Postnatal development of a brain-specific subspecies of protein kinase C in rat

Protein kinase C in the developing rat brain was investigated by a biochemical assay and by light-microscopic immunocytochemistry. The protein kinase was resolved on hydroxyapatite column chromatography into 3 fractions, designated types I, II, and III. Type I, with structure encoded by a gamma-sequence, was not detected early postnatally, maintained a low level of activity during the first week, which increased gradually, and reached its maximum around postnatal day 28. This type of enzyme was expressed specifically in nervous tissues, and was not found in any other tissues thus far tested. Type II enzyme activity, a mixture of the 2 subspecies encoded by the beta I- and beta II-sequences, was found at birth, increased rapidly, and reached a plateau level between postnatal days 14 and 28. This type was the predominant subspecies of protein kinase C in the brain. Type III, its structure encoded by the alpha-sequence, was also detected at birth, and reached its maximum level on postnatal day 7. Immunocytochemical studies with a monoclonal antibody, which recognized preferentially the type I enzyme, visualized the developmental pattern of type I subspecies in the Purkinje cell, a typical cell having a large quantity of type I protein kinase C.