Cloning and expression of interleukin-18 binding protein

被引:112
作者
Aizawa, Y [1 ]
Akita, K [1 ]
Taniai, M [1 ]
Torigoe, K [1 ]
Mori, T [1 ]
Nishida, Y [1 ]
Ushio, S [1 ]
Nukada, Y [1 ]
Tanimoto, T [1 ]
Ikegami, H [1 ]
Ikeda, M [1 ]
Kurimoto, M [1 ]
机构
[1] Hayashibara Biochem Labs, Fujisaki Inst, Okayama 7028006, Japan
关键词
interleukin-18 binding protein; interleukin-18; receptor; complex; antagonist;
D O I
10.1016/S0014-5793(99)00148-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Interleukin-18 binding protein is a novel glycoprotein that we successfully cloned and expressed. First, murine interleukin-18 binding protein was purified from the sera of mice with endotoxin shock using ligand affinity chromatography. The murine interleukin-18 binding protein cDNA was cloned after RT-PCR using mixed primer pair sequences based on partial murine interleukin-18 binding protein amino acid sequence analysis. Subsequently, human interleukin-18 binding protein cDNA was cloned from cDNA libraries of normal human liver using murine interleukin-18 binding protein cDNA as a probe. Next, we transiently expressed recombinant human and murine interleukin-18 binding proteins in COS-1 cells and purified them from culture supernatants. Both recombinant interleukin-18 binding proteins did not exhibit species specificity and prevented interleukin-18 binding to its receptor. In addition, they inhibited interleukine-18 dependent IFN-gamma production from KG-1 cells effectively. These results suggest that the interleukin-18 binding protein may possess interleukine-18 antagonist activity. (C) 1999 Federation of European Biochemical Societies.
引用
收藏
页码:338 / 342
页数:5
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