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)

Reactive oxygen species (ROS) have been shown to impair sperm function. The actions of ROS are reduced by antioxidant enzymes, including catalase. Although catalase-like activity has been demonstrated in semen, there has been no localization or characterization of catalase mRNA expression in the male reproductive tract. Catalase mRNA levels were evaluated by northern blot analysis and in situ hybridization from the male reproductive organs of normal 60-day-old rats, testes of 10- to 90-day-old rats, and testes of rats subjected to efferent duct ligation. Radioactive DNA probes were synthesized using a Klenow polymerase-based specific primer synthetic procedure with a known published sequence for rat catalase. All tissues demonstrated a single transcript of 2.5 kilobases (kb). Low levels of catalase mRNA were detected in the normal testis, epididymis, vas deferens, and prostate. No expression was detectable with northern analysis in seminal vesicle. The levels of catalase mRNA in reproductive organs were compared with the high levels of expression detectable in rat liver. In the testis, catalase expression was primarily localized to peritubular and interstitial cells. In the epididymis and prostate, mRNA was detected in the epithelium. The observed decrease in catalase mRNA levels in the maturing rat testis is consistent with its interstitial localization. The increase in testicular catalase mRNA levels seen in parallel with progressive thinning of the germinal epithelium after efferent duct ligation is also in keeping with a peritubular or interstitial cell localization. The relatively low levels of catalase mRNA expression in the normal adult male reproductive tract undermine the role of catalase as a major antioxidant enzyme in these tissues. The low levels of catalase mRNA in the testis, and the undetectable levels in the seminiferous epithelium, however, imply that the germinal epithelium is predisposed to an oxidative state. These findings may help to explain the known susceptibility of the testis to oxidative stress.
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PMID:Catalase mRNA expression in the male rat reproductive tract. 895 90

Catalase, glutathione peroxidase and superoxide dismutase enzymes were determined after administering dexamethasone. Catalase increased its activity over six times (0.388 U/mg DNA) the normal rate, while glutathione peroxidase caused 3 times an increase one hour after dexamethasone injection. Superoxide dismutase increased gradually during the 3 hour treatment. The antioxidant enzyme activities decreased to basal values in the presence of protein synthesis (Cycloheximide) and RNA synthesis (Actinomycin D) inhibitors. The current report demonstrates that the increase of antioxidant enzymes is due to an enzymatic induction mechanism, and not due to an activation process.
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PMID:Induction of antioxidant enzymes by dexamethasone in the adult rat lung. 918 Mar 60

Human blood mononuclear cells exposed to UVB radiation develop increased antioxidant enzyme activities. Catalase (5.50 +/- 0.65 pmol (mg protein)-1), CuZn-superoxide dismutase (16.7 +/- 2.1 pmol (mg protein)-1), Mn-superoxide dismutase (11.3 +/- 1.7 pmol (mg protein)-1), Se-dependent glutathione peroxidase (13.2 +/- 1.5 mU (mg protein)-1) and Se-independent glutathione peroxidase (3.30 +/- 0.52 mU (mg protein)-1) activities increase by 1.3-1.5-fold from the control activities after exposure to 0.3 W m-2 of 280-315 nm light for 15 min and a 3 h dark incubation period. DT-diaphorase activity (2.86 +/- 0.21 mumol DCPIP min-1 (mg protein)-1) increases threefold from the indicated control values. In contrast, cytochrome oxidase (0.36 +/- 0.04 min-1 (k') (mg protein)-1) and succinate dehydrogenase (3.06 +/- 0.25 mumol DCPIP min-1 (mg protein)-1) activities remain unchanged during the same irradiation and incubation period. The treatment of cells with cycloheximide prevents the response triggered by UVB exposure. These findings suggest that an inducible antioxidant defence mechanism operates on photo-oxidative stress and that both superoxide dismutase and DT-diaphorase may display a concerted antioxidant role.
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PMID:Antioxidant adaptive response in human blood mononuclear cells exposed to UVB. 920 76

Antioxidant enzyme expression was determined in rat pancreatic islets and RINm5F insulin-producing cells on the level of mRNA, protein, and enzyme activity in comparison with 11 other rat tissues. Although superoxide dismutase expression was in the range of 30% of the liver values, the expression of the hydrogen peroxide-inactivating enzymes catalase and glutathione peroxidase was extremely low, in the range of 5% of the liver. Pancreatic islets but not RINm5F cells expressed an additional phospholipid hydroperoxide glutathione peroxidase that exerted protective effects against lipid peroxidation of the plasma membrane. Regression analysis for mRNA and protein expression and enzyme activities from 12 rat tissues revealed that the mRNA levels determine the enzyme activities of the tissues. The induction of cellular stress by high glucose, high oxygen, and heat shock treatment did not affect antioxidant enzyme expression in rat pancreatic islets or in RINm5F cells. Thus insulin-producing cells cannot adapt the low antioxidant enzyme activity levels to typical situations of cellular stress by an upregulation of gene expression. Through stable transfection, however, we were able to increase catalase and glutathione peroxidase gene expression in RINm5F cells, resulting in enzyme activities more than 100-fold higher than in nontransfected controls. Catalase-transfected RINm5F cells showed a 10-fold greater resistance toward hydrogen peroxide toxicity, whereas glutathione peroxidase overexpression was much less effective. Thus inactivation of hydrogen peroxide through catalase seems to be a step of critical importance for the removal of reactive oxygen species in insulin-producing cells. Overexpression of catalase may therefore be an effective means of preventing the toxic action of reactive oxygen species.
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PMID:Relation between antioxidant enzyme gene expression and antioxidative defense status of insulin-producing cells. 935 19

1. At premature birth, man and animals are exposed to relatively high oxygen levels, compared with intra-uterine conditions, at a time when their antioxidant enzyme (AOE) system is still immature. Using the chick embryo as a study model, we investigated changes in the AOE system in response to hyperoxia applied at different time points during the incubation period. Relations between hyperoxia and AOE activity were studied in selected organs (brain, heart, liver, intestine and lungs) of developing chick embryos (during the second half of the incubation period). 2. Incubated White Leghorn eggs were divided into four groups: control (n = 100) and three test groups exposed for 48 h to 60 % O2 on day 10 (test group 1, n = 80), day 14 (test group 2, n = 60) and day 18 (test group 3, n = 30). Superoxide dismutase (SOD), catalase and glutathione peroxidase (GPx) enzyme activities were measured in homogenates of the brain, heart, liver, intestine and lungs. 3. Exposure to hyperoxia at different time points during incubation resulted in a 2- to 10-fold increase in SOD activity in all organs except the brain. Catalase and GPx enzyme activities were only induced in test group 1, 48 h after initiation of hyperoxia. 4. In the developing chick embryo, hyperoxia can produce a temporary induction of AOE activity, which is dependent on the AOE, organ, incubation time and time point of exposure.
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PMID:Induction of antioxidant enzyme activity by hyperoxia (60 % O2) in the developing chick embryo. 954 1

Antioxidant enzyme activities were measured following exposure to hypericin +/- irradiation in EMT6 cells. CuZnSOD and catalase activities peaked within 0.5 h following irradiation for nontoxic 0.5 microM hypericin and toxic 1.0 microM hypericin. Catalase remained elevated up to 3 h for 1.0 microM hypericin + light. MnSOD activity was elevated immediately following irradiation for both doses. These levels returned to control by 1 h for 0.5 microM hypericin, but were depressed after 1 h for 1.0 microM hypericin. This suggests that mitochondria impairment may be a critical factor in hypericin phototoxicity. Glutathione reductase was inhibited immediately following irradiation with 1.0 microM hypericin, suggesting that an altered status of the glutathione pool contributed to cytotoxicity. Glutathione peroxidase activities were elevated following irradiation but returned to control levels within 0.5 h for both doses, implicating hydroperoxide formation as an early event in hypericin phototoxicity. Inhibition by hypericin in the dark was demonstrated for purified CuZnSOD, Se-dependent glutathione peroxidase, glutathione S-transferase, and glutathione reductase activities in vitro. Irradiation did not potentiate hypericin-mediated glutathione reductase inhibition and decrease inhibition for the other enzymes. Collectively, these data demonstrate an antioxidant enzyme response to hypericin photoactivation and confirm a role for oxygen in hypericin phototoxicity.
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PMID:Antioxidant enzyme response to hypericin in EMT6 mouse mammary carcinoma cells. 958 12

Catalase is an antioxidant enzyme that has been shown to inhibit apoptotic or necrotic neuronal death induced by hydrogen peroxide. We report the purification of a contaminating antiapoptotic activity from a commercial bovine liver catalase preparation by following its ability to inhibit apoptosis when applied extracellularly in multiple death paradigms. The antiapoptotic activity was identified by protein microsequencing as arginase, a urea cycle and nitric oxide synthase-regulating enzyme, and confirmed by demonstrating the presence of antiapoptotic activity in a >97% pure preparation of recombinant arginase. The pluripotency of recombinant arginase was demonstrated by its ability to inhibit apoptosis in multiple paradigms including rat cortical neurons induced to die by glutathione depletion and oxidative stress, by 100 nM staurosporine treatment, or by Sindbis virus infection. The protective effects of arginase in these apoptotic paradigms, in contrast to previous studies on excitotoxic neuronal necrosis, are independent of nitric oxide synthase inhibition. Rather, arginase-induced depletion of arginine leads to inhibition of protein synthesis, resulting in cell survival. Because inhibitors of nitric oxide synthesis and of protein synthesis have been shown to decrease necrotic and apoptotic death, respectively, in animal models of stroke and spinal cord injury, arginine-depleting enzymes, capable of simultaneously inhibiting protein synthesis and nitric oxide generation, may be propitious therapeutic agents for acute neurological diseases. Furthermore, our results suggest caution in attributing the cytoprotective effects of some catalase preparations to catalase.
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PMID:Purification of a multipotent antideath activity from bovine liver and its identification as arginase: nitric oxide-independent inhibition of neuronal apoptosis. 959 89

Comparative studies were performed on the antioxidant enzyme activities and thiobarbituric acid reactive substance (TBARS) concentration in liver and red cells of two groups of rainbow trout (Oncorhynchus mykiss). The fish of the first group were cultured in freshwater and the others were adapted to sea-water by by being transferred from freshwater at 5-6 months of age. Catalase (CAT), glutathione peroxidase (GPX), and glutathione S-transferase (GST) activities were significantly higher in hepatic and extrahepatic tissues in both of the fish groups. Superoxide dismutase (SOD) activities were found lower in the seawater-adapted trout than in the freshwater-cultured trout. In both tissues, TBARS were found significantly higher in the seawater-adapted trout than in the freshwater trout. It was also observed that the red cells of the seawater-adapted trout were much more resistant to oxidative stress than the red cells of the freshwater-cultured trout. The results implicate that antioxidant capacities in the seawater-adapted trout and freshwater trout may be related to physical and chemical characteristics of the environment.
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PMID:A comparative study of antioxidant enzyme activities in freshwater and seawater-adapted rainbow trout. 1048 21

Short-term effects of physiological concentrations of conjugated linoleic acid (CLA) on membrane integrity, metabolic function, cellular lipid composition, lipid peroxidation, and antioxidant enzymes were examined using rat hepatocyte suspension cultures. Incubation with CLA (5-20 ppm) for 3 h decreased the ability of hepatocyte plasma membranes to exclude trypan blue by approximately 25%, and caused leakage of cytosolic lactate dehydrogenase (LDH) into the medium. The significant decrease (P< 0.02) in hepatocyte viability as measured by LDH leakage during cell incubation with 10 and 20 ppm CLA was not associated with significant changes in cellular ATP content. Protein synthesis in hepatocytes was elevated (P < 0.05) in the presence of 5 and 10 ppm CLA, but at a higher concentration (20 ppm), protein synthesis was similar to that of control cells. Gluconeogenesis was maintained in cells incubated with lower concentrations of CLA (5 and 10 ppm) but was decreased (P < 0.02) at the higher concentration. Incubation with 20 ppm CLA for 3 h did not affect the specific activity of 3-hydroxy-3-methylglutaryl coenzyme A reductase, the rate-limiting enzyme of cholesterol synthesis. Both cis-9,trans-11/trans-9,cis-11, and cis-10,trans-12/trans-10,cis-12 isomers of CLA were incorporated to a similar level into hepatocytes. Levels ranged from 3.9 to 4.1%, respectively, of total fatty acids in neutral lipids, and from 0.7 to 0.8%, respectively, of total fatty acids in phospholipids. Cellular lipid peroxidation remained unchanged in the presence of CLA (5-20 ppm), despite significant inhibition (P < 0.05) of superoxide dismutase. Catalase activity was maintained near control levels in the presence of 5 and 10 ppm CLA but was significantly decreased in the presence of 20 ppm CLA. Glutathione peroxidase activity was significantly decreased in the presence of 10 ppm CLA. The apparent sensitivity of the antioxidant enzyme defense system of liver cells to CLA, coupled with the lack of effect of CLA on lipid peroxidation in cells, suggests that cytotoxic effects of CLA as described by LDH leakage and decreased gluconeogenesis were not mediated by a prooxidant action in hepatocytes.
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PMID:The effect of conjugated linoleic acid on the antioxidant enzyme defense system in rat hepatocytes. 1052 94

The deficiency of methionine, an essential amino acid, is associated with cardiovascular lesions. Because different types of cardiac pathologies are caused by a decrease in antioxidants, we examined the effects of methionine on myocardial antioxidant enzymes in hemodynamically assessed rats that were treated with methionine (10 mg/ml) in drinking water for 12, 24, and 48 h. Glutathione peroxidase (GSHPx) activity was significantly increased to 150.5 +/- 12.2 and 191.7 +/- 13.7% of the control value at 12 and 24 h, respectively, followed by a decline to 120 +/- 24.6% at 48 h. The mRNA levels of GSHPx at these time points were 151.2 +/- 12.0, 218.7 +/- 35.3, and 173.5 +/- 25.2%, respectively. Superoxide dismutase (SOD) activity was 144.3 +/- 3.7, 114.3 +/- 10.1, and 143.1 +/- 11. 2% at 12, 24, and 48 h, respectively. Catalase (Cat) activity was 272.4 +/- 5.4, 237.8 +/- 16.6, and 224.1 +/- 17.3% of the control value. The expression of Cat and SOD mRNA was unchanged at 12, 24, and 48 h. The lipid peroxidation was decreased by 24.4 +/- 11.2, 54. 9 +/- 0.1, and 6.4 +/- 2.1% at 12, 24, and 48 h, respectively. Methionine had no effect on the ventricular or aortic pressures, heart rate, and myocardial glutathione levels at any of the time points. The study shows that methionine has a significant effect on the myocardial antioxidant enzyme activities, and only changes in GSHPx enzyme activity correlated with the mRNA changes. These antioxidant changes may have a role in the beneficial effects of methionine in pathological rather than physiological conditions.
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PMID:Effects of methionine on endogenous antioxidants in the heart. 1060 Aug 29


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