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Induction of IL‐6 release from human T cells by PAR‐1 and PAR‐2 agonists
Author(s) -
Li Tao,
He Shaoheng
Publication year - 2006
Publication title -
immunology and cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0818-9641
DOI - 10.1111/j.1440-1711.2006.01456.x
Subject(s) - chemistry , microbiology and biotechnology , pharmacology , biology
Proteinase‐activated receptors (PAR) have been recognized as playing an important role in inflammation and immune response. However, little is known of the expression and function of PAR on human T cells. In this study, the expression of PAR on highly purified human T cells was determined and the secretion of IL‐6 from cultured T cells in response to serine proteinases and agonist peptides of PAR was examined. The results showed that T cells express PAR‐1, PAR‐2 and PAR‐3 proteins and genes. Thrombin, trypsin and tryptase, but not elastase, were able to stimulate concentration‐dependent secretion of IL‐6 from T cells following a 16 h incubation period. The specific inhibitors of thrombin, trypsin and tryptase inhibited the actions of these proteinases on T cells, indicating that the enzymatic activity is essential for their actions. Agonist peptides of PAR SFLLR‐NH 2 , TFLLRN‐NH 2 and SLIGKV‐NH 2 , but not TFRGAP‐NH 2 , GYPGQV‐NH 2 and AYPGKF‐NH 2 , are also capable of inducing IL‐6 release from T cells. In conclusion, induction of IL‐6 secretion from T cells by thrombin, trypsin and tryptase is probably through the activation of PAR, suggesting that serine proteinases are involved in the regulation of immune response of the body.