ArticleJournal of applied physiology (Bethesda, Md. : 1985)2008
Carbonic anhydrase III and four-and-a-half LIM protein 1 are preferentially oxidized with muscle unloading.
Article in Journal of applied physiology (Bethesda, Md. : 1985), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Age-dependent effects of caloric restriction on mTOR and ubiquitin-proteasome pathways in skeletal muscles.GeroScience · 2019Article
- Development of autoantibodies against muscle-specific FHL1 in severe inflammatory myopathies.The Journal of clinical investigation · 2015Article
- Interplay between aging and unloading on oxidative stress in fast-twitch muscles.The journals of gerontology. Series A, Biological sciences and medical sciences · 2013Article
- Carbonic anhydrase III regulates peroxisome proliferator-activated receptor-γ2.Experimental cell research · 2012Article
- Article
- Muscle oxidative capacity during IL-6-dependent cancer cachexia.American journal of physiology. Regulatory, integrative and comparative physiology · 2011Article
- Asymmetric superoxide release inside and outside the mitochondria in skeletal muscle under conditions of aging and disuse.Journal of applied physiology (Bethesda, Md. : 1985) · 2010Article
- Aging impairs the expression of the catalytic subunit of glutamate cysteine ligase in soleus muscle under stress.The journals of gerontology. Series A, Biological sciences and medical sciences · 2010Article
- Site-specific protein adducts of 4-hydroxy-2(E)-nonenal in human THP-1 monocytic cells: protein carbonylation is diminished by ascorbic acid.Chemical research in toxicology · 2010Article
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Authors and funding
3 authors.
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Abstract
The identities of proteins that show disuse-related changes in the content of oxidative modification are unknown. Furthermore, it is unknown whether the global accumulation of oxidized proteins is greater in aged animals with muscle disuse. The purposes of this study are 1) to identify the exact proteins that show disuse-related changes in oxidation levels and 2) to test the hypothesis that the global accumulation of oxidized proteins with muscle disuse would be greater in aged animals. Adult and old rats were randomized into four groups: weight bearing and 3, 7, or 14 days of hindlimb unloading. Soleus muscles were harvested to investigate the protein oxidation with unloading. Slot blot, SDS-PAGE, and Western blot analyses were used to detect the accumulation of 4-hydroxy-2-nonenol (HNE)- and nitrotyrosine (NT)-modified proteins. Matrix-assisted laser desorption ionization-time of flight and tandem mass spectroscopy were used to identify modified proteins. We found that global HNE- and NT-modified proteins accumulated significantly with aging but not with muscle unloading. Two HNE and NT target proteins, four-and-a-half LIM protein 1 (FHL1) and carbonic anhydrase III (CAIII), showed changes in the oxidation levels with muscle unloading. The changes in the oxidation levels happened to adult rats but not old rats. However, old rats had higher baseline levels of HNE-modified FHL1. In summary, the data suggest that the muscle unloading-related changes of protein oxidation are more significant in specific proteins and that the changes are age related.
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