Screening for increased protein thiol oxidation in oxidatively stressed muscle tissue

Free Radic Res. 2011 Sep;45(9):991-9. doi: 10.3109/10715762.2011.590136. Epub 2011 Jun 22.


Elevated oxidative stress can alter the function of proteins through the reversible oxidation of the thiol groups of key cysteine residues. This study evaluated a method to scan for reversible protein thiol oxidation in tissue by measuring reduced and oxidized protein thiols. It assessed the responsiveness of protein thiols to oxidative stress in vivo using a dystrophic (mdx) mouse model and compared the changes to commonly used oxidative biomarkers. In mdx mice, protein thiol oxidation was significantly elevated in the diaphragm, gastrocnemius and quadriceps muscles. Neither malondialdehyde nor degree of glutathione oxidation was elevated in mdx muscles. Protein carbonyl content was elevated, but changes in protein carbonyl did not reflect changes in protein thiol oxidation. Collectively, these data indicate that where there is an interest in protein thiol oxidation as a mechanism to cause or exacerbate pathology, the direct measurement of protein thiols in tissue would be the most appropriate screening tool.

Publication types

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

MeSH terms

  • Animals
  • Cysteine / metabolism*
  • Glutathione / metabolism
  • Lipid Peroxidation
  • Male
  • Malondialdehyde / analysis
  • Malondialdehyde / blood
  • Mice
  • Mice, Inbred C57BL
  • Mice, Inbred mdx
  • Muscle, Skeletal / metabolism*
  • Muscular Dystrophy, Duchenne / metabolism
  • Oxidation-Reduction
  • Oxidative Stress*
  • Protein Carbonylation
  • Proteins / chemistry
  • Proteins / metabolism*
  • Sulfhydryl Compounds / metabolism*


  • Proteins
  • Sulfhydryl Compounds
  • Malondialdehyde
  • Glutathione
  • Cysteine