NOX5 (original) (raw)

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Protein-coding gene in the species Homo sapiens

NOX5
Identifiers
Aliases	NOX5, NADPH oxidase 5
External IDs	OMIM: 606572; HomoloGene: 41568; GeneCards: NOX5; OMA:NOX5 - orthologs
Gene location (Human)Chr.Chromosome 15 (human)[1]Band15q23Start68,930,525 bp[1]End69,062,762 bp[1]
RNA expression patternBgeeHuman Mouse (ortholog)Top expressed inoocytethymusspleensecondary oocytemuscle tissuetesticleright testisleft testismetanephrosplacentan/aMore reference expression dataBioGPSMore reference expression data
Gene ontologyMolecular function metal ion binding proton channel activity calcium ion binding heme binding oxidoreductase activity flavin adenine dinucleotide binding NADP binding protein binding superoxide-generating NAD(P)H oxidase activity Cellular component integral component of membrane membrane endoplasmic reticulum endoplasmic reticulum membrane plasma membrane NADPH oxidase complex Biological process angiogenesis superoxide anion generation positive regulation of reactive oxygen species metabolic process regulation of fusion of sperm to egg plasma membrane apoptotic process ion transport regulation of proton transport cell population proliferation endothelial cell proliferation cellular response to oxidative stress proton transmembrane transport cytoskeleton-dependent cytokinesis defense response Sources:Amigo / QuickGO
OrthologsSpeciesHuman MouseEntrez79400n/aEnsemblENSG00000255346n/aUniProtQ96PH1n/aRefSeq (mRNA)NM_001184779NM_001184780NM_024505n/aRefSeq (protein)NP_001171708NP_001171709NP_078781n/aLocation (UCSC)Chr 15: 68.93 – 69.06 Mbn/aPubMed search[2]n/a
Wikidata
View/Edit Human

NADPH oxidase, EF-hand calcium binding domain 5, also known as NOX5, is a protein which in humans is encoded by the NOX5 gene.[3][4]

NOX5 is a novel NADPH oxidase that generates superoxide.[3]

Nox5 interacts with c-abl, superoxide production leads to phosphorylation of c-abl, while inhibition of c-abl kinase activity inhibits Nox5 superoxide production.[5]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000255346 – Ensembl, May 2017
2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. ^ a b "Entrez Gene: NOX5 NADPH oxidase, EF-hand calcium binding domain 5".
4. ^ 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.
5. ^ 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.

• 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.
• 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. S2CID 9576123.
• 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.