The Phosphorylation of Protein Kinase C As a Potential Measure of Activation

Overview

Journal Biochem J

Specialty Biochemistry

Date 1989 Jul 1

PMID 2789040

Citations 17

Authors

F E Mitchell

R M Marais

P J Parker

Affiliations

Soon will be listed here.

Abstract

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.

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