| pubmed-article:2112585 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2112585 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:2112585 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:2112585 | lifeskim:mentions | umls-concept:C1511625 | lld:lifeskim |
| pubmed-article:2112585 | lifeskim:mentions | umls-concept:C0063717 | lld:lifeskim |
| pubmed-article:2112585 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:2112585 | lifeskim:mentions | umls-concept:C0021873 | lld:lifeskim |
| pubmed-article:2112585 | lifeskim:mentions | umls-concept:C1704222 | lld:lifeskim |
| pubmed-article:2112585 | lifeskim:mentions | umls-concept:C0591833 | lld:lifeskim |
| pubmed-article:2112585 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:2112585 | pubmed:dateCreated | 1990-7-16 | lld:pubmed |
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| pubmed-article:2112585 | pubmed:abstractText | Two species of the cDNAs encoding murine IL-6-R (one is abnormal and the other authentic) have been cloned from a plasmacytoma cell line, P3U1, and BALB/c mouse spleen cDNA libraries. In the cDNA encoding the abnormal IL-6-R, the region corresponding to an intracytoplasmic domain was replaced with a part of the long terminal repeat of the intracisternal A particle gene (IAP-LTR). The authentic IL-6-R consists of 460 amino acids with the domain of the Ig superfamily. The overall homology between murine and human IL-6-R was 69 and 54% at DNA and protein levels, respectively. The extracellular domain after the Ig-like domain of murine IL-6-R was found to have an homology with those of murine erythropoietin R, human IL-2-R beta chain, murine IL-4-R, and human granulocyte-macrophage CSF-R, as in the case of human IL-6-R, and these receptors have been classified as members of the IL receptor family. In P3U1 cells, the expression of the mRNA encoding abnormal IL-6-R was much higher than that of the mRNA encoding authentic IL-6-R. An IL-6-dependent human T cell line, KT-3, which did not respond to murine IL-6, acquired the responsiveness to murine IL-6 when transfected with the cDNA encoding abnormal IL-6-R, indicating that abnormal IL-6-R lacking a normal cytoplasmic domain can function. Since IL-6 functions as a potent growth factor for murine plasmacytomas, over-expression of abnormal IL-6-R may function as a positive selection element for the development of certain plasmacytomas. | lld:pubmed |
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| pubmed-article:2112585 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2112585 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2112585 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2112585 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2112585 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:2112585 | pubmed:issn | 0022-1007 | lld:pubmed |
| pubmed-article:2112585 | pubmed:author | pubmed-author:YamasakiKK | lld:pubmed |
| pubmed-article:2112585 | pubmed:author | pubmed-author:SaitoMM | lld:pubmed |
| pubmed-article:2112585 | pubmed:author | pubmed-author:HiranoTT | lld:pubmed |
| pubmed-article:2112585 | pubmed:author | pubmed-author:KishimotoTT | lld:pubmed |
| pubmed-article:2112585 | pubmed:author | pubmed-author:SugitaTT | lld:pubmed |
| pubmed-article:2112585 | pubmed:author | pubmed-author:TotsukaTT | lld:pubmed |
| pubmed-article:2112585 | pubmed:author | pubmed-author:TagaTT | lld:pubmed |
| pubmed-article:2112585 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2112585 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:2112585 | pubmed:volume | 171 | lld:pubmed |
| pubmed-article:2112585 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2112585 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2112585 | pubmed:pagination | 2001-9 | lld:pubmed |
| pubmed-article:2112585 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2112585 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2112585 | pubmed:articleTitle | Functional murine interleukin 6 receptor with the intracisternal A particle gene product at its cytoplasmic domain. Its possible role in plasmacytomagenesis. | lld:pubmed |
| pubmed-article:2112585 | pubmed:affiliation | Institute for Molecular and Cellular Biology, Osaka University, Japan. | lld:pubmed |
| pubmed-article:2112585 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2112585 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:2112585 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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