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Titolo:
THE UROKINASE RECEPTOR IS A MAJOR VITRONECTIN-BINDING PROTEIN ON ENDOTHELIAL-CELLS
Autore:
KANSE SM; KOST C; WILHELM OG; ANDREASEN PA; PREISSNER KT;
Indirizzi:
MPI,KERCKHOFF KLIN,HAEMOSTASIS RES UNIT,SPRUDELHOF 11 D-61231 BAD NAUHEIM GERMANY MPI,KERCKHOFF KLIN,HAEMOSTASIS RES UNIT D-61231 BAD NAUHEIM GERMANY TECH UNIV MUNICH,FRAUENKLIN W-8000 MUNICH GERMANY AARHUS UNIV,DEPT MOLEC BIOL DK-8000 AARHUS DENMARK
Titolo Testata:
Experimental cell research
fascicolo: 2, volume: 224, anno: 1996,
pagine: 344 - 353
SICI:
0014-4827(1996)224:2<344:TURIAM>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMINOGEN-ACTIVATOR INHIBITOR; THROMBIN-ANTITHROMBIN-III; EXTRACELLULAR-MATRIX; HUMAN-PLASMA; S-PROTEIN; MULTIMERIC VITRONECTIN; TYPE-1 INHIBITOR; HT-1080 CELLS; IDENTIFICATION; DIFFERENTIATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
51
Recensione:
Indirizzi per estratti:
Citazione:
S.M. Kanse et al., "THE UROKINASE RECEPTOR IS A MAJOR VITRONECTIN-BINDING PROTEIN ON ENDOTHELIAL-CELLS", Experimental cell research, 224(2), 1996, pp. 344-353

Abstract

We have previously demonstrated that vitronectin (VN), a morphoregulatory protein in the vessel wall, is internalized and translocated to the subendothelial matrix by an integrin-independent mechanism (J. Histochem. Cytochem. 41, 1823-1832, 1993). The cell surface component which mediates the initial contact of VN with endothelial cells is definedhere. The specific binding of VN to endothelial cells demonstrated the following properties: a threefold increase after phorbol ester treatment; 85% inhibition by pretreatment of cells with phosphatidylinositol-phospholipase C to release glycolipid-anchored surface proteins; a 90% inhibition by urokinase (u-PA) receptor blocking antibody, u-PA increased VN binding to cells due to an eightfold increase in the affinity of VN for the u-PA receptor. Structure-function studies showed that the amino-terminal fragment of u-PA, devoid of any proteolytic activity, mediated this effect. Active plasminogen activator inhibitor-1 (PAI-1), but not inactivated PAI-1, inhibited VN binding to cells and displaced VN that was prebound to endothelial cell monolayers. Similarly, VN binding to purified (immobilized) u-PA receptor, but not to integrin, was enhanced by u-PA and inhibited by PAC-1. Hence, the binding of soluble VN to endothelial cell surfaces is mediated by the u-PA receptor, and the relative concentrations of u-PA and PAI-1 are able to regulate the strength of this interaction. Endothelial cell adhesion to immobilized VN was found to be integrin-mediated without any involvementof the VN-uPA-receptor system. Hence, the interaction of VN with the u-PA receptor may be involved in the regulation of cellular processes necessary for endothelial cell invasion and migration at VN-rich extracellular matrix sites. (C) 1996 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 08:07:15