| 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. |
| Authors | U Bank, B Küpper, D Reinhold, T Hoffmann, S Ansorge
(Affiliation: Institute of Immunology, Center of Internal Medicine, Otto-von-Guericke-University, Leipziger Strasse 44, D-39120, Magdeburg, Germany. ute.bank at medizin.uni-magdeburg.de)
|
| Journal | FEBS letters
(FEBS Lett)
Vol. 461
Issue 3
Pg. 235-40
(Nov 19 1999)
ISSN: 0014-5793 NETHERLANDS |
| PMID | 10567703
(Publication Type: Comparative Study, Journal Article)
|
| Chemical References |
- Interleukin-6
- Cathepsins
- Serine Endopeptidases
- cathepsin G
- Leukocyte Elastase
- Myeloblastin
|
| Topics |
- Cathepsins
(physiology)
- Exudates and Transudates
(enzymology, immunology)
- Feedback
- Humans
- Inflammation
(enzymology, immunology)
- Interleukin-6
(analysis, antagonists & inhibitors)
- Leukocyte Elastase
(physiology)
- Myeloblastin
- Neutrophils
(enzymology)
- Serine Endopeptidases
(physiology)
|
