Title : A novel antithrombotic role for high molecular weight kininogen as inhibitor of plasminogen activator inhibitor-1 function.

Pub. Date : 2002 Sep 6

PMID : 12082110






2 Functional Relationships(s)
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1 VN also interacts with two-chain high molecular weight kininogen (HKa), particularly its His-Gly-Lys-rich domain 5, and both HKa and PAI-1 are antiadhesive factors that have been shown to compete for binding to VN. Glycine vitronectin Homo sapiens
2 Although having no direct effect on PAI-1 activity itself, HKa domain 5 or the peptide Gly(486)-Lys(502) markedly destabilized the VN.PAI-1 complex interaction, resulting in a significant reduction of PAI-1 inhibitory function on plasminogen activators, resembling the effect of VN antibodies that prevent stabilization of PAI-1. Glycine vitronectin Homo sapiens