Reactivity of 2?,7?-dichlorodihydrofluorescein and dihydrorhodamine 123 and their oxidized forms toward carbonate, nitrogen dioxide, and hydroxyl radicals

Wrona, Marta; Patel, Kantilal B.; Wardman, Peter

doi:10.1016/j.freeradbiomed.2004.10.022

Cited by 177 publications

(142 citation statements)

References 43 publications

Supporting

Mentioning

133

Contrasting

Unclassified

Order By: Relevance

“…After a 10-min incubation at the ambient temperature, the fluorescence intensity of the oxidation product (rhodamine 123) was measured. H 2 R 123 is known to be oxidized to the fluorescent compound rhodamine 123 by hydrogen peroxide and organic peroxides in reactions catalyzed by peroxidases or ferric ions, but also by a range of other oxidants [20,21]. Though the identification of specific oxidants of H 2 R 123 in a cell is not easy, the rate of oxidation is usually assumed to reflect the overall level of the reactive oxygen species.…”

Section: Resultsmentioning

confidence: 99%

The effect of growth medium on the antioxidant defense of Saccharomyces cerevisiae

Macierzyńska

Grzelak

Bartosz

2007

Cellular and Molecular Biology Letters

View full text Add to dashboard Cite

Abbreviations used: DTNB -5,5'-dithiobis-(2-nitrobenzoic acid); H 2 R 123 -dihydrorhodamine 123; MES -2-morpholinoethanesulfonic acid; ROS -reactive oxygen species; SOD -superoxide dismutase; YPD medium -1% yeast extract, 1% Bacto-peptone, 2% glucose, YPG medium, 1% yeast extract, 1% Bacto-peptone,2% glycerol; YPE medium -1% yeast extract, 1% Bacto-peptone, 3% ethanol Abstract: We compared the oxidation of dihydrorhodamine 123, glutathione contents and activities of superoxide dismutase (SOD) and catalase for three wild-type strains of Saccharomyces cerevisiae grown on media with different carbon sources. The rate of oxidation of dihydrorhodamine 123 was much higher in respiring cells grown on ethanol or glycerol media than in fermenting cells grown on glucose medium. The total SOD activity was highest on glycerol medium and lowest on ethanol medium, while the catalase activity was highest on glycerol medium. The sequence of glutathione content values was: glucose > ethanol > glycerol.

show abstract

Section: Resultsmentioning

confidence: 99%

The effect of growth medium on the antioxidant defense of Saccharomyces cerevisiae

Macierzyńska

Grzelak

Bartosz

2007

Cellular and Molecular Biology Letters

View full text Add to dashboard Cite

show abstract

“…Intracellular level of reactive oxygen species (ROS) was determined using the redox-sensitive probes DCFH-DA in conjunction with fluorescent microscopy (41,44,46). Briefly, neutrophils (2.5 ϫ 10 6 /well) were incubated with DCFH-DA (10 M) in a four-well chambered coverglass (Nalge, Naperville, IL) Fig.…”

Section: Methodsmentioning

confidence: 99%

Differential activation of RAGE by HMGB1 modulates neutrophil-associated NADPH oxidase activity and bacterial killing

Tadié

Bae

Banerjee

et al. 2012

American Journal of Physiology-Cell Physiology

View full text Add to dashboard Cite

The receptor for advanced glycation end products (RAGE) plays an important role in host defense against bacterial infection. In the present experiments, we investigated the mechanisms by which RAGE contributes to the ability of neutrophils to eradicate bacteria. Wild-type (RAGE ϩ/ϩ ) neutrophils demonstrated significantly greater ability to kill Eschericia coli compared with RAGE Ϫ/Ϫ neutrophils. After intraperitoneal injection of E. coli, increased numbers of bacteria were found in the peritoneal fluid from RAGE Ϫ/Ϫ as compared with RAGE ϩ/ϩ mice. Exposure of neutrophils to the protypical RAGE ligand AGE resulted in activation of nicotinamide adenine dinucleotide phosphate (NA-DPH) oxidase and enhanced killing of E. coli, and intraperitoneal injection of AGE enhanced bacterial clearance during peritonitis. However, incubation of neutrophils with high mobility group box 1 protein (HMGB1), which also binds to RAGE, diminished E. coliinduced activation of NADPH oxidase in neutrophils and bacterial killing both in vitro and in vivo. Deletion of the COOH-terminal tail of HMGB1, a region necessary for binding to RAGE, abrogated the ability of HMGB1 to inhibit bacterial killing. Incubation of neutrophils with HMGB1 diminished bacterial or AGE-dependent activation of NADPH oxidase. The increase in phosphorylation of the p40 phox subunit of NADPH oxidase that occurred after culture of neutrophils with E. coli was inhibited by exposure of the cells to HMGB1. These results showing that HMGB1, through RAGE-dependent mechanisms, diminishes bacterial killing by neutrophils as well as NADPH oxidase activation provide a novel mechanism by which HMGB1 can potentiate sepsis-associated organ dysfunction and mortality.receptor for advanced glycation end products; nicotinamide adenine dinucleotide phosphate oxidase; peritonitis; sepsis; inflammation; Eschericia coli NEUTROPHILS play central roles in acute inflammatory and innate immune responses through producing anti-bacterial peptides, cytokines, and other proinflammatory mediators, including reactive oxygen intermediates, and contributing to the formation of extracellular traps (8,22,33). Nicotinamide adenine dinucleotide phosphate (NADPH) oxidase, a high-output, superoxide-generating system, is an important source of the reactive oxygen intermediates produced by activated neutrophils. Deficiency in NADPH oxidase is associated with diminished ability of neutrophils to effectively kill bacteria. There is increased susceptibility to infection with Staphylococci and other extracellular bacteria in patients with chronic granulomatous disease, a condition associated with a hereditary defect of NADPH oxidase (14,15,17,18).The receptor for advanced glycation end products (RAGE) recognizes a diverse spectrum of ligands, including nonenzymatically modified glycoproteins such as advanced glycation end products (AGE) (31, 32), as well as high mobility group box 1 protein (HMGB1) and calgranulin (calcium binding cellular factors, S100B) (19,20). Cellular activation through RAGE engagement i...

show abstract

“…Figures 1B and 1C). The DCFH-DA probe is not a specific indicator of H 2 O 2 because it is oxidized by reactive nitrogen species and hydroxyl radical (39,40). Because ATZ inhibits catalase but not other enzymes involved in H 2 O 2 removal, the observed increase in DCF fluorescence in ATZ-treated neutrophils is likely to reflect elevated intracellular H 2 O 2 concentrations.…”

Section: Catalase Inhibition Increases Intracellular Levels Of H 2 O mentioning

confidence: 99%

Antiinflammatory Effects of Hydrogen Peroxide in Neutrophil Activation and Acute Lung Injury

Żmijewski¹,

Lorne²,

Zhao³

et al. 2009

Am J Respir Crit Care Med

View full text Add to dashboard Cite

Rationale: Although reactive oxygen species (ROS) are generally considered to be proinflammatory and to contribute to cellular and organ dysfunction when present in excessive amounts, there is evidence that specific ROS, particularly hydrogen peroxide (H 2 O 2 ), may have antiinflammatory properties. Objectives: To address the role that increases in intracellular H 2 O 2 may play in acute inflammatory processes, we examined the effects of catalase inhibition or the absence of catalase on LPS-induced inflammatory responses. Methods: Neutrophils from control or acatalasemic mice, or control neutrophils incubated with the catalase inhibitor aminotriazole, were treated with LPS, and levels of reactive oxygen species, proteasomal activity, NF-kB activation, and proinflammatory cytokine expression were measured. Acute lung injury (ALI) was produced by intratracheal injection of LPS into control, acatalasemic-, or aminotriazole-treated mice. Measurements and Main Results: Intracellular levels of H 2 O 2 were increased in acatalasemic neutrophils and in neutrophils exposed to aminotriazole. Compared with LPS-stimulated neutrophils from control mice, neutrophils from acatalasemic mice or neutrophils treated with aminotriazole demonstrated reduced 20S and 26S proteasomal activity, IkB-a degradation, NF-kB nuclear accumulation, and production of the proinflammatory cytokines TNF-a and macrophage inhibitory protein (MIP)-2. The severity of LPS-induced ALI was less in acatalasemic mice and in mice treated with aminotriazole as compared with that found in control mice. Conclusions: These results indicate that H 2 O 2 has antiinflammatory effects on neutrophil activation and inflammatory processes, such as ALI, in which activated neutrophils play a major role.

show abstract

Reactivity of 2?,7?-dichlorodihydrofluorescein and dihydrorhodamine 123 and their oxidized forms toward carbonate, nitrogen dioxide, and hydroxyl radicals

Cited by 177 publications

References 43 publications

The effect of growth medium on the antioxidant defense of Saccharomyces cerevisiae

The effect of growth medium on the antioxidant defense of Saccharomyces cerevisiae

Differential activation of RAGE by HMGB1 modulates neutrophil-associated NADPH oxidase activity and bacterial killing

Antiinflammatory Effects of Hydrogen Peroxide in Neutrophil Activation and Acute Lung Injury

Contact Info

Product

Resources

About