Effect of human glutathione S-transferases on glutathione-dependent inactivation of cytochrome P450-dependent reactive intermediates of diclofenac.

@article{Dragovic2013EffectOH,
  title={Effect of human glutathione S-transferases on glutathione-dependent inactivation of cytochrome P450-dependent reactive intermediates of diclofenac.},
  author={Sanja Dragovic and Jan Simon Boerma and Nico P E Vermeulen and Jan N. M. Commandeur},
  journal={Chemical research in toxicology},
  year={2013},
  volume={26 11},
  pages={1632-41}
}
Idiosyncratic adverse drug reactions due to the anti-inflammatory drug diclofenac have been proposed to be caused by the generation of reactive acyl glucuronides and oxidative metabolites. For the oxidative metabolism of diclofenac by cytochromes P450 at least five different reactive intermediates have been proposed previously based on structural identification of their corresponding GSH-conjugates. In the present study, the ability of four human glutathione S-transferases (hGSTs) to catalyze… CONTINUE READING

References

Publications referenced by this paper.
Showing 1-10 of 56 references

Human precision-cut liver

T M., G.M.M. Groothuis
2013

Regio - and stereoselective hydroxylation of optically active α - ionone enantiomers by engineered cytochrome P 450 BM 3 mutants

H. Venkataraman, S. B. A. Beer, D. P. Geerke, N. P. E. Vermeulen, J. N. M. Commandeur
Adv . Synth . Catal . • 2012

Role of intestinal cytochrome P 450 enzymes in diclofenac - induced toxicity in the small intestine

Q. Y. Zhang
J . Pharmacol . Exp . Ther . • 2012

Application of a fluorescence-based

J.N.M. Commandeur
2011

Similar Papers

Loading similar papers…