NOX1

NOX1
Identifiers
Aliases	NOX1 , GP91-2, MOX1, NOH-1, NOH1, NADPH oxidase 1, NOH-1L
External IDs	OMIM: 300225 MGI: 2450016 HomoloGene: 48495 GeneCards: NOX1
Gene location (Human)
Chr.	X chromosome (human)
End	100,874,359 bp
Gene location (Mouse)
Chr.	X chromosome (mouse)
End	133,122,705 bp
RNA expression pattern
	Top expressed in
	rectum; ; pancreatic ductal cell; ; appendix; ; smooth muscle tissue; ; palpebral conjunctiva; ; seminal vesicula; ; metanephros; ; gallbladder; ; hypothalamus; ; cerebellar hemisphere;
	Top expressed in
	ileum; ; duodenum; ; colon; ; jejunum; ; secondary oocyte; ; embryo; ; lung; ; quadriceps femoris muscle; ; cerebellar cortex; ; thymus;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	metal ion binding ; voltage-gated ion channel activity ; protein binding ; NADP binding ; oxidoreductase activity ; superoxide-generating NAD(P)H oxidase activity ;
Cellular component	cytoplasm ; integral component of membrane ; endosome ; cell projection ; membrane ; plasma membrane ; cell junction ; NADPH oxidase complex ; early endosome ;
Biological process	cellular stress response to acidic pH ; NADP metabolic process ; intracellular pH elevation ; cellular response to hyperoxia ; regulation of ion transmembrane transport ; extracellular matrix organization ; positive regulation of JNK cascade ; oxygen metabolic process ; ion transport ; positive regulation of integrin biosynthetic process ; regulation of blood pressure ; respiratory burst ; hydrogen peroxide metabolic process ; angiogenesis ; positive regulation of cell population proliferation ; positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway ; positive regulation of vascular endothelial growth factor production ; inflammatory response ; regulation of systemic arterial blood pressure by renin-angiotensin ; cell migration ; signal transduction ; positive regulation of smooth muscle cell proliferation ; positive regulation of MAPK cascade ; ion transmembrane transport ; superoxide anion generation ; defense response ;
	Sources:Amigo / QuickGO
Orthologs
	27035
	237038
	ENSG00000007952
	ENSMUSG00000031257
	Q9Y5S8
	Q8CIZ9
	NM_013955 ; NM_001271815 ; NM_007052 ; NM_013954
	NM_172203
	NP_001258744 ; NP_008983 ; NP_039249
	NP_757340
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated September 05, 2022

NADPH oxidase 1 is an enzyme that in humans is encoded by the NOX1 gene.^[5]

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.^[6]

Related Research Articles

Respiratory burst is the rapid release of the reactive oxygen species (ROS), superoxide anion and hydrogen peroxide, from different cell types.

NADPH oxidase is a membrane-bound enzyme complex that faces the extracellular space. It can be found in the plasma membrane as well as in the membranes of phagosomes used by neutrophil white blood cells to engulf microorganisms. Human isoforms of the catalytic component of the complex include NOX1, NOX2, NOX3, NOX4, NOX5, DUOX1, and DUOX2.

NADPH oxidase 2 (Nox2), also known as cytochrome b(558) subunit beta or Cytochrome b-245 heavy chain, is a protein that in humans is encoded by the NOX2 gene. The protein is a superoxide generating enzyme which forms reactive oxygen species (ROS).

Neutrophil cytosol factor 1, also known as p47phox, is a protein that in humans is encoded by the NCF1 gene.

NADPH oxidase 4 is an enzyme that in humans is encoded by the NOX4 gene, and is a member of the NOX family of NADPH oxidases.

Cytochrome b-245 light chain is a protein that in humans is encoded by the CYBA gene involved in superoxide production and phagocytosis.

P2Y purinoceptor 11 is a protein that in humans is encoded by the P2RY11 gene.i

Rac2 is a small signaling G protein, and is a member of the Rac subfamily of the family Rho family of GTPases. It is encoded by the gene RAC2.

Neutrophil cytosol factor 4 is a protein that in humans is encoded by the NCF4 gene.

Chloride intracellular channel protein 1 is a protein that in humans is encoded by the CLIC1 gene.

DnaJ homolog subfamily B member 1 is a protein that in humans is encoded by the DNAJB1 gene.

Peroxiredoxin-6 is a protein that in humans is encoded by the PRDX6 gene. It is a member of the peroxiredoxin family of antioxidant enzymes.

Dual oxidase 2, also known as DUOX2 or ThOX2, is an enzyme that in humans is encoded by the DUOX2 gene. Dual oxidase is an enzyme that was first identified in the mammalian thyroid gland. In humans, two isoforms are found; hDUOX1 and hDUOX2. The protein location is not exclusive to thyroid tissue; hDUOX1 is prominent in airway epithelial cells and hDUOX2 in the salivary glands and gastrointestinal tract.

Dual oxidase 1, also known as DUOX1 or ThOX1, is an enzyme which in humans is encoded by the DUOX1 gene. DUOX1 was first identified in the mammalian thyroid gland. In humans, two isoforms are found; hDUOX1 and hDUOX2. Human DUOX protein localization is not exclusive to thyroid tissue; hDUOX1 is prominent in airway epithelial cells and hDUOX2 in the salivary glands and gastrointestinal tract.

NADPH oxidase, EF-hand calcium binding domain 5, also known as NOX5, is a protein which in humans is encoded by the NOX5 gene.

NADPH oxidase organizer 1 is an enzyme that in humans is encoded by the NOXO1 gene.

NADPH oxidase 3 is an enzyme that in humans is encoded by the NOX3 gene.

NADPH oxidase activator 1 is an enzyme that in humans is encoded by the NOXA1 gene.

p22phox Protein, also known as the human neutrophil cytochrome b light chain (CYBA), is an essential component of the membrane-associated enzyme phagocyte NADPH-oxidase This enzyme uses NADH or NADPH as the electron donor for the one electron reduction of oxygen to produce superoxide anion, a reactive oxygen species (ROS), and a functionally important step for the antimicrobial activity of phagocytic cells. p22phox is also expressed in many other human cells such as endothelial and vascular smooth muscle cells, including those within the coronary arteries. Specific polymorphisms of the CYBA gene have been identified that are associated with a decreased risk of coronary artery disease (CAD).

Edgar Pick is an Israeli immunologist who is Professor Emeritus of Immunology in the Department of Clinical Microbiology and Immunology at the Sackler Faculty of Medicine at Tel Aviv University, Israel.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000007952 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000031257 - 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.
↑ 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. Bibcode:1999Natur.401...79S. doi:10.1038/43459. PMID 10485709. S2CID 4365361.
↑ "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. doi:10.1128/JVI.73.2.1447-1452.1999. 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. Bibcode:2002PNAS...9916899M. 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. S2CID 22933040.
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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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000007952 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000031257 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10485709-5] 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. Bibcode:1999Natur.401...79S. doi:10.1038/43459. PMID 10485709. S2CID 4365361.

[entrez-6] "Entrez Gene: NOX1 NADPH oxidase 1".

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NOX1

Related Research Articles

References

Further reading