cosyntropin and malic-acid

Rat adrenal mitochondria have an active rotenone-insensitive outer mitochondrial membrane NADH-semidehydroascorbate (NADH-SDA) reductase which supports cholesterol side chain cleavage at a rate equal to that supported by malate. Side chain cleavage activity supported by both of these electron donor systems is equally inhibited by cycloheximide. Catalase or butylated hydroxyanisole are required for the NADH-SDA reductase-supported cholesterol side chain cleavage. This requirement can be removed by briefly subjecting the mitochondrial preparations to -20 degrees C. Ascorbic acid alone or with malate is either inhibitory or has no effect on side chain cleavage activity. These observations demonstrate that outer mitochondrial membrane NADH-SDA reductase in rat adrenal functions to provide cytoplasmic reducing equivalents to intramitochondrial cytochrome P-450scc and provides a new explanation for the function of ascorbic acid in corticosteroidogenesis.

Topics: Adrenal Glands; Animals; Ascorbic Acid; Butylated Hydroxyanisole; Catalase; Cholesterol; Cold Temperature; Cosyntropin; Cycloheximide; Female; Malates; Mitochondria; NADH, NADPH Oxidoreductases; Pregnenolone; Rats; Rats, Inbred Strains