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Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-Cys peroxiredoxins

Title
Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-Cys peroxiredoxins
Authors
Hyun A.W.Jeong W.Chang T.-S.Kwang J.P.Sung J.P.Jeong S.Y.Sue G.R.
Ewha Authors
이서구정우진창동신우현애
SCOPUS Author ID
이서구scopusscopus; 정우진scopus; 창동신scopus; 우현애scopus
Issue Date
2005
Journal Title
Journal of Biological Chemistry
ISSN
0021-9258JCR Link
Citation
vol. 280, no. 5, pp. 3125 - 3128
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Cysteine residues of certain peroxiredoxins (Prxs) undergo reversible oxidation to sulfinic acid (Cys-SO2H) and the reduction reaction is catalyzed by sulfiredoxin (Srx). Specific Cys residues of various other proteins are also oxidized to sulfinic acid, suggesting that formation of Cys-SO 2H might be a novel posttranslational modification that contributes to regulation of protein function. To examine the susceptibility of sulfinic forms of proteins to reduction by Srx, we prepared such forms of all six mammalian Prx isoforms and glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Purified sulfiredoxin reduced the sulfinic forms of the four 2-Cys members (Prx I to Prx IV) of the Prx family in vitro, but it did not affect those of Prx V, Prx VI, or GAPDH. Furthermore, Srx bound specifically to the four 2-Cys Prxs in vitro and in cells. Sulfinic forms of Prx I and Prx II, but not of Prx VI or GAPDH, present in H2O2-treated A549 cells were gradually reduced after removal of H2O2; overexpression of Srx increased the rate of the reduction of Prx I and Prx II but did not induce that of Prx VI or GAPDH. These results suggest that reduction of Cys-SO2H by Srx is specific to 2-Cys Prx isoforms. For proteins such as Prx VI and GAPDH, sulfinic acid formation might be an irreversible process that causes protein damage.
DOI
10.1074/jbc.C400496200
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일반대학원 > 생명·약학부 > Journal papers
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