FP

Prostaglandin receptor FP (PTGFR) is a rhodopsin-like G protein-coupled receptor that binds prostaglandin F_2α (PGF_2α) and mediates contractile and remodeling responses in multiple tissues^[1][2]. Upon activation, FP primarily couples to G_q-dependent signaling, triggering phospholipase C activation, intracellular Ca²⁺ mobilization, protein kinase C signaling, and downstream MAPK-related pathways that regulate cellular contraction, proliferation, and gene expression^[1][3]. These signaling mechanisms are particularly important in smooth muscle-containing tissues, including the uterus, where FP functions as a contractile prostanoid receptor and contributes to physiological responses associated with PGF_2α signaling^[1][2]. In disease and experimental models, FP signaling has been linked to regulation of intraocular pressure, cardiovascular function, vascular remodeling, and bone turnover, making the receptor a useful target for mechanistic studies of prostanoid biology^[1][4]. Compared with related prostanoid receptor isoforms that preferentially recognize other prostaglandins, FP exhibits highest responsiveness to PGF_2α and is encoded by alternatively spliced transcript variants that generate the FP_A and FP_B isoforms with distinct C-terminal regions^[1][2]. For experimental and translational applications, selective FP agonists including latanoprost, travoprost, tafluprost, and fluprostenol are widely used to activate FP signaling, particularly in ocular research and glaucoma models where enhanced aqueous humor outflow lowers intraocular pressure^[1][4]. Collectively, the PGF_2α-FP axis represents a well-characterized prostanoid signaling pathway with broad utility for studying receptor-mediated contraction, tissue remodeling, and therapeutic modulation of prostaglandin responses^[1][3][4].