Comparative proteomic analysis of myotube caveolae after milli-calpain deregulation |
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Authors: | Goudenege Sébastien Dargelos Elise Claverol Stéphane Bonneu Marc Cottin Patrick Poussard Sylvie |
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Institution: | Université Bordeaux I, USC-INRA 2009, Unité Protéolyse, Croissance et Développement Musculaire, ISTAB, Talence, France. |
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Abstract: | Caveolae are specialised RAFTs (detergent-resistant membrane microdomains enriched in cholesterol and glycosphingolipids). Caveolin, the main caveolae protein, is essential to the organisation of proteins and lipids, and interacts with numerous mediating proteins through a 'Caveolin Scalfolding Domain'. Consequently, caveolae play a major role in signal transduction and appear to be veritable signalling platforms. In muscle cells, caveolae are essential for fusion and differentiation, and are also implicated in a type of muscular dystrophy (LGMD1C). In a preceding work, we demonstrated the presence of active milli-calpain (m-calpain) in myotube caveolae. Calpains are calcium-dependent proteases involved in several cellular processes, including myoblast fusion and migration, PKC-mediated intracellular signalling and remodelling of the cytoskeleton. For the first time, we have proved the cholesterol-dependent localisation of m-calpain in the caveolae of C(2)C(12) myotubes. Calpain-dependent caveolae involvement in myoblast fusion was also strongly suggested. Furthermore, eight differentially expressed caveolae associated proteins were identified by 2-DE and LC-MS/MS analyses using an m-calpain antisense strategy. This proteomic study also demonstrates the action of m-calpain on vimentin, desmin and vinculin in myotube caveolae and suggests m-calpain's role in several mitochondrial pathways. |
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Keywords: | Calpain Caveolae Cytoskeletal proteins Mitochondrial proteins Myotubes |
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