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PubMedDate not supplied

Taurine modulates catalase, aldehyde dehydrogenase, and ethanol elimination rates in rat brain.

Chronic administration of either the sulphonated amino acid taurine (0.32 or 0.62 g/kg for 2 weeks) or the catalase inhibitor, 3-amino, 1,2,4-triazole (AT: 0.5 or 1.0 g/kg for 5 days) significantly reduced catalase activities both in the brain and liver of male Wistar rats. The total brain activity of aldehyde dehydrogenase was significantly increased after the lower dose of taurine and after administration of both doses of AT. Hepatic alcohol dehydrogenase activity was not altered by either AT or taurine administration. In taurine-supplemented rats, a significant increase in the ethanol elimination rates (EER) was discernible in the livers after a 2 g/kg dose of ethanol. In contrast, significant decreases in the EER were observed in both plasmas and livers of rats in which catalase was inhibited by AT. However, the brain EERs were comparable in both catalase-inhibited and taurine-supplemented rats, both showing a decrease by comparison to controls. The similar psychopharmacological effects induced by both of these compounds on ethanol-induced effects might indicate that this is mediated in part via the catalase pathway. Since both catalase and the EERs are diminished in the brain after the administration of either of these compounds, this may be an important factor in the moderation of ethanol-induced behaviour.

Aldehyde Dehydrogenase↗
PubMed1998

Liver-specific catalase expression in transgenic mice inhibits NF-kappaB activation and DNA synthesis induced by the peroxisome proliferator ciprofibrate.

Peroxisome proliferators are a group of non-genotoxic hepatic carcinogens that have been proposed to act by increasing oxidative damage in the liver. To test this hypothesis, we have examined if hepatic catalase overexpression in peroxisome proliferator-treated mice influences the induction of cell proliferation or the activation of transcription factors involved in cell proliferation. Transgenic mice or non-transgenic littermates were fed either 0.01% ciprofibrate or a control diet for 21 days. Fatty acyl CoA oxidase activity was not significantly affected by catalase overexpression, although the ratio of fatty acyl CoA oxidase to catalase was significantly decreased in transgenic animals. The labeling index in hepatocytes was significantly increased by ciprofibrate in non-transgenic mice, but catalase overexpression significantly inhibited this increase. Ciprofibrate increased the activation of nuclear factor (NF)-kappaB in non-transgenic mice, but this increase was inhibited by catalase overexpression. Ciprofibrate also increased AP-1 activation, but catalase overexpression did not significantly inhibit this increase, although AP-1 activation was 40% lower in transgenic mice. These results support the hypothesis that active oxygen plays a role in the induction of cell proliferation by the peroxisome proliferator ciprofibrate and therefore may be important in the carcinogenicity of these agents.

Animals↗
PubMed1981

Diminution of mouse epidermal superoxide dismutase and catalase activities by tumor promoters.

The effects of phorbol ester tumor promoters and related compounds on superoxide dismutase (SOD) and catalase were examined. The treatment of adult mouse skin with 2 micrograms 12-O-tetradecanoylphorbol-13-acetate (TPA) resulted in a sustained decrease in the basal levels of both SOD and catalase activities in the epidermis. A decline in SOD activity occurred within 3 h after application and the maximum effect was seen at 16--17 h. The decrease in SOD activity was always accompanied by a similar decline in the epidermal catalase activity. The alterations in both enzymes occurred against a high background of enhanced protein synthesis which indicates that the effect of TPA is selective for SOD and catalase. Other tumor promoters such as phorbol 12,13-dibutyrate and the non-phorbol tumor promoter anthraline also lowered the activities of both the enzymes. Mezerein, a resiniferonol derivative with weak promoting activity but a potent stage-II promoter, appeared to be more potent than TPA in lowering the basal levels. These results indicate that damage which favors neoplastic progression could occur in TPA-treated mouse skin due to the accumulation of free radicals resulting from low levels of SOD and catalase activity. In addition, the TPA-caused decrease in the levels of SOD and catalase was not prevented by either retinoic acid, fluocinolone acetonide, tosyl amino-2-phenylethyl chloromethyl ketone, or butylated hydroxytoluene, suggesting that inhibition of tumor promotion by these agents is not mediated through alterations in the levels of enzymatic activities which decrease free radical concentrations.

Animals↗
PubMed2003

Short-term depletion of catalase suppresses cadmium-elicited c-Jun N-terminal kinase activation and apoptosis: role of protein phosphatases.

The c-Jun N-terminal kinase (JNK) is a vital stress-activated signal that can be regulated differentially under oxidant or antioxidant conditions. Recently, we have reported that activation of JNK by cadmium chloride (Cd) contributes to apoptosis in CL3 human lung adenocarcinoma cells. Although oxidative stress has been implicated in numerous biochemical effects altered by Cd, its role in Cd-elicited JNK activation has not been established. Here we report that catalase is crucial for the activation of JNK by Cd. Short-term treatment of 3-amino-1,2,4-triazole (3AT), a specific catalase inhibitor, completely suppressed the Cd-elicited JNK activation, conversely, exogenous addition of catalase increased the intensity and duration of JNK activation in Cd-treated CL3 cells. Co-administering high doses of H(2)O(2) (500-1000 micro M) with Cd also markedly decreased JNK activity, although at doses <200 micro M H(2)O(2) enhanced the Cd-elicited JNK activation in CL3 cells. 3AT also blocked JNK activation in Cd-treated normal human fibroblasts and Chinese hamster ovary cells, and in UV-irradiated CL3 cells. However, mannitol, a hydroxyl radical scavenger, did not alter the JNK activity in Cd-treated human and rodent cells. Intriguingly, sodium fluoride or okadaic acid, inhibitors for serine/threonine protein phosphatases (PP), recovered the JNK activity in CL3 cells exposed to Cd plus 3AT; however, the protein tyrosine phosphatases inhibitor sodium orthovanadate did not. Furthermore, 3AT decreased but catalase increased the Cd-induced cytotoxicity, apoptosis and procaspase-3 degradation in CL3 cells. Together, these results indicate that persistent activation of apoptotic JNK signal by Cd requires functional catalase and that short-term depletion of catalase activity may facilitate okadaic acid-sensitive PP to down-regulate the JNK activation and may predispose these cells to carcinogenic transformation upon Cd exposure.

Amitrole↗
PubMed1984

Genetic variation affecting the expression of catalase in Drosophila melanogaster: correlations with rates of enzyme synthesis and degradation.

Both second and third chromosome substitution lines isolated from natural populations of Drosophila melanogaster affect the expression of catalase (EC 1.11.1.6) at both the larval and adult stages of development. In each case, the level of catalase activity is strongly related to the level of catalase-specific cross-reacting material. Turnover studies employing the catalase inhibitor 3-amino-1,2,4-triazole were conducted on a selected number of lines. Although the variation in steady state levels of catalase protein was highly significant among lines, variation in intracellular degradation rate was not. These results suggest that the different steady state levels observed among lines largely reflect different rates of catalase synthesis.

Animals↗
PubMed1994

Effects of H2O2-producing lactobacilli on Neisseria gonorrhoeae growth and catalase activity.

In the vagina and endocervix, Neisseria gonorrhoeae must interact with complex microflora. Among these are lactobacilli, which may inhibit the growth of gonococci. Lactobacillus acidophilus, which produce H2O2 (LB+), and L. acidophilus and Lactobacillus casei, which do not produce H2O2 (LB-), were coincubated with catalase-positive and -deficient strains of N. gonorrhoeae. When the incubation medium was maintained at pH 7.3, neither LB+ nor LB- affected gonococcal growth. However, LB+ caused a significant increase in expression of gonococcal catalase, which could be offset by exposure of the bacteria to exogenous catalase. When coincubation medium was at lower pH (4.8-5.0), there was a significant decrease in gonococcal survival and catalase activity, which was only partly reversed by exogenous catalase. Lysates of LB+ also effectively inhibited gonococcal catalase. This inhibition was retained upon heating of the lysate to 100 degrees C for 15 min but was lost with proteinase K treatment. Thus, LB+ may inhibit growth of gonococci by acidification of the environment, secretion of H2O2, and production of protein inhibitors.

Catalase↗
PubMed1990

Purification and characterization of catalase from a facultative alkalophilic Bacillus.

Catalase was purified to an electrophoretically homogeneous state from the facultative alkalophilic bacterium, Bacillus YN-2000, and some of its properties were studied. Its molecular weight was 282,000 and its molecule was composed of four identical subunits. The enzyme contained two protoheme molecules per tetramer. The enzyme showed an absorption spectrum of typical high-spin ferric heme with a peak at 406 nm in the oxidized form and peaks at 440, 559, and 592 nm in the reduced form. In contrast to the typical catalases, the enzyme was reduced with sodium dithionite, like peroxidases. The enzyme showed an appreciable peroxidase activity in addition to high catalase activity. The amino acid composition of Bacillus YN-2000 catalase was very similar to those of catalase from Neurospora crassa and peroxidase from Halobacterium halobium. The catalase content in the soluble fraction from the bacterium was higher with the cells grown at pH 10 than with the cells grown at lower pHs (pH 7-9).

Amino Acids↗
PubMed1980

Studies on rat liver catalase. XI. Site of synthesis and segregation by stripped ER membranes.

We reinvestigated the site of synthesis of rat liver catalase, and it has been reconfirmed that catalase is synthesized not only by free polysomes but also by membrane-bound polysomes. Considerable amounts of nascent catalase on rough microsomes were released from the membrane into the medium upon incubation with puromycin, not transported directly into the intracisternal cavity of microsomes. On the other hand, catalase newly synthesized in vitro was shown to be segregated by stripped rat liver microsomal membranes in a state resistant to proteolysis. Since this segregation occurred without coupled protein synthesis, catalase appears to be transported by a mechanism different from co-translational transfer. A hypothesis is presented regarding the mechanism of intracellular transport of liver catalase.

Animals↗
PubMed1981

Subcellular distribution and characterization of porcine kidney catalase.

Subcellular distribution of catalase for porcine kidney was analyzed by differential centrifugation of kidney homogenate. The specific activity of catalase was the highest in light mitochondrial fraction, followed by mitochondrial, cytosolic, nuclear, and microsomal fractions. However, about a half of the total activity was found in supernatant (cytosol) fraction and the other half was mainly associated with both mitochondrial and light mitochondrial fractions. Osmotic shock using hypotonic solution, 50 mm sodium phosphate buffer (pH 7.0) was found to be most effective for solubilization of particulate-bound catalase. Both particulate and cytosol catalases from porcine kidney were purified by ammonium sulfate fractionation followed by DEAE-cellulose, CM-cellulose, and Sephadex G-100 column chromatographies. The purified enzymes showed two distinct bands, one major and the other minor, on disc gel electrophoresis. Both particulate and cytosol enzymes showed identical molecular weights estimated from disc gel electrophoresis; that of the major component was 219,000 corresponding to native molecule and that of the minor one 421,000. A similar value, 210,000, was also obtained for the major component by gel filtration on a Bio Gel A-1.5 m column. It was inferred that the minor component was formed by dimerization of native molecule caused by formation of disulfide cross-links due to oxidation of SH groups in protein moiety. The particulate and cytosol catalases showed essentially identical molecular characteristics, although a slight difference was detected in stability in guanidine-HCl solution. The effect of NaCl on enzyme activity and optical properties of catalase were also measured.

Animals↗
PubMed2006

Genotype-activity relationship for Mn-superoxide dismutase, glutathione peroxidase 1 and catalase in humans.

OBJECTIVES: This study examined the association between genetic polymorphisms and enzyme activity for antioxidant enzymes that share a common detoxification pathway: manganese superoxide dismutase (MnSOD), glutathione peroxidase-1 (GPX1) and catalase. METHODS: MnSOD, GPX1, and catalase activities were measured in isolated erythrocytes of 231 healthy, non-smoking student volunteers (55% women, ages 17-21, majority Asian or Caucasian). DNA from blood clots was genotyped by Taqman PCR (C47T : MnSOD and C593T : GPX1) and standard PCR (-262C>T : catalase). Associations between genotype and enzyme activity were analyzed by multiple linear regression, adjusted for baseline factors including gender and ethnicity. RESULTS: Minor allele frequencies ranged from 13% for catalase (T) to 18% for GPX1 (T), and 33% for MnSOD(C) with significant variation between ethnicities. Median GPX1 activity was 13.2 U/g Hb with a six-fold difference between lowest and highest levels. Catalase activity ranged eight-fold (median: 86.3 k/g Hb), while median MnSOD activity was 2.8 U/mg Hb with a 56-fold range of values. MnSOD enzyme activity was 15% higher in females than males (95%CI : -1%, 32%), and 33% higher in CT or TT individuals (C47T) versus CC individuals (95%CI : 7-59%). On average, catalase activity was 18.1 k/g Hb lower for TT subjects (-262C>T) versus CC subjects (95% CI: -32.3, -4.0). All enzyme activities were correlated (r=0.3-0.4, P<0.001). CONCLUSIONS: Interindividual variability of antioxidant enzyme activity in healthy young adults was partially explained by significant associations with three known genetic polymorphisms, and was further modified by gender and ethnicity. A substantial component of this variability may be attributable to differences in diet, environmental exposures, and additional genetic factors.

Adolescent↗
PubMed1989

Purification, properties and immunological detection of a bromoperoxidase-catalase from Streptomyces venezuelae and from a chloramphenicol-nonproducing mutant.

A new bromoperoxidase-catalase was purified from the chloramphenicol-producing actinomycete Streptomyces venezuelae ISP 5230. The homogeneous enzyme showed brominating activity, catalase activity and a very low peroxidase activity. The spectral properties and pH dependence of the catalase activity showed similarities to conventional catalases. In contrast to other haem-bromoperoxidases, the bromoperoxidase-catalase was stable when treated with an ethanol/chloroform mixture. Gel filtration gave an estimated Mr of 127,000-136,000. SDS-PAGE showed a single band corresponding in mobility to a species with an Mr of 61,000. The pI was estimated to be 4.5. The bromoperoxidase-catalase was not present in active form in a mutant of S. venezuelae ISP 5230, blocked in the chlorination step of chloramphenicol biosynthesis. However, an inactive species of the enzyme was detected in crude extracts of the mutant by using antibodies. From these results it is concluded that this bromoperoxidase participates in the chlorination step during chloramphenicol biosynthesis.

Catalase↗
PubMed1991

Helicobacter pylori catalase.

Helicobacter pylori is the major aetiological agent of gastroduodenitis in humans. Due to the potential importance of catalase in the growth and survival of Helicobacter pylori on the surface of inflamed mucosae, we have characterized catalase from H. pylori as a prelude to further studies on the function of the enzyme in vivo. The catalase activity of H. pylori was significantly affected by the presence of blood, serum or erythrocytes in the growth medium: the greatest activity was expressed when the bacterium was grown on medium containing serum. H. pylori catalase is a tetramer with a subunit Mr of 50,000. The enzyme had a pI of 9.0-9.3, was active over a broad pH range and was stable at 56 degrees C. It was non-competitively inhibited by sodium azide, and had no detectable peroxidase activity. The Km for the purified catalase was measured as 43 +/- 3 mM-H2O2 and the V as 60 +/- 3 mmol H2O2 min-1 (mg protein)-1. The native catalase has absorption maxima at 280 nm and 405 nm with further minor shoulders or peaks at 510 nm, 535 nm and 625 nm, consistent with the presence of an iron-porphyrin prosthetic group.

Azides↗
PubMed1993

Response of catalase activity and membrane fluidity of aerobically grown Schizosaccharomyces pombe and Saccharomyces cerevisiae to aeration and the presence of substrates.

Intracellular catalase (EC 1.11.1.6) activity of permeabilized aerobically grown cells of Schizosaccharomyces pombe was insensitive to cell aeration and inhibition of protein synthesis, and was only mildly enhanced by the presence of glucose and ethanol via de novo protein synthesis. By contrast, the intracellular catalase activity of Saccharomyces cerevisiae, which, in freshly harvested cells, was two to three times lower than that in Sch. pombe, increased on aeration without substrates or with ethanol and was inhibited on aeration with glucose following cell permeabilization. The enhanced intracellular activity was due to de novo protein synthesis while the inhibitory effect of glucose, absent in Sch. pombe, was caused by one of the major glucose metabolites, succinate. The intact-cell catalase activity of both yeasts increased greatly during aeration. In Sacch. cerevisiae, this increase was again prevented by glucose. In parallel, export of catalase to the cell surface increased in both yeasts. This was especially conspicuous in Sch. pombe aerated in the presence of ethanol, and may represent a protective mechanism against the damaging effects of ethanol. The cell-surface-bound catalase activity was confirmed in isolated plasma membranes of both yeasts. The fluidity of the plasma membrane increased during aeration. This effect was further stimulated by the presence of glucose and to a lesser extent by ethanol. Both yeasts exhibited increased extracellular catalase activity during aeration which could not be caused entirely by cell lysis. In Sch. pombe this activity was strongly enhanced by the presence of ethanol.

Aerobiosis↗
PubMed1999

Role of the lateral channel in catalase HPII of Escherichia coli.

The heme-containing catalase HPII of Escherichia coli consists of a homotetramer in which each subunit contains a core region with the highly conserved catalase tertiary structure, to which are appended N- and C-terminal extensions making it the largest known catalase. HPII does not bind NADPH, a cofactor often found in catalases. In HPII, residues 585-590 of the C-terminal extension protrude into the pocket corresponding to the NADPH binding site in the bovine liver catalase. Despite this difference, residues that define the NADPH pocket in the bovine enzyme appear to be well preserved in HPII. Only two residues that interact ionically with NADPH in the bovine enzyme (Asp212 and His304) differ in HPII (Glu270 and Glu362), but their mutation to the bovine sequence did not promote nucleotide binding. The active-site heme groups are deeply buried inside the molecular structure requiring the movement of substrate and products through long channels. One potential channel is about 30 A in length, approaches the heme active site laterally, and is structurally related to the branched channel associated with the NADPH binding pocket in catalases that bind the dinucleotide. In HPII, the upper branch of this channel is interrupted by the presence of Arg260 ionically bound to Glu270. When Arg260 is replaced by alanine, there is a threefold increase in the catalytic activity of the enzyme. Inhibitors of HPII, including azide, cyanide, various sulfhydryl reagents, and alkylhydroxylamine derivatives, are effective at lower concentration on the Ala260 mutant enzyme compared to the wild-type enzyme. The crystal structure of the Ala260 mutant variant of HPII, determined at 2.3 A resolution, revealed a number of local structural changes resulting in the opening of a second branch in the lateral channel, which appears to be used by inhibitors for access to the active site, either as an inlet channel for substrate or an exhaust channel for reaction products.

Alanine↗
PubMed2006

The nature of plant growth-promoting effects of a pseudoalteromonad associated with the marine algae Laminaria japonica and linked to catalase excretion.

AIMS: The goal of this study was to identify a marine algae-associated bacterium isolated from Laminaria japonica and investigate this microorganism's growth-promoting effects on plants. METHODS AND RESULTS: The bacterium, identified as Pseudoalteromonas porphyrae, was determined to display a biostimulatory activity for seed germination and shoot growth in several agricultural plants and also for growth in ginseng callus cell culture. This biostimulatory activity was linked to a catalase enzyme that was excreted in the maximal amount during the transition from logarithmic growth phase to stationary growth phase. In addition, selected shifts in growth temperature and medium salinity affected the amount of enzyme excreted. The purified catalase was determined to be composed of identical subunits. The catalase of interest displayed significantly higher biostimulatory activity than the catalase from bovine liver. CONCLUSIONS: The catalase investigated in this study is unique in that it promotes growth in and possibly contributes to stress tolerance of plants. SIGNIFICANCE AND IMPACT OF THE STUDY: The catalase of interest has the potential for use in treatments that aim to improve percent seed germination as well as obtaining tall shoots in a shorter time period.

Bacterial Typing Techniques↗
PubMed1993

The catR gene encoding a catalase from Aspergillus niger: primary structure and elevated expression through increased gene copy number and use of a strong promoter.

Synthetic oligonucleotide probes based on amino acid sequence data were used to identify and clone cDNA sequences encoding a catalase (catalase-R) of Aspergillus niger. One cDNA clone was subsequently used to isolate the corresponding genomic DNA sequences (designated catR). Nucleotide sequence analysis of both genomic and cDNA clones suggested that the catR coding region consists of five exons interrupted by four small introns. The deduced amino acid sequence of catalase-R spans 730 residues which show significant homology to both prokaryotic and eukaryotic catalases, particularly in regions involved in catalytic activity and binding of the haem prosthetic group. Increased expression of the catR gene was obtained by transformation of an A. niger host strain with an integrative vector carrying the cloned genomic DNA segment. Several of these transformants produced three- to fivefold higher levels of catalase than the untransformed parent strain. Hybridization analyses indicated that these strains contained multiple copies of catR integrated into the genome. A second expression vector was constructed in which the catR coding region was functionally joined to the promoter and terminator elements of the A. niger glucoamylase (glaA) gene. A. niger transformants containing this vector produced from three- to 10-fold higher levels of catalase-R than the untransformed parent strain.

Amino Acid Sequence↗
PubMed1986

Effect of elevated temperature on catalase and superoxide dismutase during maize development.

Seeds of the inbred maize lines, W64A, R6-67, and D10, were germinated and grown at 25 degrees, 35 degrees, or 40 degrees C for up to 10 days. The catalase activity in scutella of W64A seedlings grown at 40 degrees C was slightly lower than that in seedlings grown at 25 degrees C. The total superoxide dismutase activity in scutella was lower in seedlings grown at 40 degrees C than in those grown at 25 degrees C during the first 3 days of germination, but thereafter was not significantly different at these temperatures. The high-catalase mutant lines, R6-67 and D10, grown at 40 degrees C exhibited a developmental pattern of catalase activity that was severalfold lower than that seen in seedlings grown at 25 degrees C. The decrease in catalase activity in R6-67 seedlings grown at 40 degrees C was correlated with lower amounts of CAT-2 protein, which is normally present at significantly high levels in this line. The application of a catalase synthesis inhibitor revealed that the low levels of CAT-2 in R6-67 grown at 40 degrees C were due to slightly higher degradation rates and a significant drop in the rate of catalase protein synthesis.

Catalase↗
PubMed1980

Inhibition studies in situ of yeast catalases.

The catalase activity of the intact yeast cells towards external substrate is generally lower than the 'cryptic' activity which is revealed after cell lysis. The physiological basis for the reduced catalytic activity of the intact cell ('patent' activity) has been investigated by establishing the inhibition profiles of catalases in situ using selected probes; to this end we utilized either non-penetrating acids and/or catalase poisons able to cross the plasmic membrane. Owing to the peculiar features of the reaction mechanism, competitive inhibitors, which are known to interact with the prosthetic group of catalases, show an efficiency that is unlinked to the hydrogen peroxide concentration under the usual assay conditions ([H2O2] much less than Km). This mode of interaction, which also characterizes the action of the penetrating probes HCOOH and HCN, is particularly well adapted to the study of the behaviour of the cytoplasmic catalases in situ. By this experimental approach, it has been shown that the catalase of the inner cellular region contributes, together with an isoenzyme present at the cell surface, to the patent activity. The mathematical processing of the data, which takes into account a rate-limiting diffusion of external substrate into the intact yeast cell, has allowed us to predict accurately the resulting apparent efficiency of inhibitors as a function of the physiological variations of the intracellular enzyme concentration.

Catalase↗