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 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.
Mitchell
F E
FE
Ludwig Institute for Cancer Research (Middlesex Hospital/University College Branch), London, U.K.
Marais
R M
RM
Parker
P J
PJ
D002478:Cells, Cultured; D004789:Enzyme Activation; D004815:Epidermal Growth Factor; D005347:Fibroblasts / Q000201:enzymology; D006801:Humans; D010766:Phosphorylation; D010982:Platelet-Derived Growth Factor; D011493:Protein Kinase C / Q000378:metabolism*; D013755:Tetradecanoylphorbol Acetate
D010982:Platelet-Derived Growth Factor; D004815:Epidermal Growth Factor; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate