Biopolym. Cell. 2011; 27(5):359-363.
http://dx.doi.org/10.7124/bc.000123
FSHD myoblasts fail to downregulate intermediate filament protein vimentin during myogenic differentiation
1Dmitriev P. V., 1Barat A. L., 1Cochet E., 1Ogryzko V. V., 2Laoudj-Chenivesse D., 1Lipinski M., 1Vassetzky Y. S.
  1. CNRS UMR 8126, Universit Paris-Sud 11, Institut Gustave Roussy
    114, rue Edouard Vaillant, Villejuif, France, 94805
  2. Inserm U1046, Universite Montpellier 1, Universite Montpellier 2
    371 Avenue du Doyen G. Giraud, Montpellier, France, 34295

Abstract

Facioscapulohumeral muscular dystrophy (FSHD) is an autosomal dominant hereditary neuromuscular disorder. The clinical features of FSHD include weakness of the facial and shoulder girdle muscles followed by wasting of skeletal muscles of the pelvic girdle and lower extremities. Although FSHD myoblasts grown in vitro can be induced to differentiate into myotubes by serum starvation, the resulting FSHD myotubes have been shown previously to be morphologically abnormal. Aim. In order to find the cause of morphological anomalies of FSHD myotubes we compared in vitro myogenic differentiation of normal and FSHD myoblasts at the protein level. Methods. We induced myogenic differentiation of normal and FSHD myoblasts by serum starvation. We then compared protein extracts from proliferating myoblasts and differentiated myotubes using SDS-PAGE followed by mass spectrometry identification of differentially expressed proteins. Results. We demonstrated that the expression of vimentin was elevated at the protein and mRNA levels in FSHD myotubes as compared to normal myotubes. Conclusions. We demonstrate for the first time that in contrast to normal myoblasts, FSHD myoblasts fail to downregulate vimentin after induction of in vitro myogenic differentiation. We suggest that vimentin could be an easily detectable marker of FSHD myotubes.
Keywords: FSHD, vimentin, myogenic differentiation, proteomics
Full text: (PDF, in English)

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