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Gut 2007;56:901-902; doi:10.1136/gut.2006.111245
Copyright © 2007 BMJ Publishing Group Ltd & British Society of Gastroenterology.

COMMENTARY

Acinar cell PAR2

Pancreatic protease-activated receptors: friend and foe

Fred Gorelick

Correspondence to:
Correspondence to:
Professor F Gorelick
VA HealthCare CT and Yale University, 950 Campbell Avenue, West Haven, CT 06516, USA; fred.gorelick@yale.edu


PAR2 activation may protect the acinar cell by enhancing secretion, but may still leave you in pain

The first 150 words of the full text of this article appear below.

Two regulatory elements of the exocrine pancreas, one new and one old, may interact to regulate previously undescribed physiological and pathological responses of the pancreas. The new targets are protease-activated receptors (PARs); the old elements are the serine proteases trypsin and tryptase, which are the most potent agonists of these G-protein-coupled receptors.1 The PAR family of G-protein-coupled receptors exhibits a distinct activation mechanism. Limited cleavage of the extracellular domain of PARs by serine proteases uncovers a peptide on the N-terminus that interacts with another extracellular region to activate the receptor. PAR isoforms exhibit a distinct tissue distribution and are selectively activated by specific classes of proteases. For example, the PAR2 isoform that is found in the pancreas on epithelial cells and nerves is selectively activated by trypsin and tryptase. While the role of the PAR2 in health and disease is currently being elucidated, recent studies have suggested . . . [Full text of this article]


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