
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.
p53, Peroxiredoxin III, Apoptosis - drug effects, Molecular Sequence Data, Reactive Oxygen Species - metabolism, Sequence Homology, Gene Expression, Apoptosis, In Vitro Techniques, Redox, Mice, Animals, Humans, Peroxidases - genetics - metabolism - pharmacology, Amino Acid Sequence, Thioredoxin peroxidase, Phylogeny, DNA Primers, Base Sequence, Sequence Homology, Amino Acid, Tumor Suppressor Protein p53 - metabolism - pharmacology, Peroxiredoxin, Reactive oxygen species (ROS), Peroxiredoxins, DNA Primers - genetics, Neoplasm Proteins, Amino Acid, Peroxidases, Reactive Oxygen Species, Oxidation-Reduction, HeLa Cells, Signal Transduction
p53, Peroxiredoxin III, Apoptosis - drug effects, Molecular Sequence Data, Reactive Oxygen Species - metabolism, Sequence Homology, Gene Expression, Apoptosis, In Vitro Techniques, Redox, Mice, Animals, Humans, Peroxidases - genetics - metabolism - pharmacology, Amino Acid Sequence, Thioredoxin peroxidase, Phylogeny, DNA Primers, Base Sequence, Sequence Homology, Amino Acid, Tumor Suppressor Protein p53 - metabolism - pharmacology, Peroxiredoxin, Reactive oxygen species (ROS), Peroxiredoxins, DNA Primers - genetics, Neoplasm Proteins, Amino Acid, Peroxidases, Reactive Oxygen Species, Oxidation-Reduction, HeLa Cells, Signal Transduction
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