Glutathione peroxidase, superoxide dismutase, and glutathione S-transferase activities in human lung.
Glutathione peroxidase (GSH-Px), superoxide dismutase (SOD), and glutathione S-transferase activities were measured in lung tissue obtained from 7 patients receiving resectional surgery because of localized lung tumors. Human-lung-soluble fractions were also fractionated on Sephadex G-150-S columns, and GSH-Px activity was measured using hydrogen peroxide and cumene hydroperoxide as substrates to investigate the presence of non-selenium-dependent GSH-Px activity. The amount of SOD activity was found to be similar to the amount of activity present in rat lung. Glutathione S-transferase activity was 3 times greater in human lung than that in rat lung. Selenium-dependent GSH-Px activity was much lower in human lung than that in rat lung (less than 30%), and no evidence of non-selenium-dependent glutathione peroxidase activity was found in human lung using gel filtration techniques. We conclude that human lung differs from rat lung in some antioxidant enzymatic defense mechanisms, and that selenium deficiency could result in marked decreases in the ability of human lung to detoxify organic hydroperoxides.
D000818:Animals; D002850:Chromatography, Gel; D005979:Glutathione Peroxidase / Q000378:metabolism*; D005982:Glutathione Transferase / Q000378:metabolism*; D006801:Humans; D008168:Lung / Q000201:enzymology*; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D013482:Superoxide Dismutase / Q000378:metabolism*
D005979:Glutathione Peroxidase; D013482:Superoxide Dismutase; D005982:Glutathione Transferase