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Science 15 February 1985:
Vol. 227. no. 4688, pp. 780 - 782
DOI: 10.1126/science.3969567
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Articles

Science, Vol 227, Issue 4688, 780-782
Copyright © 1985 by American Association for the Advancement of Science

articles

Continued expression of neonatal myosin heavy chain in adult dystrophic skeletal muscle

E Bandman

The expression of myosin heavy chain isoforms was examined in normal and dystrophic chicken muscle with a monoclonal antibody specific for neonatal myosin. Adult dystrophic muscle continued to contain neonatal myosin long after it disappeared from adult normal muscle. A new technique involving western blotting and peptide mapping demonstrated that the immunoreactive myosin in adult dystrophic muscle was identical to that found in neonatal normal muscle. Immunocytochemistry revealed that all fibers in the dystrophic muscle failed to repress neonatal myosin heavy chain. These studies suggest that muscular dystrophy inhibits the myosin gene switching that normally occurs during muscle maturation.


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