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Induction of Interleukin‐6 Release from Monocytes by Serine Proteinases and its Potential Mechanisms
Author(s) -
Li T.,
Wang H.,
He S.
Publication year - 2006
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.2006.01772.x
Subject(s) - serine , secretion , elastase , trypsin , thrombin , microbiology and biotechnology , chemistry , serine protease , receptor , serine proteinase inhibitors , tryptase , monocyte , enzyme , biochemistry , biology , immunology , protease , mast cell , platelet
Serine proteinases have been recognized playing an important role in inflammation via proteinase‐activated receptors (PAR). However, little is known of the influence of serine proteinases and PAR on interleukin‐6 (IL‐6) secretion from highly purified monocytes. We challenged monocytes from human peripheral blood with serine proteinases and agonist peptides of PAR and measured the levels of IL‐6, IL‐1β and IL‐12 in culture supernatants by enzyme‐linked immunosorbent assay. The results showed that thrombin, trypsin, tryptase and elastase stimulated approximately up to 2.9‐, 2.0‐, 1.8‐ and 2.1‐fold increase in IL‐6 release from monocytes following 16 h of incubation, respectively. Proteinase inhibitors inhibited the actions of proteinases on monocytes. Agonist peptides of PAR‐1 (SFLLR‐NH 3 ) and PAR‐4 (GYPGQV‐NH 2 ), but not PAR‐3 (TFRGAP‐NH 2 ), also induced IL‐6 release from monocytes. The proteinases and agonists of PAR failed to stimulate IL‐1β and IL‐12 secretion. In conclusion, the induction of IL‐6 secretion by serine proteinases may be through the activation of PAR.