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Titolo:
HEPARAN-SULFATE PROTEOGLYCANS FUNCTION IN THE BINDING AND DEGRADATIONOF VITRONECTIN BY FIBROBLAST MONOLAYERS
Autore:
WILKINSPORT CE; MCKEOWNLONGO PJ;
Indirizzi:
ALBANY MED COLL UNION UNIV,ALBANY MED COLL,DEPT PHYSIOL & CELL BIOL,NEIL HELLMAN MED RES BLDG ALBANY NY 12208 ALBANY MED COLL UNION UNIV,ALBANY MED COLL,DEPT PHYSIOL & CELL BIOL ALBANY NY 12208
Titolo Testata:
Biochemistry and cell biology
fascicolo: 6, volume: 74, anno: 1996,
pagine: 887 - 897
SICI:
0829-8211(1996)74:6<887:HPFITB>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMINOGEN-ACTIVATOR INHIBITOR; RECEPTOR-MEDIATED ENDOCYTOSIS; CELL-SURFACE PROTEOGLYCANS; HUMAN-ENDOTHELIAL-CELLS; GLYCINE-ASPARTIC ACID; SOMATOMEDIN-B DOMAIN; HUMAN-MELANOMA; STRUCTURAL REQUIREMENTS; ADHESION RECEPTOR; INTEGRIN RECEPTOR;
Keywords:
ENDOCYTOSIS; VITRONECTIN; PROTEOGLYCAN; EXTRACELLULAR MATRIX;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
88
Recensione:
Indirizzi per estratti:
Citazione:
C.E. Wilkinsport e P.J. Mckeownlongo, "HEPARAN-SULFATE PROTEOGLYCANS FUNCTION IN THE BINDING AND DEGRADATIONOF VITRONECTIN BY FIBROBLAST MONOLAYERS", Biochemistry and cell biology, 74(6), 1996, pp. 887-897

Abstract

Vitronectin, a 75-kDa plasma protein is also found in the extracellular matrix, where it is believed to promote cell adhesion and migration. In addition to its role in adhesion, matrix vitronectin is also believed to function as an opsonin promoting the clearance of thrombin-serpin complexes from the matrix. Vitronectin is cleared from the matrix by receptor-mediated endocytosis followed by lysosomal degradation, suggesting that cells can regulate the levels of vitronectin present in the matrix. However, the mechanism by which plasma vitronectin associates with the extracellular matrix remains unclear. Studies were conducted to define the binding site(s) for vitronectin in fibroblast cell layers. Sodium chlorate, a competitive inhibitor of proteoglycan sulfation, produced a dose-dependent decrease in both binding and degradation of vitronectin. This inhibition was reversible in that removal of chlorate returned both binding and degradation of vitronectin to near control levels within 24 h. The binding of vitronectin to cell layers was not dependent on cells because vitronectin bound directly to isolated matrix. Isolated matrices prepared from cell layers treated with sodium chlorate also exhibited a dose-dependent decrease in vitronectin binding, consistent with the binding site for vitronectin in the matrixbeing sulfated proteoglycans. Binding and degradation of vitronectin were also sensitive to the addition of exogenous heparin, suggesting that the heparin binding domain of vitronectin was mediating binding tothe matrix. Incubating fibroblast monolayers with heparinase III resulted in a 40% decrease in binding and degradation of vitronectin. Taken together, the above findings suggest that vitronectin's binding to the matrix and its subsequent degradation are dependent on heparan sulfate proteoglycans.

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Documento generato il 24/11/20 alle ore 13:37:38