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Articles in PresS, published online ahead of print October 3, 2001
Am J Physiol Cell Physiol, 10.1152/ajpcell.00322.2001
Submitted on July 17, 2001
Accepted on December 31, 1969
1 Cell and Molecular Biology, Catholic University of Chile, Santiago, Chile
* To whom correspondence should be addressed. E-mail: ebrandan{at}genes.bio.puc.cl.
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 ß-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 reverted by the addition of exogenous ECM. Myoblasts 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 myoblasts 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 ß-D-Xyloside, an effect reverted by the addition of exogenous ECM gel. These results suggested that the expression of myogenin was not sufficient to successfully drive skeletal muscle formation and that ECM was required to complete the skeletal muscle differentiation process.
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