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PubMed2003

Catalase activity in arctic microfungi grown at different temperatures.

The total of 98 strains of moulds were isolated from soils collected in arctic tundra (Spitzbergen). Among these strains Penicillium cyclopium 1, the most effective for production of catalase, was selected by the method of test-tube microculture. The time course of growth and catalase production by this strain showed the intracellular activity of this enzyme to be about 3-fold higher than its extracellular level Some properties of crude catalase preparation, isolated from postculture liquids by lyophilization, were also examined. Catalase activity showed its maximum at 15 degrees C, indicating adaptation of the enzyme to lower temperatures of the arctic environment.

Arctic Regions↗
PubMed2006

NADPH oxidase p22phox and catalase gene variants are associated with biomarkers of oxidative stress and adverse outcomes in acute renal failure.

Reactive oxygen species are important mediators of injury in acute renal failure (ARF). Although polymorphisms that affect key pro- and antioxidant enzymes might alter the susceptibility to oxidative stress-mediated injury, the use of genetic epidemiology for the study of oxidative stress-related genes has received little attention in ARF. The relationship of single-nucleotide polymorphisms in the coding region (C to T substitution at position +242) of the pro-oxidant enzyme NADPH oxidase p22phox subunit gene and in the promoter region (C to T substitution at position -262) of the antioxidant enzyme catalase gene to adverse clinical outcomes was evaluated prospectively in a cohort of 200 hospitalized patients with established ARF of mixed cause and severity. Genomic DNA was extracted from peripheral blood leukocytes and analyzed with a restriction fragment length polymorphism PCR method. Genotype-phenotype associations were characterized by measuring circulating nitrotyrosine and catalase activity. Observed and expected genotype frequencies were not significantly different, and overall baseline characteristics were not significantly different according to the various genotype groups. A genotype-phenotype association was demonstrable between the NADPH oxidase p22phox genotypes and plasma nitrotyrosine level (P = 0.06), as well as between the catalase genotypes and whole-blood catalase activity (P < 0.001). Compared with the NADPH oxidase p22phox CC genotype group, the T-allele group had a higher cumulative probability of remaining hospitalized (P = 0.03). Compared with the NADPH oxidase p22phox CC genotype, the T-allele carrier state was associated with 2.1-fold higher odds for dialysis requirement or hospital death (P = 0.01). This association persisted with 2.0- to 2.2-fold higher odds for this composite outcome after adjustment for race; gender; age; and the Acute Physiology and Chronic Health Evaluation II score (P = 0.03), the Multiple Organ Failure score (P = 0.01), or presence of sepsis (P = 0.02). The polymorphism in the gene that encodes the NADPH oxidase p22phox subunit at position +242 is associated with dialysis requirement or hospital death among patients with ARF. Larger studies are needed to confirm these relationships.

Acute Kidney Injury↗
PubMed1991

The role of catalase in protecting erythrocytes against methemoglobin formation.

Some mechanisms to reduce methemoglobin (metHb) formation for the maintenance of normal oxygen transport have been proposed. To study the role of catalase (EC 1.11.1.6), metHb formation in the hemolysate of normal and Japanese acatalasemic human subjects were examined spectrophotometrically. Significantly increased level of metHb was induced by potassium ferrocyanide in the hemolysate of acatalasemic subject. The addition of catalase reduced the metHb formation, while 3-amino-1,2,4-triazole (AT), a specific inhibitor of catalase-H2O2 compound I, increased it. These results obtained from human subjects were well consistent with those from mice and suggested that catalase plays a role in protecting erythrocytes against metHb formation.

Amitrole↗
PubMed2004

Flow-injection assay of catalase activity.

A novel flow-injection assay (FIA) system with a double line for catalase activity was constructed in which an oxidase is immobilized and the substrate is continuously pumped to reduce the dissolved oxygen and to generate a given level of hydrogen peroxide. The catalase in a sample decomposed the hydrogen peroxide, and thus the increase in dissolved oxygen dependent on the activity was amperometrically monitored using a Clark-type oxygen electrode. Among the examined several oxidases, uricase was most suitable for the continuous formation of hydrogen peroxide from a consideration of the stability and the conversion efficiency. Under the optimum conditions, a linear calibration curve was obtained in the range from 21 to 210 units/mg and the reproducibility (CV) was better than 2% by 35 successive determinations of 210 units/ml catalase preparation. The sampling frequency was about 15 samples/h. The present FIA system was applicable to monitor the inactivation of catalase by glycation.

Calibration↗
PubMed2005

MnSOD and catalase transgenes demonstrate that protection of islets from oxidative stress does not alter cytokine toxicity.

Reactive oxygen species (ROS) and nitric oxide (NO) are proposed mediators of cytokine-induced beta-cell destruction in type 1 diabetes. We produced transgenic mice with increased beta-cell expression of manganese superoxide dismutase (MnSOD) and catalase. Expression of these antioxidants increased beta-cell ROS scavenging and improved beta-cell survival after treatment with different sources of ROS. MnSOD or catalase conferred protection against streptozotocin (STZ)-induced beta-cell injury. Coexpression of MnSOD and catalase provided synergistic protection against peroxynitrite and STZ. To determine the potential effect of these antioxidants on cytokine-induced toxicity, we exposed isolated islets to a cytokine mixture, including interleukin-1beta and interferon-gamma. Cytokine toxicity was measured as reduced metabolic activity after 6 days and reduced insulin secretion after 1 day. Cytokines increased ROS production, and both antioxidants were effective in reducing cytokine-induced ROS. However, MnSOD and/or catalase provided no protection against cytokine-induced injury. To understand this, the nuclear factor-kappaB (NF-kappaB) signaling cascade was investigated. Antioxidants reduced NF-kappaB activation by ROS, but none of the antioxidants altered activation by cytokines, as measured by inhibitor of kappaB phosphorylation, NF-kappaB translocation, inducible NO synthase activation, and NO production. Our data agree with previous reports that antioxidants benefit beta-cell survival against ROS damage, but they are not consistent with reports that antioxidants reduce cytokine toxicity. ROS appear to have no role in cytokine toxicity in primary beta-cells.

Animals↗
PubMed2002

Regulation of catalase: inhibition by peroxynitrite and reactivation by reduced glutathione and glutathione S-transferase.

The regulation of stable catalase from Aspergillus niger was investigated. The preincubation of catalase with peroxynitrite (PN) resulted in a significant decrease in the production of O2, while the subsequent incubation with reduced glutathione (GSH, 1mM) led to restoration of the enzymatic activity. Western blot analysis revealed not only the increased immunoreactivities of 3-nitrotyrosine and S-nitrosocysteine in a PN-dose-dependent manner, but also conversely decreased immunoreactivity of 3-nitrotyrosine by the subsequent preincubation of catalase with GSH (1mM)/glutathione S-transferase (GST). The inhibition of the catalase after PN-treatment may be due to conformational changes of the enzyme via tyrosine-nitration/cysteine-nitrosation and the binding of active nitrogen/oxygen species to the Fe3+-protoporphyrin groups of the enzyme. The reverse of these processes to restore enzymatic activity by GSH/GST may be a vital antioxidative mechanism.

Aspergillus niger↗
PubMed2007

Laminar xanthine oxidase, superoxide dismutase and catalase activities in the prodromal stage of black-walnut induced equine laminitis.

UNLABELLED: REASONS FOR STUDY: Xanthine oxidase (XO)-dependent production of superoxide anion and hydrogen peroxide, a characteristic of ischaemia-reperfusion injury, may contribute to the development of equine laminitis. OBJECTIVE: To determine the levels of XO and antioxidant enzymes (catalase, superoxide dismutase [SOD]) in the digital laminae of normal horses (CON) and horses in the developmental stage of laminitis using the black walnut extract (BWE) model. METHODS: Healthy horses (n = 12) were administered BWE (BWE group, n = 6), or water (CON group, n = 6) through a nasogastric tube. At the onset of leucopenia in the BWE-treated animals, all horses were anaesthetised, digital laminae and other samples collected rapidly and flash frozen, and the animals subjected to euthanasia. Extracts of the frozen tissues were assayed for the 2 conformational forms of xanthine: oxygen oxidoreductase (XOR), namely, xanthine dehydrogenase (XDH) and xanthine oxidase (XO), as well as the antioxidant enzymes, SOD and catalase. RESULTS: Extracts of liver, lungs and skin, but not digital laminae, from either CON or BWE-treated horses had endogenous SOD, whereas all had endogenous XO and catalase. The levels of XDH, XO and catalase were similar in extracts of laminae from CON and BWE-treated horses as was the ratio of XDH to XO in extracts. CONCLUSIONS AND POTENTIAL RELEVANCE: The absence of increased XO activity suggest against the involvement of this reactive oxygen intermediate-generating system in the development of laminar pathology in BWE-treated horses. Conversely, the absence of SOD from extracts of equine digital laminae, but not other tissues, suggests that the equine digital laminae are highly susceptible to damage by superoxide anion, produced, for example, by emigrant inflammatory leucocytes.

Animals↗
PubMedDate not supplied

Influence of catalase on the radiation sensitizing effect of misonidazole.

The radiation modifying action of misonidazole and catalase was investigated in Bacillus megaterium spores at various oxygen concentrations. Catalase (120 micrograms/ml) decreased the radiation sensitizing action of misonidazole. Misonidazole as an electron affinic radiation sensitizer enhanced the build up of H2O2, thus promoting the reaction with catalase. Protection by catalase was not enough to eliminate the total radiation sensitizing effect of misonidazole.

Bacillus megaterium↗
PubMed1993

Intracellular catalase inhibition does not predispose rat heart to ischemia-reperfusion and hydrogen peroxide-induced injuries.

The objective of this study was to determine whether inhibition of intracellular catalase would decrease the tolerance of the heart to ischemia-reperfusion and hydrogen peroxide-induced injuries. Isolated bicarbonate buffer-perfused rat hearts were used in the study. Intracellular catalase was inhibited with 3-amino-1,2,4-triazole (ATZ, 1.5 g/kg body weight, two hours prior to heart perfusion). In the ischemia-reperfusion protocol, hearts were arrested with St. Thomas'II cardioplegic solution, made ischemic for 35 min at 37 degrees C, and reperfused with Krebs-Henseleit buffer for 30 min. The extent of ischemic injury was assessed using postischemic contractile recovery and lactate dehydrogenase (LDH) leakage into reperfusate. In the hydrogen peroxide infusion protocol, hearts were perfused with increasing concentrations of hydrogen peroxide (inflow rates 0.05-1.25 mumol/min). Inhibition of catalase activity (30.4 +/- 1.8 mU/mg protein in control vs 2.4 +/- 0.3 mU/mg in ATZ-treated hearts) affected neither pre-ischemic aerobic cardiac function nor post-ischemic functional recovery and LDH release in hearts subjected to 35 min cardioplegic ischemic arrest. Myocardial contents of lipid hydroperoxides were similar in control and ATZ-treated animals after 20 min aerobic perfusion, ischemia, and ischemia-reperfusion. During hydrogen peroxide perfusion, there was an increase in coronary flow rate followed by an elevation in diastolic pressure and inhibition of contractile function in comparison with control hearts. The functional parameters between control and ATZ-treated groups remained unchanged. The concentrations of myocardial lipid hydroperoxides were the same in both groups. We conclude that inhibition of myocardial catalase activity with ATZ does not predispose the rat heart to ischemia-reperfusion and hydrogen peroxide-induced injury.

Amitrole↗
PubMed1995

Reactions of bovine liver catalase with superoxide radicals and hydrogen peroxide.

The oxidized intermediates generated upon exposure of bovine liver catalase to hydrogen peroxide (H2O2) and superoxide radical (O2-) fluxes were examined with UV-visible spectrophotometry. H2O2 and O2- were generated by means of glucose/glucose oxidase and xanthine/xanthine oxidase systems. Serial overlay of absorption spectra in the Soret (350-450 nm) and visible (450-700 nm) regions showed that three oxidized intermediates, namely Compounds I, II and III, can be observed upon exposure of catalase to enzymatically generated H2O2 and O2-. Compound I is formed during the reaction of native enzyme with H2O2 and disappears in two ways: (i) via the catalytic reaction with H2O2 to restore native catalase and (ii) via the reaction with O2- to form Compound II. At low H2O2 concentrations (< 4.8 x 10(-9) M H2O2), Compound II reverts towards the native state mainly in a direct one-step reaction, whereas at higher H2O2 concentrations the pathway of Compound II back to the native enzyme involves Compound III. Formation of the latter from Compound II and H2O2 is irreversible and the rate constant of this reaction is 6.1 +/- 0.2 x 10(4) M-1 s-1. The formation of Compound III through the direct reaction of O2- with native enzyme has also been observed. Depending on the experimental conditions, the inactivation of catalase by O2- can be due to accumulation of Compound II ("slow" inhibition) or to the formation of Compound III ("rapid" inhibition) part of which leads to a dead end product. Formation of Compound III and of this dead end product are responsible for the irreversible inactivation in presence of an excess of H2O2.

Animals↗
PubMed2006

Nitric oxide protects macrophages from hydrogen peroxide-induced apoptosis by inducing the formation of catalase.

We investigated the cytoprotective effect of NO on H2O2-induced cell death in mouse macrophage-like cell line RAW264. H2O2-treated cells showed apoptotic features, such as activation of caspase-9 and caspase-3, nuclear fragmentation, and DNA fragmentation. These apoptotic features were significantly inhibited by pretreatment for 24 h with NO donors, sodium nitroprusside and 1-hydroxy-2-oxo-3,3-bis-(2-aminoethyl)-1-triazene, at a low nontoxic concentration. The cytoprotective effect of NO was abrogated by the catalase inhibitor 3-amino-1,2,4-triazole but was not affected by a glutathione synthesis inhibitor, L-buthionine-(S,R)-sulfoximine. NO donors increased the level of catalase and its activity in a concentration-dependent manner. Cycloheximide, a protein synthesis inhibitor, inhibited both the NO-induced increase in the catalase level and the cytoprotective effect of NO. These results indicate that NO at a low concentration protects macrophages from H2O2-induced apoptosis by inducing the production of catalase.

Animals↗
PubMed2003

Growth of Escherichia coli in iron-enriched medium increases HPI catalase activity.

Escherichia coli has two catalases, HPI and HPII. HPI is induced during logarithmic growth in response to low concentrations of hydrogen peroxide. This induction is OxyR-dependent. On the other hand, HPII is not peroxide-inducible but is induced in entry to the stationary phase. We demonstrate here that E. coli displayed higher HPI catalase activity when compared to the cultures that were grown in a normal medium, if grown in a medium supplemented with iron-citrate. Iron supplementation had no effect on HPII catalase. This increase of HPI activity was OxyR-independent and not observed in a Deltafur mutant. The physiological significance of the increase of HPI activity is unclear, but it appears that the katG gene that codes for HPI catalase is among the genes that are regulated by Fur.

Catalase↗
PubMed1998

Simultaneous production of catalase, glucose oxidase and gluconic acid by Aspergillus niger mutant.

The production of gluconic acid, extracellular glucose oxidase and catalase in submerged culture by a number of biochemical mutants has been evaluated. Optimization of stirrer speed, time cultivation and buffering action of some chemicals on glucose oxidase, catalase and gluconic acid production by the most active mutant, AM-11, grown in a 3-L glass bioreactor was investigated. Three hundred rpm appeared to be optimum to ensure good growth and best glucose oxidase production, but gluconic acid or catalase activity obtained maximal value at 500 or 900 rpm, respectively. Significant increase of dissolved oxygen concentration in culture (16-21%) and extracellular catalase activity were obtained when the traditional aeration was employed together with automatic dosed hydrogen peroxide.

Aspergillus niger↗
PubMed1999

Molecular cloning of a catalase cDNA from Nicotiana glutinosa L. and its repression by tobacco mosaic virus infection.

Recent reports revealed that catalase has a role in the plant defense mechanism against a broad range of pathogens through being inhibited by salicylic acid (SA). During an effort to clone disease resistance-responsive genes, a cDNA encoding catalase (Ngcat1; Nicotiana glutinosa cat1) was isolated from a tobacco cDNA library. In N. glutinosa, catalase is encoded by a small gene family. The deduced amino acid sequence of the Ngcat1 cDNA has 98% homology with the cat1 gene of N. plumbaginifolia. The Ngcat1 expression is controlled by the circadian clock, and its mRNA level is the most abundant in leaves. Both the expression of Ngcat1 mRNA and its enzyme activity in the tobacco plant undergoing a hypersensitive response (HR) to TMV infection were repressed. The repression of the mRNA level was also observed following treatment with SA. These results imply that SA may act as an inhibitor of catalase transcription during the HR of tobacco. Cloning and expression of the Ngcat1 in tobacco following pathogen infection and SA treatment are presented.

Amino Acid Sequence↗
PubMedDate not supplied

[Features of the inhibition of catalase activity by 3-amino-1,2,4-triazole in erythrocytes and liver of rats with streptozotocin diabetes].

Lipid peroxidation was intensified by streptozotocin induced diabetes mellitus in erythrocytes and liver. Activity of antioxidant enzyme superoxide-dismutase was decreased, activity of catalase was increased. Concentration of lipid peroxidation products was decreased after nicotinamide injections. It was investigated liver- and erythrocyte catalase inhibition in the presence of 3-amino-1,2,4-triazole. Effective inhibitor concentration for liver catalase by streptozotocin induced diabetes mellitus was 10 mM, by control-20 mM. Ascorbic acid induced catalase inhibition in the erythrocytes by diabetes mellitus increased by ascorbic acid concentration from 25 to 150 mM. [DHAA]/[AA]-ratio increased from 0.26 by control to 1.6 by diabetes mellitus and decreased to 0.44 after nicotinamide injections.

Amitrole↗
PubMedDate not supplied

[Superoxide dismutase and catalase activity in tracheobronchial secretions after surfactant treatment of newborn infants with respiratory distress syndrome].

Oxygen toxicity and mechanical ventilation are main factors in the development of chronic lung disease in preterm infants. We examined two antioxidant enzymes, superoxide dismutase (SOD) and catalase, in tracheal fluid of preterm infants with severe respiratory distress syndrome (RDS) treated with surfactant. SOD and catalase catalyse the transformation of oxygen radicals and hydrogen peroxide to less toxic metabolites. 31 preterm infants were randomised to either single or multiple dose treatment with surfactant (Curosurf). Tracheal aspirates were obtained during routine tracheal suctioning and the two enzymes were measured during the first week of life. 11 of 31 preterm babies (35%) did not show any SOD-activity in tracheal fluid. Four out of the eleven preterm infants developed bronchopulmonary dysplasia. Patients receiving multiple dose treatment had significantly higher SOD-activity (> 10 micrograms/mg albumin, p < 0.01) than patients with single dose treatment. Only 2 of 31 preterm babies (6%) lacked catalase activity in tracheal aspirate. 94% had catalase activity between 1 and 12 micrograms/mg albumin. We conclude that, the majority of preterm infants with severe RDS do not have protective superoxide dismutase activity in tracheal fluid. Following multiple dose surfactant replacement significantly higher SOD activity was observed as compared to single dose therapy.

Biological Products↗
PubMed2000

The role of HNF-1alpha in controlling hepatic catalase activity.

Mice deficient in hepatocyte nuclear factor 1alpha (HNF-1alpha) develop Laron dwarfism and non-insulin-dependent diabetes mellitus (Lee et al., 1998). Oxidative stress was present in the diabetic HNF-1alpha-null mice. To understand the mechanism underlying the oxidative stress in HNF-1alpha-null mice, we examined whether HNF-1alpha deficiency affects the integrity of the cellular defense system against oxidative stress. The glutathione level and activities of superoxide dismutase and glutathione reductase in liver and other tissues examined were not affected by HNF-1alpha deficiency. However, activities of cytosolic glutathione peroxidase and catalase, two enzymes responsible for detoxification of hydrogen peroxide within cells, were reduced specifically in liver of HNF-1alpha-null mice. The mRNA and protein levels of hepatic catalase in HNF-1alpha-null mice did not differ from those in normal mice. The loss of hepatic catalase activity in HNF-1alpha-null mice is probably caused by an insufficient heme pool in liver cells, because the mRNA level of ferrochelatase, the enzyme that catalyzes the last step of heme biosynthesis, was significantly reduced in liver, and the daily hemin treatment restored partial catalase activity in liver of HNF-1alpha-null mice. Furthermore, our results of cell transfection and luciferase reporter assay indicated that the mouse ferrochelatase promoter could be trans-activated directly by HNF-1alpha.

Aging↗
PubMed1975

The favourable effect of adding a catalase to the treatment of syndromes due to intervertebral disc degenerations.

Over a period of one year, 648 patients suffering from 4 different but very resistant syndromes due to intervertebral disc degenerations of the cervical and lumbosacral spine were treated in an identical way, but 50% of them received also catalase (Optidase¿) injections. Half of each group were males and half of them females, the age being 30--50 years. Catalase accelerates the recovery already within the first 3 weeks and the final results after 24 weeks are still significant. In addition, the study of the ischial syndrome was extended to a group of 1208 patients over a period of 5 years, confirming again the favourable effect of catalase. Catalase is generally well tolerated; dangerous reactions have not been noticed.

Adult↗