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

We have identified human and mouse peroxiredoxin V (Prx-V) by virtue of the sequence homologies to yeast peroxisomal antioxidant enzyme PMP20. Prx-V r epresents the fifth of the six currently known subfamilies of mammalian per oxiredoxins. 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 med iated by redox. We show that overexpression of Prx-V prevented the p53-depe ndent generation of reactive oxygen species. Likewise, Prx-V inhibited p53- induced apoptosis. Thus, Prx-V is critically involved in intracellular redo x signaling. (C) 2000 Academic Press.