Protein kinase C mediates endotoxin and zymosan-induced prostaglandin synthesis.
Addition of the protein kinase C activators phorbol-12-myristate-13-acetate or 1-oleoyl-2-acetylglycerol, or endotoxin (lipopolysaccharide) or zymosan, to RAW264.7 murine macrophages markedly stimulated prostaglandin E2 synthesis. The protein kinase C inhibitor 1-(5-isoquinolinesulfonyl)-2-methylpiperazine (H-7) blocked prostaglandin E2 synthesis in response to all these agonists. The present results suggest that activation of protein kinase C is a step in the stimulation of arachidonic acid metabolism by agonists in macrophages.
D000818:Animals; D016718:Arachidonic Acid; D001095:Arachidonic Acids / Q000378:metabolism; D002473:Cell Wall / Q000187:drug effects / Q000378:metabolism; D015232:Dinoprostone; D004731:Endotoxins / Q000494:pharmacology*; D007942:Leukemia, Experimental / Q000378:metabolism; D051379:Mice; D011453:Prostaglandins / Q000096:biosynthesis*; D011458:Prostaglandins E / Q000096:biosynthesis; D011493:Protein Kinase C / Q000037:antagonists & inhibitors / Q000502:physiology*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D015054:Zymosan / Q000494:pharmacology*
D001095:Arachidonic Acids; D004731:Endotoxins; D011453:Prostaglandins; D011458:Prostaglandins E; D016718:Arachidonic Acid; D015054:Zymosan; D011493:Protein Kinase C; D015232:Dinoprostone; D013755:Tetradecanoylphorbol Acetate