pubmed-article:8088325 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8088325 | lifeskim:mentions | umls-concept:C0007600 | lld:lifeskim |
pubmed-article:8088325 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
pubmed-article:8088325 | lifeskim:mentions | umls-concept:C0021756 | lld:lifeskim |
pubmed-article:8088325 | lifeskim:mentions | umls-concept:C0021761 | lld:lifeskim |
pubmed-article:8088325 | lifeskim:mentions | umls-concept:C0312738 | lld:lifeskim |
pubmed-article:8088325 | lifeskim:mentions | umls-concept:C0021764 | lld:lifeskim |
pubmed-article:8088325 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
pubmed-article:8088325 | lifeskim:mentions | umls-concept:C1519726 | lld:lifeskim |
pubmed-article:8088325 | lifeskim:mentions | umls-concept:C1524075 | lld:lifeskim |
pubmed-article:8088325 | lifeskim:mentions | umls-concept:C0023636 | lld:lifeskim |
pubmed-article:8088325 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
pubmed-article:8088325 | lifeskim:mentions | umls-concept:C1517499 | lld:lifeskim |
pubmed-article:8088325 | lifeskim:mentions | umls-concept:C1514485 | lld:lifeskim |
pubmed-article:8088325 | lifeskim:mentions | umls-concept:C0337112 | lld:lifeskim |
pubmed-article:8088325 | pubmed:issue | 9 | lld:pubmed |
pubmed-article:8088325 | pubmed:dateCreated | 1994-10-18 | lld:pubmed |
pubmed-article:8088325 | pubmed:abstractText | Expression of the interleukin (IL)-2 receptor beta chain in the IL-7-dependent pre-B cell line IxN/2B permitted growth in presence of either IL-2 or IL-7, allowing for a direct comparison of intracellular signaling events. Protein tyrosine phosphorylation was essential for IL-2 and IL-7-induced signal transduction since the tyrosine kinase inhibitor herbimycin A blocked proliferation in response to both factors. Western blot analysis of tyrosine-phosphorylated proteins revealed that both IL-2 and IL-7 stimulation led to enhanced phosphorylation of proteins of 170-, 145-, 115- and 99-kDa, as well as induction of phosphorylation of a 96-kDa protein. However, a 55- and a 155-kDa protein were only phosphorylated after IL-2 stimulation. The 55-kDa protein specifically phosphorylated by IL-2 could be identified as p52shc which has recently been shown to be critically involved in Ras activation. Shc tyrosine phosphorylation as a result of IL-2 stimulation was consistently found in CTLL-2 cells and human T lymphoblasts. Taken together our results indicate that the IL-2- and IL-7-stimulated intracellular pathways are partially different and that Shc is a target of IL-2-, but not IL-7-, stimulated tyrosine phosphorylation. | lld:pubmed |
pubmed-article:8088325 | pubmed:language | eng | lld:pubmed |
pubmed-article:8088325 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8088325 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8088325 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8088325 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8088325 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8088325 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:8088325 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8088325 | pubmed:month | Sep | lld:pubmed |
pubmed-article:8088325 | pubmed:issn | 0014-2980 | lld:pubmed |
pubmed-article:8088325 | pubmed:author | pubmed-author:DiamantsteinT... | lld:pubmed |
pubmed-article:8088325 | pubmed:author | pubmed-author:HockHH | lld:pubmed |
pubmed-article:8088325 | pubmed:author | pubmed-author:DorschMM | lld:pubmed |
pubmed-article:8088325 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8088325 | pubmed:volume | 24 | lld:pubmed |
pubmed-article:8088325 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8088325 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8088325 | pubmed:pagination | 2049-54 | lld:pubmed |
pubmed-article:8088325 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:8088325 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:8088325 | pubmed:articleTitle | Gene transfer of the interleukin (IL)-2 receptor beta chain into an IL-7-dependent pre-B cell line permits IL-2-driven proliferation: tyrosine phosphorylation of Shc is induced by IL-2 but not IL-7. | lld:pubmed |
pubmed-article:8088325 | pubmed:affiliation | Institut für Immunologie, Universitätsklinikum Steglitz, Freie Universität Berlin. | lld:pubmed |
pubmed-article:8088325 | pubmed:publicationType | Journal Article | lld:pubmed |
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