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PubMed1976

Cytochemical demonstration of extraperoxisomal catalase. I. Sheep liver.

In sheep hepatocytes catalase activity was demonstrated both within peroxisomes and within the cytosol. In the cytosol the catalase reaction product is contiguous to the plasma membrane and surrounds the nuclei, rough endoplasmic reticulum, cisternae, mitochondria and Golgi apparatus. This is the first cytochemical demonstration of guine extraperoxisomal catalase. No catalase reaction product was seen in the cytosol of nonparenchymal cells. To demonstrate catalase, both glutaraldehyde and formaldehyde fixation were used, followed by a diaminobenzidine technique modified from Novikoff and Goldfischer. Control reactions were performed to distinguish catalase reaction product from adsorption of oxidized diaminobenzidine and from precipitate due to oxidase-, peroxidase- or heat-stable peroxidatic activities. The results were evaluated in the light and electron microscopes.

Animals↗

PubMed2006

Up-regulation of P-glycoprotein expression by catalase via JNK activation in HepG2 cells.

Overexpression of the MDR1 gene is one of the reasons for multidrug resistance (MDR). Some studies suggested that antioxidants could down-regulate MDR1 expression as a possible cancer treatment. In this report, we try to determine the effects of antioxidants (catalase or N-acetylcysteine [NAC]) on the regulation of intrinsic MDR1 overexpression in HepG2 cells. Adding catalase or N-acetylcysteine to the HepG2 culture led to a significant increase of MDR1 mRNA and P-glycoprotein drug transporter activity. After catalase or NAC treatment, a reduced intracellular reactive oxygen species (ROS) was observed. The JNK inhibitor SP600125 abolished the positive effects of catalase on drug transporter activity in a dose-dependent manner. Furthermore, the up-regulation of P-glycoprotein functions by catalase was only observed in HepG2 cells but not in other cell lines tested (MCF-7, A549, A431). These data suggested that catalase can up-regulate P-glycoprotein expression in HepG2 cells via reducing intracellular ROS, and JNK may mediate this process.

ATP Binding Cassette Transporter, Subfamily B, Mem↗

PubMed1999

Catalase activity and hydrogen peroxide levels are inversely correlated in maize scutella during seed germination.

Temporal patterns of hydrogen peroxide (H2O2) levels and total catalase activity are presented for post-imbibition scutella from six maize inbred lines expressing variable catalase activity. In all lines examined, H2O2 levels were highest during the initial days post-imbibition (1-2 dpi) and decreased thereafter, while total catalase activity was lowest during early dpi (1-2 dpi) and reached maximal activity at 4-6 dpi. In three of the six lines tested, a simple inverse correlation between catalase activity and H2O2 level was significant by Spearman's rank (P < 0.01). In addition to the general decline in H2O2 level throughout the dpi period, a reproducible increase in H2O2 level was observed at 4-5 dpi in five of six lines examined. Mutant lines lacking CAT-3 activity demonstrated a temporal shift in the occurrence of this increase. The role of total catalase (and individual isozymes) in controlling H2O2 levels during germination and the role of H2O2 as a potential regulator of catalase expression during germination are discussed.

Catalase↗

PubMed2000

Toxoplasma gondii catalase: are there peroxisomes in toxoplasma?

The intracellular protozoan parasite Toxoplasma gondii, like all members of the phylum Apicomplexa, is known to possess many organelles: in addition to mitochondria and the compartments of the secretory pathway, there is a reduced chloroplast (the apicoplast) and the phylum-specific components of the apical complex: dense granules, micronemes and rhoptries. Conspicuously missing so far are microbodies, organelles that can be found in nearly all eukaryotic organisms. Microbodies show a large variation with regard to their size, number and contents, depending on the organism and cell type. One marker enzyme of this single membrane-bound organelle is catalase, which is responsible for the degradation of hydrogen peroxide to water and oxygen. The EST project in T. gondii revealed the existence of two overlapping clones which showed similarity with catalase, and these were used to clone the corresponding gene. The predicted sequence of T. gondii catalase has -AKM at the C terminus, which falls within the consensus of the PTS1 peroxisomal targeting signal. Southern blot analysis confirmed the presence of a single copy gene. Northern and western blot analyses showed that the catalase gene is transcribed and translated. Immunofluorescence assays using an antibody raised against a catalase peptide identified a distinct structure towards the apical end, but other catalase-specific antibodies failed to confirm this localisation. Cell fractionations indicated that the majority of the enzyme was in the cytosol. The fusion of the C-terminal twelve amino acids, including AKM, or the canonical peroxisomal targeting signal, -SKL, to GFP resulted in predominantly cytosolic localization in T. gondii. There was therefore no evidence for membrane-bound peroxisomes in Toxoplasma.

Amino Acids↗

PubMed2005

Cloning and expression analysis of two catalase genes from Aspergillus oryzae.

Fungi contain distinct genes encoding the same class of enzyme that are differentially regulated according to conditions. We cloned two catalase genes, catA and catB, from Aspergillus oryzae. The catA gene predicts a 747-amino-acid polypeptide sharing 81% identity with Aspergillus fumigatus catalase (catA) and 77% with Aspergillus nidulans catalase (catA). The catB gene predicts a 725-amino-acid polypeptide sharing 82% identity with A. fumigatus catalase (catB) and 75% with A. nidulans catalase (catB). However, the catA and catB genes share little homology (41%) with one another, suggesting that each gene belongs to a distinct gene family. Overexpression studies demonstrated that both genes encode a functional catalase. Promoter assays indicated that the catA gene is developmentally regulated as it was preferentially expressed in solid-state cultures undergoing sporulation. However, its expression was not affected by hydrogen peroxide treatment. Conversely, the catB gene was highly expressed under all culture conditions tested, and it was induced by hydrogen peroxide treatment. These results suggest that the catB gene may be mainly used for detoxification of oxidative stress while the catA gene may have another role such as chaperoning proteins in the spore.

Amino Acid Sequence↗

PubMed2002

Purification, characterization, and gene sequencing of a catalase from an alkali- and halo-tolerant bacterium, Halomonas sp. SK1.

An alkali- and halo-tolerant bacterium with high catalase activity was isolated and identified as a new species of the genus Halomonas. Its catalase (HktA) was simply purified by two steps of liquid chromatography. A 71.4% yield of the catalase was obtained with 97% purity on SDS-PAGE. The specific activity of HktA (57,900 U/mg protein) was two times higher than that of bovine liver catalase. The purified enzyme is inhibited by KCN, NH2OH, NaN3, and 3-amino-1,2,4-triazole, active at pH 5.0-11.0, thermo-sensitive, and KCl-tolerant. HktA is suggested to be a typical catalase, a homotetrameric protein containing heme groups in the active sites. The nucleotide sequence of the catalase gene (hktA) comprises 1,530 bp, encoding a protein of 509 amino acid residues. The deduced amino acid sequence of the hktA shares 99% identity with that of Vibrio rumoiensis S-1T.

Amino Acid Sequence↗

PubMed1999

Tissue and organ expression of catalase in acatalasemic beagle dogs.

Acatalasemic Beagle dogs which were maintained in our laboratories showed no sign of catalase activity at all in the erythrocytes, and glutathione peroxidase and superoxide dismutase were at normal levels. Immunoblotting analysis demonstrated that no catalase protein is detectable in their erythrocytes. On the other hand, catalase activity was detected in other tissues and organs, albeit at varying, lower levels than in normal dogs. Quantitative immunoblotting analysis consistently demonstrated that the catalase protein is expressed in the liver and kidneys of acatalasemic dogs in proportion to the activity in these organs. The catalase mRNA expressions in the blood, liver and kidneys in acatalasemic dogs were almost the same as those in normal dogs. These results suggested that catalytically normal catalase protein is translated from mRNA in the tissues and organs including erythrocytes, but in erythrocytes this enzyme protein is disposed of by an unknown mechanism.

Acatalasia↗

PubMed1987

Immunohistochemical localization of catalase in ocular tissue.

Localization of catalase in rat and bovine ocular tissues was investigated by an immunohistochemical method. Antisera to purified catalase was raised in a rabbit. Purity of catalase was determined by gel electrophoresis and specificity of the antibody was tested by immunoblot. The immunohistochemical method revealed the presence of catalase predominantly in epithelial and endothelial structures of the eye and in the retina, except in the outer segments. Catalase was found in abundance in those structures that are frequently exposed to oxygen metabolites under physiologic conditions and in such pathologic states as intraocular inflammations. These findings thus suggest that catalase, along with other antioxidant enzymes, may offer protection against the damaging effects of hydrogen peroxide.

Animals↗

PubMed1998

Milk catalase activity as an indicator of thermization treatments used in the manufacture of cheddar cheese.

Pilot-scale studies were carried out to determine the effect of different heat treatments on catalase activity during the manufacture and maturation of Cheddar cheese. Three trials were conducted to monitor catalase activity using disk flotation and polarographic methods. Cheese was manufactured from raw milk and from milk that had been treated at 60, 65 and 72 degrees C for 16 s using a high temperature, short time heat exchanger. Catalase activity was also determined in samples of commercial milk and in samples of mild, medium, sharp, and extra sharp Cheddar cheeses obtained from different manufacturers in order to verify that the enzyme could be used as an indicator of the type of heat treatment applied to cheese milk. Catalase activity was present in cheese made from raw milk but was only present at low concentrations in cheese manufactured from thermized milk. However, high catalase activity was observed in commercial samples of sharp and extra sharp Cheddar cheese that was apparently due to the growth of catalase-producing yeasts in the cheese during maturation.

Animals↗

PubMed1996

A positive correlation between catalase activity and ascorbate uptake in the tissues of guinea pigs and cultured cells of mammals.

We recently reported that the concentration of supplemental ascorbate which inhibits cell growth is positively related to intracellular catalase activity. It is assumed that the cells with high catalase activity are resistant to high concentrations of ascorbate since catalase can decompose hydrogen peroxide (H2O2) induced by the auto-oxidation of ascorbate in cultured medium. In this study, we investigated whether intracellular catalase activity affects the uptake of ascorbate into animal tissue and cultured cells. Ascorbate concentrations in the tissues of guinea pigs and various cultured cells, with and without supplementation of ascorbate, were determined to evaluate the efficiency of ascorbate uptake. We found a positive correlation between the efficiency of ascorbate uptake and catalase activity in various tissues of guinea pigs (r = 0.767, p < 0.05). Furthermore, a positive correlation between the two was also found in various species of cultured cells. This study indicates that tissues and cells with higher efficiency of ascorbate uptake are required for higher catalase activity, presumably for the decomposition of H2O2 from ascorbate.

Animals↗

PubMed1983

Effect of AY-25,712 and other lipid-lowering agents on liver catalase and liver carnitine acetyltransferase in rats.

The effect of the hypolipidemic agent AY-25,712 on liver catalase and carnitine acetyltransferase was studied in rats. At 250 mg/kg/day for 2 or 4 weeks, i.e., at least 125 times the minimum effective hypolipidemic dose, AY-25,712 had no effect on liver weight or liver catalase. Liver catalase was elevated after a 2-week treatment with clofibrate (+ 30%), bezafibrate (+71%), and fenofibrate (+77%) at doses of 250 mg/kg/day, and with ciprofibrate (+111%) at 25 mg/kg/day. Gemfibrozil at 250 mg/kg/day for 4 weeks increased catalase by 86%. The relative increase in liver weight induced by these compounds showed a good correlation to increased catalase. Nicotinic acid (250 mg/kg/day for 2 weeks) did not alter liver weight or catalase. Clofibrate increased carnitine acetyltransferase by 176% while AY-25,712 had no effect. The results show that AY-25,712 and nicotinic acid did not induce changes in the livers of rats which are associated with treatment by various other hypolipidemic agents.

Acetyltransferases↗

PubMed2003

Isolation and identification of an antioxidant enzyme catalase stimulatory compound from Garnoderma lucidum.

Antioxidant enzymes are scavenger reactive-oxygen intermediates and are involved in many cellular defense systems. We previously reported that a crude extract of Garnoderma lucidum, a medicinally potent mushroom, profoundly increased the catalase gene expression and enzyme activities in mouse livers (Park et al., J. Biochem. Mol. Biol. 34. 144-149, 2001). In this study, we elucidated the detailed mechanism whereby G. lucidum stimulates the catalase activity and expression. The major active fraction was isolated from G. lucidum and methyl linoleate was considered the most major component of the fraction. In order to determine whether methyl linoleate increases mRNA and protein synthesis of catalase, Northern and Western blot analyses were performed in vivo with methyl linoleate-treated mouse liver homogenate after feeding methyl linoleate to the mice. Northern and Western blot analyses of the crude liver homogenates in the mice that were administered methyl linoleate revealed that the expression catalase was significantly increased when compared to the untreated controls. In addition, the catalase protein levels and enzymatic activities increased in the mouse liver homogenates. These results suggest that methyl linoleate that is produced by G. lucidum stimulates the catalase expression at the transcription level.

Agaricales↗

PubMed1976

[Localization of the Meler's reaction with ethanol catalase trap in the chain of photosynthetic electron transport].

The common view of photosystem I as the action site of catalase and ethanol at oxygen uptake in chloroplasts are based on indirect data on this reaction. That is why the question on Mehler reaction localization in electron transport chain with ethanolcatalase trap has been investigated anew. It has been demonstrated that oxygen uptake with catalase and ethanol does not decrease in presence of dibromothymoquinone (2,5-dibromo-3-methyl-6 isopropyl-p-benzoquinone--DBTQ) which blocks electron transfer to photosystem I at plastoquinones level. The summation of oxygen uptake activities is observed on the combined action of catalase and ethanol with any of the Mehler reagents functioning in photosystem I (methylviologen,FMN, epinephrine, ferredoxin). Catalase and ethanol in contrast to methylviologen have no effect on photooxidation rate of reduced dichlorphenolindophenol in photosystem I. The quatum yield of oxygen uptake with catalase and ethanol versus wave length of actinic light shows a distinct maximum in the photosystem II absorption area and a "red drop" in the longware area. The obtained data show that the Mehler reaction with catalase and ethanol takes place in photosystem II only.

2,6-Dichloroindophenol↗

PubMed1999

[Biologic effects of the static magnetic field generated by a 0.5 T magnetic resonance tomograph on the enzyme activity of catalase and creatine kinase in the rat].

PURPOSE: We investigated possible alterations in the enzyme activity of catalase and isozyme MB-creatine kinase induced by prolonged exposure of laboratory rodents to a static magnetic field generated by a .5 T Magnetic Resonance unit. MATERIAL AND METHODS: Thirty Wistar albino mice were divided into two groups of 15 mice, one to be exposed to the static magnetic field for 12 hours and the other to be kept in the same environmental conditions as a control group. Immediately after the exposure a peripheral venous blood sample was collected, the cardiac muscle was removed from the mice and the enzyme activity of catalase and MB-creatine kinase were assayed using the spectrophotometric analysis. RESULTS: No statistically significant variation was detected between the enzyme activity of catalase and MB-creatine kinase in the serum and cardiac muscle of the exposed versus the control mice. In the mice exposed to the static magnetic field the enzyme activity of serum and cardiac muscle catalase were respectively .2154 U/L and .0707 U/L after 10 minutes; they were; .2699 U/L and .0946 U/L after 160 minutes. In the control mice the enzyme activity of serum and cardiac muscle catalase were respectively .1941 U/L and .0707 U/L after 10 minutes; they were .2061 U/L and .1068 U/L after 160 minutes. The enzyme activity of MB-creatine kinase in mice was measured in the exposed (80.8 U/L) versus the control (79.6 U/L) group: the difference does not exceed standard deviation. DISCUSSION AND CONCLUSION: Our results seem to exclude any alteration in the activity of catalase and MB-CK after 12 hours' exposure to the static magnetic field. However some homeostatic mechanisms peculiar to pluricellular organisms might act in vivo to adapt to the effects of the static magnetic field during exposure.

Animals↗

PubMed1999

Amyloid-beta binds catalase with high affinity and inhibits hydrogen peroxide breakdown.

Amyloid-beta (Abeta) specifically bound purified catalase with high affinity and inhibited catalase breakdown of H(2)O(2). The Abeta-induced catalase inhibition involved formation of the inactive catalase Compound II and was reversible. Catalase<-->Abeta interactions provide rapid functional assays for the cytotoxic domain of Abeta and suggest a mechanism for some of the observed actions of Abeta plus catalase in vitro.

Amyloid beta-Peptides↗

PubMed2001

Comparison of the PR mutant with the wild-type strain of proteus mirabilis brings insight into peroxide resistance factors and regulation of catalase expression.

The peroxide resistant mutant (PR) of Proteus mirabilis was characterized by an increased constitutive catalase activity concomitant with a large production of specific mRNA. Survival toward hydrogen peroxide during exponential phase was increased by H2O2 pretreatment in the wild type but not in the mutant, although the catalase of both strains was not inducible under these conditions. In the mutant, besides catalase, over-produced proteins comprised two different alkyl hydroperoxide reductase subunit C (AhpC) proteins and a protein homologous to the stationary phase transcription factor SspA of Escherichia coli. Conversely, the flagellin A (FlaA) of P. mirabilis was repressed in the PR mutant. Genomic DNA fragments of 2.9 kb carrying the catalase gene (katA) together with the 5' and 3' flanking regions were isolated from both strains and found to be identical. Upstream of katA, a Fur box-like sequence was found, but surprisingly, restricting iron in the culture medium caused a decrease in catalase production. The PR mutant presents similarities with other peroxide resistant mutants, but the regulation of catalase biosynthesis in P. mirabilis seems somewhat different from other close species such as E. coli.

Adhesins, Bacterial↗

PubMed2001

Differential expression of manganese superoxide dismutase and catalase in lung cancer.

Reactive oxygen species (ROS) are important in the initiation and promotion of cells to neoplastic growth. In this context, cigarette smoke exposure, the primary risk factor in lung cancer development, leads to high levels of ROS within the human airway. Although well-equipped with an integrated antioxidant defense system consisting of low-molecular weight antioxidants such as glutathione and intracellular enzymes such as superoxide dismutase (SOD), catalase, and glutathione peroxidase, the lungs are vulnerable to increased endogenous and exogenous oxidative insults. Antioxidants increase in response to oxidative stress and minimize ROS-induced injury in experimental systems, indicating that antioxidant levels may determine whether ROS can initiate lung carcinogenesis. On this basis, we hypothesized that antioxidants would be decreased in lung carcinoma cells as compared with tumor-free adjacent lung tissues. Antioxidant expression was evaluated in 16 lung tumor and 21 tumor-free lung tissues collected between the years 1993 and 2001 from 24 individuals with surgically resectable non-small cell lung cancer, i.e., adenocarcinoma and squamous cell carcinoma. Total SOD activity was increased (P = 0.035), catalase activity decreased (P = 0.002), and glutathione and glutathione peroxidase were similar in tumors compared with tumor-free lung tissues. Alterations in antioxidant activities were attributable to increased manganese SOD and decreased catalase protein and mRNA expression in tumors. Immunohistochemical localization of catalase in the lung revealed decreased or no expression in the tumor cells, although healthy adjacent airway epithelial cells were strongly positive for catalase. Parallel changes in antioxidant activities, protein, and mRNA expression were noted in A549 lung carcinoma cell lines exposed to cytokines (tumor necrosis factor-alpha, interleukin 1beta, and IFN-gamma). Thus, inflammation in the lung may contribute to high levels of manganese SOD and decreased catalase, which together may lead to increased hydrogen peroxide intracellularly and create an intracellular environment favorable to DNA damage and the promotion of cancer.

Aged↗

PubMed2002

[Catalase-negative Rothia dentocariosa: evaluation of additional descriptive tests].

Rothia dentocariosa is one of the human oral flora members, and classified in the group of coryneform bacteria which are taxonomically heterogeneous. Although R. dentocariosa is considered as a contaminant in throat cultures generally, it may be the causative infectious agent in the presence of predisposing factors. The catalase activity which is used as a simple and initial identification test, becomes contradictory because of the detection of the catalase negative strains recently. The aim of this study was to compare several biochemical and enzymatic reactions for the identification of catalase positive and negative R. dentocariosa strains. A total of 42 R. dentocariosa strains which were isolated from throat cultures have been studied, and the positivity rate of mannose fermentation in catalase negative R. dentocariosa isolates was found to be significantly higher than those catalase positive (p < 0.05). In conclusion, mannose fermentation test seems to be a useful tool as an additional identification method of catalase negative R. dentocariosa isolates.

Bacteriological Techniques↗