Coagulation factor II thrombin receptor (Proteinase-activated receptor 1) (PAR1)

The coagulation factor II thrombin receptor, commonly referred to as **Proteinase-activated receptor 1 (PAR1)**, is a seven-transmembrane **G protein-coupled receptor**. It is activated by proteolytic cleavage by thrombin, which exposes a new N-terminus that acts as a ligand to initiate signal transduction. This receptor plays a crucial role in regulating platelet activation, vascular integrity, and the cellular response to injury. PAR1 is a validated therapeutic target in thrombotic disorders, and its antagonists, notably vorapaxar, have demonstrated clinical efficacy in reducing thrombotic events. However, therapeutic inhibition of PAR1 carries a risk of bleeding complications due to diminished platelet reactivity[3][5]. The receptor is encoded by the F2R gene and is involved in central pathways of cardiovascular disease, making it important in both research and clinical practice[3][5].

Other names

Proteinase-activated receptor 1PAR1F2R (gene symbol)Thrombin receptorCoagulation factor II receptor

Competitive inhibition of thrombin binding and activation of PAR1; Blocking signal transduction by preventing receptor activation by proteolytic cleavage