Linked Life Data

2449128

Source:http://linkedlifedata.com/resource/pubmed/id/2449128

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-3-4
pubmed:abstractText
Monoclonal antibody (MAb) R24 was previously shown to be directed toward ganglioside GD3 [Pukel, C. S., Lloyd, K. O., Travassos, L. R., Dippold, W. G., Oettgen, H. F., and Old, L. J. (1982) J. Exp. Med. 155, 1133-1147]. The structural specificity of the MAb has now been further characterized based on binding to structurally related glycolipids, including four GD3 derivatives with different N-acetylneuraminic acid (NeuAc) and N-glycolylneuraminic acid (NeuGc) substituents. Three assay systems (enzyme immunostaining on thin-layer chromatography, enzyme-linked immunosorbent assay, and immune adherence inhibition assay) were used. MAb R24 was found to react with (NeuAc-NeuAc-)GD3 and (NeuAc-NeuGc-)GD3 but not with (NeuGc-NeuAc-)GD3 or (NeuGc-NeuGc-)GD3. These results clearly indicate that the outer sialic acid (Sia) moiety of GD3 is crucial and must be a NeuAc residue, while the inner sialic acid is less involved in binding to the MAb and can be either NeuAc or NeuGc. The MAb was also found to cross-react weakly with two gangliosides, GT1a and GQ1b, but none of other gangliosides nor neutral glycolipids tested reacted. These findings suggest that the epitope detected by MAb R24 is the trisaccharide structure NeuAc alpha 2----8Sia alpha 2----3Gal-, which must be in a terminal position.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:volume
260
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
51-5
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Monoclonal antibody R24 distinguishes between different N-acetyl- and N-glycolylneuraminic acid derivatives of ganglioside GD3.
pubmed:affiliation
Department of Oncology, Tokyo Metropolitan Institute of Medical Science, Japan.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't