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Identification of a reversible inhibitor of plasminogen activators in blood plasma

Author: Kluft, C. · Jie, A.F.H. · Sprengers, E.D. · Verheijen, J.H.
Institution: Gaubius Instituut TNO
Source:FEBS Letters, 2, 190, 315-318
Identifier: 229992
Keywords: plasminogen activator · plasminogen activator inhibitor · proteinase inhibitor · clinical article · diagnosis · human · plasma · priority journal · Glycoproteins · Heat · Human · Immunochemistry · Kinetics · Plasminogen Inactivators · Protein Binding · Tissue Plasminogen Activator


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. Chemicals/CAS: plasminogen activator inhibitor, 105844-41-5; plasminogen activator, 9039-53-6; proteinase inhibitor, 37205-61-1; Glycoproteins; Plasminogen Inactivators; Tissue Plasminogen Activator, EC