Fukuyama-type Congenital Muscular Dystrophy and Abnormal Glycosylation of α-Dystroglycan
نویسندگان
چکیده
Fukuyama-type congenital muscular dystrophy (FCMD), Walker-Warburg syndrome (WWS), and muscle-eye-brain (MEB) disease are clinically similar autosomal recessive disorders characterized by congenital muscular dystrophy, lissencephaly, and eye anomalies. We identified the gene for FCMD and MEB, which encodes the fukutin protein and the protein O-linked mannose β1, 2-N-acetylglucosaminyltransferase (POMGnT1), respectively. α-dystroglycan is a key component of the dystrophin-glycoprotein-complex, providing a tight linkage between the cell and basement membranes by binding laminin via its carbohydrate residues. Recent studies have revealed that posttranslational modification of α-dystroglycan is associated with these congenital muscular dystrophies with brain malformations.
منابع مشابه
Fukutin is prerequisite to ameliorate muscular dystrophic phenotype by myofiber-selective LARGE expression
α-Dystroglycanopathy (α-DGP) is a group of muscular dystrophy characterized by abnormal glycosylation of α-dystroglycan (α-DG), including Fukuyama congenital muscular dystrophy (FCMD), muscle-eye-brain disease, Walker-Warburg syndrome, and congenital muscular dystrophy type 1D (MDC1D), etc. LARGE, the causative gene for MDC1D, encodes a glycosyltransferase to form [-3Xyl-α1,3GlcAβ1-] polymer in...
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OBJECTIVE The fukutin gene (FKTN) is the causative gene for Fukuyama-type congenital muscular dystrophy, characterized by rather homogeneous clinical features of severe muscle wasting and hypotonia from early infancy with mental retardation. In contrast with the severe dystrophic involvement of skeletal muscle, cardiac insufficiency is quite rare. Fukuyama-type congenital muscular dystrophy is ...
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Dystroglycanopathies are neuromuscular disorders due to abnormal glycosylation of dystroglycan which is a cell-surface glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains. The reduced ability of abnormally glycosylated α-DG to bind laminin is associated with abnormal neuronal migration and muscular dystrophy. Clinical manifestations are extremely ...
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Several types of muscular dystrophy are caused by defective linkage between α-dystroglycan (α-DG) and laminin. Among these, dystroglycanopathy, including Fukuyama-type congenital muscular dystrophy (FCMD), results from abnormal glycosylation of α-DG. Recent studies have shown that like-acetylglucosaminyltransferase (LARGE) strongly enhances the laminin-binding activity of α-DG. Therefore, resto...
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