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PubMed1995

Peroxisomal beta-oxidation activity and catalase activity during development and aging in mouse liver.

Liver peroxisomal beta-oxidation activity on stearate, oleate, linoleate and alpha-linolenate was investigated as a function of age in two mouse strains. Each fatty acid showed a similar beta-oxidation activity pattern with age characterized by a rapid increase (200%) from day 2 to 20 followed by a dramatic weaning-related decrease (70%) from day 20 to 22. There was a new increase (260%) from day 22 to 75, then a plateau up to day 300 days, and finally an age-related decrease (70%) from day 300 to 540. Oleic, linoleic and alpha-linolenic acids were respectively 5-, 7.5- and 9-fold more degraded than stearic acid. Catalase specific activity showed the same age-related pattern as fatty acid beta-oxidation. Both mouse strains showed the age-related decreases. The longer-lived strain exhibited higher activity for both peroxisomal beta-oxidation and catalase and the rate of decrease of these two activities during aging was the same for both strains. The catalase/alpha-linolenic acid beta-oxidation ratio was constant during adulthood and aging. These results suggest that peroxisomal beta-oxidation and catalase activities are closely related throughout and implications for long-chain and very long-chain fatty acid metabolism, maintenance of membrane fatty acid composition and anti-oxidant status during aging are discussed.

Age Factors↗
PubMed1996

Expression of heat shock proteins, glutathione peroxidase and catalase in childhood acute lymphoblastic leukemia and nephroblastoma.

In this study we analyzed the mRNA expression of the heat shock proteins 27 and 70, and the expression of the radical scavenging enzymes catalase and glutathione peroxidase (GPX) in childhood acute lymphoblastic leukemia (ALL, n = 54) and in nephroblastoma (n = 34). We found a significant positive correlation between both heat shock proteins and also between glutathione peroxidase and both heat shock proteins in ALL and nephroblastoma. There was also a significant correlation between catalase and glutathione peroxidase detectable. Furthermore, we investigated whether the expression of the heat shock proteins and the antioxidant enzymes glutathione peroxidase and catalase have implications in the clinical outcome in ALL. However, we found no significant correlation between the expression of these proteins and relapse rate, the relapse free intervals or the overall survival.

Adolescent↗
PubMed1991

NGF restores decrease in catalase and increases glutathione peroxidase activity in the brain of aged rats.

The effects of subchronic administration of nerve growth factor (NGF) into the lateral ventricle on catalase and selenium-dependent glutathione-peroxidase (GSH-Px) activity in several areas of the brain in 3-, 12- and 24-month-old rats were studied. NGF given daily (1 microgram for 28 consecutive days) produced in all brain areas studied a significant increase in catalase activity in 12- and 24-month-old rats. The most important finding was a complete restoration in 12- and 24-month-old rats of catalase activity to levels similar to those occurring in young (3-month-old) rats. In addition, NGF produced in comparison to 3-month-old rats and to same age vehicle-treated rats a significant increase in selenium-dependent GSH-Px in all the brain areas studied in 12- and 24-month-old animals, whereas selenium-independent GSH-Px was unaffected. In conclusion, the present results show that long-term administration of NGF into the lateral ventricle significantly increases in old animals the activity of key enzymes involved in the metabolic degradation of hydrogen peroxide.

Aging↗
PubMed1990

Comparative studies of catalase and superoxide dismutase activity within salmon fish erythrocytes.

1. Superoxide dismutase isolated from erythrocytes of several species of salmon and the rainbow trout exhibited single electrophoretic bands of activity which migrated anodally similar to the human erythrocyte enzyme; two discrete bands were observed for the coho salmon. 2. No polymorphism was observed for 30 samples from sockeye salmon and six samples from king salmon. Only one sample of rainbow trout (one of 12) exhibited an electrophoretic mobility difference. 3. Catalase migration on starch-gel resembled the human enzyme's electrophoretic mobility for all salmon species and rainbow trout. Catalase activity of the sockeye salmon (2929 +/- 895 mumol min-1 gHb-1) was determined to be lower than human catalase activity. 4. All samples differed from the human enzymes in that they required the presence of a detergent, Triton X-100, for solubilization.

Animals↗
PubMed1992

Location of catalase in crystalline peroxisomes of methanol-grown Hansenula polymorpha.

We have studied the intraperoxisomal location of catalase in peroxisomes of methanol-grown Hansenula polymorpha by (immuno)cytochemical means. In completely crystalline peroxisomes, in which the crystalline matrix is composed of octameric alcohol oxidase (AO) molecules, most of the catalase protein is located in a narrow zone between the crystalloid and the peroxisomal membrane. In non-crystalline organelles the enzyme was present throughout the peroxisomal matrix. Other peroxisomal matrix enzymes studied for comparison, namely dihydroxyacetone synthase, amine oxidase and malate synthase, all were present throughout the AO crystalloid. The advantage of location of catalase at the edges of the AO crystalloids for growth of the organism on methanol is discussed.

Alcohol Oxidoreductases↗
PubMed1992

Polyclonal antibodies against Staphylococcus aureus ATCC 12600 catalase do not recognize any protein in cellular extracts from S. aureus subsp. anaerobius.

Rabbits were immunized with electrophoretically pure catalase from Staphylococcus aureus ATCC 12 600. The antiserum was used to study whether S. aureus subsp. anaerobius was able to synthesize the apoprotein of catalase. Proteins were separated on polyacrylamide gels (SDS-PAGE) and transferred to nitrocellulose membranes and were detected by immunoblotting. No protein reacting with the purified immunoglobulins against S. aureus ATCC 12,600 catalase could be detected in crude and partially purified cellular extracts from S. aureus subsp. anaerobius or its aerotolerant mutants.

Acatalasia↗
PubMed1987

Decrease in catalase activity of cultured cells by Mycoplasma gallisepticum infection.

The effect of Mycoplasma gallisepticum infection on the host cell catalase activity was histochemically examined in cultured chicken embryo fibroblasts (CEF) and kidney cells. The activity in normal cells was detected as fine, brown granules in the cytoplasm, which appeared ultrastructurally to correspond to anucleoid microbodies. By infecting cultured cells with a CEF-passaged strain of M. gallisepticum, the catalase-positive granules clearly decreased in amount, whereas the UV light-killed mycoplasma and the original strain failed to decrease the granules. The cell-passaged strain was able to induce cytopathic effects and this appeared to be due to its enhanced adherent ability as compared with the original strain. These findings suggest that attachment of viable organisms to cells is crucial to decrease the catalase activity and that the decreased activity may be an important process for the subsequent development of cytopathic effects.

Animals↗
PubMedDate not supplied

Age-related activity of catalase in different genotypes of Drosophila melanogaster.

The enzyme catalase protects aerobic organisms from oxygen free radical damage by converting hydrogen peroxide to molecular oxygen and water before it can decompose to form the highly reactive hydroxyl radical. This damage has been implicated in the increased risk of disease and death associated with aging. In order to study the age-specific activity of catalase in male D. melanogaster, three different genotypes (Oregon w.t., ebony mutant, and the F1 hybrids of the two), whose mean life spans are about 55, 40, and 63 days, respectively, were used in the experiments. As the mean life span of the mutant is the shortest the enzyme activity was measured until the 43rd day, whereas in Oregon w.t., it continued until the 72nd day and in hybrids until the 79th day (longest-lived group). Although the enzyme activity in mutant flies increased sharply till the 9th day (and attained the highest level), later it declined sharply. In the other genotypes, the enzyme activity increased gradually until the 20-25th days, and then declined steadily in comparison to that of the ebony mutant. We found that higher catalase activity is associated with reduced life span for ebony mutant. It is obvious that some relationship exists between life span and antioxidant enzymes; however, a review of the literature does not at the moment allow as to understand the underlying mechanism involved in aging.

Aging↗
PubMedDate not supplied

Hepatic catalase and superoxide dismutases after acute ethanol administration in rats.

The administration of an acute ethanol load (2.3 g/kg, IP) to rats is followed by a decrease of the hepatic activity of cytosolic catalase, a decrease which precedes a reduction in the cytosolic Cu, Zn-superoxide dismutase (SOD) activity. Desferrioxamine, an iron chelator and scavenger of superoxide radicals, administered prior to ethanol, prevents the changes in the cytosolic catalase activity, changes which are unaffected by the administration of allopurinol, an inhibitor of xanthine oxidase. These data favour the hypothesis that acute ethanol results in an overproduction of oxygen free radicals which affects primarily the cytosolic catalase activity and increases hereby susceptibility of Cu, Zn-SOD to these radicals. They suggest also that xanthine oxidase does not play a major role in oxygen radical production in the liver cytosol during acute alcohol intoxication.

Allopurinol↗
PubMedDate not supplied

Effects of 3-amino-1,2,4-triazole on brain catalase in the mediation of ethanol consumption in mice.

Research has suggested that catalase plays a role in mediating ethanol's psychopharmacological effects. It has been shown that acatalasemic (C3H-A) mice differing in the activity of this enzyme consume larger amounts of ethanol. It has also been reported that when catalase activity is pharmacologically reduced, via 3-amino-1,2,4-triazole (AT), rats reduce their intake and preference for ethanol. The present research attempted to investigate AT's effects in nonselected mice. Swiss Webster mice were randomly assigned to groups of four per cage and further assigned to either a 5%, a 10%, or a 15% ethanol exposure condition. Mice were given a choice between water and increasing 1% concentrations of ethanol starting with 2%. Following five days of baseline, mice were injected daily with either AT (0.5 g/kg) or saline for five days. Results showed that AT significantly reduced ethanol consumption across treatment, but not posttreatment days. Results could not be explained by differences in total fluid intake. These results suggest a role for brain catalase in ethanol consumption across a variety of strains and species and further support the involvement of centrally formed acetaldehyde in the mediation of ethanol's psychopharmacological effects.

Acetaldehyde↗
PubMed1988

Hematin iron valence in catalase and peroxidase compound I: relationship to free radical reaction mechanism.

The material in this paper is centered on the structure of compound I (first reaction intermediate) in the case of catalase and a classical peroxidase (horseradish peroxidase, HRP). The concept of a pi-cation radical is accepted for HRP but is rejected in the case of catalase. A possible mechanism for catalatic action previously proposed assumes FeV for the hematin iron of catalase and hydride ion transfer in the reduction of FeV by the second molecule of H2O2, no free radical being involved. In the case of HRP however, FeIV is assumed for compound I. A hypothetical .OH needed to balance the reaction for the formation of compound I is thought to interact with the pi electron cloud of the hematin prosthetic group, forming the now generally accepted pi cation radical and an OH- ion. Attempts to apply the pi cation mechanism to catalatic action lead to contradictions and implausible chemical reactions.

Catalase↗
PubMed1993

Application of an integrated rate equation to the inactivation of catalase.

A feature of catalase that has received scant attention in recent years and that may have physiological significance is the peroxide-dependent inactivation of the enzyme. In this article we show how to obtain the second-order rate constant for the inactivation reaction by fitting the reaction progress curve to an integrated rate equation. This method will simplify quantitation of the inactivation and reactivation of catalase. These measurements in tissues with altered metabolic states may reveal new information about the role of catalase in nutrition, aging, and pathology.

Animals↗
PubMed1995

Protective effects of lazaroid U74389F (16-desmethyl tirilazad) on endrin-induced lipid peroxidation and DNA damage in brain and liver and regional distribution of catalase activity in rat brain.

Endrin, a poly-halogenated cyclic hydrocarbon, induces hepatic lipid peroxidation, modulates calcium homeostasis, decreases membrane fluidity, and increases nuclear DNA damage. Little information is available on the neurotoxicity of endrin. The effects of endrin on lipid peroxidation, DNA damage, and regional distribution of catalase activity were assessed in rat brain and liver 24 h following an acute oral dose of 4.5 mg endrin/kg. Lipid peroxidation associated with whole brain mitochondria increased 2.4-fold, whereas microsomal lipid peroxidation increased 2.8-fold following endrin administration. Lipid peroxidation also increased 2.0-fold both in hepatic mitochondria and microsomes. Catalase activity decreased 24% in the hypothalamus, 23% in the cortex, 38% in the cerebellum, and 11% in the brain stem in response to endrin. A 4.3-fold increase in brain nuclear DNA-single strand breaks (SSB) was observed in endrin-treated rats. Pretreatment of rats intraperitoneally with the lazaroid U74389F (16-desmethyl tirilazad) (10 mg/kg in two doses) attenuated the biochemical consequences of endrin-induced oxidative stress. The administration of U74389F in citrate buffer (pH 3.8) provided better protection than administering the lazaroid in corn oil, decreasing endrin-induced lipid peroxidation by 50-80% and DNA-SSB by approximately 72% in liver and 85% in brain, while ameliorating the suppressed catalase activity. The data suggest an involvement of an oxidative stress in the neurotoxicity and hepatotoxicity induced by endrin, which can be attenuated by the lazaroid U74389F.

Animals↗
PubMed1991

Oxidative stress effects on conjugational recombination and mutation in catalase-deficient Escherichia coli.

The objective of the present investigation was to determine the effects on genetic recombination and mutation in Escherichia coli of either endogenous increases in oxygen radicals resulting from catalase deficiencies, or exogenous increases resulting from H2O2 treatment. Using the classical paradigm of Escherichia coli bacterial conjugation, strains deficient in the production of hydroperoxidase I (HPI) and/or hydroperoxidase II (HPII) were used as recipients in Hfr x F- matings. 'Background' recombination rates, measured by the rate of appearance of threonine prototrophs, was similar to wild-type levels in the HPI-deficient (katG) strain, but were significantly decreased in HPII- (katE) mutants. The addition of relatively nontoxic H2O2 concentrations (0.25 mmoles dm-3) to the mating mixtures stimulated recombination rates in wild-type and katE strains, but decreased rates in katG and katEkatG strains. A 0.5 mmoles dm-3 concentration of H2O2 inhibited recombination rates in all strains. In order to gauge the level of recA-dependent 'SOS' processes occurring under the experimental conditions, 'background' mutation rates were determined in both fluctuation and forward mutation (thyA) assays. Mutation rates in aerobically-grown cultures were increased up to 2.2-fold in katG and katEkatG strains. Treatment with relatively nontoxic H2O2 concentrations elevated the thyA mutagenesis up to 8-fold in catalase-deficient cultures. Furthermore, these studies along with data presented elsewhere show that the SOS phenotype of katEkatG is more resistant than that of katG strains. These studies clearly show that cellular oxidative stress occurring from catalase deficiency interferes with normal DNA metabolism.

Antioxidants↗
PubMed1994

The rapid potentiometric detection of catalase positive microorganisms.

The rate of fluoride ion release from the enzymatic cleavage of fluoride ion from 4-fluorophenol by horseradish peroxidase, in the presence of hydrogen peroxide, was measured using a fluoride ion selective electrode. Monitoring the utilisation of hydrogen peroxide by catalase (intracellularly present in almost all aerobic microorganisms) in the presence of 4-fluorophenol demonstrated the inhibition of the enzyme. Horseradish peroxidase appeared to impart a partial protective mechanism of this inhibition. The development of a sequential assay demonstrated the applicability of the proposed method in the assessment of aerobic microorganism numbers. The judicious variation of three parameters, the length of incubation, the concentration of the primary substrate (hydrogen peroxide) and the indicator enzyme activity (horseradish peroxidase), affected both the detection limit and the sensitivity of the assay. Typically with a 15 minute incubation, a detection limit for catalase activity of 1.5 x 10(-6) Uml-1 was obtained together with a sensitivity of 2.42 mumol l-1 s-1 per decade change in activity. Application of the developed catalase assay to the detection of Escherichia coli achieved a detection limit of 1 x 10(2) colony forming units (cfu) ml-1 with a sensitivity of 3.26 mumol l-1 s-1 per decade change in intact microorganisms. By lysis of the microorganisms the detection limit was further reduced to less than 10 cfu ml-1, indicating the future possibilities of the assay.

Bacteria, Aerobic↗
PubMed1995

Absence of mutations in the Mn superoxide dismutase or catalase genes in familial amyotrophic lateral sclerosis.

Familial amyotrophic lateral sclerosis (FALS) is an autosomal dominant, adult onset, neurological disorder caused by the degeneration of motor neurons of the cortex, brainstem and spinal cord. Recently, the defective gene in some FALS families was identified as the Cu/Zn superoxide dismutase (SOD1) gene. However, SOD1 mutations are present in approximately 20% of patients with FALS. We have tested the genes of two more free radical detoxifying enzymes, Mn superoxide dismutase (SOD2) and catalase by single strand conformation analysis (SSCA) for mutations in the remaining FALS cases. No mutations were found in the catalase enzyme in 73 unrelated FALS cases; mutations were not detected in the 66% of the SOD2 gene analyzed. FALS does not appear to be caused by mutations in the SOD2 nor the catalase genes.

Amyotrophic Lateral Sclerosis↗
PubMed2004

Catalase transgenic mice: characterization and sensitivity to oxidative stress.

The role of catalase in the antioxidant defense system was studied using transgenic mice [Tg(CAT)] harboring a human genomic clone containing the entire human CAT gene. Catalase activity was 2-fold higher in the tissues of hemizygous [Tg(CAT)(+/o)] mice and 3- to 4-fold higher in the tissues of homozygous [Tg(CAT)(+/+)] mice compared to wild type mice. The human CAT transgene was expressed in a tissue-specific pattern that was similar to the endogenous catalase gene. The levels of other major antioxidant enzymes were not altered in the tissues of the transgenic mice. Hepatocytes and fibroblasts from the Tg(CAT)(+/+) mice were more resistant to hydrogen peroxide-induced cell death but were more sensitive to paraquat and TNFalpha toxicity. Fibroblasts from the Tg(CAT)(+/+) mice showed reduced growth rate in culture without treatment and reduced colony-forming capability after gamma-irradiation compared to fibroblasts from wild type mice. In addition, the Tg(CAT)(+/+) animals were more sensitive to gamma-irradiation.

Animals↗
PubMed2004

Overexpression of catalase or Bcl-2 alters glucose and energy metabolism concomitant with dexamethasone resistance.

Glucocorticoids induce apoptosis in lymphocytes by causing the release of cytochrome c into the cytosol; however, the events in the signaling phase between translocation of the steroid-receptor complex to the nucleus and the release of cytochrome c have not been elucidated. Previously, we found that, in response to steroid treatment, WEHI7.2 mouse thymic lymphoma cells overexpressing catalase (CAT38) show delayed apoptosis (delayed cytochrome c release) compared to the parental cells, while Bcl-2 overexpressing cells (Hb12) are protected from steroid-induced apoptosis. In lymphocytes, glucocorticoid treatment decreases glucose uptake. Both glucose deprivation and the attendant ATP drop are known inducers of apoptosis. Therefore, we used (31)P and (1)H NMR spectroscopy to compare metabolic profiles of WEHI7.2, CAT38 and Hb12 cells in the presence and absence of dexamethasone to determine: (1) whether glucocorticoid effects on glucose metabolism contribute to the mechanism of steroid-induced apoptosis; and (2) whether catalase or Bcl-2 overexpression altered metabolism thereby providing a mechanism of steroid resistance. Loss of mitochondrial hexokinase activity was correlated to the induction of apoptosis in WEHI7.2 and CAT38 cells. CAT38 and Hb12 cells have an altered basal metabolism which includes increases in hexokinase activity, lactate production when subcultured into new medium, use of mitochondria for ATP production and potentially increased glutaminolysis. These data suggest that: (1) glucocorticoid effects on glucose metabolism may contribute to the mechanism of steroid-induced lymphocyte apoptosis; and (2) the altered metabolism seen in catalase and Bcl-2 overexpressing cells may contribute to both the steroid resistance and increased tumorigenicity of these variants.

Adenosine Triphosphate↗