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

Nature. 1992 Feb 20;355(6362):696-702. doi: 10.1038/355696a0.


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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • Cytoskeletal Proteins / chemistry*
  • Cytoskeletal Proteins / genetics
  • Cytoskeletal Proteins / metabolism
  • Dystroglycans
  • Dystrophin / metabolism*
  • Extracellular Matrix / metabolism*
  • Gene Expression
  • Humans
  • Immunoblotting
  • Laminin / metabolism
  • Membrane Glycoproteins*
  • Molecular Sequence Data
  • Molecular Weight
  • Muscles / chemistry
  • Muscles / metabolism
  • Muscular Dystrophies / genetics
  • Muscular Dystrophies / metabolism*
  • RNA, Messenger / analysis
  • Recombinant Fusion Proteins
  • Restriction Mapping
  • Sarcolemma / metabolism*
  • Tissue Distribution


  • Cytoskeletal Proteins
  • DAG1 protein, human
  • Dystrophin
  • Laminin
  • Membrane Glycoproteins
  • RNA, Messenger
  • Recombinant Fusion Proteins
  • Dystroglycans

Associated data

  • GENBANK/X64393