ECM is required for skeletal muscle differentiation independently of muscle regulatory factor expression

Centro de Regulación Celular y Patología, Departamento de Biología Celular y Molecular, Facultad de Ciencias Biológicas, Millennium Institute for Fundamental and Applied Biology, Pontificia Universidad Católica de Chile, Santiago, Chile Transcription of specific skeletal muscle genes requires the ex...

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Bibliographic Details
Published in:American Journal of Physiology: Cell Physiology 2002-02, Vol.282 (2), p.C383-C394
Main Authors: Osses, Nelson, Brandan, Enrique
Format: Article
Language:English
Subjects:
Animals
Biomarkers
Cell Differentiation - physiology
Cells, Cultured
Extracellular Matrix - drug effects
Extracellular Matrix - physiology
Glycosides - pharmacology
Mice
Muscle, Skeletal - cytology
Muscle, Skeletal - physiology
Myogenin - physiology
Proteoglycans - physiology
Transcription Factors - metabolism
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Summary:Centro de Regulación Celular y Patología, Departamento de Biología Celular y Molecular, Facultad de Ciencias Biológicas, Millennium Institute for Fundamental and Applied Biology, Pontificia Universidad Católica de Chile, Santiago, Chile Transcription of specific skeletal muscle genes requires the expression of the muscle regulatory factor myogenin. To assess the role of the extracellular matrix (ECM) in skeletal muscle differentiation, the specific inhibitors of proteoglycan synthesis, sodium chlorate and - D -xyloside, were used. Treatment of cultured skeletal muscle cells with each inhibitor substantially abolished the expression of creatine kinase and -dystroglycan. This inhibition was totally reversed by the addition of exogenous ECM. Myoblast treatment with each inhibitor affected the deposition and assembly of the ECM constituents glypican, fibronectin, and laminin. These treatments did not affect MyoD, MEF2A, and myogenin expression and nuclear localization. Differentiated myoblast treatment with RGDS peptides completely inhibited myogenesis without affecting the expression or nuclear localization of myogenin. Integrin-mediated signaling of focal adhesion kinase was partially inhibited by chlorate and - D -xyloside, an effect reversed by the addition of exogenous ECM gel. These results suggested that the expression of myogenin is not sufficient to successfully drive skeletal muscle formation and that ECM is required to complete the skeletal muscle differentiation process. myogenin; proteoglycans; extracellular matrix; proteoglycan inhibitors; satellite cells
ISSN:0363-6143
1522-1563
DOI:10.1152/ajpcell.00322.2001