Evidence for direct binding of fatty acids and eicosanoids to human peroxisome proliferators-activated receptor alpha - PubMed (original) (raw)
. 1999 Jul 14;260(3):609-13.
doi: 10.1006/bbrc.1999.0951.
Affiliations
- PMID: 10403814
- DOI: 10.1006/bbrc.1999.0951
Evidence for direct binding of fatty acids and eicosanoids to human peroxisome proliferators-activated receptor alpha
K Murakami et al. Biochem Biophys Res Commun. 1999.
Abstract
The alpha isoform of peroxisome proliferators-activated receptor (PPAR) is activated by fatty acids, their metabolites, and the fibrate class of lipid-lowering agents. To test the ability of these activators to directly bind the ligand-binding domain of human PPARalpha, we performed a competitive binding assay using radiolabeled [(3)H]KRP-297, a known ligand for human PPARalpha. Long-chain fatty acids and eicosanoids were even more potent ligands for human PPARalpha than the hitherto most potent PPARalpha ligand WY-14,643. Moreover, these natural ligands avidly activated this receptor in a transient transcriptional assay. This study provides the direct evidence that human PPARalpha is activated through the direct binding of fatty acids and eicosanoids, as well as of a fibrate, to its ligand-binding domain.
Copyright 1999 Academic Press.
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