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

Damiano Angoli, Paola Corona, Rita Baresi, Marina Mora, Enzo Wanke

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)341-344
Number of pages4
JournalFEBS Letters
Issue number3
Publication statusPublished - May 26 1997


  • α-Dystroglycan
  • Duchenne dystrophy
  • Laminin
  • mdx myotube
  • Merosin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


Dive into the research topics of 'Laminin-α2 but not -α1-mediated adhesion of human (Duchenne) and murine (mdx) dystrophic myotubes is seriously defective'. Together they form a unique fingerprint.

Cite this