Involvement of porcine and human carbonyl reductases in the metabolism of epiandrosterone, 11-oxygenated steroids, neurosteroids, and corticosteroids

J Steroid Biochem Mol Biol. 2024 Oct:243:106574. doi: 10.1016/j.jsbmb.2024.106574. Epub 2024 Jun 28.

Abstract

Porcine carbonyl reductases (pCBR1 and pCBR-N1) and aldo-keto reductases (pAKR1C1 and pAKR1C4) exhibit hydroxysteroid dehydrogenase (HSD) activity. However, their roles in the metabolism of porcine-specific androgens (19-nortestosterone and epiandrosterone), 11-oxygenated androgens, neurosteroids, and corticosteroids remain unclear. Here, we compared the steroid specificity of the four recombinant enzymes by kinetic and product analyses. In C18/C19-steroids,11-keto- and 11β-hydroxy-5α-androstane-3,17-diones were reduced by all the enzymes, whereas 5α-dihydronandrolone (19-nortestosterone metabolite) and 11-ketodihydrotestosterone were reduced by pCBR1, pCBR-N1, and pAKR1C1, of which pCBR1 exhibited the lowest (submicromolar) Km values. Product analysis showed that pCBR1 and pCBR-N1 function as 3α/β-HSDs, in contrast to pAKR1C1 and pAKR1C4 (acting as 3β-HSD and 3α-HSD, respectively). Additionally, 17β-HSD activity was observed in pCBR1 and pCBR-N1 (toward epiandrosterone and its 11-oxygenated derivatives) and in pAKR1C1 (toward androsterone, 4-androstene-3,17-dione and their 11-oxygenated derivatives). The four enzymes also showed different substrate specificity for 3-keto-5α/β-dihydro-C21-steroids, including GABAergic neurosteroid precursors and corticosteroid metabolites. 5β-Dihydroprogesterone was reduced by all the enzymes, whereas 5α-dihydroprogesterone was reduced only by pCBR1, and 5α/β-dihydrodeoxycorticosterones by pCBR1 and pCBR-N1. The two pCBRs also reduced the 5α/β-dihydro-metabolites of cortisol, 11-deoxycortisol, cortisone, and corticosterone. pCBR1 exhibited lower Km values (0.3-2.9 μM) for the 3-keto-C21-steroids than pCBR-N1 (Km=10-36 μM). The reduced products of the 3-keto-C21-steroids by pCBR1 and pCBR-N1 were their 3α-hydroxy-metabolites. Finally, we found that human CBR1 has similar substrate specificity for the C18/C19/C21-steroids to pCBR-N1. Based on these results, it was concluded that porcine and human CBRs can be involved in the metabolism of the aforementioned steroids as 3α/β,17β-HSDs.

Keywords: 11-Oxygenated androgen; Carbonyl reductase; Corticosteroid; Epiandrosterone; Neurosteroid.

MeSH terms

  • Adrenal Cortex Hormones / chemistry
  • Adrenal Cortex Hormones / metabolism
  • Alcohol Oxidoreductases / chemistry
  • Alcohol Oxidoreductases / genetics
  • Alcohol Oxidoreductases / metabolism
  • Aldo-Keto Reductases / chemistry
  • Aldo-Keto Reductases / genetics
  • Aldo-Keto Reductases / metabolism
  • Androsterone* / analogs & derivatives
  • Androsterone* / chemistry
  • Androsterone* / metabolism
  • Animals
  • Carbonyl Reductase (NADPH) / chemistry
  • Carbonyl Reductase (NADPH) / metabolism
  • Humans
  • Kinetics
  • Neurosteroids / chemistry
  • Neurosteroids / metabolism
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Steroids / chemistry
  • Steroids / metabolism
  • Substrate Specificity
  • Swine

Substances

  • Androsterone
  • Adrenal Cortex Hormones
  • Neurosteroids
  • Steroids
  • Recombinant Proteins
  • Aldo-Keto Reductases
  • Alcohol Oxidoreductases
  • Carbonyl Reductase (NADPH)