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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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Published in: | FEBS letters 1985-10, Vol.190 (2), p.315-318 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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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 |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(85)81309-0 |