Differential distribution of protein kinase C isozymes in the various regions of brain.

Abstract

We have previously identified three types of protein kinase C (a Ca2+-activated phospholipid-dependent kinase) isozymes, designated types I, II, and III, from rat brain (Huang, K.-P., Nakabayashi, H., and Huang, F. L. (1986) Proc. Natl. Acad. Sci. U. S. A. 83, 8535-8539). These enzymes are different in their elution profile from hydroxylapatite column, sites of autophosphorylation, and immunoreactivity toward two types of monoclonal antibodies. Now we describe the purification of similar protein kinase C isozymes from monkey brain and their regional distribution in the brain. These primate enzymes all have the same molecular weight of 82,000, and each type of isozyme cross-reacts with the purified monospecific antibodies against its corresponding rat brain counterpart isozyme. These purified antibodies were used to quantify the relative contents of three types of protein kinase C isozymes in various regions of rat and monkey brains. In rat brain, cerebellum contained a high level of the type I isozyme; cerebral cortex, thalamus, and corpus callosum were high in the type II enzyme; and olfactory bulb was highest in the type III enzyme. In monkey brain, the type I isozyme was found to be enriched in cerebellum, hippocampus, and amygdala; the type II enzyme was at very high level in caudate, frontal and motor cerebral cortices, substantia nigra, and thalamus; and the type III enzyme was at the highest level in olfactory bulb. These results indicate that protein kinase C isozymes are differentially distributed in various regions of rat and monkey brains and suggest a unique role for each isozyme in controlling the different neuronal functions in the brain.