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

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 IC50 values for the binding of [125I]macrophage inflammatory protein-1 alpha to human and murine CC CKR-4 were 14.5 ...
+/- 9.0 nM and 10.1 +/- 3.0 nM, respectively, and the IC50 values 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.
Mesh Terms:
Amino Acid Sequence, Animals, Base Sequence, Chemokine CCL4, Chemokine CCL5, Cloning, Molecular, Gene Expression, Gene Library, HL-60 Cells, Humans, Kinetics, Lymphocytes, Macrophage Inflammatory Proteins, Mice, Molecular Sequence Data, Monokines, Organ Specificity, RNA, Messenger, Receptors, Cytokine, Recombinant Proteins, Sequence Homology, Amino Acid, Spleen, Substrate Specificity, Thymus Gland, Transfection
Biochem. Biophys. Res. Commun.
Date: Jan. 05, 1996
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