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Int J Cell Biol. 2014;2014:715867. doi: 10.1155/2014/715867. Epub 2014 Feb 4.

2-cys peroxiredoxins: emerging hubs determining redox dependency of Mammalian signaling networks.

Author information

1
Korean Bioinformation Center, KRIBB, Daejeon 305-806, Republic of Korea.
2
Department of Life Science and Research Center for Cell Homeostasis, Ewha Womans University, 52 Ewhayeodaegil, Seodaemun-gu, Seoul 120-750, Republic of Korea.
3
Department of Life Science and Research Center for Cell Homeostasis, Ewha Womans University, 52 Ewhayeodaegil, Seodaemun-gu, Seoul 120-750, Republic of Korea ; Global Top 5 Research Program, Ewha Womans University, 52 Ewhayeodaegil, Seodaemun-gu, Seoul 120-750, Republic of Korea.

Abstract

Mammalian cells have a well-defined set of antioxidant enzymes, which includes superoxide dismutases, catalase, glutathione peroxidases, and peroxiredoxins. Peroxiredoxins are the most recently identified family of antioxidant enzymes that catalyze the reduction reaction of peroxides, such as H2O2. In particular, typical 2-Cys peroxiredoxins are the featured peroxidase enzymes that receive the electrons from NADPH by coupling with thioredoxin and thioredoxin reductase. These enzymes distribute throughout the cellular compartments and, therefore, are thought to be broad-range antioxidant defenders. However, recent evidence demonstrates that typical 2-Cys peroxiredoxins play key signal regulatory roles in the various signaling networks by interacting with or residing near a specific redox-sensitive molecule. These discoveries help reveal the redox signaling landscape in mammalian cells and may further provide a new paradigm of therapeutic approaches based on redox signaling.

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