Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-10-17
pubmed:abstractText
The relative expression of large (L) and small (S) isoforms of the myelin-associated glycoprotein (MAG) and their glycosylation were compared in developing spinal cord of quaking and control mice. Using antisera specific for L- and S-MAG, respectively, it was shown that S-MAG is the principal isoform in quaking mice at all ages between 13 and 72 days, although L-MAG was just detectable by western blotting at the early ages. Both L- and S-MAG have higher apparent molecular weights in quaking mice than in controls. Experiments involving lectin binding and glycosidase treatment demonstrated that the higher molecular weight of MAG in the quaking mutant was due to a higher content of N-acetylneuraminic acid residues linked alpha 2-3 to galactose as well as to more branching of oligosaccharide moieties indicated by a higher content of subterminal galactose residues. The total sialic acid measured by HPAE-chromatography in purified quaking MAG was 40% higher than in control MAG. By contrast, quaking MAG contained less of the adhesion-related, HNK-1 carbohydrate epitope. Another difference was that a lower molecular weight form of MAG with predominantly high mannose oligosaccharides was prominent in young quaking mice, but not in controls. The abnormalities of MAG expression related to splicing of its mRNA and glycosylation may contribute to the myelin pathology in quaking mutants.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0360-4012
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27-38
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7545761-Amidohydrolases, pubmed-meshheading:7545761-Animals, pubmed-meshheading:7545761-Carbohydrate Metabolism, pubmed-meshheading:7545761-Demyelinating Diseases, pubmed-meshheading:7545761-Disease Models, Animal, pubmed-meshheading:7545761-Female, pubmed-meshheading:7545761-Gene Expression Regulation, Developmental, pubmed-meshheading:7545761-Glycoside Hydrolases, pubmed-meshheading:7545761-Glycosylation, pubmed-meshheading:7545761-Immunoblotting, pubmed-meshheading:7545761-Lectins, pubmed-meshheading:7545761-Male, pubmed-meshheading:7545761-Mice, pubmed-meshheading:7545761-Mice, Quaking, pubmed-meshheading:7545761-Molecular Weight, pubmed-meshheading:7545761-Myelin Proteins, pubmed-meshheading:7545761-Myelin-Associated Glycoprotein, pubmed-meshheading:7545761-Neuraminidase, pubmed-meshheading:7545761-Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase, pubmed-meshheading:7545761-Sciatic Nerve, pubmed-meshheading:7545761-Spinal Cord
pubmed:year
1995
pubmed:articleTitle
Abnormal expression and glycosylation of the large and small isoforms of myelin-associated glycoprotein in dysmyelinating quaking mutants.
pubmed:affiliation
Myelin and Brain Development Section, NINDS, National Institutes of Health, Bethesda, Maryland, USA.
pubmed:publicationType
Journal Article