Abstract
The way in which genes specify the ordered appearance of contractile and regulatory proteins in differentiating muscle cells is an important problem in developmental biology. The existence of easily detectable markers of cell differentiation at every stage of myogenesis, the ease with which myoblasts can be grown in vitro, and the fact that muscle is an electrically excitable tissue combine to make skeletal muscle a rich model system for studying many aspects of cell differentiation in higher organisms. The potential for muscle cell development exists in DNA molecules that contain the appropriate sequences. The actual genesis of a myotube, however, requires regulated transcription of the DNA sequences into mRNA, and controlled translation of the mRNA into proteins. Investigators who have begun to attack these interrelated processes experimentally have seen similarities in the behavior of many muscle genes. For example, the genes coding for actin, myosin heavy chains, myosin light chains, troponins, tropomyosin, creatine kinase, and aldolase, all have more than one nonidentical copy per haploid genome. That is, they exist as small gene families with each member of a family encoding a slight variant (isoform) of the family gene. In most cases, the isoforms are expressed differently during development, both in time and tissue distribution. For example, during skeletal myogenesis, α-actin, creatine kinase M, aldolase A4, and adult type myosin heavy and light chains are “switched on” and actively expressed, while embryonic myosins, β- and γ-actin, creatine kinase B, and aldolase C are all “switched off” and no longer synthesized.
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Schwartz, R.J., Stone, E.M. (1983). Cloning of Contractile Protein Genes. In: Dowben, R.M., Shay, J.W. (eds) Cell and Muscle Motility. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9296-9_7
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