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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
1994-1-14
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pubmed:abstractText |
Macrophage cell-surface protein 2 (Mac-2), a galactose specific S-type lectin identified in inflammatory macrophages, presents a high degree of homology with the rat IgE-binding protein (epsilon BP). In the present study, we show by different experimental approaches that human eosinophils can express Mac-2/epsilon BP. Flow cytometry analysis revealed that a large proportion of eosinophilic patients expressing binding sites for IgE on their eosinophil membrane, were able to bind anti-Mac-2 monoclonal antibody (mAb). Northern blot performed with eosinophil RNA hybridized with the human Mac-2 or epsilon BP cDNA probes revealed that eosinophils presented a unique transcript at 1.2 kb. Immunoprecipitation of eosinophil extracts with anti-Mac-2 mAb revealed the presence of a molecule of 29 kDa corresponding to Mac-2 protein, as well as one additional molecule of 15 kDa, absent from control alveolar macrophages. The function of these molecules was investigated in a radiolabeled IgE binding assay. Anti-Mac-2 mAb as well as galactose and lactose saccharides significantly inhibited the binding of radiolabeled human myeloma IgE protein to eosinophils. Moreover, the dose-dependent inhibition by anti-Mac-2 mAb of IgE-dependent eosinophil-mediated cytotoxicity towards parasite targets indicated the role of these IgE-binding molecules in the function of human eosinophils. These results suggest that in addition to transmembrane receptors, lectin-type molecules can participate in the IgE-dependent effector function of eosinophils.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation,
http://linkedlifedata.com/resource/pubmed/chemical/Galectin 3,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin E,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, IgE
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0014-2980
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3230-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8258338-Animals,
pubmed-meshheading:8258338-Antigens, Differentiation,
pubmed-meshheading:8258338-Binding Sites,
pubmed-meshheading:8258338-Cytotoxicity, Immunologic,
pubmed-meshheading:8258338-Eosinophils,
pubmed-meshheading:8258338-Flow Cytometry,
pubmed-meshheading:8258338-Galectin 3,
pubmed-meshheading:8258338-Humans,
pubmed-meshheading:8258338-Immunoglobulin E,
pubmed-meshheading:8258338-Lectins,
pubmed-meshheading:8258338-RNA, Messenger,
pubmed-meshheading:8258338-Rats,
pubmed-meshheading:8258338-Receptors, IgE
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pubmed:year |
1993
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pubmed:articleTitle |
IgE-binding molecules (Mac-2/epsilon BP) expressed by human eosinophils. Implication in IgE-dependent eosinophil cytotoxicity.
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pubmed:affiliation |
Centre d'Immunologie et de Biologie Parasitaire, Unité Mixte INSERM U 167--CNRS 624, Institut Pasteur, Lille, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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