Depression of alcohol dehydrogenase activity in rat hepatocyte culture by dihydrotestosterone.

Journal Article (Journal Article)

Hepatocytes harvested from castrated rats retained a higher alcohol dehydrogenase (EC activity than hepatocytes harvested from normal rats during 7 days of culture. Dihydrotestosterone (1 microM) decreased the enzyme activity, after 2 and 5 days of culture, in hepatocytes from castrated and control animals respectively. Dihydrotestosterone decreased the enzyme activity to similar values in both groups of hepatocytes by the end of 7 days of culture. Testosterone (1 microM) had no effect on the enzyme activity in normal hepatocytes and only a transitory effect in decreasing the enzyme activity in hepatocytes from castrated animals. The increases in alcohol dehydrogenase activity after castration and their suppression by dihydrotestosterone were associated with parallel changes in the rate of ethanol elimination. Additions of substrates of the malate-aspartate shuttle or dinitrophenol did not modify ethanol elimination. These observations indicate that dihydrotestosterone has a direct suppressant effect on hepatocyte alcohol dehydrogenase and that the enzyme activity is a major determinant of the rate of ethanol elimination.

Full Text

Duke Authors

Cited Authors

  • Mezey, E; Potter, JJ; Diehl, AM

Published Date

  • January 15, 1986

Published In

Volume / Issue

  • 35 / 2

Start / End Page

  • 335 - 339

PubMed ID

  • 2935156

International Standard Serial Number (ISSN)

  • 0006-2952

Digital Object Identifier (DOI)

  • 10.1016/0006-2952(86)90535-6


  • eng

Conference Location

  • England