Abstract
It has been 30 years since the first member of the protease -activated receptor (PAR) family was discovered. This was followed by the discovery of three other receptors, including PAR2.
PAR2 is a G protein-coupled receptor activated by trypsin site-specific proteolysis. The process starts with serine proteases acting between arginine and serine, creating an N-terminus that functions as a tethered ligand that binds, after a conformational change, to the second extracellular loop of the receptor, leading to activation of G-proteins.
The physiological and pathological functions of this ubiquitous receptor are still elusive. This review focuses on PAR2 activation and its distribution under physiological and pathological conditions, with a particular focus on the pancreas, a significant producer of trypsin, which is the prototype activator of the receptor.
The role in acute or chronic pancreatitis, pancreatic cancer, and diabetes mellitus will be highlighted.