| pubmed-article:1377056 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1377056 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:1377056 | lifeskim:mentions | umls-concept:C0080096 | lld:lifeskim |
| pubmed-article:1377056 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:1377056 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1377056 | pubmed:dateCreated | 1992-7-29 | lld:pubmed |
| pubmed-article:1377056 | pubmed:abstractText | The high-affinity receptors for human interleukin-3 (IL-3), GM-CSF, and IL-5 are composed of alpha and beta subunits. The alpha subunits are primary ligand binding proteins specific for each ligand, whereas the three human receptors share a common beta subunit (beta c). In contrast to humans mice have two closely related genes, AIC2A and AIC2B, which are homologous to human beta c. The AIC2A gene encodes a low-affinity murine IL-3 binding protein, and the AIC2B protein is the beta subunit shared between murine GM-CSF receptors (mGMR) and IL-5 receptors (mIL-5R). To examine the function of these receptor components, we established various stable transfectants of murine IL-2-dependent CTLL-2 cells. CTLL-2 transfectants expressing both the alpha and beta subunits of the human IL-3 receptor (hIL-3R) proliferated in response to physiologic concentrations of hIL-3. Coexpression of hIL-3R alpha with AIC2B but not with AIC2A in CTLL-2 cells conferred a growth response to hIL-3. Although CTLL-2 transfectants expressing hIL-3R alpha alone did not proliferate in the presence of hIL-3, hIL-3-responsive sublines were repeatedly isolated. These sublines expressed endogenous AIC2B but not AIC2A. These results indicate that human beta c is essential for hIL-3 signaling and that AIC2B is a murine equivalent of human beta c. We also showed that hIL-3 and hGM-CSF induced tyrosine phosphorylation of several proteins in CTLL transfectants, similar to those observed in human factor-dependent TF-1 cells stimulated with hIL-3 and hGM-CSF. | lld:pubmed |
| pubmed-article:1377056 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1377056 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1377056 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:1377056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1377056 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1377056 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:1377056 | pubmed:issn | 0006-4971 | lld:pubmed |
| pubmed-article:1377056 | pubmed:author | pubmed-author:KitamuraTT | lld:pubmed |
| pubmed-article:1377056 | pubmed:author | pubmed-author:MiyajimaAA | lld:pubmed |
| pubmed-article:1377056 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1377056 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:1377056 | pubmed:volume | 80 | lld:pubmed |
| pubmed-article:1377056 | pubmed:geneSymbol | AIC2B | lld:pubmed |
| pubmed-article:1377056 | pubmed:geneSymbol | AIC2A | lld:pubmed |
| pubmed-article:1377056 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1377056 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1377056 | pubmed:pagination | 84-90 | lld:pubmed |
| pubmed-article:1377056 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:1377056 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1377056 | pubmed:articleTitle | Functional reconstitution of the human interleukin-3 receptor. | lld:pubmed |
| pubmed-article:1377056 | pubmed:affiliation | Department of Molecular Biology, DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, CA 94304. | lld:pubmed |
| pubmed-article:1377056 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1377056 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:1377056 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:1377056 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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