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NEUROLOGY 1986;36:693
© 1986 American Academy of Neurology

Myosin light chains and muscle pathology

Giovanni Salviati, MD, Romeo Betto, MS, Daniela Danieli-Betto, MS, Enrico Biasia, M. Serena, MD, Massimo Mini, MD and Guglielmo Scarlato, MD

National Research Council Center for Muscle Biology and Physiopathology, Institute of General Pathology (Dr. Salviati. Mr. Betto. and Mr. Biasia). and Institute of Human Physiology (Ms. Danieli-Betto), University of Padua; and Divisione Neurologica (Dr. Serena), Ospedale Civile di Treviso, and Institute of Neurology (Drs. Mini and Scarlato), University of Milan, Italy.

We evaluated the isoform composition of heavy and light chains of myosin in single muscle fibers from patients with Duchenne dystrophy, myotonic dystrophy, or polymyositis. In all myopathic muscles, there was an increase in the proportion of intermediate fibers which, by analysis of myosin isoforms, fell into two subpopulations, one that contained both fast and slow myosin and another that contained myosin molecular hybrids. The increased proportion of intermediate (or transitional) fibers suggests changes in the equilibrium between fast and slow motor units. These changes could result from regeneration and subsequent maturation of fibers or from direct transformation of mature fibers of one type into the opposite.

Address correspondence and reprint requests to Dr. Salviati, N.R.C. Center for Muscle Biology and Physiopathology. Institute of General Pathology, University of Padua, Via Loredan 16, 35131 Padua, Italy.

Supported by institutional funds from the Consiglio Nazionale delle Ricerche to the N.R.C. unit for Muscle Biology and Physiopathology. and by grants from the Ministero della Pubblica Istruzione.

Accepted for publication September 20, 1985.






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