Oxidized Phospholipids Induce Expression of Human Heme Oxygenase-1 Involving Activation of cAMP-responsive Element-binding Protein *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 278, Issue: 51, Page: 51006-51014
2003
- 176Citations
- 59Captures
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Metrics Details
- Citations176
- Citation Indexes176
- 176
- CrossRef155
- Captures59
- Readers59
- 59
Article Description
Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, protects against oxidative stress, and shows potent anti-inflammatory effects. Oxidized phospholipids, which are generated during inflammation and apoptosis, modulate the inflammatory response by inducing the expression of several genes including HO-1. Here we investigated the signaling pathways and transcriptional events involved in the induction of HO-1 gene expression by oxidized 1-palmitoyl-2-arachidonoyl- sn -glycero-3-phosphorylcholine (OxPAPC) in human umbilical vein endothelial cells. OxPAPC up-regulated HO-1 mRNA and protein in a time- and concentration-dependent manner, whereas pro-inflammatory agents like TNF-α and lipopolysaccharide did not significantly induce HO-1 expression in human umbilical vein endothelial cells. Signaling pathways involved in the OxPAPC-mediated HO-1 induction included protein kinases A and C, as well as the mitogen-activated protein kinases p38 and ERK. The cAMP-responsive element-binding protein (CREB) was phosphorylated via these pathways in response to OxPAPC treatment and expression of a dominant-negative mutant of CREB inhibited OxPAPC-induced activity of a human heme oxygenase-1 promoter-driven luciferase reporter construct. We identified a cAMP-responsive element and a Maf recognition element to be involved in the transcriptional activation of the HO-1 promoter by OxPAPC. In gel shift assays we observed binding of CREB to the cAMP-responsive element after OxPAPC treatment. Induction of HO-1 expression by lipid oxidation products via CREB may represent a feedback mechanism to limit inflammation and associated tissue damage.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S002192582075355X; http://dx.doi.org/10.1074/jbc.m304103200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0345803942&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/14523007; http://www.jbc.org/lookup/doi/10.1074/jbc.M304103200; https://syndication.highwire.org/content/doi/10.1074/jbc.M304103200; https://linkinghub.elsevier.com/retrieve/pii/S002192582075355X; https://dx.doi.org/10.1074/jbc.m304103200
American Society for Biochemistry & Molecular Biology (ASBMB)
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