Leukotriene B4, C4, D4 and E4 inactivation by hydroxyl radicals.
Leukotriene B4 chemotactic activity and leukotriene C4, D4 and E4 slow reacting substance activity were rapidly decreased by hydroxyl radicals generated by two different iron-supplemented acetaldehyde-xanthine oxidase systems. At low Fe2+, leukotriene inactivation was inhibited by catalase, superoxide dismutase, mannitol and ethanol, suggesting involvement of hydroxyl radicals generated by the iron-catalyzed interaction of superoxide and H2O2 (Haber-Weiss reaction). Leukotriene inactivation increased at high Fe2+ concentrations, but was no longer inhibitable by superoxide dismutase, suggesting that inactivation resulted from a direct interaction between H2O2 and Fe2+ to form hydroxyl radicals (Fenton reaction). The inactivation of leukotrienes by hydroxyl radicals suggests that oxygen metabolites generated by phagocytes may play a role in modulating leukotriene activity.
D000818:Animals; D002417:Cattle; D005260:Female; D005609:Free Radicals; D006878:Hydroxides / Q000378:metabolism*; D017665:Hydroxyl Radical; D007700:Kinetics; D007975:Leukotriene B4 / Q000378:metabolism*; D017999:Leukotriene E4; D008892:Milk / Q000201:enzymology; D013189:SRS-A / Q000031:analogs & derivatives* / Q000378:metabolism*; D013329:Structure-Activity Relationship; D014969:Xanthine Oxidase / Q000378:metabolism
D005609:Free Radicals; D006878:Hydroxides; D013189:SRS-A; D007975:Leukotriene B4; D017665:Hydroxyl Radical; D017999:Leukotriene E4; D014969:Xanthine Oxidase