Service Communautaire d'Information sur la Recherche et le Développement - CORDIS

Evaluation of aged human skeletal muscle

In order to extend the animal studies to human skeletal muscle, we have determined whether potential changes in the relative expression of the voltage sensor occur in senescent human fibres. Besides small inter-individual variations in expression levels, the microsomal immunoblot analysis of vastus lateralis autopsy specimens from male humans aged 18 to 82 years of age showed no major changes in the relative abundance of the dihydropyridine receptor, fast calsequestrin and the slow/fast myosin heavy chains. The oligomeric status of the a1S-dihydropyridine receptor was unaltered in aged human fibres.

One potential way forward is the use of proteomics research tools such as the global comparative survey of mature versus aged muscle protein complement using 2D gel electrophoresis in combination with mass spectrometry. Depending on the availability of proteomics equipment, such an analysis is planned for the next 3 years. This should lead to the identification of novel candidate proteins involved in the molecular pathogenesis of sarcopenia of old age and such data can then be complemented with detailed biomedical studies into the mechanism of age-related muscle weakness.

Reported by

National University of Ireland
Maynooth, Co.