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

Article Details

Citation

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

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

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

PubMed ID
10679306 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Peroxiredoxin-5, mitochondrialP30044Details