Decomposition of hydroperoxides derived from microsomes or lipoprotein by glutathione peroxidase and glutathione S-transferase.
Protective effects of glutathione peroxidase, glutathione S-transferase purified from human liver and superoxide dismutase against lipid peroxidation were investigated. In the presence of glutathione, lipid hydroperoxides found in microsomal membrane were decomposed by glutathione peroxidase and cationic glutathione S-transferase, but anionic glutathione S-transferase had no effect on them. Superoxide dismutase exhibited antioxidation effect by preventing accumulation of lipid hydroperoxides. Serum lipid hydroperoxides existing in low density lipoprotein fraction were also decomposed by glutathione peroxidase and cationic glutathione S-transferase. These findings suggest that the hydroperoxide level, which has high toxicity, could be controlled by these glutathione-dependent glutathione peroxidase and cationic glutathione S-transferase.
D000818:Animals; D005979:Glutathione Peroxidase / Q000494:pharmacology*; D005982:Glutathione Transferase / Q000494:pharmacology*; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D008054:Lipid Peroxides / Q000378:metabolism*; D008074:Lipoproteins / Q000378:metabolism*; D008862:Microsomes, Liver / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D013482:Superoxide Dismutase / Q000494:pharmacology
D008054:Lipid Peroxides; D008074:Lipoproteins; D005979:Glutathione Peroxidase; D013482:Superoxide Dismutase; D005982:Glutathione Transferase