NADPH oxidase activity is required for endothelial cell proliferation and migration

Abid, M. Ruhul; Kachra, Z.; Spokes, Katherine; Aird, William C.

doi:10.1016/s0014-5793(00)02305-x

Cited by 186 publications

(165 citation statements)

References 41 publications

(45 reference statements)

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“…These results were in agreement with a previous study using three different human endothelial cell lines and showing ROS derived from NAD(P)H oxidase but not eNOS or xanthine oxidase as critical elements in endothelial cell growth [35].…”

Section: Discussionsupporting

confidence: 93%

Nitric oxide synthase and NAD(P)H oxidase modulate coronary endothelial cell growth

Bayraktutan

2004

Journal of Molecular and Cellular Cardiology

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Reactive oxygen species (ROS) including nitric oxide (NO) and superoxide anion (O 2 -) are associated with cell migration, proliferation and many growth-related diseases. The objective of this study was to determine whether there was a reciprocal relationship between rat coronary microvascular endothelial cell (CMEC) growth and activity/expressions (mRNA and protein) of endothelial NO synthase (eNOS) and

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Section: Discussionsupporting

confidence: 93%

Nitric oxide synthase and NAD(P)H oxidase modulate coronary endothelial cell growth

Bayraktutan

2004

Journal of Molecular and Cellular Cardiology

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“…However, the TNF-induced ROS production was significantly reduced by pretreatment with DPI (10 M) an inhibitor of flavincontaining enzymes such as NADPH oxidase (26) or by the NADPH oxidase inhibitor apocynin (10 M) (27,28). Furthermore, in separate experiments, we confirmed the effect of DPI by adding this agent 30 min after TNF.…”

Section: Nadph Oxidase Is the Main Source Of Tnf-induced Ros Productisupporting

confidence: 57%

“…Furthermore, we demonstrate that the NADPH oxidase complex was the main source of ROS in ASM cells under TNF stimulation. Indeed, incubation of ASM cells with two structurally different pharmacological inhibitors of NADPH oxidase (DPI (26) and apocynin (27,28)) significantly reduced TNFinduced ROS production, while the substrate NADPH significantly increased it. Moreover, inhibitors of mitochondrial respiratory chain, NO synthase, cyclooxygenase, and xanthine oxidase had no effect on TNF-induced ROS production.…”

Section: Discussionmentioning

confidence: 99%

Tumor Necrosis Factor-α Increases Airway Smooth Muscle Oxidants Production through a NADPH Oxidase-like System to Enhance Myosin Light Chain Phosphorylation and Contractility

Thabut¹,

El-Benna²,

A³

et al. 2002

Journal of Biological Chemistry

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Tumor necrosis factor plays a critical role in airway smooth muscle hyperresponsiveness observed in asthma. However, the mechanisms underlying this phenomenon are poorly understood. We investigated if tumor necrosis factor-stimulated airway smooth muscle produced reactive oxygen species, leading to muscular hyperresponsiveness. Tumor necrosis factor increased intracellular and extracellular oxidants production in guinea pig airway smooth muscle cells and tissue homogenates. This production was abolished by inhibitors of NADPH oxidase (diphenylene iodinium or apocynin) and was enhanced by NADPH, whereas inhibitors of mitochondrial respiratory chain, nitric-oxide synthase, cyclooxygenase, and xanthine oxidase had no effect. NADPH oxidase subunits p22 Collectively, these results demonstrate that tumor necrosis factor-stimulated airway smooth muscle produces oxidants through a NADPH oxidase-like system, which plays a pivotal role in muscle hyperresponsiveness and myosin light chain phosphorylation.Asthma is a complex inflammatory disease of the lung whose incidence, morbidity, and mortality have dramatically increased worldwide over the last two decades. Airway inflammation and ASM 1 hyperresponsiveness, leading to an increased airway resistance, are characteristic features of asthma (1). The inflammatory response in the asthmatic lung is characterized by an infiltration of the airway wall by mast cells, lymphocytes, and eosinophils. Activation of these cells results in the release of a plethora of inflammatory mediators that individually or in concert induce changes in the airway wall geometry and produce the symptoms of the disease. There is increasing evidence that one of these mediators, the pro-inflammatory cytokine TNF may be one of the primary components responsible for the ASM hyperresponsiveness observed in asthma (see Ref. 2 for review). However, the mechanism of this TNF-induced ASM hyperresponsiveness remains unclear. TNF may act indirectly, via the release of other inflammatory or bronchoconstricting agents such as leukotrienes, by inflammatory cells (2), or directly on ASM cells that express TNF receptors (3). Indeed, different investigators have shown that a short time incubation of tracheal smooth muscle strips with TNF enhances the contractile response to acethylcholine (4, 5) secondary, at least partially, to an increase in MLC phosphorylation (6).This direct effect of TNF on ASM contractility could be mediated by ROS synthesized by the muscular cells. At least three lines of evidence support this hypothesis: 1) TNF leads to the generation of ROS in various cell systems (7,8), 2) incubation of guinea pig tracheal smooth muscle with SOD decreases the contractile response to metacholine (9), suggesting that endogenous ROS can increase ASM contractility, and 3) ROS could increase phosphorylation of the MLC by activating the MLC kinase and/or by inhibiting the MLC phosphatase, as previously described with other kinases/phosphatases systems (10). However, very few studies investigated the capacity of AS...

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“…Using in vitro wound models in cultured airway epithelial systems, DUOX1 was found to play a critical role in cell migration as part of the wound repair response (87,108), illustrating an additional function of DUOX1 in maintenance of epithelial integrity. This is not a unique property of DUOX1, as other NOX isoforms have also been linked to proliferation and/or migration in various other cell types (70,71,116,117), pointing to a possible common mechanism by which NOX/DUOX activation promotes these processes.…”

Section: Functions Of Epithelial Duox: Host Defense and Intracellularmentioning

confidence: 99%

NADPH oxidases in lung biology and pathology: Host defense enzymes, and more

Vliet

2008

Free Radical Biology and Medicine

187

192

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The deliberate production of reactive oxygen species (ROS) by phagocyte NADPH oxidase is widely appreciated as a critical component of antimicrobial host defense. Recently, additional homologs of NADPH oxidase (NOX) have been discovered throughout the animal and plant kingdoms, which appear to possess diverse functions in addition to host defense, including cell proliferation, differentiation, and regulation of gene expression. Several of these NOX homologs are also expressed within the respiratory tract, where they participate in innate host defense as well as in epithelial and inflammatory cell signaling and gene expression, and fibroblast and smooth muscle cell proliferation, in response to bacterial or viral infection and environmental stress. Inappropriate expression or activation of NOX/DUOX during various lung pathologies suggests their specific involvement in respiratory disease. This review summarizes the current state of knowledge regarding the general functional properties of mammalian NOX enzymes, and their specific importance in respiratory tract physiology and pathology.

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NADPH oxidase activity is required for endothelial cell proliferation and migration

Cited by 186 publications

References 41 publications

Nitric oxide synthase and NAD(P)H oxidase modulate coronary endothelial cell growth

Nitric oxide synthase and NAD(P)H oxidase modulate coronary endothelial cell growth

Tumor Necrosis Factor-α Increases Airway Smooth Muscle Oxidants Production through a NADPH Oxidase-like System to Enhance Myosin Light Chain Phosphorylation and Contractility

NADPH oxidases in lung biology and pathology: Host defense enzymes, and more

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