PAR-2 elicits afferent arteriolar vasodilation by NO-dependent and NO-independent actions

American Journal of Physiology. Renal Physiology
G TrottierR Loutzenhiser

Abstract

Proteinase-activated receptors (PARs) are a novel class of G protein-coupled receptors that respond to signals through endogenous proteinases. PAR activation involves enzymatic cleavage of the extracellular NH(2)-terminal domain and unmasking of a new NH(2) terminus, which serves as an anchored ligand to activate the receptor. At least four PAR subtypes have been identified. In the present study, we used the in vitro perfused hydronephrotic rat kidney to examine the effects of activating PAR-2 on the afferent arteriole. The synthetic peptide SLIGRL-NH(2), which corresponds to the exposed ligand sequence and selectively activates PAR-2, did not alter basal afferent arteriolar diameter but caused a concentration-dependent vasodilation (3-30 microM) of arterioles preconstricted by angiotensin II (0.1 nM). A modified peptide sequence (LSIGRL-NH(2), inactive at PAR-2) had no effect. This vasodilation was characterized by an initial transient component followed by a smaller sustained response. A similar pattern of vasodilation was seen when SLIGRL-NH(2) was administered to isolated perfused normal rat kidney. The sustained component of the PAR-2-induced afferent arteriolar vasodilation was eliminated by nitric oxide (NO) synthase inh...Continue Reading

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Citations

Oct 26, 2010·Basic Research in Cardiology·Yoonjung ParkCuihua Zhang
Jul 21, 2007·The American Journal of Pathology·Leon MoussaPeter G Tipping
Dec 7, 2007·British Journal of Pharmacology·R Ramachandran, M D Hollenberg
Sep 27, 2005·Vascular Pharmacology·Mariarosaria BucciGiuseppe Cirino
Mar 30, 2004·Journal of Smooth Muscle Research = Nihon Heikatsukin Gakkai Kikanshi·Chris R TriggleMalarvannan Pannirselvam
Jan 13, 2005·Canadian Journal of Physiology and Pharmacology·John J McGuireChris R Triggle
Aug 5, 2017·Frontiers in Pharmacology·Ambra VillariSalvatore Salomone

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