• integral component of membrane • membrane • mast cell granule • plasma membrane • integral component of plasma membrane • intracellular anatomical structure • cell surface • secretory granule membrane • external side of plasma membrane
Biological process
• neutrophil activation • receptor internalization • dendritic cell chemotaxis • chemotaxis • cellular defense response • phospholipase C-activating G protein-coupled receptor signaling pathway • cell surface receptor signaling pathway • positive regulation of cell population proliferation • inflammatory response • chemokine-mediated signaling pathway • neutrophil degranulation • G protein-coupled receptor signaling pathway • acute inflammatory response to antigenic stimulus • positive regulation of leukocyte chemotaxis • positive regulation of cytosolic calcium ion concentration • positive regulation of cardiac muscle cell apoptotic process • neutrophil chemotaxis • midbrain development • negative regulation of neutrophil apoptotic process • negative regulation of apoptotic process • positive regulation of vascular permeability • positive regulation of angiogenesis • metanephric tubule morphogenesis • positive regulation of neutrophil chemotaxis • signal transduction • interleukin-8-mediated signaling pathway • immune response • calcium-mediated signaling • cell chemotaxis
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
3579
12765
Ensembl
ENSG00000180871
ENSMUSG00000026180
UniProt
P25025
P35343
RefSeq (mRNA)
NM_001168298 NM_001557
NM_009909
RefSeq (protein)
NP_001161770 NP_001548
NP_034039
Location (UCSC)
Chr 2: 218.13 – 218.14 Mb
Chr 1: 74.15 – 74.16 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
Interleukin 8 receptor, beta is a chemokine receptor. IL8RB is also known as CXCR2, and CXCR2 is now the IUPHAR Committee on Receptor Nomenclature and Drug classification-recommended name.[5]
Contents
1Function
2Senescence
3See also
4References
5Further reading
6External links
Function
The protein encoded by this gene is a member of the G-protein-coupled receptor family. This protein is a receptor for interleukin 8 (IL8). It binds to IL8 with high affinity, and transduces the signal through a G-protein-activated second messenger system (Gi/o-coupled[6]). This receptor also binds to chemokine (C-X-C motif) ligand 1 (CXCL1/MGSA), a protein with melanoma growth stimulating activity, and has been shown to be a major component required for serum-dependent melanoma cell growth. In addition, it binds ligands CXCL2, CXCL3, and CXCL5.
The angiogenic effects of IL8 in intestinal microvascular endothelial cells are found to be mediated by this receptor. Knockout studies in mice suggested that this receptor controls the positioning of oligodendrocyte precursors in developing spinal cord by arresting their migration. This gene, IL8RA, a gene encoding another high affinity IL8 receptor, and IL8RBP, a pseudogene of IL8RB, form a gene cluster in a region mapped to chromosome 2q33-q36.[7]
Mutations in CXCR2 cause hematological traits.[8]
Senescence
Knock-down studies involving the chemokine receptor CXCR2 alleviates both replicative and oncogene-induced senescence (OIS) and diminishes the DNA-damage response. Also, ectopic expression of CXCR2 results in premature senescence via a p53-dependent mechanism.[9]
See also
Interleukin 8 receptor, alpha
Interleukin 8
Interleukin
Interleukin receptor
Cluster of differentiation
G protein-coupled receptor
References
^ abcGRCh38: Ensembl release 89: ENSG00000180871 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000026180 - Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Morris SW, Nelson N, Valentine MB, Shapiro DN, Look AT, Kozlosky CJ, Beckmann MP, Cerretti DP (Nov 1992). "Assignment of the genes encoding human interleukin-8 receptor types 1 and 2 and an interleukin-8 receptor pseudogene to chromosome 2q35". Genomics. 14 (3): 685–91. doi:10.1016/S0888-7543(05)80169-7. PMID 1427896.
^"Entry in: gpDB, database of GPCRs, G-proteins, Effectors and their interactions". Retrieved 3 October 2012.
^Auer PL, Teumer A, Schick U, O'Shaughnessy A, Lo KS, Chami N, Carlson C, de Denus S, Dubé MP, Haessler J, Jackson RD, Kooperberg C, Perreault LP, Nauck M, Peters U, Rioux JD, Schmidt F, Turcot V, Völker U, Völzke H, Greinacher A, Hsu L, Tardif JC, Diaz GA, Reiner AP, Lettre G (Jun 2014). "Rare and low-frequency coding variants in CXCR2 and other genes are associated with hematological traits". Nature Genetics. 46 (6): 629–34. doi:10.1038/ng.2962. PMC 4050975. PMID 24777453.
^Acosta JC, O'Loghlen A, Banito A, Guijarro MV, Augert A, Raguz S, Fumagalli M, Da Costa M, Brown C, Popov N, Takatsu Y, Melamed J, d'Adda di Fagagna F, Bernard D, Hernando E, Gil J (Jun 2008). "Chemokine signaling via the CXCR2 receptor reinforces senescence". Cell. 133 (6): 1006–18. doi:10.1016/j.cell.2008.03.038. PMID 18555777. S2CID 6708172.
Further reading
Brandt E, Ludwig A, Petersen F, Flad HD (Oct 2000). "Platelet-derived CXC chemokines: old players in new games". Immunological Reviews. 177: 204–16. doi:10.1034/j.1600-065X.2000.17705.x. PMID 11138777. S2CID 46515022.
Robertson MJ (Feb 2002). "Role of chemokines in the biology of natural killer cells". Journal of Leukocyte Biology. 71 (2): 173–83. PMID 11818437.
Ahuja SK, Ozçelik T, Milatovitch A, Francke U, Murphy PM (Sep 1992). "Molecular evolution of the human interleukin-8 receptor gene cluster". Nature Genetics. 2 (1): 31–6. doi:10.1038/ng0992-31. PMID 1303245. S2CID 19732372.
Lee J, Horuk R, Rice GC, Bennett GL, Camerato T, Wood WI (Aug 1992). "Characterization of two high affinity human interleukin-8 receptors". The Journal of Biological Chemistry. 267 (23): 16283–7. doi:10.1016/S0021-9258(18)41997-7. PMID 1379593.
Morris SW, Nelson N, Valentine MB, Shapiro DN, Look AT, Kozlosky CJ, Beckmann MP, Cerretti DP (Nov 1992). "Assignment of the genes encoding human interleukin-8 receptor types 1 and 2 and an interleukin-8 receptor pseudogene to chromosome 2q35". Genomics. 14 (3): 685–91. doi:10.1016/S0888-7543(05)80169-7. PMID 1427896.
Holmes WE, Lee J, Kuang WJ, Rice GC, Wood WI (Sep 1991). "Structure and functional expression of a human interleukin-8 receptor". Science. 253 (5025): 1278–80. Bibcode:1991Sci...253.1278H. doi:10.1126/science.1840701. PMID 1840701.
Murphy PM, Tiffany HL (Sep 1991). "Cloning of complementary DNA encoding a functional human interleukin-8 receptor". Science. 253 (5025): 1280–3. Bibcode:1991Sci...253.1280M. doi:10.1126/science.1891716. PMID 1891716.
Sprenger H, Lloyd AR, Lautens LL, Bonner TI, Kelvin DJ (Apr 1994). "Structure, genomic organization, and expression of the human interleukin-8 receptor B gene". The Journal of Biological Chemistry. 269 (15): 11065–72. doi:10.1016/S0021-9258(19)78092-2. PMID 7512557.
Morohashi H, Miyawaki T, Nomura H, Kuno K, Murakami S, Matsushima K, Mukaida N (Jan 1995). "Expression of both types of human interleukin-8 receptors on mature neutrophils, monocytes, and natural killer cells". Journal of Leukocyte Biology. 57 (1): 180–7. doi:10.1002/jlb.57.1.180. PMID 7829970. S2CID 7819367.
Ahuja SK, Shetty A, Tiffany HL, Murphy PM (Oct 1994). "Comparison of the genomic organization and promoter function for human interleukin-8 receptors A and B". The Journal of Biological Chemistry. 269 (42): 26381–9. doi:10.1016/S0021-9258(18)47205-5. PMID 7929358.
Cacalano G, Lee J, Kikly K, Ryan AM, Pitts-Meek S, Hultgren B, Wood WI, Moore MW (Jul 1994). "Neutrophil and B cell expansion in mice that lack the murine IL-8 receptor homolog". Science. 265 (5172): 682–4. Bibcode:1994Sci...265..682C. doi:10.1126/science.8036519. PMID 8036519.
Harada A, Kuno K, Nomura H, Mukaida N, Murakami S, Matsushima K (May 1994). "Cloning of a cDNA encoding a mouse homolog of the interleukin-8 receptor". Gene. 142 (2): 297–300. doi:10.1016/0378-1119(94)90278-X. PMID 8194768.
Schnitzel W, Monschein U, Besemer J (Jun 1994). "Monomer-dimer equilibria of interleukin-8 and neutrophil-activating peptide 2. Evidence for IL-8 binding as a dimer and oligomer to IL-8 receptor B". Journal of Leukocyte Biology. 55 (6): 763–70. doi:10.1002/jlb.55.6.763. PMID 8195702. S2CID 5948202.
Mueller SG, Schraw WP, Richmond A (Jan 1994). "Melanoma growth stimulatory activity enhances the phosphorylation of the class II interleukin-8 receptor in non-hematopoietic cells". The Journal of Biological Chemistry. 269 (3): 1973–80. doi:10.1016/S0021-9258(17)42123-5. PMID 8294449.
Wu D, LaRosa GJ, Simon MI (Jul 1993). "G protein-coupled signal transduction pathways for interleukin-8". Science. 261 (5117): 101–3. Bibcode:1993Sci...261..101W. doi:10.1126/science.8316840. PMID 8316840.
Cerretti DP, Kozlosky CJ, Vanden Bos T, Nelson N, Gearing DP, Beckmann MP (Mar 1993). "Molecular characterization of receptors for human interleukin-8, GRO/melanoma growth-stimulatory activity and neutrophil activating peptide-2". Molecular Immunology. 30 (4): 359–67. doi:10.1016/0161-5890(93)90065-J. PMID 8384312.
Ahuja SK, Lee JC, Murphy PM (Jan 1996). "CXC chemokines bind to unique sets of selectivity determinants that can function independently and are broadly distributed on multiple domains of human interleukin-8 receptor B. Determinants of high affinity binding and receptor activation are distinct". The Journal of Biological Chemistry. 271 (1): 225–32. doi:10.1074/jbc.271.1.225. PMID 8550564.
Hammond ME, Shyamala V, Siani MA, Gallegos CA, Feucht PH, Abbott J, Lapointe GR, Moghadam M, Khoja H, Zakel J, Tekamp-Olson P (Apr 1996). "Receptor recognition and specificity of interleukin-8 is determined by residues that cluster near a surface-accessible hydrophobic pocket". The Journal of Biological Chemistry. 271 (14): 8228–35. doi:10.1074/jbc.271.14.8228. PMID 8626516.
Damaj BB, McColl SR, Mahana W, Crouch MF, Naccache PH (May 1996). "Physical association of Gi2alpha with interleukin-8 receptors". The Journal of Biological Chemistry. 271 (22): 12783–9. doi:10.1074/jbc.271.22.12783. PMID 8662698.
Ahuja SK, Murphy PM (Aug 1996). "The CXC chemokines growth-regulated oncogene (GRO) alpha, GRObeta, GROgamma, neutrophil-activating peptide-2, and epithelial cell-derived neutrophil-activating peptide-78 are potent agonists for the type B, but not the type A, human interleukin-8 receptor". The Journal of Biological Chemistry. 271 (34): 20545–50. doi:10.1074/jbc.271.34.20545. PMID 8702798.
External links
CD182+Antigen at the US National Library of Medicine Medical Subject Headings (MeSH)
"Chemokine Receptors: CXCR2". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology.
v
t
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Proteins: clusters of differentiation (see also list of human clusters of differentiation)
2. 2型糖尿病の病因 pathogenesis of type 2 diabetes mellitus
English Journal
A study on IL8RB gene polymorphism as a potential immuno-compromised adherent in exaggeration of parenteral and mammo-crine oxidative stress during mastitis in buffalo.
El Nahas SM1, El Kasas AH1, Abou Mossallem AA1, Abdelhamid MI2, Warda M2.
… Anti-mouse CXCR2 antibody was injected into Il1rn and Ccr2-double-deficient mice for blocking experiments. … Finally, neutralizing antibodies to CXCR2, the receptor for keratinocyte chemoattractant and MIP-2, dramatically attenuated arthritis in Il1rn and Ccr2-double-deficient mice. …
CXCR1 and CXCR2 are closely related receptors that recognize CXC chemokines that possess an E-L-R amino acid motif immediately adjacent to their CXC motif. CXCL8 (otherwise known as interleukin-8) and CXCL6 can both bind CXCR1 ...
The protein encoded by this gene is a member of the G-protein-coupled receptor family. This protein is a receptor for interleukin 8 (IL8). It binds to IL8 with high affinity, and transduces the signal through a G-protein activated second messenger ...
