Selenium-dependent glutathione peroxidasesA highlight of the role of phospholipid hydroperoxide glutathione peroxidase in protection against oxidative damage |
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Authors: | WILLIAMSON Gary BAO Yongping |
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Institution: | 1. Diet,Health and Consumer Sciences Division,Institute of Food Research,Norwich Research Park,Norwich,NR4 7UA,UK 2. Department of Nutrition and Food Hygiene,Harbin Medical University,Harbin 150001,China;Diet,Health and Consumer Sciences Division,Institute of Food Research,Norwich Research Park,Norwich,NR4 7UA,UK |
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Abstract: | Since the discovery that selenium is an integral component of the active site of the mammalian glutathione peroxidase, four members of the glutathione peroxidase family have been characterised: classical cellular glutathione peroxidase, gastrointestinal glutathione peroxidase; plasma glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase ( PHGPx) . They are products of different genes and have different specificities on hydrogen peroxide and lipid hydroperoxides, the latter are generated by free radicals and can damage cell membranes and disrupt cellular functions. Interestingly, PHGPx is not only active on phospholipid hydroperoxide, but also active on thymine hydroperoxide (a model compound for DNA damage) and protein hydroperoxides. This review highlights the role of PHGPx in protection against peroxidative damage of lipids, protein and DNA. |
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Keywords: | selenium selenoprotein phospholipid hydroperoxide glutathione peroxidase oxidative damage |
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