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Departamento de Inmunología y Oncología, Centro Nacional de Biotecnología, Madrid, Spain
Chemokine receptor-like 1 (CKR-L1) was described recently as a
putative seven-transmembrane human receptor with many of the structural
features of chemokine receptors. To identify the ligand of CKR-L1, we
have studied chemokine-induced calcium mobilization in 293 cells
transfected with CKR-L1. Of 20 different chemokines tested, only I-309
was able to elicit a significant calcium mobilization. In addition,
I-309 induced the transfectants to migrate in vitro. As expected for
chemokine receptor-mediated effects, pertussis toxin, but not cholera
toxin, inhibited both the calcium flux and migration of the CKR-L1
transfectants in response to I-309. All of these data support the
conclusion that I-309 is a functional ligand for CKR-L1. According to
the current chemokine receptor nomenclature, we have designated this
gene as CCR8. The murine CCR8 (mCCR8) gene was cloned, and its
predicted amino acid sequence showed a 71% identity with that of human
CCR8. As human CCR8, mCCR8 is expressed in thymus. Both I-309 and its
murine homologue TCA-3 were able to induce calcium mobilization in
transiently transfected 293-EBNA cells expressing mCCR8. The affinity
of the binding of 125I-labeled TCA-3 to mCCR8 was
high (Kd 
2 nM); the binding was
prevented completely by an excess of cold TCA-3, and only partially
competed (40%) by I-309. The identification of I-309 and TCA-3 as the
functional ligands for CCR8 receptors will help to unravel the role of
these proteins in physiologic and pathologic situations.
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