Stimulation of phospholipase activity and prostaglandin biosynthesis by melittin in cell culture and in vivo.
Melittin, a membrane-active peptide of bee venom, as well as synthetic melittin, stimulated the biosynthesis of prostaglandins by mouse transformed fibroblasts (MC5-5), human fibroblasts (D550), rabbit aorta endothelial cells (CLO), rat lung type II alveolar pneumocytes (L-2) and rabbit smooth muscle cells (R-I). The melittin peptides also stimulated the release of arachidonic acid from the cellular phospholipids of MC5-5 cells. The stimulated prostaglandin biosynthesis by MC5-5 cells was inhibited by indomethacin and dexamethasone. Dexamethasone inhibited also the release of arachidonic acid by MC5-5 cells. In mice, intraperitoneal inoculation of melittin increased 13,14-dihydro-15-keto-PGE2 levels in peripheral blood. Prior injections of the mice with indomethacin prevented the melittin-induced increase in this PGE2 metabolite.
D000818:Animals; D001514:Bee Venoms / Q000494:pharmacology*; D002478:Cells, Cultured; D005347:Fibroblasts / Q000378:metabolism; D008555:Melitten / Q000494:pharmacology*; D051379:Mice; D010740:Phospholipases / Q000378:metabolism*; D011453:Prostaglandins / Q000096:biosynthesis*; D011458:Prostaglandins E / Q000096:biosynthesis; D011817:Rabbits; D013268:Stimulation, Chemical; D013997:Time Factors
D001514:Bee Venoms; D011453:Prostaglandins; D011458:Prostaglandins E; D008555:Melitten; D010740:Phospholipases