Antioxidant cytoprotection by peroxisomal peroxiredoxin-5 |
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| Institution: | 1. KU Leuven — University of Leuven, Department of Pharmaceutical and Pharmacological Sciences, Laboratory of Cell Metabolism, B-3000 Leuven, Belgium;2. Department of Paediatrics, Division of Paediatric Neurology and Metabolism, University Hospital Ghent, B-9000 Ghent, Belgium;3. KU Leuven — University of Leuven, Department of Oncology, Laboratory of Angiogenesis and Neurovascular Link, B-3000 Leuven, Belgium;4. VIB, Vesalius Research Center, Laboratory of Angiogenesis and Neurovascular Link, B-3000 Leuven, Belgium;5. Dept Basic Medical Sciences, UGhent, B-9000 Ghent, Belgium;6. KU Leuven — University of Leuven, Department of Cellular and Molecular Medicine, Laboratory of Intensive Care Medicine, B-3000 Leuven, Belgium;7. KU Leuven — University of Leuven, Department of Cellular and Molecular Medicine, Laboratory for Lipid Biochemistry and Protein Interactions, B-3000 Leuven, Belgium;1. Department of Chemical Engineering and Institute of Biomedical Engineering, National Tsing Hua University, Hsinchu, Taiwan, ROC;2. Department of Biological Science and Technology and Department of Medical Research, China Medical University, Taichung, Taiwan, ROC |
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| Abstract: | Peroxiredoxin-5 (PRDX5) is a thioredoxin peroxidase that reduces hydrogen peroxide, alkyl hydroperoxides, and peroxynitrite. This enzyme is present in the cytosol, mitochondria, peroxisomes, and nucleus in human cells. Antioxidant cytoprotective functions have been previously documented for cytosolic, mitochondrial, and nuclear mammalian PRDX5. However, the exact function of PRDX5 in peroxisomes is still not clear. The aim of this work was to determine the function of peroxisomal PRDX5 in mammalian cells and, more specifically, in glial cells. To study the role of PRDX5 in peroxisomes, the endogenous expression of PRDX5 in murine oligodendrocyte 158 N cells was silenced by RNA interference. In addition, human PRDX5 was also overexpressed in peroxisomes using a vector coding for human PRDX5, whose unconventional peroxisomal targeting sequence 1 (PTS1; SQL) was replaced by the prototypical PTS1 SKL. Stable 158 N clones were obtained. The antioxidant cytoprotective function of peroxisomal PRDX5 against peroxisomal and mitochondrial KillerRed-mediated reactive oxygen species production as well as H2O2 was examined using MTT viability assays, roGFP2, and C11-BOBIPY probes. Altogether our results show that peroxisomal PRDX5 protects 158 N oligodendrocytes against peroxisomal and mitochondrial KillerRed- and H2O2-induced oxidative stress. |
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| Keywords: | Peroxiredoxin-5 Peroxisomes Mitochondria Oxidative stress KillerRed Lipid peroxidation roGFP2 Free radicals |
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