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INHIBITION OF THROMBOXANE A 2 BIOSYNTHESIS IN HUMAN PLATELETS BY BURIMAMIDE
Author(s) -
ALLAN G.,
EAKINS K.E.,
KULKARNI P.S.,
LEVI R.
Publication year - 1980
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.1980.tb10920.x
Subject(s) - prostacyclin , chemistry , thromboxane a synthase , thromboxane a2 , platelet , thromboxane , metiamide , prostaglandin h2 , medicine , endocrinology , biochemistry , receptor , biology , histamine h2 receptor , antagonist
1 Burimamide selectively inhibited the formation of thromboxane A 2 from prostaglandin endoperoxides by human platelet microsomes in a dose‐dependent manner (IC 50 = 2.5 × 10 −5 m ). Burimamide was found to be equipotent to imidazole as a thromboxane synthetase inhibitor. 2 Metiamide, cimetidine and a series of compounds either bearing a structural or pharmacological relationship to histamine caused little or no inhibition of thromboxane A 2 biosynthesis by human platelet microsomes. 3 Burimamide (5 × 10 −4 to 2.3 × 10 −3 m ) did not inhibit either the cyclo‐oxygenase or the prostacyclin synthetase of sheep seminal vesicles or the prostacyclin synthetase of dog aortic microsomes. 4 Burimamide (2.5 × 10 −5 to 1.2 × 10 −4 m ) inhibited sodium arachidonate‐induced human platelet aggregation; the degree of inhibition was dependent upon the concentration of arachidonic acid used to aggregate the platelets.