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Department of Animal Sciences, Ohio Agricultural Research and Development Center, The Ohio State University, Wooster 44691
1 Correspondence: phone: 330-263-3905; fax: 330-263-3949; E-mail: velleman.1{at}osu.edu.
Abstract
Skeletal muscle fibers are surrounded by an extracellular matrix. The extracellular matrix forms a complex dynamic architecture and is composed of glycoproteins, collagen, and proteoglycans. Proteoglycans have been suggested to play an important functional role in tissue differentiation. Proteoglycans affect the myogenic process by regulating collagen fibrillo-genesis, modulating cell growth and the response to growth factors. The extracellular matrix communicates information back to the cell through integrin receptors. Integrins are heterodimeric transmembrane glycoproteins that contain extracellular, transmembrane, and cytoplasmic domains. During myogenesis, integrins play a role in both cell ahesion to the extracellular matrix and sarcomere formation. Therefore, the regulation of myoblast integrin temporal and spatial expression is critical in the formation of differentiated muscle. Although specific extracellular matrix components have been identified as being essential in myogenesis, the exact functions of these macromolecular proteins as they relate to muscle formation and growth is still not well understood.
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