Hydrogen peroxide as intracellular messenger production, target, and elimination

Sue Goo Rhee, Tong Shin Chang, Yun Soo Bae, Seung Rock Lee, Sang Won Kang

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

2 Scopus citations


Engagement of peptide growth-factor receptors induces a transient production of low levels of H2O2 in various cells. The H2O 2 response to platelet-derived growth factor requires the intrinsic tyrosine kinase activity of the receptor as well as the activation of phosphatidylinositol 3-kinase (PI 3-kinase). It appears that PtdIns(3,4,5)P3, a product of PI 3-kinase, is necessary to activate an isoform of NADPH oxidase through the small GTP-binding protein Rac. H2O2 thus produced propagates its signal by specifically acting on protein tyrosine phosphatases. And enhancement of protein tyrosine phosphorylation in growth factor-stimulated cells depends on the H2O2 production. This is probably because the activation of a receptor tyrosine kinase is not sufficient to increase the steady-state level of protein tyrosine phosphorylation in cells, and that concurrent inhibition of protein tyrosine phosphatase by H2O2 might be needed as well. Elimination of H2O 2 appears to be an extensively regulated process. Peroxiredoxin I (Prx I) and Prx II, two cytosolic thioredoxin-dependent peroxidases, are inactivated at the G2-M transition through Cdc2 kinase-dependent phosphorylation.

Original languageEnglish
Title of host publicationCell Signaling in Vascular Inflammation
PublisherHumana Press
Number of pages12
ISBN (Print)1588295257, 9781588295255
StatePublished - 2005


  • Cdc2 kinase
  • Hydrogen peroxide
  • intracellular messenger
  • NADPH oxidase
  • PDGF receptor
  • peroxiredoxin
  • protein
  • tyrosine phosphatase


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