An NADPH-dependent reductase in neonatal pig testes that metabolizes androgens and xenobiotics

Biol Pharm Bull. 1998 Dec;21(12):1356-60. doi: 10.1248/bpb.21.1356.

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.

MeSH terms

  • Androgens / metabolism*
  • Animals
  • Barbital / pharmacology
  • Blotting, Western
  • Enzyme Inhibitors / pharmacology
  • Hydroxysteroid Dehydrogenases / immunology
  • Hydroxysteroid Dehydrogenases / metabolism
  • In Vitro Techniques
  • Male
  • NADH, NADPH Oxidoreductases / antagonists & inhibitors
  • NADH, NADPH Oxidoreductases / isolation & purification
  • NADH, NADPH Oxidoreductases / metabolism*
  • Substrate Specificity
  • Swine
  • Testis / enzymology
  • Testis / metabolism*
  • Xenobiotics / metabolism*

Substances

  • Androgens
  • Enzyme Inhibitors
  • Xenobiotics
  • Barbital
  • Hydroxysteroid Dehydrogenases
  • NADH, NADPH Oxidoreductases