Enhanced laminin binding by alpha-dystroglycan after enzymatic deglycosylation.

ABSTRACT: Carbohydrate modifications are clearly important to the function of alpha-dystroglycan but their composition and structure remain poorly understood. In the present study, we describe experiments aimed at identifying the alpha-dystroglycan oligosaccharides important for its binding to laminin-1 and carbohydrate-dependent mAbs (monoclonal antibodies) IIH6 and VIA4(1). We digested highly purified skeletal muscle alpha-dystroglycan with an array of linkage-specific endo- and exoglycosidases, which were verified for action on alpha-dystroglycan by loss/gain of reactivity for lectins with defined glyco-epitopes. Notably, digestion with a combination of Arthrobacter ureafaciens sialidase, beta(1-4)galactosidase and beta-N-acetylglucosaminidase substantially degraded SiaAalpha2-3Galbeta1-4GlcNAcbe

SUBMITTER: Combs AC 

PROVIDER: S-EPMC1184583 | biostudies-literature | 2005 Aug

REPOSITORIES: biostudies-literature