Thioredoxin reductase reduces lipid hydroperoxides and spares alpha-tocopherol.

May JM, Morrow JD, Burk RF
Biochem Biophys Res Commun. 2002 292 (1): 45-9

PMID: 11890669 · DOI:10.1006/bbrc.2002.6617

We investigated whether and how rat liver thioredoxin reductase spares alpha-tocopherol in biomembranes. Purified hydroperoxides of beta-linoleoyl-gamma-palmitoylphosphatidylcholine were decreased 35% by treatment with thioredoxin reductase and 54% by thioredoxin reductase plus E. coli thioredoxin. Thioredoxin reductase also halved the amount of hydroperoxides that had been formed during photoperoxidation of liposomes composed of beta-linoleoyl-gamma-palmitoylphosphatidylcholine, and of emulsions of both cholesterol and cholesteryl linolenate. In erythrocyte ghosts, thioredoxin reductase spared alpha-tocopherol from oxidation by both soybean lipoxygenase and ferricyanide. Thioredoxin reductase also decreased F(2)-isoprostanes in ghosts oxidized by ferricyanide, suggesting that its ability to spare alpha-tocopherol relates to reduction of lipid hydroperoxides.

(C)2002 Elsevier Science (USA).

MeSH Terms (13)

alpha-Tocopherol Animals Erythrocyte Membrane Ferricyanides Humans Kinetics Lipid Peroxidation Lipid Peroxides Lipoxygenase Liver Oxidation-Reduction Rats Thioredoxin-Disulfide Reductase

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