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Interleukin 8 receptor, alpha

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Title: Interleukin 8 receptor, alpha  
Author: World Heritage Encyclopedia
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Subject: Interleukin 8 receptor, beta, CCR9, CXCR6, IL3RA, C-C chemokine receptor type 7
Collection: Chemokine Receptors, Clusters of Differentiation
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Interleukin 8 receptor, alpha

Chemokine (C-X-C motif) receptor 1

Rendering of
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols  ; C-C; C-C-CKR-1; CD128; CD181; CDw128a; CKR-1; CMKAR1; IL8R1; IL8RA; IL8RBA
External IDs IUPHAR: ChEMBL: GeneCards:
RNA expression pattern
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Interleukin 8 receptor, alpha is a chemokine receptor. IL8RA is its human gene. IL8RA has also been designated CD181 (cluster of differentiation 181), and CXCR1. CXCR1 is now the IUPHAR Committee on Receptor Nomenclature and Drug Classification recommended name.

Contents

  • Function 1
  • Clinical significance 2
  • Interactions 3
  • See also 4
  • References 5
  • External links 6
  • Further_reading 7

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. Knockout studies in mice suggested that this protein inhibits embryonic oligodendrocyte precursor migration in developing spinal cord. This gene, IL8RB, 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.[1] Stimulation of CXCR1 in neutrophils by its primary ligand, Interleukin 8, leads to neutrophil chemotaxis and activation.[2]

Clinical significance

Blocking CXCR1 (e.g., with repertaxin[3]) inhibits some human breast cancer stem cells (in vitro and in mice).[4]

CXCR1 can be cleaved and inactivated by Neutrophil Derived Serine Proteases (NSPs), leading to neutrophil dysfunction and impaired bacterial killing in Cystic Fibrosis lung disease.[5]

Interactions

Interleukin 8 receptor, alpha has been shown to interact with GNAI2.[6][7]

See also

References

  1. ^ "Entrez Gene: IL8RA interleukin 8 receptor, alpha". 
  2. ^ Bergin DA, Reeves EP, Meleady P, Henry M, McElvaney OJ, Carroll TP, Condron C, Chotirmall SH, Clynes M, O'Neill SJ, McElvaney NG (December 2010). "α-1 Antitrypsin regulates human neutrophil chemotaxis induced by soluble immune complexes and IL-8". J. Clin. Invest. 120 (12): 4236–50.  
  3. ^ Casilli F, Bianchini A, Gloaguen I, Biordi L, Alesse E, Festuccia C, Cavalieri B, Strippoli R, Cervellera MN, Di Bitondo R, Ferretti E, Mainiero F, Bizzarri C, Colotta F, Bertini R (February 2005). "Inhibition of interleukin-8 (CXCL8/IL-8) responses by repertaxin, a new inhibitor of the chemokine receptors CXCR1 and CXCR2". Biochem. Pharmacol. 69 (3): 385–94.  
  4. ^ Ginestier C, Liu S, Diebel ME, Korkaya H, Luo M, Brown M, Wicinski J, Cabaud O, Charafe-Jauffret E, Birnbaum D, Guan JL, Dontu G, Wicha MS (February 2010). "CXCR1 blockade selectively targets human breast cancer stem cells in vitro and in xenografts". J. Clin. Invest. 120 (2): 485–97.  
  5. ^ Hartl D, Latzin P, Hordijk P, Marcos V, Rudolph C, Woischnik M, Krauss-Etschmann S, Koller B, Reinhardt D, Roscher AA, Roos D, Griese M (December 2007). "Cleavage of CXCR1 on neutrophils disables bacterial killing in cystic fibrosis lung disease". Nat. Med. 13 (12): 1423–30.  
  6. ^ Damaj BB, McColl SR, Neote K, Songqing N, Ogborn KT, Hébert CA, Naccache PH (October 1996). "Identification of G-protein binding sites of the human interleukin-8 receptors by functional mapping of the intracellular loops". FASEB J. 10 (12): 1426–34.  
  7. ^ Damaj BB, McColl SR, Mahana W, Crouch MF, Naccache PH (May 1996). "Physical association of Gi2alpha with interleukin-8 receptors". J. Biol. Chem. 271 (22): 12783–9.  

External links

  • "Chemokine Receptors: CXCR1". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology. 

Further_reading

  • Ahuja SK, Ozçelik T, Milatovitch A et al. (1993). "Molecular evolution of the human interleukin-8 receptor gene cluster". Nat. Genet. 2 (1): 31–6.  
  • Lee J, Horuk R, Rice GC et al. (1992). "Characterization of two high affinity human interleukin-8 receptors". J. Biol. Chem. 267 (23): 16283–7.  
  • Morris SW, Nelson N, Valentine MB et al. (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.  
  • Holmes WE, Lee J, Kuang WJ et al. (1991). "Structure and functional expression of a human interleukin-8 receptor". Science 253 (5025): 1278–80.  
  • Chuntharapai A, Lee J, Hébert CA, Kim KJ (1995). "Monoclonal antibodies detect different distribution patterns of IL-8 receptor A and IL-8 receptor B on human peripheral blood leukocytes". J. Immunol. 153 (12): 5682–8.  
  • Chuntharapai A, Kim KJ (1995). "Regulation of the expression of IL-8 receptor A/B by IL-8: possible functions of each receptor". J. Immunol. 155 (5): 2587–94.  
  • Morohashi H, Miyawaki T, Nomura H et al. (1995). "Expression of both types of human interleukin-8 receptors on mature neutrophils, monocytes, and natural killer cells". J. Leukoc. Biol. 57 (1): 180–7.  
  • Schönbeck U, Brandt E, Petersen F et al. (1995). "IL-8 specifically binds to endothelial but not to smooth muscle cells". J. Immunol. 154 (5): 2375–83.  
  • Ahuja SK, Shetty A, Tiffany HL, Murphy PM (1994). "Comparison of the genomic organization and promoter function for human interleukin-8 receptors A and B". J. Biol. Chem. 269 (42): 26381–9.  
  • Sprenger H, Lloyd AR, Meyer RG et al. (1994). "Genomic structure, characterization, and identification of the promoter of the human IL-8 receptor A gene". J. Immunol. 153 (6): 2524–32.  
  • Schnitzel W, Monschein U, Besemer J (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". J. Leukoc. Biol. 55 (6): 763–70.  
  • Wu D, LaRosa GJ, Simon MI (1993). "G protein-coupled signal transduction pathways for interleukin-8". Science 261 (5117): 101–3.  
  • Sebok K, Woodside D, al-Aoukaty A et al. (1993). "IL-8 induces the locomotion of human IL-2-activated natural killer cells. Involvement of a guanine nucleotide binding (Go) protein". J. Immunol. 150 (4): 1524–34.  
  • Cerretti DP, Kozlosky CJ, Vanden Bos T et al. (1993). "Molecular characterization of receptors for human interleukin-8, GRO/melanoma growth-stimulatory activity and neutrophil activating peptide-2". Mol. Immunol. 30 (4): 359–67.  
  • Mollereau C, Muscatelli F, Mattei MG et al. (1993). "The high-affinity interleukin 8 receptor gene (IL8RA) maps to the 2q33-q36 region of the human genome: cloning of a pseudogene (IL8RBP) for the low-affinity receptor". Genomics 16 (1): 248–51.  
  • Lloyd A, Modi W, Sprenger H et al. (1993). "Assignment of genes for interleukin-8 receptors (IL8R) A and B to human chromosome band 2q35". Cytogenet. Cell Genet. 63 (4): 238–40.  
  • Damaj BB, McColl SR, Mahana W et al. (1996). "Physical association of Gi2alpha with interleukin-8 receptors". J. Biol. Chem. 271 (22): 12783–9.  
  • Ahuja SK, Murphy PM (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". J. Biol. Chem. 271 (34): 20545–50.  
  • Damaj BB, McColl SR, Neote K et al. (1996). "Identification of G-protein binding sites of the human interleukin-8 receptors by functional mapping of the intracellular loops". FASEB J. 10 (12): 1426–34.  
  • Jerva LF, Sullivan G, Lolis E (1997). "Functional and receptor binding characterization of recombinant murine macrophage inflammatory protein 2: sequence analysis and mutagenesis identify receptor binding epitopes". Protein Sci. 6 (8): 1643–52.  

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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