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纤溶酶原激活物抑制剂-1对细胞黏附的调节作用

Regulation of cell adhesion by PAI-1.

作者信息

Loskutoff D J, Curriden S A, Hu G, Deng G

机构信息

Department of Vascular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.

出版信息

APMIS. 1999 Jan;107(1):54-61. doi: 10.1111/j.1699-0463.1999.tb01526.x.

Abstract

Type I plasminogen activator inhibitor (PAI-1) is the primary inhibitor of tissue- and urokinase-type plasminogen activators. It circulates in plasma complexed with vitronectin (VN), the primary PAI-1 binding protein. The somatomedin B (SMB) domain of VN contains both the high affinity PAI-1 binding site and the specific site for urokinase plasminogen activator receptor (uPAR). PAI-1 is able to regulate uPAR-mediated cell adhesion by competing with uPAR for VN binding. Binding of PAI-1 to SMD may also affect integrin-mediated cell adhesion to VN by hindering integrin binding to the RGD sequence adjacent to the uPAR binding site.

摘要

I型纤溶酶原激活物抑制剂(PAI-1)是组织型和尿激酶型纤溶酶原激活物的主要抑制剂。它在血浆中与玻连蛋白(VN)结合循环,玻连蛋白是PAI-1的主要结合蛋白。VN的生长调节素B(SMB)结构域既包含高亲和力的PAI-1结合位点,也包含尿激酶型纤溶酶原激活物受体(uPAR)的特异性位点。PAI-1能够通过与uPAR竞争VN结合来调节uPAR介导的细胞黏附。PAI-1与SMD的结合还可能通过阻碍整合素与uPAR结合位点相邻的RGD序列结合,从而影响整合素介导的细胞与VN的黏附。

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