| Literature DB >> 16709410 |
Erin L McDearmon1, Ariana C Combs, Kiyotoshi Sekiguchi, Hironobu Fujiwara, James M Ervasti.
Abstract
alpha-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 alpha-dystroglycan but absent from alpha-dystroglycan expressed in all other tissues examined. Finally, we found that laminin-10/11 preferentially bound to brain alpha-dystroglycan compared to skeletal muscle alpha-dystroglycan. Our results suggest that tissue-specific glycosylation modifies the laminin binding specificity of alpha-dystroglycan.Entities:
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Year: 2006 PMID: 16709410 DOI: 10.1016/j.febslet.2006.05.010
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124