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Inhibition of 12-O-Tetradecanoylphorbol-13-acetate-induced Tumor Promotion and Epidermal Ornithine Decarboxylase Activity in Mouse Skin by Palmitoylcarnitine¹

Department of Pharmacology, School of Medicine, Keio University, 35 Shinanomachi, Shinjuku-ku, Tokyo 160, Japan

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. Therefore, 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.

¹ Part of this work was supported by an award from the Princess Takamatsu Cancer Research Fund, by Grants-in-Aid for Cancer Research and for Encouragement of Young Scientists from the Ministry of Education, Science, and Culture of Japan, and by a Grant-in-Aid for Cancer Research from the Ministry of Health and Welfare of Japan.

² Present address: Molecular Mechanisms of Tumor Promotion Section, Laboratory of Cellular Carcinogenesis and Tumor Promotion, National Cancer Institute, Bethesda, MD 20205.

³ To whom requests for reprints should be addressed.

Received 3/15/85. Revised 8/21/85. Accepted 12/11/85.

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