Superoxide dependent lipid peroxidation.
Rat liver microsomal NADPH-dependent lipid peroxidation and xanthine oxidase-promoted lipid peroxidation were reviewed and compared to see if a unified mechanism is involved in each system. These systems were also compared to hydroxyl radical-dependent lipid peroxidation in order to determine the physiological significance of the different mechanisms of lipid peroxidation. Fenton's reagent very readily promotes lipid peroxidation, which is inhibited by catalase and hydroxyl radical traps but not by superoxide dismutase. However, the addition of ADP to Fenton's reagent results in a type of lipid peroxidation that is not inhibited by hydroxyl radical traps and the amount of hydroxyl radical spin trap adducts formed is much less. Xanthine oxidase-promoted lipid peroxidation is not inhibited by catalase and is greatly stimulated by ADP. Microsomal NADPH-dependent lipid peroxidation is also dramatically stimulated by ADP in Tris buffer but not in phosphate buffer. Hydroxyl radical traps are without effect in both microsomes and xanthine oxidase-promoted lipid peroxidation. These results suggest several in vitro mechanisms for the initiation of lipid peroxidation but do not support the hydroxyl radical for a role in physiological lipid peroxidation.
D000818:Animals; D005231:Fatty Acids, Unsaturated; D007501:Iron / Q000378:metabolism; D008054:Lipid Peroxides / Q000378:metabolism*; D008862:Microsomes, Liver / Q000378:metabolism*; D009249:NADP / Q000378:metabolism; D051381:Rats; D013481:Superoxides; D014969:Xanthine Oxidase / Q000378:metabolism*
D005231:Fatty Acids, Unsaturated; D008054:Lipid Peroxides; D013481:Superoxides; D009249:NADP; D007501:Iron; D014969:Xanthine Oxidase