Health Dictionary
Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.
NOX3
Introduction
NADPH oxidase 3 is an enzyme that in humans is encoded by the NOX3 gene.[1][2]
Function
Function
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][2]
References
References
- ↑ 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.
- ↑ 2.0 2.1 “Entrez Gene: NOX3 NADPH oxidase 3”.
Further reading
Further reading
- 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. 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.
- 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.