Atsufumi Kawabata and Ryotaro Kuroda
Department of Pathophysiology and Therapeutics, Faculty of Pharmaceutical
Sciences, Kinki University, Higashi-Osaka 577-8502, Japan
Abstract: The protease-activated receptor (PAR) belongs to the
large superfamily of G-protein-coupled seven trans-membrane domain receptors.
The activation of PARs is achieved by proteolytic unmasking of the cryptic
N-terminal receptor-activating sequence that binds to the body of the same
receptor molecule. PARs-1, -3 and -4 are activated by thrombin, while PAR-2
is activated by trypsin or mast cell tryptase, but not by thrombin. PARs
are widely distributed to a variety of tissues and participate in a number
of physiological or pathophysiological phenomena such as platelet aggregation,
inflammation and cardiovascular, digestive or respiratory functions. Thus,
PARs are of physiological importance and also of pharmacological interest
as the novel target for drug development.
Keywords: Protease-activated receptor (PAR), G-protein-coupled receptor,
Thrombin, Trypsin, Tryptase