From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
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]
References
- ^
a
b
c
GRCh38: Ensembl release 89: ENSG00000007952 –
Ensembl, May 2017
- ^
a
b
c
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".
Further reading
- 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.