| First Author | Del Prete A | Year | 2017 |
| Journal | Blood | Volume | 130 |
| Issue | 10 | Pages | 1223-1234 |
| PubMed ID | 28743719 | Mgi Jnum | J:247010 |
| Mgi Id | MGI:5922550 | Doi | 10.1182/blood-2017-04-777680 |
| Citation | Del Prete A, et al. (2017) The atypical receptor CCRL2 is required for CXCR2-dependent neutrophil recruitment and tissue damage. Blood 130(10):1223-1234 |
| abstractText | CCRL2 is a 7-transmembrane domain receptor that shares structural and functional similarities with the family of atypical chemokine receptors (ACKRs). CCRL2 is upregulated by inflammatory signals and, unlike other ACKRs, it is not a chemoattractant-scavenging receptor, does not activate beta-arrestins, and is widely expressed by many leukocyte subsets. Therefore, the biological role of CCRL2 in immunity is still unclear. We report that CCRL2-deficient mice have a defect in neutrophil recruitment and are protected in 2 models of inflammatory arthritis. In vitro, CCRL2 was found to constitutively form homodimers and heterodimers with CXCR2, a main neutrophil chemotactic receptor. By heterodimerization, CCRL2 could regulate membrane expression and promote CXCR2 functions, including the activation of beta2-integrins. Therefore, upregulation of CCRL2 observed under inflammatory conditions is functional to finely tune CXCR2-mediated neutrophil recruitment at sites of inflammation. |
