PMID: 9636225Jun 24, 1998Paper

Proteinase-activated receptor 2 (PAR2)-activating peptides: identification of a receptor distinct from PAR2 that regulates intestinal transport

Proceedings of the National Academy of Sciences of the United States of America
Nathalie VergnolleMorley D Hollenberg

Abstract

The effects of PAR2-activating PAR2-activating peptides, SLIGRL (SL)-NH2, and trans-cinnamoyl-LIGRLO (tc)-NH2 were compared with the action of trypsin, thrombin, and the PAR1 selective-activating peptide: Ala-parafluoroPhe-Arg-cyclohexylAla-Citrulline-Tyr (Cit)-NH2 for stimulating intestinal ion transport. These agonists were added to the serosa of stripped rat jejunum segments mounted in Ussing chambers, and short circuit current (Isc) was used to monitor active ion transport. The relative potencies of these agonists also were evaluated in two bioassays specific for the activation of rat PAR2: a cloned rat PAR2 cell calcium-signaling assay (PAR2-KNRK cells) and an aorta ring relaxation (AR) assay. In the Isc assay, all agonists, except thrombin, induced an Isc increase. The SL-NH2-induced Isc changes were blocked by indomethacin but not by tetrodotoxin. The relative potencies of the agonists in the Isc assay (trypsin>SL-NH2>tc-NH2>Cit-NH2) were strikingly different from their relative potencies in the cloned PAR2-KNRK cell calcium assay (trypsin>tc-NH2 congruent with SL-NH2>Cit-NH2) and in the AR assay (trypsin>tc-NH2 congruent with SL-NH2). Furthermore, all agonists were maximally active in the PAR2-KNRK cell and AR assays at...Continue Reading

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Citations

Mar 27, 2010·Inflammation Research : Official Journal of the European Histamine Research Society ... [et Al.]·Eric HyunNathalie Vergnolle
Nov 11, 2003·Life Sciences·Atsufumi Kawabata
Feb 1, 2003·Clinica Chimica Acta; International Journal of Clinical Chemistry·Seung-Woo HanYoung-Mi Lee
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