Abstract
Dystrophin, the protein product of the Duchenne muscular dystrophy (DMD) gene, is associated with a large oligomeric complex of sarcolemmal glycoproteins, including dystroglycan which provides a linkage to the extracellular matrix component, laminin. In patients with DMD, the absence of dystrophin leads to the loss in all of the dystrophin-associated proteins, causing the disruption of the linkage between the subsarcolemmal cytoskeleton and the extracellular matrix. This may render the sarcolemma vulnerable to physical stress. These recent developments in the research concerning the function of the dystrophin-glycoprotein complex pave a way for the better understanding of the pathogenesis of muscular dystrophies.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Animals
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Cytoskeletal Proteins / genetics
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Cytoskeletal Proteins / metabolism
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Dystroglycans
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Dystrophin / genetics*
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Dystrophin / metabolism*
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Extracellular Matrix / metabolism
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Glycoproteins / genetics
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Glycoproteins / metabolism*
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Humans
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Laminin / metabolism
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Membrane Glycoproteins / genetics
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Membrane Glycoproteins / metabolism
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Membrane Proteins*
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Mice
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Mice, Transgenic
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Muscular Dystrophies / diagnosis
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Muscular Dystrophies / genetics*
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Muscular Dystrophies / metabolism*
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Muscular Dystrophies / therapy
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Muscular Dystrophy, Animal / genetics
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Muscular Dystrophy, Animal / metabolism*
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Muscular Dystrophy, Animal / therapy
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Sarcoglycans
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Sarcolemma / metabolism
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Utrophin
Substances
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Cytoskeletal Proteins
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DAG1 protein, human
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Dystrophin
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Glycoproteins
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Laminin
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Membrane Glycoproteins
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Membrane Proteins
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Sarcoglycans
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Utrn protein, mouse
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Utrophin
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Dystroglycans