The participation of cAMP and protein kinase C in the regulation of aldosterone biosynthesis by potassium.

Biomedical science Pub Date : 1991-01-01
V M Pushkarev, A S Mikosha
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Abstract

The mechanism of the effect of potassium ions (K+) on aldosterone production in guinea pig adrenal cortex was examined. At high K+ concentrations (approximately 8 mM) in the incubation media, aldosterone output and content was elevated, and there was a significant increase in the phosphorylation of intracellular proteins and of protein kinase C activity. Cyclic AMP levels showed a less significant increase. EGTA and lanthanum ions (La3+), and also chlorpromazine with regard to protein phosphorylation, appeared to remove the effect of raised K+ concentrations on steroidogenesis and protein phosphorylation. At low K+ concentrations, addition of EGTA led to a significant accumulation of cyclic AMP. Evidence that steroidogenesis is regulated by a cyclic-AMP-dependent mechanism at low K+ levels is presented, and we also report the first direct evidence of activation of aldosterone synthesis by protein kinase C at high K+ concentration.

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cAMP和蛋白激酶C参与钾对醛固酮生物合成的调节。
探讨了钾离子(K+)对豚鼠肾上腺皮质醛固酮生成的影响机制。在高K+浓度(约8 mM)的培养培养基中,醛固酮的输出和含量升高,细胞内蛋白的磷酸化和蛋白激酶C的活性显著增加。循环AMP水平的增加不太显著。EGTA和镧离子(La3+)以及氯丙嗪对蛋白质磷酸化的影响似乎可以消除K+浓度升高对甾体生成和蛋白质磷酸化的影响。在低K+浓度下,EGTA的加入导致环AMP的显著积累。有证据表明,在低K+水平下,类固醇生成受环AMP依赖机制的调节,我们还报告了高K+浓度下蛋白激酶C激活醛固酮合成的第一个直接证据。
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