Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
|
pubmed:dateCreated |
1994-7-13
|
pubmed:abstractText |
The binding of IL-2 to its specific receptor (IL-2R) triggers various cellular events including the induction of nuclear proto-oncogenes (c-fos, c-jun and c-myc genes) and the proliferation of hemopoietic cells. In the present study, we have established NIH 3T3 fibroblasts in which the three IL-2R subunits, the alpha-chain (IL-2R alpha), the beta-chain (IL-2R beta), and the gamma-chain (IL-2R gamma), are constitutively expressed. The resulting cell lines express high affinity IL-2R on their cell surface at levels comparable with those of IL-2-responsive lymphoid cells. We observed that the high affinity IL-2R in NIH 3T3 fibroblasts can mediate the IL-2-stimulated tyrosine phosphorylation of p42/p44 (mitogen-activated protein kinase) and the induction of the c-fos, c-jun and c-myc genes. In NIH 3T3 fibroblasts the high affinity IL-2R bearing a deletion of a region rich in acidic amino acids (the "acidic" region) in the IL-2R beta-chain failed to induce the tyrosine phosphorylation of MAP kinase as well as the expression of the all three nuclear proto-oncogenes. On the other hand, our previous studies had demonstrated that the high affinity IL-2R bearing the same mutant IL-2R beta-chain retained the ability to induce c-myc gene in response to IL-2 in a murine IL-3-dependent pro-B cell line, BAF/B03. Hence, these results reveal the underlying complexity of signal transduction among different cell types. The inability of the reconstituted high affinity receptor to mediate the IL-2-induced proliferation of NIH 3T3 fibroblasts suggests that induction of the three nuclear proto-oncogenes and the tyrosine phosphorylation of mitogen-activated protein kinase in NIH 3T3 fibroblasts are not sufficient to induce cellular proliferation.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
AIM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0022-1767
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
152
|
pubmed:geneSymbol |
c-fos,
c-jun,
c-myc
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
5680-90
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:8207200-3T3 Cells,
pubmed-meshheading:8207200-Amino Acid Sequence,
pubmed-meshheading:8207200-Animals,
pubmed-meshheading:8207200-Cell Division,
pubmed-meshheading:8207200-Gene Expression,
pubmed-meshheading:8207200-Genes, fos,
pubmed-meshheading:8207200-Genes, jun,
pubmed-meshheading:8207200-Genes, myc,
pubmed-meshheading:8207200-Humans,
pubmed-meshheading:8207200-Interleukin-2,
pubmed-meshheading:8207200-Mice,
pubmed-meshheading:8207200-Phosphorylation,
pubmed-meshheading:8207200-Receptors, Interleukin-2,
pubmed-meshheading:8207200-Signal Transduction,
pubmed-meshheading:8207200-Tyrosine
|
pubmed:year |
1994
|
pubmed:articleTitle |
Signal transduction mediated by the reconstituted IL-2 receptor. Evidence for a cell type-specific function of IL-2 receptor beta-chain.
|
pubmed:affiliation |
Institute for Molecular and Cellular Biology, Osaka University, Japan.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|