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- W2136050828 abstract "The glutathione peroxidase ( GP x) family is a major antioxidant enzyme family that catalyzes the reduction of a variety of hydroperoxides. GP xs are divided into selenium‐ and nonselenium‐containing GP xs. Because of their efficient antioxidant activity, which depends on the presence of the amino acid residue selenocysteine, selenium‐containing GP xs have been the subject of many studies. However, the physiological roles of the nonselenium GP xs remain unclear. Here, we report that the deletion of phospholipid hydroperoxide glutathione peroxidase ( PHGP x) homologues causes accelerated aging that leads to a shortened lifespan in C aenorhabditis elegans . PHGP x is an antioxidant enzyme that directly reduces the phospholipid hydroperoxides generated in biomembranes. The quadruple phgpx mutant gpx‐1 ; gpx‐2 ; gpx‐6 ; gpx‐7 developed normally, reached adulthood and reproduced as well as the wild type. However, a lifespan analysis showed that the quadruple phgpx mutant had a short maximum lifespan, with an age‐related increase in its mortality rate. The intestine is the primary tissue expressing gpx‐1 , gpx‐2 , gpx‐6 and gpx‐7 in C . elegans , and the expression of gpx‐6 is greatly enhanced under starvation conditions. These results suggest that the C . elegans PHGP x homologues have important functions in the regulation of aging, probably by reducing oxidative damage in the intestine." @default.
- W2136050828 created "2016-06-24" @default.
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- W2136050828 date "2014-09-08" @default.
- W2136050828 modified "2023-10-16" @default.
- W2136050828 title "Deletion of the four phospholipid hydroperoxide glutathione peroxidase genes accelerates aging in <i><scp>C</scp>aenorhabditis elegans</i>" @default.
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- W2136050828 doi "https://doi.org/10.1111/gtc.12175" @default.
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