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Titolo:
ALPHA(V)BETA(5) INTEGRIN RECEPTOR-MEDIATED ENDOCYTOSIS OF VITRONECTINIS PROTEIN-KINASE C-DEPENDENT
Autore:
PANETTI TS; WILCOX SA; HORZEMPA C; MCKEOWNLONGO PJ;
Indirizzi:
ALBANY MED COLL,DEPT PHYSIOL & CELL BIOL,47 NEW SCOTLAND AVE ALBANY NY 12208 ALBANY MED COLL,DEPT PHYSIOL & CELL BIOL ALBANY NY 12208
Titolo Testata:
The Journal of biological chemistry
fascicolo: 31, volume: 270, anno: 1995,
pagine: 18593 - 18597
SICI:
0021-9258(1995)270:31<18593:AIREOV>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMINOGEN-ACTIVATOR INHIBITOR-1; THROMBIN-ANTITHROMBIN-III; ENDOTHELIAL-CELL MATRIX; BETA-SUBUNIT; MULTIMERIC VITRONECTIN; HT-1080 CELLS; ADHESION; BINDING; HEPARIN; COMPLEX;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
50
Recensione:
Indirizzi per estratti:
Citazione:
T.S. Panetti et al., "ALPHA(V)BETA(5) INTEGRIN RECEPTOR-MEDIATED ENDOCYTOSIS OF VITRONECTINIS PROTEIN-KINASE C-DEPENDENT", The Journal of biological chemistry, 270(31), 1995, pp. 18593-18597

Abstract

Previous studies have demonstrated that the alpha(v) beta(5) integrinreceptor functions in the endocytosis and degradation of matrix-boundvitronectin by human skin fibroblasts (Panetti, T. S., and McKeown-Longo, P. J. (1993) J. Biol, Chem. 268, 11988-11993; Panetti, T. S., andMcKeown-Longo, P. J. (1993) J. Biol. Chem. 268, 11492-11495). These earlier studies demonstrated that vitronectin degradation was inhibitedby either antibodies to the beta(5) integrin or exogenous heparin, suggesting that both integrin receptors and cell surface heparan sulfateproteoglycans are involved in the endocytosis and degradation of vitronectin, The present study was done to define intracellular signaling pathways involved in endocytosis of vitronectin and to evaluate the relative contribution of cell surface heparan sulfate pro teoglycans andthe alpha(v) beta(5) integrin in the activation of these signaling pathways, The addition of the phorbol ester phorbol 12-myristate 13-acetate (PMA), a protein kinase C activator, to monolayers of human skin fibroblasts, increased vitronectin degradation, Staurosporine and calphostin C, inhibitors of protein kinase C, blocked internalization and subsequent degradation of vitronectin, while KT5720, an inhibitor of protein kinase A, had no effect on the degradation of vitronectin. PMA was also able to reverse the inhibition of vitronectin degradation seenwhen cells were pretreated with heparinase or incubated with exogenous heparin. In contrast, the inhibitory effect of either RGD peptides or anti-alpha(v) beta(5) antibodies on vitronectin degradation were notovercome by the addition of PMA. These data suggest that the internalization of vitronectin from the matrix is mediated by the alpha(v) beta(5) integrin following activation of protein kinase C.

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Documento generato il 21/09/20 alle ore 18:01:24