Differential susceptibility of fish and rat liver cells to oxidative stress and cytotoxicity upon exposure to prooxidants

Rau, Michelle; Whitaker, Julia; Freedman, Jonathan H.; Giulio, Richard T. Di

doi:10.1016/j.cca.2004.03.001

Cited by 40 publications

(29 citation statements)

References 38 publications

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“…The present results showed that the mechanisms of apoptosis in fish erythrocytes were similar to those in mammal erythrocytes and nucleated cells. It has been demonstrated that the mechanisms of oxidative stress in fish cells are similar to those in mammal cells [31,[39][40][41]. Moreover, as the mammal erythrocytes, fish erythrocytes contain the high concentrations of Hb that transports O 2 and CO 2 for respiration and continuously produce ROS [24,30].…”

Section: • Oh-induced Apoptosis In Fish Erythrocytesmentioning

confidence: 99%

“…Fish erythrocytes could be used as the model in mammal non-nucleated erythrocytes or nucleated cells. As the mammal erythrocytes, fish erythrocytes contain the high Hb concentrations in the cytoplasm, which can continuously produce ROS, and the high PUFAs content in the membrane, which is very sensitive to ROS [30][31][32]. ROS can induce the influx of Ca 2 þ that activates scramblase with subsequent phosphatidylserine (PS) externalization at the cell surface (a biomarker of apoptosis) in mammal erythrocytes [33].…”

Section: Introductionmentioning

confidence: 99%

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The metabolites of glutamine prevent hydroxyl radical-induced apoptosis through inhibiting mitochondria and calcium ion involved pathways in fish erythrocytes

Jiang

Liu

et al. 2016

Free Radical Biology and Medicine

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a b s t r a c tThe present study explored the apoptosis pathways in hydroxyl radicals ( • OH)-induced carp erythrocytes. Carp erythrocytes were treated with the caspase inhibitors in physiological carp saline (PCS) or Ca 2 þ -free PCS in the presence of 40 μM FeSO 4 /20 μM H 2 O 2 . The results showed that the generation of reactive oxygen species (ROS), the release of cytochrome c and DNA fragmentation were caspase-dependent, and Ca 2 þ was involved in calpain activation and phosphatidylserine (PS) exposure in • OH-induced carp erythrocytes. Moreover, the results suggested that caspases were involved in PS exposure, and Ca 2 þ was involved in DNA fragmentation in • OH-induced fish erythrocytes. These results demonstrated that there might be two apoptosis pathways in fish erythrocytes, one is the caspase and cytochrome c-dependent apoptosis that is similar to that in mammal nucleated cells, the other is the Ca 2 þ -involved apoptosis that was similar to that in mammal non-nucleated erythrocytes. So, fish erythrocytes may be used as a model for studying oxidative stress and apoptosis in mammal cells. Furthermore, the present study investigated the effects of glutamine (Gln)'s metabolites [alanine (Ala), citrulline (Cit), proline (Pro) and their combination (Ala 10 Pro 4 Cit 1 )] on the pathways of apoptosis in fish erythrocytes. The results displayed that Ala, Cit, Pro and Ala 10 Pro 4 Cit 1 effectively suppressed ROS generation, cytochrome c release, activation of caspase-3, caspase-8 and caspase-9 at the physiological concentrations, prevented Ca 2 þ influx, calpain activation, PS exposure, DNA fragmentation and the degradation of the cytoskeleton and oxidation of membrane and hemoglobin (Hb) and increased activity of anti-hydroxyl radical (AHR) in • OH-induced carp erythrocytes. Ala 10 Pro 4 Cit 1 produced a synergistic effect of inhibited oxidative stress and apoptosis in fish erythrocytes. These results demonstrated that Ala, Cit, Pro and their combination can protect mammal erythrocytes and nucleated cells against oxidative stress and apoptosis. The studies supported the use of Gln, Ala, Cit and Pro as oxidative stress and apoptosis inhibitors in mammal cells and the hypothesis that the inhibited effects of Gln on oxidative stress and apoptosis are at least partly dependent on that of its metabolites in mammalian.

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Section: • Oh-induced Apoptosis In Fish Erythrocytesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The metabolites of glutamine prevent hydroxyl radical-induced apoptosis through inhibiting mitochondria and calcium ion involved pathways in fish erythrocytes

Jiang

Liu

et al. 2016

Free Radical Biology and Medicine

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“…Workers in eukaryotic systems have reported that copper stress elicits markers of oxidative damage, including DNA damage (39)(40)(41)(42). Speculation as to the basis of this phenomenon has centered on the possibility that copper generates hydroxyl radicals by participating in Fentonlike chemistry, after the fashion of iron.…”

Section: Mechanisms Of Protection: Compartmentalization or Chelation?mentioning

confidence: 99%

The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity

Macomber

Imlay²

2009

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

961

908

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Excess copper is poisonous to all forms of life, and copper overloading is responsible for several human pathologic processes. The primary mechanisms of toxicity are unknown. In this study, mutants of Escherichia coli that lack copper homeostatic systems (copA cueO cus) were used to identify intracellular targets and to test the hypothesis that toxicity involves the action of reactive oxygen species. Low micromolar levels of copper were sufficient to inhibit the growth of both WT and mutant strains. The addition of branched-chain amino acids restored growth, indicating that copper blocks their biosynthesis. Indeed, copper treatment rapidly inactivated isopropylmalate dehydratase, an iron-sulfur cluster enzyme in this pathway. Other enzymes in this iron-sulfur dehydratase family were similarly affected. Inactivation did not require oxygen, in vivo or with purified enzyme. Damage occurred concomitant with the displacement of iron atoms from the solventexposed cluster, suggesting that Cu(I) damages these proteins by liganding to the coordinating sulfur atoms. Copper efflux by dedicated export systems, chelation by glutathione, and cluster repair by assembly systems all enhance the resistance of cells to this metal.copA ͉ Escherichia coli ͉ glutathione ͉ hydrogen peroxide ͉ Suf

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“…In studies of eukaryotic cells treated with excess copper, workers detected elevated levels of DNA lesions, protein oxidation, lipid peroxidation, and reactive oxygen species generation (3,36,53,55,59). In vitro studies showed that copper is capable of generating hydroxyl radicals from H 2 O 2 and thereby facilitates oxidative DNA damage (26):…”

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confidence: 99%

Intracellular Copper Does Not Catalyze the Formation of Oxidative DNA Damage in Escherichia coli

2007

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Because copper catalyzes the conversion of H2O2 to hydroxyl radicals in vitro, it has been proposed that oxidative DNA damage may be an important component of copper toxicity. Elimination of the copper export genes, copA, cueO, and cusCFBA, rendered Escherichia coli sensitive to growth inhibition by copper and provided forcing circumstances in which this hypothesis could be tested. When the cells were grown in medium supplemented with copper, the intracellular copper content increased 20-fold. However, the copper-loaded mutants were actually less sensitive to killing by H2O2 than cells grown without copper supplementation. The kinetics of cell death showed that excessive intracellular copper eliminated iron-mediated oxidative killing without contributing a copper-mediated component. Measurements of mutagenesis and quantitative PCR analysis confirmed that copper decreased the rate at which H2O2 damaged DNA. Electron paramagnetic resonance (EPR) spin trapping showed that the copper-dependent H2O2 resistance was not caused by inhibition of the Fenton reaction, for copper-supplemented cells exhibited substantial hydroxyl radical formation. However, copper EPR spectroscopy suggested that the majority of H2O2-oxidizable copper is located in the periplasm; therefore, most of the copper-mediated hydroxyl radical formation occurs in this compartment and away from the DNA. Indeed, while E. coli responds to H2O2 stress by inducing iron sequestration proteins, H2O2-stressed cells do not induce proteins that control copper levels. These observations do not explain how copper suppresses iron-mediated damage. However, it is clear that copper does not catalyze significant oxidative DNA damage in vivo; therefore, copper toxicity must occur by a different mechanism.

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Differential susceptibility of fish and rat liver cells to oxidative stress and cytotoxicity upon exposure to prooxidants

Cited by 40 publications

References 38 publications

The metabolites of glutamine prevent hydroxyl radical-induced apoptosis through inhibiting mitochondria and calcium ion involved pathways in fish erythrocytes

The metabolites of glutamine prevent hydroxyl radical-induced apoptosis through inhibiting mitochondria and calcium ion involved pathways in fish erythrocytes

The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity

Intracellular Copper Does Not Catalyze the Formation of Oxidative DNA Damage in Escherichia coli

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