Premium
Comparative proteomic analysis of myotube caveolae after milli‐calpain deregulation
Author(s) -
Goudenege Sébastien,
Dargelos Elise,
Claverol Stéphane,
Bonneu Marc,
Cottin Patrick,
Poussard Sylvie
Publication year - 2007
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200700124
Subject(s) - caveolae , calpain , microbiology and biotechnology , lipid raft , caveolin , biology , caveolin 3 , myogenesis , myocyte , cytoskeleton , signal transduction , biochemistry , cell , enzyme
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.