Esmon N L, Carroll R C, Esmon C T
J Biol Chem. 1983 Oct 25;258(20):12238-42.
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.
当凝血酶与内皮细胞表面受体血栓调节蛋白结合形成复合物时，它会失去其促凝活性，因为它不再使纤维蛋白原凝固或激活因子V。于是开展了研究以确定复合物的形成是否也会阻断凝血酶的其他主要促凝功能，即血小板的激活。当与血栓调节蛋白结合时，凝血酶不再诱导血小板聚集或释放[14C]5-羟色胺。使用125I标记的凝血酶或二异丙基磷酰凝血酶进行的结合研究表明，该复合物不会与血小板结合。当在凝血酶与血小板结合后加入血栓调节蛋白时，凝血酶会迅速重新分布到血栓调节蛋白上。这些数据表明，除了其其他抗凝作用外，血栓调节蛋白还可能通过抑制和/或逆转凝血酶引起的血小板激活发挥作用。
