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Query: UNIPROT:P14784 (IL-2 receptor)
 3,849 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Full length cDNAs encoding the human and murine p70 genes were isolated using polymerase chain reaction (PCR) and conventional cDNA library screening techniques, respectively. To validate their functional potential, expression vectors containing human, murine and chimeric human/murine p70 cDNAs were transfected into the murine IL-3-dependent cell line FDC-P1. Transfected cells expressed a combination of high and low-affinity IL-2 binding sites while parental cells displayed only the low-affinity sites associated with expression of endogenous p55 IL-2 receptor chains. The role of the transfected p70 chains in formation of the high-affinity receptor sites was confirmed by the finding that the species-specific inhibitory antibody TU27 blocked high-affinity binding to human p70 and chimeric human/murine p70-expressing cells while having no effect on cells transfected with the murine p70 cDNA construct. As consequences of the expression of the transfected p70 chains, the cells responded to IL-2 with increased levels of endogenous p55 receptor subunit and both short and long-term proliferation. These studies substantiate the role of the p70 receptor chain in functional responses to IL-2 and provide a model system for future dissection of the structure/function relationships of the IL-2 receptor.
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PMID:Functional expression of native and chimeric human and murine IL-2 receptor p70 chains in an IL-3-dependent murine cell line. 209 Aug 77

A B cell lymphoma A20.2J and splenic B cells produced an active material to support the proliferation of an interleukin 2 (IL-2)-dependent T cell line, CTLL-2, by stimulation with both calcium ionophore A23187 and phorbol myristate acetate (PMA). Although the production of the active material was induced by stimulation with A23187 alone in A20.2J cells, both A23187 and PMA were essential for the stimulation of splenic B cells. Neither A20.2J cells nor splenic B cells produced the active material by stimulation with PMA alone. The production was inversely proportional to the concentration of fetal calf serum in culture medium. The active material produced by B cells was indicated to be IL-2 and not B cell-stimulating factor 1 (BSF-1) for the following reasons: 1) the proliferation of CTLL-2 cells in the presence of active material was inhibited by the inclusion of anti-IL-2 receptor or anti-IL-2 in culture medium but not by anti-BSF-1; 2) the material showed no co-mitogenic activity to purified splenic B cells with anti-immunoglobulins and did not support the proliferation of FDC-P2 which are known to grow in the presence of BSF-1; and 3) IL-2 mRNA could be detected in A20.2J and splenic B cells stimulated with A23187 and PMA in Northern blot analysis. Some B cell hybridomas were also shown to produce IL-2 by similar stimulation to A20.2J. Splenic B cells as well as A20.2J cells were able to produce IL-2 by stimulation with anti-immunoglobulins. These results suggest that under certain conditions IL-2 can be produced by splenic B cells, at least some subsets of B cells, and B cell lines.
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PMID:Interleukin secretion by B cell lines and splenic B cells stimulated with calcium ionophore and phorbol ester. 311 82

Interleukin-13 (IL-13) induced a potent mitogenic response in IL-3-dependent TF-1 cells and DNA synthesis to a lesser extent in MO7E and FDC-P1 cells. IL-13 stimulation of these lines, like IL-4 and insulin-like growth factor-1 (IGF-1), resulted in tyrosine phosphorylation of a 170-kD substrate. The tyrosine-phosphorylated 170-kD substrate strongly associated with the 85-kD subunit of phosphoinositol-3 (PI-3) kinase and with Grb-2. Anti-4PS serum readily detected the 170-kD substrate in lysates from both TF-1 and FDC-P1 cells stimulated with IL-13 or IL-4. These data provide evidence that IL-13 induces tyrosine phosphorylation of the 4PS substrate, providing an essential interface between the IL-13 receptor and signaling molecules containing SH2 domains. IL-13 and IL-4 stimulation of murine L cell fibroblasts, which endogenously express the IL-4 receptor (IL-4R alpha) and lack expression of the IL-2 receptor gamma subunit (IL-2R gamma), resulted in tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1)/4PS. Enhanced tyrosine phosphorylation of IRS-1/4PS was observed in response to IL-4, but not IL-13 treatment of L cells transfected with the IL-2R gamma chain. These results indicate that IL-13 does not use the IL-2R gamma subunit in its receptor complex and that expression of IL-2R gamma enhances, but is not absolutely required for mediating IL-4-induced tyrosine phosphorylation of IRS-1/4PS.
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PMID:The insulin receptor substrate-1-related 4PS substrate but not the interleukin-2R gamma chain is involved in interleukin-13-mediated signal transduction. 749 80

Cells of 7 tested human leukemia cell lines of pre-B cell origin (as characterized by immunophenotyping and by the expression of cytoplasmic mu chains, but not by surface immunoglobulins) produced after stimulation with bacterial lipopolysaccharide (LPS) or phorbol myristate acetate (PMA) a lymphokine activity which supported the growth of the interleukin-2 (IL-2)-dependent CTLL-2 cell line. Three pieces of evidence indicate that the secreted lymphokine was functionally and antigenically very similar, if not identical, to human IL-2: (1) The lymphokine supported the growth of murine IL-2-dependent CTLL-2 cells, which did not respond to human lymphokines other than IL-2, but it did not stimulate the growth of murine IL-3-dependent FDC-P2 cells, (2) the biological activity of the lymphokine was inhibited by monoclonal antibody (mAb) anti-human-IL-2, and (3) the proliferation of IL-2-dependent cells in the presence of the active material was completely inhibited by the inclusion of the anti-mouse-IL-2 receptor (IL-2R) mAb. Since leukemia cells of immature B-cell origin also synthesize IL-2R, the human pre-B cell leukemias could represent another type of hematological malignancy where the autocrine processes of IL-2 production and utilization are involved in the expansion of the disease.
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PMID:Interleukin-2 production by human leukemia cell lines of pre-B cell origin. 835 Sep 45