Laminin‐α2 but not ‐α1‐mediated adhesion of human (Duchenne) and murine (mdx) dystrophic myotubes is seriously defective

FEBS Letters

Angoli, Damiano²  Wanke, Enzo²  Mora, Marina¹  Baresi, Rita¹  Corona, Paola² 

[1] ‘C. Besta’ National Neurological Institute, Department of Neuromuscular Diseases, Via Celoria 11, I-20133 Milan, Italy;Department of General Physiology and Biochemistry, University of Milan, Via Celoria 26, I-20133 Milan, Italy

关键词: Duchenne dystrophy;    mdx myotube;    Merosin;    Laminin;    α-dystroglycan;   

DOI  :  10.1016/S0014-5793(97)00460-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

It has been suggested that α-dystroglycan links the dystrophin-associated protein complex and extracellular matrix and that the absence of dystrophin and α-dystroglycan in Duchenne muscular dystrophy (DMD) may lead to the breakdown of this linkage. In the present study, myotubes from DMD patients and murine X-linked muscular dystrophic mice (mdx) were used to measure their adhesive force to the physiological laminin-α2 substrate, and it was found that the dystrophic myotubes were selectively unable to sustain adhesion. However, normal and dystrophic myotubes attached equally well to the laminin-α1 substrate. As far as we know, this is the first experimental evidence that the absence of dystrophin causes the complete loss of a still unknown laminin-α2-dependent adhesion force, therefore suggesting that the primary consequence of Duchenne dystrophy consists of the loss of an authentic mechanical linkage at the level of the α-dystroglycan/basal lamina interface.

【 授权许可】

Unknown