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• W1981012746 abstract "Expression of the interleukin (IL)-2 receptor β chain in the IL-7-dependent pre-B cell line I × N/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 IL2-, but not IL-7-, stimulated tyrosine phosphorylation." @default.
• W1981012746 created "2016-06-24" @default.
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• W1981012746 date "1994-09-01" @default.
• W1981012746 modified "2023-09-25" @default.
• W1981012746 title "Gene transfer of the interleukin (IL)-2 receptor β 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" @default.
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• W1981012746 doi "https://doi.org/10.1002/eji.1830240917" @default.
• W1981012746 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8088325" @default.
• W1981012746 hasPublicationYear "1994" @default.
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