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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Dong, Wei-ren Shao, Jian-zhong Xiang, Li-xin Zhao, Jing Zhu, Guan Nie, Li Sun, Cen-cen |
| Description | Author Affiliation: Sun CC ( From the College of Life Sciences, Zhejiang University and Key Laboratory for Cell and Gene Engineering of Zhejiang Province, Hangzhou 310058, China and.); Dong WR ( From the College of Life Sciences, Zhejiang University and Key Laboratory for Cell and Gene Engineering of Zhejiang Province, Hangzhou 310058, China and.); Zhao J ( From the College of Life Sciences, Zhejiang University and Key Laboratory for Cell and Gene Engineering of Zhejiang Province, Hangzhou 310058, China and.); Nie L ( From the College of Life Sciences, Zhejiang University and Key Laboratory for Cell and Gene Engineering of Zhejiang Province, Hangzhou 310058, China and.); Xiang LX ( From the College of Life Sciences, Zhejiang University and Key Laboratory for Cell and Gene Engineering of Zhejiang Province, Hangzhou 310058, China and xianglx@zju.edu.cn.); Zhu G ( From the College of Life Sciences, Zhejiang University and Key Laboratory for Cell and Gene Engineering of Zhejiang Province, Hangzhou 310058, China and the Department of Veterinary Pathobiology, College of Veterinary Medicine and Biomedical Sciences, Texas A&M University, College Station, Texas); Shao JZ ( From the College of Life Sciences, Zhejiang University and Key Laboratory for Cell and Gene Engineering of Zhejiang Province, Hangzhou 310058, China and shaojz@zju.edu.cn.) |
| Abstract | Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins that are known as thioredoxin peroxidases. Here we report that Prx1 proteins from Tetraodon nigroviridis and humans also possess a previously unknown catalase-like activity that is independent of Cys residues and reductants but dependent on iron. We identified that the GVL motif was essential to the catalase (CAT)-like activity of Prx1 but not to the Cys-dependent thioredoxin peroxidase (POX) activity, and we generated mutants lacking POX and/or CAT activities for individually delineating their functional features. We discovered that the TnPrx1 POX and CAT activities possessed different kinetic features in reducing H2O2. The overexpression of wild-type TnPrx1 and mutants differentially regulated the intracellular levels of reactive oxygen species and p38 phosphorylation in HEK-293T cells treated with H2O2. These observations suggest that the dual antioxidant activities of Prx1 may be crucial for organisms to mediate intracellular redox homeostasis. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 32 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-08-07 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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