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The Role of Peroxiredoxins in the Transduction of H2O2 Signals

Title
The Role of Peroxiredoxins in the Transduction of H2O2 Signals
Authors
Rhee, Sue GooWoo, Hyun AeKang, Dongmin
Ewha Authors
우현애강동민
SCOPUS Author ID
강동민scopus; 우현애scopus
Issue Date
2018
Journal Title
ANTIOXIDANTS & REDOX SIGNALING
ISSN
1523-0864JCR Link

1557-7716JCR Link
Citation
ANTIOXIDANTS & REDOX SIGNALING vol. 28, no. 7, pp. 537 - 557
Keywords
peroxiredoxinhydrogen peroxideintracellular messengerthiol oxidation
Publisher
MARY ANN LIEBERT, INC
Indexed
SCI; SCIE; SCOPUS WOS scopus
Document Type
Review
Abstract
Significance: Hydrogen peroxide (H2O2) is produced on stimulation of many cell surface receptors and serves as an intracellular messenger in the regulation of diverse physiological events, mostly by oxidizing cysteine residues of effector proteins. Mammalian cells express multiple H2O2-eliminating enzymes, including catalase, glutathione peroxidase (GPx), and peroxiredoxin (Prx). A conserved cysteine in Prx family members is the site of oxidation by H2O2. Peroxiredoxins possess a high-affinity binding site for H2O2 that is lacking in catalase and GPx and which renders the catalytic cysteine highly susceptible to oxidation, with a rate constant several orders of magnitude greater than that for oxidation of cysteine in most H2O2 effector proteins. Moreover, Prxs are abundant and present in all subcellular compartments. The cysteines of most H2O2 effectors are therefore at a competitive disadvantage for reaction with H2O2. Recent Advances: Here we review intracellular sources of H2O2 as well as H2O2 target proteins classified according to biochemical and cellular function. We then highlight two strategies implemented by cells to overcome the kinetic disadvantage of most target proteins with regard to H2O2-mediated oxidation: transient inactivation of local Prx molecules via phosphorylation, and indirect oxidation of target cysteines via oxidized Prx. Critical Issues and Future Directions: Recent studies suggest that only a small fraction of the total pools of Prxs and H2O2 effector proteins localized in specific subcellular compartments participates in H2O2 signaling. Development of sensitive tools to selectively detect phosphorylated Prxs and oxidized effector proteins is needed to provide further insight into H2O2 signaling.
DOI
10.1089/ars.2017.7167
Appears in Collections:
일반대학원 > 생명·약학부 > Journal papers
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