Nature. 1992 Feb 20;355(6362):696-702.

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

Ibraghimov-Beskrovnaya O, Ervasti JM, Leveille CJ, Slaughter CA, Sernett SW, Campbell KP.

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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]

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Review Dystrophin-glycoprotein complex: its role in the molecular pathogenesis of muscular dystrophies. [Muscle Nerve. 1994]
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