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

Research output: Contribution to journalArticle

1115 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)696-702
Number of pages7
JournalNature
Volume355
Issue number6362
DOIs
StatePublished - Jan 1 1992
Externally publishedYes

ASJC Scopus subject areas

  • General

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    Ibraghimov-Beskrovnaya, O., Ervasti, J. M., Leveille, C. J., Slaughter, C. A., Sernett, S. W., & Campbell, K. P. (1992). Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix. Nature, 355(6362), 696-702. https://doi.org/10.1038/355696a0