Krakauer T
J Leukoc Biol. 1985 May;37(5):511-8. doi: 10.1002/jlb.37.5.511.
A protein with interleukin 1 (IL-1) activity was obtained from the human acute monocytic leukemia cell line (THP-1) and purified by ultrafiltration, Ultrogel AcA54 chromatography, isoelectric focusing, and discontinuous polyacrylamide gel electrophoresis. Like the pI 6.8 species of IL-1 from human peripheral blood monocytes (PBM), the cell line IL-1 has a molecular weight (MW) of 14,000, a pI of 6.8, is heat labile, and does not bind to concanavalin A-Sepharose. Chemical modification of arginine residues by phenylglyoxal or sulfhydryl groups by N-ethyl maleimide and iodoacetamide completely destroys the activity of IL-1 from THP-1 cells as well as that of the pI 6.8 component from PBM. In contrast, the pI 5.1 component of PBM IL-1 is resistant to heat denaturation and sulfhydryl reagents, although it is totally inactivated by phenylglyoxal. IL-1 from THP-1 cells enhanced the proliferative response of the same subpopulations of PNA- thymocytes as IL-1 from PBM. These observations suggest that IL-1 derived from this cell line is similar to the IL-1 pI 6.8 species produced by human monocytes, and distinct from the pI 5.1 species.
从人急性单核细胞白血病细胞系（THP-1）中获得了一种具有白细胞介素1（IL-1）活性的蛋白质，并通过超滤、Ultrogel AcA54层析、等电聚焦和不连续聚丙烯酰胺凝胶电泳进行纯化。与来自人外周血单核细胞（PBM）的pI 6.8的IL-1一样，细胞系IL-1的分子量（MW）为14,000，pI为6.8，对热不稳定，且不与伴刀豆球蛋白A-琼脂糖结合。用苯乙二醛对精氨酸残基进行化学修饰，或用N-乙基马来酰亚胺和碘乙酰胺对巯基进行化学修饰，会完全破坏THP-1细胞来源的IL-1以及PBM来源的pI 6.8组分的活性。相比之下，PBM来源的IL-1的pI 5.1组分对热变性和巯基试剂具有抗性，尽管它会被苯乙二醛完全灭活。THP-1细胞来源的IL-1增强了与PBM来源的IL-1相同亚群的PNA-胸腺细胞的增殖反应。这些观察结果表明，源自该细胞系的IL-1与人单核细胞产生的IL-1的pI 6.8组分相似，且与pI 5.1组分不同。
