Display Settings:

Format

Send to:

Choose Destination
We are sorry, but NCBI web applications do not support your browser and may not function properly. More information
    Nature. 1992 Feb 20;355(6362):696-702.

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

    Source

    Howard Hughes Medical Institute, University of Iowa College of Medicine, Iowa City 52242.

    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.

    PMID:
    1741056
    [PubMed - indexed for MEDLINE]

      Supplemental Content

      Icon for Nature Publishing Group
      Loading ...
      Write to the Help Desk