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PubMed1994

Superoxide dismutase, catalase and glutathione peroxidase activities in the lymphoid organs of diabetic rats.

The effect of alloxan-induced diabetes on CuZn- and Mn-superoxide dismutase (SOD), catalase and glutathione peroxidase (GPX) activities, as well as the content of thiobarbituric acid reactive substances (TBARs) were examined in rat lymphoid organs (mesenteric lymph nodes (MLN), thymus and spleen) and, for comparison, red and white muscle fibres. The capacity for generation of reduced equivalents was also evaluated by measuring the activities of glucose-6-phosphate dehydrogenase (pentose-phosphate pathway-cytosol) and citrate synthase (Krebs cycle-mitochondria). Diabetes raised the capacity for the generation of reducing equivalents in the lymphoid organs: in the mitochondria of the thymus and spleen and in the cytosol of the mesenteric lymph nodes and thymus. In muscles, diabetes reduced CuZn-SOD activity in soleus and raised the activity in gastrocnemius, and depressed the activities of catalase in soleus and of glutathione peroxidase in both soleus and gastrocnemius. In relation to the lymphoid organs, the spleen showed a decrease in the antioxidant enzyme activities (except for glutathione peroxidase), whereas the thymus showed an increased level (except for Mn-SOD), and the MLN presented a reduction in Mn-SOD and catalase activities and an increase in GPX activity caused by diabetes. The content of TBARs in the tissues followed the changes in GPX activity inversely: i.e. a decrease in the lymphoid organs (except in the spleen) and an increase in the muscles of diabetic rats compared with the control group. All these changes found in diabetic rats were reversed by insulin treatment and were not modified by the normalization of glycaemia.

Animals↗
PubMed2000

Effects of estrogens and androgens on erythrocyte antioxidant superoxide dismutase, catalase and glutathione peroxidase activities during the menstrual cycle.

The effects of physiological changes in estrogens and androgens on the erythrocyte antioxidant superoxide dismutase, catalase and glutathione peroxidase enzyme activities during the menstrual cycle were investigated in healthy eumenorrheic women. Blood samples were taken on alternate days from twelve normally cyclic women (age range: 20 to 27 years; mean age: 24.1 years) from the first day of one menstrual cycle until the first day of the subsequent one. Plasma was analyzed for FSH, LH, estradiol, progesterone, testosterone, free testosterone and androstenedione concentrations. Erythrocyte superoxide dismutase, catalase and glutathione peroxidase activities were evaluated on the same days and cycle length was standardized on the basis of the preovulatory estradiol peak. Significant cyclic phase-related changes were observed in glutathione peroxidase (P<0.05), with higher glutathione peroxidase activity levels from the late follicular to the early luteal phase compared with those found in the early follicular phase (P<0.001 and P<0.002 respectively). A significant positive correlation was observed between mean estradiol and glutathione peroxidase cycle-related variations (r=0.80, P<0.001), whereas no significant cycle phase-dependent changes were seen in superoxide dismutase and catalase. No effect of progesterone and androgens on the erythrocyte antioxidant enzyme system was documented. The findings indicate that physiological ovarian estradiol production during the menstrual cycle may have an important role in regulating erythrocyte glutathione peroxidase activity.

Adult↗
PubMed1996

Protective effects of trolox C, vitamin C, and catalase on bromobenzene-induced damage to rat hepatocytes.

BACKGROUND/METHODS: The protective effects of trolox C (water-soluble vitamin E), vitamin C, and catalase on bromobenzene (BB)-induced toxicity to isolated rat hepatocytes were evaluated. The glutathione (GSH) content of the hepatocytes exposed to BB was measured. RESULTS: BB caused acute damage to the cells during 2 h of incubation (short) when BB was added directly to the culture wells, whereas a late-occurring and time-dependent increase in lactate dehydrogenase (LDH) leakage rate was observed during 24 h of incubation (long) when BB was dissolved in a different way. Incubation of the cells with trolox C (0.5-2.0 mM) prevented the hepatocellular damage induced by BB at 2.4 mM during the long-term incubation. Vitamin C (0.1-1.0 mM) had a protective effect on BB-induced toxicity during both the short- (BB, 1.6 mM) and the long- (BB, 2.4 mM) term incubations. Catalase (3200 U/ml) also showed a beneficial effect on the cells during the short-term BB exposure. Trolox C (2.0 mM) and vitamin C (0.5 mM) restored BB-induced GSH depletion in the cells. CONCLUSIONS: BB induced two patterns of LDH leakage from isolated hepatocytes on the basis of different ways of BB exposure and incubation periods. Trolox C, vitamin C, and catalase exerted protective effects on BB-induced toxicity during short- or/and long-term incubations. The effects were concentration-dependent. Restoration of GSH content in BB-exposed hepatocytes suggests that trolox C and vitamin C could reduce GSH consumption during BB metabolism and exert an antioxidant effect.

Analysis of Variance↗
PubMed1995

Increased catalase levels and hypoxanthine-enhanced nitro-blue tetrazolium staining in rat retina after ischemia followed by recirculation.

In the present study, using retinal ischemia as a model, we examined if different periods of ischemia and recirculation influenced the generation of reactive oxygen species, i.e. in hydrogen peroxide generation and nitroblue tetrazolium (NBT) reduction. Ischemia was induced for 30 and 90 min by ligation of the optic nerve with the vessels and recirculation was established by removing the ligature. The rats were sacrificed after 15 min or 3 days of recirculation. The retinas were separated from the pigment epithelium for measurements of catalase activity and examination of NBT staining. Compared to controls, the catalase activity was increased after 30 and 90 min of ischemia followed by 15 min of recirculation, and after 90 min of ischemia followed by 3 days of recirculation. As in controls, NBT staining was observed, both after 30 and 90 min of ischemia followed by 15 min of recirculation, in photoreceptors, in both plexiform layers, in some ganglion and glial cells, and, occasionally, in cells in the inner nuclear layer. Opposite to controls, addition of hypoxanthine to the NBT solution resulted in an increased staining in vessels in the inner nuclear layer in retinas subjected to 30 min of ischemia followed by 3 days of recirculation. The increased catalase activity suggests an increased amount of this free radical scavenger after ischemia followed by short-term and long-term recirculation. The hypoxanthine-enhanced NBT staining of blood vessel walls after ischemia followed by long-term recirculation indicates an activation of xanthine oxidase and an increased production of NBT reductants, some of which may represent oxygen free radicals.

Animals↗
PubMed1998

cDNA and deduced amino acid sequences of dog catalase.

The nucleotide sequence of dog catalase was determined from cDNA obtained by reverse transcriptase-polymerase chain reaction (RT-PCR) and 5'- and 3'- rapid amplification of cDNA ends (RACE) using dog liver mRNA. The deduced amino acid sequence was compared with the sequences of other mammalian catalases and was found to show 93.0, 92.0, 93.3 and 91.7% similarity with mouse, rat, bovine and human catalases, respectively.

Amino Acid Sequence↗
PubMed1999

Cloning and characterization of a cDNA encoding catalase in wheat.

We determined the nucleotide sequence of a cDNA encoding the catalase (CAT) isolated from wheat (Triticum aestivum L.). The deduced amino acid sequence suggests that this wheat catalase isozyme shared higher amino acid homology with group I CATs of barley CAT-1, rice CAT B and maize CAT-1 and CAT-2 but lower homology with group II CATs of barley CAT-2, rice CAT A and maize CAT-3. Both group I and II specific sequences of Ser-Arg-Leu and Ser-Ser-Ser, respectively considered as peroxisomal targeting signals were found first in monocot plant of wheat. Functionally important amino acids at active center and heme-binding sites detected in all other plant catalase were conserved.

Amino Acid Sequence↗
PubMed1988

Antioxidant enzymes of larvae of the cabbage looper moth, Trichoplusia ni: subcellular distribution and activities of superoxide dismutase, catalase and glutathione reductase.

In the mid-fifth instar larvae of the cabbage looper moth, Trichoplusia ni, the subcellular distribution of total superoxide dismutase was as follows: 3.05 units (70.0%), 0.97 units (22.3%), and 0.33 units (7.6%) mg-1 protein in the mitochondrial, cytosolic and nuclear fractions, respectively. No superoxide dismutase activity was detected in the microsomal fraction. Catalase activity was unusually high and as follows: 283.4 units (47.3%), 150.1 units (25.1%), 142.3 units (23.8%), and 22.9 units (3.8%) mg-1 protein in the mitochondrial, cytosolic, microsomal (containing peroxisomes), and nuclear fractions. No glutathione peroxidase activity was found, but appreciable glutathione reductase activity was detected with broad subcellular distribution as follows: 3.86 units (36.1%), 3.68 units (34.0%), 2.46 units (23.0%), and 0.70 units (6.5%) mg-1 protein in the nuclear, mitochondrial, and cytosolic fractions, respectively. The unusually wide intracellular distribution of catalase in this phytophagous insect is apparently an evolutionary adaptation to the absence of glutathione peroxidase; hence, lack of a glutathione peroxidase-glutathione reductase role in alleviating stress from lipid peroxidation. Catalase working sequentially to superoxide dismutase, may nearly completely prevent the formation of the lipid peroxidizing .OH radical from all intracellular compartments by the destruction of H2O2 which together with O2- is a precursor of .OH.

Animals↗
PubMed1992

Changes in superoxide dismutase and catalase in aging heat-shocked Drosophila.

We have examined the age-dependent expression of CuZn superoxide dismutase (SOD) and catalase (CAT) in Drosophila melanogaster following heat shock. Quantitative northern blot analysis was performed after heat shock on 2-, 23- and 49-day-old flies, using a 0.48 kb Sal1 EcoR1 fragment of the Drosophila SOD cDNA and a 1.4 kb fragment of the human catalase cDNA. Heat shock induction was monitored with a 5.4 kb DNA fragment of the Drosophila hsp70 gene. After exposure to 37 degrees C for 30 min and 60 min, the level of SOD RNA in young flies was elevated above that of nonstressed conditions. Changes in the transcription of SOD gene with age paralleled the expression of hsp70 RNA. The SOD RNA was elevated in heat-shocked middle aged (23-25 days old) flies compared to young Drosophila (2 days old), then it decreased in 49-50-day-old flies. The relative expression of CAT RNA did not change with age or after heat shock. Enzymatic activities of these two antioxidant enzymes were evaluated in nondenaturing polyacrylamide electrophoresis gels. SOD migrates on this gel as three different electromorphs. These were designated as fast, intermediate and slow migrating bands. The most intense activity was associated with the fast band in these flies. In the absence of heat shock, there was an age-dependent decrease in the intermediate, but not in the slow or fast bands. Heat shock does not affect the intensity of the fast band in young or old flies, however; in middle aged flies, there is a shift in this band toward the slow position. No change was detected in the activity of catalase with age or heat shock, although flies of all ages exhibited a shift toward a faster-migrating electromorph with increasing time of heat shock. This effect was also observed in flies fed H2O2 and is more pronounced in insects fed higher concentrations. These results are discussed in relation to the role of these antioxidant enzymes in protecting against age-induced oxidative stresses.

Aging↗
PubMed1996

Determination of the kinetic parameters for the "suicide substrate" inactivation of bovine liver catalase by hydrogen peroxide.

The kinetics of the bovine liver catalase inactivation by its suicide substrate, H2O2 was investigated in sodium phosphate buffer, 50 mM pH 7.0, at 27 degrees C. By combination of the rate equations of two concurrent reactions, decomposition of H2O2 by catalase and suicide inactivation of catalase by H2O2, simple, semiempirical kinetic equations were defined and used for the determination of the inactivation rate constant and the partition ratio which were found to be 6.86 +/- 0.19 M-1 min-1 and 1.82 x 10(7) +/- 5.0 x 10(5), respectively. A close match was found between the experimental data and the equations.

Animals↗
PubMed1998

Resistance of biofilms to the catalase inhibitor 3-amino-1,2, 4-triazole.

Consortia of catalase positive bacteria consisting of Pseudomonas aeruginosa, Pseudomonas fluorescens, and Klebsiella pneumoniae, in both the planktonic form and as biofilms, disproportionate hydrogen peroxide into oxygen and water. The biofilm, however, continued to disproportionate the hydrogen peroxide in the presence of the catalase inhibitor, 3-amino-1,2,4-triazole, while the planktonic organisms did not. While the bacterial catalase-peroxidase-dismutase system was probably responsible for the disproportionation of hydrogen peroxide in both cases, biofilms resisted inhibition of this enzyme system.

Amitrole↗
PubMed1976

[Effect of several surface-active substances on the biological and mechanical properties of a catalase monolayer].

It is found out that surface pressure of catalase monolayers increases when some medicinal surface-active agents are added to its substrate, while its enzymic activity decreases depending on the increase of surface activity of the medicinal substance. Catalase monolayer viscosity grows with a decrease in the area. The viscosity decreases with a rise in the dimedrol concentration in the substrate. The same is recorded for the shear module. As to the shear stress characterizing the strength of the monolayers it decreases with the addition of medicinal substances. This change in rheological properties of the catalase monolayer evidences for its structural destruction with an increase in the mixed monolayer pressure.

Catalase↗
PubMed1998

[Lipid and protein peroxidation process and catalase activity in pre-eclamptic placenta].

There are some suggestions that free radicals are involved in some dysfunctions observed in preeclampsia. In this study we have examined the antioxidant status of preeclamptic placentas. We have used placentas obtained from normal pregnant women and women with preeclampsia. Lipoperoxidative process was measured by means of Okhawa method. Sedlak method was used to measured the total thiol groups. The catalase activity was measured by means of Pffeifer method. The results show that the catalase activity decreases, the amount of MDA increases and the total amount of thiol groups is smaller in preeclamptic placentas. The level of lipid peroxides in preeclamptic placentas is about 1.8 times higher in comparison with normal placentas. The decreased level of total thiol groups in preeclamptic placentas can be caused by a more intensive process of protein peroxidation. Catalase is less active in preeclamptic placentas. It can be due to lower activity of antioxidant systems or the destruction of antioxidant systems by reactive oxygen species. The results of our experiments confirm lower antioxidant status in preeclamptic placentas and suggest that peroxidative reaction may cause many dysfunctions associated with preeclampsia.

Catalase↗
PubMed1976

Effect of vitamin E deficiency on the level of superoxide dismutase, glutathione peroxidase, catalase and lipid peroxide in rat liver.

The activities of superoxide dismutase, glutathione peroxidase, catalase and xanthine oxidase were simultaneously studied in vitamin-E deficient and -supplemented rat liver and also measured the lipid peroxide content in liver. The lipid peroxide content of vitamin E-deficient rat liver, estimated by thiobarbituric acid, increased as compared with that of vitamin E-supplemented rat liver. No marked changes of activities of superoxide dismutase, glutathione peroxidase and catalase were observed, but the activity of xanthine oxidase which is strong superoxide generator increased in vitamin E-deficient rat liver. These results suggest that vitamin E prevents the accumulation of lipid peroxide, but not controls the level of peroxide scavenging system such as superoxide dismutase, glutathione peroxidase and catalase.

Animals↗
PubMedDate not supplied

In vitro and in vivo effects of chlorpyrifos on glutathione peroxidase and catalase in developing rat brain.

Preliminary findings of a study on the role of oxidative stress in the developmental neurotoxicity of chlorpyrifos (CPF) indicates that in vitro exposure to 1-100 microM CPF or 1-100 nM CPF-oxon had no effect on the activity of glutathione peroxidase (GSHpx) in brain homogenates from postnatal day (PN) 21 rats, or on the activity of purified GSHpx. A single high-dose acute injection of 45 mg/kg CPF to PN19 rats also did not significantly alter GSHpx activity at PN21, in spite of extensive (72%) brain acetylcholinesterase (AChE) inhibition. However, catalase activity was significantly reduced by 28%. PN21 pups exposed maternally to a lower effective dose of CPF throughout development (dams injected with 50 mg/kg every 3 days) also had normal GSHpx activity, but a 30% increase in H2O2-independent NADPH consumption. Brain catalase activity in these rats was significantly increased by 24%. These preliminary data suggest that specific GSHpx activity is not altered by in vitro or in vivo exposures to CPF-oxon or CPF, but catalase and an unknown H2O2-independent NADPH-consuming factor were affected differentially depending on the type and timing of exposure.

Acetylcholinesterase↗
PubMed2000

Free radical scavengers, catalase and superoxide dismutase provide protection from oxalate-associated injury to LLC-PK1 and MDCK cells.

PURPOSE: Current studies have provided evidence that exposure of renal epithelial cells to oxalate and calcium oxalate crystals induces lipid peroxidation and injures the cells. Since oxidant/antioxidant balance is likely to play a critical role, we determined the effect of antioxidant scavengers on production of free radicals and injury to LLC-PK1 and MDCK cells from exposure to oxalate (Ox) or Ox + calcium oxalate monohydrate (COM) crystals. MATERIALS AND METHODS: LLC-PK1 and MDCK cells were grown in monolayers and exposed to 1.0 mmol. Ox or 1.0 mmol. Ox + 500 microg. /ml. COM crystals for 120 or 240 minutes. We measured the release of lactate dehydrogenase (LDH) as a marker for cell injury and malondialdehyde (MDA) as a marker of lipid peroxidation. Superoxide and hydroxyl radicals were measured in the presence or absence of 400 U/ml. catalase, or superoxide dismutase (SOD). RESULTS: Exposure of LLC-PK1 cells to Ox resulted in a significant increase in MDA and release of LDH, which was further elevated when COM crystals were added. MDCK cells responded similarly to both challenges, but showed significantly less impact when compared with LLC-PK1 cells. Both treatments were associated with significant increase in the generation of hydroxyl and superoxide radicals by both cell types. In both cell lines, the addition of catalase or SOD significantly reduced the increase of MDA and release of LDH. CONCLUSIONS: Results of the present study indicate that both Ox and COM crystals are injurious to renal epithelial cells and the injury is associated with generation of free radicals. Cells of proximal tubular origin are more susceptible than those of distal tubules and collecting ducts. Free radical scavengers, catalase and SOD provide significant protection.

Animals↗
PubMed2001

The C-terminal domain of HPII catalase is a member of the type I glutamine amidotransferase superfamily.

Discovering distant evolutionary relationships between proteins requires detecting subtle similarities. Here we use a combination of sequence and structure analysis to show that the C-terminal domain of Escherichia coli HPII catalase with available spatial structure is a divergent member of the type I glutamine amidotransferase (GAT) superfamily. GAT-containing proteins include many biosynthetic enzymes such as E. coli carbamoyl phosphate synthetase and anthranilate synthase. Typical GAT domains have Rossmann fold-like topology and possess a catalytic triad similar to that of proteases. The C-terminal domain of HPII catalase has the GAT Rossmann fold but lacks the triad and therefore loses enzymatic activity. In addition, we detect significant sequence similarity between thiJ domains, some of which are known to have protease activity, and typical GAT proteins. Evolutionary tree analysis of the entire GAT superfamily indicates that the HPII catalase is more closely related to thiJ domains than to classical GAT domains and is likely to have evolved from a thiJ-like protein. This work illustrates the strength of sequence-based profile analysis techniques coupled with structural superpositions in developing an evolutionarily relevant classification of protein structures. Proteins 2001;42:230-236.

Amino Acid Motifs↗
PubMed2001

Regulation of the catalase gene promoter by Sp1, CCAAT-recognizing factors, and a WT1/Egr-related factor in hydrogen peroxide-resistant HP100 cells.

Reactive oxygen species play a critical role in the onset of apoptosis induced by various extracellular stimuli, including ionizing radiation. Therefore active regulation of reactive oxygen species-metabolizing enzymes may be one response to an apoptotic stimulus. In this regard, HP100 cells, H(2)O(2)-resistant variants derived from human leukemia HL60 cells, display an interesting phenotype in which the activity of catalase is constitutively high, whereas its mRNA is reduced after X-ray irradiation. In the present study, we investigated the molecular mechanisms underlying this phenomenon. By combining analyses from nuclear run-on, reporter gene transient transfection, genomic footprinting, site-directed mutagenesis, electrophoretic mobility shift analysis, and Western blotting experiments, we found that constitutively elevated catalase expression is strongly regulated at the transcriptional level by both Sp1 and CCAAT-recognizing factors and that much higher levels of nuclear Sp1 and NF-Y are present in HP100 nuclei as compared with HL60 nuclei. In addition, we demonstrated an X-ray-inducible association of a WT1/Egr-related factor with an overlapping Sp1/Egr-1 recognition sequence located within the core promoter of the catalase gene. This association may lead to inactivation of the promoter by disturbing or competing with the transactivating ability of Sp1.

Base Sequence↗
PubMed2001

Prevention of neutrophil-mediated hepatic ischemia/reperfusion injury by superoxide dismutase and catalase derivatives.

Our previous study demonstrated that the combination of mannosylated superoxide dismutase (Man-SOD) and succinylated catalase (Suc-CAT), both of which are designed to be targeted to liver nonparenchymal cells, is a promising approach to prevent the initial phase of hepatic ischemia/reperfusion injury induced by occlusion of the portal vein for 30 min followed by a 1-h reperfusion in mice. In this study, the preventive effects of these agents were examined on late-phase injury mediated by infiltrating neutrophils, a more severe condition than the initial one. Administration of Suc-CAT alone or with Man-SOD to mice undergoing hepatic ischemia/reperfusion significantly suppressed the expression of intercellular adhesion molecule-1 along the hepatic sinusoid and prevented neutrophil infiltration in the liver. Man-SOD and Suc-CAT also prevented the increase in plasma glutamic pyruvic transaminase and glutamic oxaloacetic transaminase activities after reperfusion lasting 3 and 6 h. Histological evaluation of liver tissues confirmed the efficacy of this treatment, suggesting that these SOD and catalase derivatives have the ability to suppress neutrophil-induced hepatic injury. These results demonstrate that targeted delivery of antioxidant enzymes to liver nonparenchymal cells is a promising approach to reducing the reactive oxygen species produced by Kupffer cells and neutrophils infiltrating into the tissue. Since Suc-CAT is partially taken up by hepatocytes via a catalase-specific uptake mechanism, such a fraction could also be involved in its preventive effect against the injury.

Alanine Transaminase↗