Abstract
Oxidation of skeletal muscle proteins has been reported to occur following contractions, with ageing, and with a variety of disease states, but the nature of the oxidised proteins has not been identified. A proteomics approach was utilised to identify major proteins that contain carbonyls and/or 3-nitrotyrosine (3-NT) groups in the gastrocnemius (GTN) muscles of adult (5-11 months of age) and old (26-28 months of age) wild type (WT) mice and adult mice lacking copper, zinc superoxide dismutase (Sod1-/- mice), manganese superoxide dismutase (Sod2+/- mice) or glutathione peroxidase 1 (GPx1-/- mice). In quiescent GTN muscles of adult and old WT mice, protein carbonylation and/or formation of 3-NT occurred in several proteins involved in glycolysis, as well as creatine kinase and carbonic anhydrase III. Following contractions, the 3-NT intensity was increased in specific protein bands from GTN muscles of both adult and old WT mice. In quiescent GTN muscles from adult Sod1-/-, Sod2+/- or GPx1-/- mice compared with age-matched WT mice only carbonic anhydrase III showed a greater 3-NT content. We conclude that formation of 3-NT occurs readily in response to oxidative stress in carbonic anhydrase III and this may provide a sensitive measure of oxidative damage to muscle proteins.
Original language | English (US) |
---|---|
Pages (from-to) | 362-372 |
Number of pages | 11 |
Journal | Proteomics - Clinical Applications |
Volume | 1 |
Issue number | 4 |
DOIs | |
State | Published - Apr 2007 |
Keywords
- 3-nitrotyrosine
- Carbonyls
- Oxidative stress
- Protein oxidation
- Skeletal muscle
ASJC Scopus subject areas
- Clinical Biochemistry