Identification of the Oxidative 3α-Hydroxysteroid Dehydrogenase Activity of Rat Leydig Cells as Type II Retinol Dehydrogenase.

Dihydrotestosterone (DHT) is the most potent naturally occurring androgen, and its production in the testis may have important consequences in developmental and reproductive processes. In the rat testis, three factors can contribute to intracellular DHT levels: 1) synthesis of DHT from T by 5α-reductase, 2) conversion of DHT to 5α-androstane-3α,17β-diol (3α-DIOL) by the reductive activity of 3α-hydroxysteroid dehydrogenase (3α-HSD), and 3) conversion of 3α-DIOL by an oxidative 3α-HSD activity. While the type I 3α-HSD enzyme (3α-HSD1 or AKR1C9) is an oxidoreductase in vitro and could theoretically be responsible for factors 2 and 3, we have shown previously that rat Leydig cells have two 3α-HSD activities: a cytosolic NADP(H)- dependent activity, characteristic of 3α-HSD1, and a microsomal NAD(H)-dependent activity. The two activities were separable by both developmental and biochemical criteria, but the identity of the second enzyme was unknown. To identify the microsomal NAD(H)-dependent 3α-HSD in rat Le...

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