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

O Ibraghimov-Beskrovnaya, JM Ervasti, CJ Leveille… - Nature, 1992 - nature.com
O Ibraghimov-Beskrovnaya, JM Ervasti, CJ Leveille, CA Slaughter, SW Sernett…
Nature, 1992nature.com
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 …
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.
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