Inhibition of 12-O-tetradecanoylphorbol-13-acetate-induced tumor promotion and epidermal ornithine decarboxylase activity in mouse skin by palmitoylcarnitine

T. Nakadate, S. Yamamoto, Eriko Yokota, R. Kato

Research output: Contribution to journalArticle

32 Citations (Scopus)

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. 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.

Original languageEnglish
Pages (from-to)1589-1593
Number of pages5
JournalCancer Research
Volume46
Issue number4
Publication statusPublished - 1986

Fingerprint

Palmitoylcarnitine
Ornithine Decarboxylase
Tetradecanoylphorbol Acetate
Protein Kinase C
Phosphatidylserines
Skin
Neoplasms
Acetylcarnitine
Palmitic Acid
Enzymes

ASJC Scopus subject areas

  • Cancer Research
  • Oncology

Cite this

Inhibition of 12-O-tetradecanoylphorbol-13-acetate-induced tumor promotion and epidermal ornithine decarboxylase activity in mouse skin by palmitoylcarnitine. / Nakadate, T.; Yamamoto, S.; Yokota, Eriko; Kato, R.

In: Cancer Research, Vol. 46, No. 4, 1986, p. 1589-1593.

Research output: Contribution to journalArticle

@article{2904d46c11bd4aedbfe32b9927a50de4,
title = "Inhibition of 12-O-tetradecanoylphorbol-13-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-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.",
author = "T. Nakadate and S. Yamamoto and Eriko Yokota and R. Kato",
year = "1986",
language = "English",
volume = "46",
pages = "1589--1593",
journal = "Cancer Research",
issn = "0008-5472",
publisher = "American Association for Cancer Research Inc.",
number = "4",

}

TY - JOUR

T1 - Inhibition of 12-O-tetradecanoylphorbol-13-acetate-induced tumor promotion and epidermal ornithine decarboxylase activity in mouse skin by palmitoylcarnitine

AU - Nakadate, T.

AU - Yamamoto, S.

AU - Yokota, Eriko

AU - Kato, R.

PY - 1986

Y1 - 1986

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0022590190&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022590190&partnerID=8YFLogxK

M3 - Article

VL - 46

SP - 1589

EP - 1593

JO - Cancer Research

JF - Cancer Research

SN - 0008-5472

IS - 4

ER -