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Characterization of Dystroglycan-Laminin Interaction in Peripheral Nerve
Authors:Hiroki Yamada,Atsuro Chiba,Tamao Endo,Akira Kobata,&dagger  Louise V. B. Anderson,&Dagger  Hisae Hori,Hiroko Fukuta-Ohi,§  Ichiro Kanazawa,&#  Kevin P. Campbell,Teruo Shimizu, Kiichiro Matsumura
Affiliation:Department of Neurology and Neuroscience, Teikyo University School of Medicine,; Department of Glycobiology, Tokyo Metropolitan Institute of Gerontology,; Department of Tissue Physiology, Medical Research Institute, Tokyo Medical and Dental University, and; Department of Neurology, Institute of Brain Research, University of Tokyo School of Medicine, Tokyo, Japan;; University School of Neuroscience and Muscular Dystrophy Group Laboratories, Regional Neuroscience Centre, Newcastle General Hospital, Newcastle-upon-Tyne, England;and; Howard Hughes Medical Institute and Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa, U.S.A.
Abstract:Abstract: Dystroglycan is encoded by a single gene and cleaved into two proteins, α- and β-dystroglycan, by posttranslational processing. The 120-kDa peripheral nerve isoform of α-dystroglycan binds laminin-2 comprised of the α2, β1, and γ1 chains. In congenital muscular dystrophy and dy mice deficient in laminin α2 chain, peripheral myelination is disturbed, suggesting a role for the dystroglycan-laminin interaction in peripheral myelinogenesis. To begin to test this hypothesis, we have characterized the dystroglycan-laminin interaction in peripheral nerve. We demonstrate that (1) α-dystroglycan is an extracellular peripheral membrane glycoprotein that links β-dystroglycan in the Schwann cell outer membrane with laminin-2 in the endoneurial basal lamina, and (2) dystrophin homologues Dp116 and utrophin are cytoskeletal proteins of the Schwann cell cytoplasm. We also present data that suggest a role for glycosylation of α-dystroglycan in the interaction with laminin.
Keywords:Dystroglycan-Laminin    Schwann cell    Myelination    Basal lamina
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