Fiche publication
Date publication
décembre 2003
Journal
Biology of the cell
Auteurs
Membres identifiés du Cancéropôle Est :
Pr DEDIEU Stéphane
Tous les auteurs :
Dedieu S, Mazères G, Poussard S, Brustis JJ, Cottin P
Lien Pubmed
Résumé
Calpains, also called calcium activated neutral cysteine proteases are presently known to play pivotal roles in physiological and biological phenomena such as signal transduction, cell spreading and motility, apoptosis, regulation of cell cycle and regulation of muscle cell differentiation. Concerning this last point, calpains have been shown to play a crucial role during the earlier myogenesis. In this study we have analyzed the involvement of calpains during an important step of myogenesis: myoblast migration. Our findings show that myoblast migration was drastically reduced when the expression of micro- and m-calpain was decreased. We have also observed that MARCKS (myristoylated alanine rich C kinase substrate), a protein localized at focal adhesion sites, was significantly accumulated when the expression levels of calpains were decreased. Also, using phorbol myristate acetate, (an activator of PKC) and plasmids carrying the full-length cDNA of MARCKS or a cDNA fragment lacking the phosphorylation site domain, we demonstrated that normal myoblast migration is dependent on MARCKS phosphorylation and localization.
Mots clés
Animals, Antibodies, pharmacology, Binding Sites, genetics, Calpain, genetics, Cell Line, Cell Movement, drug effects, Immunoblotting, Intracellular Signaling Peptides and Proteins, Lipoproteins, genetics, Membrane Proteins, genetics, Mutation, Myoblasts, Skeletal, cytology, Oligodeoxyribonucleotides, Antisense, genetics, Phosphorylation, Tetradecanoylphorbol Acetate, pharmacology
Référence
Biol. Cell. 2003 Dec;95(9):615-23
