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• W2100375780 abstract "We previously demonstrated that cholesterol deprivation increases endothelial cyclooxygenase-2 (COX-2)-dependent prostacyclin [prostaglandin I₂ (PGI₂)] production in vitro. Cholesterol directly regulates gene transcription through the sterol response element binding protein (SREBP). In this work, we demonstrate that SREBP directly regulates COX-2 expression. Cholesterol reduces human COX-2 promoter-luciferase reporter construct activity in transiently transfected endothelial cells. Conversely, cotransfection with a constitutively active mutant SREBP increases COX-2 promoter activity. SREBP-1a and -2 specifically bind a putative sterol response element (SRE) sequence in the COX-2 promoter. This sequence competes for SREBP binding to a low density lipoprotein receptor consensus sequence in an electromobility-shift assay. These data indicate that endothelial COX-2 is regulated by cholesterol via the SREBP pathway. The present study identifies COX-2 as the first vascular gene without a clear role in lipid metabolism transactivated by SREBP, and suggests that enhanced production of PGI₂ through this pathway may be an additional benefit of cholesterol-lowering therapies." @default.
• W2100375780 created "2016-06-24" @default.
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• W2100375780 date "2005-05-01" @default.
• W2100375780 modified "2023-10-13" @default.
• W2100375780 title "The sterol response element binding protein regulates cyclooxygenase-2 gene expression in endothelial cells" @default.
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• W2100375780 doi "https://doi.org/10.1194/jlr.m500021-jlr200" @default.
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