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Thromb Haemost 1991; 66(04): 489-493
DOI: 10.1055/s-0038-1646444
Review Article
Schattauer GmbH Stuttgart

Mechanism of Action of a Potent Antiplatelet Peptide, Triflavin from Trimeresurus flavoviridis Snake Venom

Tur-Fu Huang
The Pharmacological Institute, College of Medicine, National Taiwan University, Taipei, Taiwan
,
Joen-Rong Sheu
The Pharmacological Institute, College of Medicine, National Taiwan University, Taipei, Taiwan
,
Che-Ming Teng
The Pharmacological Institute, College of Medicine, National Taiwan University, Taipei, Taiwan
› Author Affiliations
Further Information

Publication History

Received 28 August 1990

Accepted 16 April 1991

Publication Date:
25 July 2018 (online)

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Summary

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.

 

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