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. 1989 Jul 1;261(1):131–136. doi: 10.1042/bj2610131

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

F E Mitchell 1, R M Marais 1, P J Parker 1
PMCID: PMC1138792  PMID: 2789040

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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