GSH‐dependent inhibition of lipid peroxidation: Properties of a potent cytosolic system which protects cell membranes

• Published in: Lipids Vol. 20; no. 10; pp. 704 - 711
• Main Authors: Gibson, Donald D., Hawrylko, Josephine, McCay, Paul B.
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer‐Verlag 01.10.1985; Springer
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Cell Membrane - drug effects; Cell Membrane - metabolism; Cysteine - pharmacology; Cytosol - metabolism; Dithiothreitol - pharmacology; Fundamental and applied biological sciences. Psychology; Glutathione - pharmacology; Iodoacetates - pharmacology; Iodoacetic Acid; Kinetics; Lipid Peroxides - metabolism; Lipids; Liver - drug effects; Liver - metabolism; Male; Mercaptoethanol - pharmacology; Other biological molecules; Oxygen Consumption - drug effects; Rats; Rats, Inbred Strains; Purification; Rat; Enzyme; Rodentia; Lipids; Cofactor; Cytosol; Vertebrata; Mammalia; Inhibitor; Inhibition; Face; Glutathione; Peroxidation
• ISSN: 0024-4201; 1558-9307
• DOI: 10.1007/BF02534391

Properties of a heat labile, nondialyzable cytosolic factor which prevents lipid peroxidation in membranous organelles are described. The factor is present in liver and other animal tissues, and its capacity to inhibit lipid peroxidation in membranes subjected to oxidative stress is greatly potentiated by glutathione (GSH), although GSH by itself has no inhibitory effect on lipid peroxidation. The data obtained thus far indicate that one or more sulfhydryl groups associated with the factor is required for the inhibition. The mechanism by which lipid peroxidation is inhibited must involve prevention of initiation of peroxidation in the membranes, presumably by a process requiring one or more sulfhydryl groups associated with the heat labile factor. The latter appears to be protected by GSH while the factor is exerting its inhibitory effect on lipid peroxidation. The factor is not one of the known GSH‐dependent enzymes, and appears to be a potent and ubiquitous system for stabilizing cell membranes against oxidative damage.