Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins

Curr Opin Cell Biol. 2005 Apr;17(2):183-9. doi: 10.1016/


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Enzyme Activation / physiology
  • Humans
  • Hydrogen Peroxide / metabolism*
  • Oxidation-Reduction
  • PTEN Phosphohydrolase
  • Peroxidases / metabolism*
  • Peroxiredoxins
  • Phosphoric Monoester Hydrolases / metabolism
  • Phosphorylation / drug effects
  • Protein Tyrosine Phosphatases / metabolism
  • Second Messenger Systems / drug effects
  • Second Messenger Systems / physiology*
  • Signal Transduction / drug effects
  • Signal Transduction / physiology*
  • Tumor Suppressor Proteins / metabolism


  • Tumor Suppressor Proteins
  • Hydrogen Peroxide
  • Peroxidases
  • Peroxiredoxins
  • Phosphoric Monoester Hydrolases
  • Protein Tyrosine Phosphatases
  • PTEN Phosphohydrolase
  • PTEN protein, human