Linked Life Data

1377056

Source:http://linkedlifedata.com/resource/pubmed/id/1377056

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-7-29
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-4971
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
80
pubmed:geneSymbol
AIC2A, AIC2B
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
84-90
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:1377056-Animals, pubmed-meshheading:1377056-Cell Division, pubmed-meshheading:1377056-Granulocyte-Macrophage Colony-Stimulating Factor, pubmed-meshheading:1377056-Humans, pubmed-meshheading:1377056-Interleukin-2, pubmed-meshheading:1377056-Interleukin-3, pubmed-meshheading:1377056-Macromolecular Substances, pubmed-meshheading:1377056-Mice, pubmed-meshheading:1377056-Molecular Weight, pubmed-meshheading:1377056-Phosphoproteins, pubmed-meshheading:1377056-Phosphorylation, pubmed-meshheading:1377056-Phosphotyrosine, pubmed-meshheading:1377056-Receptors, Granulocyte-Macrophage Colony-Stimulating Factor, pubmed-meshheading:1377056-Receptors, Interleukin-3, pubmed-meshheading:1377056-Recombinant Proteins, pubmed-meshheading:1377056-Signal Transduction, pubmed-meshheading:1377056-Species Specificity, pubmed-meshheading:1377056-Structure-Activity Relationship, pubmed-meshheading:1377056-Transfection, pubmed-meshheading:1377056-Tyrosine
pubmed:year
1992
pubmed:articleTitle
Functional reconstitution of the human interleukin-3 receptor.
pubmed:affiliation
Department of Molecular Biology, DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, CA 94304.
pubmed:publicationType
Journal Article, Comparative Study, In Vitro, Research Support, Non-U.S. Gov't