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 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.
Zhou
Y
Y
Institute of Molecular Biology, Division of Medical Physics, Department of Medicine, University of Hong Kong, Pokfulam, Hong Kong, China.
Kok
K H
KH
Chun
A C
AC
Wong
C M
CM
Wu
H W
HW
Lin
M C
MC
Fung
P C
PC
Kung
H
H
Jin
D Y
DY
D000595:Amino Acid Sequence; D000818:Animals; D017209:Apoptosis / Q000187:drug effects*; D001483:Base Sequence; D017931:DNA Primers / Q000235:genetics; D015870:Gene Expression; D006367:HeLa Cells; D006801:Humans; D066298:In Vitro Techniques; D051379:Mice; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology*; D061105:Peroxiredoxin III; D054464:Peroxiredoxins; D010802:Phylogeny; D017382:Reactive Oxygen Species / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism / Q000494:pharmacology*
D017931:DNA Primers; D009363:Neoplasm Proteins; C516116:Prdx3 protein, mouse; D017382:Reactive Oxygen Species; D016159:Tumor Suppressor Protein p53; D010544:Peroxidases; C516115:PRDX3 protein, human; C515974:PRDX5 protein, human; D061105:Peroxiredoxin III; D054464:Peroxiredoxins; C515975:Prdx5 protein, mouse