期刊
ANTIOXIDANTS & REDOX SIGNALING
卷 15, 期 3, 页码 817-829出版社
MARY ANN LIEBERT, INC
DOI: 10.1089/ars.2010.3584
关键词
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资金
- Fonds National de la Recherche Scientifique (FNRS)
- Communaute francaise de Belgique-Actions de Recherche Concertees (ARC)
- DIANE research program of the Walloon Region
Peroxiredoxin 5 (PRDX5) was the last member to be identified among the six mammalian peroxiredoxins. It is also the unique atypical 2-Cys peroxiredoxin in mammals. Like the other five members, PRDX5 is widely expressed in tissues but differs by its surprisingly large subcellular distribution. In human cells, it has been shown that PRDX5 can be addressed to mitochondria, peroxisomes, the cytosol, and the nucleus. PRDX5 is a peroxidase that can use cytosolic or mitochondrial thioredoxins to reduce alkyl hydroperoxides or peroxynitrite with high rate constants in the 10(6) to 10(7) M-1 s(-1) range, whereas its reaction with hydrogen peroxide is more modest, in the 10(5) M-1 s(-1) range. PRDX5 crystal structures confirmed the proposed enzymatic mechanisms based on biochemical data but revealed also some specific unexpected structural features. So far, PRDX5 has been viewed mainly as a cytoprotective antioxidant enzyme acting against endogenous or exogenous peroxide attacks rather than as a redox sensor. Accordingly, overexpression of the enzyme in different subcellular compartments protects cells against death caused by nitro-oxidative stresses, whereas gene silencing makes them more vulnerable. Thus, more than 10 years after its molecular cloning, mammalian PRDX5 appears to be a unique peroxiredoxin exhibiting specific functional and structural features. Antioxid. Redox Signal. 15, 817-829.
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