Domain 1 of the urokinase receptor (uPAR) is required for uPAR-mediated cell binding to vitronectin

被引：72

作者：

Sidenius, N ^{[1
]}

Blasi, F ^{[1
]}

机构：

[1] Ist Sci San Raffaele, DIBIT, Dept Mol Pathol & Med, Mol Genet Unit, I-20132 Milan, Italy

来源：

FEBS LETTERS | 2000年 / 470卷 / 01期

关键词：

uPAR; vitronectin; adhesion;

D O I：

10.1016/S0014-5793(00)01282-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In the present paper we have analyzed uPAR-mediated cellular binding to vitronectin using the murine erythroid progenitor cell line 32D, We show that expression of uPAR in 32D cells promotes cellular binding to vitronectin, but fails to support cell spreading, The strength of binding is correlated to the expression level of uPAR and is strongly stimulated by the presence of uPAR ligands, Using a truncated variant of uPAR lacking domain 1 and by antibody inhibition experiments, we demonstrate that domain 1 plays a crucial role in uPAR-mediated cellular binding. The failure of the mutant uPAR to promote cellular binding is paralleled by a strong reduction in the affinity for vitronectin in vitro. (C) 2000 Federation of European Biochemical Societies.

引用

页码：40 / 46

页数：7

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