Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins

Sue Goo Rhee, Sang Won Kang, Woojin Jeong, Tong Shin Chang, Kap Seok Yang, Hyun Ae Woo

Research output: Contribution to journalReview articlepeer-review

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Hydrogen peroxide (H2O2) accumulates transiently in various cell types stimulated with peptide growth factors and participates in receptor signaling by oxidizing the essential cysteine residues of protein tyrosine phosphatases and the lipid phosphatase PTEN. The reversible inactivation of these phosphatases by H2O2 is likely required to prevent futile cycles of phosphorylation-dephosphorylation of proteins and phosphoinositides. The accumulation of H2O2 is possible even in the presence of large amounts of the antioxidant enzymes peroxiredoxin I and II in the cytosol, probably because of a built-in mechanism of peroxiredoxin inactivation that is mediated by H2O2 and reversed by an ATP-dependent reduction reaction catalyzed by sulfiredoxin.

Original languageEnglish
Pages (from-to)183-189
Number of pages7
JournalCurrent Opinion in Cell Biology
Issue number2
StatePublished - Apr 2005

Bibliographical note

Funding Information:
This work was supported by the 21C Frontier Functional Proteomics Project (FPR02A7-32-110) through Ewha Womans University. HAW was the recipient of a BK21 scholarship.


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