12/15-lipoxygenase-derived lipid peroxides control receptor tyrosine kinase signaling through oxidation of protein tyrosine phosphatases.

@article{Conrad20101215lipoxygenasederivedLP,
  title={12/15-lipoxygenase-derived lipid peroxides control receptor tyrosine kinase signaling through oxidation of protein tyrosine phosphatases.},
  author={Marcus Conrad and Asa Sandin and Heidi F{\"o}rster and Alexander Seiler and Jeroen Frijhoff and Markus Dagnell and Georg W. Bornkamm and Olof R{\aa}dmark and Rob Hooft van Huijsduijnen and Pontus Aspenstr{\"o}m and Frank B{\"o}hmer and Arne Ostman},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2010},
  volume={107 36},
  pages={15774-9}
}
Protein tyrosine phosphatases (PTPs) are regulated through reversible oxidation of the active-site cysteine. Previous studies have implied soluble reactive oxygen species (ROS), like H(2)O(2), as the mediators of PTP oxidation. The potential role(s) of peroxidized lipids in PTP oxidation have not been described. This study demonstrates that increases in cellular lipid peroxides, induced by disruption of glutathione peroxidase 4, induce cellular PTP oxidation and reduce the activity of PDGF… CONTINUE READING