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

Cell number, protein, and phorbol myristate acetate (PMA)-induced H2O2 production were measured in cultured human peripheral blood monocytes for six days after exposure to varying doses of gamma-radiation. Both the number of adherent cells and the protein per dish decreased with increasing radiation doses. The dose of radiation decreasing the number of adherent cells by 37% on days 4 and 6 postirradiation was 29 Gy. Four hours postirradiation there was a small decrease in PMA-induced H2O2 production for doses of 7.5 Gy or greater; levels returned to normal by eight hours and increased at 24 hours postirradiation. By day 4 postirradiation significant increases in PMA-induced H2O2 production were noted at all radiation doses (2.5 to 50 Gy). This increase was not due to a shift in the PMA dose-response curve, a change in the time course of the PMA response, or an effect of decreased cell density on the assay system. Superoxide levels were not significantly changed in cells exposed to 20 Gy. Catalase, glutathione peroxidase, and superoxide dismutase levels also were unchanged. Culturing irradiated cells with gamma-interferon increased PMA-induced H2O2 release, which indicated that irradiated cells retained their capacity to respond to gamma-interferon. These data demonstrate that irradiation affects the PMA-induced H2O2 production of human monocytes in a time- and dose-dependent manner. An increase in the release of reactive oxygen intermediates by the macrophage may play a role in enhancing the deleterious effects of radiation in vivo.
Blood 1987 Sep
PMID:Exposure to gamma-irradiation increases phorbol myristate acetate-induced H2O2 production in human macrophages. 304 Jan 53

Aerobic incubations of the Tritrichomonas foetus hydrogenosomal fraction containing pyruvate, CoA, and the spin trap 5,5-dimethyl-1-pyrroline N-oxide (DMPO) gave spectra of two radical adducts. One was a carbon-centered radical adduct of DMPO. This radical was centered at C-3 of pyruvate as determined in experiments using [13C]pyruvate. The other radical detected was identified as the CoA radical adduct of DMPO by comparison with an adduct obtained by incubating CoA with DMPO, H2O2 and horseradish peroxidase. Deletion of CoA led to an increased stability of the carbon-centered radical adduct of DMPO, disappearance of the thiyl radical adduct of DMPO, and appearance of a hydroxyl radical adduct of DMPO. Superoxide dismutase suppressed the appearance of the DMPO-hydroxyl radical adduct but did not have any inhibitory effect on the appearance of the other adducts. Catalase had no significant effect on any of the adducts. Addition of pyruvate to these hydrogenosomal preparations stimulated oxygen consumption. Addition of CoA led to a further increase in the rate of O2 uptake but had no effect in the absence of pyruvate. The formation of two substrate free radicals as intermediates in the generation of acetyl-CoA represents a novel mechanism for this enzymatic reaction and indicates that the pyruvate:ferredoxin oxidoreductase from T. foetus differs significantly from the pyridine nucleotide-dependent pyruvate dehydrogenase complex of other eukaryotic cells in its catalytic mechanism.
J Biol Chem 1987 Sep 15
PMID:Free radical intermediates in the reaction of pyruvate:ferredoxin oxidoreductase in Tritrichomonas foetus hydrogenosomes. 304 Jul 44

The nucleotide sequence of a 2785-base-pair stretch of DNA containing the Saccharomyces cerevisiae catalase A (CTA1) gene has been determined. This gene contains an uninterrupted open reading frame encoding a protein of 515 amino acids (relative molecular mass 58,490). Catalase A, the peroxisomal catalase of S. cerevisiae was compared to the peroxisomal catalases from bovine liver and from Candida tropicalis and to the non-peroxisomal, presumably cytoplasmic, catalase T of S. cerevisiae. Whereas the peroxisomal catalases are almost colinear, three major insertions have to be introduced in the catalase T sequence to obtain an optimal fit with the other proteins. Catalase A is most closely related to the C. tropicalis enzyme. It is also more similar to the bovine liver catalase than to the second S. cerevisiae catalase. The differences between the two S. cerevisiae enzymes are most striking within four blocks of amino acids consisting of a total of 37 residues with high homology between the three peroxisomal, but low conservation between the S. cerevisiae catalases. The results obtained indicate that the peroxisomal catalases compared have very similar three-dimensional structures and might have similar targeting signals.
Eur J Biochem 1988 Sep 01
PMID:Sequence of the Saccharomyces cerevisiae CTA1 gene and amino acid sequence of catalase A derived from it. 304 40

The mutagenic activities of 6 of the chemicals identified in coffee solutions were assayed with the Salmonella Ara test, under experimental conditions optimized for coffee mutagenicity. Caffeine was the only non-mutagenic compound. Among the other 5 chemicals, hydrogen peroxide was the strongest mutagen and chlorogenic acid the weakest; methylglyoxal, glyoxal and caffeic acid exhibited intermediate mutagenicities. The minimal mutagenic doses of these components correlated negatively with their relative concentrations in coffee. It was concluded that chlorogenic acid, caffeic acid, glyoxal and methylglyoxal cannot contribute alone to the mutagenicity of coffee in the Ara test, since their minimal mutagenic concentrations were much higher than their respective levels in the coffee samples assayed. By contrast, 40-60% of the mutagenic activity in coffee and also in tea could be attributed to their H2O2 contents. Catalase abolished more than 95% of the mutagenic activity of coffee, as detected by the Ara test. A similar sensitivity to catalase has been reported by other authors in relation to the coffee mutagenicity identified by the Salmonella His test. Nevertheless, the results presented in this paper suggest that the Ara forward and the His reverse mutation tests are sensitive to the mutagenicity of different constituents in coffee solutions. We propose that the His test, sensitive at high coffee doses, mainly recognizes the mutagenicity of methylglyoxal, whilst the Ara test, sensitive at low coffee doses, mainly detects the mutagenic activity of hydrogen peroxide. The data reported also suggest that the direct-acting mutagenicity(ies) detected by the Ara test in tea solutions is (are) based on similar, if not identical, mechanisms.
Mutat Res 1988 Sep
PMID:Study of the causes of direct-acting mutagenicity in coffee and tea using the Ara test in Salmonella typhimurium. 304 75

We determined the effect of H2O2 on both the physiological and biochemical lung changes seen in the adult sheep after endotoxin. Fourteen unanesthetized adult sheep with chronic lung lymph fistula were given Escherichia coli endotoxin (1 microgram/kg) over 30 min. Seven sheep were given catalase (32,500 U/kg body wt) as an intravenous bolus 30 min before endotoxin. Four sheep were given catalase alone. Oxidant lung changes were measured using arterial plasma conjugated dienes and lung tissue malondialdehyde (MDA) content, both reflecting the lipid peroxidation process. Animals were killed 5 h after endotoxin. We found that endotoxin alone caused an early increase in pulmonary arterial pressure lung lymph flow (QL), plasma thromboxane B2, 6-keto-prostaglandin F1 alpha, and plasma conjugated dienes. A decrease in cardiac output and arterial PO2 was also seen. A three- to four-fold increase in protein-rich QL was noted at 3-4 h as well as a continued increase in arterial conjugated dienes. Lung MDA and water content were also significantly increased from base line. Catalase pretreatment significantly attenuated both the physiological changes and the prostanoid and conjugated diene release. Lung MDA and water content also remained at base line. We conclude that H2O2 plays a major role in endotoxin-induced lung injury as well as the resulting lipid peroxidation process.
J Appl Physiol (1985) 1988 Sep
PMID:Catalase prevents prostanoid release and lung lipid peroxidation after endotoxemia in sheep. 318 91

In the presence of intact Ehrlich ascite carcinoma cells and the supernatant obtained by preincubation and subsequent precipitation of cells, egg phosphatidylcholine is oxidized in liposomes to form malonic dialdehyde (MDA). Catalase and carbon dioxide markedly reduce, whereas sodium azide increases MDA accumulation during liposome incubation with the cells. EDTA, diethylthiocarbonate and alpha-tocopherol effectively inhibit, whereas ascorbate and cysteine strongly activate MDA synthesis in both cases. Superoxide dismutase has no appreciable effect on these processes. It is concluded that metal-containing catalysts and the H2O2 released by intact cells into the incubation medium induce lipid peroxidation in liposomes.
Biokhimiia 1988 Sep
PMID:[Mechanism of formation of malonic dialdehyde during liposome interaction with cells]. 320 6

Significant pulmonary toxicity is associated with the use of nitrofurantoin; however, the mechanism of cellular toxicity remains poorly characterized. By using a novel in vitro red blood cell (RBC) chromium 51 cytotoxicity assay, cell injury induced by nitrofurantoin was quantified with normocatalasemic BALB/c RBCs and hypocatalasemic (but otherwise genetically identical) CCN RBCs as target cell populations. Nitrofurantoin at concentrations of 2 x 10(-4) and 4 x 10(-4) mol/L resulted in significant injury to normocatalasemic RBCs with a cytotoxic index (CI) of 21.7% +/- 3.7% and 65.3% +/- 3.7% (p less than 0.05, both comparisons). This injury was substantially increased when nitrofurantoin (2 x 10(-4) and 4 x 10(-4) mol/L was incubated with hypocatalasemic RBCs, resulting in CIs of 59.0% +/- 7.4% and 91.0% +/- 2.0% respectively (p less than 0.05, both comparisons with normocatalasemic RBCs). Direct oxidant-mediated cytotoxicity induced by either H2O2 or the superoxide anion radical (as generated by xanthine-xanthine oxidase) also resulted in more significant injury to hypocatalasemic RBCs than to normocatalasemic RBCs (p less than 0.05, both comparisons). Catalase levels of CCN RBCs were approximately 7% of control BALB/c RBC values; however, the activities of superoxide dismutase and glutathione peroxidase were identical in both populations of RBCs. This model, using genetically defined target cell populations, clearly demonstrates the importance of endogenous catalase in protecting against nitrofurantoin-induced cytotoxicity, suggesting that H2O2 is a critical intermediary in the direct cell injury mediated by the drug.
J Lab Clin Med 1988 Sep
PMID:Importance of hydrogen peroxide in nitrofurantoin-induced cytotoxicity: evidence from an inbred catalase-deficient strain of mice. 341 Nov 91

The ability of granulocyte-macrophage colony-stimulating factor (CSF-H) to modulate human neutrophil functions was studied by using an in vitro system in which this cell type interacted with intracellular (amastigote [AMA]) forms of Trypanosoma cruzi. The presence of CSF-H during the 30-min period of neutrophil incubation with the AMA markedly enhanced parasite internalization. This effect was evidenced by significant increases in both the percentage of neutrophils incorporating AMA and the average number of AMA per 100 neutrophils with respect to mock-treated neutrophils. Pretreatment of the neutrophils with CSF-H reproduced the enhancement effect, whereas pretreatment of the AMA had no detectable consequence. The minimal neutrophil CSF-H pretreatment period required to significantly increase the number of AMA per 100 neutrophils was 20 min--suggesting that CSF-H induced time-dependent events ultimately leading to the manifestation of the noted effect--but neutrophil treatment with CSF-H for longer periods of time (up to 60 min) caused a much greater enhancement. Consistent with the notion of a regulatory action of CSF-H on neutrophils was the fact that the enhancing effect subsided gradually after removal of the factor and was no longer detectable after 16 hr. When 3H-labeled AMA were used, CSF-H-treated neutrophils released greater amounts of radiolabeled substances than mock-treated cells, indicating a stimulatory effect of CSF-H on the killing capacity of neutrophils. This was confirmed by the fact that untreated neutrophils that had internalized 3H-AMA killed the parasites at a faster rate when subsequently incubated with CSF-H. Catalase, but not superoxide dismutase, mannitol, benzoate, or histidine, inhibited neutrophil killing of the 3H-AMA whether the granulocytes had been exposed to CSF-H or not. This indicated that the cytotoxic mechanism involved the production of hydrogen peroxide in both cases, but possibly at a higher rate in the CSF-H-treated neutrophils. These results point to a regulatory effect of CSF-H on neutrophils that promotes cellular activities that might be relevant to the mechanisms of clearance of T. cruzi in vivo.
J Immunol 1986 Sep 01
PMID:Effects of human colony-stimulating factor on the uptake and destruction of a pathogenic parasite (Trypanosoma cruzi) by human neutrophils. 352 88

We report in detail the ontogeny and the response of antioxidant enzymes to glucocorticoids in the rat small intestine. Pregnant rats in the treatment group received four injections of dexamethasone starting on days 18, 19, or 20 of gestation; fetuses were killed 2 days later. Control rats were injected with 0.9% saline solution. Postnatal rats reaching 14, 19, and 104 days of age received four injections of hydrocortisone and were killed 2 days later. Age-matched controls were injected with 0.9% saline solution. The activities of xanthine oxidase, superoxide dismutase, and catalase were measured in small intestines from fetal (20 and 21 days gestation), newborn, and older (aged 16, 21, and 106 days) rats. Xanthine oxidase rose with maturation; the major increase occurred on postnatal day 21. Catalase and superoxide dismutase rose minimally during intrauterine life. On day 16 postpartum, catalase and superoxide dismutase values were 160% and 60%, respectively, higher than at birth. Glucocorticoid administration stimulated maltase and sucrase activities, but had no effect on the antioxidant enzymes or xanthine oxidase.
J Pediatr 1987 Sep
PMID:Maturation of antioxidant enzymes in rat small intestine: lack of glucocorticoid stimulation. 362 18

In germinating pumpkin seeds, catalase is synthesized as a precursor (59-kDa) form, with molecular mass larger than the mature molecule (55 kDa). Both the precursor and mature forms of catalase are localized in the microbodies, i.e., glyoxysomes and leaf peroxisomes [Proc. Natl. Acad. Sci. USA 81, 4809-4813 (1984)]. We have now purified the 59-kDa catalase precursor and compared its properties with those of the 55-kDa mature molecule. The molar catalytic activity of the 59-kDa catalase was tenfold lower than that of the 55-kDa molecule, whereas the heme content was found to be same, with both forms containing four hematin groups per molecule. It is inferred from these results that the low activity of the 59-kDa molecule is not related to the binding of heme to the protein, but presumably involves conformational differences between the 59-kDa and 55-kDa molecules. We have further found that the reduction of total catalase activity in pumpkin cotyledons during greening was due to a decrease in the amount of the enzymically active 55-kDa catalase accompanying an increase in the 59-kDa molecule.
Eur J Biochem 1986 Sep 01
PMID:Purification and characterization of heme-containing low-activity form of catalase from greening pumpkin cotyledons. 375 67


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>