Characterization of dp6troglycan-laminin interaction in peripheral nerve

J Neurochem. 1996 Apr;66(4):1518-24. doi: 10.1046/j.1471-4159.1996.66041518.x.


Dystoroglycan is encoded by a single gene and cleaved into two proteins, alpha and beta-dystroglycan, by posttranslational processing. The 120kDa peripheral nerve isoform of alpha-dystroglycan binds laminin-2 comprised of the alpha 2, beta 1, and gamma 1 chains. In congenital muscular dystrophy and dy mice deficient in laminin alpha 2 chain, peripheral myelination is disturbed, suggesting a role for the dystroglycan- laminin interaction in peripheral myelinogenesis. To begin to test this hypothesis, we have characterized the dystroglycan-laminin interaction in peripheral nerve. We demonstrate that (1) alpha-dystroglycan is an extracellular peripheral membrane glycoprotein that links beta-dystroglycan in the Schwann cell outer membrane with laminin-2 in the endoneurial basal lamina, and (2) dystrophin homologues Dp116 and utrophin are cytoskeletal proteins of the Schwann cell cytoplasm. We also present data that suggest a role for glycosylation of alpha-dystroglycan in the interaction with laminin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carbohydrates / physiology
  • Cattle
  • Cytoskeletal Proteins / metabolism*
  • Cytoskeletal Proteins / ultrastructure
  • Dystroglycans
  • Dystrophin / metabolism*
  • Dystrophin / ultrastructure
  • Laminin / metabolism*
  • Membrane Glycoproteins / metabolism*
  • Membrane Glycoproteins / ultrastructure
  • Peripheral Nerves / metabolism*
  • Rabbits
  • Sciatic Nerve / metabolism*


  • Carbohydrates
  • Cytoskeletal Proteins
  • Dystrophin
  • Laminin
  • Membrane Glycoproteins
  • Dystroglycans