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Plasminogen activators in dextran sulfate-activated euglobulin fractions: a
molecular analysis of factor XII- and prekallikrein- dependent fibrinolysis
J Hauert, G Nicoloso, WD Schleuning, F Bachmann and M Schapira
Laboratoire Central d'Hematologie, Centre Hospitalier Universitaire
Vaudois, Lausanne, Switzerland.
To elucidate the mechanism by which activation of the contact system of
blood coagulation leads to expression of fibrinolytic activity, we have
determined the molecular characteristics of the plasminogen activators
present in dextran sulfate-treated euglobulin fractions by
electrophoretic-zymographic analysis and specific immunoadsorption. In
addition to free and protease inhibitor-bound tissue-type plasminogen
activator (t-PA), dextran sulfate precipitates of euglobulins contained the
complex formed between plasma kallikrein and C1-inhibitor, an indicator of
prekallikrein activation. These precipitates also contained substantial
fibrinolytic activity related to urinary-type plasminogen activator (u-PA).
Autoradiographic analysis was then used to evaluate the cleavage of
125I-single-chain u-PA (prourokinase) in dextran sulfate euglobulins as
well as after exposure to kallikrein or beta-factor XIIa. This analysis
supported the conclusion that plasma kallikrein-mediated cleavage and
activation of single-chain u-PA is the mechanism operative for the
development of lytic activity in euglobulin precipitates following
activation of the contact system.
Volume 73,
Issue 4,
pp. 994-999,
03/01/1989
Copyright © 1989 by The American Society of Hematology
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