induced IL-6 production in alveolar type II epithelial cells further suggests that its function may be cell specific. The exact molecular mechanism whereby C/EBPc regulates gene expression is not clear. In IL-1b-stimulated alveolar epithelial cells, C/EBPc exists as both homodimers and heterodimers . It is possible that the lack of one transactivation domain in C/EBPc:b heterodimers may contribute to the inhibitory effect of C/EBPc. On the other hand, in C/EBPc-overexpressed cells, the major C/EBPc binding species is C/EBPc:c homodimers, suggesting that C/ EBPc:c homodimers may compete with the stimulatory C/EBP b:b to bind to IL-6 promoter region. In addition, we observed an increased C/EBPc:b heterodimers binding to IL-6 promoter in C/EBPc-overexpressed cells C/EBPc Suppresses IL-6 Production 8 C/EBPc Suppresses IL-6 Production . This suggests that there is a free C/ EBPb pool in the nucleus. However, whether C/EBPc is a preferential dimerization partner for C/EBPb or C/EBPc:b heterodimers have a higher affinity than C/EBPb:b in lung epithelial cells remains an open question. Interestingly, C/EBPc does not seem to affect NF-kB DNA binding, suggesting that C/EBPc has no effect on the synergistic activity between NF-kB and C/EBPb in IL-6 promoter in alveolar epithelial cells. Taken together, we identified a previously unrecognized role for C/EBPc in inflammation in alveolar epithelial cells. Not surprisingly, many transcription factors such as NF-kB and C/ EBPb are activated in the acute lung inflammatory reaction. However, our current study suggests that the acute inflammatory response in the lung can also be counter-regulated by other transcription factors such as C/EBPc. Understanding the underlying roles and mechanisms whereby C/EBPc regulates the network of inflammatory system in the lung may be a crucial step for the development of new therapeutic targets for treatment of lung inflammatory diseases. Materials and Methods Cells and Search Here...
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