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1.
Biogerontology ; 15(1): 87-98, 2014 Feb.
Article in English | MEDLINE | ID: mdl-24311290

ABSTRACT

Oxidative stress caused by reactive oxygen species is proposed to cause age related muscle wasting (sarcopenia). Reversible oxidation of protein thiols by reactive oxygen species can affect protein function, so we evaluated whether muscle wasting in normal aging was associated with a pervasive increase in reversible oxidation of protein thiols or with an increase in irreversible oxidative damage to macromolecules. In gastrocnemius muscles of C57BL/6J female mice aged 3, 15, 24, 27, and 29 months there was no age related increase in protein thiol oxidation. In contrast, there was a significant correlation (R (2) = 0.698) between increasing protein carbonylation, a measure of irreversible oxidative damage to proteins, and loss of mass of gastrocnemius muscles in aging female mice. In addition, there was an age-related increase in lipofuscin content, an aggregate of oxidised proteins and lipids, in quadriceps limb muscles in aging female mice. However, there was no evidence of an age-related increase in malondialdehyde or F2-isoprostanes levels, which are measures of oxidative damage to lipids, in gastrocnemius muscles. In summary, this study does not support the hypothesis that a pervasive increase in protein thiol oxidation is a contributing factor to sarcopenia. Instead, the data are consistent with an aging theory which proposes that molecular damage to macromolecules leads to the structural and functional disorders associated with aging.


Subject(s)
Aging/metabolism , Muscle, Skeletal/metabolism , Sarcopenia/metabolism , Sulfhydryl Compounds/metabolism , Aging/pathology , Animals , Female , Lipofuscin/metabolism , Malondialdehyde/metabolism , Mice , Mice, Inbred C57BL , Models, Animal , Muscle, Skeletal/pathology , Oxidation-Reduction , Reactive Oxygen Species/metabolism , Sarcopenia/pathology
2.
Free Radic Res ; 45(9): 991-9, 2011 Sep.
Article in English | MEDLINE | ID: mdl-21696323

ABSTRACT

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.


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