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Volume 271, Number 42, Issue of October 18, 1996 pp. 25971-25975
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Calcium Stimulates Intramitochondrial Cholesterol Transfer in Bovine Adrenal Glomerulosa Cells

(Received for publication, April 8, 1996, and in revised form, July 7, 1996)

From the Division of Endocrinology and Diabetology, Department of Medicine, Faculty of Medicine, CH-1211 Geneva, 14 Switzerland

In adrenal glomerulosa cells, angiotensin II (Ang II) stimulates aldosterone synthesis through rises of cytosolic calcium ([Ca²⁺]_c). The rate-limiting step in this process is the transfer of cholesterol to the inner mitochondrial membrane, where it is converted to pregnenolone by the P450 side chain cleavage enzyme. The aim of the present study was to examine the effect of changes in [Ca²⁺]_c and of Ang II on intramitochondrial cholesterol distribution. Freshly prepared bovine zona glomerulosa cells were submitted to a cytosolic Ca²⁺ clamp (600 nM) or stimulated with Ang II (10 nM). Mitochondria were isolated and subfractionated into outer membranes (OM), inner membranes (IM), and contact sites (CS). Cholesterol content was determined by the cholesterol oxidase assay. Stimulation of intact cells with Ca²⁺ led to a marked decrease in cholesterol content of OM (to 54 ± 24% of controls, n = 5) and to a concomitant increase of cholesterol in CS and IM (to 145 ± 14%, n = 5). When glomerulosa cells were exposed to Ang II, a marked increase of cholesterol in CS occurred (to 172 ± 16% of controls, n = 5). No significant changes were detected in OM cholesterol, suggesting a stimulation of cholesterol supply to the mitochondria in response to Ang II. Cycloheximide specifically and significantly reduced Ca²⁺-activated cholesterol transfer to CS and IM. In conclusion, our data indicate that one of the main functions of the Ca²⁺ messenger is to increase cholesterol supply to the P450 side chain cleavage enzyme by enhancing endogenous intermembrane cholesterol transfer to a mitochondrial site containing the enzymes responsible for the initial steps of the steroidogenic cascade.

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