Inhibition of mammalian hepatic glutathione S-transferases by acetylenic fatty acids.
Micromolar concentrations of 2 classical inhibitors of lipoxygenase, 5,8,11-eicosatriynoic acid (ETI) and 5,8,11,14-eicosatetraynoic acid (ETYA), were found to cause a significant inhibition of the mixture of isozymes of affinity purified rat and human liver glutathione S-transferase (GST) with activity towards 1-chloro-2,4-dinitrobenzene (CDNB). ETI was a more potent inhibitor of both rat and human liver GST than ETYA. Analysis of kinetic data suggested noncompetitive inhibition of human liver GST by ETI towards reduced glutathione and CDNB. ETI also inhibited the hepatic GST activity towards 1,2-dichloro-4-nitrobenzene, p-nitrobenzyl chloride and 4-nitropyridine N-oxide.
Datta
K
K
Florida Toxicology Research Center, College of Public Health, University of South Florida, Tampa 33612.
Kulkarni
A P
AP
D015117:5,8,11,14-Eicosatetraynoic Acid / Q000494:pharmacology*; D000818:Animals; D005231:Fatty Acids, Unsaturated / Q000494:pharmacology*; D005260:Female; D005982:Glutathione Transferase / Q000037:antagonists & inhibitors*; D006801:Humans; D066298:In Vitro Techniques; D008099:Liver / Q000201:enzymology*; D051381:Rats
D005231:Fatty Acids, Unsaturated; D015117:5,8,11,14-Eicosatetraynoic Acid; C026603:5,8,11-eicosatriynoic acid; D005982:Glutathione Transferase