| pubmed-article:8276883 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8276883 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:8276883 | lifeskim:mentions | umls-concept:C0063717 | lld:lifeskim |
| pubmed-article:8276883 | lifeskim:mentions | umls-concept:C1527148 | lld:lifeskim |
| pubmed-article:8276883 | lifeskim:mentions | umls-concept:C0231491 | lld:lifeskim |
| pubmed-article:8276883 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8276883 | pubmed:dateCreated | 1994-2-8 | lld:pubmed |
| pubmed-article:8276883 | pubmed:abstractText | Neutralizing monoclonal antibodies specific for human interleukin-6 (IL-6) bind two distinct sites on the IL-6 protein (sites I and II). Their interference with IL-6 receptor binding suggested that site I is a receptor-binding site of IL-6, whereas site II is important for signal transduction. Mutagenesis of site II could therefore result in the isolation of IL-6 receptor antagonists. To test this hypothesis, a panel of IL-6 mutant proteins was constructed that did not bind to a site II-specific monoclonal antibody. One such site II mutant protein (with double substitution of Gln-160 with Glu and Thr-163 with Pro) was found to be an antagonist of human IL-6. It was inactive on human CESS cells, weakly active on human HepG2 cells, but active on mouse B9 cells. It could specifically antagonize the activity of wild-type IL-6 on CESS and HepG2 cells. The binding affinity of this variant for the 80-kDa IL-6 receptor was similar to that of wild-type IL-6. High affinity binding to CESS cells, however, was abolished, suggesting that the mutant protein is inactive because the complex of the 80-kDa IL-6 receptor and the mutant protein cannot associate with the signal transducer gp130. The human IL-6 antagonist protein may be potentially useful as a therapeutic agent. | lld:pubmed |
| pubmed-article:8276883 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8276883 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8276883 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8276883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8276883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8276883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8276883 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8276883 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8276883 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8276883 | pubmed:author | pubmed-author:HeinrichP CPC | lld:pubmed |
| pubmed-article:8276883 | pubmed:author | pubmed-author:AardenL ALA | lld:pubmed |
| pubmed-article:8276883 | pubmed:author | pubmed-author:ContentJJ | lld:pubmed |
| pubmed-article:8276883 | pubmed:author | pubmed-author:Rose-JohnSS | lld:pubmed |
| pubmed-article:8276883 | pubmed:author | pubmed-author:SchooltinkHH | lld:pubmed |
| pubmed-article:8276883 | pubmed:author | pubmed-author:BrakenhoffJ... | lld:pubmed |
| pubmed-article:8276883 | pubmed:author | pubmed-author:FontaineVV | lld:pubmed |
| pubmed-article:8276883 | pubmed:author | pubmed-author:de HonF DFD | lld:pubmed |
| pubmed-article:8276883 | pubmed:author | pubmed-author:ten BoekelEE | lld:pubmed |
| pubmed-article:8276883 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8276883 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:8276883 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:8276883 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8276883 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8276883 | pubmed:pagination | 86-93 | lld:pubmed |
| pubmed-article:8276883 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8276883 | pubmed:meshHeading | pubmed-meshheading:8276883-... | lld:pubmed |
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| pubmed-article:8276883 | pubmed:meshHeading | pubmed-meshheading:8276883-... | lld:pubmed |
| pubmed-article:8276883 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8276883 | pubmed:articleTitle | Development of a human interleukin-6 receptor antagonist. | lld:pubmed |
| pubmed-article:8276883 | pubmed:affiliation | Department of Autoimmune Diseases, Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, Amsterdam. | lld:pubmed |
| pubmed-article:8276883 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8276883 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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