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NEUROLOGY 1982;32:37
© 1982 American Academy of Neurology

Fast to slow change of myosin in nemaline myopathy

Electrophoretic and immunologic evidence

Pompeo Volpe, M.D., Ernesto Damiani, M.D., Alfredo Margreth, M.D., Giulio Pellegrini, M.D. and Guglielmo Scarlato, M.D.

National Research Council Center for Muscle Biology and Physiopathology, Institute of General Pathology (Drs. Volpe, Damiani, and Margreth), University of Padova, Padova, and the Institute of Neurology (Drs. Pellegrini and Scarlato), University of Milano, Milano, Italy.

Muscle biopsies from two familial and one sporadic case with congenital nemaline myopathy and seven healthy family members were examined for myosin composition. Myosin was characterized with respect to light chain (LC) composition by one-dimensional and two-dimensional electrophoresis, and by immunologic methods (enzyme-linked immunosorbent assay [ELISA]), using specific antibody for rabbit fast myosin LC1 (LC1F). Type I fiber predominance was associated with the substitution of a hybrid, predominantly "slow" to a virtually pure "slow" myosin LC pattern for the "mixed" pattern found with myosin of normal muscle. Muscle myosin from the relatives had apparently normal light chain composition.

Address correspondence and reprint requests to Dr. Margreth, N.R.C. Center for Muscle Biology and Physiopathology, Institute of General Pathology, University of Padova, Via Loredan 16, 35100 Padova, Italy.

This work was supported by funds from the Consiglio Nazionale delle Ricerche. Dr. Volpe has a postdoctoral fellowship from the "Dino Ferrari" Foundation.

Accepted for publication June 17, 1981.




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