Abstract
The ultrastructure and mode of existence of the dystrophin molecule and its relations to actin filaments were examined in murine skeletal myofibers. Electron microscopy of freeze-etched replicas of goldlabelled dystrophin molecules in quick-freeze, deepetch, rotary-shadow preparations revealed rod-like structures 108.2±16.3 nm long and 3.1±1.5 nm thick. Some dystrophin molecules appeared to link their ends to form anastomosing networks; others were separate from each other. The dystrophin molecules were parallel or nearly parallel to the inner surface of the muscle plasma membrane. Double immuno-labelling transmission electron microscopy using N- and C-terminal dystrophin antibodies showed that the group mean distances of the N- and C-terminal signals from the muscle plasma membrane were 52.7±8.1 nm and 45.9±11.3 nm, respectively, which were not significantly different. Histograms of the distribution of the N- and C-terminal distances from the muscle plasma membrane had similar patterns with peaks 10∼20 nm from the membrane. This was consistent with the findings of the mode of existence of dystrophin molecules seen in freeze-etched replicas. Finally, the dystrophin molecules were linked with the most peripheral sarcoplasmic actin like filaments, end to side as well as end to end.
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Supported by a grant (2A-2) from the National Center for Nervous, Mental and Muscular Disorders of the Ministry of Heath and Welfare, Japan
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Wakayama, Y., Shibuya, S., Jimi, T. et al. Size and localization of dystrophin molecule: immunoelectron microscopic and freeze etching studies of muscle plasma membranes of murine skeletal myofibers. Acta Neuropathol 86, 567–577 (1993). https://doi.org/10.1007/BF00294294
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DOI: https://doi.org/10.1007/BF00294294