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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

McDearmon EL,Combs AC,Sekiguchi K,Fujiwara H,Ervasti JM

doi

10.1016/j.febslet.2006.05.010

subject

Has Abstract

pub_date

2006-06-12 00:00:00

pages

3381-5

issue

14

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(06)00595-3

journal_volume

580

pub_type

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