DUOX1-mediated hydrogen peroxide release regulates sodium transport in H441 bronchiolar epithelial cells

2018 ◽  
Vol 225 (1) ◽  
pp. e13166 ◽  
Author(s):  
Frédérique Mies ◽  
Myrna Virreira ◽  
Arnaud Goolaerts ◽  
Sami Djerbib ◽  
Renaud Beauwens ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Epithelial Cells ◽  
Sodium Transport ◽  
Hydrogen Peroxide Release

scholarly journals Iron prochelator BSIH protects retinal pigment epithelial cells against cell death induced by hydrogen peroxide

2008 ◽  
Vol 102 (12) ◽  
pp. 2130-2135 ◽  
Author(s):  
Louise K. Charkoudian ◽  
Tzvete Dentchev ◽  
Nina Lukinova ◽  
Natalie Wolkow ◽  
Joshua L. Dunaief ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Cell Death ◽  
Epithelial Cells ◽  
Retinal Pigment Epithelial ◽  
Retinal Pigment ◽  
Retinal Pigment Epithelial Cells ◽  
Pigment Epithelial ◽  
Pigment Epithelial Cells

EGFR-dependent ERK activation triggers hydrogen peroxide-induced apoptosis in OK renal epithelial cells

2005 ◽  
Vol 80 (6) ◽  
pp. 337-346 ◽  
Author(s):  
Ju Suk Lee ◽  
Su Yung Kim ◽  
Chae Hwa Kwon ◽  
Yong Keun Kim
Keyword(s):  
Hydrogen Peroxide ◽  
Epithelial Cells ◽  
Erk Activation ◽  
Renal Epithelial Cells ◽  
Induced Apoptosis

Hydrogen peroxide promotes transformation of rat liver non-neoplastic epithelial cells through activation of epidermal growth factor receptor

2001 ◽  
Vol 30 (4) ◽  
pp. 209-217 ◽  
Author(s):  
Ruo-Pan Huang ◽  
Ao Peng ◽  
Andre Golard ◽  
Moharmmad Z. Hossain ◽  
Ruochun Huang ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Epithelial Cells ◽  
Rat Liver ◽  
Growth Factor Receptor ◽  
Epidermal Growth ◽  
Neoplastic Epithelial Cells

scholarly journals Physiological levels of formate activate mitochondrial superoxide/hydrogen peroxide release from mouse liver mitochondria

FEBS Letters ◽  
2017 ◽  
Vol 591 (16) ◽  
pp. 2426-2438 ◽  
Author(s):  
Adrian Young ◽  
Danielle Gardiner ◽  
Margaret E. Brosnan ◽  
John T. Brosnan ◽  
Ryan J. Mailloux
Keyword(s):  
Hydrogen Peroxide ◽  
Mouse Liver ◽  
Liver Mitochondria ◽  
Mitochondrial Superoxide ◽  
Hydrogen Peroxide Release

ERK promotes hydrogen peroxide-induced apoptosis through caspase-3 activation and inhibition of Akt in renal epithelial cells

2007 ◽  
Vol 292 (1) ◽  
pp. F440-F447 ◽  
Author(s):  
Shougang Zhuang ◽  
Yan Yan ◽  
Rebecca A. Daubert ◽  
Jiahuai Han ◽  
Rick G. Schnellmann
Keyword(s):  
Hydrogen Peroxide ◽  
Epithelial Cells ◽  
Caspase 3 ◽  
Ischemia Reperfusion ◽  
Nuclear Condensation ◽  
Histone H2b ◽  
Adenoviral Infection ◽  
Akt Phosphorylation ◽  
Renal Proximal Tubular Cells ◽  
Induced Apoptosis

Reactive oxygen species, including hydrogen peroxide (H2O2), are generated during ischemia-reperfusion and are critically involved in acute renal failure. The present studies examined the role of the extracellular signal-regulated kinase (ERK) pathway in H2O2-induced renal proximal tubular cells (RPTC) apoptosis. Exposure of RPTC to 1 mM H2O2resulted in apoptosis and activation of ERK1/2 and Akt. Pretreatment with the specific MEK inhibitors, U0126 and PD98059, or adenoviral infection with a construct that encodes a negative mutant of MEK1, protected cells against H2O2-induced apoptosis. In contrast, expression of constitutively active MEK1 enhanced H2O2-induced apoptosis. H2O2induced activation of caspase-3 and phosphorylation of histone H2B at serine 14, a posttranslational modification required for nuclear condensation, which also were blocked by ERK1/2 inhibition. Furthermore, blockade of ERK1/2 resulted in an increase in Akt phosphorylation and blockade of Akt potentiated apoptosis and diminished the protective effect conferred by ERK inhibition in H2O2-treated cells. Although Z-DEVD-FMK, a caspase-3 inhibitor, was able to inhibit histone H2B phosphorylation and apoptosis, it did not affect ERK1/2 phosphorylation. We suggest that ERK elicits apoptosis in epithelial cells by activating caspase-3 and inhibiting Akt pathways and elicits nuclear condensation through caspase-3 and histone H2B phosophorylation during oxidant injury.

Actin re-distribution in response to hydrogen peroxide in airway epithelial cells

2004 ◽  
Vol 199 (1) ◽  
pp. 57-66 ◽  
Author(s):  
Kendrick C. Boardman ◽  
Ashish M. Aryal ◽  
William M. Miller ◽  
Christopher M. Waters
Keyword(s):  
Hydrogen Peroxide ◽  
Epithelial Cells ◽  
Airway Epithelial Cells ◽  
Airway Epithelial

Aldosterone-stimulated transmethylations are linked to sodium transport

1985 ◽  
Vol 248 (1) ◽  
pp. F43-F47 ◽  
Author(s):  
W. P. Wiesmann ◽  
J. P. Johnson ◽  
G. A. Miura ◽  
P. K. Chaing
Keyword(s):  
Epithelial Cells ◽  
Sodium Transport ◽  
Short Circuit ◽  
Short Circuit Current ◽  
Toad Bladder ◽  
Methylation Inhibitor ◽  
In Cells

The effect of aldosterone (Aldo) on phospholipid (PL) biosynthesis in cultured toad bladder epithelial cells was studied in cells incubated with [1,2-14C]choline and [methyl-3H]methionine over a 5-h period. Aldo (10(-7) M) did not alter the uptake of either precursor but significantly stimulated the incorporation of both labels into phosphatidylcholine (PC), the only PL labeled. 3H labeling of PC increased 29% and 14C incorporation into PC increased 34% in cells exposed to Aldo. A similar 30% increase in protein carboxymethylation occurred in cells treated with Aldo. 3-Deazaadenosine (DZA), a methylation inhibitor, abolished the Aldo-stimulated increase in PC labeling from [3H]methionine. PC labeling from [1,2-14C]choline was not affected by DZA. Basal and Aldo-stimulated protein carboxy-methylation were inhibited by DZA. DZA (300 microM) caused a mild decrease in basal short-circuit current (ISC) but completely inhibited the ISC response to 10(-7) M Aldo. Inhibition was complete when DZA was added up to 2 h following exposure to Aldo, and was reversible. Cells previously exposed to Aldo showed a significant increase in ISC within 2 h following removal of DZA. We conclude that Aldo stimulates PL methylation, protein carboxymethylation, and turnover of PC from choline. Inhibition of methylation reactions coincides with the inhibition of ISC response to Aldo.

scholarly journals Calcium Flashes Orchestrate the Wound Inflammatory Response through DUOX Activation and Hydrogen Peroxide Release

2013 ◽  
Vol 23 (5) ◽  
pp. 424-429 ◽  
Author(s):  
William Razzell ◽  
Iwan Robert Evans ◽  
Paul Martin ◽  
Will Wood
Keyword(s):  
Hydrogen Peroxide ◽  
Inflammatory Response ◽  
Hydrogen Peroxide Release

Decreased Mitochondrial Hydrogen Peroxide Release in Transgenic Drosophila melanogaster Expressing Intramitochondrial Catalase

2000 ◽  
Vol 383 (2) ◽  
pp. 303-308 ◽  
Author(s):  
Linda K. Kwong ◽  
Robin J. Mockett ◽  
Anne-Cécile V. Bayne ◽  
William C. Orr ◽  
Rajindar S. Sohal
Keyword(s):  
Hydrogen Peroxide ◽  
Drosophila Melanogaster ◽  
Hydrogen Peroxide Release ◽  
Transgenic Drosophila
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