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Prostaglandin F2 alpha synthase is an enzyme responsible for converting precursor prostaglandins (PGD2, PGH2, PGE2) to PGF2α, a bioactive lipid that mediates diverse biological functions such as uterine contraction, luteolysis, and inflammation[1][5][7][6]. The enzyme belongs to the aldo-keto reductase (AKR) family, most notably AKR1C3 in humans, and uses NADPH as a cofactor for reduction reactions[1][5]. It is mainly expressed in the lung and liver, but its activity is relevant across many tissues, particularly the reproductive system. Multiple isoforms and related enzymes contribute to PGF2α synthesis, with functional overlap in lipid metabolism and steroid transformation[7][5]. Disorders involving PGFS often manifest in reproductive health and inflammation, though the enzyme itself is an indirect drug target (most therapeutics act on the FP receptor downstream of PGF2α production). Clarifying Note: There is frequent confusion between Prostaglandin F2 alpha synthase (the enzyme) and the Prostaglandin F2-alpha receptor (FP receptor). Most drugs act on the receptor, but the synthase is molecularly and therapeutically distinct[1][4][5][8]. If you seek information on the receptor, use "Prostaglandin F2-alpha receptor (FP receptor; PTGFR)". If you want the biosynthetic enzyme, "Prostaglandin F2 alpha synthase (PGFS, AKR1C3)" is correct.
Drugs such as dinoprost mimic PGF2α produced by PGFS, activating the FP receptor to stimulate uterine contraction or lower intraocular pressure
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