• 1 April 1986
    • journal article
    • research article
    • Vol. 46  (4) , 1589-1593
Abstract
Palmitoylcarnitine, which has been reported to be an inhibitor of calcium-activated, phospholipid-dependent protein kinase (protein kinase C), inhibited 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced epidermal ornithine decarboxylase in mouse skin in a dose-dependent manner. Neither acetylcarnitine nor palmitic acid inhibited TPA-caused ornithine decarboxylase induction. In addition, palmitoylcarnitine markedly inhibited skin tumor promotion induced by TPA. Palmitoylcarnitine inhibited epidermal protein kinase C activity which was stimulated by Ca2+ in the presence of phosphatidylserine but failed to inhibit the enzyme activity which was stimulated by TPA in the presence of either phosphatidylserine or Ca2+ plus phosphatidylserine. Therfore, it seems unlikely that the potent anti-tumor-promoting action of palmitoylcarnitine, which is shown in the present study, is explained solely by its effect on protein kinase C.

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