Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P30044 (antioxidant enzyme)
 8,037 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Injury to the gastrointestinal tract by oxygen dependent processes is important in ischemia, inflammatory bowel disease, and necrotizing enterocolitis. The Caco-2 cell line is an important tool in assessing various gastrointestinal functions and offers a unique opportunity to assess gastrointestinal oxidant metabolism on a cellular level. However, some Caco-2 cell functions change with time after confluence. To determine if antioxidant enzyme activity changes during differentiation, Caco-2 cells were grown to confluence, and superoxide dismutase, glutathione peroxidase, glutathione reductase, and catalase activities and specific mRNA content were quantitated. With time after confluence the enzymes demonstrated a small, but statistically significant increase in activity. Neither superoxide dismutase nor glutathione peroxidase mRNA levels correlated with enzyme activity changes. Catalase mRNA levels increased as catalase activity increased. Thus, differentiated Caco-2 cells express superoxide dismutase, glutathione peroxidase, glutathione reductase, and catalase activities and the superoxide dismutase, glutathione peroxidase, and catalase genes. Superoxide dismutase activity and glutathione peroxidase activity do not correlate with mRNA levels, and suggest that regulation may be at a level other than transcription. The correlation between catalase activity and catalase mRNA suggests differentiation may occur at transcription. If Caco-2 cells are used to elucidate oxidative metabolism, changes in activities of antioxidant enzymes as a function of cell differentiation should be considered.
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PMID:Antioxidant enzymes in the differentiated Caco-2 cell line. 142 66

Forty-three twin lamb fetuses of 121 +/- 1 d gestation were catheterized and received i.v. saline (n = 8), 0.75 mg/kg/h cortisol for 60 h (n = 15), 5 micrograms/kg thyrotropin-releasing hormone (TRH) every 12 h for five doses (n = 9), or cortisol and TRH (n = 11) before delivery at 128 +/- 1 d. After delivery, the lambs were randomized for natural sheep surfactant treatment or sham treatment, ventilated for 75 min, and killed. Superoxide dismutase, catalase, and glutathione peroxidase activities were measured in fetal lung tissue. Superoxide dismutase and catalase activities were increased in both the corticosteroid (p less than 0.001) and the corticosteroid with TRH (p less than 0.01) groups. Glutathione peroxidase activity was higher after prenatal corticosteroid treatment, but statistical significance was not reached (p = 0.06). Although prenatal exposure to corticosteroids increased superoxide dismutase, catalase, and glutathione peroxidase activities, TRH alone or TRH added to corticosteroids provided no additional benefit. Lambs treated with surfactant had higher lung catalase activities than lambs that did not receive surfactant, probably secondary to the presence of catalase activity in the surfactant preparation. Increased pulmonary antioxidant enzyme activity may be an additional feature of the overall beneficial effect of corticosteroids on fetal lung development.
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PMID:Corticosteroids, thyrotropin-releasing hormone, and antioxidant enzymes in preterm lamb lungs. 180 46

Buthionine sulfoximine (BSO), an inhibitor of de novo synthesis of glutathione (GSH), was used to deplete rats of GSH and determine the effect of treatment on antioxidant enzyme responses, lung injury, and the susceptibility to concurrent sublethal or lethal hyperoxia. In a preliminary experiment, total lung nonprotein sulfhydryl (NPSH) and GSH levels were measured at various times after single doses of BSO. The lowest concentrations were observed at 12 to 18 h. These experiments were used to establish a repeated dosing protocol for more prolonged GSH depletion. The lungs of rats treated with BSO for 4 days demonstrated markedly decreased GSH and NPSH levels (10 to 40% of control values) and glutathione peroxidase activity (45 to 60% of control values). Superoxide dismutase activities were elevated, glutathione reductase activity was slightly elevated, and catalase activity was unchanged. These changes were dose-responsive. The lungs of treated rats were grossly and microscopically normal. BSO treatment of additional rats did not increase susceptibility to lethal hyperoxia (greater than 98% oxygen). Combined treatment of rats with both BSO and sublethal hyperoxia (80% oxygen) for 4 days did not alter the biochemical responses demonstrated by rats treated solely with BSO. The marked increase in catalase activity obtained after hyperoxia alone was not observed in rats treated with both hyperoxia and BSO. The lungs of saline- and BSO-treated rats exposed to sublethal hyperoxia demonstrated a patchy distribution of slight perivascular and peribronchiolar edema.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:The pulmonary effects of buthionine sulfoximine treatment and glutathione depletion in rats. 320 1

Fetal rat lung fibroblasts were cultured in a gas phase of 20% O2, 5% CO2 (PO2 measured, 150 Torr) or 2% oxygen, 5% CO2 (PO2 measured, 25 Torr) with or without 100 nM dexamethasone (Dex). Superoxide dismutase (SOD) activity per cell increased spontaneously during 4 days of incubation at both PO2, but catalase (CAT) activity tended to fall during this time and glutathione peroxidase (GPx) activity showed no consistent trend during this interval. Cells cultured at a low PO2 had a lower protein content and SOD activity compared with air controls. Dex inhibited cell proliferation and enhanced intracellular accumulation of protein at the low PO2 but prevented the increase in protein content without affecting cell multiplication at a PO2 of 150 Torr. SOD activity per cell was enhanced by Dex at a low PO2 but reduced in 20% O2, 5% CO2. An increase in CAT and GPx activity per cell resulted on exposing fibroblasts to Dex in the presence of low PO2. These results show that Dex affects the growth and antioxidant enzyme activity of fetal lung fibroblasts, and this action of Dex can be modulated by changing the ambient PO2.
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PMID:PO2-dexamethasone interactions in fibroblast growth and antioxidant enzyme activity. 356 58

It has recently been determined that fetal lung antioxidant enzyme activity markedly increases late in gestation. A test was made of whether this normal late-in-gestation change in O2-protective enzymes would be responsive to the maturing effect of hormonal (glucocorticoid) treatment. Pregnant rats received 0.2 mg/kg of dexamethasone (or saline) at 48 and 24 hours prior to delivery of their fetuses on gestational days 19, 20, 21, and 22 (newborn). Lung disaturated phosphatidylcholine showed an expected response to prenatal dexamethasone exposure with significant elevations of surfactant lipid at gestational days 20 and 21. A similar effect of prenatal dexamethasone treatment on the lung antioxidant defensive system was found. Superoxide dismutase, catalase, and glutathione peroxidase--enzymes protective against hyperoxia-induced lung injury--showed an accelerated pattern of maturation with significant increases in the dexamethasone-treated fetal lungs compared with control fetal lung enzyme levels at gestational days 20 and 21. The results suggest that prenatal dexamethasone treatment may have dual benefits when used in impending premature deliveries--that is, it may stimulate maturation of both the surfactant system and also the antioxidant enzyme system, and this maturation can help protect the premature newborn's lungs from the toxic complications of hyperoxic therapy that may be required because of immaturity.
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PMID:Dexamethasone stimulation of fetal rat lung antioxidant enzyme activity in parallel with surfactant stimulation. 384 97

Current evidence suggests that bleomycin toxicity may be attributable to its DNA degradative activity possibly via generation of free radicals and O2 metabolites as mediators. Since lipopolysaccharide (LPS) has been known to provide protection against O2 toxicity, which is correlated with increased activity of O2 metabolite-detoxifying enzymes, the effect of this agent on bleomycin-induced pulmonary fibrosis was examined. Endotracheal bleomycin administration caused increased lung collagen synthesis. A single intraperitoneal injection of LPS (500 micrograms/kg) at day zero significantly decreased these increases. Total bleomycin-induced lung collagen increase was also significantly reduced. LPS alone had no significant effect on total lung catalase activity. Glutathiione peroxidase activity, however, was significantly decreased by 15.8% compared to untreated animals at 2 days after LPS treatment and remained unchanged at other time points. In addition, superoxide dismutase activity was significantly elevated by 30% above untreated animals only at 14 days after LPS administration and remained unchanged at other time points. Endotracheal bleomycin administration alone caused significant reductions in catalase activity at 2 days and 2 weeks after treatment, whereas glutathione peroxidase activity increased above control untreated animals at 2 and 4 weeks, respectively. Superoxide dismutase activity was unaffected by bleomycin treatment. Pretreatment with LPS before bleomycin prevented these reductions or caused increases in the activities of these enzymes at 2 days. Glutathione peroxidase was increased and was significantly greater than those animals treated with bleomycin alone. Catalase also was higher in the LPS plus bleomycin group (by 22.2%, p less than 0.05) than the bleomycin group alone. Compared to the effects on lung collagen synthesis and content, LPS treatment resulted in much less dramatic changes in total lung antioxidant enzyme activities. This discrepancy between the intensity of LPS effects on lung O2 metabolite-detoxifying enzymes and that on pulmonary fibrosis implies that the LPS-ameliorating effect on pulmonary fibrosis could not be totally explained by increased ability to detoxify O2 metabolites. Rather, the data would favor the possibility that LPS inhibits bleomycin-induced pulmonary fibrosis either by its known immunosuppressive effects or some other unknown mechanism. The former would be in agreement with previous data which suggest that an intact immune response is necessary for complete expression of the fibrogenic response to bleomycin.
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PMID:Inhibition of bleomycin-induced pulmonary fibrosis by lipopolysaccharide. 620 76

The dose and duration limiting toxic effects of cisplatin are ototoxicity and nephrotoxicity. While several studies have attempted to shed some light on the causes of nephrotoxicity, the reasons for ototoxicity induced by cisplatin are poorly understood. Therefore, this investigation was undertaken to delineate the potential mechanisms underlying cisplatin ototoxicity. The role of glutathione (GSH), oxidized glutathione (GSSG) and malondialdehyde levels, and antioxidant enzyme activities [superoxide dismutase, catalase, GSH peroxidase, and GSH reductase] were examined in cochlear toxicity following an acute dose of cisplatin. Male Wistar rats were treated with various doses of cisplatin. Pretreatment auditory brain stem evoked responses (ABR) were performed and then post-treatment ABRs and endocochlear potentials were also performed after three days. Acute cochlear toxicity (ototoxicity) was evidenced as elevated hearing thresholds and prolonged wave I latencies in response to various stimuli (clicks and tone bursts at 2, 8, 16 and 32 kHz) on ABRs. The endocochlear potentials were reduced (50% control) in cisplatin-treated rats as compared to control animals. The rats were sacrificed and cochleae isolated. The GSH, GSSG and malondialdehyde levels, and antioxidant enzyme activities were determined. Cisplatin ototoxicity correlated with a decrease in cochlear GSH [0.45 +/- 0.012 nmol/mg] after cisplatin administration compared to 0.95-012 nmol/mg in control cochleae (P < 0.05). Superoxide dismutase, catalase activities and malondialdehyde levels were significantly increased in the cochleae of cisplatin injected rats. Cochlear GSH-peroxidase and GSH reductase activity significantly decreased after cisplatin administration.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Mechanism of cisplatin ototoxicity: antioxidant system. 747 81

Ricin, a glycoprotein from castor oil seeds, is specifically toxic to Kupffer cells and at low doses it leaves parenchymal cells comparatively unaffected. At a dose of approximately 1.5 microgram/100 g body weight, ricin significantly increases the hepatic antioxidant enzyme system in rats within 24 hr. Superoxide dismutase, catalase and glutathione peroxidase show an increase in liver tissue levels of 19-24%. However, hepatic lipid peroxidation is elevated by about 34% and non-protein sulphydryl is reduced by 26%. The enhanced levels of antioxidant enzymes appear to protect the hepatocytes from the toxin. The observed elevation of hepatic thiobarbituric acid-reactive substances appears to originate mainly from the damaged Kupffer cells.
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PMID:Role of antioxidant enzyme defence in sparing rat hepatocytes from toxicity of ricin at low dose. 792 30

Ozone-induced lung injury in rats is focal, with the primary target sites being the distal trachea and the central acinus. In both area, ozone causes cellular injury and necrosis after short-term exposures, but the areas become tolerant to further injury after long-term exposure. To investigate the role of antioxidant enzymes in the resistance of the lung to injury from long-term ozone exposure, we measured activities of three antioxidant enzymes in airway samples microdissected from specific sites within the lung: distal trachea, lobar bronchi, major daughter axial bronchi, minor daughter bronchi, distal bronchiole, and parenchyma. Fischer 344 rats were exposed to 0, 0.5, and 1 ppm ozone 6 hr/day, 5 days/week for 20 months, or to 0, 0.12, and 1 ppm for 90 days. Glutathione transferase, glutathione peroxidase, and superoxide dismutase activities were measured at the end of the exposure periods. Data were normalized for DNA content (Units/mg DNA). For both the 90-day and 20-month exposures, the activities of all three enzymes were significantly elevated in a concentration-dependent fashion in the distal bronchioles. Compared to controls, animals exposed to 1.0 ppm ozone had superoxide dismutase activities 1.6x (90 days) and 2x (20 months) greater; glutathione peroxidase had activities 1.4x (90 days) and 1.6x (20 months) greater; and glutathione S-transferase had activities 1.5x (90 days and 20 months) greater. In animals exposed for 90 days, superoxide dismutase activity was lower in major daughter bronchi and greater in minor daughter bronchi and glutathione peroxidase activity was lower in major daughter bronchi. After 20 months of exposure, superoxide dismutase activity was significantly elevated in a dose-dependent fashion in the distal trachea; glutathione peroxidase activity decreased in the major daughter bronchi and increased in the minor daughter bronchi; and glutathione S-transferase activity decreased in the major daughter bronchi. There were no changes in antioxidant enzyme levels in other subcompartments. Superoxide dismutase activity increased in a concentration-dependent fashion in the whole lung homogenate of animals exposed for 90 days, but no differences were detected in whole lung homogenates of any other exposure groups. We conclude that (1) antioxidant enzyme activities are altered on a site-specific basis in response to long-term exposure to ozone; (2) the antioxidant enzymes respond differently in different lung subcompartments; (3) activities determined for the whole lung do not reflect changes in subcompartments with variable susceptibility to injury; and (4) changes in antioxidant enzyme activities are concentration-dependent and altered by length of exposure.
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PMID:Dose-dependent tolerance to ozone. IV. Site-specific elevation in antioxidant enzymes in the lungs of rats exposed for 90 days or 20 months. 804 44

Superoxide dismutase (SOD), which breaks down superoxide to oxygen and hydrogen peroxide, is generally considered an antioxidant enzyme. However, superoxide is a potent reducing agent and as such could affect cellular function by reducing disulfides in important proteins, such as, ionic channels and pumps. In support of this concept, we show that superoxide, generated by two different sources, is able to reduce disulfide bonds in an in vitro model. Depending on the source of superoxide this reduction is accelerated by an unsaturated fatty acid or ferric iron and is inhibited by SOD.
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PMID:Superoxide reduction of a disulfide: a model of intracellular redox modulation? 818 13


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