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Titolo:
Angiotensin II regulates phosphorylation of translation elongation factor-2 in cardiac myocytes
Autore:
Everett, AD; Stoops, TD; Nairn, AC; Brautigan, D;
Indirizzi:
Univ Virginia, Dept Pediat, Div Pediat Cardiol, Charlottesville, VA 22908 USA Univ Virginia Charlottesville VA USA 22908 Charlottesville, VA 22908 USA Univ Virginia, Ctr Cell Signaling, Charlottesville, VA 22908 USA Univ Virginia Charlottesville VA USA 22908 Charlottesville, VA 22908 USA Rockefeller Univ, Mol & Cellular Neurosci Lab, New York, NY 10021 USA Rockefeller Univ New York NY USA 10021 urosci Lab, New York, NY 10021 USA
Titolo Testata:
AMERICAN JOURNAL OF PHYSIOLOGY-HEART AND CIRCULATORY PHYSIOLOGY
fascicolo: 1, volume: 281, anno: 2001,
pagine: H161 - H167
SICI:
0363-6135(200107)281:1<H161:AIRPOT>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACTIVATED PROTEIN-KINASE; P70 S6 KINASE; GROWTH-FACTOR RECEPTOR; SMOOTH-MUSCLE CELLS; PHOSPHATIDYLINOSITOL 3-KINASE; VENTRICULAR MYOCYTES; OKADAIC ACID; HYPERTROPHY; PHOSPHATASES; RAPAMYCIN;
Keywords:
protein translation; mitogen-activated protein kinase; protein phosphatase 2A; phosphoinositide 3-kinase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Everett, AD Univ Virginia, Dept Pediat, Div Pediat Cardiol, MR4 Bldg,Rm 3033,POB 801356, Charlottesville, VA 22908 USA Univ Virginia MR4 Bldg,Rm 3033,POB 801356 Charlottesville VA USA 22908
Citazione:
A.D. Everett et al., "Angiotensin II regulates phosphorylation of translation elongation factor-2 in cardiac myocytes", AM J P-HEAR, 281(1), 2001, pp. H161-H167

Abstract

Increased protein synthesis is the cardinal feature of cardiac hypertrophy. We have studied angiotensin II (ANG II)-dependent regulation of eukaryotic elongation factor-2 (eEF-2), an essential component of protein translation required for polypeptide elongation, in rat neonatal cardiac myocytes. eEF2 is fully active in its dephosphorylated state and is inhibited followingphosphorylation by eEF2 kinase. ANG II treatment (10(-10)-10(-7) M) for 30min produced an AT(1) receptor-specific and concentration- and time-dependent reduction in the phosphorylation of eEF-2. Protein phosphatase 2A (PP2A) inhibitors okadaic acid and fostriecin, but not the PP2B inhibitor FK506,attenuated ANG II-dependent dephosphorylation of eEF-2. ANG II activated mitogen-activated protein kinase, (MAPK) within 10 min of treatment, and blockade of MAPK activation with PD-98059 (1-20 nM) inhibited eEF-2 dephosphorylation. The effect of ANG II on eEF- 2 dephosphorylation was also blocked by LY-29004 (1-20 nM), suggesting a role for phosphoinositide 3-kinase, butthe mammalian target rapamycin inhibitor rapamycin (10-100 nM) had no effect. Together these results suggest that the ANG II-dependent increase in protein synthesis includes activation of eEF- 2 via dephosphorylation by PP2Aby a process that involves both PI3K and MAPK.

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Documento generato il 02/04/20 alle ore 19:17:17