NADPH Oxidase Complex-Derived Reactive Oxygen Species, the Actin Cytoskeleton, and Rho GTPases in Cell Migration

Stanley, Alanna; Thompson, Kerry; Hynes, A. C.; Brakebusch, Cord; Quondamatteo, Fabio

doi:10.1089/ars.2013.5713

Cited by 59 publications

(41 citation statements)

References 135 publications

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“…It is interesting to note that SFB have putative ADP-ribosyl transferases that have sequence similarities to the Clostridium perfringens iota toxin, which ribosylates G-actin and thereby inhibits its polymerization (Pamp et al, 2012). Furthermore, because ROS suppresses the activity of certain Rho GTPase family members (Stanley et al, 2014), ROS produced by the Duox2/Duoxa2 system in ECs may, in addition or instead, affect actin reorganization. In any case, there may be a link between actin cytoskeletal modulation by adherent SFB and subsequent gene induction in ECs, possibly through mechanosensing mechanisms (Dupont et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

Th17 Cell Induction by Adhesion of Microbes to Intestinal Epithelial Cells

Atarashi

Tanoue

Ando

et al. 2015

Cell

872

779

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SUMMARY Intestinal Th17 cells are induced and accumulate in response to colonization with a subgroup of intestinal microbes such as segmented filamentous bacteria (SFB) and certain extracellular pathogens. Here, we show that adhesion of microbes to intestinal epithelial cells (ECs) is a critical cue for Th17 induction. Upon monocolonization of germ-free mice or rats with SFB indigenous to mice (M-SFB) or rats (R-SFB), M-SFB and R-SFB showed host-specific adhesion to small intestinal ECs, accompanied by host-specific induction of Th17 cells. Citrobacter rodentium and Escherichia coli O157 triggered similar Th17 responses, whereas adhesion-defective mutants of these microbes failed to do so. Moreover, a mixture of 20 bacterial strains, which were selected and isolated from fecal samples of a patient with ulcerative colitis on the basis of their ability to cause a robust induction of Th17 cells in the mouse colon, also exhibited EC-adhesive characteristics.

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Section: Discussionmentioning

confidence: 99%

Th17 Cell Induction by Adhesion of Microbes to Intestinal Epithelial Cells

Atarashi

Tanoue

Ando

et al. 2015

Cell

872

779

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“…Reactive oxygen species, in turn, have multiple complex effects on Rho signaling and cytoskeletal structure (83). We propose that alterations to membrane chemical composition may lead to enhanced recruitment of cytoskeletal anchors into the membrane and increased membrane/cytoskeleton attachment and adhesion.…”

Section: Impact Of Oxidized Lipids On Endothelial Membrane Lipid Packmentioning

confidence: 94%

Molecular-Scale Biophysical Modulation of an Endothelial Membrane by Oxidized Phospholipids

Ayee

LeMaster

Shentu

et al. 2017

Biophysical Journal

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The influence of two bioactive oxidized phospholipids on model bilayer properties, membrane packing, and endothelial cell biomechanics was investigated computationally and experimentally. The truncated tail phospholipids, 1-palmitoyl-2-(5-oxovaleroyl)-sn-glycero-3-phosphocholine (POVPC) and 1-palmitoyl-2-glutaroyl-sn-glycero-3-phosphocholine (PGPC), are two major oxidation products of the unsaturated phospholipid 1-palmitoyl-2-arachidonoyl-sn-glycero-phosphocholine. A combination of coarse-grained molecular dynamics simulations, Laurdan multiphoton imaging, and atomic force microscopy microindentation experiments was used to determine the impact of POVPC and PGPC on the structure of a multicomponent phospholipid bilayer and to assess the consequences of their incorporation on membrane packing and endothelial cell stiffness. Molecular simulations predicted differential bilayer perturbation effects of the two oxidized phospholipids based on the chemical identities of their truncated tails, including decreased bilayer packing, decreased bilayer bending modulus, and increased water penetration. Disruption of lipid order was consistent with Laurdan imaging results indicating that POVPC and PGPC decrease the lipid packing of both ordered and disordered membrane domains. Computational predictions of a larger membrane perturbation effect by PGPC correspond to greater stiffness of PGPC-treated endothelial cells observed by measuring cellular elastic moduli using atomic force microscopy. Our results suggest that disruptions in membrane structure by oxidized phospholipids play a role in the regulation of overall endothelial cell stiffness.

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“…NADPH oxidase-generated ROS have been shown to act as a second messenger to regulate migration of metastasis-committed-cancer cells and as a chemoattractant for immune cells during wound healing (Stanley et al, 2014; Hurd et al, 2012). Mediator of ErbB2 driven cell motility (Memo1) has been shown to play an important role in migration of breast cancer cells and is needed for robust metastatic dissemination from primary tumors to lungs (Marone et al, 2004; MacDonald et al., 2014).…”

Section: Introductionmentioning

confidence: 99%

NADPH oxidase-mediated redox signaling promotes oxidative stress resistance and longevity through memo-1 in C. elegans

Ewald

Hourihan

Bland

et al. 2017

eLife

103

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Transient increases in mitochondrially-derived reactive oxygen species (ROS) activate an adaptive stress response to promote longevity. Nicotinamide adenine dinucleotide phosphate (NADPH) oxidases produce ROS locally in response to various stimuli, and thereby regulate many cellular processes, but their role in aging remains unexplored. Here, we identified the C. elegans orthologue of mammalian mediator of ErbB2-driven cell motility, MEMO-1, as a protein that inhibits BLI-3/NADPH oxidase. MEMO-1 is complexed with RHO-1/RhoA/GTPase and loss of memo-1 results in an enhanced interaction of RHO-1 with BLI-3/NADPH oxidase, thereby stimulating ROS production that signal via p38 MAP kinase to the transcription factor SKN-1/NRF1,2,3 to promote stress resistance and longevity. Either loss of memo-1 or increasing BLI-3/NADPH oxidase activity by overexpression is sufficient to increase lifespan. Together, these findings demonstrate that NADPH oxidase-induced redox signaling initiates a transcriptional response that protects the cell and organism, and can promote both stress resistance and longevity.DOI: http://dx.doi.org/10.7554/eLife.19493.001

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NADPH Oxidase Complex-Derived Reactive Oxygen Species, the Actin Cytoskeleton, and Rho GTPases in Cell Migration

Cited by 59 publications

References 135 publications

Th17 Cell Induction by Adhesion of Microbes to Intestinal Epithelial Cells

Th17 Cell Induction by Adhesion of Microbes to Intestinal Epithelial Cells

Molecular-Scale Biophysical Modulation of an Endothelial Membrane by Oxidized Phospholipids

NADPH oxidase-mediated redox signaling promotes oxidative stress resistance and longevity through memo-1 in C. elegans

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