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Formation of 3‐nitrotyrosines in carbonic anhydrase III is a sensitive marker of oxidative stress in skeletal muscle
Author(s) -
Vasilaki Aphrodite,
Simpson Deborah,
McArdle Francis,
McLean Lynne,
Bey Robert J.,
Van Remmen Holly,
Richardson Arlan G.,
McArdle Anne,
Faulkner John A,
Jackson Malcolm J.
Publication year - 2007
Publication title -
proteomics – clinical applications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.948
H-Index - 54
eISSN - 1862-8354
pISSN - 1862-8346
DOI - 10.1002/prca.200600702
Subject(s) - sod2 , gpx1 , oxidative stress , superoxide dismutase , chemistry , carbonic anhydrase , skeletal muscle , creatine kinase , sod1 , protein carbonylation , biochemistry , glutathione peroxidase , medicine , endocrinology , oxidative phosphorylation , biology , enzyme , lipid peroxidation
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.