Several dystrophin-glycoprotein complex members are present in crude surface membranes but they are sodium dodecyl sulphate invisible in KCl-washed microsomes from <Emphasis Type="Italic">mdx</Emphasis> mouse muscle |
| |
Authors: | Stéphanie Daval Chantal Rocher Yan Cherel Elisabeth Le Rumeur |
| |
Institution: | (1) Department of Biology, National University of Ireland, Maynooth, Co. Kildare, Ireland; |
| |
Abstract: | 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. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|