Chemotactic peptide-induced arachidonic acid mobilization in human polymorphonuclear leukocytes.
Human polymorphonuclear leukocytes prelabeled with tritiated arachidonic acid liberated radiolabeled products when exposed to the chemotactic peptide fMet-Leu-Phe. The effect was enhanced in the presence of phorbol-12-myristate 13-acetate or 1-oleoyl-2-acetyl glycerol; these agents activate phospholipid- and Ca2+-dependent protein kinase C. In contrast, arachidonic acid mobilization was suppressed by two compounds known to inhibit protein kinase C activity: polymyxin B and 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine. These results suggest that protein kinase C was involved in arachidonic acid mobilization in leukocytes stimulated with chemotactic peptide.
D016718:Arachidonic Acid; D001095:Arachidonic Acids / Q000378:metabolism*; D002118:Calcium / Q000378:metabolism; D002855:Chromatography, Thin Layer; D003600:Cytosol / Q000378:metabolism; D006801:Humans; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000494:pharmacology*; D009504:Neutrophils / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism; D013997:Time Factors; D014316:Tritium
D001095:Arachidonic Acids; D010743:Phospholipids; D014316:Tritium; D016718:Arachidonic Acid; D009240:N-Formylmethionine Leucyl-Phenylalanine; D002118:Calcium