Palmitoylcarnitine, which has been reported to be an inhibitor of calcium-activated, phospholipid-dependent protein kinase (protein kinase C), inhibited 12-0-tetradecanoylphorbol-13-acetate (TPA)-induced epidermal ornithine decarboxylase in mouse skin in a dose-dependent manner. Neither acetylcarnitine nor palmitk acid inhibited TPA-caused ornithine decarboxyhtse 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. Therefore, it seems unlikely that the potent anti-tumor-promoting action of palmitoylatrnitine which is shown in the present study, is explained solely by its effect on protein kinase C.
|Number of pages||5|
|Publication status||Published - 1986 Apr|
ASJC Scopus subject areas
- Cancer Research