Frangulin B, an antagonist of collagen-induced platelet aggregation and adhesion, isolated from Rhamnus formosana

C. M. Teng, Chien-Huang Lin, C. N. Lin, M. I. Chung, T. F. Huang

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)


Emodin and its glycoside frangulin B were isolated from the plant Rhamnus formosana. Emodin inhibited the aggregation of rabbit platelets induced by arachidonic acid and collagen, without affecting that by ADP or PAF, while emodin acetate had no any antiplatelet effect. Frangulin B inhibited selectively and concentration-dependently collagen-induced aggregation and ATP release in rabbit platelets, without affecting those induced by arachidonic acid, ADP, PAF and thrombin. Frangulin B also inhibited the platelet aggregation induced by trimucytin which was reported to be a collagen receptor agonist isolated from Trimeresurus muscrosquamatus snake venom. The aggregability of platelets inhibited by frangulin B could be recovered after washing the platelets. Frangulin B also selectively suppressed the thromboxane B2 formation caused by collagen, but not those by arachidonic acid and thrombin. Similarly, the formation of inositol phosphate caused by collagen was also suppressed by frangulin B, while that of PAF or thrombin was not affected. In the presence of PGE1, frangulin B also decreased Mg2+-dependent platelet adhesion to collagen. It is concluded that frangulin B may be an antagonist of collagen receptor in platelet membrane.

Original languageEnglish
Pages (from-to)1014-1018
Number of pages5
JournalThrombosis and Haemostasis
Issue number6
Publication statusPublished - 1993
Externally publishedYes

ASJC Scopus subject areas

  • Hematology


Dive into the research topics of 'Frangulin B, an antagonist of collagen-induced platelet aggregation and adhesion, isolated from Rhamnus formosana'. Together they form a unique fingerprint.

Cite this