Abstract
Adenosine 3',5'-monophosphate (3',5'-AMP) inhibited the conversion of pregnenolone to progesterone and of dehydroepiandrosterone to Δ4-androstenedione in vitro system. Under similar conditions N6-2-O-dibutyryl-adenosine 3',5'-monophosphate (dibutyryl 3', 5'-AMP) had no effect on the enzymic reaction. The inhibition of Δ5-3 β-hydroxysteroid dehydrogenase by 3', 5'-AMP was released by increasing the concentrations of exogenous NAD+. 3', 5'-AMP and dibutyryl 3', 5'-AMP given subcutaneously 2 mg/female immature mouse twice daily for five days, had no effect on the ovarian conversion of pregnenolone to progesterone, whereas the synthesis of Δ4-androstenedione from dehydroepiandrosterone was inhibited by 3', 5'-AMP and to a lesser extent by dibutyryl 3', 5'-AMP. Human chorionic gonadotropin (HCG) administered in vivo stimulated the mouse ovarian Δ-3β-hydroxysteroid dehydrogenase. The physiological significance of the inhibition by the 3', 5'-AMP of the NAD+ dependent steroid dehydrogenase is discussed. 1 This work was supported by Ford Foundation Grant No. 67-470.

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