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IL‐13 and IL‐4 share signal transduction elements as well as receptor components in TF‐1 cells
Author(s) -
Lefort Sylvie,
Vita Natalio,
Reeb Renée,
Caput Daniel,
Ferrara Pascual
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00512-8
Subject(s) - phosphorylation , signal transduction , microbiology and biotechnology , phosphatidylinositol , extracellular , receptor , interleukin 3 , interleukin 13 receptor , chemistry , monoclonal antibody , biology , biochemistry , antibody , growth factor , t cell , il 2 receptor , insulin like growth factor 1 receptor , immunology , immune system
IL‐13 and IL‐4 are growth factors for the human erythroleukemia cell line TF‐1. In these cells both cytokines share overlapping binding sites, but the number of sites for IL‐13 is half of that for IL‐4. Two monoclonal antibodies against the extracellular domain of the IL‐4Rα chain completely abolish the binding of IL‐13, although IL‐13 does not bind to this chain. Following receptor triggering, IL‐13 and IL‐4 induce the phosphorylation of a 170 kDa protein, probably the IL‐4‐induced phosphotyrosine substrate. In addition the phosphorylation of the 170 kDa protein results in its tight association with phosphatidylinositol‐3‐kinase.