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)

The effects of dietary vitamin E and selenium on the oxidant defense system (glutathione peroxidase, catalase, glutathione reductase, reduced glutathione, and superoxide dismutase) were investigated in the chick. Two-week-old chicks were reared using a vitamin E-free, low-selenium, semipurified basal diet alone or supplemental with vitamin E (100 IU/kg) and/or selenium (.10 ppm). Whereas vitamin E sustained chick growth, survival, and protection from exudative diathesis (ED), it did not significantly affect the enzymatic components of the oxidant defense system. Dietary selenium promoted chick growth and protection against ED in the absence of vitamin E and sustained glutathione peroxidase activity in several tissues. The latter effect was associated with decreases in reduced glutathione concentrations observed in liver and blood. Catalase and superoxide dismutase activities were increased in liver and brain in selenium deficiency. Glutathione reductase activities in liver, kidney, lung, and brain were not affected by diet.
Poult Sci 1981 Sep
PMID:Influences of dietary vitamin E and selenium on the oxidant defense system of the chick. 732 95

In experiments carried out in rabbit eyes, UV rays of 254 or 312 nm wavelength damaged the anterior eye segment, whereas those of 365 nm wavelength did not. Two min irradiation with 254 nm UV rays led to a decrease of catalase activity in the corneal epithelium. After 5 min irradiation the catalase activity in the epithelium was not detectable at all. Catalase activity was also diminished in the corneal endothelium and lens epithelium. In this stage the changes were accompanied by decreased activities of Na(+)--K(+)-dependent adenosine triphosphatase, gamma-glutamyl transpeptidase and increased activities of lysosomal enzymes in the corneal and lens epithelium as well as in the corneal endothelium. The transparency of the cornea and lens was decreased. Plasmin activity appeared in the tear fluid. The irradiation with UV rays of 312 nm caused similar disturbances, however, a longer exposure was necessary. In contrast, irradiation with UV rays of 365 nm did not produce any changes. The described corneal disturbances were prevented by dropping of catalase solution on the eye surface during the irradiation or shortly after it. However, after a protracted irradiation aprotinin had to be added to catalase to achieve the healing. The decrease of catalase activity and its prevention by a local application of catalase suggests a key role of oxyradicals in the damage of the eye by UV rays.
Acta Histochem 1994 Sep
PMID:The damaging effect of UV rays (with the wavelength shorter than 320 nm) on the rabbit anterior eye segment. I. Early changes and their prevention by catalase-aprotinin application. 753 31

Catalase-bound NADPH both prevents and reverses the accumulation of compound II, an inactive form of catalase that is generated from the normal active intermediate form (compound I) when catalase is exposed to a steady flow of hydrogen peroxide. The mechanism for the regeneration reaction is unknown although NADPH could act either as a one-electron or a two-electron donor. Recently, a reaction scheme has been proposed in which the formation of compound II from compound I generates a neighboring radical species within the protein. NADPH would then donate two electrons, one to compound II for reduction of the iron and the other to the protein free radical. In this paper, we report calculations to find the dominant electron tunneling pathways between NADPH and the heme iron in the catalase from the peroxide-resistant mutant of Proteus mirabilis. Two major tunneling pathways are found which fuse together on Ser-196. It is suggested that the sequence Gly-Ser of the loop that divides the beta 5-strand is the key element for shielding a radical amino acid.
Biochim Biophys Acta 1995 Sep 27
PMID:Simulations of electron transfer in the NADPH-bound catalase from Proteus mirabilis PR. 754 61

Acetaminophen was given to mice at a single dose of 375 mg/kg. In situ liver chemiluminescence, H2O2 steady-state concentration, and the liver concentrations of total and oxidized glutathione were measured 15, 30, and 60 min after acetaminophen administration. Increases of 145% and 72% in spontaneous chemiluminescence and H2O2 concentration were observed 15 min after the injection, respectively. Total glutathione was decreased by acetaminophen administration at all the times studied. The maximal decrease, 83%, was found 60 min postinjection. The ratio GSH/GSSG was found significantly decreased at all the times studied. Microsomal superoxide production was increased by 2.4-fold by addition of acetaminophen. The activities of the antioxidant enzymes superoxide dismutase, catalase, and glutathione peroxidase were determined. Catalase was slightly inhibited (30%) 15 min after acetaminophen administration. No significant changes were found in superoxide dismutase activity. Se and non-Se glutathione peroxidase activities were decreased by 40% and 53% respectively, 15 min after acetaminophen administration. The decrease in catalase and glutathione peroxidase would result in an increased steady state level of H2O2 and hydroperoxides, contributing to cell injury. Damaged hepatocytes were observed, and severe lesions and necrosis appeared 60 min after acetaminophen administration. Our results indicate the occurrence of oxidative stress as a possible mechanism for acetaminophen-induced hepatotoxicity.
Free Radic Biol Med 1995 Sep
PMID:Oxidative stress by acute acetaminophen administration in mouse liver. 755 44

3-Morpholinosydnonimine (SIN-1) is widely used to generate nitric oxide (NO(x).) and superoxide radical (O2-.). The effect of SOD on the toxicity of SIN-1 is complex, depending on what is the ultimate species responsible for toxicity. SIN-1 (< 1 mM) was only slightly toxic to HepG2 cells. Copper, zinc superoxide dismutase (Cu,Zn-SOD) or manganese superoxide dismutase (Mn-SOD) increased the toxicity of SIN-1. Catalase abolished, while sodium azide potentiated, this toxicity, suggesting a key role for H2O2 in the overall mechanism. Depletion of GSH from the HepG2 cells also potentiated the toxicity of SIN-1 plus SOD. Although Me2SO, sodium formate, and mannitol had no protective effect, iron chelators, thiourea and urate protected the cells against the SIN-1 plus Cu,Zn-SOD-mediated cytotoxicity. The cytotoxic effect of Cu,Zn-SOD but not Mn-SOD, showed a biphasic dose response being most pronounced at lower concentrations (10-100 units/ml). In the presence of SIN-1, Mn-SOD increased accumulation of H2O2 in a concentration-dependent manner. In contrast, Cu,Zn-SOD increased H2O2 accumulation from SIN-1 at low but not high concentrations of the enzyme, suggesting that high concentrations of the Cu,Zn-SOD interacted with the H2O2. EPR spin trapping studies demonstrated the formation of hydroxyl radical from the decomposition of H2O2 by high concentrations of the Cu,Zn-SOD. The cytotoxic effect of the NO donors SNAP and DEA/NO was only slightly enhanced by SOD; catalase had no effect. Thus, the oxidants responsible for the toxicity of SIN-1 and SNAP or DEA/NO to HepG2 cells under these conditions are different, with H2O2 derived from O2-. dismutation playing a major role with SIN-1. These results suggest that the potentiation of SIN-1 toxicity by SOD is due to enhanced production of H2O2, followed by site-specific damage of critical cellular sites by a transition metal-catalyzed reaction. These results also emphasize that the role of SOD as a protectant against oxidant damage is complex and dependent, in part, on the subsequent fate and reactivity of the generated H2O2.
J Biol Chem 1995 Sep 08
PMID:Increased cytotoxicity of 3-morpholinosydnonimine to HepG2 cells in the presence of superoxide dismutase. Role of hydrogen peroxide and iron. 767 15

NADPH-quinone reductase catalyzes the two-electron reduction of quinones such as menadione, and generally is considered to play a protective role against quinone-mediated toxicity. Recent studies have shown that reactive oxygen intermediates may be produced during metabolism of quinones by quinone reductase. Experiments were carried out to evaluate the effect of iron complexes on production of hydroxyl radical (.OH) when menadione was oxidized by a rat liver cytosolic fraction. Menadione-stimulated H2O2 production when added to the cytosol; dicoumarol, a potent inhibitor of quinone reductase, completely blocked this stimulation. Results were identical with either NADH or NADPH as reductant. In the absence of added iron, .OH, assessed as oxidation of chemical scavengers, was not produced. Various ferric chelates, added to the cytosol in the absence of menadione, did not catalyze .OH production. However, .OH was produced in the presence of menadione with all ferric complexes evaluated except for ferric-desferrioxamine. Catalase, competitive scavengers and GSH inhibited .OH production, as did dicoumarol. Superoxide dismutase inhibited with ferric-ATP, ferric-citrate, ferric-histidine or ferric ammonium sulfate as iron catalysts, but had no effect with ferric-EDTA or ferric-diethylenetriamine penta-acetic acid. Reduction of the ferric complexes was increased by menadione. NADH and NADPH were equally effective as cofactor for all these reactions. Metabolism of menadione in the presence of iron complexes caused inactivation of enzymes present in the cytosolic fraction such as glutamine synthetase and lactic dehydrogenase. These results indicate that metabolism of menadione by quinone reductase can lead to the production of .OH in the presence of various ferric catalysts.(ABSTRACT TRUNCATED AT 250 WORDS)
J Pharmacol Exp Ther 1993 Sep
PMID:Requirement for iron for the production of hydroxyl radicals by rat liver quinone reductase. 769 Apr

Established cell lines derived from newborn livers of c14CoS/c14CoS and cch/cch mice were examined for differences in menadione toxicity. The 14CoS/14CoS cells exhibit 10-fold higher NAD(P)H:menadione oxidoreductase (NMO1) activity and 3-fold greater concentrations of reduced glutathione (GSH) than the ch/ch cells. In 14CoS/14CoS cells there are also 50% to 3-fold increases in glutathione transferase (GSTA1), UDP glucuronosyltransferase, and the copper, zinc-dependent superoxide dismutase activities. Catalase activity, on the other hand, is six times lower in the 14CoS/14CoS than the ch/ch line. The 14CoS/14CoS cells are two to four times more resistant to menadione killing than ch/ch cells. At concentrations of dicumarol that completely block NMO1 and GSTA1 activities, the 14CoS/14CoS cells show more than twice as much resistance to menadione toxicity than the ch/ch cells. Although superoxide formation is three times higher in untreated 14CoS/14CoS than ch/ch cells, menadione-induced superoxide formation is greater in the dying ch/ch than in the 14CoS/14CoS cells. Cellular resistance to menadione toxicity is correlated with intracellular GSH levels, rather than with the percentage of oxidized glutathione; cytotoxicity is not observed as long as GSH concentrations are sufficiently high (about 5-8 nmol/mg protein). For menadione, the results are consistent with a dominant role of GSH depletion in mediating toxicity and support a protective role for NMO1 activity. This report demonstrates the usefulness of these cell lines as a model system to study mechanisms of oxidative chemically induced toxicity, as well as to understand how intracellular levels of GSH are regulated.
Toxicol Appl Pharmacol 1993 Sep
PMID:Menadione toxicity in two mouse liver established cell lines having striking genetic differences in quinone reductase activity and glutathione concentrations. 769 Sep 96

We compared the mortality rate and the lung and liver histologic injury with the degree of tissue lipid peroxidation after zymosan-induced peritonitis. Male Wistar rats were given .75 or 1 mg/g of zymosan intraperitoneally and monitored for 24 h. Tissue lipid peroxides were measured as conjugated dienes and malondialdehyde (MDA) as were the antioxidants, ascorbic acid and catalase. Mortality rates for the .75 and 1 mg/g groups were 15 and 50%, respectively. In lung, the degree of increase in conjugated dienes and MDA was significantly greater in nonsurvivors than survivors. Ascorbic acid and catalase levels were also significantly decreased to a greater degree in the sicker animals with ascorbic acid decreased to a greater degree in the higher dose and sicker animals. The level of MDA corresponded with the degree of histologic change. Catalase decreased to a greater degree in liver than lung. We conclude that the degree of lung and liver lipid peroxidation correlates with the degree of inflammation induced tissue injury and mortality.
Shock 1994 Sep
PMID:Comparison between lung and liver lipid peroxidation and mortality after zymosan peritonitis in the rat. 774 53

This study was to investigate the effects of hydrogen peroxide on membrane fluidity and Ca(2+)-ATPase activity of rabbit myocardial sarcoplasmic reticulum (SR). The membrane fluidity of SR was monitored by measuring the changes in the steady state fluorescence anisotropies (rs) using diphenylhexatriene as a probe. The Ca(2+)-ATPase activity was determined by assaying the amount of inorganic phosphate (Pi) released from ATP. It was found that the membrane fluidity (rs: 0.154 +/- 0.014 vs 0.113 +/- 0.010, P < 0.01) and Ca(2+)-ATPase activity (3.1 +/- 1.3 vs 25.3 +/- 2.4 mumol Pi.h-1/mg protein, P < 0.01) were reduced in SR exposed to H2O2 (2 mmol.L-1) for 40 min. Catalase 20 micrograms.ml-1 completely prevented the SR damages caused by H2O2. H2O2 jeopardized the SR in a concentration- and time-dependent manner as measured by changes in rs values and Ca(2+)-ATPase activities, which were negatively correlated (r = 0.981, P < 0.01). These results suggest that H2O2 produces dysfunctions of the rabbit myocardial SR, and that the alteration of membrane fluidity may be one of the mechanisms responsible for the decrease of Ca(2+)-ATPase activity.
Zhongguo Yao Li Xue Bao 1993 Sep
PMID:Effects of hydrogen peroxide on membrane fluidity and Ca(2+)-transporting ATPase activity of rabbit myocardial sarcoplasmic reticulum. 801 24

Iron, presumably by participating in generation of hydroxyl radical or other oxidant species or initiation of lipid peroxidation, has been shown to play an important role in several models of tissue injury, including acute renal failure induced by the antibiotic gentamicin. However, the sources of iron remain unknown. Rat renal mitochondria incubated at 37 degrees C with gentamicin resulted in a time- (15-60 min) and a dose-dependent (0.01-5 mM) iron release as measured by formation of iron-bathophenanthroline sulfonate complex FeII-(BPS)3 [at 60 min, control: 1.2 +/- 0.1 nmol/mg protein, n = 7; gentamicin (5 mM): 5.1 +/- 0.4 nmol/mg protein, n = 7]. No formation of FeII(BPS)3 complex was detected in the absence of mitochondria or when incubations were carried out at 0 degrees C. Similar results were obtained when 2,2'-dipyridyl, another iron chelator, was used for measurement of iron release. On the basis on our previous study that gentamicin enhances generation of hydrogen peroxide by renal cortical mitochondria, we examined whether effect of gentamicin on iron release is mediated by hydrogen peroxide. Catalase (which decomposes hydrogen peroxide), but not heat-inactivated catalase, as well as pyruvate, a potent scavenger of hydrogen peroxide, prevented gentamicin-induced iron mobilization. Superoxide dismutase, a scavenger of superoxide anion, or hydroxyl radical scavengers (dimethylthiourea or sodium benzoate) had no effect. Taken together, the data with scavengers indicate that gentamicin-induced iron mobilization from mitochondria is mediated by hydrogen peroxide.
Am J Physiol 1993 Sep
PMID:Gentamicin-induced mobilization of iron from renal cortical mitochondria. 821 3


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