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Alpha‐dystroglycan interactions affect cerebellar granule neuron migration
Author(s) -
Qu Qiang,
Smith Frances I.
Publication year - 2004
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.20129
Subject(s) - agrin , dystroglycan , cerebellum , neurite , microbiology and biotechnology , neuron , neuroscience , chemistry , granule (geology) , biology , laminin , postsynaptic potential , extracellular matrix , in vitro , biochemistry , receptor , paleontology
The interaction of alpha‐dystroglycan (a‐DG) with its extracellular binding partners requires glycans attached to its mucin core domain, and defects in the glycosylation of a‐DG are associated with both muscular dystrophy and neuronal migration defects. The involvement of a‐DG and one of its ligands, agrin, in cerebellar neuronal migration was investigated. Antibodies directed against glycosylated a‐DG inhibited granule neuron migration in cerebellar slice cultures. a‐DG interactions did not appear to influence neurite outgrowth in cerebellar explant cultures, but enhanced granule neuron binding was observed on cells transfected with a‐DG. These results suggest that interactions involving a‐DG influence the strength of attachment of granule neurons to the a‐DG‐expressing Bergmann glial cells that guide granule neuron migration in the cerebellum. Experiments using anti‐agrin antibodies suggest that agrin is not involved in these interactions. © 2004 Wiley‐Liss, Inc.