Journal ArticleDOI
Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle.
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It is shown that four glycoproteins are integral components of the dystrophin complex and that the concentration of one of these is greatly reduced in DMD patients, suggesting the reduction in this glycoprotein may be one of the first stages of the molecular pathogenesis of muscular dystrophy.Abstract:
Dystrophin, the protein encoded by the Duchenne muscular dystrophy (DMD) gene, exists in a large oligomeric complex. We show here that four glycoproteins are integral components of the dystrophin complex and that the concentration of one of these is greatly reduced in DMD patients. Thus, the absence of dystrophin may lead to the loss of a dystrophin-associated glycoprotein, and the reduction in this glycoprotein may be one of the first stages of the molecular pathogenesis of muscular dystrophy.read more
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Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix
Oxana Ibraghimov-Beskrovnaya,James M. Ervasti,Cynthia J. Leveille,Clive A. Slaughter,Suzanne W. Sernett,Kevin P. Campbell +5 more
TL;DR: 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 extra-cellular matrix and that this may render muscle fibres more susceptible to necrosis is supported.
Journal ArticleDOI
A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
TL;DR: The results support a role for the striated muscle dystrophin-glycoprotein complex in linking the actin- based cytoskeleton with the extracellular matrix and suggest that dystophin and dystroglycan may play substantially different functional roles in nonmuscle tissues.
Journal ArticleDOI
Membrane organization of the dystrophin-glycoprotein complex
TL;DR: It is demonstrated that dystrophin and its 59 kd associated protein are cytoskeletal elements that are tightly linked to a 156 kd extracellular glycoprotein by way of a complex of transmembrane proteins.
Journal ArticleDOI
Function and genetics of dystrophin and dystrophin-related proteins in muscle
TL;DR: The role of the dystrophin complex and protein family in muscle is discussed and the physiological processes that are affected in Duchenne muscular dystrophy are described.
Journal ArticleDOI
Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy.
TL;DR: In this paper, it was shown that dystrophin complex interacts with an N-terminal domain of nNOS that contains a GLGF motif, which may contribute to preferential degeneration of fast-twitch muscle fibers in Duchenne muscular dystrophy.
References
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Journal ArticleDOI
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article
Cleavage of structural proteins during the assemble of the head of bacterio-phage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Journal ArticleDOI
Dystrophin: The protein product of the duchenne muscular dystrophy locus
TL;DR: The identification of the mdx mouse as an animal model for DMD has important implications with regard to the etiology of the lethal DMD phenotype, and the protein dystrophin is named because of its identification via the isolation of the Duchenne muscular dystrophy locus.
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The Complete Sequence of Dystrophin Predicts a Rod-Shaped Cytoskeletal Protein
M. Koenig,M. Koenig,Anthony P. Monaco,Anthony P. Monaco,Louis M. Kunkel,Louis M. Kunkel,Louis M. Kunkel +6 more
TL;DR: The complete sequence of the human Duchenne muscular dystrophy cDNA has been determined and dystrophin shares many features with the cytoskeletal protein spectrin and alpha-actinin and is likely to adopt a rod shape about 150 nm in length.
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Conversion of mdx myofibres from dystrophin-negative to -positive by injection of normal myoblasts
TL;DR: It is shown that injected normal muscle precursor cells can fuse with pre-existing or regenerating mdx muscle fibres to render many of these fibres dystrophin-positive and so to partially or wholly rescue them from their biochemical defect.