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PubMed1983

Morphometric cytochemistry of catalase and myeloperoxidase-containing granules in the rabbit polymorphonuclear leukocyte.

Recently developed morphometric and statistical techniques were applied to the study of heterogeneity of the granule population of rabbit polymorphonuclear leukocytes. The cytochemical activities of myeloperoxidase and catalase were differentiated by incubation at pH 7.6, and pH 9.7 to 10.5, respectively. Each activity was found in more than one granule. Statistical evaluation suggested that in addition to the primary granule, two myeloperoxidase-containing granules and two catalase-containing granules existed. Although the presence of catalase activity has been described in the immature polymorphonuclear leukocyte previously, this is the first report indicating cytochemical reactivity in mature polymorphs.

Animals↗
PubMed1995

Antioxidant defence mechanism of the skin against UV irradiation: study of the role of catalase using acatalasaemia fibroblasts.

To clarify the role of catalase, an antioxidant enzyme, in response to UV irradiation, we compared the effects of irradiation on cytotoxicity, activities of antioxidant enzymes, total glutathione concentrations, lipid peroxidation and the rate of collagen synthesis in skin fibroblasts from a patient with acatalasaemia and in those from a normal individual. The cells were irradiated with UVA (6 and 12 J/cm2 or UVB (0.5 and 1 J/cm2). Cell survival curves after UV irradiation were similar in cells from both subjects. Although superoxide dismutase activity in acatalasaemia cells was higher than in the control cells before irradiation, after irradiation the activity decreased in acatalasaemia cells (76% with 12 J/cm2 UVA, 47% with 1 J/cm2 UVB), but remained unchanged in control cells. Total glutathione concentrations also decreased in acatalasaemia cells (60% with 12 J/cm2) in response to UVA irradiation, but remained unchanged in control cells. Lipid peroxidation did not increase significantly in either cell type. The rate of collagen synthesis decreased to a similar extent in response to UV exposure in the two cell types (60-80% with 8.2 J/cm2 UVA, 40-50% with 10 mJ/cm2 UVB). We conclude from the results of cytotoxicity and lipid peroxidation that although acatalasaemia cells were killed by hydrogen peroxide at low concentrations with a single UV exposure, catalase functions only to a small degree as an antioxidant enzyme. There remains the possibility, however, that a deficiency of catalase may chronically damage the skin resulting in a reduced defence function of superoxide dismutase and glutathione with repeated exposures to UV, which is becoming more common in our daily life.

Acatalasia↗
PubMed1985

Post-irradiation inactivation, protection, and repair of the sulfhydryl enzyme malate synthase. Effects of formate, superoxide dismutase, catalase, and dithiothreitol.

Malate synthase from baker's yeast, a trimeric sulfhydryl enzyme with one essential sulfhydryl group per subunit, was inactivated by 2 kGy X-irradiation in air-saturated aqueous solution (enzyme concentration: 0.5 mg/ml). The radiation induced changes of enzymic activity were registered at about 0, 30, 60 h after irradiation. To elucidate the role of OH., O-.2, and H2O2 in the X-ray inactivation of the enzyme, experiments were performed in the absence or presence of different concentrations of specific additives (formate, superoxide dismutase, catalase). These additives were added to malate synthase solutions before or after X-irradiation. Moreover, repairs of inactivated malate synthase were initiated at about 0 or 30 h after irradiation by means of the sulfhydryl agent dithiothreitol. Experiments yielded the following results: Irradiation of malate synthase in the absence of additives inactivated the enzyme immediately to a residual activity Ar = 3% (corresponding to a D37 = 0.6 kGy), and led to further slow inactivation in the post-irradiation phase. Repairs, initiated at different times after irradiation, restored enzymic activity considerably. The repair initiated at t = 0 led to Ar = 21%; repairs started later on resulted in somewhat lower activities. The decay of repairability, however, was found to progress more slowly than post-irradiation inactivation itself. After completion of repair the activities of repaired samples did not decrease significantly. The presence of specific additives during irradiation caused significant protective effects against primary inactivation. The protection by formate was very pronounced (e.g., Ar = 72% and D37 = 6 kGy for 100 mM formate). The presence of catalytic amounts of superoxide dismutase and/or catalase exhibited only minor effects, depending on the presence and concentration of formate. Both the presence of specific additives during irradiation and the addition of additives after irradiation may alter the post-irradiation inactivation. Catalase turned out to be the most potent inhibitor of post-irradiation inactivation; superoxide dismutase showed an ambivalent behaviour, it accelerated or impeded post-irradiation inactivation; formate, when added after irradiation, exhibited a moderate protective effect. The presence of specific additives, added before and/or after irradiation, influenced the repair behaviour to some extent. The highest activity achieved by repair amounted to about 90% of the activity of the corresponding unirradiated sample. The percentual gain of activity was found to be the greater the lower the residual activity of the enzyme was before initiation of repair.(ABSTRACT TRUNCATED AT 400 WORDS)

Catalase↗
PubMed1985

Establishment of mouse cell lines homozygous for temperature-sensitive mutation in catalase gene.

Contact-inhibited and-transformed fibroblast cell lines have been established from the homozygous C3H/CSb mutant mouse. These cell lines have low levels of a temperature-sensitive catalase enzyme activity. When compared to wild-type C3H cells, the catalase-deficient cells are markedly more sensitive to the toxicity of hydrogen peroxide. Furthermore, this cellular sensitivity to external hydrogen peroxide is temperature sensitive. These cell lines will be of use in the study of the role which catalase plays in the intracellular prevention of transformation induced by oxidative stress.

Acatalasia↗
PubMed1991

The effect of superoxide dismutase and catalase on myocardial reperfusion injury in the isolated rat heart.

This study was designed to evaluate the efficacy of superoxide dismutase (SOD) and catalase on ischemic and reperfusion injury in the isolated working rat heart. The temperature and duration of ischemia varied under three conditions: 1) at 37 degrees C for 35 minutes, 2) at 28 degrees C for 120 minutes and 3) at 20 degrees C for 120 minutes. SOD (100 mg/L) and catalase 10 mg/L) were either added to St. Thomas' Hospital cardioplegic solution during ischemia (CP group) or to the reperfusion solution for 10 minutes after reflow (RS group). They were compared with a control group which received no free radical scavengers. The postischemic recovery ratio of cardiac functions were markedly superior to the values of the control group with a significant difference being noted in the CP and RS groups under ischemia at 37 degrees C and 28 degrees C. In the series done at 20 degrees C, a significant improvement was seen in the RS group, and the CP group also showed better functional recovery rates compared with the control group, although the differences were not statistically significant. Thus, SOD and catalase added to the cardioplegic solution or reperfusion fluid demonstrated an excellent protective effect on the myocardium against ischemic or reperfusion injury in both hypothermic ischemia and normothermia.

Animals↗
PubMed1996

Anomalous phylogenies based on bacterial catalase gene sequences.

Phylogenies based on nine prokaryotic catalase sequences demonstrate no relationship to phylogenies based on rDNA sequences or other known criteria. When this observation is considered together with the monophyletic relationship observed for eukaryotic catalase sequences, it seems likely that the catalase gene sequence has migrated repeatedly from eukaryotes to prokaryotes.

Bacteria↗
PubMed2000

Effects of microbial metabolites on catalase activity and growth of Staphylococcus aureus 6538 P.

The effects of cell extracts and supernatants of Lactobacillus spp. and Corynebacterium spp. on catalase activity and growth of Staphylococcus aureus 6538 P were studied. Intra- and extracellular metabolites of lactobacilli and corynebacteria inhibited catalase activity of S. aureus 6538 P. The growth of S. aureus 6538 P decreased after incubation with lactobacillus metabolites. The inhibitory effect of intra- and extracellular metabolites of lactobacilli and corynebacteria on catalase activity of S. aureus is a possible pathway of microbial interrelations responsible for the formation and/or development of microbial biocenoses.

Catalase↗
PubMed1995

Induction of peroxisome proliferation and increase of catalase activity in yeast, Candida albicans, by cadmium.

The effects of cadmium on the growth rate, catalase activity, and peroxisome proliferation in yeast, Candida albicans, were evaluated. The yeast growth was markedly inhibited by 1 mM cadmium at the initial hours. The toxic effect of cadmium on the cell growth persisted. The catalase activity of the cells treated with 1 mM Cd2+ first decreased, and then rose at 24 h to about 2.6 times that of the controls. The average number of peroxisomes per cell in the yeast treated with 1 mM Cd2+ was about sixfold higher than the control groups. The proliferation of peroxisomes and the increase of catalase activity following cadmium toxicity gives credence to the hypothesis that cadmium toxicity is related to its potential to induce oxidative stress in cells.

Cadmium↗
PubMed1991

Characterization of catalase-negative mutants of methylotrophic yeast Hansenula polymorpha.

Three recently isolated catalase-negative mutants of Hansenula polymorpha lost the ability to grow on methanol but grew in media containing glucose, ethanol or glycerol. Their incubation in a medium with methanol resulted in an accumulation of hydrogen peroxide and cell death. During growth of a catalase-negative mutant in chemostat on a mixture of methanol and glucose, neither H2O2 accumulation nor cell death were observed up to the molar ratio of 10:1 of the two substrates. Cytochrome-c peroxidase and NADH-peroxidase activities were detected in the cells. In methylotrophic yeasts, catalase seems to be an enzyme characteristic of the metabolism of methanol but not needed for the metabolism of multicarbon substrates. The hydrogen peroxide produced during growth of the mutants on mixed substrates is detoxified by cytochrome-c peroxidase and other peroxidases.

Catalase↗
PubMed2000

Interaction of nitric oxide with the oxygen evolving complex of photosystem II and manganese catalase: a comparative study.

We compare the interaction of nitric oxide with the S states of the oxygen evolving complex (OEC) of photosystem II and the dinuclear Mn cluster of Thermus thermophilus catalase. Flash fluorescence studies indicate that the S3 state of the OEC in the presence of ca. 0.6 mM NO is reduced to the S1 with an apparent halftime of ca. 0.4 s at about 18 degrees C, compared with a biphasic decay, with approximate halftimes of 28 s for S3 to S2 and 140 s for S2 to S1 in the absence of NO. Under similar conditions the S2 state is reduced by NO to the S1 state with an approximate halftime of 2 s. These results extend a recent study indicating a slow reduction of the S1 state at -30 degrees C, via the S0 and S(-1) states, to a Mn(II)-Mn(III) state resembling the corresponding state in catalase. The reductive mode of action of NO is repeated with the di-Mn cluster of catalase: the Mn(III)-Mn(III) redox state is reduced to the Mn(II)-Mn(II) state via the intermediate Mn(II)-Mn(III) state. The kinetics of this reduction suggest a decreasing reduction potential with decreasing oxidation state, similar to what is observed with the active states of the OEC. What is unique about the OEC is the rapid interaction of NO with the S3 state of the OEC, which is compatible with a metalloradical character of this state.

Catalase↗
PubMed1998

Adenovirus-mediated catalase gene transfer reduces oxidant stress in human, porcine and rat pancreatic islets.

Susceptibility of pancreatic islets to oxidant stress may affect islet viability and contribute to primary non function of allo- or xenogenic grafts. We investigated the influence of overexpression of catalase (CAT) on the viability of human, porcine and rat islets, as well as INS-1 beta-cell line. Islets were transfected with a replication-deficient adenovirus vector containing human CAT cDNA under the control of the adenovirus major late promoter (AdCAT) or a vector containing no foreign gene (AdNull) and used as a control. Oxidant stress was induced 48 h later by xanthine oxidase-hypoxanthine (XO 25 mU/ml, HX 0.5 mmol/l) or hydrogen peroxide (100 or 250 micromol/l). Islet cell viability was assessed 72 h after CAT transfer by 4-[3-(4-Idophenyl)-2-(4 nitrophenyl)-2H-5-tetrazolio]-1,2,benzene disulphonate (WST-1) test. Baseline catalase activity was three to fourfold lower in porcine than in human islets. CAT activity was reproducibly increased 2.5- to 7-fold in AdCAT infected islets, at least for 13 days. Overall, AdCAT conferred on human and pig islets a protection of 26.1 +/- 6.1 and 21.2 +/- 9.8% on XOHX injury and 35.4 +/- 4.2 and 57.9 +/- 10.5% on H2O2 stress. Similarly, rat islet cells and INS-1 cells were protected on XOHX stress by 17.8 +/- 2.3 and 30.8 +/- 8.7%, respectively. AdNull had no effect. Basal and stimulated insulin secretion was preserved in AdCAT-transfected human islets despite a XOHX challenge. This study validates adenovirus-mediated catalase gene transfer as a realistic approach to reduce non specific inflammation effects on human or porcine islet grafts. Moreover the relevance of defense mechanisms, previously suggested in human islets, is here illustrated in porcine islets.

Adenoviridae↗
PubMed1998

Glutathione, glutathione-related enzymes, and catalase activities in the earthworm Eisenia fetida andrei.

The aim of this work was to provide basic data on the antioxidant defences in the annelid Eisenia fetida andrei (E. f. a.). Methods for measurement of three antioxidant enzymes-catalase (CAT), glutathione peroxidase (GPX), and glutathione reductase (GR)-and of glutathione-S-transferase (GST) were optimized. GPX activity differed according to the substrate used: cumene hydroperoxide (CUOOH) or hydrogen peroxide (H2O2). The effects on the enzyme activities of storage up to 2 months at -80 degrees C, -20 degrees C, and +4 degrees C were evaluated. The subcellular distribution (in cytosol, mitochondrial, and microsomal fractions) was examined. The properties and subcellular distribution of the enzymes and glutathione were also characterized in dissected tissues and body fluids. The GR activity decreased at -80 degrees C and was the only one not stable at this temperature. The four enzymes were localized mainly in the cytosolic fraction. CAT distribution was unusual as it was not associated with peroxisomes, its properties being consistent with a catalase-peroxidase, rather than a true catalase. However, this result could also be an artifact linked to the use of an inappropriate method to obtain the fractions. Our observations indicate the presence of a distinct cytosolic selenium-dependent GPX (Se-GPX), and of a possible microsomal Se-GPX. A strong non-Se-GPX activity was measured in the CF and CL, which could be linked to the peroxidase activity of fetidins secreted by coelomocytes and with the ROS production of these cells. This study seems to indicate that E. f. a. is well equipped for the metabolism of electrophilic and pro-oxidants through glutathione.

Animals↗
PubMed1997

Selection of biochemical mutants of Aspergillus niger with enhanced catalase production.

The production of extracellular catalase in a submerged culture by a number of biochemical mutants has been evaluated. Eight of these mutants showed increased extracellular catalase, the level of which ranged widely in individual cases from 44% to over 94% in comparison with the parental strain. Studies of the relationship between a criterion of selection and the frequency of mutation showed that the highest frequency of positive mutations (15.8% and 24.2%) was obtained with respect to mutants resistant to ethidium bromide (1 mmol/l) and sodium gluconate (45%) respectively. The time course of growth and enzyme production by the most active mutant, AM-20, showed extra- and intracellular catalase activities increasing about 2- and 2.6-fold respectively, compared with the parental strain.

Aspergillus niger↗
PubMed1998

Differential role of catalase and glutathione peroxidase in cultured human fibroblasts under exposure of H2O2 or ultraviolet B light.

The purpose of this study was to elucidate the differential contribution of catalase and glutathione peroxidase (GSH-Px) to H2O2 scavenging in cultured human dermal fibroblasts. Responses of the cells in terms of both enzyme activities were examined by using two sorts of inhibitors, 3-amino-1H-1,2,4-triazole (AT) for catalase and DL-buthionine-[S,R]-sulfoximine (BSO) for GSH-Px, under exposure to H2O2 or ultraviolet (UV) B radiation. AT treatment resulted in a decrease in H2O2 scavenging activity, while BSO treatment did not affect H2O2 scavenging. When fibroblasts were exposed to a low concentration of H2O2 (100 microM). AT treatment resulted in a significant decrease in cell survival, but BSO treatment did not affect survival. At higher concentrations of H2O2 ranging from 500 microM to 1 mM, BSO-treated fibroblasts showed reduced survival. In addition, AT treatment was much more cytotoxic in the presence of UVB than BSO treatment. The intracellular levels of H2O2 in fibroblasts treated with AT or BSO were also determined. BSO-treated cells showed similar H2O2 levels to control cells, but the intracellular H2O2 levels of AT-treated fibroblasts were 1.4-fold higher than found in control cells. These results with human dermal fibroblasts indicate that catalase acts as a primary defence against oxidative stress from exogenous or endogenous H2O2 at low concentrations. In contrast, GSH-Px helps protect the cell from damage during exposure to high concentrations of H2O2.

Amitrole↗
PubMed2001

Hyperbaric oxygenation pretreatment induces catalase and reduces infarct size in ischemic rat myocardium.

Ischemia-reperfusion injury is a major complication occurring in heart stroke, cardiopulmonary bypass surgeries, and heart transplantation. Reactive oxygen species generated during the reperfusion phase overwhelm the scavenging capacities of antioxidant enzymes, and result in oxidative damage to the myocardium. We examined whether hyperbaric oxygenation (HBO) pretreatment induces antioxidant enzymes and protects the heart from subsequent ischemia-reperfusion injury. Rats were intermittently exposed to 100% O2 at 3 ATA (where ATA is absolute atmosphere) for 1 h daily and then sacrificed after 24 h of recovery in room air. Isolated hearts were subjected to 40 min of ischemia and 90 min of reperfusion. HBO pretreatment was found to condition the heart and enhance enzymatic activity and gene expression of catalase, thereby significantly reducing infarct size after reperfusion. A catalase inhibitor, 3-amino-1,2,4-triazole, completely abolished the infarct-limiting effect of HBO pretreatment, which suggests that HBO-induced tolerance against ischemia-reperfusion injury is due to catalase induction. Our results imply that HBO preconditioning may be developed as a new preventive measure for reperfusion injury in the heart.

Amitrole↗
PubMed2004

Catalase and alternative oxidase cooperatively regulate programmed cell death induced by beta-glucan elicitor in potato suspension cultures.

In potato (Solanum tuberosum L.) suspension cells, the expression of the gene encoding alternative oxidase (AOX) and H2O2 accumulation were induced by treatment with beta-glucan elicitor. The inhibition of catalase activity enhanced both AOX mRNA expression and the production of H2O2, whereas the ascorbate peroxidase inhibitor did not have any effect on these responses. Simultaneous inhibition of catalase and AOX activities in elicited cells dramatically increased H2O2 accumulation, leading to the disruption of mitochondrial membrane potential (deltapsi(m)) and programmed cell death (PCD). The results demonstrate, for the first time, that not only AOX but also catalase plays a central role in the suppression of mitochondrial deltapsi(m) breakdown and PCD induced by beta-glucan elicitor.

Apoptosis↗
PubMed2004

The bacterial catalase from filarial DNA preparations derives from common pseudomonad contaminants and not from Wolbachia endosymbionts.

Wolbachia are obligatory endosymbionts in many species of filarial nematodes. Certain bacterial molecules induce antibody responses in mammalian hosts infected with filariae, while others activate inflammatory responses that contribute to pathology. These findings, coupled with antibiotic studies demonstrating the dependence of filarial embryogenesis on the presence of Wolbachia, have intensified research on Wolbachia-nematode interactions, and the effects of Wolbachia molecules on the mammalian immune system. By amplification and sequencing of 16S rDNA and catalase sequences, we show that filarial DNA samples prepared from nematodes collected under typical conditions are frequently contaminated with Pseudomonas DNA. Analysis of a published DNA fragment containing a catalase attributed to the Wolbachia of Onchocerca volvulus showed it to be most like Pseudomonas, both in terms of sequence similarity and genomic organization. Additionally, there was no obvious catalase in either of two available Wolbachia genome sequences. Contamination of filarial DNA with bacterial sequences other than Wolbachia can complicate studies of the role of these symbionts in filarial biology.

Animals↗
PubMed1984

Effects of molecular oxygen on detection of superoxide radical with nitroblue tetrazolium and on activity stains for catalase.

The usual method of staining polyacrylamide gel electropherograms for superoxide dismutase activity utilizes a photochemical flux of O2- to reduce nitroblue tetrazolium. Superoxide dismutases intercept O2-, preventing formazan production and thus causing achromatic bands. In the presence of H2O2, catalases also yield achromatic bands during this staining procedure. This is due to local elevation of pO2 by the catalatic decomposition of H2O2. O2, in turn, inhibits the reduction of the tetrazolium by O2-. This phenomenon provides a new activity stain for catalase. A previously described activity stain for catalase has also been reexamined and significantly improved.

3,3'-Diaminobenzidine↗