Inhibition of 12-0-Tetradecanoylphorbol43-Acetate-Induced Tumor Promotion and Epidermal Ornithine Decarboxylase Activity in Mouse Skin by Palmitoylcarnitine

Teruo Nakadate; Satoshi Yamamoto; Eriko Aizu; Ryuichi Kato

Inhibition of 12-0-Tetradecanoylphorbol43-Acetate-Induced Tumor Promotion and Epidermal Ornithine Decarboxylase Activity in Mouse Skin by Palmitoylcarnitine

Teruo Nakadate, Satoshi Yamamoto, Eriko Aizu, Ryuichi Kato

School of Pharmacy

Research output: Contribution to journal › Article › peer-review

36 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	1589-1593
Number of pages	5
Journal	Cancer Research
Volume	46
Publication status	Published - 1986 Apr

ASJC Scopus subject areas

Oncology
Cancer Research

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title = "Inhibition of 12-0-Tetradecanoylphorbol43-Acetate-Induced Tumor Promotion and Epidermal Ornithine Decarboxylase Activity in Mouse Skin by Palmitoylcarnitine",

abstract = "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.",

author = "Teruo Nakadate and Satoshi Yamamoto and Eriko Aizu and Ryuichi Kato",

year = "1986",

month = apr,

language = "English",

volume = "46",

pages = "1589--1593",

journal = "Cancer Research",

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publisher = "American Association for Cancer Research Inc.",

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T1 - Inhibition of 12-0-Tetradecanoylphorbol43-Acetate-Induced Tumor Promotion and Epidermal Ornithine Decarboxylase Activity in Mouse Skin by Palmitoylcarnitine

AU - Nakadate, Teruo

AU - Yamamoto, Satoshi

AU - Aizu, Eriko

AU - Kato, Ryuichi

PY - 1986/4

Y1 - 1986/4

N2 - 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.

AB - 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.

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SN - 0008-5472

VL - 46

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JO - Cancer Research

JF - Cancer Research

ER -

Inhibition of 12-0-Tetradecanoylphorbol43-Acetate-Induced Tumor Promotion and Epidermal Ornithine Decarboxylase Activity in Mouse Skin by Palmitoylcarnitine

Abstract

ASJC Scopus subject areas

UN SDGs

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