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)

The effectiveness of 24-hour hypothermic machine perfusion with TP-V (a hyperosmolar colloid solution containing dextrose, sucrose and ATP-MgCl2) alone, or in combination with oxygen free radical scavengers, was evaluated in isolated-perfused canine heart-lungs. Heart-lungs were perfused at 4 degrees C in either TP-V (n = 6), TP-V/Allopurinol (500 mg/L) (n = 6), or TP-V/Allopurinol (500 mg/L) & Catalase (5000 U/L) (n = 5). Lung inflation was maintained with 100% nitrogen. Following preservation, the heart-lungs were perfused with an albumin-mannitol perfusate for 3 hours at 37 degrees C, for functional, hemodynamic, and laboratory determinations. Cold preservation with TP-V/Allopurinol, and TP-V/Allopurinol & Catalase resulted in physiologically normal LDH levels during the 3-hour normothermic isolated perfusion test period. Significantly lower enzyme activity for CPK was evident at 0 (p less than .005) and 3 hours (p less than .05) of perfusion, while no significant differences in lactate production were seen among the groups. In addition, pH, PCO2, PO2, and left ventricular, aortic, and coronary artery pressures all remained within normal physiologic range, with no significant differences seen among the three groups. 99m Technetium scans demonstrated adequate patency among the heart-lungs, with better flow seen in those perfused with TP-V/Allopurinol & Catalase. Histological specimens confirmed a decrease in myocardial and pulmonary damage when Allopurinol and/or Catalase was used. It appears that oxygen free radical scavengers provide some protection from canine heart-lungs which have been hypothermically preserved for 24 hours.
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PMID:Effect of 24-hour preservation with oxygen free radical scavengers on isolated-perfused canine heart-lungs. 302 18

In this study we tried to define the possible benefits of the oxygen-derived free radical scavengers after 3 hours of cold myocardial global ischemia, as required in the setting of cardiac transplantation. Twenty-one pig hearts were harvested after preservation with a cold cardioplegic solution (St. Thomas' Hospital solution) and topical cooling. Normothermic reperfusion with blood was achieved with a special heart-lung machine preparation, which allows the heart to beat in a working or nonworking mode. Twelve hearts served as control hearts (group I), and nine (group II) were subjected to superoxide dismutase and catalase. Superoxide dismutase was applied at a dose of 40 U/ml of cardioplegic solution and 1500 U/kg body weight with the start of reperfusion. Catalase was added to the cardioplegic solution in a dose of 100 U/kg and 3500 U/kg body weight with the start of reperfusion. After 15 minutes of retrograde reperfusion, both left ventricular developed pressure and its first derivative were significantly higher in group II (137 +/- 7.6 mm Hg, 2467 +/- 162 mm Hg/sec) than in group I (105 +/- 6 mm Hg, 1676 +/- 231 mm Hg/sec, p less than 0.05 for each). In addition, a considerably higher coronary blood flow was observed in group II throughout the 180-minute period of reperfusion (p = 0.047). We therefore conclude that the combined administration of superoxide dismutase and catalase during the initial period of cardioplegic arrest and during early reperfusion of donor hearts submitted to 3 hours of cold ischemia has a beneficial effect on myocardial performance.
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PMID:Oxygen-derived free radical scavengers for amelioration of reperfusion damage in heart transplantation. 327 68

The morphological alterations of hepatocytes of golden ide, Leuciscus idus melanotus, following adaptation to low and high temperatures (14 and 28 degrees C) were investigated by means of light and electron microscopy. The temperature-dependent behaviour of peroxisomes was visualized cytochemically with the alkaline diaminobenzidine medium; the morphological studies were supplemented by the biochemical determination of catalase activity. Cold adaptation of ide hepatocytes is manifested by proliferation and stacking of endoplasmic reticulum, an enhanced secretory activity of Golgi fields and a higher number of peroxisomes as compared with the warm-adapted animals. The latter organelles are characterized by a marked heterogeneity in size, shape and catalase activity, and by a more intimate association with mitochondria and endoplasmic reticulum. The occurrence of small peroxisomal profiles is restricted to lower temperature. Catalase activity can be shown both cytochemically and biochemically to increase during cold adaptation. Whereas the number of mitochondria seems to be unaffected by thermal adaptation, stacking of mitochondria as well as the formation of intramitochondrial membrane piles indicate cold-adaptive processes. A feature typical of warm-adaptation is the formation of membrane-glycogen complexes, which may represent the morphological expression of enhanced carbohydrate metabolism documented in a decreased storage of glycogen at 28 degrees C. At 28 degrees C lipid is the predominant storage product. These findings indicate that fish liver is well-suited to serve as a model for the analysis of the interaction of environmental temperature conditions and hepatic morphology.
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PMID:Ultrastructure of hepatocytes in golden ide (Leuciscus idus melanotus L.; Cyprinidae: Teleostei) during thermal adaptation. 382 56

In the rat brown fat peroxisomes - thermogenetic organules - an peroxisomal enzyme activities undergo remarkable changes during the adaptation to cold of the animals (see 3). In this paper was show that changes of peroxisomal enzyme activities occur also in liver and kidney during cold-adaptation. Catalase, L-hydroxyacid oxidase, uricase and D-aminoacid oxidase (DAO) were assayed as in (6). During cold-adaptation, the activity of the former three enzymes (Table 2) increases with the weight of the organs (Table 1) whereas that of DAO exhibits a much larger increase (Table 3). Results are discussed with regard to the contribution of the liver to non-shivering thermogenesis.
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PMID:[Cold adaptation and changes in peroxisome enzyme in various organs of the rat]. 612 6

The production of H2O2 by cells in cold paraformaldehyde-fixed frozen sections of inflammatory lesions was histochemically demonstrated by incubating them with diaminobenzidine (DAB) for 2 to 6 h. Catalase (150 micrograms/ml, about 1400 U/ml) inhibited the reaction, indicating that H2O2 was required to produce the chromogenic DAB product. Granulocytes (PMNs and eosinophils) were the main types of cells stained by the DAB reaction. Positive staining of macrophages was less frequent. The H2O2 was produced by metabolic enzymes that were still active after cell death and mild fixation. An atmosphere of 95 to 100% oxygen enhanced the specific DAB reaction, and an atmosphere of 100% nitrogen eliminated it. The DAB histochemical reaction to detect H2O2 requires the presence of peroxidases to produce the colored reaction product. Within our tissue sections, such peroxidases were evidently present in excess, because addition of low concentrations of H2O2 significantly increased the reaction product. Although some of the H2O2 produced by the granulocytes may have been derived from the dismutation of superoxide (O2-), the NADPH oxidase pathway for O2- formation did not seem to be involved: NADPH oxidase, a rather labile enzyme, should not be active after mild fixation, and diphenyleneiodonium (100 microM), an inhibitor of flavine-requiring NADPH oxidase, did not inhibit the reaction. Reactive nitrogen intermediates were also not involved, because NG-monomethyl-L-arginine and NG-nitro-L-arginine methyl ester, inhibitors of nitric oxide synthetase, did not appreciably inhibit the reaction. We conclude that stable, non-flavine-requiring oxidases, possibly cyclooxygenases or lipoxygenases, produced the H2O2 measured histochemically by our DAB reaction. These studies were made on tissue sections of acute dermal inflammatory lesions produced in rabbits by the topical application of 1% sulfur mustard [bis(2-chloroethyl) sulfide] in methylene chloride. Both intact PMNs and disintegrating PMNs in the base of the crust produced H2O2. Despite the production of H2O2 and the presence of peroxidase activity, no tissue damage was seen microscopically near the H2O2-producing cells, which indicates that the tissues are well protected by the antioxidants present in this self-limiting inflammatory reaction.
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PMID:Histochemical demonstration of hydrogen peroxide production by leukocytes in fixed-frozen tissue sections of inflammatory lesions. 793 Sep 39

Catalase (CAT), glutathione peroxidase (GSH-Px), glutathione reductase (GR), and glutathione-S-transferase (GST) activities as well as glutathione (GSH), ascorbic acid (AsA), and vitamin E concentrations were analyzed in the blood, liver, brain, interscapular brown adipose tissue (IBAT), and small intestine of rats exposed to low environmental temperature (4 degrees C; 35, 75, and 105 d of exposure) and in controls of the same age exposed to an environmental temperature of 22 +/- 2 degrees C. Prolonged cold exposure resulted in an increase in GSH-Px in IBAT and in small intestine after 35, 75, and 105 d of exposure. Catalase activity in cold-exposed animals was higher in IBAT after 75 and 105 d of cold exposure. Glutathione reductase activity was greater in brain after 35 d, in liver after 75 d, and in IBAT after 105 d of exposure to low temperatures as compared to the controls. In contrast, GST activity was lower in liver and IBAT after 35 and 75 d of cold exposure. AsA and GSH (determined only 105 d after cold exposure) were markedly higher in IBAT, whereas plasma GSH was lower and plasma AsA was higher in cold-exposed animals. The observed changes in analysed components of the antioxidant defense system under conditions of prolonged exposure to low temperature suggest that a reorganization the activity of this system at the molecular level occurred. Although other studies indicate that a 21-d cold exposure is sufficient for adaptation of thermogenesis, the present study shows that in general, longer periods are required for the registration of the changes in the antioxidant defense system.
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PMID:Effect of long-term exposure to cold on the antioxidant defense system in the rat. 840 29

The promutagenic base 8-hydroxy-2'-deoxyguanosine (8-OH-dG) in DNA is known to be formed from oxygen radical attack on 2'-deoxyguanosine (dG) as a result of oxidative stress. Formation of 8-OH-dG from dG during workup is strongly dependent on temperature and transition metals and is mediated by oxygen radicals. The 8-OH-dG formation at temperatures between 0 and 140 degrees C for 1.5 h in an "ultrapure" solution followed a third-order equation. Fe2+ in the nM range mediated the formation of 8-OH-dG from dG without addition of H2O2. Fe3+, Cu+, and Cu2+ were shown to have weaker oxidative effects in comparison to Fe2+. The pH (5.0-9.0) had a very limited effect on 8-OH-dG formation. Acid phosphatase, which contains iron at its active site, caused the formation of 8-OH-dG, whereas alkaline phosphatase did not. Phenol was not found to be oxidative. Fe2+-catalyzed formation of 8-OH-dG was completely blocked by the nitroxide 2,2,6,6-tetramethylpiperidine-N-oxyl (TEMPO), whereas DMSO, mannitol, and DMPO had a significantly weaker protecting effect. Catalase cleaved the dG molecule and was not suitable for use. A simple, fast, and inexpensive method for 8-OH-dG workup and analysis was developed, and the background level seen in liver from 13-week-old male Sprague-Dawley rat was 0.23 +/- 0.020 8-OH-dG/10(5) dG, which is up to 200 times lower than reported values from some other methods and up to 26 times lower when compared to other reports using HPLC-EC methods. In summary, the TEMPO method reduces oxidation of dG to 8-OH-dG during workup by (1) using chemicals low in transition metals, (2) using a cold workup procedure, (3) limiting the incubation time, and (4) using the nitroxide TEMPO in all steps.
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PMID:Reduction of oxidation during the preparation of DNA and analysis of 8-hydroxy-2'-deoxyguanosine. 970 49

The goal of this study was to test the hypothesis that the rate of mitochondrial oxidant production governs the aging process of the fruit fly, Drosophila melanogaster. Catalase, an antioxidative enzyme expressed in the cytosol and peroxisomes of Drosophila, was targetted ectopically to the mitochondrial matrix by fusion of a leader peptide derived from ornithine aminotransferase with its N-terminus. The presence of the transgene encoding this fusion protein was associated with moderate (35 +/- 13%) increases in total catalase activity in most lines, and measurable levels of catalase activity in the mitochondria (30-140 U/mg protein). There was no impact on the life span of the flies at 25 degrees C, even in an exceptional line with a 149% increase in total catalase activity, and there was a small decrease in longevity at 29 degrees C. There were no compensatory changes in the rate of metabolism or physical activity, or in the levels of other major antioxidants, suggesting that the aging process was largely unaffected. Resistance to exogenous hydrogen peroxide, paraquat, and cold stress was enhanced, but there was no appreciable effect on resistance to hyperoxia. The results demonstrate the importance of mitochondrial antioxidant levels in the resistance to oxidative stress at the organismal level, and illustrate that different effects on aging and stress resistance may ensue from a single treatment. The main inferences drawn are that: (i) levels of stress resistance may neither be a cause nor a reliable indicator of the rate of aging, and (ii) bolstering antioxidant levels in Drosophila may not delay or slow down the aging process.
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PMID:Ectopic expression of catalase in Drosophila mitochondria increases stress resistance but not longevity. 1252 2

The aim of this study was to determine the effects of cold stress on antioxidant enzyme activities and examine protein oxidation and lipid peroxidation in various tissues (brain, liver, kidney, heart and stomach). Twenty male Wistar rats (3 months old) weighing 220 +/- 20 g were used. The rats were randomly divided into two groups of ten: the control group and the cold stress group. Cold stress was applied to the animals by maintaining them in a cold room (5 degrees C) for 15 min/day for 15 days. Blood samples were taken for measuring plasma corticosterone levels. Tissues were obtained from each rat for measuring the antioxidant enzyme activities, protein oxidation and lipid peroxidation. Corticosterone levels were increased in the cold stress group. Copper, zinc superoxide dismutase activities were increased in the brains, livers and kidneys, whereas they decreased in the hearts and stomachs of rats in the cold stress group. Catalase activities were increased in the brains, livers, kidneys and hearts, whereas they decreased in the stomachs of rats in the cold stress group. Selenium-dependent glutathione peroxidase activities were increased in the brain, liver, heart and stomach. Reduced glutathione levels were decreased, while levels of protein carbonyl, conjugated diene and thiobarbituric-acid-reactive substances were increased in all tissues of the cold stress group. These results lead us to conclude that cold stress can disrupt the balance in an oxidant/antioxidant system and cause oxidative damage to several tissues by altering the enzymatic and non-enzymatic antioxidant status, protein oxidation and lipid peroxidation.
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PMID:Cold-stress-induced modulation of antioxidant defence: role of stressed conditions in tissue injury followed by protein oxidation and lipid peroxidation. 1502 90

Plant geranylgeranyl hydrogenase (CHL P) reduces free geranylgeranyl diphosphate to phytil diphosphate, which provides the side chain to chlorophylls, tocopherols, and plastoquinones. In peach, the single copy gene (PpCHL P) encodes a deduced product of 51.68 kDa, which harbours a transit peptide for cytoplasm-to-chloroplast transport and a nicotinamide binding domain. The PpCHL P message was abundant in chlorophyll-containing tissues and flower organs, but barely detected in the roots and mesocarp of ripening fruits, suggesting that transcription was related to plastid types and maturation. The message was not revealed in shoot apical meristems, but spread thoroughly in leaf cells during the early stages and was located mainly in the palisade of mature leaves, which exhibited higher transcript levels than young ones. Hence, the transcription of PpCHL P was likely to be regulated during leaf development. Gene expression was monitored in leaves responding to natural dark, cold, wounding, stress by imposed darkening, and during the curl disease. Transcription was stimulated by light, but repressed by dark and cold stress. In darkened leaves, the PpCHL P message was augmented concomitantly with that of CATALASE. In wounded leaves, the message decreased, but recovered rapidly, whereas in curled leaves, a reduction in gene expression was related to leaf damage intensity. However, transcript signals increased locally both in cells mechanically wounded by a needle and in those naturally injured by the pathogenic fungus Taphrina deformans. These data suggest that PpCHL P expression was regulated by photosynthetic activity and was possibly involved in the defence response.
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PMID:The gene geranylgeranyl reductase of peach (Prunus persica [L.] Batsch) is regulated during leaf development and responds differentially to distinct stress factors. 1528 45


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