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PubMed1984

Molecular cloning of cDNA for rat liver catalase.

For the studies on the induction of peroxisomal enzymes by hypolipidemic agents, we have tried to isolate a cDNA clone for rat liver catalase. A recombinant clone, pMJ501, was isolated, of which cDNA insert specifically hybridized to catalase mRNA in hybridization-selected translation. On RNA blot hybridization, it hybridized to 2.4-kilobases RNA which was increased about 1.5-fold by the administration of di-(2-ethylhexyl)phthalate to the rats. The nucleotide sequence of the cDNA contains a reading frame for 109 amino acid residues which match the reported amino acid sequence of bovine liver catalase at the carboxyl end with 82% homology. It is concluded that pMJ501 contains a cDNA sequence for rat liver catalase.

Amino Acid Sequence↗

PubMed1984

Activity of peroxisomal enzymes and intracellular distribution of catalase in Zellweger syndrome.

The activity of peroxisomal enzymes was studied in human liver and cultured human skin fibroblasts in relation to the finding (Goldfischer, S. et al. (1973) Science 182, 62-64) that morphologically distinct peroxisomes are not detectable in patients with the cerebro-hepato-renal (Zellweger) syndrome. In homogenates of liver from the patients, dihydroxyacetone phosphate acyltransferase, a membrane-bound peroxisomal enzyme, is deficient (Schutgens, R.B.H., et al. (1984) Biochem. Biophys. Res. Commun. 120, 179-184). In contrast, there is no deficiency of the soluble peroxisomal matrix enzymes catalase, L-alpha-hydroxyacid oxidase and E-aminoacid oxidase. Catalase is also not deficient in homogenates of cultured skin fibroblasts from the patients. The results of digitonin titration experiments showed that in control fibroblasts at least 70% of the catalase activity is present in subcellular particles distinct from mitochondria or lysosomes. In contrast, all of the catalase activity in fibroblasts from Zellweger patients is found in the same compartment as the cytosolic marker enzyme lactate dehydrogenase.

Acyltransferases↗

PubMed2002

Identification of catalase in human livers as a factor that enhances phenytoin dihydroxy metabolite formation by human liver microsomes.

We have reported previously that the formation of a 3',4'-dihydroxylated metabolite of phenytoin (3',4'-diHPPH) by human liver microsomal cytochrome P450 (P450) is enhanced by the addition of human liver cytosol [Komatsu et al., Drug Metab Dispos 2000;28:1361-8]. The enhancing factor was determined in this study. The addition of cytosolic proteins precipitated by 50% ammonium sulfate to incubation mixtures increased the rate of microsomal 3',4'-diHPPH formation. This fraction was separated further by diethylaminoethyl-, carboxymethyl-, and hydroxyapatite-column chromatography. The amino acid sequence of the purified protein of approximately 55kDa by electrophoresis revealed this protein to be a catalase. The addition of purified or authentic catalase to the incubation mixtures increased the rates of microsomal 3',4'-diHPPH formation from 3'- and 4'-hydroxylated metabolites and from phenytoin in a concentration-dependent manner. In reconstituted systems containing CYP2C9, CYP2C19, and CYP3A4, the formation of 3',4'-diHPPH was also enhanced by catalase to different extents. This is the first report that catalase in livers enhances drug oxidation activities catalyzed by P450 in human liver microsomes.

Catalase↗

PubMed2001

The influence of oxidative stress on catalase and MnSOD gene transcription in astrocytes.

The brain is particularly vulnerable to oxygen free radicals, which have been implicated in the pathology of several neurological disorders. The antioxidant enzyme (AOE) system of the brain may play an important role in the protection against such oxidative stress. We investigated the influence of oxidative stress on the transcription of catalase and MnSOD mRNA. Primary rat astroglial cell cultures were treated either with hydrogen peroxide (H2O2), as a direct mediator of oxidative stress, or with the redox cycling compound paraquat. Both substances led to an increase of catalase and MnSOD mRNA levels. To further elucidate the mechanisms residing behind this increase, transfection experiments were performed. Transient transfection of primary astroglial cells with a reporter plasmid containing the upstream region of the catalase gene showed a decrease in reporter gene activity after exposure of transfected cells to either H2O2 or paraquat. In contrast, transfection experiments done with reporter plasmids for the MnSOD upstream region resulted in an increase of reporter gene activity after H2O2 as well as after paraquat treatment of transfected cells. These results indicate transcriptional regulation of MnSOD and post-transcriptional regulation of catalase gene expression after oxidative stress in primary rat astrocytes.

Animals↗

PubMed2000

Fully-automated spectrophotometric method for measurement of antioxidant activity of catalase.

OBJECTIVES: Develop fully automated assay of antioxidant catalatic activity of catalase. DESIGN AND METHODS: The assay is based on standard, clinical chemistry automated analyzer methods for measuring hydrogen peroxide by using the Trinder reagent. Catalase competes with 324 U/L horseradish peroxidase (type XII) and Trinder reagent for hydrogen peroxide produced by 46 U/L uricase action on urate. Unit activity is defined as 50% inhibition of maximal color development. RESULTS: Within-run coefficients of variation (cv) were 2% for standards and samples, whereas between-run cv was 3.1% for standards and 7.3% for samples. Dilutional parallelism and linearity were demonstrated for 8-fold dilutions of samples over the range 0.1 to 1.1 U/mL. Recovery of added catalase was complete. Samples are stable to freezing and storage for 1 week at -80 degrees C. Activities (units/mL) ranged from 0.29 to 0.41 in human and canine plasma, and for erythrocytes from 48 to 70 in man, 17 to 19 in dogs, and 60 to 89 in rats. Rat liver activity (units/g wet weight) was age-dependent and ranged from 17 to 24 at 2 months, and from 19 to 37 at 6 months. CONCLUSION: The first, fully automated assay for the measurement of catalatic activity of catalase in plasma, erythrocytes, and liver is demonstrated for multiple species. The assay is simple, precise, relatively inexpensive, and rapid.

Animals↗

PubMed2000

Distinctive properties of the catalase B of Aspergillus nidulans.

Aspergillus nidulans catalase B (CatB) was purified to homogeneity and characterized as a hydroperoxidase which resembles typical catalases in some physicochemical characteristics: (1) it has an apparent molecular weight of 360000 and is composed of four glycosylated subunits, (2) it has hydrophobic properties as revealed by extractability in ethanol/chloroform and binding to phenyl-Superose, and (3) it has an acidic isoelectric point at pH 3. 5. Also CatB exhibits some distinctive properties, e.g. it is not inhibited by the presence of 2% sodium dodecyl sulfate, 9 M urea or reducing agents. Furthermore, even though CatB does not exhibit any residual peroxidase activity, it is able to retain up to 38% of its initial catalase activity after incubation with the typical catalase inhibitor 3-amino-1,2,4-triazole.

Amitrole↗

PubMed2001

Haemonchus contortus utilises catalase in defence against exogenous hydrogen peroxide in vitro.

The toxicity of activated oxygen species towards adult Haemonchus contortus nematodes was examined in in vitro assays using ingestion of [3H]inulin to assess nematode viability. Both glucose/glucose oxidase (generation of hydrogen peroxide) and xanthine/xanthine oxidase (generation of superoxide anion) systems showed concentration-dependent toxicity to the nematodes. Both adult and larval Haemonchus contortus enzyme preparations showed significant catalase activities. Adult nematodes exposed to aminotriazole for 24 h showed catalase activities reduced to less than 20% of controls. Aminotriazole-treated nematodes exposed to a glucose/glucose oxidase system were significantly more susceptible to the toxic effects of the oxidant-generating system than controls (no aminotriazole pre-treatment). The concentration of glucose oxidase required to inhibit feeding by 50% was decreased 33-fold in aminotriazole-treated nematodes compared with controls. The effect of aminotriazole pre-treatment implicates hydrogen peroxide as a significant toxic agent in the glucose/glucose oxidase system. It is apparent that inhibition of Haemonchus contortus catalase increases the susceptibility of the parasite to the toxic effects of hydrogen peroxide, demonstrating a protective role for this enzyme. This suggests that catalase has the potential to play a significant role in the defence of this parasite against hydrogen peroxide produced as part of the respiratory burst of activated phagocytes within the host during its response to nematode infection.

Amitrole↗

PubMed2003

Cardiac-specific overexpression of catalase rescues ventricular myocytes from ethanol-induced cardiac contractile defect.

Oxidative stress is intimately involved in alcoholic cardiomyopathy. Catalase is responsible for detoxification of hydrogen peroxide (H(2)O(2)) and may interfere with ethanol-induced cardiac toxicity. To test this hypothesis, a transgenic mouse line was produced to overexpress catalase (~50-fold) in the heart, ranging from sarcoplasm, the nucleus and peroxisomes within myocytes. Mechanical and intracellular Ca(2+) properties were evaluated in ventricular myocytes from catalase transgenic (CAT) and wild-type FVB mice. Protein abundance of sarco (endo) plasmic reticulum Ca(2+)-ATPase (SERCA), phospholamban (PLB), Na(+)/Ca(2+) exchanger (NCX), dihydropyridine Ca(2+) receptor (DHPR), ryanodine receptor (RyR), Akt and phosphorylated Akt (pAkt) were measured by western blot. CAT itself did not alter body and organ weights, as well as myocyte contractile properties. Acute exposure of ethanol elicited a concentration-dependent depression in cell shortening and intracellular Ca(2+) in FVB mice with maximal inhibitions of 65.4% and 35.8%, respectively. The ethanol-induced cardiac depression was significantly attenuated in myocytes from CAT with maximal inhibitions of 42.4% and 27.3%. CAT also abrogated the ethanol-induced inhibition of maximal velocity of shortening/relengthening, prolongation of relengthening duration and intracellular Ca(2+) clearing time. Cell shortening at different extracellular Ca(2+) revealed stronger myocyte-shortening amplitude under lower (0.5 mM) Ca(2+) in CAT mice. Protein expression of NCX, RyR, Akt and pAkt were elevated in myocytes from CAT mice, while those of SERCA, PLB and DHPR were not affected. In conclusion, our data suggest that catalase overexpression may protect cardiac myocytes from ethanol-induced contractile defect, partially through improved intracellular Ca(2+) handling and Akt signaling.

Animals↗

PubMed1985

Involvement of hydrogen peroxide and hydroxyl radical in the 'oxygen paradox': reduction of creatine kinase release by catalase, allopurinol or deferoxamine, but not by superoxide dismutase.

The objective of this study was to test the hypothesis that cytotoxic oxygen metabolites participate in lytic cardiac cell damage, detected as creatine kinase release, upon reoxygenation of hypoxic, isolated buffer-perfused hearts (oxygen paradox). Perfusate additives included: superoxide dismutase (30 mg/l); catalase (2 mg/l); deferoxamine (0.5 mM); and allopurinol (1 mM). Creatine kinase release upon reoxygenation was reduced, to levels not significantly different from nonhypoxic controls, by adding either catalase, allopurinol or deferoxamine to the buffer during hypoxia. Reduced creatine kinase leakage was not accompanied by parallel preservation of ventricular function or coronary vascular resistance. Administration of catalase during hypoxia was superior to administering it only during reoxygenation. Treatment with catalase during both hypoxia and reoxygenation provided no more protection than administration only during hypoxia. The data suggest that an important component of hypoxia-induced cardiac cell damage is due primarily to hydrogen peroxide, which may then form hydroxyl radical. Superoxide anion plays an important role as a precursor of these species, but added superoxide dismutase alone did not significantly reduce creatine kinase loss. The data also suggest that damage resulting in creatine kinase release upon reoxygenation occurs during oxygen deprivation, and it is mediated in part by cytotoxic oxygen metabolites.

Allopurinol↗

PubMed1995

Studies of hypoxemic/reoxygenation injury: without aortic clamping. VI. Counteraction of oxidant damage by exogenous antioxidants: N-(2-mercaptopropionyl)-glycine and catalase.

This study tests the hypothesis that antioxidants administered before reoxygenation can reduce oxygen-mediated damage and improve myocardial performance. Of 25 Duroc-Yorkshire piglets (2 to 3 weeks, 3 to 5 kg) five underwent 60 minutes of cardiopulmonary bypass without hypoxemia (control group), and five others underwent 30 minutes of hypoxemia on cardiopulmonary bypass with a circuit primed with oxygen tension about 25 mm Hg blood followed by reoxygenation on cardiopulmonary bypass (no treatment). In vitro studies were performed to obtain the optimal dosage of the antioxidants N-(2-mercaptopropionyl)-glycine and and catalase to be used in subsequent in vivo experimental studies; cardiac homogenates were incubated in 0 to 5 mmol/L concentrations of the oxidant t-butylhydroperoxide and malondialdehyde production was measured. Fifteen piglets were made hypoxemic on cardiopulmonary bypass for 30 minutes, and the antioxidants N-(2-mercaptopropionyl)-glycine at either 30 or 80 mg/kg body weight or N-(2-mercaptopropionyl)-glycine, 30 mg/kg body weight, and catalase, 50,000 U/kg body weight, were added to the cardiopulmonary bypass circuit 15 minutes before reoxygenation. Left ventricular contractility, which was expressed as end-systolic elastance, was measured by conductance catheter before hypoxemia and after reoxygenation. Myocardial antioxidant reserve capacity was determined after reoxygenation by incubating cardiac homogenates in the oxidant t-butylhydroperoxide and measuring subsequent malondialdehyde elution. The in vitro bioassay studies showed a dose-dependent reduction of lipid peroxidation with N-(2-mercaptopropionyl)-glycine, with maximal benefits of a 40% decrease and malondialdehyde elaboration occurring with N-(2-mercaptopropionyl)-glycine and catalase compared with untreated cardiac homogenates. Cardiopulmonary bypass (no hypoxemia) caused no oxidant damage or changes in contractile function after cardiopulmonary bypass. Reoxygenation without treatment raised conjugated diene levels 57%,* lowered antioxidant reserve capacity 51%,* and was associated with only 38%* recovery of contractile function (p < 0.05 vs control). In contrast, treatment with antioxidants avoided lipid peroxidation, maintained antioxidant reserve capacity, and resulted in a dose-dependent improvement in left ventricular contractility with complete recovery occurring in N-(2-mercaptopropionyl)-glycine and catalase-treated piglets (*p < 0.05 vs no treatment). This study confirms the occurrence of hypoxemic/reoxygenation injury in immature hearts placed on cardiopulmonary bypass and shows that biochemical and functional damage can be counteracted by adding antioxidants to the cardiopulmonary bypass priming fluid. Contractile function improved in a dose-dependent manner, and oxygen-mediated damage could be avoided by mercaptopropionyl glycine/catalase treatment.(ABSTRACT TRUNCATED AT 400 WORDS)

Alkadienes↗

PubMed1984

Effects of multiple doxorubicin doses on mouse cardiac and hepatic catalase.

Catalase activity was followed up in the hearts and livers of CD 1 mice treated with Doxorubicin 4 mg/Kg, i.v., weekly for 9 weeks. In this murine model the antiblastic induces cardiac morphological lesions which are progressively severer with the increase of the administered cumulative dose. Heart catalase showed a consistent elevation which reached a maximum (+116.2%, P less than 0.05) after the 5th dose. In the case of hepatic catalase no significant variation was observed except a transitory elevation following the first administration. The specific increase of heart catalase activity following multiple Doxorubicin doses could be an indicator that an enhanced free radical generation acts "in vivo" along with the onset of the cardiac lesions due to antiblastic.

Animals↗

PubMed2000

Hereditary catalase deficiencies and increased risk of diabetes.

Partial or near-total lack of erythrocyte catalase activity is a rare condition, generally thought to be benign. However, little is known of the frequency of common diseases of adult onset in human beings with catalase deficiency. We report that, in a series of Hungarian patients with catalase deficiency, there is a higher frequency of diabetes than in unaffected first-degree relatives and the general Hungarian population. We speculate that quantitative deficiency of catalase might predispose to cumulative oxidant damage of pancreatic beta-cells and diabetes.

Acatalasia↗

PubMed1996

Peroxidatic degradation of azide by catalase and irreversible enzyme inactivation.

A study of the azide reaction with bovine liver catalase in presence of hydrogen peroxide has been performed, using conventional UV-visible spectrometry and activity measurements. Compound III and NO-ferrocatalase were the predominant forms of the enzyme observed in air and under nitrogen, respectively. A reaction scheme for peroxidatic degradation of azide by catalase is proposed. Accordingly, accumulation of Compound III is the main factor responsible for the reversible inhibition of 'catalatic' activity by azide, while formation of a complex between native catalase and azide has a negligible effect. Catalase is irreversibly inactivated by prolonged exposure to high levels of H2O2 and azide. The latter involves cleavage of the prosthetic group with liberation of the heme iron. Both in air and under nitrogen, generation of azidyl radicals seems to play a minor role in the irreversible inactivation process.

Animals↗

PubMed2001

Thermo-alkali-stable catalases from newly isolated Bacillus sp. for the treatment and recycling of textile bleaching effluents.

Three thermoalkaliphilic bacteria, which were grown at pH 9.3-10 and 60-65 degrees C were isolated out of a textile wastewater drain. The unknown micro-organisms were identified as thermoalkaliphilic Bacillus sp. Growth conditions were studied and catalase activities and stabilities compared. Catalases from Bacillus SF showed high stabilities at 60 degrees C and pH 9 (t1/2=38 h) and thus this strain was chosen for further investigations, such as electron microscopy, immobilization of catalase and hydrogen peroxide degradation studies. Degradation of hydrogen peroxide with an immobilized catalase from Bacillus SF enabled the reuse of the water for the dyeing process. In contrast, application of the free enzyme for treatment of bleaching effluents, caused interaction between the denaturated protein and the dye, resulting in reduced dye uptake, and a higher color difference of 1.3DeltaE* of dyed fabrics compared to 0.9DeltaE* when using the immobilized enzyme.

Alkalies↗

PubMed2001

Targeting of superoxide dismutase and catalase to vascular endothelium.

Reactive oxygen species, such as superoxide anion (O2(-)) and H2O2, cause oxidative stress in endothelial cells, a condition implicated in the pathogenesis of many cardiovascular and pulmonary diseases. Antioxidant enzymes, superoxide dismutases (SOD, converting superoxide anion into H2O2) and catalase (converting H2O2 into water), are candidate drugs for augmentation of antioxidant defenses in endothelium. However, SOD and catalase undergo fast elimination from the bloodstream, which compromises delivery and permits rather modest, if any, protection against vascular oxidative stress. Coupling of polyethylene glycol (PEG) to the enzymes and encapsulating them in liposomes increases their bioavailability and enhances their protective effect. Chemical modifications and genetic manipulations of SOD and catalase have been proposed in order to provide more effective delivery to endothelium. For example, chimeric protein constructs consisting of SOD and heparin-binding peptides have an affinity for charged components of the endothelial glycocalix. However, the problem of developing a more effective and precise delivery of the drugs to endothelial cells persists. Endothelial surface antigens may be employed to provide targeting and subcellular addressing of drugs (vascular immunotargeting strategy). Thus, SOD and catalase conjugated to antibodies directed against the constitutively expressed endothelial antigens, angiotensin-converting enzyme (ACE) and adhesion molecules (ICAM-1 or PECAM-1), bind to endothelium in intact animals after intravascular administration, accumulate in the pulmonary vasculature, enter endothelial cells and augment their antioxidant defenses. Such immunotargeting strategies may provide secondary therapeutic benefits by inhibiting the function of target antigens. For example, blocking of ICAM-1 and PECAM-1 by carrier antibodies may attenuate inflammation and leukocyte-mediated vascular damage. Additional studies in animal models of vascular oxidative stress are necessary in order to more fully characterize potential therapeutic effects and limitations of targeting of antioxidant enzymes to endothelial cells.

Animals↗

PubMed1997

Effects of vitamins E, C and catalase on bromobenzene- and hydrogen peroxide-induced intracellular oxidation and DNA single-strand breakage in Hep G2 cells.

BACKGROUND/AIMS: Water-soluble vitamin E (Trolox C), ascorbic acid and catalase were shown in our previous study to protect isolated rat hepatocytes against bromobenzene-induced toxicity. METHODS: In order to study the mechanisms of this protection and the pathogenesis of bromobenzene-induced hepatocellular injury, a fluorometric assay for the investigation of intracellular oxidation, indicated by conversion of dichlorofluorescein diacetate to dichlorofluorescein, was used. Single-strand DNA breakage was also evaluated in Hep G2 cells by a radio-labelling method. RESULTS: Bromobenzene (2.4 and 4.8 mM) induced a significant increase in dichlorofluorescein fluorescence intensity compared to the controls. Trolox C, ascorbic acid or catalase significantly inhibited bromobenzene-induced enhancement of fluorescence intensity (p<0.05-0.001), as well as reduced auto-intracellular oxidation in untreated Hep G2 cells. Hydrogen peroxide (H2O2) evoked a dose-dependent increase in dichlorofluorescein fluorescence intensity in Hep G2 cells, and the effect was completely blocked by Trolox C (2.0 mM) and catalase (4800 unit/ml). Bromobenzene caused significant single-strand DNA breakage in Hep G2 cells during 2 h suspension incubation and 24 h primary incubation. H2O2 (400 microM) led to marked single-strand DNA breakage in 20 min, and the effect was attenuated by Trolox C. CONCLUSIONS: Metabolism of bromobenzene in Hep G2 cells induces production of H2O2, indicated by enhancement of dichlorofluorescein fluorescence intensity, or other free radicals, which leads to single-strand DNA breakage in the cells. Vitamins E and C and catalase display strong intracellular antioxidative effects. Vitamin E could partially inhibit H2O2-induced single-strand DNA breakage in the cells.

Antioxidants↗

PubMed1981

Inducible catalase in Pseudomonas fluorescens.

The catalase activity of a non-proliferating suspension of Pseudomonas fluorescens doubled after six hours incubation in a 50 mM phosphate buffer medium (pH 7.3). The same effect was observed in a peptone medium. The increased activity was due to induced enzyme synthesis, and not to activation of preexisting catalase. Induced catalase was separated by electrophoresis from deuterium labelled constitutive catalase. The enzyme was also induced under anaerobic conditions in phosphate buffer or in culture when nitrate was supplied as an electron acceptor. Induction was considerably increased by the addition of various nucleotides and amino acids to the incubation medium.

Amino Acids↗

PubMed2003

Hydrogen-peroxide-induced heme degradation in red blood cells: the protective roles of catalase and glutathione peroxidase.

Catalase and glutathione peroxidase (GSHPX) react with red cell hydrogen peroxide. A number of recent studies indicate that catalase is the primary enzyme responsible for protecting the red cell from hydrogen peroxide. We have used flow cytometry in intact cells as a sensitive measure of the hydrogen-peroxide-induced formation of fluorescent heme degradation products. Using this method, we have been able to delineate a unique role for GSHPX in protecting the red cell from hydrogen peroxide. For extracellular hydrogen peroxide, catalase completely protected the cells, while the ability of GSHPX to protect the cells was limited by the availability of glutathione. The effect of endogenously generated hydrogen peroxide in conjunction with hemoglobin autoxidation was investigated by in vitro incubation studies. These studies indicate that fluorescent products are not formed during incubation unless the glutathione is reduced to at least 40% of its initial value as a result of incubation or by reacting the glutathione with iodoacetamide. Reactive catalase only slows down the depletion of glutathione, but does not directly prevent the formation of these fluorescent products. The unique role of GSHPX is attributed to its ability to react with hydrogen peroxide generated in close proximity to the red cell membrane in conjunction with the autoxidation of membrane-bound hemoglobin.

Catalase↗