ADP-RIBOSYLATION OF RHO ENHANCES ADHESION OF U937 CELLS TO FIBRONECTIN VIA THE ALPHA-5-BETA-1-INTEGRIN RECEPTOR
ADP-RIBOSYLATION OF RHO ENHANCES ADHESION OF U937 CELLS TO FIBRONECTIN VIA THE ALPHA-5-BETA-1-INTEGRIN RECEPTOR
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DOI：
10.1016/0014-5793(95)00285-h
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发表时间：
1995-04-17
期刊：
影响因子：
3.5
通讯作者：
AEPFELBACHER, M
中科院分区：
文献类型：
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作者：
AEPFELBACHER, M
为了研究Rho GTP结合蛋白在单核细胞与纤维连接蛋白黏附中的作用，我们利用肉毒梭菌的C3胞外酶，ADP-核糖化和原位失活Rho蛋白。人单核细胞U937细胞经C3胞外酶(10µg/ml，24 h)处理后，与纤维连接蛋白的粘附率增加2倍，但对胶原和人血清白蛋白的粘附率无明显影响。抗α5和β1整合素亚基的抗体可阻止纤维连接蛋白黏附的增加，但不改变β1和α5的表面表达。这些结果表明，Rho蛋白通过受体后机制调节单核细胞α5β1整合素受体与纤维连接蛋白的相互作用。
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.