title: An NADPH-dependent reductase in neonatal pig testes that metabolizes androgens and xenobiotics.
abstract: We have isolated an NADPH-dependent reductase from neonatal pig testes that metabolizes androgens and a variety of xenobiotics. This enzyme is distinct from 3alpha/beta,20beta-hydroxysteroid dehydrogenase or its homologue, carbonyl reductase, as judged by its immunological and molecular properties and its much narrower specificity for steroids. This reductase and 3alpha/beta,20beta-hydroxysteroid dehydrogenase may be part of a mechanism for regulating androgen levels the neonatal pig testes. Interestingly, we could not find multiple isoforms of 3alpha/beta,20beta-hydroxysteroid dehydrogenase/carbonyl reductase in pig testes unlike human and rat testes and other organs in which multiple isoforms are expressed.
authors.affiliation: Department of Biochemistry, Faculty of Pharmaceutical Sciences, Hoshi University, Tokyo, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Nakajin
authors.forename: N
authors.initials: N
authors.lastname: Minamikawa
authors.forename: M E
authors.initials: ME
authors.lastname: Baker
authors.forename: S
authors.initials: S
authors.lastname: Toyoshima
mesh_terms: D000728:Androgens / Q000378:metabolism*; D000818:Animals; D001462:Barbital / Q000494:pharmacology; D015153:Blotting, Western; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006913:Hydroxysteroid Dehydrogenases / Q000276:immunology / Q000378:metabolism; D066298:In Vitro Techniques; D008297:Male; D009247:NADH, NADPH Oxidoreductases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity; D013552:Swine; D013737:Testis / Q000201:enzymology / Q000378:metabolism*; D015262:Xenobiotics / Q000378:metabolism*
chemical_list: D000728:Androgens; D004791:Enzyme Inhibitors; D015262:Xenobiotics; D001462:Barbital; D006913:Hydroxysteroid Dehydrogenases; D009247:NADH, NADPH Oxidoreductases