E-resources
Peer reviewed
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Ibraghimov-Beskrovnaya, O; Ervasti, J M; Leveille, C J; Slaughter, C A; Sernett, S W; Campbell, K P
Nature (London), 02/1992, Volume: 355, Issue: 6362Journal Article
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.
