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PMID: 14759598 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S. Review

An assessment of proposed mechanisms for sensing hydrogen peroxide in mammalian systems.

Archives of biochemistry and biophysics ·Vol. 422 ·No. 2 ·2004-02-15 ·Pages 119-24

Stone JR

Abstract

Despite much recent interest in the biochemistry of reactive oxygen species, the mechanisms by which hydrogen peroxide (H2O2) functions in mammalian cells remain poorly defined. Proposed mechanisms for sensing H2O2 in mammalian cells include inactivation of protein tyrosine phosphatases and dual specificity phosphatases as well as inactivation of peroxiredoxins. In this critical review, proteins proposed to serve as sensors for H2O2 in mammals will be compared to peroxidases, catalases, and the bacterial H2O2 sensor OxyR for their ability to react with H2O2, in the context of our current knowledge concerning the concentrations of H2O2 present in cells.

MeSH Terms
Animals Binding Sites Biosensing Techniques/methods Cysteine/chemistry DNA-Binding Proteins Hydrogen Peroxide/analysis,metabolism Kinetics Peptides/chemistry,metabolism Peroxidases/chemistry,metabolism Protein Tyrosine Phosphatases/chemistry,metabolism Repressor Proteins/chemistry,metabolism Sulfhydryl Compounds/chemistry Transcription Factors/chemistry,metabolism
Chemicals
DNA-Binding Proteins Peptides Repressor Proteins Sulfhydryl Compounds Transcription Factors Hydrogen Peroxide Peroxidases Protein Tyrosine Phosphatases Cysteine
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Stone James R
Department of Pathology, Massachusetts General Hospital, Harvard Medical School, Boston, MA 02114, USA. jrstone@partners.org
Article Info
Journal
Archives of biochemistry and biophysics
Abbr.
Arch Biochem Biophys
ISSN
0003-9861
Published
2004-02-15
Pages
119-24
Language
English
Region
United States
NLM ID
0372430
Subset
IM
Grants
NHLBI NIH HHS · R01 HL074324 · United States
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