Quinone-Induced Oxidative Injury to Cells and Tissues

Smith, Martyn T.; Evans, Celia G.; Thor, Hjördis; Orrenius, Sten

doi:10.1016/b978-0-12-642760-8.50009-0

Cited by 64 publications

(36 citation statements)

References 72 publications

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“…Menadione causes necrotic cell death by participating in oxidative cycling, which generates superoxide and more reactive oxygen species by depletion of sulfhydryl groups and by accumulation of toxic intracellular levels of calcium (25). The relative toxicological importance of these processes probably depends on the tissue and local conditions.…”

Section: Induction Of Phase 2 Response By Sulforaphanementioning

confidence: 99%

Powerful and prolonged protection of human retinal pigment epithelial cells, keratinocytes, and mouse leukemia cells against oxidative damage: The indirect antioxidant effects of sulforaphane

Gao

Dinkova‐Kostova

Talalay³

2001

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

182

119

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Section: Induction Of Phase 2 Response By Sulforaphanementioning

confidence: 99%

Powerful and prolonged protection of human retinal pigment epithelial cells, keratinocytes, and mouse leukemia cells against oxidative damage: The indirect antioxidant effects of sulforaphane

Gao

Dinkova‐Kostova

Talalay³

2001

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

182

119

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“…The reason for this is unclear, but may relate to different degrees of membrane stretching and multiple effects of anisotonicity on the cytoskeleton (C. Stournaras, B. Stoll and D. Haussinger, unpublished observation) and hepatocellular metabolism (for a review see [l]). t-Butylhydroperoxide perturbs cellular CaZ+ homeostasis and leads to blebbing of the hepatocyte surface (for a review see [37]). Theoretically enhanced bleb formation, bleb dissociation and rupture in hypertonic perfusions could contribute to increased LDH release (Fig.…”

Section: Cell Volume and Cell Injury During Oxidative Stressmentioning

confidence: 99%

Effect of anisotonic cell‐volume modulation on glutathione‐S‐conjugate release, t‐butylhydroperoxide metabolism and the pentose‐phosphate shunt in perfused rat liver

Saha

Stoll

Läng

et al. 1992

European Journal of Biochemistry

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EJB 92 06351. Addition of 1 -chloro-2,4-dinitrobenzene to isolated perfused rat liver results in the rapid formation of its glutathione-S-conjugate [S-(2,4-dinitrophenyl)glutathione], which is released into both, bile and effluent perfusate. Anisotonic perfusion did not affect total S-conjugate formation, but release of the S-conjugate into the perfusate was increased (decreased) following hypertonic (hypotonic) exposure at the expense of excretion into bile. Stimulation of S-conjugate release into the perfusate following hypertonic exposure paralleled the time course of volume-regulatory net K + uptake.2. Basal steady-state release of oxidized glutathione (GSSG) into bile was 1.30+0.12 nmol . g -i .mi"-' (n = 18) during normotonic (305 mOsmol/l) perfusion and was 3.8 f 0.3 nmol . g ' . min ' in the presence of t-butylhydroperoxide (50 pmol/l). Hypotonic exposure (225 mOsmol/ 1) lowered both, basal and ~butylhydroperoxide(50 pmol/l)-stimulated GSSG release into bile by 35% and 20%, respectively, whereas hypertonic exposure (385 mOsmol/l) increased. Anisotonic exposure was without effect on t-butylhydroperoxide removal by the liver. GSSG release into bile also decreased by 33% upon liver-cell swelling due to addition of glutamine plus glycine (2 mmol/l, each). 3. Hypotonic exposure led to a persistent stimulation 14C02 production from [l-'4C]glucose by about 80%, whereas 14C02 production from [6-'4C]glucose increased by only 10%. Conversely, hypertonic exposure inhibited 14C02 production from [l-'4C]glucose by about 40%, whereas I4CO2 production from [6-i4C]glucose was unaffected. The effect of anisotonicity on 14C02 production from [l-i4C]glucose was also observed in presence of t-butylhydroperoxide (50 pmol/l), which increased I4CO2 production from [I -'4C]glucose by about 40%.4. t-Butylhydroperoxide (50 pmol/l) was without significant effect on volume-regulatory K + fluxes following exposure to hypotonic (225 mOsmol/l) or hypertonic (385 mOsmol/l) perfusate. Lactate dehydrogenase release from perfused rat liver under the influence of t-butylhydroperoxide was increased by hypertonic exposure compared to hypotonic perfusions.5. The data suggest that hypotonic cell swelling stimulates flux through the pentose-phosphate pathway and diminishes loss of GSSG under conditions of mild oxidative stress. Hypotonically swollen cells arc less prone to hydroperoxide-induced lactate dehydrogenase release than hypertonically shrunken cells. Hypertonic cell shrinkage stimulates the excretion of glutathione-S-conjugates into the sinusoidal circulation at the expense of biliary secretion.Liver-cell volume is an important determinant of metabolic liver-cell function, and several known, but mechanistically unclear, hormone and amino acid effects on hepatic metabolism recently found an explanation in hormone-induced and amino-acid-induccd cell-volume changes (for a review see [I] taurocholate is accomplished by an ATP-dependent transport system [3 -51. Glutathione-S-conjugates are also transported by ATP-dependent systems across th...

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“…The influence of hyperoxia on another critical antioxidant defense system, namely, the cellular GSH pool, to our knowledge has not been studied. In the presence of hyperoxia, we expected to find a decrease in the levels of GSH, because reactive oxygen species are known to deplete the GSH pool (20). Surprisingly, we found that hyperoxia increased GSH levels sixfold in P. aeruginosa.…”

mentioning

confidence: 69%

“…In E. coli, denatured proteins are more susceptible to recognition and degradation by ATP-independent, nonlysosomal enzymes (5). Certain critical proteins may be more susceptible to oxidative damage or modification (2,20). In E. coli, hydrogen peroxide oxidized all three methionine residues of ribosomal protein L12 to methionine sulfoxide, thereby converting the active dimer form to the inactive monomer form (2).…”

mentioning

confidence: 99%

Hyperoxia and prolongation of aminoglycoside-induced postantibiotic effect in Pseudomonas aeruginosa: role of reactive oxygen species

Park

Myers

Marzella

1993

Antimicrob Agents Chemother

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Hyperoxia prolongs the postantibiotic effect (PAE) of the aminoglycoside tobramycin in Pseudomonas aeruginosa. We tested the hypothesis that the PAE is prolonged because hyperoxia increases free radical flux while tobramycin inhibits the induction of antioxidant defenses. Exposure ofP. aeruginosa to hyperoxia (100%O 02) for 1 h increased superoxide dismutase, catalase, and glutathione levels. In the presence of tobramycin (1 x the MIC), the induction of antioxidant defenses by hyperoxia was nearly abrogated. Neither preexposure ofP. aeruginosa to hyperoxia nor supplementation with the antioxidants copper(II) (diisopropylsalicylate)2 (superoxide dismutase-like), catalase, or dimethyl sulfoxide abolished prolongation of the PAE of tobramycin induced by hyperoxia.We recently showed that hyperoxia acts in synergy with an aminoglycoside antibiotic to prolong the postantibiotic effect (PAE) of tobramycin against Pseudomonas aeruginosa (18). The PAE describes the period of bacterial growth suppression that results from a brief exposure to an antimicrobial agent (14). For aminoglycosides, the PAE represents the time required for synthesis of new ribosomes (4).Hyperoxia increases the intracellular flux of 02 and other reactive oxygen species (8). In the study described here, we tested the hypothesis that hyperoxia enhances the PAE of tobramycin against P. aeruginosa by increasing the intracel- MIC of tobramycin for P. aeruginosa ATCC 27853 was 0.5 p,g/ml.The antioxidant enzymes and free radical scavengers were used at the highest concentration which did not inhibit bacterial growth, namely, CuDIPS at 1 x 10-4 M, CAT at 4 x 10' M, and DMSO at 0.4 M. The antioxidants were added before exposure to hyperoxia. The PAE was measured as described previously (18).For enymatic and thiol assays, bacteria (final concentration, -10' CFU/ml) were grown for 2 h in a shaking water bath under ambient conditions (21% 02, 37°C, 100 rpm) before a 1-h exposure to hyperoxia and/or tobramycin (lx the MIC). Bacteria were then filtered onto 0.2-,m-pore-size filters, washed, and resuspended in 50 mM phosphate buffer (pH 7.0); filters were removed after vortexing. Bacteria were centrifuged at 10,000 x g for 15 min at 4°C. After decanting and resuspending with 50 mM phosphate buffer (pH 7.0) with 0.1 mM EDTA, bacterial cells were lysed by sonication (model W185 sonifier; Branson, Plainview, N.Y.) at 60 W (45 s, eight times). Membranes were sedimented by centrifugation at 27,500 x g for 30 min.

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Quinone-Induced Oxidative Injury to Cells and Tissues

Cited by 64 publications

References 72 publications

Powerful and prolonged protection of human retinal pigment epithelial cells, keratinocytes, and mouse leukemia cells against oxidative damage: The indirect antioxidant effects of sulforaphane

Powerful and prolonged protection of human retinal pigment epithelial cells, keratinocytes, and mouse leukemia cells against oxidative damage: The indirect antioxidant effects of sulforaphane

Effect of anisotonic cell‐volume modulation on glutathione‐S‐conjugate release, t‐butylhydroperoxide metabolism and the pentose‐phosphate shunt in perfused rat liver

Hyperoxia and prolongation of aminoglycoside-induced postantibiotic effect in Pseudomonas aeruginosa: role of reactive oxygen species

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