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Redox Modulation of PTEN Phosphatase Activity by Hydrogen Peroxide and Bisperoxidovanadium Complexes

Chang-Uk Lee1,2, Gernot Hahne1,2, Jonas Hanske3

  • 1Chemical Genomics Centre of the Max Planck Society, Otto-Hahn-Strasse 15, 44227 Dortmund (Germany).

Angewandte Chemie (International Ed. in English)
|September 30, 2015
PubMed

Insights

Reactive oxygen species, like hydrogen peroxide (H2O2), and bpV complexes inhibit PTEN phosphatase through oxidation. This forms a disulfide bond, allowing PTEN reactivation under reducing conditions.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Homeostasis

Background:

  • PTEN is a crucial tumor suppressor regulating cellular homeostasis.
  • Mechanisms of PTEN inhibition by reactive oxygen species (ROS) and bpV complexes are not well understood.
  • Understanding PTEN inhibition is vital for potential therapeutic applications.

Purpose of the Study:

  • To elucidate the molecular basis of PTEN inhibition by hydrogen peroxide (H2O2) and bisperoxidovanadium (bpV) complexes.
  • To investigate the structural consequences of PTEN inhibition by these agents.
  • To identify potential strategies for PTEN reactivation.

Main Methods:

  • Protein crystallography
  • Mass spectrometry
  • NMR spectroscopy

Main Results:

  • Both H2O2 and bpV complexes inhibit PTEN through oxidative mechanisms.
  • Oxidative inhibition results in the formation of a specific intramolecular disulfide bond in PTEN.
  • PTEN activity can be restored under reductive conditions.

Conclusions:

  • The study reveals the molecular mechanism of PTEN inhibition by H2O2 and bpV.
  • The formation of an intramolecular disulfide bond is key to PTEN inhibition and reactivation.
  • This finding opens avenues for optimizing bpV complexes for therapeutic use.
Keywords:
bpV-phendisulfidesinhibitorsprotein tyrosine phosphatasetumor suppressors

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