FEBS Lett. 1999 Nov 19;461(3):235-40.

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

Bank U, Küpper B, Reinhold D, Hoffmann T, Ansorge S.

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Institute of Immunology, Center of Internal Medicine, Otto-von-Guericke-University, Leipziger Strasse 44, D-39120, Magdeburg, Germany. ute.bank@medizin.uni-magdeburg.de

Abstract

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.

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