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Wikipedia

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.[3][4]

NOX5
Identifiers
AliasesNOX5, NADPH oxidase 5
External IDsOMIM: 606572 HomoloGene: 41568 GeneCards: NOX5
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001184779
NM_001184780
NM_024505

n/a

RefSeq (protein)

NP_001171708
NP_001171709
NP_078781

n/a

Location (UCSC)Chr 15: 68.93 – 69.06 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

Function edit

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]

References edit

  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.

Further reading edit

  • 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.


nox5, nadph, oxidase, hand, calcium, binding, domain, also, known, protein, which, humans, encoded, gene, identifiersaliases, nadph, oxidase, 5external, idsomim, 606572, homologene, 41568, genecards, gene, location, human, chromosome, human, band15q23start68, . 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 NOX5IdentifiersAliasesNOX5 NADPH oxidase 5External IDsOMIM 606572 HomoloGene 41568 GeneCards NOX5Gene location Human Chr Chromosome 15 human 1 Band15q23Start68 930 525 bp 1 End69 062 762 bp 1 RNA expression patternBgeeHumanMouse ortholog Top expressed inoocytethymusspleensecondary oocytemuscle tissuemetanephrosplacentarenal cortexseminal vesiculamammary glandn aMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionmetal 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 activityCellular componentintegral component of membrane membrane endoplasmic reticulum endoplasmic reticulum membrane plasma membrane NADPH oxidase complexBiological processangiogenesis 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 responseSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez79400n 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 aWikidataView Edit HumanFunction editNOX5 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 References edit a b c GRCh38 Ensembl release 89 ENSG00000255346 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine a b Entrez Gene NOX5 NADPH oxidase EF hand calcium binding domain 5 Banfi B Molnar G Maturana A Steger K Hegedus 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 editLachgar 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 Banfi B Molnar 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 Banfi 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 nbsp This article on a gene on human chromosome 15 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title NOX5 amp oldid 1142732012, wikipedia, wiki, book, books, 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