Superoxide dismutase, catalase and glutathione peroxidase activities in the brain of streptozotocin induced diabetic rats

Brain antioxidant enzymes, superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPX) levels were studied in the brains of early diabetic (72 hr) and long term diabetic (one month) rats. Diabetes was induced by injecting streptozotocin (50 mg/kg, i.p.) in citrate buffer. One group of diabetic rats was treated with insulin (1U/day/animal). The results indicate that early diabetic rats exhibit increased SOD and CAT activities with no alteration in the GPX activity. On the contrary, increased CAT decreased GPX activities with no alteration in the SOD activity, was noted in the long-term Diabetic rats. Insulin treatment reversed these alterations in both the groups. It can be concluded that, in diabetic condition antioxidant enzyme levels are elevated and insulin treatment attenuated these changes. Hence, diabetes mellitus, if left untreated, may initiate degenerative processes and other CNS complications due to accumulation of oxidative free radicals.     

Superoxide dismutase, glutathione peroxidase, and glutathione reductase in sheep organs

The enzyme activities of the superoxide dismutase (SOD), glutathione peroxidase (GSHPx), glutathione reductase (GR) and thiobarbituric acid reactive substances (TBARS) content were measured in tissue extracts of the liver, kidney and lung of sheep in a nonpolluted control area (C), a polluted area pasture (PP) and those from polluted areas but fed in the laboratory with an experimental emission supplement diet (EEF). Compared with the control SOD, activity was significantly increased (1.75 times) only in the liver of the PP group. In the EEF group there was a tendency toward lower activities in all organs. The Cu,Zn-SOD isoenzymes pattern analyzed by isoelectrofocusing was different in the organs of the animals exposed to pollutants when compared with those of the controls. In the liver, two new isoenzymes with pI 5.30 and 5.70 were found in the PP group and an additional isoenzyme with pI 5.10 in the EEF group. The kidney isoenzymes with pl 5.30 and 5.40 were inhibited in the EEF group. In the lung, two new isoenzymes appeared with pl 5.30 and 5.40 in the PP group and two new isoenzymes with pI 6.10 and 6.50 in the EEF group. GSHPx activity was inhibited in the liver and kidney of the sheep exposed to pollutants. GR activity was significantly changed only in the liver. The activity in the PP group was 2.30 and 2.10 times higher than in the C and EEF groups, respectively. TBARS content was increased in the liver and kidney of the EEF group compared with the control.     

Superoxide dismutase, glutathione peroxidase, catalase, and lipid peroxidation in the major organs of the aging rats

Glutathione peroxidase (GSh-Px), superoxide dismutase (SOD), catalase (CAT) activities and malon-dialdehyde (MDA) content were determined in heart, liver, kidney and brain of rats. Two different age groups (4 months; 24 months) were considered. GSH-Px and SOD activities decrease significantly for the aged liver and kidney. During aging, the activity of catalase increase in cardiac muscle and, in contrast, decrease in other organs. Lipids peroxidation, expressed in term of MDA formation, decrease in all the organs of the aged rats. The results indicate that: 1) the liver and kidney antioxidative defense decrease with age; 2) the enzymatic activities evolve in a different manner for different enzymes and organs. Furthermore, the results suggest that there is not any correlation between the SOD, CAT, and GSH-Px activities and the peroxidative status of the organs; thus, the age-related increase in the MDA content proposed as a criterion of aging process should be considered with caution.     

Superoxide dismutase,glutathione peroxidase and catalase in oxidative hemolysis. A study of Fanconi's anemia erythrocytes

Superoxide dismutase, glutathione peroxidase and catalase were assayed in the erythrocytes of three patients of Fanconi's anemia. Superoxide dismutase was found to be significantly decreased, as previously reported. The enzymes metabolizing H₂O₂ are normal (glutathione peroxidase in the higher limits of the normal value). The abnormal erythrocytes were found to be as resistant (perhaps more resistant) as normal red blood cells to oxidative hemolysis induced by drugs. Malonyl dialdehyde production was found to be comparable to that of normal erythrocytes. It is concluded that a significant (30–40%) deficiency of superoxide dismutase, when associated to normal values of H₂O₂-removing enzymes, does not affect the antioxidative defense capability of erythrocytes, even in conditions of augmented oxidative injury.     

Superoxide dismutase,catalase, and glutathione peroxidase in the swim bladder of the physoclistous fish,Opsanus tau L

Summary The antioxidant enzymes superoxide dismutase, glutathione peroxidase, and catalase were measured in the rete mirabile and gas gland epithelium area of the swim bladder of the toadfish Opsanus tau. When the concentration of enzyme in the swim bladder was compared with the concentration in other organs (kidney, heart, gills) of the same fish, the swim bladder was found to have the highest concentration of superoxide dismutase but relatively low levels of glutathione peroxidase and catalase.Cytochemical assay for the peroxidatic activity of catalase confirmed that virtually no catalase is present in epithelial cells of the gas gland. A similar assay for peroxidase revealed a cyanide-sensitive peroxidase in the multilamellar bodies of these cells. Most of the catalase and peroxidase in the rete mirabile appears to be confined to the granules of neutrophils and the cytoplasm of erythrocytes. Enzyme activity in the neutrophils is not inhibited by 10^-1 M KCN. Cyanide does appear to inhibit the peroxidase activity in erythrocytes but has little effect on catalase in these cells.Supported by grant No. HL23338 from the National Institutes of Health     

Automated assays for superoxide dismutase, catalase, glutathione peroxidase, and glutathione reductase activity

Automated assays for catalase, glutathione peroxidase, glutathione reductase, and superoxide dismutase are presented. The assay for catalase is based on the peroxidatic activity of the enzyme. The glutathione peroxidase and reductase assays measure the consumption of NADPH following the reduction of t-butyl hydroperoxide and oxidized glutathione, respectively. The assay for superoxide dismutase is based on the reduction of cytochrome c. All assays utilize the Cobas FARA clinical automated analyzer and provide considerable time savings over the manual assays.     

Correlation between superoxide dismutase,glutathione peroxidase and catalase in isolated rat hepatocytes during fetal development

Superoxide dismutase, glutathione peroxidase and catalase activities were determined in isolated fetal rat hepatocytes of various ages and compared with the values of neonatal and adult cells. The developmental pattern of superoxide dismutase and glutathione peroxidase were very similar with a low constant activity in the fetal cells and a postnatal burst. On the contrary catalase begins to increase already since the 18th day of the fetal life. The results suggest a functional correlation of superoxide dismutase and glutathione peroxidase in the antioxidative enzyme defense of liver cells.     

CuZn superoxide dismutase, Mn superoxide dismutase, catalase and glutathione peroxidase in glutathione-deficient human fibroblasts

The effect of genetically determined glutathione deficiency on the fibroblast content of CuZn superoxide dismutase, Mn superoxide dismutase, catalase and glutathione peroxidase was investigated. No significant differences between glutathione-deficient and -proficient human fibroblasts were revealed. There was a large variation in the content of the investigated enzymes in fibroblasts grown and analysed on different occasions. Whereas the contents of CuZn superoxide dismutase, catalase and glutathione peroxidase did not deviate much from what has been found in other human cell-lines and tissues, the fibroblasts were found to contain exceptional amounts of Mn superoxide dismutase.     

Superoxide dismutase, catalase and glutathione peroxidase activities in the lymphoid organs and skeletal muscles of rats treated with dexamethasone

The effect of dexamethasone (a synthetic glucocorticoid) on the activity of antioxidant enzymes (superoxide dismutase (SOD), catalase and glutathione peroxidase) of the lymphoid organs (mesenteric lymph nodes (MLN), spleen and thymus) was investigated. For comparison with non-immune tissues, skeletal muscles (soleus and gastrocnemius (GC) were also studied. As an indication of the occurrence of lipid peroxidation, the content of thiobarbituric acid reactant substances (TBARs) was also determined. Dexamethasone treatment decreased the TBARs content of the lymphoid organs and raised it in the GC and soleus muscles. The activity of Cu/Zn-SOD was reduced in all tissues. However, the activity of Mn-SOD was decreased in the MLN and soleus muscle only. The activity of catalase was reduced in the MLN and thymus and raised in the spleen and GC and soleus muscles. The imposed treatment raised the activity of GPX in the MLN, thymus and spleen and reduced it in GC and soleus muscles. These data led us to postulate that the mechanism for the therapeutic effect of glucocorticoids as antiinflammatory and immunosuppressive agents might include modification of antioxidant enzyme activities.     

Coisolation of glutathione peroxidase, catalase and superoxide dismutase from human erythrocytes

Glutathione peroxidase (GSH-Px; glutathione: hydrogen peroxide oxidoreductase; EC 1.11.1.9), catalase (H2O2: H2O2 oxidoreductase; EC 1.11.1.6) and superoxide dismutase (superoxide: superoxide oxidoreductase; EC 1.15.1.1) were coisolated from human erythrocyte lysate by chromatography on DEAE-cellulose. Glutathione peroxidase was separated from superoxide dismutase and catalase by thiol-disulfide exchange chromatography and then purified to approximately 90% homogeneity by gel permeation chromatography and dye-ligand affinity chromatography. Catalase and superoxide dismutase were separated from each other and purified further by gel permeation chromatography. Catalase was then purified to approximately 90% homogeneity by ammonium sulfate precipitation and superoxide dismutase was purified to apparent homogeneity by hydrophobic interaction chromatography. The results for glutathione peroxidase represent an improvement of approximately 10-fold in yield and 3-fold in specific activity compared with the established method for the purification of this enzyme. The yields for superoxide dismutase and catalase were high (45 mg and 232 mg, respectively, from 820 ml of washed packed cells), and the specific activities of both enzymes were comparable to values found in the literature.     

CuZn-superoxide dismutase, Mn-superoxide dismutase, catalase and glutathione peroxidase in pancreatic islets and other tissues in the mouse.

Exogenous superoxide dismutase, catalase and scavengers of the hydroxyl radical protect pancreatic-islet cells against the toxic actions of alloxan in vitro [Grankvist et al. (1979) Biochem. J. 182, 17--25]. To test whether the extraordinary sensitivity of islet cells to alloxan is due to a deficiency of endogenous enzymes protecting against oxygen-reduction products, we assayed CuZn-superoxide dismutase, Mn-superoxide dismutase, catalase and glutathione peroxidase in mouse islets and other tissues. To correct for any blood contamination, haemoglobin was also measured in the tissue samples. Pancreatic islets were found to belong to tissues with relatively little activity of the protective enzymes. However, the deviation from other tissues in this respect is probably not large enough to explain the especially great susceptibility of islet cells to alloxan.     

Superoxide dismutase, catalase, glutathione peroxidase and gluthatione S-transferases M1 and T1 gene polymorphisms in three Brazilian population groups

Antioxidants such as superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPX1) reduce the oxidation rates in the organism. Gluthatione S-transferases (GSTs) play a vital role in phase 2 of biotransformation of many substances. Variation in the expression of these enzymes suggests individual differences for the degree of antioxidant protection and geographical differences in the distribution of these variants. We described the distribution frequency of CAT (21A/T), SOD2 (Ala9Val), GPX1 (Pro198Leu), GSTM1 and GSTT1 polymorphisms in three Brazilian population groups: Kayabi Amerindians (n = 60), Kalunga Afro-descendants (n = 72), and an urban mixed population from Federal District (n = 162). Frequencies of the variants observed in Kalunga (18% to 58%) and Federal District (33% to 63%) were similar to those observed in Euro and Afro-descendants, while in Kayabi (3% to 68%), depending on the marker, frequencies were similar to the ones found in different ethnic groups. Except for SOD2 in all population groups studied here, and for GPX1 in Kalunga, the genotypic distributions were in accordance with Hardy-Weinberg Equilibrium. These data can clarify the contribution of different ethnicities in the formation of mixed populations, such as that of Brazil. Moreover, outcomes will be valuable resources for future functional studies and for genetic studies in specific populations. If these studies are designed to comprehensively explore the role of these genetic polymorphisms in the etiology of human diseases they may help to prevent inconsistent genotype-phenotype associations in pharmacogenetic studies.     

Vanadium effect on the activity of horseradish peroxidase, catalase, glutathione peroxidase, and superoxide dismutase in vitro.

The effect of vanadium (V) on the activity of horseradish peroxidase, catalase, glutathione peroxidase, and superoxide dismutase has been studied. A competitive inhibition pattern was evident for vanadate ions on the activity of horseradish peroxidase (Ki = 41.2 microM). No significant inhibitory effects were found when V(V) was tested with catalase and when either V(IV) or V(V) were assayed with glutathione peroxidase. For the latter, the effect of V on the different components of the reaction system was investigated. V(V) did not significantly affect SOD activity when assayed with the sulfite method, which is devoid of interferences with V(V); however, there was an apparent inhibitory dose-response pattern for either V(IV) or V(V) using the pyrogallol assay, owing to an interference of pyrogallol with the metal. Besides, no significant binding of V(IV) or V(V) to the enzyme could be demonstrated. The lack of a direct inhibitory effect of V on the activity of the main antioxidant enzymes suggests that many biological and toxicological effects of V may be mediated more by oxidative reactions of the metal or of its complexes with physiologically relevant biomolecules than by a direct modulation of enzymatic activities.     

Lipoperoxides, vitamin E, and activities of superoxide dismutase, glutathione peroxidase, and catalase in regenerating rat liver

Lipoperoxides in homogenates of regenerating rat liver increased from 6 hours after the operation and reached a peak (about 7 times the control level) 18-24 hours after the operation. The concentration of blood lipoperoxides rapidly decreased after the operation. The enzymatic activities of superoxide dismutase, catalase, and glutathione peroxidase, and vitamin E content in regenerating livers were also determined. Among these antioxidant factors, the catalase level changed markedly.     

Superoxide dismutase, catalase and peroxidase in four strains of Neisseria meningitidis of different virulence

Abstract The effects of growth media on superoxide dismutase (SOD), catalase and peroxidase were compared in cell-free extracts from four strains of Neisseria meningitidis . The highly virulent strains, DRES-14 and M-1011, were consistently higher in SOD and catalase than the less virulent strains, DRES-03 and DRES-04. Cells grown in brain-heart infusion medium contained the highest levels of catalase. N. meningitidis contained one electrophoretic SOD band which was identified as iron-containing SOD (FeSOD). It was also shown that the presence of catalase could yield an artifactual SOD-band when the SOD activity stain is performed in the presence of 10 mM H₂O₂, normally required to inactivate and identify FeSODs.     

Correlative links between superoxide dismutase, catalase and glutathione peroxidase activities in mouse liver

Qualitative and quantitative differences in correlative and regressive links between superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase were assessed in the mice liver by two- and three-dimensional statistical methods. Paired linear correlation analysis indicated SOD-CAT tandem as the correlatively acting enzymatic pair. Three-dimensional analysis revealed uniform response surfaces which exhibited higher activities at disproportional values of the other two and lower activities at proportional activities of the other two enzymes. The direct effect of the enzymes on each other was positive [table: see text] while the effect of their product was always negative.     

Effect of erythropoietin on membrane lipid peroxidation, superoxide dismutase, catalase, and glutathione peroxidase of rat RBC

Starved animals having low levels of erythropoietin in blood showed increased MDA, fluorescent pigments, and met-Hb values whereas the hemoglobin concentration decreased significantly on starvation. In vivo and in vitro studies with Ep reversed the effects of starvation and brought these values close to normal. The activities of the enzymes (SOD, catalase, GSH-PX, GR G6PD, and 6PGD) which protect the RBC membrane directly or indirectly from peroxidative threat, decreased on starvation and restored to normal levels after Ep treatment.