Regulation of cell adhesion by PAI‐1
David J. Loskutoff, Scott A. Curriden, Geng Hu, Gang Deng
Abstract
David J. Loskutoff, Scott A. Curriden, Geng Hu, Gang Deng
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.
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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.
Key concepts: Vitronectin, Urokinase receptor, Integrin, Plasminogen activator, Urokinase, Chemistry, Cell adhesion, Receptor