Abstract
The primary sequence of two components of the dystrophin-glycoprotein complex has been established by complementary, DNA cloning. The transmembrane 43K and extracellular 156K dystrophin-associated glycoproteins (DAGs) are encoded by a single messenger RNA and the extracellular 156K DAG binds laminin. Thus, the 156K DAG is a new laminin-binding glycoprotein which may provide a linkage between the sarcolemma and extracellular matrix. These results support the hypothesis that the dramatic reduction in the 156K DAG in Duchenne muscular dystrophy leads to a loss of a linkage between the sarcolemma and extracellular matrix and that this may render muscle fibres more susceptible to necrosis.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Cloning, Molecular
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Cytoskeletal Proteins / chemistry*
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Cytoskeletal Proteins / genetics
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Cytoskeletal Proteins / metabolism
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Dystroglycans
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Dystrophin / metabolism*
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Extracellular Matrix / metabolism*
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Gene Expression
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Humans
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Immunoblotting
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Laminin / metabolism
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Membrane Glycoproteins*
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Molecular Sequence Data
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Molecular Weight
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Muscles / chemistry
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Muscles / metabolism
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Muscular Dystrophies / genetics
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Muscular Dystrophies / metabolism*
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RNA, Messenger / analysis
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Recombinant Fusion Proteins
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Restriction Mapping
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Sarcolemma / metabolism*
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Tissue Distribution
Substances
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Cytoskeletal Proteins
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DAG1 protein, human
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Dystrophin
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Laminin
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Membrane Glycoproteins
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RNA, Messenger
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Recombinant Fusion Proteins
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Dystroglycans