Several dystrophin-glycoprotein complex members are present in crude surface membranes but they are sodium dodecyl sulphate invisible in KCI-washed microsomes from mdx mouse muscle

• Autorzy: Daval S , Rocher C. , Cherel Y. , Rumeur E.
• Języki publikacji: EN

Abstrakty

EN

The dystrophin-glycoprotein complex (DGC) is a large trans-sarcolemmal complex that provides a linkage between the subsarcolemmal cytoskeleton and the extracellular matrix. In skeletal muscle, it consists of the dystroglycan, sarcoglycan and cytoplasmic complexes, with dystrophin forming the core protein. The DGC has been described as being absent or greatly reduced in dystrophin-deficient muscles, and this lack is considered to be involved in the dystrophic phenotype. Such a decrease in the DGC content was observed in dystrophin-deficient muscle from humans with muscular dystrophy and in mice with X-linked muscular dystrophy (mdx mice). These deficits were observed in total muscle homogenates and in partially membrane-purified muscle fractions, the so-called KCl-washed microsomes. Here, we report that most of the proteins of the DGC are actually present at normal levels in the mdx mouse muscle plasma membrane. The proteins are detected in dystrophic animal muscles when the immunoblot assay is performed with crude surface membrane fractions instead of the usually employed KCl-washed microsomes. We propose that these proteins form SDS-insoluble membrane complexes when dystrophin is absent.

Słowa kluczowe

EN

dystrophin-glycoprotein complex; crude surface membrane; sodium dodecyl sulphate; washed microsome; mouse; mice; muscle; dystrophin-associated glycoprotein; muscular dystrophy; skeletal muscle

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 2010
• Tom: 15
• Numer: 1
• Opis fizyczny: p.134-152,fig.,ref.

Twórcy

autor

Daval S

• Ecole Nationale Veterinaire de Nantes, Atlanpole - La Chantrerie, BP 40706, Nantes, 44307 France

autor

Rocher C.

autor

Cherel Y.

autor

Rumeur E.

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