| pubmed-article:8910323 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8910323 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:8910323 | lifeskim:mentions | umls-concept:C0021757 | lld:lifeskim |
| pubmed-article:8910323 | lifeskim:mentions | umls-concept:C0007589 | lld:lifeskim |
| pubmed-article:8910323 | lifeskim:mentions | umls-concept:C0017963 | lld:lifeskim |
| pubmed-article:8910323 | lifeskim:mentions | umls-concept:C0080096 | lld:lifeskim |
| pubmed-article:8910323 | lifeskim:mentions | umls-concept:C1511938 | lld:lifeskim |
| pubmed-article:8910323 | lifeskim:mentions | umls-concept:C1321758 | lld:lifeskim |
| pubmed-article:8910323 | pubmed:issue | 44 | lld:pubmed |
| pubmed-article:8910323 | pubmed:dateCreated | 1996-12-26 | lld:pubmed |
| pubmed-article:8910323 | pubmed:abstractText | Introduction of erythropoietin receptors (EpoRs) into the interleukin-3 (IL-3)-dependent murine hemopoietic cell line, Ba/F3, enables these cells to not only proliferate, after an initial lag in G1, but also to increase beta-globin mRNA levels in response to erythropoietin (Epo). With IL-3 and Epo costimulation, IL-3-induced signaling appears to be dominant since no increase in beta-globin mRNA occurs. Differentiation and proliferation signals may be uncoupled since EpoRs lacking all eight intracellular tyrosines were compromised in proliferative signaling but retained erythroid differentiation ability. Intriguingly, a chimeric receptor of the extracellular domain of the EpoR and the transmembrane and intracellular domains of IL-3RbetaIL-3 chain (EpoR/IL-3RbetaIL-3) was capable of Epo-induced proliferative and differentiating signaling, suggesting either the existence of a second EpoR subunit responsible for differentiation or that the alpha subunit of the IL-3 receptor (IL-3R) prevents it. Arguing against the former, a truncated EpoR lacking an intracellular domain was incapable of promoting proliferation or differentiation. An EpoR/IL-3Ralpha chimera, in contrast, was capable of transmitting a weak Epo-induced proliferative signal but failed to stimulate accumulation of beta-globin mRNA. Most significantly, coexpression of the EpoR/IL-3Ralpha chimera with either EpoR/IL-3Rbeta or wild-type EpoRs suppressed Epo-induced beta-globin mRNA accumulation. Taken together, these results suggest an active role for the IL-3Ralpha subunit in inhibiting EpoR-specific differentiating signals. | lld:pubmed |
| pubmed-article:8910323 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8910323 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8910323 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8910323 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8910323 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8910323 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8910323 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8910323 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8910323 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8910323 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8910323 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8910323 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8910323 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:8910323 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8910323 | pubmed:author | pubmed-author:KrystalGG | lld:pubmed |
| pubmed-article:8910323 | pubmed:author | pubmed-author:HumphriesR... | lld:pubmed |
| pubmed-article:8910323 | pubmed:author | pubmed-author:DamenJ EJE | lld:pubmed |
| pubmed-article:8910323 | pubmed:author | pubmed-author:KroslJJ | lld:pubmed |
| pubmed-article:8910323 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8910323 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:8910323 | pubmed:volume | 271 | lld:pubmed |
| pubmed-article:8910323 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8910323 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8910323 | pubmed:pagination | 27432-7 | lld:pubmed |
| pubmed-article:8910323 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:meshHeading | pubmed-meshheading:8910323-... | lld:pubmed |
| pubmed-article:8910323 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8910323 | pubmed:articleTitle | Interleukin-3 (IL-3) inhibits erythropoietin-induced differentiation in Ba/F3 cells via the IL-3 receptor alpha subunit. | lld:pubmed |
| pubmed-article:8910323 | pubmed:affiliation | Terry Fox Laboratory, British Columbia Cancer Agency, Vancouver, British Columbia V5Z 1L3, Canada. keith@terryfox.ubc.ca | lld:pubmed |
| pubmed-article:8910323 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8910323 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8910323 | lld:pubmed |
