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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1994-12-6
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pubmed:abstractText |
Gp80 human IL-6R was studied using 7 murine mAb (M37, M91, M113, M139, M164, M182 and M195) obtained after fusion of splenocytes of Balb/c mice immunised with a mixture of recombinant IL-6 receptor (rIL-6R) and cells from 2 cell lines expressing IL-6R. These were U266, which is IL-6 independent and XG-1 which is IL-6-dependent. In ELISA the 7 mAb reacted against the rIL-6R and against the natural soluble form found in plasma (nIL-6R), which both lack transmembrane and cytoplasmic domains. However, M195 reacted less with the natural than with the recombinant soluble IL-6R. Using FACS analysis, the 7 mAb were shown to bind to U266 cells but not to the Namalva cell line which is deprived of IL-6R. This showed that they all recognised the membrane form of the IL-6R. Three of the anti-IL-6R mAb reacted with rIL-6R by Western blotting. Four different epitopes of the molecule were identified, either by cross-blocking experiments of mAb binding to IL6R in ELISA or by the biosensor Biacore technology. A group of 4 mAb (M37, M113, M139 and M164) and another mAb (M195) identified 2 different epitopes involved in IL-6 binding. These antibodies were able to inhibit the binding of IL-6 to IL-6R and the proliferation of the IL-6-dependent XG-1 cell line. M91 and M182 recognized 2 other epitopes that were not involved in IL-6 binding. As expected, M91 did not inhibit XG-1 proliferation; in contrast, M182 interfered with the proliferative response of the XG-1 cell line.(ABSTRACT TRUNCATED AT 250 WORDS)
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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/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/IL6R protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-6,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-6,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:issn |
1148-5493
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
293-300
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7524715-Antibodies, Monoclonal,
pubmed-meshheading:7524715-Antibody Specificity,
pubmed-meshheading:7524715-Epitopes,
pubmed-meshheading:7524715-Humans,
pubmed-meshheading:7524715-Interleukin-6,
pubmed-meshheading:7524715-Membrane Glycoproteins,
pubmed-meshheading:7524715-Receptors, Interleukin,
pubmed-meshheading:7524715-Receptors, Interleukin-6,
pubmed-meshheading:7524715-Recombinant Proteins
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pubmed:articleTitle |
Epitope analysis of human IL-6 receptor gp80 molecule with monoclonal antibodies.
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pubmed:affiliation |
INSERM U291, Montpellier, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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