Thrombin Receptor Agonist

Cloning and expression of a functional human thrombin receptor have revealed a protein with seven transmembrane domains and a large extracellular amino-terminal extension. Thrombin cleaves within this extension, thereby creating a new receptor amino-terminus that functions as a tethered ligand and activates the receptor. A 14-amino acid peptide mimicking this new amino-terminus has been found to be a potent thrombin receptor activator as well as an effective agonist for platelet activation.