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Complement proteins C5b-9 stimulate procoagulant activity through platelet
prothrombinase
T Wiedmer, CT Esmon and PJ Sims
The capacity of platelets treated with nonlytic concentrations of the C5b-9
proteins to catalyze prothrombin activation and thereby trigger clot
formation has been investigated. When suspended in the presence of
exogenous factors Xa and Va, gel-filtered platelets treated with purified
C5b-9 proteins catalyzed prothrombin to thrombin conversion at rates up to
tenfold above controls, and exceeded by up to fourfold the prothrombinase
activity observed for thrombin-stimulated platelets. In the absence of
added factor Va, C5b-9 assembly on the platelet surface significantly
shortened the lag period before prothrombinase expression that was observed
for untreated platelets and increased the maximum catalytic rate of
thrombin formation. A comparison with other platelet stimuli revealed that
the C5b-9-induced activation of platelet prothrombinase closely paralleled
the effects mediated by calcium ionophore A23187. Our data suggest that the
C5b-9 proteins promote the release of platelet factor V and the assembly of
the prothrombinase complex, thereby potentiating the effects of thrombin on
the activation of prothrombinase. Membrane assembly of the C5b-9 proteins
was also observed to markedly accelerate the rate of platelet-catalyzed
plasma clotting, suggesting a direct link between C5b-9-mediated
prothrombinase activation and procoagulant activity accompanying
immunologic damage to the platelet.
Volume 68,
Issue 4,
pp. 875-880,
10/01/1986
Copyright © 1986 by The American Society of Hematology
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