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
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
^
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
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 .