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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.

Author information

1
Institute of Molecular Biology, Division of Medical Physics, Department of Medicine, University of Hong Kong, Pokfulam, Hong Kong, China.

Abstract

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.

PMID:
10679306
DOI:
10.1006/bbrc.2000.2231
[Indexed for MEDLINE]

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