NOX1

NADPH oxidase 1

Identifiers

NOX1 ; GP91-2; MOX1; NOH-1; NOH1

External IDs

OMIM: 300225 MGI: 2450016 HomoloGene: 48495 ChEMBL: 1287628 GeneCards: NOX1 Gene

Gene ontology
Molecular function	• protein binding • superoxide-generating NADPH oxidase activity • voltage-gated proton channel activity • metal ion binding • Rac GTPase binding • NADP binding
Cellular component	• early endosome • plasma membrane • integral component of membrane • cell junction • NADPH oxidase complex • invadopodium membrane
Biological process	• angiogenesis • regulation of systemic arterial blood pressure by renin-angiotensin • NADP metabolic process • superoxide metabolic process • inflammatory response • signal transduction • small GTPase mediated signal transduction • regulation of blood pressure • positive regulation of cell proliferation • positive regulation of vascular endothelial growth factor production • proton transport • cell migration • extracellular matrix organization • regulation of ion transmembrane transport • superoxide anion generation • hydrogen peroxide metabolic process • positive regulation of integrin biosynthetic process • respiratory burst • positive regulation of JNK cascade • positive regulation of smooth muscle cell proliferation • intracellular pH elevation • oxidation-reduction process • cellular response to hyperoxia • oxygen metabolic process • positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway • cellular stress response to acidic pH
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr X:
100.84 – 100.87 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

↑ 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.
↑ "Entrez Gene: NOX1 NADPH oxidase 1".

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.

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NOX1

References

Further reading