Reversible regulation of SHP-1 tyrosine phosphatase activity by oxidation

Jess M. Cunnick, Jay F. Dorsey, Lin Mei, Jie Wu

Research output: Contribution to journalArticlepeer-review

45 Scopus citations


Increasing evidence indicates that redox regulation is an important signaling mechanism. Protein tyrosine phosphatases (PTPases) are sensitive to oxidative inactivation and are potential targets of redox regulation. In this study, we analyzed the reversibility of oxidative inactivation of the PTPase SHP-1, which negatively regulates protein tyrosine kinase signaling. H2O2 inactivated SHP-1 in vitro. Incubation of the H2O2-inactivated SHP-1 with dithiothreitol recovered 44-99% of the PTPase activity, depending on the H2O2 concentrations used to inactivate SHP-1. Glutathione and N-acetylcysteine also reactivated H2O2-treated SHP-1. Stimulation of SHP-1-transfected HeLa cells with H2O2 rapidly decreased SHP-1 activity, which was completely reversed within 15 min. Thus, oxidative inactivation of SHP-1 is a reversible process.

Original languageEnglish (US)
Pages (from-to)887-894
Number of pages8
JournalBiochemistry and Molecular Biology International
Issue number5
StatePublished - Aug 1998
Externally publishedYes


  • Dithiothreitol
  • Glutathione
  • Oxidation
  • SHP-1
  • Tyrosine phosphatase

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics


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