Journal article
Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix
Nature (London), Vol.355(6362), pp.696-702
02/1992
DOI: 10.1038/355696a0
PMID: 1741056
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.
Details
- Title: Subtitle
- Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix
- Creators
- Oxana Ibraghimov-BeskrovnayaJames M ErvastiCynthia J LeveilleClive A SlaughterSuzanne W SernettKevin P Campbell
- Resource Type
- Journal article
- Publication Details
- Nature (London), Vol.355(6362), pp.696-702
- DOI
- 10.1038/355696a0
- PMID
- 1741056
- ISSN
- 0028-0836
- eISSN
- 1476-4687
- Language
- English
- Date published
- 02/1992
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
- Record Identifier
- 9984020876502771
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