| First Author | Angoli D | Year | 1997 |
| Journal | FEBS Lett | Volume | 408 |
| Issue | 3 | Pages | 341-4 |
| PubMed ID | 9188790 | Mgi Jnum | J:40762 |
| Mgi Id | MGI:892128 | Doi | 10.1016/s0014-5793(97)00460-2 |
| Citation | Angoli D, et al. (1997) Laminin-alpha2 but not -alpha1-mediated adhesion of human (Duchenne) and murine (mdx) dystrophic myotubes is seriously defective. FEBS Lett 408(3):341-4 |
| abstractText | It has been suggested that alpha-dystroglycan links the dystrophin-associated protein complex and extracellular matrix and that the absence of dystrophin and alpha-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-alpha2 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-alpha1 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-alpha2-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 alpha-dystroglycan/basal lamina interface. |
