Monocyte chemoattractant protein 1 (CCL2/JE/MCP-1), also called CCL2, belongs to a group of CC chemokines located in chromosome 17q11.2. CCL2/JE/MCP-1 protein interacts with chemokine C-C motif receptor 2 (CCR2) to activate and recruit monocytes, macrophages, CD4+ T cells and immature dendritic cells to the site of infection. The presence of CCL2/JE/MCP-1 protein in an adequate concentration is important for granuloma formation and M. tuberculosis clearance.
The chemokine (C-C motif) ligand 2 (CCL2), also known as monocyte chemoattractant protein (MCP)-1 and small inducible cytokine A2 (SCYA2)), is a small cytokine that belongs to the CC chemokine family responsible for monocyte attraction. Its cognate receptor, CCR2, play a critical role in regulating nociceptive processes during neuropathic pain. Both CCL2 and CCR2 are implicated in induction of autoimmunity. CCL2 recruits monocytes, memory T cells, and dendritic cells to the sites of inflammation produced by either tissue injury or infection. Recently research also showed that CCL2 might be useful as a biomarker of fibrosis as well as a target for therapeutic intervention.
CCL4 (C-C chemokine ligand 4), is a macrophage inflammatory protein with a chief effect in inflammation and immune-regulation, and was documented in cancer progression by promoting instability in the tumor environment. The inflammatory chemokine (C-C motif) ligand 4 (CCL4) plays an important role in the pathogenesis and progression of cancer. In particular, higher serum CCL4 levels in patients with oral squamous cell carcinoma (OSCC) are associated with a more advanced stage of disease. CCL4 may be a new molecular therapeutic target for inhibition of lymphangiogenesis and metastasis in OSCC. CCL3 and CCL4 loci may be marker SNPs for risk of HCV treatment outcome. CCL4 can enhance the recruitment of preosteoclasts to bone in the early stage, and the reduction of CCR5 promotes osteoclastogenesis when RANKL is prevalent.
C-C motif chemokine 5(CCL5) is a β-chemokine that plays a primary role in the inflammatory immune response by means of its ability to attract and activate leukocytes. CCL5 is secreted by many cell types at inflammatory sites, and it exerts a wide range of activities through the receptors CCR1, CCR3, CCR4, and CCR5. Inflammatory responses can be impaired by the sequestration of CCL5 by the cytomegalovirus protein US28. Oligomerization of CCL5 on glycosaminoglycans is required for CCR1mediated leukocyte adhesion and activation as well as CCL5’s interaction with the chemokine CXCL4/PF4.The deposition of CCL5 on activated vascular endothelial cells is crucial for monocyte adhesion to damaged vasculature, but CCL5 oligomerization is not required for the extravasation of adherent leukocytes.CCL5 is upregulated in breast cancer and promotes tumor progression through the attraction of proinflammatory macrophages in addition to its actions on tumor cells, stromal cells, and the vasculature.
CD109 is a GPI-anchored member of the alpha-2-macroglobulin (A2M) and complement family of proteins.Cleavage of A2M family proteins within the bait region activates the thioester bond to promote covalent bonding to nucleophilic groups in adjacent molecules.It shares 27-33% aa sequence identity with A2M and complement factors C3, C4, and C5. Alternate splicing of human CD109 generates two isoforms with short deletions and one that is truncated within the bait region. CD109 is expressed on activated T cells and platelets, hematopoietic stem cells, megakaryocyte precursors, vascular endothelial cells, basal and myoepithelial cells of secretory glands, and squamous cell carcinomas.
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