Disintegrin interaction with alpha(v)beta(3) integrin on human umbilical vein endothelial cells: Expression of ligand-induced binding site on beta(3) subunit

被引:63
作者
Juliano, D
Wang, YQ
Marcinkiewicz, C
Rosenthal, LA
Stewart, GJ
Niewiarowski, S
机构
[1] TEMPLE UNIV,SCH MED,DEPT PHYSIOL,PHILADELPHIA,PA 19140
[2] TEMPLE UNIV,SCH MED,SOL SHERRY THROMBOSIS RES CTR,PHILADELPHIA,PA 19140
[3] TEMPLE UNIV,SCH MED,DEPT MICROBIOL & IMMUNOL,PHILADELPHIA,PA 19140
关键词
D O I
10.1006/excr.1996.0164
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
The effect of seven disintegrins (albolabrin, barbourin, bitistatin, echistatin, eristostatin, flavoridin, and kistrin) and the neurotoxin analogue, mambin, on the adhesion of human umbilical vein endothelial cells (HUVEC) to immobilized vitronectin and fibronectin has been studied. Adhesion to vitronectin was significantly inhibited by echistatin, kistrin, flavoridin, and mambin. Echistatin, flavoridin, and kistrin bound with high affinity to immobilized alpha(v) beta(3) in solid phase assay; other disintegrins bound at a much lower level. Echistatin and flavoridin had a modest inhibitory effect on HUVEC adhesion to fibronectin. HUVEC adhered to disintegrins with a high selectivity toward bitistatin, echistatin, flavoridin, kistrin, and mambin. Adhesion of HUVEC to fibronectin and vitronectin resulted in cell spreading, whereas cells adhering to immobilized echistatin remained globular and cells adhering to kistrin showed abnormal morphology. Echistatin and kistrin potently inhibited the binding of monoclonal antibody (Mab) 7E3, which recognizes the alpha(v) beta(3) complex, to HUVEC. Echistatin and kistrin also induced the binding to HUVEC of Mab 62, which recognizes the ligand-induced binding site (LIBS) epitope on the beta(3) subunit, enhancing HUVEC binding to immobilized Mab 62. Similar results with both antibodies were obtained in Chinese hamster ovary cells transfected with alpha(v) beta(3) genes. In conclusion, disintegrin interaction with HUVEC appears to be selectively mediated by a;Ps receptors, and it results in an expression of LIBS epitope that may play a role in the regulation of ligand-binding affinity and intracellular signaling. (C) 1996 Academic Press, Inc.
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页码:132 / 142
页数:11
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