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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
44
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pubmed:dateCreated |
1996-12-26
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Erythropoietin,
http://linkedlifedata.com/resource/pubmed/chemical/Globins,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-3,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Erythropoietin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-3,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
27432-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8910323-Animals,
pubmed-meshheading:8910323-Cell Differentiation,
pubmed-meshheading:8910323-Cell Division,
pubmed-meshheading:8910323-Cell Line,
pubmed-meshheading:8910323-Clone Cells,
pubmed-meshheading:8910323-Erythropoietin,
pubmed-meshheading:8910323-Genetic Vectors,
pubmed-meshheading:8910323-Globins,
pubmed-meshheading:8910323-Hematopoietic Stem Cells,
pubmed-meshheading:8910323-Interleukin-3,
pubmed-meshheading:8910323-Kinetics,
pubmed-meshheading:8910323-Macromolecular Substances,
pubmed-meshheading:8910323-Mice,
pubmed-meshheading:8910323-Mutagenesis, Site-Directed,
pubmed-meshheading:8910323-RNA, Messenger,
pubmed-meshheading:8910323-Receptors, Erythropoietin,
pubmed-meshheading:8910323-Receptors, Interleukin-3,
pubmed-meshheading:8910323-Recombinant Fusion Proteins,
pubmed-meshheading:8910323-Retroviridae,
pubmed-meshheading:8910323-Transcription, Genetic,
pubmed-meshheading:8910323-Transfection
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pubmed:year |
1996
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pubmed:articleTitle |
Interleukin-3 (IL-3) inhibits erythropoietin-induced differentiation in Ba/F3 cells via the IL-3 receptor alpha subunit.
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pubmed:affiliation |
Terry Fox Laboratory, British Columbia Cancer Agency, Vancouver, British Columbia V5Z 1L3, Canada. keith@terryfox.ubc.ca
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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