Kashima N, Matsui H, Yamasaki S, Kondo N, Hamuro J
Central Research Laboratories, Ajinomoto Co., Inc., Kanagawa.
J Biochem. 1987 Oct;102(4):715-24. doi: 10.1093/oxfordjournals.jbchem.a122109.
Murine interleukin-2 (MIL-2) cDNA was inserted into an expression vector carrying an Escherichia coli tryptophan promoter and was expressed in E. coli. Recombinant MIL-2 produced by E. coli supported the growth of murine CTLL-2 cells, but not that of human T-cell blasts. Recombinant MIL-2 strongly inhibited the binding of recombinant human IL-2 (HIL-2) to murine responder cells, but only very weakly inhibited the binding to human responder cells. Moreover, recombinant MIL-2 induced secondary alloantigen specific cytotoxic T lymphocytes (2 degrees CTL) from memory CTL and activated natural killer (NK) cells in murine systems in the same manner as recombinant HIL-2. The results suggest that the species hierarchy (that MIL-2 derived from native cell culture does not act on human T-cells) is due to the protein moiety, not the sugar moiety, and is to be ascribed to the difference in binding affinity of MIL-2 and HIL-2 to murine and human responder cells respectively, and that recombinant MIL-2 shares identical biological and immunological activities with recombinant HIL-2. Thus, MIL-2 might be a convenient tool for extensive studies of the pharmacological and physiological activities of IL-2 in murine models.
将小鼠白细胞介素-2（MIL-2）cDNA插入携带大肠杆菌色氨酸启动子的表达载体中，并在大肠杆菌中表达。大肠杆菌产生的重组MIL-2支持小鼠CTLL-2细胞的生长，但不支持人T细胞母细胞的生长。重组MIL-2强烈抑制重组人IL-2（HIL-2）与小鼠反应细胞的结合，但仅非常微弱地抑制与人类反应细胞的结合。此外，重组MIL-2与重组HIL-2一样，能以相同方式在小鼠系统中从记忆CTL诱导产生二级同种异体抗原特异性细胞毒性T淋巴细胞（2度CTL）并激活自然杀伤（NK）细胞。结果表明，物种层次差异（即源自天然细胞培养的MIL-2对人T细胞无作用）是由于蛋白质部分而非糖部分，这归因于MIL-2和HIL-2分别与小鼠和人类反应细胞结合亲和力的差异，并且重组MIL-2与重组HIL-2具有相同的生物学和免疫学活性。因此，MIL-2可能是在小鼠模型中广泛研究IL-2药理和生理活性的便利工具。
