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Endothelium‐dependent and ‐independent responses to protease‐activated receptor‐2 (PAR‐2) activation in mouse isolated renal arteries
Author(s) -
Moffatt J D,
Cocks T M
Publication year - 1998
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1038/sj.bjp.0702157
Subject(s) - endothelium , receptor , thrombin , thrombin receptor , protease activated receptor , trypsin , vascular smooth muscle , chemistry , nitric oxide , protease , nitric oxide synthase , contraction (grammar) , medicine , endocrinology , enzyme , biochemistry , microbiology and biotechnology , biology , smooth muscle , platelet
Protease‐activated receptors (PARs) are receptors which require proteolytic cleavage to be self‐activated by newly exposed N‐terminal ‘tethered ligands’, and hence serve as sensors for protelytic enzymes. While both the thrombin receptor (PAR‐1) and PAR‐2 (activated by tryptic enzymes) have been shown to mediate endothelium‐dependent vasorelaxation, only PAR‐1 has been shown to cause direct vascular smooth muscle contraction. In this study, we report that trypsin and the PAR‐2 selective peptide ligand SLIGRL‐NH 2 not only caused endothelium‐dependent relaxation of mouse renal arteries but also direct smooth muscle contraction if endothelial nitric oxide synthase was inhibited or if the endothelium was removed. British Journal of Pharmacology (1998) 125 , 591–594; doi: 10.1038/sj.bjp.0702157