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J. Biol. Chem., Vol. 258, Issue 20, 12238-12242, Oct, 1983
NL Esmon, RC Carroll and CT Esmon
When thrombin is complexed to the endothelial cell surface receptor
thrombomodulin, it loses its procoagulant activities in that it no longer
clots fibrinogen or activates factor V. Studies were initiated to determine
if complex formation also blocks thrombin's other major procoagulant
function, the activation of platelets. When bound to thrombomodulin,
thrombin no longer induces platelets to either aggregate or release [14C]
serotonin. Binding studies using 125I- labeled thrombin or diisopropyl
phosphorothrombin indicate that the complex does not bind to the platelet.
When thrombomodulin is added after thrombin has bound to the platelets, the
thrombin rapidly redistributes onto the thrombomodulin. These data suggest
that in addition to its other anticoagulant effects, thrombomodulin may
also act to inhibit and/or reverse platelet activation by thrombin.
Thrombomodulin blocks the ability of thrombin to activate platelets
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