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Identification of a reversible inhibitor of plasminogen activators in blood plasma

Inhibition of tissue-type plasminogen activator (t-PA) by pooled plasma could be ascribed for only 60% to the endothelial cell type PA inhibitor. The residual inhibition is ascribed to a so-far undescribed plasma component present at 0.2 nmol l . This component shows reversible binding to t-PA with...

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Bibliographic Details
Published in:FEBS letters 1985-10, Vol.190 (2), p.315-318
Main Authors: Kluft, C., Jie, A.F.H., Sprengers, E.D., Verheijen, J.H.
Format: Article
Language:English
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Summary:Inhibition of tissue-type plasminogen activator (t-PA) by pooled plasma could be ascribed for only 60% to the endothelial cell type PA inhibitor. The residual inhibition is ascribed to a so-far undescribed plasma component present at 0.2 nmol l . This component shows reversible binding to t-PA with an apparent K i of 10 pmol l (does not hinder t-PA binding to fibrin); also reacts with urokinase, but not with DIP-t-PA; is stable at 37°C and does not occur in media of endothelial cells, hepatocytes and fibroblasts. This PA binding component in plasma adds to the regulation of plasminogen activator activities. Fibrinolysis Tissue-type plasminogen activator Urokinase Blood plasma Endothelial cell type plasminogen activator inhibitor Protease inhibitor
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(85)81309-0