| Literature DB >> 15114678 |
Werner Hallatschek1, Gesa Fiedler, Carsten J Kirschning, Fränzi Creutzburg, Norbert Lamping, Andreas Nüssler, Ralf R Schumann.
Abstract
LPS-binding protein (LBP) is an acute-phase protein with the ability to bind and transfer LPS of Gram-negative bacteria, as well as cell wall compounds of other pathogenic bacteria. This soluble pattern-recognition molecule is present in high concentrations in serum and represents an important defense mechanism of the host. Regulation of the hepatic acute-phase response and its termination are important mechanisms for limiting systemic inflammatory activity of the host organism. We show here that TGF-beta 1, in a dose-dependent fashion, is able to inhibit LBP transcript accumulation and LBP protein synthesis induced by IL-6, IL-1 beta and dexamethasone in hepatoma cell lines. These data were confirmed employing primary human hepatocytes, where TGF-beta 1 also inhibited LBP protein synthesis. We identified and analyzed several Smad-binding sites (Smads are major regulatory elements of TGF-beta 1) within the LBP promoter, and found that one of them was active. We furthermore identified an AP-1-binding site clearly conferring inhibitory effects of TGF-beta 1 towards LBP promoter activity, shown by gel shift and promoter mutagenesis experiments. Further elucidating the mechanism of transcriptional regulation of proteins involved in innate immune responses may potentially help to develop novel intervention strategies for the acute-phase response, sepsis, and septic shock.Entities:
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Year: 2004 PMID: 15114678 DOI: 10.1002/eji.200324874
Source DB: PubMed Journal: Eur J Immunol ISSN: 0014-2980 Impact factor: 5.532