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They form heterodimers with the retinoid X receptor (RXR) and activate transcription by binding to a specific DNA element termed the PPAR response element (PPRE) </csml:comment>
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They form heterodimers with the retinoid X receptor (RXR) and activate transcription by binding to a specific DNA element termed the PPAR response element (PPRE)
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For example, the PPARγ ligand troglitazone increased expression of the chemokine MCP-1 (CCL2) and enhanced monocyte/macrophage infiltration in a rat model of glomerulonephritis, and the PPARδ ligand GW0742 worsened the course of colitis in IL-10-deficient mice</csml:comment>
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For example, the PPARgamma ligand troglitazone increased expression of the chemokine MCP-1 (CCL2) and enhanced monocyte/macrophage infiltration in a rat model of glomerulonephritis, and the PPARdelta ligand GW0742 worsened the course of colitis in IL-10-deficient mice
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For example, the PPARgamma ligand troglitazone increased expression of the chemokine MCP-1 (CCL2) and enhanced monocyte/macrophage infiltration in a rat model of glomerulonephritis, and the PPARδ ligand GW0742 worsened the course of colitis in IL-10-deficient mice
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Repression of lipopolysaccharide (LPS)-induced iNOS (NOS2) gene expression in macrophages has been characterized in detail</csml:comment>
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In the “off” state, the iNOS gene is actively repressed by a multisubunit complex containing NCoR, histone deacetylase 3 (HDAC3), TBL1, and TBLR1.</csml:comment>
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When LPS binds to TLR4, the NF-KappaB signaling pathway is activated, IKappaB is degraded, and NF-KappaB p65-p50 heterodimers enter the nucleus.</csml:comment>
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When LPS binds to TLR4, the NF-KappaB signaling pathway is activated, IKappaB is degraded, and NF-KappaB p65-p50 heterodimers enter the nucleus.
</csml:comment>
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<csml:comment type="text">PMID: 17981503
When LPS binds to TLR4, the NF-KappaB signaling pathway is activated, IKappaB is degraded, and NF-KappaB p65-p50 heterodimers enter the nucleus.
</csml:comment>
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<csml:comment type="text">PMID: 17981503
When LPS binds to TLR4, the NF-KappaB signaling pathway is activated, IKappaB is degraded, and NF-KappaB p65-p50 heterodimers enter the nucleus.
</csml:comment>
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<csml:comment type="text">PMID: 17981503
Concomitant with these events, the corepressor complex is ubiquitinated and degraded by the 19 S proteasome.</csml:comment>
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Concomitant with these events, the corepressor complex is ubiquitinated and degraded by the 19 S proteasome.</csml:comment>
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NF-KappaB p65-p50 heterodimers bind to the KappaB element located in the iNOS promoter, facilitating the recruitment of coactivator complexes and activation of iNOS gene transcription.</csml:comment>
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NF-KappaB p65-p50 heterodimers bind to the KappaB element located in the iNOS promoter, facilitating the recruitment of coactivator complexes and activation of iNOS gene transcription.</csml:comment>
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NF-KappaB p65-p50 heterodimers bind to the KappaB element located in the iNOS promoter, facilitating the recruitment of coactivator complexes and activation of iNOS gene transcription.</csml:comment>
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In cells treated with PPARgamma ligand plus LPS, ligand binding triggers conjugation of a small fraction of cellular PPARgamma with SUMO1 (small ubiquitin-like modifier) on lysine 365 (K365), mediated by the SUMOylation pathway E2 ligase Ubc9 and E3 ligase PIAS1

PMID: 17981503
Figure 2</csml:comment>
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The SUMOylated PPARgamma binds to NCoR and interferes with clearance of the corepressor complex, thereby maintaining the promoter in the repressed state</csml:comment>
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SUMOylation of PPARgamma is predicted to prevent its heterodimerization with RXR, thereby dedicating this form of PPARgamma to a repressor function.</csml:comment>
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<csml:comment type="text">PMID: 17981503,12970571
Binding of ligand to PPARdelta releases BCL-6, which then represses inflammatory-response genes

PMID: 17981503,17218271
The liver X receptors (LXRalpha and -beta) repress a subset of inflammatory-response genes that overlaps with, yet is distinct from, the subset repressed by PPARgamma</csml:comment>
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Direct binding of PPARalpha to NF-KappaB p65 was demonstrated by in vitro assays, suggesting that transrepression might involve direct interference with transcriptional activation by NF-KappaB</csml:comment>
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Binding of ligand to PPARdelta releases BCL-6, which then represses inflammatory-response genes
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Binding of ligand to the LXRs triggers covalent conjugation with SUMO2 and -3.</csml:comment>
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Binding of ligand to the LXRs triggers covalent conjugation with SUMO2 and -3.</csml:comment>
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Binding of ligand to the LXRs triggers covalent conjugation with SUMO2 and -3

PMID: 17981503
Here, the E3 ligase is HDAC4 rather than PIAS1.

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As with PPARgamma, SUMOylated LXR interferes with clearance of NCoR-containing corepressor complexes from the promoters of target genes.</csml:comment>
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Binding of ligand to the LXRs triggers covalent conjugation with SUMO2 and -3

PMID: 17981503
Here, the E3 ligase is HDAC4 rather than PIAS1.

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As with PPARgamma, SUMOylated LXR interferes with clearance of NCoR-containing corepressor complexes from the promoters of target genes.</csml:comment>
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Ligand-bound GR interacts strongly with the p65 subunit of NF-KappaB, in contrast to ligand-bound PPARgamma, which interacts very weakly with p65</csml:comment>
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Ligand-bound GR interacts strongly with the p65 subunit of NF-KappaB, in contrast to ligand-bound PPARgamma, which interacts very weakly with p65</csml:comment>
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<csml:comment type="text">PMID: 17981503,15879558
Interestingly, repression by GR of tumor necrosis factor (TNF)-stimulated gene transcription in A549 lung adenocarcinoma cells is also target-gene specific: some NF-KappaB-dependent genes such as IL-8 (CXCL8) are repressed, whereas others, such as IKappaBalpha, are not</csml:comment>
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In the case of AP-1, several mechanisms for transrepression by nuclear receptors have been identified, including inhibition of c-Jun N-terminal kinase (JNK) signaling by GR, and direct interaction of PPARalpha with c-Jun, resulting in interference with transcriptional activation</csml:comment>
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PPARgamma ligands inhibit DC maturation and repress the expression by DC of CD1a, CD40, CD83, CCR7, and the costimulatory molecule CD80 (B7.1)</csml:comment>
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PPARgamma ligands inhibit DC maturation and repress the expression by DC of CD1a, CD40, CD83, CCR7, and the costimulatory molecule CD80 (B7.1)</csml:comment>
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PPARgamma ligands inhibit DC maturation and repress the expression by DC of CD1a, CD40, CD83, CCR7, and the costimulatory molecule CD80 (B7.1)</csml:comment>
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PPARgamma ligands inhibit DC maturation and repress the expression by DC of CD1a, CD40, CD83, CCR7, and the costimulatory molecule CD80 (B7.1)</csml:comment>
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PPARgamma ligands also repress DC production of IL-12 and several chemokines, including CXCL10 and RANTES</csml:comment>
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PPARgamma ligands also repress DC production of IL-12 and several chemokines, including CXCL10 and RANTES</csml:comment>
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PPARgamma ligands also repress DC production of IL-12 and several chemokines, including CXCL10 and RANTES</csml:comment>
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The PPARalpha ligand fenofibrate represses IFNgamma expression in anti-CD3-treated cultured human CD4+ lymphocytes</csml:comment>
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<csml:comment type="text">PMID: 17981503,11884448
Similarly, another PPARalpha ligand, Wy14643, represses IFNgamma in activated mouse splenocytes</csml:comment>
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<csml:comment type="text">PMID: 17981503,17631136
More recently, fenofibrate has been shown to repress IL-17 expression in cultured splenocytes activated by PMA plus ionomycin and by Th17 cells in a pathogenic CD4+ T-cell line cultured from C3H Bir mice treated with cecal bacterial antigens </csml:comment>
</csml:comments>
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<csml:comment type="text">PMID: 17981503
Expression of the adhesion molecules ICAM-1, and -2, and VCAM-1 is induced by proinflammatory cytokines, including TNFalpha.

PMID: 17981503,10377075,16115476,16439686
PPARalpha is expressed in vascular endothelial cells, and PPARalpha ligands repress TNFalpha-elicited expression of VCAM-1 by these cells</csml:comment>
</csml:comments>
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<csml:comment type="text">PMID: 17981503
Expression of the adhesion molecules ICAM-1, and -2, and VCAM-1 is induced by proinflammatory cytokines, including TNFalpha.

PMID: 17981503,10377075,16115476,16439686
PPARalpha is expressed in vascular endothelial cells, and PPARalpha ligands repress TNFalpha-elicited expression of VCAM-1 by these cells</csml:comment>
</csml:comments>
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</csml:processKinetic>
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<csml:comments>
<csml:comment type="text">PMID: 17981503
Expression of the adhesion molecules ICAM-1, and -2, and VCAM-1 is induced by proinflammatory cytokines, including TNFalpha.

PMID: 17981503,10377075,16115476,16439686
PPARalpha is expressed in vascular endothelial cells, and PPARalpha ligands repress TNFalpha-elicited expression of VCAM-1 by these cells</csml:comment>
</csml:comments>
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<csml:comments>
<csml:comment type="text">indirect</csml:comment>
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<csml:priority value="0"/>
<csml:firing firingOnce="false" firingStyle="csml-firingStyle:and" type="csml-variable:Boolean" value="true"/>
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<csml:parameter key="coefficient2" value="1.0"/>
<csml:parameter key="coefficient1" value="0.1"/>
</csml:processKinetic>
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<csml:biologicalProperty refBiologicalEventID="cso30:i:ME_GeneExpression" refCellComponentID="cso30:i:CC_Cytosol"/>
<csml:comments>
<csml:comment type="text">PMID: 17981503,16798734
Interestingly, the proinflammatory cytokine IL-17 induces CXCL8 gene transcription and also stabilizes CXCL8 mRNA via a p38 MAP kinase-dependent pathway</csml:comment>
</csml:comments>
</csml:process>
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PMID: 17981503,17486092 
For example, in chronic inflammatory diseases perpetuated by effector T cells, activated Th1 cells are attracted to the site of inflammation by chemokines that interact with the CXCR3 receptor, including CXCL9, -10, and -11

PMID: 17981503,11208713
Expression of these chemokines is highly induced by the combination of IFNgamma and TNFalpha</csml:comment>
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In a recent microarray survey of genes highly induced by LPS in mouse macrophages, the PPARgamma ligand GW7845 repressed expression of several chemokine genes, including those encoding CXCL1, -9, and -10 as well as CCL2, -4, -7, -12, -17, and -19, by &gt;40%.</csml:comment>
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The PPARalpha ligands fenofibrate and GW7647 also repress CXCL10 mRNA expression and promoter activity in human HT-29 cells, a model for colonic epithelial cells</csml:comment>
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The PPARalpha ligands fenofibrate and GW7647 also repress CXCL10 mRNA expression and promoter activity in human HT-29 cells, a model for colonic epithelial cells</csml:comment>
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For example, in chronic inflammatory diseases perpetuated by effector T cells, activated Th1 cells are attracted to the site of inflammation by chemokines that interact with the CXCR3 receptor, including CXCL9, -10, and -11</csml:comment>
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<csml:comment type="text">PMID: 17981503,17486092 
For example, in chronic inflammatory diseases perpetuated by effector T cells, activated Th1 cells are attracted to the site of inflammation by chemokines that interact with the CXCR3 receptor, including CXCL9, -10, and -11

PMID: 17981503,11208713
Expression of these chemokines is highly induced by the combination of IFNgamma and TNFalpha</csml:comment>
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PMID: 17981503,11208713
Expression of these chemokines is highly induced by the combination of IFNgamma and TNFalpha</csml:comment>
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For example, in chronic inflammatory diseases perpetuated by effector T cells, activated Th1 cells are attracted to the site of inflammation by chemokines that interact with the CXCR3 receptor, including CXCL9, -10, and -11</csml:comment>
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PMID: 17981503,11208713
Expression of these chemokines is highly induced by the combination of IFNgamma and TNFalpha</csml:comment>
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For example, in chronic inflammatory diseases perpetuated by effector T cells, activated Th1 cells are attracted to the site of inflammation by chemokines that interact with the CXCR3 receptor, including CXCL9, -10, and -11</csml:comment>
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PPARgamma then represses expression of the inflammatory-response gene Egr-1.</csml:comment>
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Recently, suppression of the inflammatory response by CO in macrophages has been ascribed to a CO-mediated burst of reactive oxygen species, which induce the expression of PPARgamma</csml:comment>
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Recently, suppression of the inflammatory response by CO in macrophages has been ascribed to a CO-mediated burst of reactive oxygen species, which induce the expression of PPARgamma</csml:comment>
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Recent studies have demonstrated that PPARdelta binds to ERK5 and is required for ERK5-mediated repression of NF-KappaB </csml:comment>
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