Phorbol ester and 1,2-diolein are not fully equivalent activators of protein kinase C in respect to phosphorylation of membrane proteins in vitro.

Phosphorylation of liver plasma proteins by protein kinase C was studied by using the two best known activators of the enzyme, 12-O-tetradecanoylphorbol-13-acetate (TPA) and 1,2-diolein. While the effects of TPA and diolein were almost identical on two proteins and similar in magnitude on four proteins, the phosphorylation of an additional four proteins was increased only by TPA. We conclude that in respect to phosphorylation of membrane proteins, TPA and diglycerides are not fully equivalent activators of kinase C.