Prostaglandin E receptor 1 (EP1) (EP1)

Prostaglandin E receptor 1 (EP1), encoded by the PTGER1 gene, is a G protein-coupled receptor (GPCR) that serves as one of the four primary receptors for prostaglandin E2 (PGE2) [3, 8]. Upon activation, EP1 typically couples with Gq proteins to trigger the phosphatidylinositol-calcium second messenger system, resulting in increased intracellular calcium levels and the activation of protein kinase C (PKC) [1, 8]. This signaling pathway is fundamental to several physiological processes, including the contraction of smooth muscle, the modulation of renal function, and the regulation of systemic blood pressure [4, 8, 12]. EP1 is also a key mediator of nociception, where it amplifies pain signals in response to inflammatory stimuli [2, 4, 5]. In pathological contexts, EP1 is significantly involved in chronic pain, inflammation, and various malignancies, where its overexpression often correlates with tumor progression and metastasis [1, 2, 12]. It has also been identified as a contributor to neurovascular damage and blood-brain barrier breakdown following ischemic stroke [15, 16]. Pharmacological targeting of EP1 includes the development of selective antagonists to treat pain and inflammatory conditions without the systemic side effects associated with non-selective cyclooxygenase (COX) inhibitors [2, 4]. Conversely, EP1 agonists are explored for their potential in neuroprotection and specific smooth muscle modulation [1].

Other names

PTGER1 [3, 6, 8]EP1 receptor [3, 6]Prostaglandin E2 receptor 1 [3, 8]PGE receptor EP1 subtype [6, 8]Prostanoid EP1 receptor [6, 8]

EP1 agonists mimic the action of PGE2 by selectively activating the receptor, which triggers Gq-mediated increases in intracellular calcium and activates protein kinase C (PKC) [1, 3, 8]. EP1 antagonists work by blocking the binding of PGE2 to the receptor, thereby preventing the downstream signaling events that lead to pain amplification and inflammatory responses [2, 15].