Dystrophin is not essential for the integrity of the cytoskeleton

R. Massa, L. Castellani, G. Silvestri, G. Sancesario, G. Bernardi

Research output: Contribution to journalArticle

Abstract

Dystrophin is localized, in normal muscle fibers, on the cytoplasmic surface of the sarcolemma. The function of this protein is not known but, according to its structure and intracellular distribution, it seems likely that dystrophin interacts with other cytoskeletal proteins to form a complex linkage between myofibrils, sarcolemma and extracellular matrix. To evaluate the possibility that dystrophin deficiency induces, per se, a disarray in the cytoskeleton, we studied three components of this structure in muscle fibers of the dystrophic mdx mouse in a phase preceding the onset of necrosis. Vinculin, abundant in sarcolemmal structures called costameres, desmin, the principal component of intermediate filaments and nebulin, constituent of the socalled "third filament" within the sarcomere, were stained with the indirect immunofluorescence technique in cryostat sections. The same monoclonal antibodies were used in Western blots of proteins extracted from the same muscles. No difference was observed in the distribution or in the relative abundance of the three proteins, comparing muscles from 18 days-old mdx and control mice. Our results indicate that the lack of dystrophin does not induce, per se, alterations in the structures linking the sarcolemma to the contractile apparatus. It is likely that the structural damage in dystrophin-less muscle fibers is initially confined to limited portions of the plasma membrane. These focal lesions, impairing intracellular calcium homeostasis, can lead to muscle fiber necrosis.

Original languageEnglish
Pages (from-to)377-384
Number of pages8
JournalActa Neuropathologica
Volume87
Issue number4
DOIs
Publication statusPublished - Apr 1994

Fingerprint

Dystrophin
Cytoskeleton
Sarcolemma
Muscles
Inbred mdx Mouse
Costameres
Necrosis
Vinculin
Sarcomeres
Cytoskeletal Proteins
Desmin
Intermediate Filaments
Muscle Proteins
Myofibrils
Indirect Fluorescent Antibody Technique
Extracellular Matrix
Proteins
Homeostasis
Western Blotting
Monoclonal Antibodies

Keywords

  • Desmin
  • mdx mouse
  • Muscular dystrophy
  • Nebulin
  • Vinculin

ASJC Scopus subject areas

  • Neuroscience(all)
  • Pathology and Forensic Medicine
  • Clinical Neurology

Cite this

Massa, R., Castellani, L., Silvestri, G., Sancesario, G., & Bernardi, G. (1994). Dystrophin is not essential for the integrity of the cytoskeleton. Acta Neuropathologica, 87(4), 377-384. https://doi.org/10.1007/BF00313607

Dystrophin is not essential for the integrity of the cytoskeleton. / Massa, R.; Castellani, L.; Silvestri, G.; Sancesario, G.; Bernardi, G.

In: Acta Neuropathologica, Vol. 87, No. 4, 04.1994, p. 377-384.

Research output: Contribution to journalArticle

Massa, R, Castellani, L, Silvestri, G, Sancesario, G & Bernardi, G 1994, 'Dystrophin is not essential for the integrity of the cytoskeleton', Acta Neuropathologica, vol. 87, no. 4, pp. 377-384. https://doi.org/10.1007/BF00313607
Massa R, Castellani L, Silvestri G, Sancesario G, Bernardi G. Dystrophin is not essential for the integrity of the cytoskeleton. Acta Neuropathologica. 1994 Apr;87(4):377-384. https://doi.org/10.1007/BF00313607
Massa, R. ; Castellani, L. ; Silvestri, G. ; Sancesario, G. ; Bernardi, G. / Dystrophin is not essential for the integrity of the cytoskeleton. In: Acta Neuropathologica. 1994 ; Vol. 87, No. 4. pp. 377-384.
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