The C-terminal flavin domain of gp91phox bound to plasma membranes of granulocyte-like X-CGD PLB-985 cells is sufficient to anchor cytosolic oxidase components and support NADPH oxidase-associated diaphorase activity independent of cytosolic phospholipase A2 regulation

Pessach, Itai M.; Shmelzer, Zeev; Leto, Thomas L.; Dinauer, Mary C.; Lévy, Rachel

doi:10.1189/jlb.1105684

Cited by 4 publications

(5 citation statements)

References 55 publications

(84 reference statements)

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“…2003). A subsequent study showed that the C‐terminal domain of gp91 phox , together with the cytosolic subunits, was sufficient to provide a docking site for the cPLA 2 (Pessach et al. 2006).…”

Section: Cpla2 Is Coupled To Oxidative Pathwaysmentioning

confidence: 99%

The roles of NADPH oxidase and phospholipases A₂ in oxidative and inflammatory responses in neurodegenerative diseases

Sun

Horrocks

Farooqui

2007

Journal of Neurochemistry

127

101

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Reactive oxygen species (ROS) are produced in mammalian cells through enzymic and non-enzymic mechanisms. Although some ROS production pathways are needed for specific physiological functions, excessive production is detrimental and is regarded as the basis of numerous neurodegenerative diseases. Among enzymes producing superoxide anions, NADPH oxidase is widespread in mammalian cells and is an important source of ROS in mediating physiological and pathological processes in the cardiovascular and the CNS. ROS production is linked to the alteration of intracellular calcium homeostasis, activation of Ca 2+ -dependent enzymes, alteration of cytoskeletal proteins, and degradation of membrane glycerophospholipids. There is evolving evidence that ROS produced by NADPH oxidase regulate neuronal functions and degrade membrane phospholipids through activation of phospholipases A 2 (PLA 2 ). This review is intended to cover recent studies describing ROS generation from NADPH oxidase in the CNS and its downstream activation of PLA 2 , namely, the group IV cytosolic cPLA 2 and the group II secretory sPLA 2 . A major focus is to elaborate the dual role of NADPH oxidase and PLA 2 in mediating the oxidative and inflammatory responses in neurodegenerative diseases, including cerebral ischemia and Alzheimer's disease. Elucidation of the signaling pathways linking NADPH oxidase with the multiple forms of PLA 2 will be important in understanding the oxidative and degradative mechanisms that underline neuronal damage and glial activation and will facilitate development of therapeutic intervention for prevention and treatment of these and other neurodegenerative diseases.

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Section: Cpla2 Is Coupled To Oxidative Pathwaysmentioning

confidence: 99%

The roles of NADPH oxidase and phospholipases A₂ in oxidative and inflammatory responses in neurodegenerative diseases

Sun

Horrocks

Farooqui

2007

Journal of Neurochemistry

127

101

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“…Like HL-60 cells, PLB-985 is a bipotential cell line that can be differentiated along the granulocytic pathway with compounds like dimethyl sulfoxide (DMSO) (Tucker et al, 1987), dimethylformamide (DMF) (Katschinski et al, 1999) or dibutyryl cyclic AMP (dbcAMP) (Hazan-Eitan et al, 2006), and toward the monocytic pathway with 1,25-dihydroxy vitamin D3 (Perkins et al, 1991), phorbol myristate acetate (PMA) (Perkins et al, 1991) or interferon-g (Hazan-Eitan et al, 2006). The PLB-985 cell line has been widely utilised to monitor activity of NADPH oxidase and production of reactive oxygen species (ROS) (Boulven et al, 2006;Fay et al, 2006;Pessach et al, 2006;Taylor et al, 2006;van Bruggen et al, 2004), but the other functional responses like degranulation and phagocytosis have been less characterised, or restricted to one type of differentiating agent (Hazan-Eitan et al, 2006;Pedruzzi et al, 2002). A recent paper reported that DMSO-differentiated PLB-985 cells responded like blood neutrophils in terms of inflammatory cytokine production and transcription factor activation, and were readily amenable to transient transfection (Ear and McDonald 2008).…”

Section: Introductionmentioning

confidence: 99%

Characterisation of degranulation and phagocytic capacity of a human neutrophilic cellular model, PLB-985 cells☆

et al. 2010

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“…As well described for Nox2, the diaphorase activity takes place at the cytosolic part of gp91phox [5,6,18,19]. This portion of gp91phox protein possesses specific domains dedicated to the binding of NADPH and FAD which are necessary to initiate the electron transfer.…”

Section: Resultsmentioning

confidence: 88%

“…In an active state, electrons travel from the NADPH to the FAD then through two heme molecules in order to reduce the oxygen leading to the generation of superoxide anion at last [4]. The electronic transfer from the NADPH to the FAD is also called diaphorase activity and has been well described [5,6].…”

Section: Introductionmentioning

confidence: 99%

Recombinant Nox4 cytosolic domain produced by a cell or cell-free base systems exhibits constitutive diaphorase activity

Nguyen¹,

Zhang²,

Lhomme³

et al. 2012

Biochemical and Biophysical Research Communications

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a b s t r a c tThe membrane protein NADPH (nicotinamide adenine dinucleotide phosphate) oxidase Nox4 constitutively generates reactive oxygen species differing from other NADPH oxidases activity, particularly in Nox2 which needs a stimulus to be active. Although the precise mechanism of production of reactive oxygen species by Nox2 is well characterized, the electronic transfer throughout Nox4 remains unclear. Our study aims to investigate the initial electronic transfer step (diaphorase activity) of the cytosolic tail of Nox4. For this purpose, we developed two different approaches to produce soluble and active truncated Nox4 proteins. We synthesized soluble recombinant proteins either by in vitro translation or by bacteria induction. While proteins obtained by bacteria induction demonstrate an activity of 4.4 ± 1.7 nmol/min/ nmol when measured against iodonitro tetrazolium chloride and 20.5 ± 2.8 nmol/min/nmol with cytochrome c, the soluble proteins produced by cell-free expression system exhibit a diaphorase activity with a turn-over of 26 ± 2.6 nmol/min/nmol when measured against iodonitro tetrazolium chloride and 48 ± 20.2 nmol/min/nmol with cytochrome c. Furthermore, the activity of the soluble proteins is constitutive and does not need any stimulus. We also show that the cytosolic tail of the isoform Nox4B lacking the first NADPH binding site is unable to demonstrate any diaphorase activity pointing out the importance of this domain.

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The C-terminal flavin domain of gp91phox bound to plasma membranes of granulocyte-like X-CGD PLB-985 cells is sufficient to anchor cytosolic oxidase components and support NADPH oxidase-associated diaphorase activity independent of cytosolic phospholipase A2 regulation

Cited by 4 publications

References 55 publications

The roles of NADPH oxidase and phospholipases A₂ in oxidative and inflammatory responses in neurodegenerative diseases

The roles of NADPH oxidase and phospholipases A₂ in oxidative and inflammatory responses in neurodegenerative diseases

Characterisation of degranulation and phagocytic capacity of a human neutrophilic cellular model, PLB-985 cells☆

Recombinant Nox4 cytosolic domain produced by a cell or cell-free base systems exhibits constitutive diaphorase activity

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The C-terminal flavin domain of gp91phox bound to plasma membranes of granulocyte-like X-CGD PLB-985 cells is sufficient to anchor cytosolic oxidase components and support NADPH oxidase-associated diaphorase activity independent of cytosolic phospholipase A2 regulation

Cited by 4 publications

References 55 publications

The roles of NADPH oxidase and phospholipases A2 in oxidative and inflammatory responses in neurodegenerative diseases

The roles of NADPH oxidase and phospholipases A2 in oxidative and inflammatory responses in neurodegenerative diseases

Characterisation of degranulation and phagocytic capacity of a human neutrophilic cellular model, PLB-985 cells☆

Recombinant Nox4 cytosolic domain produced by a cell or cell-free base systems exhibits constitutive diaphorase activity

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The roles of NADPH oxidase and phospholipases A₂ in oxidative and inflammatory responses in neurodegenerative diseases

The roles of NADPH oxidase and phospholipases A₂ in oxidative and inflammatory responses in neurodegenerative diseases