Activation of Dual Oxidases Duox1 and Duox2

Rigutto, Sabrina; Hoste, Candice; Grasberger, Helmut; Milenkovic, Milutin; Communi, David; Dumont, Jacques Emile; Corvilain, Bernard; Miot, Françoise; Deken, Xavier De

doi:10.1074/jbc.m806893200

Cited by 186 publications

(53 citation statements)

References 50 publications

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“…7 It has been reported that H 2 O 2 production increases with increasing DUOX expression at the plasma membrane. 18 A model of bacterial killing at the airway epithelial cells is now considered that is similar to the killing mechanism of the NADPH oxidase in phagocytes. 19 …”

Section: Discussionmentioning

confidence: 99%

Expression of dual oxidases and secreted cytokines in chronic rhinosinusitis

Cho

Nayak

Bravo

et al. 2012

Int Forum Allergy Rhinol

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Background The airway epithelium generates reactive oxygen species (ROS) as a first line of defense. Dual oxidases (DUOX1 and DUOX2) are the H2O2-producing isoforms of the nicotinamide adenine dinucleotide phosphate (NADPH) oxidase family in the airway epithelium. The purpose of this study was to explore the molecular expression, function, and regulation of DUOXs in chronic rhinosinusitis (CRS). Methods Human nasal tissue samples and nasal secretions were collected from 3 groups of patients undergoing sinus surgery (normal, n = 7; CRS with polyposis [CRSwP], n = 6; CRS without polyposis [CRSsP], n = 6). Nasal secretions were studied for cytokine and H2O2 content. Tissue samples were used to determine DUOX mRNA and protein expression. Results DUOX1 mRNA level (80.7 ± 60.5) was significantly increased in CRSwP compared to normal (2.7 ± 1.2) and CRSsP (2.3 ± 0.5, p = 0.042). DUOX2 mRNA levels were increased in both CRSwP (18.6 ± 9.9) and CRSsP (4.0 ± 1.3) compared to normal (1.1 ± 0.3; p = 0.008). DUOX protein was found in the apical portion of the nasal epithelium and protein expression was increased in CRSwP and CRSsP. H2O2 production was significantly higher in CRSwP (160.9 ± 59.4 nM) and CRSsP (81.7 ± 5.6 nM) compared to normal (53.5 ± 11.5 nM, p = 0.032). H2O2 content of nasal secretions correlated tightly with DUOX expression (p < 0.001). Cytokines (eotaxin, monokine-induced by interferon γ [MIG], tumor necrosis factor [TNF]-α, interleukin [IL]-8) showed significantly higher levels in nasal secretions from CRSwP compared to normal (p < 0.05). Levels of eotaxin, MIG, and TNF-α correlated closely with DUOX expression. Conclusion DUOX1 and DUOX2 were identified as factors upregulated in CRS. Close correlations between DUOX expression and H2O2 release, and correlation between key inflammatory cytokines and DUOX expression, indicate DUOX in the inflammatory response in CRS.

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Section: Discussionmentioning

confidence: 99%

Expression of dual oxidases and secreted cytokines in chronic rhinosinusitis

Cho

Nayak

Bravo

et al. 2012

Int Forum Allergy Rhinol

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“…[18] Thei ntracellular loop between transmembrane helix Ia nd II contains two Ca 2+ -binding EF-hand motifs,a nd calcium binding to DUOX2 enhances H 2 O 2 production. [19] TheN OX2-like domain of DUOXs contains one NADPH and one flavine adenine dinucleotide (FAD) binding site,a nd it retains the structural features of phagocyte NOX2 for effective electron transfer from NADPH to FADa sw ell as the Comp.I Ib inding of heme and molecular oxygen. [20] Interestingly,t he generation of H 2 O 2 by Comp.III DUOX2 does not depend on TSH, [21] but decreases as the concentration of iodide increases.…”

Section: Production Of Hydrogen Peroxide By Dual Oxidasesmentioning

confidence: 99%

Chemistry and Biology in the Biosynthesis and Action of Thyroid Hormones

et al. 2016

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Thyroid hormones (THs) are secreted by the thyroid gland. They control lipid, carbohydrate, and protein metabolism, heart rate, neural development, as well as cardiovascular, renal, and brain functions. The thyroid gland mainly produces l-thyroxine (T4) as a prohormone, and 5'-deiodination of T4 by iodothyronine deiodinases generates the nuclear receptor binding hormone T3. In this Review, we discuss the basic aspects of the chemistry and biology as well as recent advances in the biosynthesis of THs in the thyroid gland, plasma transport, and internalization of THs in their target organs, in addition to the deiodination and various other enzyme-mediated metabolic pathways of THs. We also discuss thyroid hormone receptors and their mechanism of action to regulate gene expression, as well as various thyroid-related disorders and the available treatments.

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“…Along the same lines, Laurindo and coworkers provide evidence for a possible regulatory association of Nox1, Nox2, Nox4 and p22 phox with protein disulfide isomerase, a redox chaperone and member of the thioredoxin family [166–168]. Nox5 and Duox enzymes are activated by agonist-induced increases in intracellular calcium in concert with various phosphorylations [169]. Finally, H 2 O 2 is detected as the primary product from Duox1, Duox2 and Nox4 rather than O 2 •− as is the case with the other isoforms.…”

Section: Functional Distinctions Among Nox Isoforms: Heterodimerizmentioning

confidence: 99%

Oxidases and peroxidases in cardiovascular and lung disease: New concepts in reactive oxygen species signaling

Ghouleh

Khoo

Knaus

et al. 2011

Free Radical Biology and Medicine

224

190

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Reactive oxygen species (ROS) are involved in numerous physiological and pathophysiological responses. Increasing evidence implicates ROS as signaling molecules involved in the propagation of cellular pathways. The NADPH oxidase (Nox) family of enzymes is a major source of ROS in the cell and has been related to the progression of many diseases and even in environmental toxicity. The complexity of this family’s effects on cellular processes stems from the fact that there are 7 members, each with unique tissue distribution, cellular localization and expression. Nox proteins also differ in activation mechanisms and the major ROS detected as their product. To add to this complexity, mounting evidence suggests that other cellular oxidases or their products may be involved in Nox regulation. The overall redox and metabolic status of the cell, specifically the mitochondria, also has implications on ROS signaling. Signaling of such molecules as electrophillic fatty acids has impact on many redox sensitive pathologies, and thus, as anti-inflammatory molecules, contributes to the complexity of ROS regulation. The following review is based on the proceedings of a recent international Oxidase Signaling Symposium at the University of Pittsburgh’s Vascular Medicine Institute and Department of Pharmacology and Chemical Biology, and encompasses further interaction and discussion among the presenters.

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Activation of Dual Oxidases Duox1 and Duox2

Cited by 186 publications

References 50 publications

Expression of dual oxidases and secreted cytokines in chronic rhinosinusitis

Expression of dual oxidases and secreted cytokines in chronic rhinosinusitis

Chemistry and Biology in the Biosynthesis and Action of Thyroid Hormones

Oxidases and peroxidases in cardiovascular and lung disease: New concepts in reactive oxygen species signaling

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