The phosphorylation of protein kinase C as a potential measure of activation

As a means of determining the role of protein kinase C in the signal transduction from novel growth factors and hormones, we investigated the effects of well-characterized agents on the phosphorylation state of protein kinase C itself. These studies show that agents that stimulate protein kinase C e...

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Bibliographic Details
Published inBiochemical journal Vol. 261; no. 1; pp. 131 - 136
Main Authors Mitchell, F E, Marais, R M, Parker, P J
Format Journal Article
LanguageEnglish
Published England 01.07.1989
Subjects
Cells, Cultured
Enzyme Activation
Epidermal Growth Factor
Fibroblasts - enzymology
growth factors
Humans
Phosphorylation
Platelet-Derived Growth Factor
protein kinase C
Protein Kinase C - metabolism
Tetradecanoylphorbol Acetate
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Summary:As a means of determining the role of protein kinase C in the signal transduction from novel growth factors and hormones, we investigated the effects of well-characterized agents on the phosphorylation state of protein kinase C itself. These studies show that agents that stimulate protein kinase C either directly (phorbol esters) or indirectly through phosphatidylinositol breakdown (platelet-derived growth factor) induce an increase in the phosphorylation state of the kinase. By contrast, epidermal growth factor, which does not stimulate protein kinase C in fibroblasts, does not increase the phosphorylation state of protein kinase C, but leads to a decrease. The data suggest that the phosphorylation state of protein kinase C is dynamically controlled and can be used to provide evidence of protein kinase C activation.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2610131