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Neutrophil elastase up-regulates interleukin-8 gene expression via a pathway involving interleukin-1 receptor-associated kinase in human bronchial epithelium

Previously it has been shown that neutrophil elastase (NE) can induce interleukin-8 (IL-8) expression in bronchial epithelial cells (BECs). We have elucidated the intracellular mechanism by which this occurs. Time course and dose response studies showed that stimulation of 16HBE140cells with N E (10 nM, 4h) induced maximal IL-8 promoter activity, IL-8 gene expression and IL-8 protein production as assessed by reporter gene assays, quantitative RT-PCRs and ELISAs, respectively. These responses were inhibited by actinomycin D, indicating a transciptional regulatory mechanism. Using electrophorestic mobility shift assays we demonstrated that NFkappaB, specifically the p50/65 heterodimer, was activated in reponse to NE and that this activation correlated with a concomitant degradation of IkappaB-P. In addition, interleukin-1 receptor-associated kinase (1RAK)was degraded following NE stimulation of 16HBE140cells, implicating it as a signal transducer for N E in this pathway in human BECs.