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

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.