Abstract
The dystrophin-glycoprotein complex (DGC) links the cytoskeleton to the extracellular matrix. Dystroglycan (DG) is a central component of the DGC and is heavily glycosylated. The O-glycan of α-DG is a novel O-mannosyl glycan. Recent data indicate that the aberrant O-mannosyl glycan of α-DG is the primary cause of some forms of congenital muscular dystrophy, and these muscular dystrophies are termed α-dystroglycanopathies. The hypoglycosylation of α-DG has been shown to greatly reduce its affinity for extracellular matrix components such as laminin, thereby disrupting the dystroglycan-extracellular matrix linkage and leading to membrane fragility. Currently, mutations in 16 genes are known to cause these diseases. The characterization of each protein associated with α-dystroglycanopathy will help to reveal not only the molecular pathomechanisms but also the biosynthetic pathway of O-mannosyl glycan. Because α-DG hypoglycosylation is a common feature of α-dystroglycanopathies, α-DG may be a potential target of new glycotherapeutic strategies for these diseases.
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Endo, T. (2015). α-Dystroglycanopathy. In: Taniguchi, N., Endo, T., Hart, G., Seeberger, P., Wong, CH. (eds) Glycoscience: Biology and Medicine. Springer, Tokyo. https://doi.org/10.1007/978-4-431-54841-6_172
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DOI: https://doi.org/10.1007/978-4-431-54841-6_172
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Publisher Name: Springer, Tokyo
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Online ISBN: 978-4-431-54841-6
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