NOX5
NADPH oxidase, EF-hand calcium binding domain 5, also known as NOX5, is a protein which in humans is encoded by the NOX5 gene.[1][2]
Function
Function
NOX5 is a novel NADPH oxidase that generates superoxide.[1]
Nox5 interacts with c-abl, superoxide production leads to phosphorylation of c-abl, while inhibition of c-abl kinase activity inhibits Nox5 superoxide production.[3]
References
References
- ↑ 1.0 1.1 “Entrez Gene: NOX5 NADPH oxidase, EF-hand calcium binding domain 5”.
- ↑ 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. PMID 11483596.
- ↑ 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. PMC 2278123. PMID 18160052.
Further reading
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. PMC 103969. PMID 9882350.
- Cheng G, Cao Z, Xu X, et al. (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.
- Bánfi B, Molnár G, Maturana A, et al. (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. PMID 11483596.
- Armstrong JS, Bivalacqua TJ, Chamulitrat W, et al. (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. PMID 12121572.
- Moskwa P, Dagher MC, Paclet MH, et al. (2002). “Participation of Rac GTPase activating proteins in the deactivation of the phagocytic NADPH oxidase”. Biochemistry. 41 (34): 10710–6. doi:10.1021/bi0257033. PMID 12186557.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). “Complete sequencing and characterization of 21,243 full-length human cDNAs”. Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Bánfi B, Tirone F, Durussel I, et al. (2004). “Mechanism of Ca2+ activation of the NADPH oxidase 5 (NOX5)”. J. Biol. Chem. 279 (18): 18583–91. doi:10.1074/jbc.M310268200. PMID 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. PMC 1955476. PMID 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. PMID 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. PMID 16177112.
- Cucoranu I, Clempus R, Dikalova A, et al. (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. PMID 16179589.
- Kamiguti AS, Serrander L, Lin K, et al. (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. PMID 16339585.
- Fu X, Beer DG, Behar J, et al. (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. PMID 16707484.
- Duerrschmidt N, Stielow C, Muller G, et al. (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. PMC 1890367. PMID 16873416.
- Chenevier-Gobeaux C, Lemarechal H, Bonnefont-Rousselot D, et al. (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. PMID 17122966.
- Jagnandan D, Church JE, Banfi B, et al. (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. PMID 17164239.
- BelAiba RS, Djordjevic T, Petry A, et al. (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. PMID 17275676.
- Tirone F, Cox JA (2007). “NADPH oxidase 5 (NOX5) interacts with and is regulated by calmodulin”. FEBS Lett. 581 (6): 1202–8. doi:10.1016/j.febslet.2007.02.047. PMID 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. PMID 17603936.
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