13-Hydroperoxylinoleic acid inhibits rat liver glyoxalase II.
13-Hydroperoxylinoleic acid (13-HPLA) inhibited glyoxalase II in rat liver supernatants with half the maximum inhibition occurring at a 13-HPLA concentration below 0.1 microgram/ml. The extent of inhibition was increased by EDTA and decreased by Mn2+ and Co2+. Zn2+ and Cu2+ inhibited control enzyme activity. Glyoxalase II catalyzes the destruction of S-lactoylglutathione. Both 13-HPLA and S-lactoylglutathione have been shown to potentiate histamine secretion. It is suggested that 13-HPLA does so, in part at least, by inhibiting glyoxalase II and thereby causing a concomitant increase in S-lactoylglutathione level. It is also possible that S-lactoylglutathione mediates other of the effects of 13-HPLA and fatty acid hydroperoxides in general.
D000818:Animals; D005227:Fatty Acids / Q000494:pharmacology; D066298:In Vitro Techniques; D007791:Lactoylglutathione Lyase / Q000037:antagonists & inhibitors; D008041:Linoleic Acids / Q000494:pharmacology*; D008099:Liver / Q000201:enzymology; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D013869:Thiolester Hydrolases / Q000037:antagonists & inhibitors*; D013997:Time Factors; D000099301:Hydroxyacylglutathione Hydrolase
D005227:Fatty Acids; D007791:Lactoylglutathione Lyase; D008041:Linoleic Acids; D013869:Thiolester Hydrolases; D000099301:Hydroxyacylglutathione Hydrolase; C032890:13-hydroperoxylinoleic acid