id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-102808-c7ajfvt5	Sundqvist, Martina	Barbadin selectively modulates FPR2-mediated neutrophil functions independent of receptor endocytosis	2020-05-01		.txt	text/plain	5708	236	34	The formyl peptide receptor 2 (FPR2), belonging to the family of G protein-coupled receptors (GPCRs), regulates directional neutrophil migration (chemotaxis), granule secretion (degranulation), formation of F-actin filaments (through polymerization of G-actin), and activation of the reactive oxygen species (ROS) producing NADPH-oxidase [3, 5, 6] . The fact that F2Pal10 and Cmp 14 cannot induce -arrestin recruitment at these concentrations ([9-11], Fig 2A) , strongly suggests that the priming effect of Barbadin on FPR2-mediated ROS production is independent of the ability of the activating agonist to recruit -arrestin. Collectively, these results suggest that Barbadin primes neutrophils in their response to FPR2 agonists, and the increased NADPH-oxidase activation is regulated independently of FPR2 internalization and FPR2-induced -arrestin recruitment. Barbadin was added to WKYMVM-activated neutrophils at a time point when ROS production had returned to a background level; interestingly, these FPR2-desensitized cells could be resensitized to produce ROS also by Barbadin, similar to the effect of latrunculin A ( Fig 5A) .	./cache/cord-102808-c7ajfvt5.txt	./txt/cord-102808-c7ajfvt5.txt