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    Biochem Biophys Res Commun. 2000 Feb 24;268(3):921-7.

    Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis.

    Zhou Y, Kok KH, Chun AC, Wong CM, Wu HW, Lin MC, Fung PC, Kung H, Jin DY.

    Institute of Molecular Biology, Division of Medical Physics, Department of Medicine, University of Hong Kong, Pokfulam, Hong Kong, China.

    We have identified human and mouse peroxiredoxin V (Prx-V) by virtue of the sequence homologies to yeast peroxisomal antioxidant enzyme PMP20. Prx-V represents the fifth of the six currently known subfamilies of mammalian peroxiredoxins. It is a novel organellar enzyme that has orthologs in bacteria. Biochemically, Prx-V is a thioredoxin peroxidase. One important aspect of p53 function in mammalian cells involves induction of apoptosis likely mediated by redox. We show that overexpression of Prx-V prevented the p53-dependent generation of reactive oxygen species. Likewise, Prx-V inhibited p53-induced apoptosis. Thus, Prx-V is critically involved in intracellular redox signaling. Copyright 2000 Academic Press.

    PMID: 10679306 [PubMed - indexed for MEDLINE]

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