Proteomics methods to study methionine oxidation

Mass Spectrom Rev. 2014 Mar-Apr;33(2):147-56. doi: 10.1002/mas.21386. Epub 2013 Oct 31.

Abstract

The oxidation and consequent reduction of protein-bound methionine residues is of great interest in understanding different aspects of how oxidative stress affects protein functions and cellular signaling. To date, few technologies are available for the study of methionine sulfoxides. And, especially the absence of highly specific antibodies has impeded the field in understanding the exact role of methionine oxidation on a proteome-wide level. Nonetheless, the different models where the responsible enzymes for repair of the oxidized methionines have been studied show that there is an important role for this modification in a cellular context. We here review different mass spectrometry based and proteomics methods for characterizing in vivo methionine oxidation.

Keywords: PTM analysis; methionine oxidation; methionine sulfoxide; oxidative stress; redox proteomics.

Publication types

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

MeSH terms

  • Animals
  • Humans
  • Mass Spectrometry / methods*
  • Methionine / analogs & derivatives*
  • Methionine / analysis
  • Methionine / metabolism
  • Oxidation-Reduction
  • Oxidative Stress
  • Proteins / chemistry*
  • Proteins / metabolism
  • Proteomics / methods*

Substances

  • Proteins
  • Methionine
  • methionine sulfoxide