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Papers In Press, published online ahead of print June 23, 2004
Huntsman Cancer Institute, University of Utah, Salt Lake City, UT 84112-5550
Corresponding Author: diana.stafforini{at}hci.utah.edu
Administration of lipopolysaccharide (LPS) to experimental animals results in the upregulation of expression of the plasma form of platelet-activating factor acetylhydrolase (PAF-AH) in tissue macrophages. To investigate the mechanism underlying induction of PAF-AH by LPS we used murine RAW264.7 and human THP-1 macrophages as model systems. We found that the p38 mitogen-activated protein kinase (p38-MAPK) pathway mediates transcriptional activation of the PAF-AH gene through the participation of nt -68/-316 relative to the transcriptional initiation site. This promoter region spans two Sp1/Sp3 binding sites (SP-A and SP-B) and is necessary and sufficient for the observed effect. Disruption of these Sp-binding sites significantly reduces promoter activity in LPS-stimulated cells. The ability of LPS to induce transcriptional activation of PAF-AH is not due to enhanced Sp1/Sp3 binding to the promoter but involves enhanced transactivation function of Sp1 via p38-MAPK activation. These studies characterize the mechanism by which LPS modulates expression of PAF-AH at the transcriptional level and they have important implications for our understanding of responses that occur during the development of LPS-mediated inflammatory diseases.
J. Biol. Chem, 10.1074/jbc.M402454200
Submitted on March 4, 2004
Revised on June 22, 2004
Accepted on June 23, 2004
The p38-MAPK pathway mediates transcriptional activation of the plasma PAF acetylhydrolase gene in macrophages stimulated with Lipopolysaccharide
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