NOX4

Identifiers

NOX4, KOX, KOX-1, RENOX, NADPH oxidase 4

External IDs

MGI: 1354184 HomoloGene: 41065 GeneCards: NOX4

Genetically Related Diseases

Gene ontology
Molecular function	• nucleotide binding • NAD(P)H oxidase activity • flavin adenine dinucleotide binding • oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor • modified amino acid binding • protein binding • heme binding • electron carrier activity • oxidoreductase activity • oxygen sensor activity • superoxide-generating NADPH oxidase activity
Cellular component	• integral component of membrane • membrane • focal adhesion • plasma membrane • stress fiber • cell junction • NADPH oxidase complex • nucleolus • apical plasma membrane • mitochondrion • endoplasmic reticulum • perinuclear region of cytoplasm • nucleus • cell periphery • endoplasmic reticulum membrane
Biological process	• cellular response to transforming growth factor beta stimulus • positive regulation of protein kinase B signaling • response to hypoxia • gene expression • positive regulation of MAP kinase activity • cardiac muscle cell differentiation • aging • bone resorption • reactive oxygen species metabolic process • superoxide anion generation • positive regulation of smooth muscle cell migration • cell aging • positive regulation of reactive oxygen species metabolic process • cellular response to gamma radiation • cell morphogenesis • positive regulation of DNA biosynthetic process • positive regulation of ERK1 and ERK2 cascade • positive regulation of apoptotic process • homocysteine metabolic process • inflammatory response • oxidation-reduction process • positive regulation of stress fiber assembly • cellular response to cAMP • cellular response to glucose stimulus • superoxide metabolic process • negative regulation of cell proliferation • response to reactive oxygen species
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


50507


50490

Ensembl


ENSG00000086991


ENSMUSG00000030562

UniProt


Q9NPH5


Q9JHI8

RefSeq (mRNA)

NM_001143836 NM_001143837 NM_001291926 NM_001291927 NM_001291929
NM_001300995 NM_016931


NM_001285833 NM_001285835 NM_015760

RefSeq (protein)

NP_001137308.1 NP_001137309.1 NP_001278855.1 NP_001278856.1 NP_001287924.1
NP_058627.1


NP_056575.1

Location (UCSC)

Chr 11: 89.32 – 89.5 Mb

Chr 7: 87.25 – 87.4 Mb

PubMed search

^[2]

^[3]

Wikidata

View/Edit Human

View/Edit Mouse

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.^[4]

Function

Oxygen sensing is essential for homeostasis in all aerobic organisms. A phagocyte-type oxidase, similar to that responsible for the production of large amounts of reactive oxygen species (ROS) in neutrophil granulocytes, with resultant antimicrobial activity, has been postulated to function in the kidney as an oxygen sensor that regulates the synthesis of erythropoietin in the renal cortex.^[4] Nox4 protects the vasculature against inflammatory stress.^[5] Nox-dependent reactive oxygen species modulation by amino endoperoxides can induce apoptosis in high Nox4-expressing cancer cells.^[6]

References

↑ "Diseases that are genetically associated with NOX4 view/edit references on wikidata".
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
1 2 "Entrez Gene: NOX4 NADPH oxidase 4".
↑ Schröder K, Zhang M, Benkhoff S, Mieth A, Pliquett R, Kosowski J, Kruse C, Luedike P, Michaelis UR, Weissmann N, Dimmeler S, Shah AM, Brandes RP (April 2012). "Nox4 is a protective reactive oxygen species generating vascular NADPH oxidase". Circ. Res. 110 (9): 1217–25. doi:10.1161/CIRCRESAHA.112.267054. PMID 22456182.
↑ Zhu P, Tong BM, Wang R, Chen JP, Foo S, Chong HC, Wang XL, Ang GY, Chiba S, Tan NS (March 2013). "Nox4-dependent ROS modulation by amino endoperoxides to induce apoptosis in cancer cells.". Cell Death Dis. 4: e552. doi:10.1038/cddis.2013.68. PMID 23519121.

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.
Geiszt M, Kopp JB, Várnai P, Leto TL (2000). "Identification of renox, an NAD(P)H oxidase in kidney.". Proc. Natl. Acad. Sci. U.S.A. 97 (14): 8010–4. doi:10.1073/pnas.130135897. PMC 16661. PMID 10869423.
Shiose A, Kuroda J, Tsuruya K, et al. (2001). "A novel superoxide-producing NAD(P)H oxidase in kidney.". J. Biol. Chem. 276 (2): 1417–23. doi:10.1074/jbc.M007597200. PMID 11032835.
Cheng G, Cao Z, Xu X, et al. (2001). "Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5.". Gene. 269 (1–2): 131–40. doi:10.1016/S0378-1119(01)00449-8. PMID 11376945.
Brar SS, Kennedy TP, Sturrock AB, et al. (2002). "An NAD(P)H oxidase regulates growth and transcription in melanoma cells". Am. J. Physiol., Cell Physiol. 282 (6): C1212–24. doi:10.1152/ajpcell.00496.2001. PMID 11997235.
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.
Kalinina N, Agrotis A, Tararak E, et al. (2002). "Cytochrome b558-dependent NAD(P)H oxidase-phox units in smooth muscle and macrophages of atherosclerotic lesions". Arterioscler. Thromb. Vasc. Biol. 22 (12): 2037–43. doi:10.1161/01.ATV.0000040222.02255.0F. PMID 12482831.
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.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Mahadev K, Motoshima H, Wu X, et al. (2004). "The NAD(P)H oxidase homolog Nox4 modulates insulin-stimulated generation of H2O2 and plays an integral role in insulin signal transduction". Mol. Cell. Biol. 24 (5): 1844–54. doi:10.1128/MCB.24.5.1844-1854.2004. PMC 350558. PMID 14966267.
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.
Vaquero EC, Edderkaoui M, Pandol SJ, et al. (2004). "Reactive oxygen species produced by NAD(P)H oxidase inhibit apoptosis in pancreatic cancer cells". J. Biol. Chem. 279 (33): 34643–54. doi:10.1074/jbc.M400078200. PMID 15155719.
Schwarzer C, Machen TE, Illek B, Fischer H (2004). "NADPH oxidase-dependent acid production in airway epithelial cells". J. Biol. Chem. 279 (35): 36454–61. doi:10.1074/jbc.M404983200. PMID 15210697.
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.
Park HS, Jung HY, Park EY, et al. (2004). "Cutting edge: direct interaction of TLR4 with NAD(P)H oxidase 4 isozyme is essential for lipopolysaccharide-induced production of reactive oxygen species and activation of NF-kappa B". J. Immunol. 173 (6): 3589–93. doi:10.4049/jimmunol.173.6.3589. PMID 15356101.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Jana A, Pahan K (2005). "Human immunodeficiency virus type 1 gp120 induces apoptosis in human primary neurons through redox-regulated activation of neutral sphingomyelinase". J. Neurosci. 24 (43): 9531–40. doi:10.1523/JNEUROSCI.3085-04.2004. PMC 1955476. PMID 15509740.
Pedruzzi E, Guichard C, Ollivier V, et al. (2004). "NAD(P)H oxidase Nox-4 mediates 7-ketocholesterol-induced endoplasmic reticulum stress and apoptosis in human aortic smooth muscle cells". Mol. Cell. Biol. 24 (24): 10703–17. doi:10.1128/MCB.24.24.10703-10717.2004. PMC 533993. PMID 15572675.
Djordjevic T, BelAiba RS, Bonello S, et al. (2005). "Human urotensin II is a novel activator of NADPH oxidase in human pulmonary artery smooth muscle cells". Arterioscler. Thromb. Vasc. Biol. 25 (3): 519–25. doi:10.1161/01.ATV.0000154279.98244.eb. PMID 15618545.

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NOX4

Function

References

Further reading