Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix
Copyright policy )Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix
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.
- Howard Hughes Medical Institute United States
- University of Iowa United States
- The University of Texas Southwestern Medical Center United States
Membrane Glycoproteins, Base Sequence, Muscles, Recombinant Fusion Proteins, Immunoblotting, Molecular Sequence Data, Restriction Mapping, Gene Expression, Muscular Dystrophies, Extracellular Matrix, Dystrophin, Molecular Weight, Cytoskeletal Proteins, Animals, Humans, Amino Acid Sequence, Laminin, RNA, Messenger, Cloning, Molecular, Dystroglycans
Membrane Glycoproteins, Base Sequence, Muscles, Recombinant Fusion Proteins, Immunoblotting, Molecular Sequence Data, Restriction Mapping, Gene Expression, Muscular Dystrophies, Extracellular Matrix, Dystrophin, Molecular Weight, Cytoskeletal Proteins, Animals, Humans, Amino Acid Sequence, Laminin, RNA, Messenger, Cloning, Molecular, Dystroglycans
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