AI Article Synopsis
- The chemokine CCL18 attracts T cells and is elevated in inflammatory diseases, but its receptor is not yet confirmed.
- Experiments showed that CCR8-expressing mouse cells responded to the ligand CCL1, but not to CCL18, which suggests CCR8 isn’t the receptor for CCL18.
- Additionally, CCL18 was found to inhibit migration through another receptor, CCR3, reinforcing the idea that CCR8 does not effectively bind CCL18 without additional factors.
Article Abstract
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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11389940 | PMC |
| http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0305312 | PLOS |
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