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Activated protein C decreases plasminogen activator-inhibitor activity in
endothelial cell-conditioned medium
VW van Hinsbergh, RM Bertina, A van Wijngaarden, NH van Tilburg, JJ Emeis and F Haverkate
Confluent cultures of endothelial cells from human umbilical cord were used
to study the effect of activated human protein C (APC) on the production of
plasminogen activators, plasminogen activator-inhibitor, and factor
VIII-related antigen. Addition of APC to the cells in a serum-free medium
did not affect the production of tissue-type plasminogen activator (t-PA)
or factor VIII-related antigen; under all measured conditions, no urokinase
activity was found. However, less plasminogen activator-inhibitor activity
accumulated in the conditioned medium in the presence of APC. This decrease
was dose dependent and could be prevented by specific anti-protein C
antibodies. No decrease was observed with the zymogen protein C or with
diisopropylfluorophosphate-inactivated APC. APC also decreased the t-PA
inhibitor activity in endothelial cell-conditioned medium in the absence of
cells, which suggests that the effect of APC is at least partly due to a
direct effect of APC on the plasminogen activator- inhibitor. High
concentrations of thrombin-but not of factor Xa or IXa-- had a similar
effect on the t-PA inhibitor activity. The effect of APC on the plasminogen
activator-inhibitor provides a new mechanism by which APC may enhance
fibrinolysis. The data suggest that activation of the coagulation system
may lead to a secondary increase of the fibrinolytic activity by changing
the balance between plasminogen activator(s) and its (their) fast-acting
inhibitor.
Volume 65,
Issue 2,
pp. 444-451,
02/01/1985
Copyright © 1985 by The American Society of Hematology
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