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Mouse Peroxiredoxin V Is a Thioredoxin Peroxidase That Inhibits p53-Induced Apoptosis

2000; Elsevier BV; Volume: 268; Issue: 3 Linguagem: Inglês

10.1006/bbrc.2000.2231

1090-2104

Yuan Zhou, Kin Hang Kok, Abel C.S. Chun, Chi‐Ming Wong, Hing Wan Wu, Marie C.M. Lin, Peter C. W. Fung, Hsiang‐Fu Kung, Dong‐Yan Jin,

interferon and immune responses

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.