Alpha-dystroglycan interactions affect cerebellar granule neuron migration.
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.
Qu
Qiang
Q
Shriver Center for Mental Retardation, Waltham, Massachusetts 02452, USA.
Smith
Frances I
FI
D018171:Agrin / Q000378:metabolism; D000818:Animals; D002465:Cell Movement / Q000502:physiology*; D002478:Cells, Cultured; D002531:Cerebellum / Q000166:cytology / Q000378:metabolism*; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D049030:Dystroglycans; D006031:Glycosylation; D008562:Membrane Glycoproteins / Q000378:metabolism*; D051379:Mice; D016501:Neurites / Q000378:metabolism; D009457:Neuroglia / Q000378:metabolism; D009474:Neurons / Q000378:metabolism*; D009924:Organ Culture Techniques
D018171:Agrin; D003598:Cytoskeletal Proteins; D008562:Membrane Glycoproteins; D049030:Dystroglycans