| Literature DB >> 6360281 |
Abstract
The enzymatic catabolism of prostacyclin (PGI2) to 6 oxo prostaglandin E1 (6 oxo PGE1) was studied in platelet-rich and platelet-poor-plasma of rat, rabbit, guinea-pig and man. Rat, rabbit and human platelets convert PGI2 to a product with biological activity and thin layer chromatographic mobility identical to that of authentic 6 oxo PGE1. Platelets from these species also converted 9 beta-[3H]-PGI2 to non-radioactive 6 oxo PGE1 as shown by the progressive loss of extracted radioactivity following incubation. Formation of 6 oxo PGE1 was inhibited by the flavonoid drugs, rutin and naringenin. Guinea-pig platelets did not convert PGI2 to 6 oxo PGE1. Rat, rabbit and guinea-pig platelets do not spontaneously release a 6 oxo PGE1-like substance when incubated at 37 degrees C in the absence of added PGI2 or aggregating agents. The relevance of these findings to the possible physiological and pathophysiological roles of 6 oxo PGE1 in the regulation of platelet function is discussed.Entities:
Mesh:
Substances:
Year: 1983 PMID: 6360281 PMCID: PMC2045025 DOI: 10.1111/j.1476-5381.1983.tb10046.x
Source DB: PubMed Journal: Br J Pharmacol ISSN: 0007-1188 Impact factor: 8.739