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Proteomic study of calpain interacting proteins during skeletal muscle aging.

Authors: Brulé, C  Dargelos, E  Diallo, R  Listrat, A  Béchet, D  Cottin, P  Poussard, S 
Citation: Brulé C, etal., Biochimie. 2010 Dec;92(12):1923-33. doi: 10.1016/j.biochi.2010.09.003. Epub 2010 Sep 17.
Pubmed: (View Article at PubMed) PMID:20850499
DOI: Full-text: DOI:10.1016/j.biochi.2010.09.003

Aging is associated with a progressive and involuntary loss of muscle mass also known as sarcopenia. This condition represents a major public health concern. Although sarcopenia is well documented, the molecular mechanisms of this condition still remain unclear. The calcium-dependent proteolytic system is composed of calcium-dependent cysteine proteases named calpains. Calpains are involved in a large number of physiological processes such as muscle growth and differentiation, and pathological conditions such as muscular dystrophies. The aim of this study was to determine the involvement of this proteolytic system in the phenotype associated with sarcopenia by identifying key proteins (substrates or regulators) interacting with calpains during muscle aging. Immunoprecipitations coupled with proteomic analyses and protein identification by mass spectrometry have been undertaken. Reverse co-immunoprecipitation, cellular colocalisation by confocal microscopy and calpain-dependent in vitro proteolysis of several of the identified proteins have been also carried out. We identified ATP synthase subunit alpha and alpha actinin 3 as key partners of calpains during muscle aging. Such interactions would suggest that calpains are implicated in many processes altered during aging including cytoskeletal disorganisation and mitochondrial dysfunction.

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CRRD Object Information
CRRD ID: 13703063
Created: 2018-07-31
Species: All species
Last Modified: 2018-07-31
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.