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PubMed2004

Catalase and superoxide dismutase: distribution, properties, and physiological role in cells of strict anaerobes.

This review considers the distribution of the main enzymes of antioxidative defense, superoxide dismutase (SOD) and catalase, in various groups of strictly anaerobic microorganisms: bacteria of the genus Clostridium, Bacteroides, sulfate-reducing and acetogenic bacteria, methanogenic archaea, etc. Molecular and biochemical properties of purified Fe-containing SODs, cambialistic SODs, and heme catalases are presented. The physiological role and origin of the enzymes of antioxidative defense in strict anaerobes are discussed. Physiological responses (induction of SOD and catalase) to factors provoking oxidative stress in the cells of strict anaerobes able to maintain viability under aerobic conditions are also considered.

Antioxidants↗
PubMed2002

Genetic association of the catalase gene (CAT) with vitiligo susceptibility.

Vitiligo susceptibility is a complex genetic trait that may involve genes important for melanin biosynthesis, response to oxidative stress, and/or regulation of autoimmunity, as well as environmental factors. We report here case-control and family-based association studies for the catalase gene (CAT) in vitiligo patients. The CAT gene was selected as a candidate gene because of the reduction of catalase enzyme activity (EC 1.11.1.6) and concomitant accumulation of excess hydrogen peroxide observed in the entire epidermis of vitiligo patients. One of three CAT genetic markers studied was found to be informative for genotypic analysis of Caucasian vitiligo patients and control subjects. Both case/control and family-based genetic association studies of the T/C single nucleotide polymorphism (SNP) in exon 9 of the CAT gene, which is detectable with the restriction endonuclease BstX I, suggest possible association between the CAT gene and vitiligo susceptibility. The observations that T/C heterozygotes are more frequent among vitiligo patients than controls and that the C allele is transmitted more frequently to patients than controls suggest that linked mutations in or near the CAT gene might contribute to a quantitative deficiency of catalase activity in the epidermis and the accumulation of excess hydrogen peroxide (H2O2). The CAT gene may, therefore, be a susceptibility gene in some vitiligo patients, further supporting the epidermal oxidative stress model for vitiligo pathogenesis.

Biomarkers↗
PubMed2004

Plasma catalase activity and malondialdehyde level in patients with cataract.

PURPOSE: Oxidative mechanisms play a major role in the aetiology and pathogenesis of cataract, especially in age-related cataract. Our study aims to investigate systemic oxidant and antioxidant markers in cataract patients. METHODS: The activity of erythrocyte catalase and the level of malondialdehyde in plasma were measured in 40 patients with cataract and 60 healthy control subjects. The malondialdehyde level, as an index of lipid peroxidation, was determined by thiobarbitüric acid reaction according to Yagi. The determination of catalase activity was measured by a method that was defined by Beutler. Catalase enzyme activity and malondialdehyde level were evaluated to find out whether there was a significant difference in these variables. Analysis of variance was used by forming a general linear model that takes age and gender as the covariate. RESULTS: CAT activity was found to be 13 920.2 +/- 847.9 U/l in cataract patients and 16 061.3 +/- 1126.6 U/l in control subjects. CAT activity in cataract patients was significantly lower than the control subjects (P = 0.008). Plasma MDA level is significantly higher in patients with cataract 4.47 +/- 0.35 nmol/ml compared to the control subjects 2.94 +/- 0.26 nmol/ml (P = 0.0001). There was no significant difference between different cataract subgroups when erythrocyte CAT activities and plasma MDA levels were compared (P = 0.322, 0.062). CONCLUSION: This study shows that oxidant/antioxidant balances alter in the presence of cataract.

Adult↗
PubMed2006

15d-Prostaglandin J2 activates peroxisome proliferator-activated receptor-gamma, promotes expression of catalase, and reduces inflammation, behavioral dysfunction, and neuronal loss after intracerebral hemorrhage in rats.

Peroxisome proliferator-activated receptor-gamma (PPARgamma) is a transcription factor that regulates the expression of various gene products that are essential in lipid and glucose metabolism, as well as that of the peroxisome-enriched antioxidant enzyme, catalase. Activation of PPARgamma is linked to anti-inflammatory activities and is beneficial for cardiovascular diseases. However, little is known about its role in intracerebral hemorrhage (ICH). 15-Deoxy-Delta(12,14)-prostaglandin J2 (15d-PGJ2) acts as a physiologic agonist for PPARgamma. In this study, we found that injection of 15d-PGJ2 into the locus of striatal hematoma increased PPARgamma-deoxyribonucleic acid (DNA) binding activity and the expression of catalase messenger ribonucleic acid (mRNA) and protein in the perihemorrhagic area. Additionally, 15d-PGJ2 significantly reduced nuclear factor-kappaB (NF-kappaB) activation and prevented neutrophil infiltration measured by myeloperoxidase (MPO) immunoassay, and also reduced cell apoptosis measured by terminal deoxynucleotide transferase dUTP nick-end labeling (TUNEL). In addition, 15d-PGJ2 reduced behavioral dysfunction produced by the ICH. Altogether, our findings indicate that injection of 15d-PGJ2 at the onset of ICH is associated with activation of PPARgamma and elevation of catalase expression, suppression of NF-kappaB activity, and restricted neutrophil infiltration. All these events predicted reduced behavioral deficit and neuronal damage.

Animals↗
PubMed2001

Catalase-like activity of horseradish peroxidase: relationship to enzyme inactivation by H2O2.

H2O2 is the usual oxidizing substrate of horseradish peroxidase C (HRP-C). In the absence in the reaction medium of a one-electron donor substrate, H2O2 is able to act as both oxidizing and reducing substrate. However, under these conditions the enzyme also undergoes a progressive loss of activity. There are several pathways that maintain the activity of the enzyme by recovering the ferric form, one of which is the decomposition of H2O2 to molecular oxygen in a similar way to the action of catalase. This production of oxygen has been kinetically characterized with a Clark-type electrode coupled to an oxygraph. HRP-C exhibits a weak catalase-like activity, the initial reaction rate of which is hyperbolically dependent on the H2O2 concentration, with values for K(2) (affinity of the first intermediate, compound I, for H2O2) and k(3) (apparent rate constant controlling catalase activity) of 4.0 +/- 0.6 mM and 1.78 +/- 0.12 s(-1) respectively. Oxygen production by HRP-C is favoured at pH values greater than approx. 6.5; under similar conditions HRP-C is also much less sensitive to inactivation during incubations with H2O2. We therefore suggest that this pathway is a major protective mechanism of HRP-C against such inactivation.

Catalase↗
PubMed1972

Formation of compound I by the reaction of catalase with peroxoacetic acid.

1. The formation of Compound I by the reactions of bacterial and ox liver catalases with peroxoacetic acid was examined. In both cases the process occurs almost entirely by reaction of catalase with un-ionized peroxoacetic acid molecules. The result suggests an important role for the bound peroxidic proton in the enzyme-substrate interaction. 2. The peroxidatic properties of the Compounds I formed when peroxoacetic acid was used were examined by studying the oxidations of ethanol and formate; the results closely resemble those previously reported when H(2)O(2) and alkyl hydroperoxides were used. 3. Compound I formed with bacterial catalase and peroxoacetic acid is remarkably stable in the absence of added donor and the preparation has considerable potential for detailed studies of the nature of this intermediate.

Acetates↗
PubMed1975

Optical measurement of the catalase-hydrogen peroxide intermediate (Compound I) in the liver of anaesthetized rats and its implication to hydrogen peroxide production in situ.

The spectrophotometric determination of the catalase-H2O2 intermediate (Compound I) was extended to the liver in situ in anaesthetized rats. The rate of H2O2 production was determined for the liver in situ with endogenous substrates, and in the presence of excess of glycollate. Glycollate infusion doubled H2O2 production rate in the liver of air-breathing rats, and caused a fourfold increase when rats breathed O2 at 1 times 10(5) Pa. Hyperbaric O2 up to 6 times 10(5) Pa did not increase H2O2 generation supported by endogenous substrates, nor did it increase H2O2 production above that produced by 1 times 10(5) Pa O2 in glycollate-supplemented rats. The rates of ethanol oxidation via hepatic catalase and via alcohol dehydrogenase in the whole body were separately measured. The contribution of hepatic catalase to ethanol oxidation was found to be approx. 10 percent in endogenous conditions and increased to 30 percent or more of the total ethanol oxidation in rats supplemented with glycolate.

Alcohol Oxidoreductases↗
PubMed1977

Regulation of maize catalase by changing rates of synthesis and degradation.

Rates of catalase synthesis and degradation were measured in the scutellum of the germinating maize seedling by the technique of Price, Sterling, Tarantola, Hartley & Rechcigl [J. Biol. Chem. (1963) 237, 3468-3475] by using the porphyrinogenic drug 2-allyl-2-isopropylacetamide to inhibit catalase synthesis. Results indicate that developmental changes in catalase activity are determined by changes in the rate of enzyme degradation as well as by changes in the rates of its synthesis.

Allylisopropylacetamide↗
PubMed1977

Tritium effect in peroxidation of ehtanol by liver catalase.

1. Simultaneous determination of the rate of appearance of 3H in water from [(1R)-1-3H1] ethanol and the rate of acetaldehyde formation in the presence of rat or ox liver catalase under conditions of steady-state generation of H2O2 allowed calculation of the 3H isotope effect. The mean value of 2.52 obtained for rat liver catalase at 37 degrees C and pH 6.3-7.7 was independent of both ethanol concentration and the rate of H2O2 generation over a wide range. At 25 degrees C a slightly lower mean value of 2.40 was obtained with the ox liver catalase. 2. Neither the product, acetaldehyde, nor 4-methylpyrazole influenced the two rates measured in the assay. 3. Relating the value obtained for the 3H isotope effect to a known value for the 2H isotope effect strongly supports the view that both values are close to the true isotope effect with the respective substituted compounds on the rate constant in the catalytic step involving scission of the C-H bond. 4. The constancy of the isotope effect under various conditions makes it possible to use it for interpretations in vivo. 5. It was established that beta-D-galactose dehydrogenase exhibits B-specificity towards the nicotinamide ring in NAD.

Acetaldehyde↗
PubMed1978

Catalase model systems. Decomposition of hydrogen peroxide catalysed by mesoferrihaem, deuteroferrihaem, coproferrihaem and haematoferrihaem.

The catalytic decomposition of H2O2 by deuteroferrihaem, mesoferrihaem, coproferrihaem and haematoferrihaem was studied as a model for the mechanism of action of catalase. For haematoferrihaem, anomalous but reproducible results were obtained, which could not be adequately explained. For each of the other ferrihaems studied, both monomeric and dimeric species catalysed decomposition, although the activity of monomer (aM) was much greater than that of dimer (aD). The pH variation of aD in the range 6.5--11 was consistent with an inverse dependence on [H+]1/2. The molecular mechanism whereby such a dependence could be achieved is not apparent. A study of the pH-dependence of aM in the range 6.5--11 revealed a linear inverse relationship with [H+]. This is interpreted in terms of attack by HO2- on ferrihaem monomer. The specific pH-independent rate constants for this reaction were in the order coproferrihaem greater than protoferrihaem greater than or equal to mesoferrihaem congruent to deuteroferrihaem. The order of magnitude of these rate constants is the same as that for catalysis by Fe(H2O)63+ and the second-order rate constant for decomposition of H2O2 by catalase. The implications on the mechanism of action of catalase are discussed.

Catalase↗
PubMed1982

Superoxide dismutase, glutathione peroxidase and catalase in developing rat brain.

The specific activities of Cu,Zn- and Mn-superoxide dismutases, of glutathione peroxidase and of catalase, the enzymes considered to be specifically involved in the defence of the cell against the partially reduced forms of oxygen, were determined as the function of postnatal age in the early (up to 60 days) period of rat brain development. The enzymes were assayed in the cytoplasmic fraction, in the crude mitochondrial fraction including peroxisomes, and in the mitochondria. The results show that the temporal changes of these enzymes cannot be correlated with each other, thus indicating that they do not concertedly parallel the increasing activity of aerobic brain metabolism during development. Specifically the cytoplasmic fraction shows a gradual increase of the Cu,Zn-superoxide dismutase activity with age, whereas the glutathione peroxidase activity is constant from birth. Furthermore the increase of the mitochondrial Mn-superoxide dismutase as a function of postnatal age is more remarkable than that of the cytoplasmic Cu,Zn-enzyme. Higher activities of catalase in adult animals are detectable only in the subcellular fraction containing peroxisomes, because of the modest catalase activity of the brain. These results indicate independent regulation of the expression of these enzyme activities in the process of brain differentiation and point to a relative deficiency of enzymic protection of the brain differentiation and point to a relative deficiency of enzymic protection of the brain against potentially toxic oxygen derivatives. This situation is similar to the pattern already described in the rat heart and in rat and mouse ascites-tumour cells, at variance with the much more efficient enzyme pattern present in rat hepatocytes.

Aging↗
PubMed1983

Effect of catalase inactivation on levels of inorganic peroxides, superoxide dismutase, glutathione, oxygen consumption and life span in adult houseflies (Musca domestica).

The effects of total inhibition of catalase, induced by 3-amino-1,2,4-triazole, on the adult housefly (Musca domestica) were examined. The lack of catalase activity had no effect on the longevity of the houseflies. Inorganic-peroxide concentration was elevated at younger ages, but declined in older flies. The rate of oxygen consumption by the flies was greatly decreased and the levels of oxidized as well as reduced glutathione were augmented. Superoxide dismutase activity showed a slight increase. This study suggests that loss of catalase activity does not affect survival of houseflies due to adaptive responses.

Amitrole↗
PubMed1985

Inhibition of catalase by 3,3'-diaminobenzidine.

3,3'-Diaminobenzidine strongly inhibits bovine liver catalase in two distinct ways. One of these was competitive with respect to H2O2, approached a limit of 100% inhibition and was rapidly reversed by dilution or by dialysis. The other was dependent upon H2O2, approached a limit of 60% and was not reversed by dilution or dialysis. Exposure to diaminobenzidine followed by dialysis did not modify the electrophoretic mobility of the enzyme, its Km for H2O2 or its optical spectrum, although Vmax. was halved. Diaminobenzidine protects catalase against the irreversible inactivation imposed by 3-amino-1,2,4-triazole plus H2O2. CN-protected catalase against the apparently irreversible inhibition by diaminobenzidine, and dialysis against CN- reversed this inhibition. Ethanol was similarly protective, and ethanol plus H2O2 reversed the inhibition by diaminobenzidine. Several other aromatic diamines inhibited in a fashion similar to that of diaminobenzidine, but were less effective. A scheme of reactions that accounts for these observations is proposed.

3,3'-Diaminobenzidine↗
PubMed1990

Two temporally synthesized charge subunits interact to form the five isoforms of cottonseed (Gossypium hirsutum) catalase.

Five charge isoforms of tetrameric catalase were isolated from cotyledons of germinated cotton (Gossypium hirsutum L.) seedlings. Denaturing isoelectric focusing of the individual isoforms in polyacrylamide gels indicated that isoforms A (most anodic) and E (most cathodic) consisted of one subunit of different charge, whereas isoforms B, C and D each consisted of a mixture of these two subunits. Thus the five isoforms apparently were formed through combinations of two subunits in different ratios. Labelling cotyledons in vivo with [35S]methionine at three daily intervals in the dark, and translation in vivo of polyadenylated RNA isolated from cotyledons at the same ages, revealed synthesis of two different subunits. One of the subunits was synthesized in cotyledons at all ages studied (days 1-3), whereas the other subunit was detected only at days 2 and 3. This differential expression of two catalase subunits helped explain previous results from this laboratory showing that the two anodic forms (A and B) found in maturing seeds were supplemented with three cathodic forms (C-E) after the seeds germinated. These subunit data also helped clarify our new findings that proteins of isoforms A, B and C (most active isoforms) accumulated in cotyledons of plants kept in the dark for 3 days, then gradually disappeared during the next several days, whereas isoforms D and E (least active isoforms) remained in the cells. This shift in isoform pattern occurred whether seedlings were kept in the dark or exposed to continuous light after day 3, although exposure to light enhanced this process. These sequential molecular events were responsible for the characteristic developmental changes (rise and fall) in total catalase activity. We believe that the isoform changeover is physiologically related to the changeover in glyoxysome to leaf-type-peroxisome metabolism.

Blotting, Western↗
PubMed1994

Radiation inactivation of proteins: temperature-dependent inter-protomeric energy transfer in ox liver catalase.

The radiation-inactivation method is widely used to determine the oligomeric structure of enzymes without need for solubilization or purification. We have used purified ox liver catalase, a tetrameric enzyme in solution, to study energy transfer between associated promoters responsible for oligomer inactivation. However, after freeze-drying the tetramer dissociates into an asymmetric dimer. In the present paper we compare both the radiation-inactivation size (obtained by following the activity decay) and the target size (obtained by measuring the amount of remaining protein by SDS/PAGE) of catalase under various states of aggregation and temperature. At -78 degrees C, only one promoter was fragmented after being hit by a gamma-ray and, as expected, this protomer was also inactivated. This result was obtained when either catalase was in tetrameric or in dimeric forms. However, at 38 degrees C, even though a single monomer was fragmented as at -78 degrees C, the whole dimer was inactivated. This result suggests that, at the higher temperature, there is a transfer of energy from the fragmented protomer to the other associated protomer, causing inactivation of the whole dimer. The inactivation of oligomeric enzymes is a two-step mechanism involving: (1) fragmentation of the hit monomer, followed by (2) temperature-dependent energy transfer from the fragmented towards the associated protomer. Thus we conclude that the radiation-inactivation size reflects the transfer of absorbed energy inside the oligomer which causes inactivation of one or several monomers.

Animals↗
PubMed2003

Identification of peroxisomal targeting signal of pumpkin catalase and the binding analysis with PTS1 receptor.

Many peroxisomal proteins are imported into peroxisomes via recognition of the peroxisomal targeting signal (PTS1) present at the C-termini by the PTS1 receptor (Pex5p). Catalase, a peroxisomal protein, has PTS1-like motifs around or at the C-terminus. However, it remains unclear whether catalase is imported into peroxisome via the PTS1 system. In this work, we analyzed the PTS of pumpkin catalase (Cat1). A full or truncated pumpkin Cat1 cDNA fused at the 3' end of the green fluorescent protein (GFP) coding sequence was introduced and stably expressed in tobacco BY-2 (Nicotiana tabacum cv. Bright Yellow 2) cells or Arabidopsis thaliana by Agrobacterium-mediated transformation. The cellular localization of GFP was analyzed by fluorescence microscopy. The results showed that the C-terminal 10-amino acid region containing an SKL motif-like tripeptide (SHL) was not required for the import into peroxisomes. Surprisingly, the C-terminal 3-amino acid region was required for the import when the fusion proteins were transiently expressed by using particle gun bombardment, suggesting that the transient expression system is inadequate to analyze the targeting signal. We proposed that the C-terminal amino acid region from 13 to 11 (QKL), which corresponds with the PTS1 consensus sequence, may function as an internal PTS1. Analysis of the binding of Cat1 to PTS1 receptor (Pex5p) by the yeast two-hybrid system revealed that Cat1 can bind with the PTS1 receptor (Pex5p), indicating that Cat1 is imported into peroxisomes by the PTS1 system.

Base Sequence↗
PubMed2002

Exposure of erythrocytes to methylene blue shows the active role of catalase in removing hydrogen peroxide.

Methylene blue (MB) is a powerful reducing agent that is widely used in clinical practice as well as for metabolic studies of the erythrocyte. We have investigated the role of catalase as a specific enzyme for the removal of hydrogen peroxide by measuring the in vitro effects of MB on human red cells. In the presence of MB, catalase underwent inactivation even with the co-existence of active generation of NADPH, leaving the glutathione concentration unaffected. The data obtained in the present investigation show, using a different tool (MB), that catalase is the active enzyme in H2O2 detoxification and that its integrity is largely dependent on an adequate generation of NADPH.

Catalase↗
PubMed2003

Catalase activity in human healthy and inflamed dental pulps.

AIM: To examine the catalase activity in clinically healthy and symptomatic human dental pulps to verify if an active defence system against oxidizing agents is present as a response to bacterial invasion. METHODOLOGY: Thirty-three systemically healthy patients, 18 females and 15 males (ages: 11.0-25.9 years; mean 18.8 +/- 3.6), were the source of the pulp tissue. The condition of the pulps was assessed using clinical and radiographic evaluations. The specimens were recovered by longitudinally grooving and splitting the teeth (if extracted) or during endodontic treatment, and were matched for age and sex between the healthy and inflamed specimen groups. Catalase activity was determined through spectrophotometric methods. RESULTS: Enzymatic activity was 1126 +/- 343 and 3074 +/- 698 mU mL(-1) x mg of total protein in the healthy and inflamed pulp tissue specimens, respectively. This difference was statistically significant (P<0.01). CONCLUSIONS: These results indicate a role for catalase during dental pulp inflammation in humans, and may represent an inherent biological defence system against reactive oxidants of this tissue.

Adolescent↗