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Controlled elimination of intracellular H2O2: Regulation of peroxiredoxin, catalase, and glutathione peroxidase via post-translational modification

Title
Controlled elimination of intracellular H2O2: Regulation of peroxiredoxin, catalase, and glutathione peroxidase via post-translational modification
Authors
Rhee S.G.Yang K.-S.Kang S.W.Woo H.A.Chang T.-S.
Ewha Authors
이서구강상원창동신우현애
SCOPUS Author ID
이서구scopusscopus; 강상원scopus; 창동신scopus; 우현애scopus
Issue Date
2005
Journal Title
Antioxidants and Redox Signaling
ISSN
1523-0864JCR Link
Citation
vol. 7, no. 41400, pp. 619 - 626
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
The predominant enzymes responsible for elimination of hydrogen peroxide (H2O2) in cells are peroxiredoxins (Prxs), catalase, and glutathione peroxidases (GPxs). Evidence suggests that catalytic activities of certain isoforms of these H2O2-eliminating enzymes are extensively regulated via posttranslational modification. Prx I and Prx II become inactivated when phosphorylated on Thr90 by cyclin B-dependent kinase Cdc2. In addition, the active-site cysteine of Prx I-IV undergoes a reversible sulfinylation (oxidation to cysteine sulfinic acid) in cells. Desulfinylation (reduction to cysteine) is achieved by a novel enzyme named sulfiredoxin. c-Abl and Arg nonreceptor protein tyrosine kinases associate with catalase in cells treated with H2O2 by mechanisms involving the SH3 domains of the kinases and the Pro293PheAsnPro motif of catalase and activate catalase by phosphorylating it on Tyr 231 and Tyr386. Similarily, GPx1 is activated by c-Abl- and Arg-mediated phosphorylation. The tyrosine phosphorylation is critical for ubiquitination-dependent degradation of catalase.
DOI
10.1089/ars.2005.7.619
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일반대학원 > 생명·약학부 > Journal papers
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