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[monocyte chemoattractant protein-3] called also monocyte chemotactic protein-3 or SCYA7. MCP-3 is encoded by the NC28 cDNA. MCP-3 is a member of the family of CC-Chemokines. The factor has been renamed CCL7. See also: SCY family of cytokines for a systematic nomenclature.

The MCP-3 protein (97 amino acids) sequence shows 74 % identity with MCP-1 and 58 % homology with MCP-2. Secreted MCP-3 differs from MCP-1 in being N-glycosylated. The MCP-3 (SCYA7) gene maps to human chromosome 17 q11.2-q12 close to the erbB2 locus. Human MCP-3 and the mouse MARC gene are porobably homologous.

Both factors specifically attract monocytes, but not neutrophils, in vitro. Intradermal injection of these two proteins into rabbits causes the selective recruitment of monocytes at the site of injection. Levels of MCP-3 mRNAs in peripheral blood mononuclear cells are increased by IFN-gamma and decreased by IL13.

MCP-3 is produced by a variety of tumor cell lines and regulates protease secretion by macrophages; its production may contribute, therefore, to invasion and metastasis of cancer cells.

Like some chemokines, and unlike other chemokines, that do, MCP-3 does not possess suppressive activity against immature subsets of myeloid progenitors (see also: hematopoiesis) stimulated to proliferate by multiple growth factors (Broxmeyer et al, 1999).

MCP-3 binds to a receptor designated D6. MCP-3 also binds to CCR10, and CCR1 (Ben-Baruch et al, 1995).

McQuibban et al (2000) have pointed out the catalytic importance of substrate-binding exosites outside the catalytic domain of the metalloproteinase MMP-2. They have identified the chemokine MCP-3 as a physiological substrate of MMP-2 that binds to the hemopexin domain. Cleaved MCP-3 binds to CC-Chemokine receptors CCR1, CCR2, and CCR3, but no longer induces calcium fluxes or promotes chemotaxis, and instead acts as a general chemokine antagonist that dampens inflammation.

Copyright 2012 by H IBELGAUFTS. All rights reserved.


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