Brain alpha-dystroglycan displays unique glycoepitopes and preferential binding to laminin-10/11.
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.
McDearmon
Erin L
EL
Department of Physiology, University of Wisconsin, Madison, 53706, USA.
Combs
Ariana C
AC
Sekiguchi
Kiyotoshi
K
Fujiwara
Hironobu
H
Ervasti
James M
JM
D000818:Animals; D015153:Blotting, Western; D001921:Brain / Q000378:metabolism*; D002417:Cattle; D049030:Dystroglycans / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D051379:Mice; D018482:Muscle, Skeletal / Q000378:metabolism; D011817:Rabbits
D049030:Dystroglycans