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Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix

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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 extra-cellular matrix and that this may render muscle fibres more susceptible to necrosis.

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Author notes

  1. Clive A. Slaughter: Howard Hughes Medical Institute, Biopolymer Facility, University of Texas Southwestern Medical Center, Dallas, Texas 75235, USA

Authors and Affiliations

  1. Howard Hughes Medical Institute and Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa, 52242, USA

    Oxana Ibraghimov-Beskrovnaya, James M. Ervasti, Cynthia J. Leveille, Clive A. Slaughter, Suzanne W. Sernett & Kevin P. Campbell

Authors
  1. Oxana Ibraghimov-Beskrovnaya
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  2. James M. Ervasti
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  3. Cynthia J. Leveille
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  4. Clive A. Slaughter
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  5. Suzanne W. Sernett
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  6. Kevin P. Campbell
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Ibraghimov-Beskrovnaya, O., Ervasti, J., Leveille, C. et al. Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix. Nature 355, 696–702 (1992). https://doi.org/10.1038/355696a0

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  • DOI: https://doi.org/10.1038/355696a0

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