Huang T F, Sheu J R, Teng C M
Pharmacological Institute, College of Medicine, National Taiwan University, Taipei.
Thromb Haemost. 1991 Oct 1;66(4):489-93.
Triflavin, an antiplatelet peptide from Trimeresurus flavoviridis snake venom, inhibits aggregation of human platelets stimulated by a variety of agonists. However, triflavin does not affect the shape change and release reaction of platelets stimulated by thrombin and collagen. In this paper, we further investigate its effect on the intracellular events occurring after the activation of platelets. Triflavin does not inhibit the intracellular free calcium rise of Quin 2-AM loaded platelets stimulated by thrombin and it also has no significant effect on thromboxane B2 formation of platelets stimulated by thrombin. Triflavin does not affect the 3(H)-inositol monophosphate formation of the 3(H)-myoinositol loaded platelets. However, triflavin dose-dependently inhibits fibrinogen-induced aggregation and 125I-fibrinogen binding of ADP-stimulated platelets. In addition, triflavin dose-dependently blocks fibrinogen-induced aggregation of elastase-treated platelets. It is concluded that triflavin specifically inhibits fibrinogen binding to fibrinogen receptors associated with glycoprotein IIb/IIIa complex on platelet membrane surface without any inhibitory effect on the platelet-activation process.
竹叶青毒素是一种从竹叶青蛇毒中提取的抗血小板肽，可抑制多种激动剂刺激的人血小板聚集。然而，竹叶青毒素并不影响凝血酶和胶原蛋白刺激的血小板的形态变化和释放反应。在本文中，我们进一步研究了其对血小板激活后细胞内事件的影响。竹叶青毒素不抑制凝血酶刺激的负载喹吖因-2-乙酰甲酯（Quin 2-AM）的血小板的细胞内游离钙升高，对凝血酶刺激的血小板血栓素B2的形成也无显著影响。竹叶青毒素不影响负载3(H)-肌醇的血小板的3(H)-肌醇单磷酸的形成。然而，竹叶青毒素剂量依赖性地抑制纤维蛋白原诱导的ADP刺激的血小板聚集和125I-纤维蛋白原结合。此外，竹叶青毒素剂量依赖性地阻断弹性蛋白酶处理的血小板的纤维蛋白原诱导的聚集。得出的结论是，竹叶青毒素特异性抑制纤维蛋白原与血小板膜表面糖蛋白IIb/IIIa复合物相关的纤维蛋白原受体的结合，而对血小板激活过程无任何抑制作用。
