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- W2007288510 abstract "Peroxisome proliferator-activated receptor (PPARs) modulate target gene expression in response to unsaturated fatty acid ligands, such as arachidonic acid (AA). Here, we report that the AA metabolite 15-hydroxyeicosatetraenoic acid (15-HETE) activates the ligand-dependent activation domain (AF2) of PPARβ/δ in vivo, competes with synthetic agonists in a PPARβ/δ ligand binding assay in vitro, and triggers the interaction of PPARβ/δ with coactivator peptides. These agonistic effects were also seen with PPARα and PPARγ, but to a significantly weaker extent. We further show that 15-HETE strongly induces the expression of the bona fide PPAR target gene <i>Angptl4</i> in a PPARβ/δ-dependent manner and, conversely, that inhibition of 15-HETE synthesis reduces PPARβ/δ transcriptional activity. Consistent with its function as an agonistic ligand, 15-HETE triggers profound changes in chromatin-associated PPARβ/δ complexes in vivo, including the recruitment of the coactivator cAMP response element-binding protein binding protein. Both 15R-HETE and 15S-HETE are similarly potent at inducing PPARβ/δ coactivator binding and transcriptional activation, indicating that 15-HETE enantiomers generated by different pathways function as PPARβ/δ agonists." @default.
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- W2007288510 date "2009-11-10" @default.
- W2007288510 modified "2023-10-15" @default.
- W2007288510 title "15-Hydroxyeicosatetraenoic Acid Is a Preferential Peroxisome Proliferator-Activated Receptor β/δ Agonist" @default.
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- W2007288510 doi "https://doi.org/10.1124/mol.109.060541" @default.
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