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Studies on the acute release of tissue-type plasminogen activator from
human endothelial cells in vitro and in rats in vivo: evidence for a
dynamic storage pool
Y van den Eijnden-Schrauwen, T Kooistra, RE de Vries and JJ Emeis
Division of Vascular and Connective Tissue Research, Gaubius Laboratory
TNO-PG, Leiden, The Netherlands.
The process of acute release of tissue-type plasminogen activator (tPA) is
important in locally speeding up fibrinolysis. Using a sensitive
enzyme-linked immunosorbent assay for tPA, we investigated the acute
release of tPA from cultured human umbilical vein endothelial cells. The
addition of thrombin (0.003 to 3 NIH U/mL) caused the dose- dependent
release of noncomplexed, enzymatically active tPA into the medium. The
amount of tPA released into the medium by thrombin was similar to the
difference in the amounts of tPA present in extracts from thrombin-treated
cells and control cells. The process of acute release of tPA was complete
in 1 minute, whereas the concomitant release of von Willebrand factor into
the medium was slightly slower (maximum after 3 minutes). By increasing
(c.q. decreasing) tPA synthesis, it was found that the amount of tPA
constitutively secreted, the amount acutely released, and the amount in
cell extracts were increased (c.q. decreased) to the same extent. The same
relation was found in vivo. When rats were pretreated with cholera toxin or
retinoic acid to increase tPA synthesis, plasma levels of tPA were
increased, whereas acute release of tPA, as induced by bradykinin, was
increased to the same extent. Acutely released tPA and constitutively
secreted tPA were liberated from different pathways in human umbilical vein
endothelial cells; tPA had, relative to the in vivo situation, a short
residence time in the acutely releasable pathway.
Volume 85,
Issue 12,
pp. 3510-3517,
06/15/1995
Copyright © 1995 by The American Society of Hematology
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