nitza; Rahat, Michal A.] Technion Israel Inst Technol, Carmel Med Ctr, Res Immunol Unit, Ruth & Bruce Rappaport Fac Med, IL-34362 Haifa, Israel.
   [Bitterman, Haim; Weiss-Cerem, Lea] Technion Israel Inst Technol, Carmel Med Ctr, Ischemia Shock Res Lab, IL-34362 Haifa, Israel.
C3 Technion Israel Institute of Technology; Rappaport Faculty of Medicine;
   Clalit Health Services; Carmel Medical Center; Clalit Health Services;
   Carmel Medical Center; Technion Israel Institute of Technology
RP Rahat, MA (corresponding author), Technion Israel Inst Technol, Carmel Med Ctr, Res Immunol Unit, Ruth & Bruce Rappaport Fac Med, 7 Michal St, IL-34362 Haifa, Israel.
EM rahat_miki@clalit.org.il
RI Rahat, M.A./AAF-1184-2020
OI Rahat, Michal Amit/0000-0002-1881-1173
FU Rappaport Family Institute for Research in the Medical Sciences
FX This work was supported by a grant from the Rappaport Family Institute
   for Research in the Medical Sciences.
CR Al-Lamki RS, 2008, TRANSPLANTATION, V86, P1340, DOI 10.1097/TP.0b013e3181891d8b
   Alexander I, 2009, CELL TRANSPLANT, V18, P255, DOI 10.3727/096368909788534997
   Arita S, 2008, EUR J IMMUNOL, V38, P1423, DOI 10.1002/eji.200737694
   Ben-Yosef Y, 2002, CIRC RES, V90, P784, DOI 10.1161/01.RES.0000015588.70132.DC
   Ben-Yosef Y, 2005, AM J PHYSIOL-CELL PH, V289, pC1321, DOI 10.1152/ajpcell.00079.2005
   Berger AC, 2009, J CELL SCI, V122, P1, DOI 10.1242/jcs.035089
   Burster T, 2010, IMMUNOLOGY, V130, P436, DOI 10.1111/j.1365-2567.2010.03247.x
   Catlett IM, 2001, J IMMUNOL, V166, P6019, DOI 10.4049/jimmunol.166.10.6019
   Daniliuc S, 2003, J IMMUNOL, V171, P3225, DOI 10.4049/jimmunol.171.6.3225
   Doisne JM, 2008, MOL IMMUNOL, V45, P709, DOI 10.1016/j.molimm.2007.07.019
   Dore-Duffy P, 1999, MICROVASC RES, V57, P75, DOI 10.1006/mvre.1998.2112
   Feitoza CQ, 2010, INFLAMM RES, V59, P167, DOI 10.1007/s00011-009-0083-x
   Gong FY, 2010, BIOCHEM PHARMACOL, V80, P218, DOI 10.1016/j.bcp.2010.03.028
   Gougoura S, 2010, FREE RADICAL RES, V44, P803, DOI 10.3109/10715762.2010.485988
   Guo WY, 2003, EUR J IMMUNOL, V33, P928, DOI 10.1002/eji.200323351
   Halloran PF, 1997, TRANSPL P, V29, P79, DOI 10.1016/S0041-1345(96)00015-2
   Heiligenhaus A, 2004, TISSUE ANTIGENS, V63, P369, DOI 10.1111/j.0001-2815.2004.00201.x
   Kolluru GK, 2008, EUR J CELL BIOL, V87, P147, DOI 10.1016/j.ejcb.2007.10.001
   Lahat N, 2003, J LEUKOCYTE BIOL, V74, P197, DOI 10.1189/jlb.0303105
   Le Bas-Bernardet S, 2004, TRANSPLANTATION, V78, P1729, DOI 10.1097/01.TP.0000147339.31581.99
   Le Roux D, 2007, MOL BIOL CELL, V18, P3451, DOI 10.1091/mbc.E06-12-1114
   Lutz J, 2010, J INFLAMM-LOND, V7, DOI 10.1186/1476-9255-7-27
   MacKay PA, 2006, EUR J IMMUNOL, V36, P2875, DOI 10.1002/eji.200636041
   Marelli-Berg FM, 1999, J IMMUNOL, V162, P696
   Methe H, 2005, J HEART LUNG TRANSPL, V24, P833, DOI 10.1016/j.healun.2004.05.014
   Meziani F, 2008, PHARMACOL REP, V60, P75
   Nishimura M, 2007, VOX SANG, V93, P78, DOI 10.1111/j.1423-0410.2007.00925.x
   Nishimura M, 2007, TRANSFUSION MED, V17, P129, DOI 10.1111/j.1365-3148.2006.00721.x
   Pathak SS, 2000, TRAFFIC, V1, P561, DOI 10.1034/j.1600-0854.2000.010706.x
   Rahat MA, 2006, J LEUKOCYTE BIOL, V79, P706, DOI 10.1189/jlb.0605302
   Rao DA, 2007, J IMMUNOL, V179, P6536, DOI 10.4049/jimmunol.179.10.6536
   Rebmann V, 2003, TISSUE ANTIGENS, V62, P536, DOI 10.1046/j.1399-0039.2003.00138.x
   Reith W, 2001, ANNU REV IMMUNOL, V19, P331, DOI 10.1146/annurev.immunol.19.1.331
   ROSE ML, 1986, TRANSPLANTATION, V41, P776, DOI 10.1097/00007890-198606000-00021
   Salahudeen AK, 2004, AM J PHYSIOL-RENAL, V287, pF181, DOI 10.1152/ajprenal.00098.2004
   Savina A, 2005, TRAFFIC, V6, P131, DOI 10.1111/j.1600-0854.2004.00257.x
   Savina A, 2002, J CELL SCI, V115, P2505
   Shiao SL, 2007, J IMMUNOL, V179, P4397, DOI 10.4049/jimmunol.179.7.4397
   Tay SS, 2004, TRANSPLANTATION, V78, P987, DOI 10.1097/01.TP.0000137205.26405.40
   Tiegs G, 2010, J AUTOIMMUN, V34, P1, DOI 10.1016/j.jaut.2009.08.008
   Ting JPY, 2002, CELL, V109, pS21, DOI 10.1016/S0092-8674(02)00696-7
   Ting YT, 2010, TRANSPLANTATION, V89, P1071, DOI 10.1097/TP.0b013e3181d15492
   Valantine HA, 2003, TRANSPLANTATION, V76, P891, DOI 10.1097/01.TP.0000080981.90718.EB
   van Kilsdonk JWJ, 2010, EUR J CELL BIOL, V89, P415, DOI 10.1016/j.ejcb.2009.11.026
   Walker JD, 2009, J IMMUNOL, V182, P1548, DOI 10.4049/jimmunol.182.3.1548
   Ye LL, 2008, J IMMUNOL, V181, P2572, DOI 10.4049/jimmunol.181.4.2572
NR 46
TC 6
Z9 7
U1 0
U2 3
PU WILEY-BLACKWELL
PI HOBOKEN
PA 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
SN 0934-0874
EI 1432-2277
J9 TRANSPL INT
JI Transpl. Int.
PD OCT
PY 2011
VL 24
IS 10
BP 1018
EP 1026
DI 10.1111/j.1432-2277.2011.01304.x
PG 9
WC Surgery; Transplantation
WE Science Citation Index Expanded (SCI-EXPANDED)
SC Surgery; Transplantation
GA 819XP
UT WOS:000294868100011
PM 21806687
DA 2025-04-10
ER

EF