Ontogénie changes of protein kinase C in the rat liver, heart and cerebrum were examined from 17-day gestation until adult. Cerebral protein kinase C activity was 19 times less at 17-day fetal as compared to 15-day postnatum or older rats. The enzyme activity in the heart was generally higher in the neonatal period than the adult, but was not correlated with the previously reported α(1)-adrenergic and cholinergic receptor ontogeny. Likewise in the liver, the enzyme activity was not correlated with previously reported α(1)-adrenergic and vasopressin receptor ontogeny. No correlation between protein kinase C and cyclic AMPdependent protein kinase activities was found among these tissues. The enzyme distribution expressed by a cytosol/particulate ratio of 0.72, 2.41 and 0.64 in the liver, heart and brain,respectively, in 20-day fetus was similar to adult values. We conclude that there is a discrete ontogénie pattern of protein kinase C in each organ and it does not sem to be correlated with the ontogénie pattern of hormone receptors which relate to phosphatidylinositol breakdown. The precise role of protein kinase C in relationship to growth and differentiation needs to be further investigated.

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