Protein Kinase C ζ Phosphorylates a Subset of Selective Sites of the NADPH Oxidase Component p47<i>phox</i> and Participates in Formyl Peptide-Mediated Neutrophil Respiratory Burst

Dang, Pham My-Chan; Fontayne, Alexandre; Hakim, Jacques; Benna, Jamel El; Périanin, Axel

doi:10.4049/jimmunol.166.2.1206

Cited by 211 publications

(183 citation statements)

References 66 publications

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“…Transmembrane signaling also leads to phosphorylation of the NADPH oxidase, which is necessary for heightened ROM production (e.g., ref. 18). Superoxide is produced according to the relationship…”

mentioning

confidence: 99%

Apparent role of traveling metabolic waves in oxidant release by living neutrophils

Kindzelskii

Petty

2002

Proc. Natl. Acad. Sci. U.S.A.

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Cell metabolism self-organizes into two types of dissipative structures: chemical oscillations and traveling metabolic waves. In the present study we test the hypothesis that traveling NAD(P)H waves within neutrophils are associated spatially and temporally with the release of reactive oxygen metabolites (ROMs). Using high-speed optical microscopy and taking advantage of the autofluorescence of NAD(P)H, we have observed the propagation of NAD(P)H waves within cells. When NAD(P)H waves reach the lamellipodium of morphologically polarized neutrophils, a diffusing plume of superoxide is released as evidenced by the conversion of hydroethidine in the extracellular environment to ethidium bromide. Parallel results were obtained by using high-speed emission microspectrophotometry. These experiments indicate that the spatial and temporal properties of NAD(P)H waves are transformed into ROM pulses in the extracellular environment. Propagating NAD(P)H waves allow neutrophils to specifically deliver substrate to the lamellipodium at high concentrations, thus facilitating the local and periodic release of ROMs in the direction of cell movement and͞or a target.

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mentioning

confidence: 99%

Apparent role of traveling metabolic waves in oxidant release by living neutrophils

Kindzelskii

Petty

2002

Proc. Natl. Acad. Sci. U.S.A.

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“…3C). These data suggest that a CD95L-induced vesicular acidification largely accounts for the stimulation of ceramide formation by ASM (38), which in turn activates NADPH oxidase through a recently reported protein kinase C-dependent phosphorylation of its activating subunit p47 phox (39). Inhibition of caspase 8 or pan-caspase inhibition, which abolish CD95L-induced endosomal acidification (Table 1), also markedly inhibited the CD95L-induced increase of the intracellular ceramide (Fig.…”

Section: Asm and Caspase 8 Are Required For Cd95 Ligand (Cd95l)-inducmentioning

confidence: 79%

Amplification of CD95 Activation by Caspase 8-induced Endosomal Acidification in Rat Hepatocytes

Reinehr

Sommerfeld

Keitel

et al. 2008

Journal of Biological Chemistry

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Although in rat hepatocytes CD95 is predominantly located inside the cell with almost undetectable immunostaining at the plasma membrane, the addition of CD95-ligand (CD95L) induces hepatocyte apoptosis, which is preceded by a targeting and activation of intracellularly localized CD95 to the plasma membrane including formation of the death-inducing signaling complex. This process involves an NADPH oxidase-dependent generation of reactive oxygen species (ROS) through a ceramide-and protein kinase C-dependent pathway, which leads to an activating phosphorylation of p47 phox . The mechanisms underlying CD95L-induced ceramide formation were addressed in the present study. It was found that CD95L lowered within seconds the apparent vesicular pH from 6.0 to 5.7 in a fluorescein isothiocyanate-dextran-accessible endosomal compartment, which was previously shown to contain acidic sphingomyelinase, and decreased N-(ethoxycarbonylmethyl)-6-methoxyquinolinium bromide fluorescence, suggestive for an increase of cytosolic [Cl ؊ ]. Bafilomycin or 4,4-diisothiocyanostilbene-2,2-disulfonic acid disodium salt largely abolished the CD95L-induced endosomal acidification, ceramide formation, and downstream events, such as p47 phox phosphorylation, ROS formation, CD95 activation, and apoptosis. These responses were also abolished after knock-down of acidic sphingomyelinase in rat hepatocytes. Interestingly, caspase 8 inhibitors abolished these CD95L-induced signaling events, including the increase in cytosolic [Cl ؊ ], endosomal acidification, ceramide formation, and ROS generation as well as CD95 targeting to the plasma membrane and CD95 activation. The data suggest that CD95L initiates a rapid caspase 8-dependent endosomal acidification, which triggers ceramide-dependent ROS formation as an upstream event of trafficking of intracellularly stored CD95 to the plasma membrane. It is concluded that a rapid caspase 8 activation in response to CD95L signals to intracellularly stored CD95, which becomes activated and targeted to the plasma membrane. This autoamplification of CD95-activation is required for apoptosis induction. CD952 (Apo-1/Fas) belongs to the death receptor family and plays an important role in apoptosis induction in many cell types. In hepatocytes, CD95 is mainly located within the cellular interior and can either be activated after ligation with its natural ligand (CD95L) or in a ligand-independent way by hydrophobic bile salts or hyperosmotic cell shrinkage (Refs. 1-4; for review, see Ref. 5). Ligand-dependent and -independent CD95 activation in hepatocytes is a complex process that finally results in CD95 trafficking from the cellular interior to the plasma membrane, subsequent formation of the death-inducing signaling complex (DISC), and eventually apoptosis (1-12).In hepatocytes, proapoptotic stimuli such as CD95 ligand (CD95L), hydrophobic bile salts, or hyperosmotic cell shrinkage induce a rapid oxidative stress (ROS) response (2, 4), which triggers a Yes-dependent but ligand-independent activation of the epiderm...

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“…phox is phosphorylated at multiple serine residues at C-terminus and is targeted by multiple pathways, such as protein kinase C-d, -b and -f, protein kinase A, Akt, ERK1/2, and p38 mitogen-activated protein kinase (62,82,83,87,94,106). The phosphorylation of p47 phox relieves it from auto-inhibitory conformation, which subsequently leads to unmasking of N-terminal SH3 domain and enabling binding to the proline-rich target in the C-terminus of p22 phox .…”

Section: A Nadph Oxidase-derived Ros In Inflammationmentioning

confidence: 99%

Reactive Oxygen Species in Inflammation and Tissue Injury

Mittal

Siddiqui

Tran

et al. 2014

Antioxidants & Redox Signaling

3,440

2,424

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Reactive oxygen species (ROS) are key signaling molecules that play an important role in the progression of inflammatory disorders. An enhanced ROS generation by polymorphonuclear neutrophils (PMNs) at the site of inflammation causes endothelial dysfunction and tissue injury. The vascular endothelium plays an important role in passage of macromolecules and inflammatory cells from the blood to tissue. Under the inflammatory conditions, oxidative stress produced by PMNs leads to the opening of inter-endothelial junctions and promotes the migration of inflammatory cells across the endothelial barrier. The migrated inflammatory cells not only help in the clearance of pathogens and foreign particles but also lead to tissue injury. The current review compiles the past and current research in the area of inflammation with particular emphasis on oxidative stress-mediated signaling mechanisms that are involved in inflammation and tissue injury. Antioxid. Redox Signal. 20, 1126-1167.

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Protein Kinase C ζ Phosphorylates a Subset of Selective Sites of the NADPH Oxidase Component p47phox and Participates in Formyl Peptide-Mediated Neutrophil Respiratory Burst

Cited by 211 publications

References 66 publications

Apparent role of traveling metabolic waves in oxidant release by living neutrophils

Apparent role of traveling metabolic waves in oxidant release by living neutrophils

Amplification of CD95 Activation by Caspase 8-induced Endosomal Acidification in Rat Hepatocytes

Reactive Oxygen Species in Inflammation and Tissue Injury

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