Thioredoxin reductase reduces lipid hydroperoxides and spares α-tocopherol

被引:24
作者
May, JM [1 ]
Morrow, JD [1 ]
Burk, RF [1 ]
机构
[1] Vanderbilt Univ, Sch Med, Dept Med, Nashville, TN 37232 USA
关键词
lipid hydroperoxides; selenium; thioredoxin reductase; thioredoxin; ferricyanide; alpha-tocopherol; human erythrocytes;
D O I
10.1006/bbrc.2002.6617
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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).
引用
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页码:45 / 49
页数:5
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