Redox modulation of tyrosine phosphorylation-dependent signal transduction pathways

Free Radic Biol Med. 1996;21(3):323-33. doi: 10.1016/0891-5849(96)00051-2.


The main purpose of this review article is to provide a better understanding of the role of oxidants as modulators/mediators of tyrosine phosphorylation-dependent signal transduction pathways. It is generally accepted that reversible phosphorylation of protein tyrosine residues by polypeptide growth factor receptor protein tyrosine kinases (e.g., epidermal growth factor receptor, platelet derived growth factor receptor, insulin receptor) is a signalling mechanism implicated in cell proliferation, adhesion, differentiation, transformation, and apoptosis. It is controlled by the opposing actions of protein tyrosine kinases and protein tyrosine phosphatases. Nevertheless, increasing amounts of experimental data indicate that intracellular redox state plays a major role in the mechanisms underlying the actions of growth factors. Furthermore, redox active species mediate signalling processes on their own. Thus, in this article we attempted to discuss these points, presenting our published as well as unpublished contribution to the field.

Publication types

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

MeSH terms

  • Animals
  • Humans
  • Oxidation-Reduction*
  • Phosphorylation
  • Protein Tyrosine Phosphatases / metabolism*
  • Protein-Tyrosine Kinases / metabolism*
  • Signal Transduction*
  • Tyrosine / metabolism*


  • Tyrosine
  • Protein-Tyrosine Kinases
  • Protein Tyrosine Phosphatases