Abstract
Retinol dehydrogenase-4 (RoDH-4) converts retinol and 13- cis-retinol to corresponding aldehydes in human liver and skin in the presence of NAD +. RoDH-4 also converts 3α-androstanediol and androsterone into dihydrotestosterone and androstanedione, which may stimulate sebum secretion. This oxidative 3α-hydroxysteroid dehydrogenase (3α-HSD) activity of RoDH-4 is competitively inhibited by retinol and 13- cis-retinol. Here, we further examine the substrate specificity of RoDH-4 and the inhibition of its 3α-HSD activity by retinoids. Recombinant RoDH-4 oxidized 3,4-didehydroretinol—a major form of vitamin A in the skin—to its corresponding aldehyde. 13- cis-retinoic acid (isotretinoin), 3,4-didehydroretinoic acid, and 3,4-didehydroretinol, but not all- trans-retinoic acid or the synthetic retinoids acitretin and adapalene, were potent competitive inhibitors of the oxidative 3α-HSD activity of RoDH-4, i.e., reduced the formation of dihydrotestosterone and androstandione in vitro. Extrapolated to the in vivo situation, this effect might explain the unique sebosuppressive effect of isotretinoin when treating acne.
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