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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1997-5-15
pubmed:abstractText
The myelin-associated glycoprotein (MAG) exhibits an abnormally high apparent molecular weight in sciatic nerve, but not in brain, of dysmyelinating trembler mutants (Inuzuka et al.: J Neurochem 44:793-797, 1985). Antibodies to the large and small isoforms of MAG (L- and S-MAG) and probes for oligosaccharide structure were used to determine if this was due to overexpression of L-MAG or increased glycosylation. Nerves from both control and trembler 36-day-old mice contained primarily S-MAG with only traces of L-MAG. The distribution of the two isoforms appeared normal in trembler mice, and both isoforms exhibited the higher apparent molecular weight. Lectin binding showed that, in contrast to brain in which most glycoproteins contain primarily alpha 2-3 linked sialic acid, most glycoproteins of both control and trembler nerve contained primarily alpha 2-6 linked sialic acid. Lectin binding and glycosidase treatments demonstrated that the higher molecular weight of MAG in trembler nerves was due to an increased content of alpha 2-3 linked sialic acid and galactose. The abnormal glycosylation of MAG in trembler mutants may contribute to the myelin pathology.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0360-4012
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
587-93
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
The myelin-associated glycoprotein of the peripheral nervous system in trembler mutants contains increased alpha 2-3 sialic acid and galactose.
pubmed:affiliation
Myelin and Brain Development Section, Laboratory of Molecular and Cellular Neurobiology, NINDS, NIH, Bethesda, Maryland, USA.
pubmed:publicationType
Journal Article