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Fetus‐like dystrophin expression and other cytoskeletal protein abnormalities in centronuclear myopathies
Author(s) -
Mora Marina,
Morandi Lucia,
Merlini Luciano,
Vita Giuseppe,
Baradello Alice,
Barresi Rita,
Di Blasi Claudia,
Blasevich Flavia,
Gebbia Marinella,
Daniel Sergio,
Cornelio Ferdinando
Publication year - 1994
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.880171008
Subject(s) - vinculin , spectrin , dystrophin , utrophin , cytoskeleton , biology , microbiology and biotechnology , dystroglycan , sarcolemma , intermediate filament , desmin , muscular dystrophy , pathology , myopathy , myocyte , medicine , genetics , cell , vimentin , laminin , immunohistochemistry , extracellular matrix
We have investigated supposed maturational arrest of muscle in ceatronuclear myopathies (CNMs) by characterizing the expression of dystrophin, other cytoskeletal proteins, and fetal myosin in the muscle fibers of 9 CNM patients (4 sporadic, 3 familial, 2 adult sporadic). Dystrophin and β‐spectrin localized intracytoplasmically in centrally nucleated fibers. Talin and vinculin were normally expressed. Desmin was radially organized in several fibers in all patients. Scattered vimentin positive fibers were found in 3 cases. Six myotonic dystrophy cases and 4 inflammatory myopathy cases with regenerating fibers were also studied: dystrophin and the membrane cytoskeletal proteins were normally expressed in the former; and dystrophin, spectrin, and vinculin were reduced in the latter. Intracytoplasmic dystrophin is further evidence of maturational arrest in CNMs. Spectrin and dystrophin codistnbute in these pathological conditions as in normal muscle. We conclude that the altered cytoskeletal network found in CNMs likely plays a pathogenetic role in these conditions. © 1994 John Wiley & Sons, Inc.