Lorberboum-Galski H, Kozak R W, Waldmann T A, Bailon P, FitzGerald D J, Pastan I
Laboratory of Molecular Biology, National Cancer Institute, Bethesda, Maryland 20892.
J Biol Chem. 1988 Dec 15;263(35):18650-6.
IL2-PE40 is a chimeric protein composed of human interleukin 2 (IL2) genetically fused to the amino terminus of a modified form of pseudomonas exotoxin (PE). Internalization of IL2 via the individual p55 and p70 subunits of the IL2 receptor was studied using IL2-PE40 on several mouse and human cell lines expressing either the p55, the p70, or both IL2 receptor subunits. Internalization was assessed by measuring inhibition of protein synthesis caused by the toxin moiety of IL2-PE40. The results demonstrate that IL2 internalization is mediated by either the p55 receptor subunit or by the p70 subunit but is much more efficient when high affinity receptors composed of both subunits are present. IL2-PE40 is a powerful reagent for studying IL2 receptor interactions and for analyzing pathways of the immune response and its regulation.
IL2-PE40是一种嵌合蛋白,由与人白细胞介素2(IL2)基因融合的修饰形式的铜绿假单胞菌外毒素(PE)的氨基末端组成。使用IL2-PE40在几种表达p55、p70或两者IL2受体亚基的小鼠和人类细胞系上研究了IL2通过IL2受体的单个p55和p70亚基的内化。通过测量由IL2-PE40的毒素部分引起的蛋白质合成抑制来评估内化。结果表明,IL2内化由p55受体亚基或p70亚基介导,但当由两个亚基组成的高亲和力受体存在时效率要高得多。IL2-PE40是研究IL2受体相互作用以及分析免疫反应及其调节途径的有力试剂。