Introduction of CCR-1

CCR-1 is a receptor for C-C type chemokine, which is encoded by CCR1 gene. This gene and other chemokine receptor genes, including CCR2, CCRL2, CCR3, CCR5, and CCXCR1, are found to form a gene cluster on chromosome 3p. CCR-1 protein is the first human CC chemokine receptor to be identified at the cDNA level. It is a member of the beta chemokine receptor family, which is predicted to be a seven transmembrane protein similar to G protein-coupled receptors. CCR-1 is mainly expressed on T cells, dendritic cells, monocytes, and neutrophils.

Function of CCR-1 Membrane Protein

CCR-1 is able to interact with multiple ligands, such as CCL3 (macrophage inflammatory protein-1α, MIP-1α), CCL5 (regulated on activation, normal T-cell expressed and secreted, RANTES), CCL7 (monocyte chemotactic protein-3, MCP-3), CCL14 (hemofiltrate C-C chemokine-1), CCL8 (monocyte chemotactic protein-2, MCP-2), CCL15 (leucotactin-1), and CCL23 (myeloid progenitor inhibitory factor-1, MPIF). When bond to these ligands, CCR-1 subsequently transduces a signal by up-regulating the intracellular calcium ions level. Since its ligand, chemokines play a crucial role in the recruitment of effector immune cells to the site of inflammation, CCR1 also up-regulates the integrins to stimulate firm adhesion of inflammatory cells to the endothelium. Moreover, CCR1 is supposed to be responsible for affecting stem cell proliferation. CCR1 and its chemokine ligands are involved in multiple human diseases, such as multiple sclerosis, rheumatoid arthritis, multiple myeloma, and associated osteolytic bone disease.

Fig.1 Structure of CCR-1 membrane protein. (Vaidehi, 2006)

Application of CCR-1 Membrane Protein in Literature

1. Li Y. CCL15/CCR1 axis is involved in hepatocellular carcinoma cells migration and invasion. Tumour Biol. 2016, 37(4): 4501-7. PubMed ID: 26501423

This article suggests that CCR1 plays critical roles in hepatocellular carcinoma metastasis, which indicates that CCR1 may be a potential molecular target in hepatocellular carcinoma therapy.

2. Inamoto S., et al. Loss of SMAD4 Promotes Colorectal Cancer Progression by Accumulation of Myeloid-Derived Suppressor Cells through the CCL15-CCR1 Chemokine Axis. Clin Cancer Res. 2016, 22(2): 492-501. PubMed ID: 26341919

This article reveals that blocking the recruitment of CCR1(+) MDSCs may represent a novel molecular-targeted therapy, and serum CCL15 concentration can be a novel biomarker for colorectal cancer.

3. Akram I.G., et al. The chemokines CCR1 and CCRL2 have a role in colorectal cancer liver metastasis. Tumour Biol. 2016, 37(2): 2461-71. PubMed ID: 26383527

This data reveals an important role of CCR1 and CCRL2 under conditions of organ colonization and both chemokine receptors qualify as targets of treatment during early colorectal cancer liver metastasis.

4. Lewis N.D., et al. CCR1 plays a critical role in modulating pain through hematopoietic and non-hematopoietic cells. PLoS One. 2014, 9(8): e105883. PubMed ID: 25170619

This article indicates that CCR1 functions to significantly modulate pain by controlling neutrophil trafficking to the inflammatory site and having an unexpected role on non-hematopoietic cells. As inflammatory diseases are often accompanied with infiltrating immune cells at the inflammatory site and pain, CCR1 antagonism may provide a dual benefit by restricting leukocyte trafficking and reducing pain.

5. Hirai H., et al. CCR1-mediated accumulation of myeloid cells in the liver microenvironment promoting mouse colon cancer metastasis. Clin Exp Metastasis. 2014, 31(8): 977-89. PubMed ID: 25326065

The outcome of this study implicates the key role of CCR1 in colon cancer metastasis in this mouse model and explains why both MMP9 and MMP2 are essential as genetically demonstrated previously. The recruitment of CCR1(+) neutrophils in early phase of colon cancer dissemination appears to cause that of fibrocytes in late phase.

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Reference

1. Vaidehi N, et al. (2006). Predictions of CCR1 chemokine receptor structure and BX 471 antagonist binding followed by experimental validation. Journal of Biological Chemistry, 281(37), 27613-27620.

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