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International Journal of Cell Biology
Volume 2014, Article ID 715867, 10 pages
Review Article

2-Cys Peroxiredoxins: Emerging Hubs Determining Redox Dependency of Mammalian Signaling Networks

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

Received 7 August 2013; Accepted 25 November 2013; Published 4 February 2014

Academic Editor: Agnès Delaunay-Moisan

Copyright © 2014 Jinah Park et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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.