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  • Title: Cloning and characterization of a novel murine macrophage inflammatory protein-1 alpha receptor.
    Author: Meyer A, Coyle AJ, Proudfoot AE, Wells TN, Power CA.
    Journal: J Biol Chem; 1996 Jun 14; 271(24):14445-51. PubMed ID: 8662890.
    Abstract:
    We have cloned a novel CC chemokine receptor cDNA from mouse thymus. The deduced amino acid sequence shows 74% identity to the human monocyte chemotactic protein (MCP)-1 receptor (CC CKR-2b) and 54% to a recently cloned murine macrophage inflammatory protein (MIP)-1alpha receptor (Gao, J. L., and Murphy, P. M.(1995) J. Biol. Chem. 270, 17494-17501). Northern blot analysis of mouse tissues showed that the mRNA was also expressed in heart, spleen and liver, and to a lesser extent in lung and brain. The rank order of CC chemokine competition for 125I-labeled human RANTES (regulated on activation, normal T-cell expressed and secreted) binding to human embryonic kidney (HEK) 293 cells stably transfected with the receptor cDNA was murine MIP-1alpha >> human MIP-1beta > human RANTES > murine RANTES > murine MIP-1beta > human MCP-2 > murine MCP-1 (JE) > human MIP-1alpha > human MCP-3 > human MCP-1. Of the chemokines tested, only murine MIP-1alpha, human and murine MIP-1beta and RANTES, human MCP-2, and JE were able to induce mobilization of intracellular Ca2+ from fura-2-loaded HEK 293 cells expressing the receptor. These results suggest that this receptor functions as a high affinity murine MIP-1alpha receptor; however, it is likely to be an important target for the biological activities of several CC chemokines in mouse.
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