NOX5

NOX5
Identifiers
Aliases	NOX5 , NADPH oxidase 5
External IDs	OMIM: 606572 HomoloGene: 41568 GeneCards: NOX5
Gene location (Human)
Chr.	Chromosome 15 (human)
End	69,062,762 bp
RNA expression pattern
	Top expressed in
	oocyte; ; thymus; ; spleen; ; secondary oocyte; ; muscle tissue; ; metanephros; ; placenta; ; renal cortex; ; seminal vesicula; ; mammary gland;
	n/a
	More reference expression data
	More reference expression data
Gene ontology
Molecular 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
Orthologs
	79400
	n/a
	ENSG00000255346
	n/a
	Q96PH1
	n/a
	NM_001184779 ; NM_001184780 ; NM_024505
	n/a
	NP_001171708 ; NP_001171709 ; NP_078781
	n/a
	Wikidata
View/Edit Human

Last updated September 26, 2022

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]

Function

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]

Related Research Articles

Respiratory burst is the rapid release of the reactive oxygen species (ROS), superoxide anion and hydrogen peroxide, from different cell types.

NADPH oxidase is a membrane-bound enzyme complex that faces the extracellular space. It can be found in the plasma membrane as well as in the membranes of phagosomes used by neutrophil white blood cells to engulf microorganisms. Human isoforms of the catalytic component of the complex include NOX1, NOX2, NOX3, NOX4, NOX5, DUOX1, and DUOX2.

Oxidative stress reflects an imbalance between the systemic manifestation of reactive oxygen species (ROS) and a biological system's ability to readily detoxify the reactive intermediates or to repair the resulting damage. Disturbances in the normal redox state of cells can cause toxic effects through the production of peroxides and free radicals that damage all components of the cell, including proteins, lipids, and DNA. Oxidative stress from oxidative metabolism causes base damage, as well as strand breaks in DNA. Base damage is mostly indirect and caused by the ROS generated, e.g., O₂⁻ (superoxide radical), OH (hydroxyl radical) and H₂O₂ (hydrogen peroxide). Further, some reactive oxidative species act as cellular messengers in redox signaling. Thus, oxidative stress can cause disruptions in normal mechanisms of cellular signaling.

NADPH oxidase 2 (Nox2), also known as cytochrome b(558) subunit beta or Cytochrome b-245 heavy chain, is a protein that in humans is encoded by the NOX2 gene. The protein is a superoxide generating enzyme which forms reactive oxygen species (ROS).

Neutrophil cytosol factor 2 is a protein that in humans is encoded by the NCF2 gene.

Neutrophil cytosol factor 1, also known as p47phox, is a protein that in humans is encoded by the NCF1 gene.

NADPH oxidase 1 is an enzyme that in humans is encoded by the NOX1 gene.

NADPH oxidase 4 is an enzyme that in humans is encoded by the NOX4 gene, and is a member of the NOX family of NADPH oxidases.

Cytochrome b-245 light chain is a protein that in humans is encoded by the CYBA gene involved in superoxide production and phagocytosis.

Rac2 is a small signaling G protein, and is a member of the Rac subfamily of the family Rho family of GTPases. It is encoded by the gene RAC2.

Neutrophil cytosol factor 4 is a protein that in humans is encoded by the NCF4 gene.

Tyrosine-protein kinase ABL2 also known as Abelson-related gene (Arg) is an enzyme that in humans is encoded by the ABL2 gene.

Peroxiredoxin-6 is a protein that in humans is encoded by the PRDX6 gene. It is a member of the peroxiredoxin family of antioxidant enzymes.

Dual oxidase 2, also known as DUOX2 or ThOX2, is an enzyme that in humans is encoded by the DUOX2 gene. Dual oxidase is an enzyme that was first identified in the mammalian thyroid gland. In humans, two isoforms are found; hDUOX1 and hDUOX2. The protein location is not exclusive to thyroid tissue; hDUOX1 is prominent in airway epithelial cells and hDUOX2 in the salivary glands and gastrointestinal tract.

Dual oxidase 1, also known as DUOX1 or ThOX1, is an enzyme which in humans is encoded by the DUOX1 gene. DUOX1 was first identified in the mammalian thyroid gland. In humans, two isoforms are found; hDUOX1 and hDUOX2. Human DUOX protein localization is not exclusive to thyroid tissue; hDUOX1 is prominent in airway epithelial cells and hDUOX2 in the salivary glands and gastrointestinal tract.

NADPH oxidase organizer 1 is an enzyme that in humans is encoded by the NOXO1 gene.

NADPH oxidase 3 is an enzyme that in humans is encoded by the NOX3 gene.

NADPH oxidase activator 1 is an enzyme that in humans is encoded by the NOXA1 gene.

NADPH-dependent diflavin oxidoreductase 1 is an enzyme that in humans is encoded by the NDOR1 gene.

Edgar Pick is an Israeli immunologist who is Professor Emeritus of Immunology in the Department of Clinical Microbiology and Immunology at the Sackler Faculty of Medicine at Tel Aviv University, Israel.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000255346 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 "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.

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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000255346 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-3] 1 2 "Entrez Gene: NOX5 NADPH oxidase, EF-hand calcium binding domain 5".

[pmid11483596-4] 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.

[pmid18160052-5] 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.

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NOX5

Contents

Function

Related Research Articles

References

Further reading