rdf:type |
|
lifeskim:mentions |
umls-concept:C0003316,
umls-concept:C0020861,
umls-concept:C0028959,
umls-concept:C0031809,
umls-concept:C0086418,
umls-concept:C0129439,
umls-concept:C0205164,
umls-concept:C0270922,
umls-concept:C0332285,
umls-concept:C0443737,
umls-concept:C0678594,
umls-concept:C1412716,
umls-concept:C1416969,
umls-concept:C1704689,
umls-concept:C1707455
|
pubmed:issue |
3
|
pubmed:dateCreated |
1992-3-13
|
pubmed:abstractText |
The epitope for HNK-1 and patient's monoclonal autoantibodies in demyelinating polyneuropathy associated with immunoglobulin M gammopathy is borne by different types of N-linked oligosaccharide structures in human P0 and myelin-associated glycoprotein (MAG). Fourteen glycopeptide fractions bearing different oligosaccharide structures were obtained from either MAG or P0 glycopeptides by serial lectin affinity chromatography on concanavalin A-Sepharose, Phaseolus vulgaris erythrophytohemagglutinin-agarose, Pisum sativum agglutinin-agarose, and Phaseolus vulgaris leucophytohemagglutinin-agarose. As shown by dot-TLC plate immunostaining, the same MAG and P0 glycopeptide fractions were recognized by HNK-1 and patient's immunoglobulin M, confirming that these antibodies display similar specificities. The antigenic carbohydrate was present in glycopeptide fractions that either interact with Pisum sativum agglutinin-agarose or were bound by Aleuria aurantia agglutinin-digoxigenin, indicating that these structures contained alpha(1-6)fucose residues. This study demonstrates that the L2/HNK-1 epitope is borne mainly or even exclusively by N-linked oligosaccharide structures alpha(1-6)fucosylated in the core.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD57,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin M,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Myelin P0 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Myelin Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myelin-Associated Glycoprotein,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
|
pubmed:issn |
0022-3042
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
58
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
854-61
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1371150-Antibodies, Monoclonal,
pubmed-meshheading:1371150-Antigens, CD57,
pubmed-meshheading:1371150-Antigens, Differentiation,
pubmed-meshheading:1371150-Chemical Fractionation,
pubmed-meshheading:1371150-Chromatography, Affinity,
pubmed-meshheading:1371150-Demyelinating Diseases,
pubmed-meshheading:1371150-Epitopes,
pubmed-meshheading:1371150-Humans,
pubmed-meshheading:1371150-Immunoglobulin M,
pubmed-meshheading:1371150-Lectins,
pubmed-meshheading:1371150-Myelin P0 Protein,
pubmed-meshheading:1371150-Myelin Proteins,
pubmed-meshheading:1371150-Myelin-Associated Glycoprotein,
pubmed-meshheading:1371150-Oligosaccharides
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pubmed:year |
1992
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pubmed:articleTitle |
Comparison of the N-linked oligosaccharide structures of the two major human myelin glycoproteins MAG and P0: assessment of the structures bearing the epitope for HNK-1 and human monoclonal immunoglobulin M found in demyelinating neuropathy.
|
pubmed:affiliation |
Department of Neurology, Centre Hospitalier Universitaire Vaudois, Lausanne, Switzerland.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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