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Brain α‐dystroglycan displays unique glycoepitopes and preferential binding to laminin‐10/11
Author(s) -
McDearmon Erin L.,
Combs Ariana C.,
Sekiguchi Kiyotoshi,
Fujiwara Hironobu,
Ervasti James M.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.05.010
Subject(s) - dystroglycan , laminin , epitope , monoclonal antibody , alpha (finance) , glycosylation , peanut agglutinin , chemistry , microbiology and biotechnology , biology , biochemistry , antibody , extracellular matrix , genetics , lectin , medicine , construct validity , nursing , patient satisfaction
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.