New insights into the membrane topology of the phagocyte NADPH oxidase: Characterization of an anti-gp91-phox conformational monoclonal antibody

Campion, Yannick; Paclet, Marie-Hélène; Jesaitis, Algirdas J.; Marques, Bruno; Grichine, Alexeï; Berthier, Sylvie; Lenormand, Jean-Luc; Lardy, Bernard; Stasia, Marie José; Morel, Françoise

doi:10.1016/j.biochi.2007.01.010

Cited by 24 publications

(35 citation statements)

References 33 publications

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“…As shown in Fig. 8A, 1 mM ATP stimulation for 15 min resulted in a 2-3-fold increased expression of endogenous gp91 phox on the cell surface of Ra2 microglia as measured by flow cytometry-based detection of mAb 8G11 binding to an external epitope of gp91 phox (22). Also by time-lapse confocal microscopy of Ra2 cells expressing the CFP-gp91 phox fusion protein, we could observe a translocation of gp91 phox to the cell surface 10 -20 min after ATP stimulation ( Fig.…”

Section: Gtp␥s Stimulation Of Slo-permeabilized Ra2 Microglia Cause Ementioning

confidence: 84%

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NADPH Oxidase Is Internalized by Clathrin-coated Pits and Localizes to a Rab27A/B GTPase-regulated Secretory Compartment in Activated Macrophages

Ejlerskov

Christensen

Beyaie

et al. 2012

Journal of Biological Chemistry

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Background: Subcellular distribution of NADPH oxidase in macrophages is unclear. Results: In mature (activated) macrophages, NADPH oxidase is contained in a storage compartment and is internalized by clathrin-coated pits. Conclusion: NADPH oxidase trafficking is regulated by external factors. Significance: Subcellular localization of NADPH oxidase relates to pathogen eradication, nature, and severity of oxidative tissue stress as well as redox signaling.

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Section: Gtp␥s Stimulation Of Slo-permeabilized Ra2 Microglia Cause Ementioning

confidence: 84%

“…Antibodies used included anti-gp91 phox mAb 54.1 recognizing an intracellular C-terminal epitope (21), mAb 8G11 recognizing an extracellular epitope (22), mAb 7D5 recognizing an extracellular epitope on human gp91…”

Section: Methodsmentioning

confidence: 99%

NADPH Oxidase Is Internalized by Clathrin-coated Pits and Localizes to a Rab27A/B GTPase-regulated Secretory Compartment in Activated Macrophages

Ejlerskov

Christensen

Beyaie

et al. 2012

Journal of Biological Chemistry

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“…As previously reported [35], human neutrophils were isolated from citrated venous blood of healthy volunteers. Blood samples were diluted twice in PBS (137 mM NaCl, 2.7 mM KCl, 1.5 mM KH 2 PO 4 , 8 mM Na 2 HPO 4 pH 7.3) containing 1% (w/v) tri-sodium citrate, using a 33% (v/v) Hypaque-Ficoll gradient.…”

Section: Isolation Of Human Neutrophilsmentioning

confidence: 99%

Quinone compounds regulate the level of ROS production by the NADPH oxidase Nox4

Nguyen

Lardy

Rousset

et al. 2013

Biochemical Pharmacology

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NADPH oxidase Nox4 is expressed in a wide range of tissues and plays a role in cellular signaling by providing reactive oxygen species (ROS) as intracellular messengers. Nox4 oxidase activity is thought to be constitutive and regulated at the transcriptional level; however, we challenge this point of view and suggest that specific quinone derivatives could modulate this activity. In fact, we demonstrated a significant stimulation of Nox4 activity by 4 quinone derivatives (AA-861, tBuBHQ, tBuBQ, and duroquinone) observed in 3 different cellular models, HEK293E, T-REx™, and chondrocyte cell lines. Our results indicate that the effect is specific toward Nox4 versus Nox2. Furthermore, we showed that NAD(P)H:quinone oxidoreductase (NQO1) may participate in this stimulation. Interestingly, Nox4 activity is also stimulated by reducing agents that possibly act by reducing the disulfide bridge (Cys226, Cys270) located in the extracellular E-loop of Nox4. Such model of Nox4 activity regulation could provide new insight into the understanding of the molecular mechanism of the electron transfer through the enzyme, i.e., its potential redox regulation, and could also define new therapeutic targets in diseases in which quinones and Nox4 are implicated

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“…Rabbit anti-p22 phox antiserum (Campion et al, 2007) was a generous gift from Dr. Françoise Morel (GREPI, CNRS, Grenoble, France). Anti-LAMP1 rat monoclonal antibody developed by J. T. August was obtained from the Developmental Studies Hybridoma Bank developed under the auspices of the NICHD and maintained by the University of Iowa (Department of Biological Sciences, Iowa City, IA).…”

Section: Methodsmentioning

confidence: 99%

Neurotoxic Activation of Microglia Is Promoted by a Nox1-Dependent NADPH Oxidase

Chéret¹,

Gervais²,

Lelli³

et al. 2008

J. Neurosci.

202

176

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Reactive oxygen species (ROS) modulate intracellular signaling but are also responsible for neuronal damage in pathological states. Microglia, the resident CNS macrophages, are prominent sources of ROS through expression of the phagocyte oxidase which catalytic subunit Nox2 generates superoxide ion (O 2 ⅐Ϫ ). Here we show that microglia also express Nox1 and other components of nonphagocyte NADPH oxidases, including p22 phox , NOXO1, NOXA1, and Rac1/2. The subcellular distribution and functions of Nox1 were determined by blocking Nox activity with diphenylene iodonium or apocynin, and by silencing the Nox1 gene in microglia purified from wild-type (WT) or Nox2-KO mice. [Nox1-p22 phox ] dimers localized in intracellular compartments are recruited to phagosome membranes during microglial phagocytosis of zymosan, and Nox1 produces O 2 ⅐Ϫ in zymosan-loaded phagosomes. In microglia activated with lipopolysaccharide (LPS), Nox1 produces O 2 ⅐Ϫ , which enhances cell expression of inducible nitric oxide synthase and secretion of interleukin-1␤. Comparisons of microglia purified from WT, Nox2-KO, or Nox1-KO mice indicate that both Nox1 and Nox2 are required to optimize microglial production of nitric oxide. By injecting LPS in the striatum of WT and Nox1-KO mice, we show that Nox1 also enhances microglial production of cytotoxic nitrite species and promotes loss of presynaptic proteins in striatal neurons. These results demonstrate the functional expression of Nox1 in resident CNS phagocytes, which can promote production of neurotoxic compounds during neuroinflammation. Our study also shows that Nox1-and Nox2-dependent oxidases play distinct roles in microglial activation and that Nox1 is a possible target for the treatment of neuroinflammatory states.

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New insights into the membrane topology of the phagocyte NADPH oxidase: Characterization of an anti-gp91-phox conformational monoclonal antibody

Cited by 24 publications

References 33 publications

NADPH Oxidase Is Internalized by Clathrin-coated Pits and Localizes to a Rab27A/B GTPase-regulated Secretory Compartment in Activated Macrophages

NADPH Oxidase Is Internalized by Clathrin-coated Pits and Localizes to a Rab27A/B GTPase-regulated Secretory Compartment in Activated Macrophages

Quinone compounds regulate the level of ROS production by the NADPH oxidase Nox4

Neurotoxic Activation of Microglia Is Promoted by a Nox1-Dependent NADPH Oxidase

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