1.6.3.1: NAD(P)H oxidase (H2O2-forming)
This is an abbreviated version!
For detailed information about NAD(P)H oxidase (H2O2-forming), go to the full flat file.
Word Map on EC 1.6.3.1
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1.6.3.1
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endothelial
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neutrophil
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artery
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p22phox
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dismutase
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angiotensin
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cardiovascular
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apocynin
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hypertension
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oxidases
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nicotinamide
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granulomatous
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cardiac
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fibrosis
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aortic
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atherosclerosis
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catalase
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sod
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leukocyte
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monocyte
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chemiluminescence
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tnf
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pkc
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phorbol
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diphenyleneiodonium
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ii-induced
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iodonium
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diphenylene
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myeloperoxidase
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endothelium-dependent
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hypothyroidism
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oxidase-derived
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renin-angiotensin
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fmlp
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dihydroethidium
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losartan
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tempol
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lucigenin
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nitrotyrosine
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peroxynitrite
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microbicidal
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oxidase-dependent
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vsmcs
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flavocytochrome
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rac2
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medicine
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ros-generating
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tiron
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oxidase-mediated
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synthesis
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agriculture
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fmlp-induced
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thyroperoxidase
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industry
- 1.6.3.1
- endothelial
- neutrophil
- artery
- p22phox
- dismutase
- angiotensin
- cardiovascular
- apocynin
- hypertension
- oxidases
- nicotinamide
- granulomatous
- cardiac
- fibrosis
- aortic
- atherosclerosis
- catalase
- sod
- leukocyte
- monocyte
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chemiluminescence
- tnf
- pkc
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phorbol
- diphenyleneiodonium
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ii-induced
- iodonium
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diphenylene
- myeloperoxidase
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endothelium-dependent
- hypothyroidism
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oxidase-derived
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renin-angiotensin
- fmlp
- dihydroethidium
- losartan
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tempol
- lucigenin
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nitrotyrosine
- peroxynitrite
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microbicidal
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oxidase-dependent
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vsmcs
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flavocytochrome
- rac2
- medicine
-
ros-generating
- tiron
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oxidase-mediated
- synthesis
- agriculture
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fmlp-induced
- thyroperoxidase
- industry
Reaction
Synonyms
100787949, 100812342, 100820185, Atrbohc, AtrbohD NADPH oxidase, AtrbohF NADPH oxidase, BLI-3, cytochrome b-245 heavy chain, dual oxidase, Duox, Duox-DuoxA NADPH oxidase, Duox1, Duox2, Glyma.03G236300, Glyma.19G233900, Glyma.20G236200, GLYMA_10G152200, gp91phox, gp91phox/Nox2, KOD1, large NOX, LNOX, NAD(P)H oxidase, NAD(P)H oxidase 4, NADH oxidase, NADPH oxidase, NADPH oxidase 1, NADPH oxidase 2, NADPH oxidase 4, NADPH oxidase 5, NADPH oxidase type 4, NADPH-oxidase, NADPHox, NAPDH oxidase, NM_001184780, NOX, NOX1, Nox2, NOX3, Nox4, NOX4-art, NOX5, p138 thyroid-oxidase, p138tox, p47phox, p67phox, phagocyte NADPH oxidase, phox, RBOH, RBOHB, RbohF, RDH2, RdxA, renal oxidase, renox, Respiratory Burst Oxidase Homolog, respiratory burst oxidase homologue, rth5, SsNOX38, superoxide-generating NADPH oxidase, ThOX, ThOX2, thyroid NADPH oxidase, thyroid oxidase, thyroid oxidase 2, TK0304, TK0828, TK1186, TK1299, TK1481
ECTree
1.6.3.1 NAD(P)H oxidase (H2O2-forming)Advanced search results
results (
results (Activating Compound
Activating Compound on EC 1.6.3.1 - NAD(P)H oxidase (H2O2-forming)
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
11alpha,9alpha-epoxymethanoprostaglandin F 2alpha
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induces the expression of subunits p22phox and gp91phox
2,4,6-trinitrophenyl-bovine serum albumin
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induces reactive oxygen species generation, which occurrs immediately. 2,4,6-Trinitrophenyl-bovine serum albumin but not TG causes extracellular release of superoxide anion/hydrogen peroxide, which is blocked by diphenyleneiodonium, apocynin, and wortmannin. When used together, 2,4,6-trinitrophenyl-bovine serum albumin and thapsigargin evoke the release of leukotriene C4, tumor necrosis factor-alpha, and interleukin-13 as well as reactive oxygen species generation synergistically
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5-cyclopropyl-2-[1-(2-fluoro-benzyl)-1H-pyrazolo[3,4-b] pyridin-3-yl]-pyrimidin-4-ylamine
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i.e. BAY 41-2272. THP-1 cells treated with BAY 41-2272 for 48 h significantly increase the superoxide anion release. BAY 41-2272 increases subunit gp91phox gene expression and causes a significant increase in cGMP and cAMP levels
A23187
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calcium ionophore. HaCaT keratinocytes overexpressing calcium- and arachidonic acid binding proteins S100A8/S100A9 showed enhanced, transient reactive oxygen species generation in response to A23187, as well as nuclear factor kappaB activation and increase in interleukin-8 mRNA levels
apigenin
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apigenin reduces cell viability, and induces apoptotic cell death in a dose-dependent manner. In addition, it evokes a dose-related elevation of intracellular reactive oxygen species level. Treatment with various inhibitors of the NADPH oxidase significantly blunts both the generation of reactive oxygen species and induction of apoptosis induced by apigenin
arachidonic acid
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maximal enzyme activity in the presence of 0.25-0.35 mM, inhibition above
betaPix
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a Rac1 guanine nucleotide exchange factor, appears to be constitutively bound to Nox1 and essential for its activity
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bovine serum albumin
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time-dependent increases in NAD(P)H oxidase activity with bovine serum albumin stimulation that is inhibited in a concentration-dependent manner with the HMG-CoA reductase inhibitor rosuvastatin, or with Rac1 inhibitor NSC23766. Following albumin stimulation, Rac1 translocates to plasma membrane for NAD(P)H oxidase activation
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calyculin
isoform RbohD is directly phosphorylated in vivo. Phophorylation is enhanced in presence of protein phosphatase inhibitor calyculin. Calyculin itself induces reactive oxygen species production and dramatically enhances the ionomycin-induced reactive oxygen species production of isoform RbohD
cytochalasin D
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enhancement of basal and hyperoxia-induced reactive oxygen species formation
doxorubicin
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induction of superoxide production by doxorubicin is much higher in hearts of wild-type mice than in subunit gp91phox knock-out mice
glucose
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oxidative stress and expression of the NADPH oxidase subunit, p22phox, are both increased, superoxide dismutase 1 and 3 expression lowered and endothelial nitric oxide synthase significantly elevated in microvessel endothelial cells treated with 40mM glucose for 72 h compared to low glucose medium. Oxidative stress, p22phox mRNA, endothelial nitric oxide synthase mRNA, and protein are lowered by concurrent incubation with sepiapterin
H2O2
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Nox5 can be upregulated and activated by minute concentrations of hydrogen peroxide
heat shock protein 90
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binding of heat shock protein 90 to the C-terminus of Nox5 appears to stabilize the protein and enhance expression and activity
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HIV regulatory protein Tat
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NADPH oxidase mediates Tat-induced superoxide release in microglia and macrophages
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isoobtusilactone A
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isoobtusilactone A elicits a concentration-dependent growth impediment with IC50 value of 37.5 microM. Treated cells also display transient increase of reactive oxygen species during the earlier stage of the experiment, followed by the disruption of mitochondrial transmembrane potential. The presence of a reactive oxygen species scavenger N-acetyl-L-cysteine and the inhibitor of NADPH oxidase diphenyleneiodonium chloride block reactive oxygen species production and the subsequent apoptotic cell death
latrunculin A
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enhancement of basal and hyperoxia-induced reactive oxygen species formation
lipopolysaccharide
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exposure tolipopolysaccharide leads to the demise of motor neurons in a dose- and time-dependent manner, whereas interneurons are impaired relatively mildly. NADPH oxidase is activated upon lipopolysaccharide challenge, and inhibitor apocynin prevents inflammation-mediated toxicity to motor neurons
NaCl
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salt stress results in activiation of plasma membrane NAD(P)H oxidase. NaCl-induced increase in total Ca2+ is partially abolished by the addition of NAD(P)H oxidase inhibitor diphenyleneiodinium
nitroglycerin
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in vascular smooth muscle cells exposed to nitroglycerin for 6-24 h, NAD(P)H oxidase activity is increased, in spite of isoform nox1 downregulation
p67phox
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activation domain of p67phox triggers FAD reduction by Nox2. P40phox appears to increase oxidase activity in cooperation with p47phox not by inducing translocation to the membrane, but by retaining the oxidase at the phagosome
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paraquat
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paraquat-induced reactive oxygen species production including superoxide anions in BV-2 cells is accompanied by translocation of the p67phox cytosolic subunit of NADPH oxidase to the membrane. Paraquat-induced reactive oxygen species production is inhibited by NADPH oxidase inhibitors, apocynin and diphenylene iodonium. Apocynin and diphenylene iodonium also rescue cells from paraquat-induced toxicity. The inhibitors for protein kinase C delta or extracellular signal-regulated kinases ERK1/2 can partially attenuate paraquat-induced reactive oxygen species production and cell death
phosphatidylinositol 3-phosphate
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subunit p40phox phosphatidylinositol 3-phosphate binding PX domain has phosphatidylinositol 3-phosphate-dependent and -independent functions. Translocation of subunit p67phox requires the PX domain but not 3-phosphoinositide binding. Activation of the oxidase by p40phox, however, requires both phosphatidylinositol 3-phosphate binding and an Src homology 3 domain competent to bind to poly-Pro ligands
platelet-derived growth factor
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increases H2O2 production in NIH-3T3 fibroblasts through NADPH oxidase activation mediated by Gi-protein coupled receptors and c-Src kinase
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Poldip2
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reactive oxygen species production is enhanced by the multifunctional Poldip2, which also interacts with p22phox, presumably at the beginning of the cytosolic C-terminus, upstream of the region dispensable for Nox4 activity
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Rac guanine nucleotide exchange factors
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activate in conjunction with ATP and nucleoside diphosphate kinase
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Rac1
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in addition to cytosolic organizers and activators, Nox1 also requires Rac1 for activity. Rac1 interacts directly with the C-terminus of Nox1, even in the absence of Noxa1. Nox1 is stimulated by constitutively active Rac1 and inhibited by Rac1 knockdown. Rac1 provides a crucial mechanism for activation by agonists, particularly in cells that exclusively express Nox1/Noxo1/Noxal. Rac1 does not activate Nox4 in transfected cells. Rac1 may participate in Nox5 activation
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salbutamol
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salbutamol treatment enhances superoxide anion production in asthma patients through nitric oxide-mediated mechanisms. It exerts beneficial antioxidant effects through activation of catalase and attenuation of lipid peroxidation
sphingosine 1-phosphate
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increases H2O2 production in NIH-3T3 fibroblasts through NADPH oxidase activation mediated by Gi-protein coupled receptors and c-Src kinase
SRC2 protein
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enhances the reactive oxygen species-producing activity of NADPH oxidase RbohF
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thapsigargin
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evokes a robust burst of intracellular reactive oxygen specie, which occurrs with a significant lag tim. When used together, 2,4,6-trinitrophenyl-bovine serum albumin and thapsigargin evoke the release of leukotriene C4, tumor necrosis factor-alpha, and interleukin-13 as well as reactive oxygen species generation synergistically
transforming growth factor-beta
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up-regulates isoform nox4 and increases the levels of Rac1 protein, a known regulator of both isoforms Nox1 and Nox2, in a transforming growth factor-beta receptor I-dependent manner and mediates activation of the nuclear factor-kappaB pathway. The inhibitors diphenyleneiodonium and apocynin, and SB431542, an inhibitor of the transforming growth factor-beta receptor I, block up-regulation of epidermal growth factor receptor ligands and Akt activation
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tumor necrosis factor
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treatment of fibroblasts induces the formation of a signaling complex containing TNF-R1-associated death domain protein TRADD, receptor interacting protein RIP1, NAD(P)H oxidase Nox1, and the small GTPase Rac1. Formation of this complex plays a key role in tumor necrosis factor-induced necrotic cell death
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tumor necrosis factor-alpha
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treatment of monocytic cells and isolated monocytes results in up-regulation of the NAD(P)H oxidase gene, neutrophil cytosolic factor 2. Treated cells have increased levels of mRNA and up-regulated expression of NADPH oxidase subunits p47phox, p67phox, and gp91phox, as well as increased oxidase activity. Pharmacological inhibitors of NF-kappaB activation block tumor necrosis factor-induced up-regulation, which correlates with a reduction in expression of the corresponding oxidase proteins and decreased superoxide anion production
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Urea
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increase of activity by 250% in presence of 1 M urea with no apparent perturbation in enzyme structure. Presence of urea prohibits the closing of the active site thus allowing the substrate to bind
(+)-(S)-2-(6-methoxynaphthalen-2-yl)propanoic acid
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i.e. naproxen, nonsteroidal anti-inflammatory drug. Treatment increases isoform Nox2 expression in endothelial cells and diminishes production of bioactive nitric oxide. In healthy volunteers, treatment reduces nitroglycerin-induced, nitric oxide-mediated vasodilatation of the brachial artery
(+)-(S)-2-(6-methoxynaphthalen-2-yl)propanoic acid
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i.e. naproxen, nonsteroidal anti-inflammatory drug. Marked increase in expression of isoforms Nox1, Nox2, Nox4, and p22phox. Up-regulation of NAD(P)H oxidases is associated with increased superoxide content in aorta and heart, which may be prevented by inhibitor apocynin
2-(2-(2,6-dichlorophenylamino)-phenyl)acetic acid
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i.e. diclofenac, nonsteroidal anti-inflammatory drug. Treatment increases isoform Nox2 expression in endothelial cells and diminishes production of bioactive nitric oxide. In healthy volunteers, treatment reduces nitroglycerin-induced, nitric oxide-mediated vasodilatation of the brachial artery
2-(2-(2,6-dichlorophenylamino)-phenyl)acetic acid
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i.e. diclofenac, nonsteroidal anti-inflammatory drug. Marked increase in expression of isoforms Nox1, Nox2, Nox4, and p22phox. Up-regulation of NAD(P)H oxidases is associated with increased superoxide content in aorta and heart, which may be prevented by inhibitor apocynin
4-(4-methylsulfonylphenyl)-3-phenyl-5H-furan-2-one
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i.e. rofecoxib, nonsteroidal anti-inflammatory drug. Treatment increases isoform Nox2 expression in endothelial cells and diminishes production of bioactive nitric oxide. In healthy volunteers, treatment reduces nitroglycerin-induced, nitric oxide-mediated vasodilatation of the brachial artery
4-(4-methylsulfonylphenyl)-3-phenyl-5H-furan-2-one
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i.e. rofecoxib, nonsteroidal anti-inflammatory drug. Moderate increase in expression of isoforms Nox1, Nox2, Nox4, and p22phox. Up-regulation of NAD(P)H oxidases is associated with increased superoxide content in aorta and heart, which may be prevented by inhibitor apocynin
4-[5-(4-methylphenyl)-3-(trifluoromethyl)pyrazol-1-yl]benzenesulfonamide
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i.e. celecoxib, nonsteroidal anti-inflammatory drug. Treatment increases isoform Nox2 expression in endothelial cells and diminishes production of bioactive nitric oxide. In healthy volunteers, treatment reduces nitroglycerin-induced, nitric oxide-mediated vasodilatation of the brachial artery
4-[5-(4-methylphenyl)-3-(trifluoromethyl)pyrazol-1-yl]benzenesulfonamide
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i.e. celecoxib, nonsteroidal anti-inflammatory drug. Moderate increase in expression of isoforms Nox1, Nox2, Nox4, and p22phox. Up-regulation of NAD(P)H oxidases is associated with increased superoxide content in aorta and heart, which may be prevented by inhibitor apocynin
angiotensin II
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potent stimulator of NAD(P)H oxidase O2- production in the vasculature
angiotensin II
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potent stimulator of NAD(P)H oxidase O2- production in the vasculature
angiotensin II
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potent stimulator of NAD(P)H oxidase O2- production in the vasculature
angiotensin II
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potent stimulator of NAD(P)H oxidase O2- production in the vasculature
formyl-Met-Leu-Phe
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stimulation. In addition, heterologous expression of subunit p40phox markedly enhances superoxide production in stimulated cells. Upon stimulation with phorbol 12-myristate 13-acetate or formyl-Met-Leu-Phe, p40phox translocates to plasma membrane in a p67phox- and p47phox-dependent manner
ionomycin
reactive oxygen species production by isoform RbohD is induced in presence of ionomycin. Ionomycin induces calcium influx into the cell, and following Ca2+ binding to the EF-hand motif of RbohD, conformational changes result in activation
N-formyl-L-methionyl-L-leucyl-L-phenylalanine
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store-operated Ca2+ entry is required at the beginning of NADPH oxidase activation in response to N-formyl-L-methionyl-L-leucyl-L-phenylalanine in neutrophil-like HL-60 cells. When extracellular Ca2+ is initially removed, early addition of Ca2+ after stimulation causes a complete restoration of Ca2+ entry and H2O2production. Both Ca2+ entry and H2O2 production are decreased by purported SOCE blockers, 2-aminoethoxydiphenyl borane (2-APB) and SK&F 96365. Ca2+ influx in HL-60 cells relies on different membrane transient receptor potential canonical channels and Orai1 for allowing NADPH oxidase activation
N-formyl-L-methionyl-L-leucyl-L-phenylalanine
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stimulation. Conditional expression of p21-activated kinase-1 PAK1 dominant-positive mutants enhances, whereas dominant-negative mutants inhibit, NADPH oxidase-mediated superoxide generation stimulated by N-formyl-L-methionyl-L-leucyl-L-phenylalanine. Both Rac1 and the GTP exchange factor VAV1 are required as upstream signaling proteins, and the effect of p21-activated kinase-1 PAK1 on the respiratory burst is mediated through phosphorylation of subunit p47phox
NOXA1
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in contrast to its Noxo1 partner, Noxa1 activity appears to be tightly regulated. Noxa1 contains four Rac-binding TPR motifs, a Nox activation domain and an SH3 domain that interacts with the prolinerich region of an organizer subunit, But the p40phox-binding PB1 domain is not well conserved and the SH3 domain in the middle of the molecule is missing. Phosphorylation of Noxa1 by protein kinase A favors binding to 14-3-3 and dissociation from Nox1, whereas other kinases appear to decrease Noxa1 affinity for Rac1 and Nox1. In contrast, phosphorylation of Noxa1 by Src on tyrosine 110 increases Nox1 activity
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NOXA1
i.e. NOX activator 1 activates, the protein is expressed predominantly in colon elithelium and is thus likely to be a physiologically relevant partner of NOX1
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NOXO1
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In contrast to its Noxo1 partner, Noxa1 activity appears to be tightly regulated. Unlike p47phox, because Noxo1 lacks an autoinhibitory domain, it is thought to constitutively bind the cytochrome, but similar to p47phox, Noxo1 facilitates oxidase assembly by binding both an activator subunit and p22phox. The proline-rich region of Noxo1 binds to an SH3 domain of the activator, whereas the tandem SH3 domains of Noxo1 bind to the proline-rich region of p22phox. Noxo1 also binds to the dehydrogenase domain of Nox1. The PX domain of Noxo1 provides an essential affinity for membrane phosphoinositides
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NOXO1
i.e. NOX organizer 1 activates, the protein is expressed predominantly in colon elithelium and is thus likely to be a physiologically relevant partner of NOX1
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phorbol 12-myristate 13-acetate
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after transfection with calcium- and arachidonic acid binding proteins S100A8/S100A9 genes, HeLa cells show dramatically increased activation of NAD(P)H oxidase in presence of phorbol 12-myristate 13-acetate
phorbol 12-myristate 13-acetate
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stimualtion. Treated dendritic cells are are more competent in killing Candida albicans
phorbol 12-myristate 13-acetate
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stimulation. In addition, heterologous expression of subunit p40phox markedly enhances superoxide production in stimulated cells. Upon stimulation with phorbol 12-myristate 13-acetate or formyl-Met-Leu-Phe, p40phox translocates to plasma membrane in a p67phox- and p47phox-dependent manner
phorbol 12-myristate 13-acetate
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upon treatment, plasma membranes from stimulated cells show an increased amount of regulatory protein Rac1, but other components of the NAD(P)H oxidase complex do not change before and after the stimulation. When the constitutively active form of Rac, Q61L or GTP-bound Rac1 is added exogenously to the membrane, superoxied anion producing activity is enhanced up to 1.5-fold above the basal level,but GDP-loaded Rac1 does not affect superoxide generating kinetics
phorbol 12-myristate 13-acetate
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stimulation. Conditional expression of p21-activated kinase-1 PAK1 dominant-positive mutants enhances, whereas dominant-negative mutants inhibit, NADPH oxidase-mediated superoxide generation stimulated by N-formyl-L-methionyl-L-leucyl-L-phenylalanine
Rac
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small GTPase Rac plays a positive role in isoform Nox3 activation in the presence of subunit p47phox and either subunits p67phox or Noxa1, whereas Rac fails to upregulate Nox3 activity when p47phox is replaced with Noxo1. Expression of constitutively active Rac1 mutant Q61L enhances not only superoxide production but also membrane translocation of p67phox
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Rac
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for the activation of Nox enzymes, cytosolic regulatory components (Rac, p67phox, p47phox, and p40phox) are recruited into the integral membrane protein flavocytochrome b558, consisting of the catalytic subunits gp91phox and p22phox
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thrombin
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administration of thrombin to endothelial cells leads to upregulation of enzyme subunit p22phox accompanied by a delayed increase in generation of reactive oxygen species and enhanced proliferation. Existence of a positive feedback mechanism, whereby reactive oxygen species lead to elevated levels of p22phox and thus, sustained generation of reactive oxygen species as is observed in endothelial dysfunction
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thrombin
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after addition to cell culture, expression of NADPH oxidase subunits p47phox and p67phox occurs, accompanied by up-regulation in the expression of cytosolic enzyme components Rac 1 and p67phox, and the translocation of cytosolic subunits p47phox and p67phox to the membrane. Thrombin-induced reactive oxygen species production, protein oxidation, and loss of cultured hippocampal neurons are partially attenuated by NADPH oxidase inhibition and/or by several antioxidants
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TNF-alpha
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activation of enzyme, resulting in an increase in intracellular H2O2 that stimulates Ca2+ sparks and transient Kca currents, leading to a reduction in global concentration of Ca2+ and vasodilation
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additional information
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upregulated by agents activationg cAMP pathway
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additional information
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presence of Candida albicans does not activate NADPH oxidase in dendritic cells
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additional information
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NADPH oxidase can be activated in a cell-free system by mixing cytosol and plasma membranes isolated from resting neutrophils or macrophages in the presence of Mg2+, GTP and an anionic amphiphile such as arachidonic acid or sodium dodecyl sulfate
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additional information
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activation of NADPH oxidase in phagocytes can be induced by a large number of inflammatory stimuli such as opsonized bacteria, opsonized zymosan, bacterial formylated peptides such as formyl-Met-Leu-Phe, C5a and platelet-activating factor, and also by pharmacological agents such as calcium ionophores A23127, ionomycin and PKC activators such as phorbol myristate acetate. In intact cells, NADPH oxidase activation is accompanied by phosphorylation of enzyme components p47phox, p67phox, p40phox, p22phox and gp91phox, along with several protein-protein interactions. In human neutrophils, various protein kinases have been implicated in the activation of NADPH oxidase, among which the PKC and MAP kinase families appear to play a major role
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additional information
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agonists appear to stimulate Nox1 in specific locations, thus determining where superoxide is produced: extracellularly by muscarinic agonists and thrombin, in endosomes by IL-1beta and TNF-alpha, both inside and outside cells by angiotensin II. Nox activators comprise p67phox and the structurally similar Noxa1. In colon the cytosolic subunits p47phox and p67phox are not expressed and are replaced by Noxo1 and Noxa1. Besides p47phox, other possible organizers include Tks4 and Tks5, two Src substrates with a PX domain and multiple SH3 domains capable of binding p22phox and Noxa1, but not p67phox. Cdc42 cannot activate Nox1
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additional information
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superoxide production is induced by addition of NADPH cytochrome P450 reductase
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additional information
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when luminal NaCl in kidney is switched from 10 to 80 mM, a situation of initiating maximum tubuloglomerular feedback response, superoxide anion production significantly increases. In the presence of apocynin, superoxide anion production is inhibited by 80%
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additional information
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treatment of animals by oral administration of isoobtusilactone A for two weeks does not result in significant difference between control animals and treated animals with respect to the body weight gain, the body weight ratio of liver, spleen and kidney, haematological and clinical chemistry parameters
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additional information
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depolarization of membrane potential of endothelial cells leads to activation of NAD(P)H oxidase and, consequently, superoxide anion production
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additional information
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StCDPK4 and StCDPK5 phosphorylate and activate the plasma membrane NADPH oxidase
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