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- Title
Dystroglycan glycosylation and its role in matrix binding in skeletal muscle.
- Authors
Martin, Paul T
- Abstract
Dystroglycan is an essential component of the dystrophin-glycoprotein complex. Three glycan sequencing studies have identified O-linked mannose chains, including NeuAcalpha 2,3Galbeta 1,4GlcNAcbeta 1,2Manalpha-O, on alpha dystroglycan. Chemical deglycosylation of alpha dystroglycan, antibody blocking studies, and glycan blocking studies all suggest that the O-linked glycans on alpha dystroglycan mediate the binding of extracellular matrix proteins in skeletal muscle. Structural data on laminin G domains and agrin-binding studies also suggest this is the case. Dystroglycan, however, is able to bind proteins via mechanisms that do not involve O-linked glycans. Moreover, laminin and other matrix proteins can bind cell adhesion molecules via their glycan chains. Thus although complex and sometimes not overly convincing, these data suggest that glycosylation plays an important role in dystroglycan binding and function in skeletal muscle.
- Publication
Glycobiology, 2003, Vol 13, Issue 8, p55R
- ISSN
0959-6658
- Publication type
Journal Article
- DOI
10.1093/glycob/cwg076