# NOX5

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> Source: https://en.wikipedia.org/wiki/NOX5
> Source revision: 1317918146
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**NADPH oxidase, EF-hand calcium binding domain 5**, also known as **NOX5**, is a [protein](/source/Protein) which in humans is encoded by the *NOX5* [gene](/source/Gene).[1][2]

## Function

NOX5 is a novel [NADPH oxidase](/source/NADPH_oxidase) that generates [superoxide](/source/Superoxide).[1]

Nox5 interacts with [c-abl](/source/Abl_gene), superoxide production leads to [phosphorylation](/source/Phosphorylation) of c-abl, while inhibition of c-abl kinase activity inhibits Nox5 superoxide production.[3]

## References

1. ["Entrez Gene: NOX5 NADPH oxidase, EF-hand calcium binding domain 5"](https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=79400)

1. Bánfi B, Molnár G, Maturana A, Steger K, Hegedûs B, Demaurex N, Krause KH (October 2001). "A Ca(2+)-activated NADPH oxidase in testis, spleen, and lymph nodes". *J. Biol. Chem.*. **276** (40): 37594–601. [doi:10.1074/jbc.M103034200](https://doi.org/10.1074/jbc.M103034200). [PMID 11483596](https://pubmed.ncbi.nlm.nih.gov/11483596)

1. El Jamali A, Valente AJ, Lechleiter JD, Gamez MJ, Pearson DW, Nauseef WM, Clark RA (March 2008). "Novel redox-dependent regulation of NOX5 by the tyrosine kinase c-Abl". *Free Radic. Biol. Med.*. **44** (5): 868–81. [doi:10.1016/j.freeradbiomed.2007.11.020](https://doi.org/10.1016/j.freeradbiomed.2007.11.020). [PMC 2278123](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2278123). [PMID 18160052](https://pubmed.ncbi.nlm.nih.gov/18160052)

## Further reading

- Lachgar A, Sojic N, Arbault S, etal (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](https://doi.org/10.1128/JVI.73.2.1447-1452.1999). [PMC 103969](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC103969). [PMID 9882350](https://pubmed.ncbi.nlm.nih.gov/9882350)
- Cheng G, Cao Z, Xu X, etal (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](https://doi.org/10.1016/S0378-1119(01)00449-8). [PMID 11376945](https://pubmed.ncbi.nlm.nih.gov/11376945)
- Bánfi B, Molnár G, Maturana A, etal (2001). "A Ca(2+)-activated NADPH oxidase in testis, spleen, and lymph nodes". *J. Biol. Chem.*. **276** (40): 37594–601. [doi:10.1074/jbc.M103034200](https://doi.org/10.1074/jbc.M103034200). [PMID 11483596](https://pubmed.ncbi.nlm.nih.gov/11483596)
- Armstrong JS, Bivalacqua TJ, Chamulitrat W, etal (2002). "A comparison of the NADPH oxidase in human sperm and white blood cells". *Int. J. Androl.*. **25** (4): 223–9. [doi:10.1046/j.1365-2605.2002.00351.x](https://doi.org/10.1046/j.1365-2605.2002.00351.x). [PMID 12121572](https://pubmed.ncbi.nlm.nih.gov/12121572)
- Moskwa P, Dagher MC, Paclet MH, etal (2002). "Participation of Rac GTPase activating proteins in the deactivation of the phagocytic NADPH oxidase". *Biochemistry*. **41** (34): 10710–6. [doi:10.1021/bi0257033](https://doi.org/10.1021/bi0257033). [PMID 12186557](https://pubmed.ncbi.nlm.nih.gov/12186557)
- Ota T, Suzuki Y, Nishikawa T, etal (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". *Nat. Genet.*. **36** (1): 40–5. [doi:10.1038/ng1285](https://doi.org/10.1038/ng1285). [PMID 14702039](https://pubmed.ncbi.nlm.nih.gov/14702039)
- Bánfi B, Tirone F, Durussel I, etal (2004). "Mechanism of Ca2+ activation of the NADPH oxidase 5 (NOX5)". *J. Biol. Chem.*. **279** (18): 18583–91. [doi:10.1074/jbc.M310268200](https://doi.org/10.1074/jbc.M310268200). [PMID 14982937](https://pubmed.ncbi.nlm.nih.gov/14982937)
- 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](https://doi.org/10.1523/JNEUROSCI.3085-04.2004). [PMC 1955476](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1955476). [PMID 15509740](https://pubmed.ncbi.nlm.nih.gov/15509740)
- Kawahara T, Ritsick D, Cheng G, Lambeth JD (2005). "Point mutations in the proline-rich region of p22phox are dominant inhibitors of Nox1- and Nox2-dependent reactive oxygen generation". *J. Biol. Chem.*. **280** (36): 31859–69. [doi:10.1074/jbc.M501882200](https://doi.org/10.1074/jbc.M501882200). [PMID 15994299](https://pubmed.ncbi.nlm.nih.gov/15994299)
- Femling JK, Nauseef WM, Weiss JP (2005). "Synergy between extracellular group IIA phospholipase A2 and phagocyte NADPH oxidase in digestion of phospholipids of Staphylococcus aureus ingested by human neutrophils". *J. Immunol.*. **175** (7): 4653–61. [doi:10.4049/jimmunol.175.7.4653](https://doi.org/10.4049/jimmunol.175.7.4653). [PMID 16177112](https://pubmed.ncbi.nlm.nih.gov/16177112)
- Cucoranu I, Clempus R, Dikalova A, etal (2005). "NAD(P)H oxidase 4 mediates transforming growth factor-beta1-induced differentiation of cardiac fibroblasts into myofibroblasts". *Circ. Res.*. **97** (9): 900–7. [doi:10.1161/01.RES.0000187457.24338.3D](https://doi.org/10.1161/01.RES.0000187457.24338.3D). [PMID 16179589](https://pubmed.ncbi.nlm.nih.gov/16179589)
- Kamiguti AS, Serrander L, Lin K, etal (2006). "Expression and activity of NOX5 in the circulating malignant B cells of hairy cell leukemia". *J. Immunol.*. **175** (12): 8424–30. [doi:10.4049/jimmunol.175.12.8424](https://doi.org/10.4049/jimmunol.175.12.8424). [PMID 16339585](https://pubmed.ncbi.nlm.nih.gov/16339585)
- Fu X, Beer DG, Behar J, etal (2006). "cAMP-response element-binding protein mediates acid-induced NADPH oxidase NOX5-S expression in Barrett esophageal adenocarcinoma cells". *J. Biol. Chem.*. **281** (29): 20368–82. [doi:10.1074/jbc.M603353200](https://doi.org/10.1074/jbc.M603353200). [PMID 16707484](https://pubmed.ncbi.nlm.nih.gov/16707484)
- Duerrschmidt N, Stielow C, Muller G, etal (2006). "NO-mediated regulation of NAD(P)H oxidase by laminar shear stress in human endothelial cells". *J. Physiol.*. **576** (Pt 2): 557–67. [doi:10.1113/jphysiol.2006.111070](https://doi.org/10.1113/jphysiol.2006.111070). [PMC 1890367](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1890367). [PMID 16873416](https://pubmed.ncbi.nlm.nih.gov/16873416)
- Chenevier-Gobeaux C, Lemarechal H, Bonnefont-Rousselot D, etal (2007). "Superoxide production and NADPH oxidase expression in human rheumatoid synovial cells: regulation by interleukin-1beta and tumour necrosis factor-alpha". *Inflamm. Res.*. **55** (11): 483–90. [doi:10.1007/s00011-006-6036-8](https://doi.org/10.1007/s00011-006-6036-8). [PMID 17122966](https://pubmed.ncbi.nlm.nih.gov/17122966). [S2CID 9576123](https://api.semanticscholar.org/CorpusID:9576123)
- Jagnandan D, Church JE, Banfi B, etal (2007). "Novel mechanism of activation of NADPH oxidase 5. calcium sensitization via phosphorylation". *J. Biol. Chem.*. **282** (9): 6494–507. [doi:10.1074/jbc.M608966200](https://doi.org/10.1074/jbc.M608966200). [PMID 17164239](https://pubmed.ncbi.nlm.nih.gov/17164239)
- BelAiba RS, Djordjevic T, Petry A, etal (2007). "NOX5 variants are functionally active in endothelial cells". *Free Radic. Biol. Med.*. **42** (4): 446–59. [doi:10.1016/j.freeradbiomed.2006.10.054](https://doi.org/10.1016/j.freeradbiomed.2006.10.054). [PMID 17275676](https://pubmed.ncbi.nlm.nih.gov/17275676)
- Tirone F, Cox JA (2007). "NADPH oxidase 5 (NOX5) interacts with and is regulated by calmodulin". *FEBS Lett.*. **581** (6): 1202–8. [Bibcode:2007FEBSL.581.1202T](https://ui.adsabs.harvard.edu/abs/2007FEBSL.581.1202T). [doi:10.1016/j.febslet.2007.02.047](https://doi.org/10.1016/j.febslet.2007.02.047). [PMID 17346712](https://pubmed.ncbi.nlm.nih.gov/17346712)
- Qin F, Simeone M, Patel R (2007). "Inhibition of NADPH oxidase reduces myocardial oxidative stress and apoptosis and improves cardiac function in heart failure after myocardial infarction". *Free Radic. Biol. Med.*. **43** (2): 271–81. [doi:10.1016/j.freeradbiomed.2007.04.021](https://doi.org/10.1016/j.freeradbiomed.2007.04.021). [PMID 17603936](https://pubmed.ncbi.nlm.nih.gov/17603936)

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Adapted from the Wikipedia article [NOX5](https://en.wikipedia.org/wiki/NOX5) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/NOX5?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.