Lefort S, Vita N, Reeb R, Caput D, Ferrara P
Sanofi Recherche, Labège Innopole, France.
FEBS Lett. 1995 Jun 12;366(2-3):122-6. doi: 10.1016/0014-5793(95)00512-8.
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-4R alpha 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.
白细胞介素-13（IL-13）和白细胞介素-4（IL-4）是人类红白血病细胞系TF-1的生长因子。在这些细胞中，这两种细胞因子共享重叠的结合位点，但IL-13的结合位点数是IL-4的一半。两种针对IL-4Rα链胞外域的单克隆抗体完全消除了IL-13的结合，尽管IL-13并不与该链结合。受体触发后，IL-13和IL-4诱导一种170 kDa蛋白的磷酸化，该蛋白可能是IL-4诱导的磷酸酪氨酸底物。此外，170 kDa蛋白的磷酸化导致其与磷脂酰肌醇-3-激酶紧密结合。
