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Titolo:
c-Src and HSP72 interact in ATP-depleted renal epithelial cells
Autore:
Wang, YH; Li, F; Schwartz, JH; Flint, PJ; Borkan, SC;
Indirizzi:
Boston Univ, Boston Med Ctr, Dept Med, Renal Sect, Boston, MA 02118 USA Boston Univ Boston MA USA 02118 ept Med, Renal Sect, Boston, MA 02118 USA Tufts Univ New England Med Ctr, Boston, MA 02111 USA Tufts Univ New England Med Ctr Boston MA USA 02111 , Boston, MA 02111 USA Tufts Univ, Sch Med, Dept Pathol, Boston, MA 02111 USA Tufts Univ Boston MA USA 02111 Sch Med, Dept Pathol, Boston, MA 02111 USA
Titolo Testata:
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY
fascicolo: 5, volume: 281, anno: 2001,
pagine: C1667 - C1675
SICI:
0363-6143(200111)281:5<C1667:CAHIIA>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
FOCAL ADHESION KINASE; CADHERIN-CATENIN COMPLEX; YES TYROSINE KINASE; HEAT-STRESS; SIGNAL-TRANSDUCTION; CARDIAC MYOCYTES; TIGHT JUNCTIONS; FAMILY KINASES; TUBULAR CELLS; RHO-FAMILY;
Keywords:
ischemia; heat shock protein 70; cytoskeleton; Yes kinase; beta-catenin; paxillin; vinculin; Triton X-100;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
62
Recensione:
Indirizzi per estratti:
Indirizzo: Borkan, SC Evans Biomed Res Ctr, Renal Sect, Rm 547,650 Albany St, Boston,MA 02118 USA Evans Biomed Res Ctr Rm 547,650 Albany St Boston MA USA 02118A
Citazione:
Y.H. Wang et al., "c-Src and HSP72 interact in ATP-depleted renal epithelial cells", AM J P-CELL, 281(5), 2001, pp. C1667-C1675

Abstract

Disruption of cell contact sites during ischemia contributes to the loss of organ function in acute renal failure. Because prior heat stress protectscell contact sites in ATP-depleted renal epithelial cells in vitro, we hypothesized that heat shock protein 72 (HSP72), the major inducible cytoprotectant in mammalian cells, interacts with protein kinases that regulate cell-cell and cell-matrix interactions. ATP depletion increased the content of Tyr(416) Src, the activated form of this kinase. c-Src activation was associated with an increase in the tyrosine phosphorylation state of beta -catenin, paxillin, and vinculin, three c-Src substrate proteins that localize toand regulate cell contact sites. Prior heat stress inhibited c-Src activation and decreased the degree of tyrosine phosphorylation of all three Src substrates during ATP depletion and/or early recovery. HSP72 coimmunoprecipitated with c-Src only in cells subjected to heat stress. ATP depletion markedly increased the interaction between HSP72 and c-Src, supporting the hypothesis that HSP72 regulates Src kinase activity. These results suggest thatalterations in the tyrosine phosphorylation state of proteins located at the cell-cell and cell-matrix interface mediate, at least in part, the functional state of these structures during ATP depletion and may be modulated by interactions between HSP72 and c-Src.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 10:29:14