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Updated: Jun 12, 2026

Characterization of G Protein-coupled Receptors by a Fluorescence-based Calcium Mobilization Assay
Published on: July 28, 2014
Endogenous ligand for an orphan receptor
1Department of Nutritional Sciences and Toxicology, University of California, Berkeley, California, USA. nutritionreviews@ilsi.org
Abstract:
The nuclear receptor peroxisome proliferator-activated receptor alpha (PPARalpha) can be activated pharmacologically by fibrate drugs, lowering triglycerides and raising high-density lipoprotein. However, until recently, the endogenous ligand of PPARalpha had been unknown. A new study reports the identity of a physiologically relevant endogenous PPARalpha ligand as a phospholipid that is dependent upon a nutritionally responsive enzyme, fatty acid synthase. Mass spectrometry identified this phospholipid as 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (16/18-GPC) and as the endogenous ligand of PPARalpha. In vivo experiments involving portal vein infusion of 16/18-GPC induced PPARalpha-dependent expression of the fatty acid metabolism genes acyl CoA oxidase and carnitine palmitoyl transferase.
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