Molecular cloning of murine CC CKR-4 and high affinity binding of chemokines to murine and human CC CKR-4

AJ Hoogewerf, D Black, AEI Proudfoot… - Biochemical and …, 1996 - Elsevier
AJ Hoogewerf, D Black, AEI Proudfoot, TNC Wells, CA Power
Biochemical and biophysical research communications, 1996Elsevier
We have cloned the murine homologue of human CC Chemokine Receptor-4 (CC CKR-4).
In equilibrium competition binding assays performed in undifferentiated HL-60 cells
transfected with human and murine CC CKR-4 cDNA, the IC50values for the binding of
[125I] macrophage inflammatory protein-1α to human and murine CC CKR-4 were 14.5±9.0
nM and 10.1±3.0 nM, respectively, and the IC50values for the binding of [125I] RANTES to
human and murine CC CKR-4 were 9.3±3.0 nM and 5.7±2.6 nM, respectively. The cDNA …
We have cloned the murine homologue of human CC Chemokine Receptor-4 (CC CKR-4). In equilibrium competition binding assays performed in undifferentiated HL-60 cells transfected with human and murine CC CKR-4 cDNA, the IC50values for the binding of [125I]macrophage inflammatory protein-1α to human and murine CC CKR-4 were 14.5 ± 9.0 nM and 10.1 ± 3.0 nM, respectively, and the IC50values for the binding of [125I]RANTES to human and murine CC CKR-4 were 9.3 ± 3.0 nM and 5.7 ± 2.6 nM, respectively. The cDNA clone for murine CC CKR-4 is 1531 bp, and the largest open reading frame encodes a protein of 360 amino acids that is 85% identical to human CC CKR-4. Murine CC CKR-4 was detected in the thymus and T-cell lines by Northern blot analysis. This first report of direct binding of chemokines to CC CKR-4 demonstrates that the highly homologous human and murine receptors have similar binding characteristics and tissue distribution.
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