| First Author | Imamura Y | Year | 2007 |
| Journal | J Steroid Biochem Mol Biol | Volume | 107 |
| Issue | 1-2 | Pages | 120-6 |
| PubMed ID | 17629694 | Mgi Jnum | J:126960 |
| Mgi Id | MGI:3762429 | Doi | 10.1016/j.jsbmb.2007.02.010 |
| Citation | Imamura Y, et al. (2007) Several distinct enzymes catalyze 20alpha-hydroxysteroid dehydrogenase activity in mouse liver and kidney. J Steroid Biochem Mol Biol 107(1-2):120-6 |
| abstractText | The effects of flavonoids and quinones on NADPH- and NADH-dependent 20alpha-hydroxysteroid dehydrogenase (20alpha-HSD) activities were examined in cytosolic fractions from the liver and kidney of mice. Judging from the data for the inhibition of NADPH- and NADH-dependent 20alpha-HSD activities by flavonoids and quinones, enzyme catalyzing renal NADPH-dependent 20alpha-HSD activity was found to be distinct from enzyme(s) catalyzing hepatic NADPH- and NADH-dependent 20alpha-HSD activities. Sulfobromophthalein (SBP) had little ability to inhibit hepatic NADPH-dependent 20alpha-HSD activity and bromophenol blue (BPB) exhibited a weak activation against the enzyme activity, whereas SBP and BPB were potent and moderate inhibitors, respectively, of hepatic NADH-dependent 20alpha-HSD activity. Thus, enzyme catalyzing hepatic NADPH-dependent 20alpha-HSD activity appeared to be distinct from enzyme catalyzing hepatic NADH-dependent 20alpha-HSD activity. The data for the pH profiles of hepatic NADPH- and NADH-dependent 20alpha-HSD activities also led us to the conclusion. Based on these results, we propose the possibility that several distinct enzymes catalyze NADPH- and NADH-dependent 20alpha-HSD activities in cytosolic fractions from the liver and kidney of mice. |
