Journal article
Characterization of Dystroglycan‐Laminin Interaction in Peripheral Nerve
Journal of neurochemistry, Vol.66(4), pp.1518-1524
04/1996
DOI: 10.1046/j.1471-4159.1996.66041518.x
PMID: 8627307
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.
Details
- Title: Subtitle
- Characterization of Dystroglycan‐Laminin Interaction in Peripheral Nerve
- Creators
- Hiroki YamadaAtsuro ChibaTamao EndoAkira KobataLouise V. B AndersonHisae HoriHiroko Fukuta‐OhiIchiro KanazawaKevin P CampbellTeruo ShimizuKiichiro Matsumura
- Resource Type
- Journal article
- Publication Details
- Journal of neurochemistry, Vol.66(4), pp.1518-1524
- DOI
- 10.1046/j.1471-4159.1996.66041518.x
- PMID
- 8627307
- NLM abbreviation
- J Neurochem
- ISSN
- 0022-3042
- eISSN
- 1471-4159
- Publisher
- Blackwell Science Ltd; Oxford, UK
- Language
- English
- Date published
- 04/1996
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
- Record Identifier
- 9984020847202771
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