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Aldosterone Rapidly Represses Protein Kinase C Activity in Neonatal Rat Cardiomyocytes in Vitro

Baker Medical Research Institute, Melbourne, Australia

Address all correspondence and requests for reprints to: Prof. John W. Funder, Baker Medical Research Institute, P.O. Box 348, Prahran, Victoria Australia 3181.

Aldosterone lowers protein kinase C (PKC) activity in myocyte-enriched cultures from neonatal Sprague-Dawley rat hearts, with activity measured by the transfer of phosphate to myristolated alanine-rich C-kinase substrate, in the presence of Ca²⁺, phosphatidylserine, and diolein. The effect is rapid, with a significant effect after 1 min exposure, half maximal at 1 nM aldosterone, with steroids showing a hierarchy of potency aldosterone = 9 fluorocortisol > deoxycorticosterone > corticosterone > spironolactone. Both Ca²⁺-dependent and -independent PKC activity appear equally inhibited by aldosterone, and PMA-stimulated increases in PKC activity appear similarly aldosterone-sensitive. No displaceable binding of [³H]aldosterone to purified PKC can be shown, evidence against a direct effect of aldosterone on PKC; aldosterone does not alter basal or PMA-stimulated PKC activity in cardiac fibroblasts, evidence for a cell-specific mediator of the myocyte effect. Taken with the previous demonstration of the potentiation of aldosterone-specific MR-mediated effects by PKC activation, the present data argue for the existence of a complex cross-talk mechanism between aldosterone and factors affecting PKC activity in the heart.

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