Synthesis of 6-keto-PGF1alpha by ram seminal vesicle microsomes.
At low substrate/enzyme ratios, and in the absence of reduced glutathione (GSH), the major prostaglandin (PG) biosynthesised by the ram seminal vesicle cyclo-oxygenase from arachidonic acid was 6-keto-PGF1alpha. The addition of nanomolar amounts of reduced GSH suppressed biosynthesis of this product and stimulated the formation of PGE2; 1-epinephrine enhanced the conversion of the substrate but had no effect on the type of product formed. 15-Hydroperoxy arachidonic acid selectively inhibited formation of 6-keto-PGF1alpha (IC50 100 muM) but blocked synthesis of all cyclo-oxygenase products at concentrations greater than 1 mM. At substrate concentrations of muM or greater, synthesis of 6-keto-PGF1alpha was inhibited and PGE2 and PGF2alpha were the main products formed.
D000818:Animals; D001095:Arachidonic Acids / Q000494:pharmacology; D004837:Epinephrine / Q000494:pharmacology; D005978:Glutathione / Q000494:pharmacology; D008297:Male; D008861:Microsomes / Q000378:metabolism*; D011458:Prostaglandins E / Q000096:biosynthesis; D011460:Prostaglandins F / Q000096:biosynthesis* / Q000378:metabolism; D012669:Seminal Vesicles / Q000378:metabolism*; D012756:Sheep
D001095:Arachidonic Acids; D011458:Prostaglandins E; D011460:Prostaglandins F; D005978:Glutathione; D004837:Epinephrine