Ohnishi T, Wada A, Lauber M, Yamano T, Okamoto M
Department of Biochemistry, Osaka University Medical School, Japan.
J Steroid Biochem. 1988 Jul;31(1):73-81. doi: 10.1016/0022-4731(88)90208-7.
An assumption that the aldosterone-synthesizing enzyme exists only in zona glomerulosa cells apparently contradicts our recent findings that a purified bovine adrenocortical cytochrome P-45011 beta catalyzes the aldosterone formation and the enzyme exists in both zones of the adrenal cortex. To gain more insight into the zone specificity of aldosterone production, the aldosterone-synthesizing activity of mitochondria prepared from the isolated zones of adrenal cortex of various animal species was investigated. The intact mitochondria from the bovine or porcine zonae fasciculata-reticularis could not produce aldosterone whereas those from the zona glomerulosa produced it at a significant rate. When the mitochondria from the zonae fasciculata-reticularis were solubilized by the addition of cholate, they produced aldosterone from corticosterone at a rate comparable to that of those from the zona glomerulosa. The presence of specific factor(s) in the zonae fasciculata-reticularis mitochondria inhibiting expression of the aldosterone synthetic activity is discussed. The mitochondria of the rat zonae fasciculata-reticularis could hardly catalyze aldosterone synthesis under the detergent-solubilized conditions, whereas those of the zona glomerulosa could. Immunoblot analysis revealed that the mitochondria of the zonae fasciculata-reticularis contained a protein of Mr 51,000 which was immunocrossreactive with a monoclonal antibody directed against P-45011 beta, whereas those of the zona glomerulosa contained two immunocrossreactive proteins of Mr 51,000 and 49,000. These results suggest that in the case of rat adrenal cortex, a specific aldosterone-synthesizing enzyme exists in the zona glomerulosa.
醛固酮合成酶仅存在于球状带细胞中的假设显然与我们最近的发现相矛盾,即纯化的牛肾上腺皮质细胞色素P - 45011β催化醛固酮的形成,且该酶存在于肾上腺皮质的两个区域。为了更深入了解醛固酮产生的区域特异性,研究了从各种动物物种分离的肾上腺皮质区域制备的线粒体的醛固酮合成活性。来自牛或猪束状带 - 网状带的完整线粒体不能产生醛固酮,而来自球状带的线粒体则能以显著速率产生醛固酮。当通过添加胆酸盐使束状带 - 网状带的线粒体溶解时,它们从皮质酮产生醛固酮的速率与球状带的线粒体相当。讨论了束状带 - 网状带线粒体中存在抑制醛固酮合成活性表达的特定因子。在去污剂溶解条件下,大鼠束状带 - 网状带的线粒体几乎不能催化醛固酮合成,而球状带的线粒体则可以。免疫印迹分析显示,束状带 - 网状带的线粒体含有一种分子量为51,000的蛋白质,它与针对P - 45011β的单克隆抗体发生免疫交叉反应,而球状带的线粒体含有两种分子量分别为51,000和49,000的免疫交叉反应蛋白。这些结果表明,在大鼠肾上腺皮质中,球状带存在一种特异性的醛固酮合成酶。