Abstract |
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.
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Authors | D Angoli, P Corona, R Baresi, M Mora, E Wanke |
Journal | FEBS letters
(FEBS Lett)
Vol. 408
Issue 3
Pg. 341-4
(May 26 1997)
ISSN: 0014-5793 [Print] England |
PMID | 9188790
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Cytoskeletal Proteins
- DAG1 protein, human
- Laminin
- Membrane Glycoproteins
- Receptors, Laminin
- laminin alpha 2
- Dystroglycans
- laminin A
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Topics |
- Animals
- Cell Adhesion
- Cells, Cultured
- Cytoskeletal Proteins
(physiology)
- Dystroglycans
- Extracellular Matrix
(physiology)
- Humans
- Laminin
(physiology)
- Membrane Glycoproteins
(physiology)
- Mice
- Mice, Inbred mdx
- Muscle Fibers, Skeletal
(physiology)
- Muscle, Skeletal
(physiology, physiopathology)
- Muscular Dystrophies
(physiopathology)
- Muscular Dystrophy, Animal
(genetics, physiopathology)
- Receptors, Laminin
(physiology)
- Reference Values
- Stress, Mechanical
- X Chromosome
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