Journal
EXPERIMENTAL CELL RESEARCH
Volume 317, Issue 14, Pages 2059-2071Publisher
ELSEVIER INC
DOI: 10.1016/j.yexcr.2011.05.020
Keywords
Mitochondria; Calcineurin; Myoblasts; Differentiation; Myosin heavy chains; Contractile type
Categories
Funding
- INRA (Institut National de Recherche Agronomique)
- Action Transversale - Fonction Mitochondria le et Biologie du Muscle (INRA)
- ARC (Association pour la Recherche contre le Cancer)
- AFM (Association Francaise contre les Myopathies)
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We have previously shown that mitochondrial protein synthesis regulates myoblast differentiation, partly through the control of c-Myc expression, a cellular oncogene regulating myogenin expression and myoblast withdrawal from the cell cycle. In this study we provide evidence of the involvement of Calcineurin in this regulation. In C2C12 myoblasts, inhibition of mitochondrial protein synthesis by chloramphenicol decreases Calcineurin expression. Conversely, stimulation of this process by overexpressing the T3 mitochondrial receptor (p43) increases Calcineurin expression. Moreover, expression of a constitutively active Calcineurin (Delta CN) stimulates myoblast differentiation, whereas a Calcineurin antisense has the opposite effect. Lastly, Delta CN expression or stimulation of mitochondrial protein synthesis specifically increases slow myosin heavy chain expression. In conclusion, these data clearly suggest that, partly via Calcineurin expression, mitochondrial protein synthesis is involved in muscle development through the control of myoblast differentiation and probably the acquisition of the contractile and metabolic phenotype of muscle fibres. (C) 2011 Elsevier Inc. All rights reserved.
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