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• W2023341675 abstract "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." @default.
• W2023341675 created "2016-06-24" @default.
• W2023341675 creator A5029506792 @default.
• W2023341675 creator A5073510977 @default.
• W2023341675 date "2006-10-01" @default.
• W2023341675 modified "2023-09-26" @default.
• W2023341675 title "Induction of IL‐6 release from human T cells by PAR‐1 and PAR‐2 agonists" @default.
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• W2023341675 doi "https://doi.org/10.1111/j.1440-1711.2006.01456.x" @default.
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