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Cyclooxygenase-2 catalyses the biosynthesis of prostaglandins from arachidonic acid but also the biosynthesis of prostaglandin glycerol esters (PG-Gs) from 2-arachidonoylglycerol. Previous studies identified PG-Gs as signalling molecules involved in inflammation. Thus, the glyceryl ester of prostaglandin E 2 , PGE 2 -G, mobilizes Ca 2+  and activates protein kinase C and ERK, suggesting the involvement of a G protein-coupled receptor (GPCR). To identify the endogenous receptor for PGE 2 -G, we performed a subtractive screening approach where mRNA from PGE 2 -G response-positive and -negative cell lines was subjected to transcriptome-wide RNA sequencing analysis. We found several GPCRs that are only expressed in the PGE 2 -G responder cell lines. Using a set of functional readouts in heterologous and endogenous expression systems, we identified the UDP receptor P2Y 6  as the specific target of PGE 2 -G. We show that PGE 2 -G and UDP are both agonists at P2Y 6 , but they activate the receptor with extremely different EC 50  values of ~1 pM and ~50 nM, respectively. The identification of the PGE 2 -G/P2Y 6  pair uncovers the signalling mode of PG-Gs as previously under-appreciated products of cyclooxygenase-2.

Prostaglandin E2 glyceryl ester is an endogenous agonist of the nucleotide receptor P2Y6