From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
NADPH oxidase 3 is an enzyme that in humans is encoded by the NOX3 gene .[5] [6] [7]
Function [ edit ] NADPH oxidases, such as NOX3, are plasma membrane-associated enzymes found in many cell types. They catalyze the production of superoxide by a 1-electron reduction of oxygen, using NADPH as the electron donor.[supplied by OMIM][7]
References [ edit ]
^ a b c GRCh38: Ensembl release 89: ENSG00000074771 – Ensembl , May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000023802 – 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 .^ Herb M (February 2024). "NADPH oxidase 3: Beyond the innear ear" . Antioxidants . 13 (2): 219. doi :10.3390/antiox13020219 PMC 10886416 PMID 38397817 . ^ Cheng G, Cao Z, Xu X, van Meir EG, Lambeth JD (May 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 . ^ a b "Entrez Gene: NOX3 NADPH oxidase 3" .
Further reading [ edit ]
Lachgar A, Sojic N, Arbault S, Bruce D, Sarasin A, Amatore C, Bizzini B, Zagury D, Vuillaume M (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 . Cheng G, Ritsick D, Lambeth JD (2004). "Nox3 regulation by NOXO1, p47phox, and p67phox" . J. Biol. Chem . 279 (33): 34250–5. doi :10.1074/jbc.M400660200 PMID 15181005 . Jana A, Pahan K (2004). "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 . Ueno N, Takeya R, Miyano K, Kikuchi H, Sumimoto H (2005). "The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-dependent manner: its regulation by oxidase organizers and activators" . J. Biol. Chem . 280 (24): 23328–39. doi :10.1074/jbc.M414548200 PMID 15824103 . Ueyama T, Geiszt M, Leto TL (2006). "Involvement of Rac1 in activation of multicomponent Nox1- and Nox3-based NADPH oxidases" (PDF) . Mol. Cell. Biol . 26 (6): 2160–74. doi :10.1128/MCB.26.6.2160-2174.2006 . PMC 1430270 PMID 16507994 . Archived from the original (PDF) on 2020-10-09. Retrieved 2018-11-04 . Carnesecchi S, Carpentier JL, Foti M, Szanto I (2006). "Insulin-induced vascular endothelial growth factor expression is mediated by the NADPH oxidase NOX3". Exp. Cell Res . 312 (17): 3413–24. doi :10.1016/j.yexcr.2006.07.003 . PMID 16949073 . Nakano Y, Banfi B, Jesaitis AJ, Dinauer MC, Allen LA, Nauseef WM (2007). "Critical roles for p22phox in the structural maturation and subcellular targeting of Nox3" . Biochem. J . 403 (1): 97–108. doi :10.1042/BJ20060819 . PMC 1828898 PMID 17140397 . Chen G, Adeyemo AA, Zhou J, Chen Y, Doumatey A, Lashley K, Huang H, Amoah A, Agyenim-Boateng K, Eghan BA, Okafor G, Acheampong J, Oli J, Fasanmade O, Johnson T, Rotimi C (2007). "A genome-wide search for linkage to renal function phenotypes in West Africans with type 2 diabetes". Am. J. Kidney Dis . 49 (3): 394–400. doi :10.1053/j.ajkd.2006.12.011 . PMID 17336700 .
