Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P04040 (Catalase)
 3,577 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ten patients with chronic renal failure (CRF) treated by hemodialysis (HD) were examined. All the patients demonstrated remarkable anemia. The red blood cell count was (2.7 +/- 0.2) x 10(12)/I the concentration of hemoglobin 79.5 +/- 5.6 g/l, on the average, hematocrit 23.2 +/- 1.8%. The content of malonic dialdehyde in the patients' red blood cells was far greater than in controls, amounting to 132% (per 1 ml of hemolysate), 134% (per 1 mg of protein) (p < 0.05). Catalase and glutathione peroxidase activity in the patients' red blood cells did not differ from that in controls. Superoxide dismutase activity reduced by 43% as compared to that in donors (p < 0.001). The authors review possible mechanisms of lipid peroxidation (LPO) and a decrease of antioxidant defense in red blood cells of CRF patients on hemodialysis. It is concluded that activation of LPO processes and the decrease of antioxidant defense produce a noticeable destructive effect on the integrity of the red blood cell membrane. They also influence the development of hemolysis.
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PMID:[Lipid peroxidation as a possible mechanism of erythrocyte damage in patients with chronic kidney failure on hemodialysis]. 144 Mar 43

Using lucigenin-enhanced chemiluminescence, isolated rat lungs perfused with physiological salt-Ficoll solution were studied to test whether phorbol myristate acetate (PMA)-induced lung injury was mediated by reactive oxygen species (ROS). PMA (0.03 micrograms ml-1) caused small but significant increases in lung ROS levels and pulmonary arterial perfusion pressure (Ppa) but did not induce lung oedema. PMA (0.15 micrograms ml-1) induced lung oedema with large increases in ROS production and Ppa. Superoxide dismutase (SOD) inhibited the increases in ROS, Ppa, and lung oedema. Catalase and dimethylthiourea inhibited lung oedema but did not attenuate the increases in ROS and Ppa entirely. Indomethacin attenuated lung oedema partially but did not inhibit the increases in ROS and Ppa. These data indicate that PMA-induced lung injury is dependent on PMA concentration and ROS are responsible for such lung injury. Thromboxane plays a minor role for PMA-induced lung injury. The different effects of oxygen radical scavengers suggest that different radical species contribute to the increased pulmonary vascular response and lung injury.
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PMID:Phorbol myristate acetate-induced lung injury: involvement of reactive oxygen species. 145 68

Reactive oxygen metabolites have been postulated to play an important role in both toxic and ischemic forms of acute renal tubular epithelial injury. In the present study, we examined the effect of enzymatically generated hydrogen peroxide on LLC-PK1 cells, a renal proximal tubule cell line. Exposure of LLC-PK1 cells to glucose and glucose oxidase (GO; which generates hydrogen peroxide) resulted in cytotoxicity (as measured by trypan blue exclusion) which was dose dependent and increased linearly over time to 81 +/- 5% at 180 minutes (8 +/- 1% at time 0; mean +/- SEM, N = 3 to 7). Catalase (which decomposes hydrogen peroxide) completely prevented the cytotoxicity, confirming that the toxicity was due to hydrogen peroxide production. To assess whether the hydrogen peroxide toxicity was a direct effect or mediated by other toxic oxygen metabolites, several scavengers of reactive oxygen metabolites and iron chelators were used. Superoxide dismutase (a scavenger of superoxide) had no effect. Deferoxamine (DFO), an iron chelator, provided marked protection (GO alone 45.9 +/- 4.4%; GO + DFO 13.0 +/- 2.0%; control 7.1 +/- 1.2%; N = 15 to 17, P less than 0.001). Pretreatment with DFO (1 hr, then 2 washes to remove DFO before GO addition) also markedly inhibited the cytotoxicity, suggesting that DFO's effect was due to iron chelation. Two other metal chelators (dihydroxybenzoic acid and 1,10-phenanthroline) also significantly decreased the GO-induced cytotoxicity. However, three of four hydroxyl radical scavengers used (mannitol, dimethyl sulfoxide, sodium benzoate) did not significantly decrease cell death. Only dimethylthiourea provided protection.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Hydrogen peroxide cytotoxicity in LLC-PK1 cells: a role for iron. 166 14

The effects of catalase, superoxide dismutase, mannitol, glutathione, and diallyl sulfide on quercetin-induced DNA damage and lipid peroxidation were investigated in a model system of isolated rat-liver nuclei under aerobic conditions and in the presence of equimolar iron or copper. Mannitol produced a small but significant inhibition of the concurrent nuclear DNA damage and lipid peroxidation induced by quercetin in the presence of iron or copper. Catalase significantly decreased quercetin-induced nuclear DNA damage only in the presence of iron and had no significant effect on lipid peroxidation. Superoxide dismutase showed no significant effect on nuclear DNA damage, but stimulated the quercetin-induced lipid peroxidation only in the presence of copper. Glutathione significantly inhibited the nuclear lipid peroxidation but enhanced the DNA damage. Diallyl sulfide significantly enhanced the nuclear DNA damage but stimulated the lipid peroxidation only in the presence of iron. These results suggest that the reactive oxygen species, especially the hydroxyl radicals, are responsible for the concurrent lipid peroxidation and DNA damage induced by quercetin in the presence of iron or copper in isolated rat-liver nuclei.
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PMID:Effects of antioxidants on quercetin-induced nuclear DNA damage and lipid peroxidation. 175 17

Superoxide dismutase (SOD) and catalase are enzymes that protect cells from radical attack. Catalase disproportionates hydrogen peroxide, and SOD is an oxidoreductase that serves to dismutate the superoxide anion. The objective of this communication was to measure the activity of these disproportionating enzymes in the chick tibial growth cartilage and to relate enzyme activity to chondrocyte maturation and tissue calcification. Analytic techniques were optimized for the measurement of both enzymes; particular care was taken to ensure that the values obtained were due to SOD and catalase, not to the presence of other oxidases or contaminants. Catalase and SOD had similar profiles of activity in cartilage. For both enzymes, the highest levels of activity were observed in premineralized cartilage; as chondrocytes matured there was a progressive decrease in the activity of SOD and catalase. Comparison of chondrocyte SOD activity with nonmineralizing tissues indicated that the activity of cultured cartilage cells was low. We also measured the SOD activity of avascular chondrodystrophic cartilage and found it to be less than that of proliferating cartilage. When cartilage was electrofocused, three SOD isozymes were detected. The pI of the major isozyme corresponded to the copper-zinc isoform. We suggest that the observed changes in enzymatic activity are dependent on a number of cartilage-specific factors that include the vascular supply, the local production of oxygen radicals by chondrocytes, and the oxidative state of the tissue.
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PMID:Superoxide dismutase and catalase activities in the growth cartilage: relationship between oxidoreductase activity and chondrocyte maturation. 188 19

To discover the relationship between the activation of protein kinase C and the generation of reactive oxygen in the tumor promotion process, we investigated the effects of radical scavengers on diacylglycerol-promoted transformation in BALB/3T3 cells. Superoxide dismutase (SOD) showed inhibitory effects on both 1-oleoyl-2-acetylglycerol (OAG)-promoted and diolein-promoted transformation. Catalase (CT) suppressed the promoting effects of diolein by up to 70%. Mannitol (MT), a hydroxyl radical (.OH) scavenger, inhibited diacylglycerol-promoted transformation dose-dependently. These results suggest that activation of protein kinase C alone is insufficient and that generation of reactive oxygen accompanied by activation of the enzyme is essential to the promotion process in BALB/3T3 cells.
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PMID:Inhibitory effects of radical scavengers on diacylglycerol-promoted transformation in BALB/3T3 cells. 190 66

Oxidative stress responses were tested in the unicellular cyanobacterium synechococcus PCC 7942 (R-2). Cells were exposed to hydrogen peroxide, cumene hydroperoxide and high light intensities. The extent and time course of oxidative stress were related to the activities of ascorbate peroxidase and catalase. Ascorbate peroxidase was found to be the major enzyme involved in the removal of hydrogen peroxide under the tested oxidative stress. Catalase activity was inhibited in cells, treated with high H2O2 concentrations, and was not induced under photooxidative stress. Catalase was specifically induced in cells treated with cumene hydroperoxide. Superoxide dismutase activity increased under conditions generating superoxide, such as high light intensities. The induction of the antioxidative enzymes was light dependent and was inhibited by chloramphenicol.
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PMID:Oxidative stress responses in the unicellular cyanobacterium Synechococcus PCC 7942. 190 71

Damage to the bases in DNA by the cupric ion-1,10-phenanthroline complex was investigated. Ten base products in DNA were identified and quantitated by the use of gas chromatography/mass spectrometry with selected-ion monitoring. DNA damage by the cupric ion-1,10-phenanthroline complex required the presence of a reducing agent such as ascorbic acid or mercaptoethanol. Products identified were typical hydroxyl radical induced products from the pyrimidines and purines in DNA, well-known from previous studies using various hydroxyl radical producing systems such as ionizing radiation, hypoxanthine/xanthine oxidase, or hydrogen peroxide in the presence of transition metal ions. Product formation was not significantly inhibited by typical scavengers of hydroxyl radical such as mannitol and sodium formate, but there was partial inhibition by dimethyl sulfoxide. Catalase substantially decreased formation of base products, and added hydrogen peroxide stimulated it, indicating the hydrogen peroxide dependency of DNA base damage. Superoxide dismutase afforded only a partial reduction in product yields in systems containing ascorbic acid. On the basis of the types of base products formed, the hydrogen peroxide dependency of product formation, and a previous report suggesting that DNA damage is due to a diffusible species [Williams, L. D., Thivierge, J., & Goldberg, I. H. (1988) Nucleic Acids Res. 16, 11607-11615], we propose that DNA base damage is caused by hydroxyl radical.
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PMID:Modification of bases in DNA by copper ion-1,10-phenanthroline complexes. 212 17

Reactivities of o-phenylphenol and its metabolites (2,5-dihydroxybiphenyl, 2-phenyl-1,4-benzoquinone) with DNA were investigated by a DNA sequencing technique, and the reaction mechanism was studied by UV-visible and ESR spectroscopies. In the presence of Cu(II), 2,5-dihydroxybiphenyl caused strong DNA damage even without piperidine treatment. Catalase, methionine, and methional inhibited the DNA damage completely, whereas mannitol, sodium formate, ethanol, tert-butyl alcohol, and superoxide dismutase did not. 2,5-Dihydroxybiphenyl plus Cu(II) frequently induced a piperidine-labile site at thymine and guanine residues. The addition of Fe(III), Mn(II), Co(II), Ni(II), Zn(II), Cd(II), or Pb(II) did not induce DNA damage with 2,5-dihydroxybiphenyl. When H2O2 was added, 2-phenyl-1,4-benzoquinone also induced DNA damage in the presence of Cu(II). Cu(II) accelerated the autoxidation of 2,5-dihydroxybiphenyl to quinone. An ESR study revealed that the semiquinone radical is an intermediate of the autoxidation. Catalase had no inhibitory effect on the acceleration by Cu(II). Superoxide dismutase promoted both the autoxidation of 2,5-dihydroxybiphenyl and the initial rate of semiquinone radical production. ESR spin trapping experiments showed that the addition of Fe(III) produced hydroxyl radical during the autoxidation of 2,5-dihydroxybiphenyl, whereas the addition of Cu(II) hardly did so. The results suggest that DNA damage by 2,5-dihydroxybiphenyl plus Cu(II) is due to active species other than hydroxyl free radical.
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PMID:DNA damage induced by metabolites of o-phenylphenol in the presence of copper(II) ion. 213 Sep 42

Desferrioxamine (DFO) nearly doubles alkaline phosphatase oxidative inactivation by the ascorbate system. The effect is dependent on ascorbate and desferrioxamine concentrations, exhibiting in both cases a saturation mechanism. Conversion of desferrioxamine to ferrioxamine abolishes the prooxidant action. Desferrioxamine also increases ascorbate-dependent oxygen consumption and nitroblue tetrazolium reduction. Superoxide dismutase, which blocks the desferrioxamine enhancing effect on enzyme inactivation, markedly slows down nitroblue tetrazolium reduction as well as oxygen consumption by ascorbate plus desferrioxamine, while it fails to protect against the ascorbate system alone. Therefore, in the presence of desferrioxamine, the metal-catalyzed ascorbate autooxidation becomes superoxide-dependent and thus inhibitable by superoxide dismutase. Catalase, peroxidase, and ascorbate oxidase protect alkaline phosphatase from inactivation by both ascorbate and ascorbate-desferrioxamine systems. Hemin shields the enzyme from ascorbate plus DFO attack but not from ascorbate alone. In air-saturated solution, desferrioxamine seems to mediate one electron transfer from ascorbate to oxygen, generating superoxide anions, which can either trigger a Fenton reaction or produce desferal nitroxide radicals. In the absence of oxygen, ascorbate alone is ineffective, but the ascorbate plus desferrioxamine system still inactivates the enzyme; catalase, peroxidase, and ascorbate oxidase, but not superoxide dismutase, afford protection.
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PMID:Prooxidant action of desferrioxamine: enhancement of alkaline phosphatase inactivation by interaction with ascorbate system. 215 77


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