ADP-RIBOSYLATION OF RHO ENHANCES ADHESION OF U937 CELLS TO FIBRONECTIN VIA THE ALPHA-5-BETA-1-INTEGRIN RECEPTOR

被引：34

作者：

AEPFELBACHER, M

机构：

[1] Institut für Prophylaxe and Epidemiologie der Kreislaufkrankheiten, Ludwig-Maximilians Universität München, 80336 München

来源：

FEBS LETTERS | 1995年 / 363卷 / 1-2期

关键词：

ADP-RIBOSYLATION; GTP BINDING PROTEIN; RHO; MONOCYTE; FIBRONECTIN; INTEGRIN;

D O I：

10.1016/0014-5793(95)00285-H

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：

To examine the role of Rho GTP binding proteins in the adhesion of monocytic cells to fibronectin we used the C3 exoenzyme of Clostridium botulinum which ADP-ribosylates and inactivates Rho proteins in situ. Treatment of human monocytic U937 cells with C3 exoenzyme (10 mu g/ml, 24 h) increased adhesion to fibronectin 2-fold but had no effect on adhesion to collagen or human serum albumin. The increase in fibronectin adhesion was prevented by antibodies against the alpha 5 and beta 1 integrin subunits, but surface expression of beta 1 and alpha 5 was not altered. These results suggest that Rho proteins regulate the interaction of the monocyte alpha 5 beta 1 integrin receptor with fibronectin by post receptor mechanisms.

引用

页码：78 / 80

页数：3

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