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Regulation of Aldosterone Synthase Cytochrome P-450 in Rat Adrenals by Angiotensin II and Potassium^*

Departments of Biochemistry (T.O., F.M., Y.I.) and Internal Medicine (H.Sh., H.Su., M.M., T.S.), School of Medicine, Keio University Shinjuku-ku, Tokyo 160, Japan

Address all correspondence and requests for reprints to: Dr. Yuzuru Ishimura, Department of Biochemistry, School of Medicine, Keio University, Shinjuku-ku, Tokyo 160, Japan.

Abstract

Changes in the levels of aldosterone synthase cytochrome P-450, a recently identified enzyme in rat adrenals, were studied in response to the renin-angiotensin system and K stimuli. As examined by an immunoblot technique, the zona glomerulosa mitochondria from rats fed on a low Na-normal K diet (8.6 mmol Na⁺ and 207 mmol K⁺/kg of diet) or a low Nahigh K (0.2 M KC1 in drinking water) diet for 4–10 days contained significantly higher amounts of aldosterone synthase cytochrome P-450 than those from rats fed on a normal diet (86 mmol Na⁺ and 207 mmol K⁺/kg of diet). Activities of the enzyme were also found to increase by about 10-fold on day 10. In concert with these changes, both plasma renin activity and plasma aldosterone concentration increased, indicating that the renin-angiotensin system was activated in these rats. Feeding with a normal Na-high K diet also induced significantly higher levels of both amount and activity of aldosterone synthase cytochrome P-450 together with an elevated serum K concentration on day 4, though they all decreased to near the control level on the following days. On the other hand, when enalapril malate, an angiotensin I-converting enzyme inhibitor, was administered to the low Na-normal K rats, the increases in the amount and activity of the enzyme as well as in plasma aldosterone concentration were suppressed altogether. However, the enalapril administration to the low Na-high K rats suppressed the increases only partially. These results indicate that the aldosterone synthase cytochrome P-450 is an ultimate target of the regulation of aldosterone biosynthesis by angiotensin II and K. (Endocrinology 128: 2534–2539, 1991)

Footnotes

^* This work was supported in part by a Grant-in-Aid for Scientific Research on Priority Areas from the Ministry of Education, Science, and Culture of Japan (to Y.I.), and by a Grant-in-Aid for Disorders of Adrenal Hormones from the Ministry of Health and Welfare of Japan (to T.S.).

Received November 19, 1990.

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