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http://purl.uniprot.org/citations/16466646http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16466646http://www.w3.org/2000/01/rdf-schema#comment"To test the hypothesis that the disruption of fukutin protein produces the brain pathology through hypoglycosylation of alpha-dystroglycan (alpha-DG), we immunostained Fukuyama congenital muscular dystrophy (FCMD) brains with an antibody that recognizes the polysaccharide epitope of alpha-DG. Immunoreactivity of the glia-limitans along the cortical surface, as well as that of the glial endfeet around vessel walls, was preserved in the FCMD cerebrum. However, fragmentation of the immunostained glia-limitans was noted in association with parenchymal protrusion and gyral fusion. In the FCMD cerebellum, this fragmentation of alpha-DG labeling was limited to the area of micropolygyria, and immunostaining at the glia-limitans and vessel walls was comparable to that of the control brains, in structurally normal areas. In the hippocampus, neurons of the dentate gyrus and corpus ammonis were immunopositive for alpha-DG in control subjects, but this staining was markedly decreased in FCMD brains. In contrast, immunolabeling of blood vessels and the glia-limitans was preserved in this region. Fukutin antisera clearly labeled hippocampal neurons in control brains, while this labeling was decreased in FCMD brains. Thus, hypoglycosylation of alpha-DG was evident in neurons, but not in the glial cell population of FCMD brains. This suggests that the mechanism of alpha-DG glycosylation may differ between neurons and glial cells, and that a fukutin gene defect may result in functional disruption through hypoglycosylation of both neuronal and glial alpha-DG."xsd:string
http://purl.uniprot.org/citations/16466646http://purl.org/dc/terms/identifier"doi:10.1016/j.brainres.2005.12.108"xsd:string
http://purl.uniprot.org/citations/16466646http://purl.uniprot.org/core/author"Kobayashi M."xsd:string
http://purl.uniprot.org/citations/16466646http://purl.uniprot.org/core/author"Mizuguchi M."xsd:string
http://purl.uniprot.org/citations/16466646http://purl.uniprot.org/core/author"Saito Y."xsd:string
http://purl.uniprot.org/citations/16466646http://purl.uniprot.org/core/author"Saito K."xsd:string
http://purl.uniprot.org/citations/16466646http://purl.uniprot.org/core/author"Yamamoto T."xsd:string
http://purl.uniprot.org/citations/16466646http://purl.uniprot.org/core/author"Ohno K."xsd:string
http://purl.uniprot.org/citations/16466646http://purl.uniprot.org/core/author"Osawa M."xsd:string
http://purl.uniprot.org/citations/16466646http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16466646http://purl.uniprot.org/core/name"Brain Res"xsd:string
http://purl.uniprot.org/citations/16466646http://purl.uniprot.org/core/pages"223-228"xsd:string
http://purl.uniprot.org/citations/16466646http://purl.uniprot.org/core/title"Altered glycosylation of alpha-dystroglycan in neurons of Fukuyama congenital muscular dystrophy brains."xsd:string
http://purl.uniprot.org/citations/16466646http://purl.uniprot.org/core/volume"1075"xsd:string
http://purl.uniprot.org/citations/16466646http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16466646
http://purl.uniprot.org/citations/16466646http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16466646
http://purl.uniprot.org/uniprot/#_Q14118-mappedCitation-16466646http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16466646
http://purl.uniprot.org/uniprot/#_B4DN78-mappedCitation-16466646http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16466646
http://purl.uniprot.org/uniprot/Q14118http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16466646
http://purl.uniprot.org/uniprot/B4DN78http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16466646