Disease relevance of CCL23

• Treatment with either pertussis toxin or anti-CCR1 antibody completely inhibited the CCL23-induced endothelial cell migration, indicating that endothelial cell migration was mediated through CCR1 [1].
• CCL23 didn't promote the migration of HT1080 human fibrosarcoma cells that did not express CCR1 [1].
• PURPOSE: The purpose of this study was to determine whether curcumin would trigger cell death in the head and neck squamous cell carcinoma (HNSCC) cell lines CCL 23, CAL 27, and UM-SCC1 in a dose-dependent fashion [2].
• These results suggest that MPIF plays a central role in the expression of histopathological features of delayed-type hypersensitivity reactions [3].

High impact information on CCL23

• Two novel human beta-chemokines, Ck beta-8 or myeloid progenitor inhibitory factor 1 (MPIF-1), and Ck beta-6 or MPIF-2, were discovered as part of a large scale cDNA sequencing effort [4].
• MPIF-1 is also a potent suppressor of bone marrow low proliferative potential colony-forming cells, a committed progenitor that gives rise to granulocyte and monocyte lineages [4].
• CCL23 , which was not coregulated in vitro with CCL20 , was also specifically expressed in the FAE [5].
• MPIF-1, a CC chemokine, is a specific inhibitor of myeloid progenitor cells and is the most potent activator of monocytes [6].
• MPIF-1 binds specifically to sites, in particular CCR1, shared with macrophage inflammatory protein-1alpha (MIP-1alpha) on the surface of human monocytes and dendritic cells, as inferred by its ability to compete for [125I]MIP-1alpha, but not for [125I]MIP-1beta or [125I]monocyte chemotactic protein-1(MCP-1) binding to intact cells [7].

Chemical compound and disease context of CCL23

• The inhibitory effect of guanosine 5'-O-(3-thio-triphosphate) (GTP-gammaS) or pertussis toxin pretreatment on MPIF-1 binding and calcium mobilization, respectively, indicates the involvement of G proteins in the interaction of MPIF-1 and its receptor(s) [7].

Biological context of CCL23

• Our results indicate that CCL23 may play a direct role in angiogenesis, via the upregulation of MMP-2 expression [8].
• CCL23 was shown to dose-dependently activate the expression of the MMP-2/Luc reporter gene, thereby indicating that it stimulates the transcription of the MMP-2 gene [8].
• When the nucleotide sequences of the MPIF-1 and HCC-2 genes are compared, they are well conserved, including introns and flanking sequences, except for the middle region of the long first intron, indicating that they have been generated recently in evolutionary terms by duplication [9].
• Vigilin, which is found predominantly in cells and tissues with high levels of protein biosynthesis, was isolated in its native form from human HEp-2 cells (A.T.C.C. CCL23) by immunoaffinity chromatography [10].
• The receptor specificity and signal transduction pathway has been identified and characterized for a truncated form of myeloid progenitor inhibitory factor-1 (MPIF-1(24-99)) [7].

Anatomical context of CCL23

• CKbeta-8 [CCL23], a novel CC chemokine, is chemotactic for human osteoclast precursors and is expressed in bone tissues [11].
• Vascular endothelial cells, when exposed to CCL23, showed a marked ability to invade through a 3D Matrigel [8].
• CCL23 promoted the chemotactic migration and differentiation of endothelial cells, and neovascularization in the chick chorioallantoic membrane [1].
• CCL23 treatment also prolonged the transit time of monocyte (43.4 +/- 3.1 hours vs 54.2 +/- 1.3 hours, control vs CCL23, p < 0.05) through the bone marrow and decreased turnover and pool size of monocytes in the bone marrow (p < 0.05) [12].
• CONCLUSION: We conclude that CCL23 suppresses PMN and monocyte progenitors, decreases the pool size and slows their turnover in the bone marrow [12].

Associations of CCL23 with chemical compounds

• Furthermore, we showed that the CCL23-induced invasion was inhibited by MMP inhibitors such as GM6001 and a specific MMP-2 Inhibitor I [8].
• In [35S]-GTPgammaS exchange assays, membranes from cells cultured with retinoic acid (4-6 days) were the most responsive to activation by MIP-1alpha and MPIF-1 [13].
• The proinflammatory stimuli lipopolysaccharide and tumor necrosis factor alpha, which induced the release of monocyte chemotactic protein-1, macrophage inflammatory protein-1alpha (MIP-1alpha), MIP-1beta, and interleukin-8, did not affect MPIF-1 release [14].
• Monocyte and macrophage procoagulants induced by MPIF would contribute significantly to the activation of coagulation which not only results in fibrin deposition but also in the production of activated serine proteases and fibrinopeptides which may potentiate an inflammatory response [3].
• Murine MPIF is chemically distinct from a number of other well characterized lymphokines in that the two major activities, MPIF alpha and MPIF beta are heparin-binding proteins with high isoelectric points [3].

Other interactions of CCL23

• The MPIF-1 and MPIF-2 cDNAs were isolated from aortic endothelium and activated monocyte libraries, respectively [4].
• Characterization of the signal transduction pathway activated in human monocytes and dendritic cells by MPIF-1, a specific ligand for CC chemokine receptor 1 [7].
• MPIF-1 induces a rapid dose-dependent release of [3H]arachidonic acid from monocytes that is dependent on extracellular calcium and is blocked by phospholipase A2 (PLA2) inhibitors [7].
• Vigilin, a protein found predominantly in cells and tissues with a high biosynthetic capacity, was isolated in its native form from human HEp-2 cells (A.T.C.C. CCL23) by immunoaffinity chromatography [15].
• In contrast, CD40 ligation and interferon-gamma treatment, while stimulating the production of the other chemokines, caused a pronounced reduction of MPIF-1 transcript and protein release [14].

References