2-Cys Peroxiredoxins: Emerging Hubs Determining Redox Dependency of Mammalian Signaling Networks
Author(s) -
Jinah Park,
Sunmi Lee,
Sanghyuk Lee,
Sang Won Kang
Publication year - 2014
Publication title -
international journal of cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.587
H-Index - 53
eISSN - 1687-8884
pISSN - 1687-8876
DOI - 10.1155/2014/715867
Subject(s) - thioredoxin , antioxidant , superoxide dismutase , redox , peroxidase , thioredoxin reductase , enzyme , cell signaling , microbiology and biotechnology , signal transduction , catalase , biology , biochemistry , reactive oxygen species , peroxiredoxin , chemistry , organic chemistry
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 H 2 O 2 . 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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