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Titolo:
Regulation of SERCA Ca2+ pump expression by cytoplasmic [Ca2+] in vascularsmooth muscle cells
Autore:
Wu, KD; Bungard, D; Lytton, J;
Indirizzi:
Univ Calgary, Hlth Sci Ctr, Dept Biochem & Mol Biol, Calgary, AB T2N 4N1, Canada Univ Calgary Calgary AB Canada T2N 4N1 Biol, Calgary, AB T2N 4N1, Canada Natl Taiwan Univ Hosp, Dept Internal Med, Taipei 100, Taiwan Natl Taiwan Univ Hosp Taipei Taiwan 100 Internal Med, Taipei 100, Taiwan Brigham & Womens Hosp, Dept Med, Div Renal, Boston, MA 02115 USA Brigham &Womens Hosp Boston MA USA 02115 Div Renal, Boston, MA 02115 USA Harvard Univ, Sch Med, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 vard Univ, Sch Med, Boston, MA 02115 USA Univ Calgary, Dept Physiol & Biophys, Calgary, AB T2N 4N1, Canada Univ Calgary Calgary AB Canada T2N 4N1 ophys, Calgary, AB T2N 4N1, Canada
Titolo Testata:
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY
fascicolo: 4, volume: 280, anno: 2001,
pagine: C843 - C851
SICI:
0363-6143(200104)280:4<C843:ROSCPE>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENDOPLASMIC-RETICULUM; SARCOPLASMIC-RETICULUM; SIGNAL-TRANSDUCTION; SKELETAL-MUSCLE; DEPENDENT RELAXATION; CALCINEURIN CONTROLS; NA+/CA2+ EXCHANGER; MOLECULAR-CLONING; GENE-EXPRESSION; PROTEIN-KINASES;
Keywords:
thapsigargin; ionophore A-23187; mRNA; Northern blotting; kinase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Lytton, J Univ Calgary, Hlth Sci Ctr, Dept Biochem & Mol Biol, 3330 Hosp Dr NW, Calgary, AB T2N 4N1, Canada Univ Calgary 3330 Hosp Dr NW Calgary AB Canada T2N 4N1 1, Canada
Citazione:
K.D. Wu et al., "Regulation of SERCA Ca2+ pump expression by cytoplasmic [Ca2+] in vascularsmooth muscle cells", AM J P-CELL, 280(4), 2001, pp. C843-C851

Abstract

Vascular smooth muscle cells (VSMC) express three isoforms of the sarcoplasmic or endoplasmic reticulum Ca2+-ATPase (SERCA) pump; SERCA2b predominates (91%), whereas SERCA2a (6%) and SERCA3 (3%) are present in much smaller amounts. Treatment with thapsigargin (Tg) or A-23187 increased the level of mRNA encoding SERCA2b four- to fivefold; SERCA3 increased about 10-fold, whereas SERCA2a was unchanged. Ca2+ chelation prevented the Tg-induced SERCA2b increase, whereas Ca2+ elevation itself increased SERCA2b expression. These responses were discordant with those of 78-kDa glucose-regulated protein/immunoglobulin-binding protein (grp78/BiP), an endoplasmic reticulum stress-response protein. SERCA2b mRNA elevation was much larger than could be accounted for by the observed increase in message stability. The induction ofSERCA2b by Tg did not require protein synthesis, nor was it affected by inhibitors of calcineurin, protein kinase C, Ca2+/calmodulin-dependent protein kinase, or tyrosine protein kinases. Treatment with the nonselective protein kinase inhibitor H-7 prevented Tg-induced SERCA2b expression from occurring, whereas another nonselective inhibitor, staurosporine, was without effect. We conclude that changes in cytosolic Ca2+ control the expression of SERCA2b in VSMC via a mechanism involving a currently uncharacterized, H-7-sensitive but staurosporinein-sensitive, protein kinase.

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Documento generato il 05/04/20 alle ore 19:41:39