PMID: 3756531Sep 1, 1986Paper

Subcellular distribution of a calmodulin-dependent protein kinase activity in rat cerebral cortex during development

Brain Research
R P Weinberger, J A Rostas

Abstract

The postnatal development of calmodulin-stimulated phosphorylation of endogenous proteins, in particular the autophosphorylated subunits of the calmodulin-stimulated protein kinase II, were investigated in subcellular fractions of rat cerebral cortex. The major subunit had a mol. wt. of 53,000 Da (designated 50 kDa) and the minor one a mol. wt. of 63,000 Da (designated 60 kDa). The 50-kDa subunit was found to be the only significant phosphoprotein in each fraction and throughout development at its molecular weight. However, the 60-kDa subunit was found to comigrate with other phosphoproteins that accounted for up to 15% of the radioactivity at this molecular weight and which differed between the fractions. 50-kDa autophosphorylation was found to be 3-fold greater in cytoplasmic fractions at day 10 and by adults was evenly distributed between membrane and cytoplasmic fractions. A similar pattern was also found for the total calmodulin-stimulated phosphorylation. Changes in autophosphorylation activity of the 50-kDa subunit were found to represent changes in kinase activity rather than alterations in phosphatase activity. In the membrane, this change was shown to be due to changes in the amount of enzyme. Although in the adult au...Continue Reading

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Citations

Oct 1, 1993·Pediatric Nephrology : Journal of the International Pediatric Nephrology Association·I Zelikovic, J Przekwas
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