The chemokine receptor CCR8 is not a high-affinity receptor for the human chemokine CCL18.

Autor: Hussain K; National Heart and Lung Institute, Imperial College London, London, United Kingdom., Lim HD; Monash Biomedicine Discovery Institute, and Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC, Australia., Devkota SR; Monash Biomedicine Discovery Institute, and Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC, Australia., Kemp-Harper BK; Monash Biomedicine Discovery Institute, and Department of Pharmacology, Monash University, Clayton, VIC, Australia., Lane JR; Division of Physiology, Pharmacology and Neuroscience, School of Life Sciences, Queen's Medical Centre, University of Nottingham, Nottingham, United Kingdom.; Centre of Membrane Protein and Receptors, Universities of Birmingham and Nottingham, Nottingham, United Kingdom., Canals M; Division of Physiology, Pharmacology and Neuroscience, School of Life Sciences, Queen's Medical Centre, University of Nottingham, Nottingham, United Kingdom.; Centre of Membrane Protein and Receptors, Universities of Birmingham and Nottingham, Nottingham, United Kingdom., Pease JE; National Heart and Lung Institute, Imperial College London, London, United Kingdom., Stone MJ; Monash Biomedicine Discovery Institute, and Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC, Australia.
Jazyk: angličtina
Zdroj: PloS one [PLoS One] 2024 Sep 11; Vol. 19 (9), pp. e0305312. Date of Electronic Publication: 2024 Sep 11 (Print Publication: 2024).
DOI: 10.1371/journal.pone.0305312
Abstrakt: The primate-specific chemokine CCL18 is a potent chemoattractant for T cells and is expressed at elevated levels in several inflammatory diseases. However, the cognate receptor for CCL18 remains unconfirmed. Here, we describe attempts to validate a previous report that the chemokine receptor CCR8 is the human CCL18 receptor (Islam et al. J Exp Med. 2013, 210:1889-98). Two mouse pre-B cell lines (4DE4 and L1.2) exogenously expressing CCR8 exhibited robust migration in response to the known CCR8 ligand CCL1 but not to CCL18. Similarly, CCL1 but not CCL18 induced internalization of CCR8 on 4DE4 cells. CCR8 expressed on Chinese hamster ovarian (CHO) cells mediated robust G protein activation, inhibition of cAMP synthesis and β-arrestin2 recruitment in response to CCL1 but not CCL18. Several N- and C-terminal variants of CCL18 also failed to stimulate CCR8 activation. On the other hand, and as previously reported, CCL18 inhibited CCL11-stimulated migration of 4DE4 cells expressing the receptor CCR3. These data suggest that CCR8, at least in the absence of unidentified cofactors, does not function as a high affinity receptor for CCL18.
Competing Interests: The authors have declared that no competing interests exist.
(Copyright: © 2024 Hussain et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.)
Databáze: MEDLINE
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