NOX1

NADPH oxidase 1
Identifiers
SymbolsNOX1 ; GP91-2; MOX1; NOH-1; NOH1
External IDsOMIM: 300225 MGI: 2450016 HomoloGene: 48495 ChEMBL: 1287628 GeneCards: NOX1 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez27035237038
EnsemblENSG00000007952ENSMUSG00000031257
UniProtQ9Y5S8Q8CIZ9
RefSeq (mRNA)NM_001271815NM_172203
RefSeq (protein)NP_001258744NP_757340
Location (UCSC)Chr X:
100.1 – 100.13 Mb		Chr X:
134.09 – 134.22 Mb
PubMed search

NADPH oxidase 1 is an enzyme that in humans is encoded by the NOX1 gene.[1]

NOX1 is a homolog of the catalytic subunit of the superoxide-generating NADPH oxidase of phagocytes, gp91phox. Two transcript variants encoding different isoforms have been found for this gene.[2]

References

  1. ↑ Suh YA, Arnold RS, Lassegue B, Shi J, Xu X, Sorescu D, Chung AB, Griendling KK, Lambeth JD (Sep 1999). "Cell transformation by the superoxide-generating oxidase Mox1". Nature 401 (6748): 79–82. doi:10.1038/43459. PMID 10485709.
  2. ↑ "Entrez Gene: NOX1 NADPH oxidase 1".

Further reading

  • Lachgar A, Sojic N, Arbault S et al. (1999). "Amplification of the inflammatory cellular redox state by human immunodeficiency virus type 1-immunosuppressive tat and gp160 proteins.". J. Virol. 73 (2): 1447–52. PMC 103969. PMID 9882350.
  • Kikuchi H, Hikage M, Miyashita H, Fukumoto M (2000). "NADPH oxidase subunit, gp91(phox) homologue, preferentially expressed in human colon epithelial cells.". Gene 254 (1–2): 237–43. doi:10.1016/S0378-1119(00)00258-4. PMID 10974555.
  • Dahlgren C, Karlsson A (2002). "Ionomycin-induced neutrophil NADPH oxidase activity is selectively inhibited by the serine protease inhibitor diisopropyl fluorophosphate". Antioxid. Redox Signal. 4 (1): 17–25. doi:10.1089/152308602753625816. PMID 11970839.
  • Babior BM (2002). "The activity of leukocyte NADPH oxidase: regulation by p47PHOX cysteine and serine residues". Antioxid. Redox Signal. 4 (1): 35–8. doi:10.1089/152308602753625834. PMID 11970841.
  • Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Geiszt M, Lekstrom K, Witta J, Leto TL (2003). "Proteins homologous to p47phox and p67phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells". J. Biol. Chem. 278 (22): 20006–12. doi:10.1074/jbc.M301289200. PMID 12657628.
  • Takeya R, Ueno N, Kami K et al. (2003). "Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases". J. Biol. Chem. 278 (27): 25234–46. doi:10.1074/jbc.M212856200. PMID 12716910.
  • Geiszt M, Lekstrom K, Brenner S et al. (2003). "NAD(P)H oxidase 1, a product of differentiated colon epithelial cells, can partially replace glycoprotein 91phox in the regulated production of superoxide by phagocytes". J. Immunol. 171 (1): 299–306. doi:10.4049/jimmunol.171.1.299. PMID 12817011.
  • Chamulitrat W, Schmidt R, Tomakidi P et al. (2003). "Association of gp91phox homolog Nox1 with anchorage-independent growth and MAP kinase-activation of transformed human keratinocytes". Oncogene 22 (38): 6045–53. doi:10.1038/sj.onc.1206654. PMID 12955083.
  • Cheng G, Lambeth JD (2004). "NOXO1, regulation of lipid binding, localization, and activation of Nox1 by the Phox homology (PX) domain". J. Biol. Chem. 279 (6): 4737–42. doi:10.1074/jbc.M305968200. PMID 14617635.
  • Hilenski LL, Clempus RE, Quinn MT et al. (2004). "Distinct subcellular localizations of Nox1 and Nox4 in vascular smooth muscle cells". Arterioscler. Thromb. Vasc. Biol. 24 (4): 677–83. doi:10.1161/01.ATV.0000112024.13727.2c. PMID 14670934.
  • Morré DM, Guo F, Morré DJ (2004). "An aging-related cell surface NADH oxidase (arNOX) generates superoxide and is inhibited by coenzyme Q". Mol. Cell. Biochem. 254 (1–2): 101–9. doi:10.1023/A:1027301405614. PMID 14674687.
  • Chamulitrat W, Stremmel W, Kawahara T et al. (2004). "A constitutive NADPH oxidase-like system containing gp91phox homologs in human keratinocytes". J. Invest. Dermatol. 122 (4): 1000–9. doi:10.1111/j.0022-202X.2004.22410.x. PMID 15102091.
  • Goyal P, Weissmann N, Grimminger F et al. (2004). "Upregulation of NAD(P)H oxidase 1 in hypoxia activates hypoxia-inducible factor 1 via increase in reactive oxygen species". Free Radic. Biol. Med. 36 (10): 1279–88. doi:10.1016/j.freeradbiomed.2004.02.071. PMID 15110393.
  • Barbieri SS, Cavalca V, Eligini S et al. (2005). "Apocynin prevents cyclooxygenase 2 expression in human monocytes through NADPH oxidase and glutathione redox-dependent mechanisms". Free Radic. Biol. Med. 37 (2): 156–65. doi:10.1016/j.freeradbiomed.2004.04.020. PMID 15203187.
  • Guzik TJ, Sadowski J, Kapelak B et al. (2005). "Systemic regulation of vascular NAD(P)H oxidase activity and nox isoform expression in human arteries and veins". Arterioscler. Thromb. Vasc. Biol. 24 (9): 1614–20. doi:10.1161/01.ATV.0000139011.94634.9d. PMID 15256399.
  • Ambasta RK, Kumar P, Griendling KK et al. (2004). "Direct interaction of the novel Nox proteins with p22phox is required for the formation of a functionally active NADPH oxidase". J. Biol. Chem. 279 (44): 45935–41. doi:10.1074/jbc.M406486200. PMID 15322091.
  • Geiszt M, Lekstrom K, Leto TL (2005). "Analysis of mRNA transcripts from the NAD(P)H oxidase 1 (Nox1) gene. Evidence against production of the NADPH oxidase homolog-1 short (NOH-1S) transcript variant". J. Biol. Chem. 279 (49): 51661–8. doi:10.1074/jbc.M409325200. PMID 15375166.