Abstract
Ca dependent, phospholipid regulated protein kinase (PK-C) serves a crucial role for receptor activation by substances such as α-adrenergic agonists which stimulate phosphatidylinositol breakdown. Ontogeny of α1-receptors is known to be organ specific and distinct from β-receptors. To assess receptor-protein kinase relationship, ontogeny of PK-C and cAMP dependent protein kinase (PK-A) activities were compared to cytosol from rat liver and heart:
Cytosol/particulate ratio of PK-C at 21d fetus were 0.72 & 2.41 for liver and heart and similar to adult. DEAE cellulose column separation of PK-C showed a major and a minor peak, & the minor peak was Ca and phosphatidylserine independent in liver and heart. This pattern did not change with age qualitatively. We conclude that PK-C activity is higher perinatally, its subcellular distribution does not seem to change with age, and it is not correlated with PK-A activity or previously reported α1-receptor density in these organs. We speculate that PK-C is not rate limiting in the receptor activation perinatally.
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Noguchi, A., Deguire, J. & Zanaboni, P. 297 PROTEIN KINASE C (PK-C) IN THE DEVELOPING RAT LIVER AND HEART. Pediatr Res 19, 160 (1985). https://doi.org/10.1203/00006450-198504000-00327
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DOI: https://doi.org/10.1203/00006450-198504000-00327
