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      Cloning, expression, and chromosomal mapping of a novel human CC-chemokine receptor (CCR10) that displays high-affinity binding for MCP-1 and MCP-3.

      DNA and cell biology
      Amino Acid Sequence, Animals, Base Sequence, Binding, Competitive, COS Cells, Chemokine CCL2, metabolism, Chemokine CCL5, Chemokine CCL7, Chromosome Mapping, Chromosomes, Human, Pair 3, genetics, Cloning, Molecular, Cytokines, Female, Gene Expression Regulation, Developmental, physiology, Humans, Kinetics, Male, Molecular Sequence Data, Monocyte Chemoattractant Proteins, Organ Specificity, RNA, Messenger, analysis, Receptors, CCR10, Receptors, Chemokine, Sequence Homology, Amino Acid

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          Abstract

          Chemokines mediate their chemotactic, proinflammatory effects by binding to and activating a variety of specific receptors belonging to the G protein-coupled superfamily of seven-transmembrane serpentine receptors. We report the cloning, chromosomal localization, expression, and ligand binding of a novel CC chemokine receptor, CCR10. CCR10 is expressed primarily in placenta and fetal liver, and binds two of the CC chemokines, monocyte chemoattractant protein (MCP)-1 and MCP-3, with highest affinity. The KD for MCP-3 binding was 1 nM, and MCP-1 competed for MCP-3 binding with an IC50 of 1.2 nM. The CC chemokines MCP-4 and RANTES competed for MCP-3 binding with IC50 values of 7.5 and 5.4 nM, respectively. The chromosomal location of CCR10 was determined to coincide with the CC chemokine receptor cluster on chromosome 3 (3p21.31-3p21.32). These results indicate that CCR10 is a novel CC chemokine receptor with a unique expression pattern that would be consistent with a role in placental immunity or hematopoiesis.

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