Back to Search
Start Over
Differentiation-related glycan epitopes identify discrete domains of the muscle glycocalyx
- Source :
- Glycobiology, vol 26, iss 10
- Publication Year :
- 2016
- Publisher :
- eScholarship, University of California, 2016.
-
Abstract
- The neuromuscular junction (NMJ) is enriched with glycoproteins modified with N-acetylgalactosamine (GalNAc) residues, and four nominally GalNAc-specific plant lectins have historically been used to identify the NMJ and the utrophin-glycoprotein complex. However, little is known about the specific glycan epitopes on skeletal muscle that are bound by these lectins, the glycoproteins that bear these epitopes or how creation of these glycan epitopes is regulated. Here, we profile changes in cell surface glycosylation during muscle cell differentiation and identify distinct differences in the binding preferences of GalNAc-specific lectins, Wisteria floribunda agglutinin (WFA), Vicia villosa agglutinin (VVA), soybean agglutinin (SBA) and Dolichos biflorus agglutinin (DBA). While we find that all four GalNAc binding lectins specifically label the NMJ, each of the four lectins binds distinct sets of muscle glycoproteins; furthermore, none of the major adhesion complexes are required for binding of any of the four GalNAc-specific lectins. Analysis of glycosylation-related transcripts identified target glycosyltransferases and glycosidases that could potentially create GalNAc-containing epitopes; reducing expression of these transcripts by siRNA highlighted differences in lectin binding specificities. In addition, we found that complex N-glycans are required for binding of WFA and SBA to murine C2C12 myotubes and for WFA binding to wild-type skeletal muscle, but not for binding of VVA or DBA. These results demonstrate that muscle cell surface glycosylation is finely regulated during muscle differentiation in a domain- and acceptor-substrate-specific manner, suggesting that temporal- and site-specific glycosylation are important for skeletal muscle cell function.
- Subjects :
- 0301 basic medicine
Glycan
Biochemistry & Molecular Biology
Glycosylation
Knockout
Glycocalyx
Biochemistry
Medical and Health Sciences
Epitope
Cell Line
03 medical and health sciences
chemistry.chemical_compound
Mice
Epitopes
Polysaccharides
utrophin–glycoprotein complex
medicine
Wisteria floribunda agglutinin
Myocyte
Animals
Soybean agglutinin
Muscle, Skeletal
chemistry.chemical_classification
Mice, Knockout
biology
neuromuscular junction
Muscle cell differentiation
Skeletal muscle
Cell Differentiation
Skeletal
Biological Sciences
Original articles
GalNAc
carbohydrates (lipids)
030104 developmental biology
medicine.anatomical_structure
chemistry
utrophin-glycoprotein complex
Musculoskeletal
biology.protein
Muscle
lipids (amino acids, peptides, and proteins)
Glycoprotein
Chickens
muscle glycosylation
Subjects
Details
- Database :
- OpenAIRE
- Journal :
- Glycobiology, vol 26, iss 10
- Accession number :
- edsair.doi.dedup.....8185149737bf4e5cc949f560b62c18a1