The effect of age and sex on glutathione reductase and glutathione peroxidase activities and on aerobic glutathione oxidation in rat liver homogenates

Pinto, Ruy E.; Bartley, W.

doi:10.1042/bj1120109

Cited by 349 publications

(133 citation statements)

References 25 publications

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“…1 unit of IDPm activity is defined as the amount of enzyme catalyzing the production of 1 mol of NADPH/min. Activities for manganese superoxide dismutase, mitochondrial glutathione reductase, and mitochondrial glutathione peroxidase were determined by published methods (30,31). Activities for Glu-6-P dehydrogenase and catalase were analyzed by the methods described (22,32).…”

Section: Molecular Cloning and Construction Of Cell Lines-bovinementioning

confidence: 99%

Control of Mitochondrial Redox Balance and Cellular Defense against Oxidative Damage by Mitochondrial NADP+-dependent Isocitrate Dehydrogenase

Jo¹,

Son²,

Koh³

et al. 2001

Journal of Biological Chemistry

496

365

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Mitochondria are the major organelles that produce reactive oxygen species (ROS) and the main target of ROS-induced damage as observed in various pathological states including aging. Production of NADPH required for the regeneration of glutathione in the mitochondria is critical for scavenging mitochondrial ROS through glutathione reductase and peroxidase systems. We investigated the role of mitochondrial NADP ؉ -dependent isocitrate dehydrogenase (IDPm) in controlling the mitochondrial redox balance and subsequent cellular defense against oxidative damage. We demonstrate in this report that IDPm is induced by ROS and that decreased expression of IDPm markedly elevates the ROS generation, DNA fragmentation, lipid peroxidation, and concurrent mitochondrial damage with a significant reduction in ATP level. Conversely, overproduction of IDPm protein efficiently protected the cells from ROS-induced damage. The protective role of IDPm against oxidative damage may be attributed to increased levels of a reducing equivalent, NADPH, needed for regeneration of glutathione in the mitochondria. Our results strongly indicate that IDPm is a major NADPH producer in the mitochondria and thus plays a key role in cellular defense against oxidative stress-induced damage.Cell damage induced by oxidative stress and reactive oxygen species (ROS) 1 has been implicated in several human diseases including aging, alcohol-mediated organ damage, neurodegenerative diseases, many types of cancers, cardiovascular diseases, and UV-mediated skin disorders (1). As one of the major sources of ROS (2), mitochondria are highly susceptible to oxidative damage. ROS can damage mitochondrial enzymes directly (3), and they can cause mutation in mitochondrial DNAs (4). At the same time, ROS can change the mitochondrial transmembrane potential (⌬m), which is indicative of mitochondrial membrane integrity (5) and precedes cell death induced by various toxic compounds and cytokines (6). Recent reports indicate that mitochondrial ROS cause apoptosis (7, 8) by activating various apoptotic effectors such as cytochrome c release, procaspase-2, procaspase-9, procaspase-3, and latent apoptosis-inducing factor, which is released from the mitochondria during apoptosis (9 -11). Another report also suggested that mitochondrial ROS directly caused apoptosis of T cells (12). It was also reported that tumor necrosis factor ␣ causes a rapid production of mitochondrial ROS (13) and that ceramide, an apoptotic stimulus, also plays a crucial role in tumor necrosis factor ␣-induced mitochondrial ROS generation (14). Furthermore, several other investigators demonstrated that ROS are involved in the signaling pathway of certain growth factors (15) and cytokines (16). In addition, mitochondrial ROS, under hypoxic conditions, activate the transcription of the genes for glycolytic enzymes as well as erythropoietin and vascular endothelial growth factor by upregulating a transcriptional factor, hypoxia-inducible factor 1 (17), suggesting that mitochondrial ROS mediate cross-talk b...

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Section: Molecular Cloning and Construction Of Cell Lines-bovinementioning

confidence: 99%

Control of Mitochondrial Redox Balance and Cellular Defense against Oxidative Damage by Mitochondrial NADP+-dependent Isocitrate Dehydrogenase

Jo¹,

Son²,

Koh³

et al. 2001

Journal of Biological Chemistry

496

365

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“…GPx activity was determined by monitoring the NADPH consumption rate at 340 nm (11). Protein concentration was determined by the Bradford assay (1).…”

Section: Enzyme Activitiesmentioning

confidence: 99%

High levels of catalase in sod mutants of Saccharomyces cerevisiae in high aeration conditions

Martins¹,

Manfredini²,

Benfato³

2005

Braz. J. Microbiol.

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Saccharomyces cerevisiae mutants deficient in superoxide dismutase genes (sod1Δ, sod2Δ and sod1Δsod2Δ mutants) in a stationary phase of growth under high aeration conditions were subjected to H2O2 stress. All the mutants were sensitive after H2O2 treatment. Glutathione peroxidase levels were significantly lower in sod1Δ and sod2Δ single mutants than in the wild-type without treatment. After exposure to H2O2 concentrations, glutathione peroxidase levels were increased in sod1Δsod2Δ double mutants and the sod2Δ single mutant, while sod1Δ maintained lower gluthatione peroxidase activities. The sod2Δ mutant demonstrated a similar catalase activity to that of the wild-type without treatment, whilst decreased catalase activity was observed in conditions of low aeration. Untreated sod1Δsod2Δ double mutant cells presented a lower catalase activity. Catalase levels were higher under high aeration conditions than under microaerophilic conditions, including in sod1Δsod2Δ cells that contain less H2O2, since SOD catalyzes the cleavage of superoxide producing H2O2 and oxygen. We suggest that catalase is not essential for sod mutants under normal conditions, but plays an important role in the acquisition of tolerance to oxidative stress induced by high aeration.

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“…Glutathione reductase (GSSG-Red) activity measured by the method of Pinto and Bartley [33] was expressed in nmoles NADPH oxidized per min per mg protein, using a molar extinction coefficient of 6.22 × 10 6 M/cm.…”

Section: Methodsmentioning

confidence: 99%

Study of the cytotoxicity and antioxidant capacity of N/OFQ(1–13)NH2 and its structural analogues

Kirkova

Zamfirova

Leśkiewicz

et al. 2009

Pharmacological Reports

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Abstract:The effect of side-chain shortening of N/OFQ(1-13)NH 2 at position 9 ([Orn 9 ]N/OFQ(1-13)NH 2 , [Dab 9 ]N/OFQ(1-13)NH 2 , [Dap 9 ]N/OFQ(1-13)NH 2 ) was studied regarding potential toxicity and antioxidant capacity. Staurosporine-and H 2 O 2 -induced damage of SH-SY5Y neuroblastoma cells was not changed in the presence of N/OFQ(1-13)NH 2 and [Orn 9 ]N/OFQ(1-13)NH 2 , but was strongly enhanced in the presence of [Dab 9 ]N/OFQ(1-13)NH 2 and [Dap 9 ]N/OFQ(1-13)NH 2 . Moreover, treatment of cells with the latter two analogues alone led to cell injury. Neuropeptide-dependent differences in the viability of SH-SY5Y cells were also observed, i.e., a cytoprotective effect was observed only in the presence of N/OFQ(1-13)NH 2 and [Orn 9 ]N/OFQ(1-13)NH 2 . Compared to [Dab 9 ]N/OFQ(1-13)NH 2 and [Dap 9 ]N/OFQ(1-13)NH 2 , the effects of N/OFQ(1-13)NH 2 and [Orn 9 ]N/OFQ(1-13)NH 2 were more beneficial in systems generating free oxygen radicals (O 2 -and . OH), as well as on the antioxidant status of rat brain and liver. Taken together, our findings show that N/OFQ(1-13)NH 2 and its structural analogue [Orn 9 ]N/OFQ(1-13)NH 2 possess more favorable profiles than the other two nociceptin (N/OFQ) analogues. The present results suggest that shortening of the side-chain of N/OFQ(1-13)NH 2 might increase cell damage and reduce the viability of SH-SY5Y neuroblastoma cells. Moreover, such alterations may lead to changes in free-oxygen generating systems and in antioxidant status in animal tissues.

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The effect of age and sex on glutathione reductase and glutathione peroxidase activities and on aerobic glutathione oxidation in rat liver homogenates

Cited by 349 publications

References 25 publications

Control of Mitochondrial Redox Balance and Cellular Defense against Oxidative Damage by Mitochondrial NADP+-dependent Isocitrate Dehydrogenase

Control of Mitochondrial Redox Balance and Cellular Defense against Oxidative Damage by Mitochondrial NADP+-dependent Isocitrate Dehydrogenase

High levels of catalase in sod mutants of Saccharomyces cerevisiae in high aeration conditions

Study of the cytotoxicity and antioxidant capacity of N/OFQ(1–13)NH2 and its structural analogues

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