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. 2010 Oct 11;2011:810242. doi: 10.1155/2011/810242

Table 2.

Summary of the models used and of the major findings obtained by applying proteomic approaches to the study of the ageing skeletal muscle.

Authors Experimental model Proteomic analysis Identified affected pathways and major findings
Mouse

Chang et al., 2003 [39] 18-months-old C57B16 mice. Studied tissue: skeletal muscle. Two-dimensional polyacrilamide gel electrophoresis. Reproducibility of the 2-D PAGE system.

Rats

Cai et al., 2000 [35] 12-, 18-, and 24-months-old rats.Studied tissue: extensor digitorum longus muscle and soleus muscle. Two-dimensional gel electrophoresis. Analysis of aqueous proteins of skeletal muscle during aging.
Cai et al., 2001 [40] 8-, 18-, and 24-months-old rats.Studied tissue: extensor digitorum longus muscle and soleus muscle. Two-dimensional gel electrophoresis. Analysis of parvalbumin expression in rat skeletal muscles.
Kanski et al., 2003 [31] 4- and -24 months old Fisher 344 rats and -6 and -34 months old Fisher 344/BN F1 rats.Studied tissue: skeletal muscle. 2-D gel electrophoresis, Western blot analysis, MALDI-TOF MS and ESI-MS/MS analysis. Age-dependent nitration in muscle energy metabolism.
Piec et al., 2005 [36] 7-, 18- and 30-months-old LOU/c/jall rats.Studied tissue: gastrocnemius muscle. Two-dimensional gel electrophoresis, MALDI-ToF MS analyses, and immunoblotting. Myofibrillar regulatory proteins, signal transduction, cytosolic and mitochondrial energy metabolisms, oxidative stress, detoxification, and RNA metabolism.
Kanski et al., 2005 [32] 34-months-old Fisher 344/Brown Norway F1 hybrid rats.Studied tissue: skeletal muscle. 2-D gel electrophoresis, Western Blot analysis, MALDI-TOF and NSI-MS/MS analysis. Proteomic analysis of protein nitration.
Dencher et al., 2006 [41] Studied tissue: skeletal muscle. Blue-native/colorless-native gel electrophoresis, 2D-SDS-PAGE and MALDI MS. Cellular dysfunction, ageing, and cellular death.
O'Connell et al., 2007 [37] 3- and 30-months-old rat. Studied tissue: gastrocnemius muscle Two-dimensional gel electrophoresis, MALDI-ToF, DALT-Twelve gel electrophoretic separation system, 2-D immunoblotting. Proteomic profiling of senescent fibres: stress response, contractile apparatus, and metabolic regulation.
Altun et al., 2007 [29] 4- and 30-months old rats.Studied tissue: gastrocnemius muscle. Two-dimensional gel electrophoresis, MALDI-ToF/ToF, MALDI-MS/MS, ESI-LC-MS/MS and Western Blot analysis. Redox homeostasis, iron load, regulation of contractile proteins, glycolisis, and oxidative phosphorylation.
O'Connell et al., 2008 [33] 3- and 30-months old rats. Studied tissue: gastrocnemius muscle Two-dimensional gel electrophoresis, MALDI-ToF MS analysis. Proteomic profiling of senescent fibers.
Gannon et al., 2008 [30] 3- and -30-months old rats.Studied tissue: gastrocnemius muscle. Two-dimensional gel electrophoresis, MALDI-ToF MS analysis. Phosphoproteomic analysis of aged skeletal muscle.
Feng et al., 2008 [42] 12- and 26-months-old Fischer 344 rats.Studied tissue: soleus, semimembranosus, plantaris, extensor digitorum longus, and tibialis anterior muscles. SDS-polyacrylamide gel electrophoresis, μLC-ESI MS/MS analysis and Ingenuity Systems Analysis. Carbonyl modifications, cellular function and maintenance, fatty acid metabolism, and citrate cycle.
Lombardi et al., 2009 [26] 3- and 24-months-old rats.Studied tissue: gastrocnemius muscle. Two-dimensional gel electrophoresis, Blue-Native PAGE, and MALDI-ToF MS analysis. Energy metabolism, mitochondrial pathways, myofibrillar filaments, and detoxification.

Human

Cobon et al., 2002 [43] 56–79 yr of age.Studied tissue: vastus lateralis muscle. Two-dimensional polyacrilamide gel electrophoresis and MALDI-TOF MS. Human aged skeletal muscle protein profile.
Gelfi et al., 2006 [34] Elderly and young subjects.Studied tissue: vastus lateralis muscle. Two-dimensional difference gel electrophoresis, SDS-PAGE and ESI-MS/MS. Elderly group: downregulation of regulatory myosin light chains, (phosphorylated isoforms), higher proportion of myosin heavy chain isoforms 1 and 2A, and enhanced oxidative and reduced glycolytic capacity.