Peroxiredoxin V, an atypical thioredoxin peroxidase, is widely expressed in mammalian tissues. In addition, Prdx V is localized in mitochondria, peroxisome, cytosol, and nucleus. Prdx V has been reported to protect a wide range of cellular environments as antioxidant enzyme, and its dysfunctions may be implicated in several diseases, such as cancer, inflammation, and neurodegenerative disease. Identification and relative quantification of proteins affected by Prdx V may help identify novel signaling mechanisms that are important for oxidative stress response. However, the role of Prdx V in the modulation of hypoxia‐related cellular response is not studied yet. In order to examine the function of endogenous Prdx V in hypoxic condition in vivo, we generated a transgenic mouse model with Prdx V siRNA expression controlled by U6 promoter. Of many tissues, the knockdown of Prdx V expression was displayed in kidney, lung, and liver, but not spleen and skin. We conducted on the basis of nano‐UPLC‐MSE proteomic study to identify the Prdx V‐affected protein networks in hypoxic kidneys. In this study, we identified protein networks associated with oxidative stress, fatty acid metabolism, and mitochondrial dysfunction. Our results indicated that Prdx V affected to regulation of kidney homeostasis under hypoxia stress.

We isolated low temperature inducible genes using suppression subtractive hybridization (SSH) method and were able to obtain to cloneMLT107 gene encoding peroxiredoxin and aminotransferase. The full-length cDNA of MLT107 is 1,049 bp with an open reading frame (ORF) consisting of 261 amino acid (aa). Genomic southern blot confirmed that mungbean genome has two copies of MLT107 gene. Northern blot analysis was also carried out for the gene expression during ABA, NaCl, drought, wounding and H2O2 stresses. The expression of MLT107 gene significantly decreased by ABA, NaCl and drought stress, but wounding and H2O2 stress significantly induced MLT107 gene expression. Especially, H2O2 strongly induced the MLT107 gene expression. The expression of MLT107gene during low temperature stress started to increase in 3 h after treatment, and than slightly decreased and again increased at 24 h. Using GFP fusion vector, smGFP-MLT107 was targeted both to mitochondria and chloroplast. However, it was mostly targeted to mitochondria and partially targeted to chloroplast. For the functional analysis of MLT107, MLT107 recombinant protein was heterologously expressed in E.coli. The MLT107 recombinant cells showed enhanced antioxidant activity compared to that of vector control cells.