Indomethacin inhibition of glutathione S-transferases.
Indomethacin inhibited rat liver glutathione S-transferases (EC 2.5.1.18). Its inhibition was non-competitive with respect to 3,4-dichloronitrobenzene with an apparent Ki of 5.3 X 10(-5) M and uncompetitive with respect to glutathione with an apparent Ki of 4.0 X 10(-5) M. 4-Chlorobenzoic acid and 5-methoxy-2-methylindole-3-acetic acid, two metabolites of indomethacin, were weak inhibitors of the enzymes. On the other hand, meclofenamic acid was a competitive inhibitor of the enzymes with an apparent Ki of 3.0 X 10(-4) M. Possible significance of these findings in arachidonic acid metabolism is discussed.
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D005982:Glutathione Transferase / Q000037:antagonists & inhibitors*; D066298:In Vitro Techniques; D007213:Indomethacin / Q000494:pharmacology*; D008099:Liver / Q000201:enzymology*; D008297:Male; D051381:Rats
D005982:Glutathione Transferase; D007213:Indomethacin