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Laminin‐α2 but not ‐α1‐mediated adhesion of human (Duchenne) and murine ( mdx ) dystrophic myotubes is seriously defective
Author(s) -
Angoli Damiano,
Corona Paola,
Baresi Rita,
Mora Marina,
Wanke Enzo
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00460-2
Subject(s) - laminin , duchenne muscular dystrophy , dystroglycan , dystrophin , myogenesis , basal lamina , utrophin , microbiology and biotechnology , muscular dystrophy , extracellular matrix , adhesion , mdx mouse , chemistry , biology , myocyte , anatomy , genetics , ultrastructure , organic chemistry
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.