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

Arch Biochem Biophys. 2004 Feb 15;422(2):119-24. doi: 10.1016/j.abb.2003.12.029.

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.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Binding Sites
  • Biosensing Techniques / methods
  • Cysteine / chemistry
  • DNA-Binding Proteins*
  • Hydrogen Peroxide / analysis*
  • Hydrogen Peroxide / metabolism
  • Kinetics
  • Peptides / chemistry
  • Peptides / metabolism
  • Peroxidases / chemistry
  • Peroxidases / metabolism
  • Protein Tyrosine Phosphatases / chemistry
  • Protein Tyrosine Phosphatases / metabolism
  • Repressor Proteins / chemistry
  • Repressor Proteins / metabolism
  • Sulfhydryl Compounds / chemistry
  • Transcription Factors / chemistry
  • Transcription Factors / metabolism

Substances

  • DNA-Binding Proteins
  • Peptides
  • Repressor Proteins
  • Sulfhydryl Compounds
  • Transcription Factors
  • Hydrogen Peroxide
  • Peroxidases
  • Protein Tyrosine Phosphatases
  • Cysteine