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. (C) 2000 Academic Press.
Original language | English |
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Pages (from-to) | 921-927 |
Number of pages | 7 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 268 |
Issue number | 3 |
DOIs | |
Publication status | Published - 24 Feb 2000 |
Externally published | Yes |
Keywords
- Apoptosis
- p53
- Peroxiredoxin
- Reactive oxygen species (ROS)
- Redox
- Thioredoxin peroxidase
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology