JLE

Hématologie

MENU

Protease-activated receptor 1: first member of a receptor family Volume 6, issue 6, Novembre - Décembre 2000

Figures

See all figures

Authors
Inserm U. 428, faculté de pharmacie, Paris

Serine proteases belong to a large family of proteins implicated in essential biological functions, such as haemostasis and the immune system. Less than ten years ago, a major discovery concerning the receptor for one of the serine protease, thrombin, has allowed to describe a new family of receptors, the so- called protease activated receptors PAR. The PAR receptors are G-protein coupled seven transmembrane domain receptors activated by proteases, but are not classically activated by the simple binding of the protease: the bound protease cleaves the receptor N-terminus, unmasking a new N-terminus which becomes a tethered ligand and is itself the activator. This family of PARs contains four members: PAR-1, PAR-3 and PAR-4 are cleaved by thrombin, whereas PAR-2 is cleaved by trypsin and trypsin-like enzymes. The present review summarizes the current knowledge on molecular structure and functions of this family of receptors and their physiopathological implications. The development of new molecules blocking these receptors could allow great progress in cardiovascular and cancer domains.