Kurscheid-Reich D, Hegemann L, Wohlfeil S
Yale University, School of Medicine, Dept. Internal Medicine, New Haven, CT 06510-8056.
Life Sci. 1992;51(14):1157-63. doi: 10.1016/0024-3205(92)90518-t.
In order to obtain further evidence for the involvement of protein kinases in the short-term ACTH-stimulated aldosterone synthesis in rat zona glomerulosa cells, the effects of three different compounds with protein kinase inhibitory properties were investigated. Staurosporine, H-7 and trifluoperazine inhibited ACTH-stimulated aldosterone release in a dose-dependent manner. While the inhibitory effect of H-7 was reversible upon washing of the cells with inhibitor-free medium, the inhibition was maintained in cells treated with staurosporine or trifluoperazine. In contrast to the stimulated production, basal release of aldosterone even at the highest drug concentrations tested was not completely inhibited. We thus conclude that protein kinases may play a crucial role in short-term ACTH-stimulated aldosterone production in rat glomerulosa cells.
为了获得蛋白激酶参与大鼠肾小球旁细胞短期促肾上腺皮质激素(ACTH)刺激的醛固酮合成的进一步证据,研究了三种具有蛋白激酶抑制特性的不同化合物的作用。星形孢菌素、H-7和三氟拉嗪以剂量依赖的方式抑制ACTH刺激的醛固酮释放。虽然用不含抑制剂的培养基洗涤细胞后,H-7的抑制作用是可逆的,但在用星形孢菌素或三氟拉嗪处理的细胞中,抑制作用得以维持。与刺激产生的情况相反,即使在测试的最高药物浓度下,醛固酮的基础释放也没有被完全抑制。因此,我们得出结论,蛋白激酶可能在大鼠肾小球旁细胞短期ACTH刺激的醛固酮产生中起关键作用。