Inhibition of purified rat liver glutathione S-transferase isozymes by diuretic drugs

Biochem Pharmacol. 1985 Jun 15;34(12):2157-61. doi: 10.1016/0006-2952(85)90411-3.


Seven soluble rat liver glutathione S-transferase isozymes were isolated and the inhibition of these isozymes by selected diuretics was investigated using 1-chloro-2,4-dinitrobenzene as substrate. All isozymes were inhibited to some extent under the experimental conditions used, but there was significant isozyme dependent selectivity of inhibition. The greatest inhibitory effect (over 80%) was found when the phenoxyacetic acid diuretics and indacrynic acid were incubated with glutathione S-transferase 3-3, 3-4 and 4-4. The sulphamoylbenzoic acid diuretics, furosemide and bumetanide, were found to have a lesser effect on the isozymes studies. As glutathione S-transferase are thought to play an important protective role in the various tissues of animals and man, by catalysing the glutathione conjugation of electrophilic drugs and drug metabolites, their inhibition may be toxicologically important.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Diuretics / metabolism
  • Diuretics / toxicity*
  • Glutathione Transferase / antagonists & inhibitors*
  • Isoenzymes / antagonists & inhibitors*
  • Liver / drug effects
  • Liver / enzymology*
  • Male
  • Rats
  • Rats, Inbred Strains


  • Diuretics
  • Isoenzymes
  • Glutathione Transferase