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From the * Infectious Disease Unit, The chemokines are a large family of cytokines that control the recruitment of leukocytes in
immune and inflammatory responses. We describe the isolation of a novel murine CC
chemokine that, based on its biological and structural features, we have named monocyte
chemoattractant protein (MCP)-5. MCP-5 mapped to the CC chemokine cluster on mouse
chromosome 11 and was most closely related to human MCP-1 in structure (66% amino acid
identity). Purified recombinant MCP-5 protein was a potent chemoattractant for peripheral
blood monocytes, was only weakly active on eosinophils at high doses, and was inactive on
neutrophils. MCP-5 induced a calcium flux in peripheral blood mononuclear cells, but not in
purified murine eosinophils or neutrophils. Consistent with these results, MCP-5 induced a
calcium flux in human embryonic kidney (HEK)-293 cells transfected with human and murine
CCR2, a CC chemokine receptor expressed on monocytes. MCP-5 did not induce a calcium
flux in HEK-293 cells transfected with CCR1, CCR3, or CCR5. Constitutive expression of
MCP-5 mRNA was detected predominantly in lymph nodes, and its expression was markedly induced in macrophages activated in vitro and in vivo. Moreover, MCP-5 expression was upregulated in the lungs of mice following aerosolized antigen challenge of sensitized mice, and
during the host response to infection with Nippostrongylus brasiliensis. These data indicate that
MCP-5 is a novel and potent monocyte active chemokine that is involved in allergic inflammation and the host response to pathogens.
Allergy and Immunology Unit, Massachusetts General Hospital,
and Harvard Medical School, Boston, Massachusetts 02114; and the § Gladstone Institute of
Cardiovascular Disease; and Department of Medicine, University of California, San Francisco,
California 94141
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