Reports

Thromboxanes: selective biosynthesis and distinct biological properties

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Science  09 Jul 1976:
Vol. 193, Issue 4248, pp. 163-165
DOI: 10.1126/science.945611

Abstract

The prostaglandin endoperoxide ring structure alone does not establish suitability as a substrate for thromboxane synthetase, but the degree of unsaturation and carbon chain length are also essential features. Thus, human platelet microsomes can synthesize thromboxane A2, thromboxane A3, but not thromboxane A1 from their respective endoperoxides. The potent vasoconstrictor property of thromboxanes can be dissociated from its capacity to produce platelet aggregation. Furthermore, thromboxane formation is not an essential process in platelet aggregation. The observations indicate the remarkable structural specificity of both the synthetic enzymes, cyclooxygenase and thromboxane synthetase, as well as the vascular and platelet receptor sites.