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Conversion of prostacyclin to 6 oxo prostaglandin E 1 by rat, rabbit, guinea‐pig and human platelets
Author(s) -
Griffiths R.J.,
Moore P.K.
Publication year - 1983
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.1476-5381.1983.tb10046.x
Subject(s) - prostacyclin , platelet , guinea pig , chemistry , endocrinology , prostaglandin e , medicine , biochemistry , biology
1 The enzymatic catabolism of prostacyclin (PGI 2 ) to 6 oxo prostaglandin E 1 (6 oxo PGE 1 ) was studied in platelet‐rich and platelet‐poor‐plasma of rat, rabbit, guinea‐pig and man. 2 Rat, rabbit and human platelets convert PGI 2 to a product with biological activity and thin layer chromatographic mobility identical to that of authentic 6 oxo PGE 1 . Platelets from these species also converted 9β‐[ 3 H]‐PGI 2 to non‐radioactive 6 oxo PGE 1 as shown by the progressive loss of extracted radioactivity following incubation. Formation of 6 oxo PGE 1 was inhibited by the flavonoid drugs, rutin and naringenin. 3 Guinea‐pig platelets did not convert PGI 2 to 6 oxo PGE 1 . 4 Rat, rabbit and guinea‐pig platelets do not spontaneously release a 6 oxo PGE 1 ‐like substance when incubated at 37°C in the absence of added PGI 2 or aggregating agents. 5 The relevance of these findings to the possible physiological and pathophysiological roles of 6 oxo PGE 1 in the regulation of platelet function is discussed.