Brain α-dystroglycan displays unique glycoepitopes and preferential binding to laminin-10/11

Abstractα-Dystroglycan was quantitatively enriched from mammalian brain based on its uniform reactivity with Vicia villosa agglutinin and resolved into sub-populations possessing or lacking the sulfated glucuronic acid epitope recognized by monoclonal antibody HNK-1. We generated a new monoclonal antibody specific for a glycoepitope on brain α-dystroglycan but absent from α-dystroglycan expressed in all other tissues examined. Finally, we found that laminin-10/11 preferentially bound to brain α-dystroglycan compared to skeletal muscle α-dystroglycan. Our results suggest that tissue-specific glycosylation modifies the laminin binding specificity of α-dystroglycan