Protease activated receptors

Protease-activated receptors (PARs, also known as thrombin receptors) are G-protein-coupled receptors which are activated by cleavage of their N-terminal domains by serine proteases. Cleavage produces a tethered peptide ligand, which influences transmembrane signaling.  Four subtypes of receptors been cloned (PAR1-4).  PAR1 is the most well characterized member of this receptor family and is activated by the endogenous serine protease thrombin.  PAR1 activation has been implicated in cardiovascular diseases.

Further reading

Ossovskaya and Bunnett (2004) Protease-Activated Receptors: Contribution to Physiology and Disease. Physiological Rev. 84(2) 579 PMID: 15044683

Alberelli and De Candia (2014) Functional role of protease activated receptors in vascular biology. Vascul. Pharmacol. 62(2) 72 doi: 10.1016/j.vph.2014.06.001. Epub 2014 Jun 9. PMID: 24924409.

Heuberger and Schuepbach, (2019) Protease-activated receptors (PARs): mechanisms of action and potential therapeutic modulators in PAR-driven inflammatory diseases. Thrombosis J. 17 4 PMID: 30976204