Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2051452 | FEBS Letters | 2006 | 5 Pages |
Abstract
α-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.
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Authors
Erin L. McDearmon, Ariana C. Combs, Kiyotoshi Sekiguchi, Hironobu Fujiwara, James M. Ervasti,