Evidence for a crucial role of neutrophil-derived serine proteases in the inactivation of interleukin-6 at sites of inflammation

被引:50
作者
Bank, U
Küpper, B
Reinhold, D
Hoffmann, T
Ansorge, S
机构
[1] Otto Von Guericke Univ, Ctr Internal Med, Inst Immunol, D-39120 Magdeburg, Germany
[2] Otto Von Guericke Univ, Ctr Internal Med, Inst Expt Internal Med, D-39120 Magdeburg, Germany
[3] Probiodrug, D-06120 Halle, Germany
来源
FEBS LETTERS | 1999年 / 461卷 / 03期
关键词
D O I
10.1016/S0014-5793(99)01466-0
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
The bioactivity of interleukin-6 (IL-6) was found to be dramatically reduced in fluids from sites of inflammation, Here, we provide evidence that the neutrophil-derived serine proteases elastase, proteinase 3 and cathepsin G are mainly involved in its degradation and subsequent inactivation. The initially hydrolyzed peptide bonds were detected to be Val(11)-Ala(12) and Leu(19)-Thr(20) (elastase), Phe(78)-Asn(79) (cathepsin G) and Ala(145)-Ser(146) (proteinase 3), The soluble IL-6 receptor elicits a protective effect against the IL-6 inactivation by cathepsin G only. The inactivation of IL-6 by neutrophil-derived serine proteases might act as a feedback mechanism terminating the IL-6-induced activation of neutrophils. (C) 1999 Federation of European Biochemical Societies.
引用
收藏
页码:235 / 240
页数:6
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