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PMID: 3689369 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Staurosporine, a potent protein kinase C inhibitor, fails to inhibit 12-O-tetradecanoylphorbol-13-acetate-caused ornithine decarboxylase induction in isolated mouse epidermal cells.

Biochemical and biophysical research communications ·Vol. 148 ·No. 2 ·1987-10-29 ·Pages 740-6

Kiyoto I, Yamamoto S, Aizu E, Kato R

Abstract

Staurosporine, a most potent protein kinase C inhibitor, actually inhibited protein kinase C activity obtained either from cytosol or particulate fraction of mouse epidermis. Staurosporine at the concentrations which exert protein kinase C inhibition, however, failed to inhibit, but markedly augmented 12-O-tetradecanoylphorbol-13-acetate (TPA)-caused ornithine decarboxylase (ODC) induction in isolated mouse epidermal cells. Staurosporine by itself induced ODC activity as TPA does. Mechanism of ODC induction seems different between these two compounds. Another protein kinase C inhibitor, H-7, inhibited both staurosporine- and TPA-caused ODC induction.

MeSH Terms
1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine Alkaloids/pharmacology Animals Animals, Newborn Enzyme Induction/drug effects Epidermis/enzymology In Vitro Techniques Isoquinolines/pharmacology Kinetics Mice Ornithine Decarboxylase/biosynthesis Piperazines/pharmacology Protein Kinase C/antagonists & inhibitors Staurosporine Tetradecanoylphorbol Acetate/pharmacology
Chemicals
Alkaloids Isoquinolines Piperazines 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine Protein Kinase C Ornithine Decarboxylase Staurosporine Tetradecanoylphorbol Acetate
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Kiyoto I
Department of Pharmacology, School of Medicine, Keio University, Tokyo, Japan.
Yamamoto S
Aizu E
Kato R
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1987-10-29
Pages
740-6
Language
English
Region
United States
NLM ID
0372516
Subset
IM
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