| pubmed-article:9373251 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9373251 | lifeskim:mentions | umls-concept:C0083031 | lld:lifeskim |
| pubmed-article:9373251 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:9373251 | lifeskim:mentions | umls-concept:C1749467 | lld:lifeskim |
| pubmed-article:9373251 | lifeskim:mentions | umls-concept:C1414557 | lld:lifeskim |
| pubmed-article:9373251 | lifeskim:mentions | umls-concept:C0231491 | lld:lifeskim |
| pubmed-article:9373251 | lifeskim:mentions | umls-concept:C1551336 | lld:lifeskim |
| pubmed-article:9373251 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:9373251 | pubmed:dateCreated | 1997-12-23 | lld:pubmed |
| pubmed-article:9373251 | pubmed:abstractText | We have expressed a soluble N-glycosylated form of the murine interleukin-11 (IL-11) receptor alpha-chain (sIL-11R) and examined signaling in cells expressing the gp130 molecule. In the presence of gp130 but not the transmembrane IL-11R, the sIL-11R mediated IL-11-dependent differentiation of M1 leukemic cells and proliferation in Ba/F3 cells. Early intracellular events stimulated by the sIL-11R including phosphorylation of gp130, STAT 3, and SHP-2 were similar to signaling through the transmembrane IL-11R. IL-11 bound to sIL-11R with low affinity (kd 10 to 50 nmol/L). Binding of sIL-11R to gp130 was IL-11 dependent with intermediate affinity (kd 1.5 to 3.0 nmol/L). However, the concentration of IL-11 required for signaling through the sIL-11R was 10- to 20-fold greater than that required for cells expressing the transmembrane IL-11R and gp130 in the absence of sIL-11R. Furthermore, the sIL-11R was capable of antagonizing the activity of IL-11 when tested on cells expressing the transmembrane IL-11R and gp130. We propose that the observed IL-11 antagonism by the sIL-11R may depend on limiting numbers of gp130 molecules on cells already expressing the transmembrane IL-11R. | lld:pubmed |
| pubmed-article:9373251 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9373251 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9373251 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:9373251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9373251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9373251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9373251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9373251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9373251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9373251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9373251 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9373251 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:9373251 | pubmed:issn | 0006-4971 | lld:pubmed |
| pubmed-article:9373251 | pubmed:author | pubmed-author:MurrayLL | lld:pubmed |
| pubmed-article:9373251 | pubmed:author | pubmed-author:CurtinD EDE | lld:pubmed |
| pubmed-article:9373251 | pubmed:author | pubmed-author:RobertsBB | lld:pubmed |
| pubmed-article:9373251 | pubmed:author | pubmed-author:NicolaNN | lld:pubmed |
| pubmed-article:9373251 | pubmed:author | pubmed-author:BegleyC GCG | lld:pubmed |
| pubmed-article:9373251 | pubmed:author | pubmed-author:HiltonD JDJ | lld:pubmed |
| pubmed-article:9373251 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9373251 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:9373251 | pubmed:volume | 90 | lld:pubmed |
| pubmed-article:9373251 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9373251 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9373251 | pubmed:pagination | 4403-12 | lld:pubmed |
| pubmed-article:9373251 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9373251 | pubmed:meshHeading | pubmed-meshheading:9373251-... | lld:pubmed |
| pubmed-article:9373251 | pubmed:meshHeading | pubmed-meshheading:9373251-... | lld:pubmed |
| pubmed-article:9373251 | pubmed:meshHeading | pubmed-meshheading:9373251-... | lld:pubmed |
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| pubmed-article:9373251 | pubmed:meshHeading | pubmed-meshheading:9373251-... | lld:pubmed |
| pubmed-article:9373251 | pubmed:meshHeading | pubmed-meshheading:9373251-... | lld:pubmed |
| pubmed-article:9373251 | pubmed:meshHeading | pubmed-meshheading:9373251-... | lld:pubmed |
| pubmed-article:9373251 | pubmed:meshHeading | pubmed-meshheading:9373251-... | lld:pubmed |
| pubmed-article:9373251 | pubmed:meshHeading | pubmed-meshheading:9373251-... | lld:pubmed |
| pubmed-article:9373251 | pubmed:meshHeading | pubmed-meshheading:9373251-... | lld:pubmed |
| pubmed-article:9373251 | pubmed:meshHeading | pubmed-meshheading:9373251-... | lld:pubmed |
| pubmed-article:9373251 | pubmed:meshHeading | pubmed-meshheading:9373251-... | lld:pubmed |
| pubmed-article:9373251 | pubmed:meshHeading | pubmed-meshheading:9373251-... | lld:pubmed |
| pubmed-article:9373251 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9373251 | pubmed:articleTitle | Recombinant soluble interleukin-11 (IL-11) receptor alpha-chain can act as an IL-11 antagonist. | lld:pubmed |
| pubmed-article:9373251 | pubmed:affiliation | Walter and Eliza Hall Institute of Medical Research, Victoria, Australia. | lld:pubmed |
| pubmed-article:9373251 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9373251 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:16157 | entrezgene:pubmed | pubmed-article:9373251 | lld:entrezgene |
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