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rdf:type |
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lifeskim:mentions |
umls-concept:C0007600,
umls-concept:C0021756,
umls-concept:C0021761,
umls-concept:C0021764,
umls-concept:C0023636,
umls-concept:C0205263,
umls-concept:C0312738,
umls-concept:C0330390,
umls-concept:C0337112,
umls-concept:C0597357,
umls-concept:C1514485,
umls-concept:C1517499,
umls-concept:C1519726,
umls-concept:C1524075
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pubmed:issue |
9
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pubmed:dateCreated |
1994-10-18
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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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Vesicular...,
http://linkedlifedata.com/resource/pubmed/chemical/Benzoquinones,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-7,
http://linkedlifedata.com/resource/pubmed/chemical/Lactams, Macrocyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Quinones,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/SHC1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Shc Signaling Adaptor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Shc1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/herbimycin
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0014-2980
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
24
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2049-54
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8088325-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:8088325-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:8088325-Animals,
pubmed-meshheading:8088325-B-Lymphocyte Subsets,
pubmed-meshheading:8088325-Base Sequence,
pubmed-meshheading:8088325-Benzoquinones,
pubmed-meshheading:8088325-Blotting, Western,
pubmed-meshheading:8088325-Cell Line,
pubmed-meshheading:8088325-Interleukin-2,
pubmed-meshheading:8088325-Interleukin-7,
pubmed-meshheading:8088325-Lactams, Macrocyclic,
pubmed-meshheading:8088325-Lymphocyte Activation,
pubmed-meshheading:8088325-Mice,
pubmed-meshheading:8088325-Molecular Sequence Data,
pubmed-meshheading:8088325-Precipitin Tests,
pubmed-meshheading:8088325-Protein-Tyrosine Kinases,
pubmed-meshheading:8088325-Proteins,
pubmed-meshheading:8088325-Quinones,
pubmed-meshheading:8088325-Receptors, Interleukin-2,
pubmed-meshheading:8088325-Retroviridae,
pubmed-meshheading:8088325-Shc Signaling Adaptor Proteins,
pubmed-meshheading:8088325-Signal Transduction,
pubmed-meshheading:8088325-Transfection
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pubmed:year |
1994
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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.
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pubmed:affiliation |
Institut für Immunologie, Universitätsklinikum Steglitz, Freie Universität Berlin.
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pubmed:publicationType |
Journal Article
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