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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1997-2-12
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pubmed:abstractText |
Myelin-associated glycoprotein (MAG), a nervous system cell adhesion molecule, is an I-type lectin that binds to sialylated glycoconjugates, including gangliosides bearing characteristic structural determinants (Yang, L. J.-S., Zeller, C. B., Shaper, N. L., Kiso, M., Hasegawa, A., Shapiro, R. E., and Schnaar, R. L. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 814-818). Two cell adhesion systems, COS-1 monkey kidney fibroblasts transiently transfected to express MAG and Chinese hamster ovary (CHO) cells stably transfected to express MAG, were used to probe the structural specificity of MAG-ganglioside binding. Both cell types bound to the same gangliosides: GQ1b alpha (IV3NeuAc,III6NeuAc,II3(NeuAc)2Gg4Cer) > GT1b = GD1a > GM3 > GM1, GD1b, and GQ1b (the latter do not support adhesion). Binding was enhanced by pretreatment of MAG-expressing cells with neuraminidase. MAG-expressing Chinese hamster ovary cells bound directly to gangliosides resolved on thin layer chromatograms, allowing detection of MAG binding species in a mixture. The simplest ganglioside ligand for MAG was GM3 bearing N-acetylneuraminic acid, whereas GM3 bearing N-glycolylneuraminic acid did not support adhesion. Chemical modifications of N-acetylneuraminic acid residues (on GD1a) abrogated MAG binding. Mild periodate oxidation of sialic acids to their corresponding seven-carbon (or eight-carbon) sialic acid aldehydes abolished MAG binding, as did further conversion to the corresponding primary alcohols. Eliminating the anionic charge by ethyl esterification, amidation, or reduction also abolished MAG-mediated cell adhesion. These data demonstrate that MAG-ganglioside binding is highly specific and defines key carbohydrate structural determinants for MAG-mediated cell adhesion to gangliosides.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Gangliosides,
http://linkedlifedata.com/resource/pubmed/chemical/Myelin-Associated Glycoprotein,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylneuraminic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Neuraminidase,
http://linkedlifedata.com/resource/pubmed/chemical/ganglioside, GD1a
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1248-55
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8995428-Animals,
pubmed-meshheading:8995428-CHO Cells,
pubmed-meshheading:8995428-COS Cells,
pubmed-meshheading:8995428-Cell Adhesion,
pubmed-meshheading:8995428-Cricetinae,
pubmed-meshheading:8995428-Cricetulus,
pubmed-meshheading:8995428-Gangliosides,
pubmed-meshheading:8995428-Haplorhini,
pubmed-meshheading:8995428-Myelin-Associated Glycoprotein,
pubmed-meshheading:8995428-N-Acetylneuraminic Acid,
pubmed-meshheading:8995428-Neuraminidase,
pubmed-meshheading:8995428-Substrate Specificity,
pubmed-meshheading:8995428-Transfection,
pubmed-meshheading:8995428-Vibrio
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pubmed:year |
1997
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pubmed:articleTitle |
Sialic acid specificity of myelin-associated glycoprotein binding.
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pubmed:affiliation |
Department of Pharmacology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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