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Effect of phorbol ester on cAMP-dependent protein kinase activity in cardiomyocytes

Zhou, W.; Xiao, D.; Zheng, C.; Wang, X.; Zhang, J.

Chinese Medical Sciences Journal 10(4): 191-194

1995

ISSN/ISBN: 1001-9294
PMID: 8745576
Document Number: 443736
Cardiomyocytes isolated from neonatal rats were treated with phorbol-12-myristate-13-acetate (PMA) ranging from 10(-11) to 10(-7) mol/L for 20 min, causing cytosol protein kinase A (PKA) activity to decrease while particulate PKA activity increase in a concentration-dependent manner. The change of PKA activity induced by PMA was abolished completely by pretreatment of polymyxin B or depletion of protein kinase C (PKC). Type II PKA activity in particulate fraction was enhanced remarkably, while that of type I PKA was not altered when the cells were treated with 100 nmol/L PMA. The results suggested that subcellular distribution and activity of PKA in cardiomyocytes may be regulated by PKC.

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