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Papers In Press, published online ahead of print January 25, 2005
Department of Pathology, Children's Hospital Boston, Boston, MA 02115
Corresponding Author: tcollins{at}rics.bwh.harvard.edu
E-selectin plays a role in the binding and extravasation of leukocytes from the bloodstream. The E-selectin gene is rapidly and transiently expressed by endothelial cells activated by inflammatory stimuli. Despite the identification of factors critical for cytokine-induced activation of the E-selectin promoter, little is known about the mechanisms that restrict the gene's expression to endothelial cells. We used in vivo approaches to characterize the E-selectin promoter in primary cultures of human umbilical vein endothelial cells and umbilical artery smooth muscle cells. In endothelial cells specifically, nucleosomes are remodeled after TNF
J. Biol. Chem, 10.1074/jbc.M412997200
Submitted on November 17, 2004
Revised on January 19, 2005
Accepted on January 25, 2005
Chromatin modifications and the endothelial-specific activation of the E-selectin gene
induction. Chromatin immunoprecipitation (ChIP) analysis demonstrated the binding of the p65 (RelA) component of nuclear factor-
B (NF-B) to the endogenous E-selectin promoter after TNF stimulation, along with IB kinase (IKK). Multiple coactivators, including p300, SRC-1 (steroid receptor coactivator-1) and p/CAF (p300/CBP associated factor) localize differentially to the E-selectin promoter. Additionally, TNF induced localized histone hyperacetylation, phosphorylation and methylation in the E-selectin gene specifically in endothelial cells. Post-induction repression of E-selectin expression is associated with recruitment of multiple deacetylases. Collectively, these studies suggest a model for the selective induction of the E-selectin gene in which the core promoter chromatin architecture is specifically modified in endothelial cells.
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