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Query: UNIPROT:P04040 (Catalase)
 3,577 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Growing evidence suggests that free radicals derived from polymorphonuclear leukocytes (PMNs) play an important role in myocardial ischemia-reperfusion injury. To elucidate the cellular mechanism by which activated PMNs exacerbate ischemic myocardial damage, we investigated the extent of cell injury, assessed by the morphological deterioration, free radical generation, and lipid peroxidation in mouse embryo myocardial cells coincubated with activated PMNs. The generation of PMN-derived free radicals was related to the extent of myocardial cell injury. When myocardial cell sheets were subjected to hypoxia and glucose-free media, myocardial cells were injured (cristalysis in the mitochondria and disruption of the sarcolemma) after adding various PMN activators, and the injury extended to the adjacent cells. Chemiluminescent emission and production of thiobarbituric acid-reactive substances in the coincubated cells increased markedly compared with myocardial cells or PMNs alone. The augmented lipid peroxidation coincided with the progression of myocardial cell injury. Catalase inhibited the myocardial cell injury by 52%, the chemiluminescence by 46%, and lipid peroxidation by 50%, whereas superoxide dismutase exhibited less pronounced inhibition. These results indicate that a chain reaction of lipid peroxidation in myocardial cells induced by PMN-derived free radicals closely correlates with membrane damage and contributes to the propagation of irreversible myocardial cell damage.
Free Radic Biol Med 1994 Dec
PMID:Polymorphonuclear leukocytes-induced injury in hypoxic cardiac myocytes. 786 66

Streptomyces coelicolor ATCC 10147 produced catalases whose electrophoretic mobility varied depending on the growth phase in liquid culture. Polyacrylamide gel electrophoresis of cell extracts resulted in six catalase activity bands, which were designated Cat1 to Ca6. Of these, Cat4 appeared during all growth phases, whereas Cat1 appeared only during the stationary phase. Catalase-deficient mutants were screened by the H2O2 bubbling test following NTG mutagenesis. In all the non-bubbling mutants tested, the Cat4 activity band significantly decreased or disappeared, suggesting that Cat4 is the major catalase. Cat4 was purified to electrophoretic homogeneity and some of its properties analysed. The enzyme has a native molecular mass of 225 kDa, as determined by gel permeation column chromatography, and consists of four identical subunits of 57 kDa, as determined by SDS-PAGE. The enzyme contains 2.6 molecules of protohaem IX per tetramer, as indicated by the absorption spectrum. It was not reducible by sodium dithionite and exhibited no peroxidase activity with o-dianisidine as the substrate. All these characteristics, as well as inhibitor studies, indicate that the major vegetative catalase in S. coelicolor, unlike E. coli vegetative catalase, is a member of the typical monofunctional catalases found in eukaryotes and some bacteria.
Microbiology (Reading) 1994 Dec
PMID:Characterization of the major catalase from Streptomyces coelicolor ATCC 10147. 788 56

The presence of catalase in heart mitochondria may prevent excessive H2O2 from reaching the cytosol, eventually reacting with myoglobin (R. Radi et al., 1991, J. Biol. Chem. 266, 22028-22034). In this report we investigated whether catalase was also present in the mitochondrial matrix of skeletal muscle as it also contains myoglobin which could react with H2O2 produced by mitochondria. Catalase content of skeletal muscle tissue was about 1.4% of that in liver. Simultaneous determinations of citrate synthase (a mitochondrial marker) and catalase in intact mitochondria and mitoplasts indicated that catalase is not associated with muscle mitochondria. The lack of catalase in muscle mitochondria is not due to a limited H2O2 production by these organelles. Rat skeletal muscle mitochondria generated H2O2 (0.64 +/- 0.04 nmol/(min.mg protein), approximately 40% the rate in heart mitochondria. Other groups have shown that training causes an increase in the concentration of mitochondrial electron carriers as well as an increase in the activity of mitochondrial glutathione peroxidase and mitochondrial electron carriers. The increased concentration of mitochondrial electron carriers and the sudden changes in oxygen supply may lead to increased intracellular H2O2 during exercise.
Arch Biochem Biophys 1994 Dec
PMID:Hydrogen peroxide metabolism in skeletal muscle mitochondria. 798 95

Reactive oxygen species have been implicated in aerobic organisms as causative agents in damage to DNA, proteins, and lipids. Catalase is a major enzyme in the defense against such oxidant damage. To determine whether increased catalase expression confers greater resistance to oxidant stress, a eukaryotic expression vector harboring a human catalase cDNA clone was constructed. Acatalasemic murine fibroblasts were then co-transfected with that catalase expression vector and pSV2-neo, and successfully transfected cells were identified by their ability to grow in the presence of geneticin. Clones that contained integrated copies of the catalase expression vector were identified by Polymerase Chain Reaction (PCR) analysis. Stably transfected geneticin-resistant cell lines that overexpressed catalase in potentially positive cell lines were confirmed by catalase enzyme assays. To examine the physiological relevance of catalase overexpression, cells were exposed to oxidant stresses (hydrogen peroxide and hyperoxia), and survival rates were determined. Results demonstrated a significant resistance to oxidative stress in cells overexpressing catalase when compared to controls. These transfected cell lines will provide important models for further evaluation of the role of catalase in protecting cells against the toxic effects of oxygen-derived free radicals and their derivatives.
Free Radic Biol Med 1993 Dec
PMID:Expression of human catalase in acatalasemic murine SV-B2 cells confers protection from oxidative damage. 813 83

The mechanism of hydroxyl (.OH) radical generation from O2- and H2O2 by vanadate [V(V)] and the role of NADH in this reaction have been investigated using electron spin resonance (ESR) and spin trapping techniques. The results show that the reaction of V(V) with O2- (generated via xanthine/xanthine oxidase) does not generate any ESR detectable V(IV) ion or .OH radical and the addition of H2O2 has little effect on the radical yield. In the presence of NADH, however, the xanthine/xanthine oxidase/V(V) system generates .OH as well as V(IV), the formation of both of which could be suppressed by superoxide dismutase. Catalase inhibits the .OH formation but enhances V(IV) generation. Reaction of V(V) with NADH alone in the presence of phosphate buffer also causes .OH radical generation albeit at a much reduced rate, and superoxide dismutase reduces the .OH yield. These observations indicate, in contrast to earlier reports, that O2- does not reduce V(V) to V(IV) in the absence of NADH. It is concluded that vanadate generates the .OH radical via not a Haber-Weiss but a Fenton-like reaction [V(IV) + H2O2-->V(V) + .OH+OH-], the V(IV) and H2O2 being generated by V(V)-stimulated, O(2-)-dependent NADH oxidation.
Arch Biochem Biophys 1993 Dec
PMID:Vanadate-mediated hydroxyl radical generation from superoxide radical in the presence of NADH: Haber-Weiss vs Fenton mechanism. 827 19

A purification scheme is described for the glyoxylate cycle enzyme malate synthase from maize scutella. With our procedure, large amounts of extremely pure enzyme can easily be prepared. Purification involves a heat denaturation step, followed by ammonium sulfate precipitation, and chromatography on DEAE-cellulose and Blue Dextran-Sepharose. Catalase and malate dehydrogenase, which are the most persistent contaminants, are completely removed by this procedure. Maize malate synthase is an octameric protein with a subunit molecular weight of 64 kDa. Purity of the enzyme preparation was demonstrated by SDS-polyacrylamide gel electrophoresis and by isoelectric focusing (pI = 5.0). Pure malate synthase can be stored without appreciable loss of activity at -70 degrees C in 200 mM Hepes buffer containing 6 mM MgCl2 and 2 mM 2-mercaptoethanol, pH 7.6. Maize malate synthase contains no covalently linked carbohydrate residues. The enzyme requires Mg2+ ions for activity. From circular dichroism measurements we estimate that the secondary structure of the enzyme consists of 30% alpha-helical and almost no (5%) beta-pleated sheet segments. A 45-kDa polypeptide, which contaminates malate synthase preparations if the purification starts from seedlings older than 2.5 days, is shown to be a degradation product of malate synthase. Together with full-length chains, these 45-kDa polypeptides are able to take part in octameric oligomer formation.
Protein Expr Purif 1993 Dec
PMID:Purification of the glyoxylate cycle enzyme malate synthase from maize (Zea mays L.) and characterization of a proteolytic fragment. 828 48

Catalase is a marker for peroxisomes, which are ubiquitous cytoplasmic organelles. Although the distribution and features of peroxisomes are well known in liver and kidney, these organelles have been rarely studied in neural tissues. Catalase is an important scavenging enzyme against reactive oxygen species, as it removes H2O2 produced during metabolic processes. Reactive oxygen species are involved in a number of brain lesions and in brain aging. We investigated the distribution of catalase in rat central nervous system by means of a newly developed immunocytochemical procedure for signal enhancement, using an affinity-purified polyclonal antiserum. The data show that catalase immunoreactivity is present in all neural cells, both neuronal and glial, albeit at different concentrations. Among glial cells, ependymal cells and tanycytes of the third ventricle and the median eminence show the most intense immunoreaction; positivity is also found in oligodendrocytes and astrocytes. In general, neurons in the brainstem are relatively more immunoreactive than those in the forebrain although, within these respective brain regions, there are areas with low and high staining intensity. Moreover, within the same area, certain types of neuron appear more immunoreactive than others. The cell bodies in the septal nuclei, pallidum, reticular thalamic nucleus, mesencephalic nucleus of the trigeminal nerve, Deiter's nucleus, locus ceruleus, cranial and spinal motor nuclei, and the Golgi cells of the cerebellar cortex are among the most densely stained neurons. Catalase immunoreactivity of the cell bodies, which presumably is proportional to catalase content, appears to be only partially correlated with cell size or type of neurotransmitter used in the nerve endings; it is likely that other unknown parameters regulate the abundance of the enzyme. In many cases, highly immunoreactive cells correspond to neurons known to be resistant to ischemia-reperfusion injury, whereas weakly stained cells correspond to neurons that are more susceptible to ischemic damage. The amount of catalase may be critical for a protective effect against oxidative stress under pathological conditions, such as ischemia-reperfusion injury.
J Histochem Cytochem 1995 Dec
PMID:Immunocytochemical localization of catalase in the central nervous system of the rat. 853 42

Direct oxidative protein damage by iron-nitrilotriacetate (NTA), as well as physiological iron complexes, iron-citrate and iron-ADP was studied in the presence or absence of H2O2, using bovine serum albumin (BSA), glucose-6-phosphate dehydrogenase (G-6-PD), glutathione reductase (GSSGRase) and catalase as the target proteins. Both Fe(III)NTA+H2O2 and Fe(II)NTA+H2O2 caused marked BSA fragmentation which accompanied the decrease in the intrinsic tryptophan fluorescence and appearance of bityrosine fluorescence. However, Fe(III)citrate+H2O2 showed only slight BSA fragmentation. In the absence of H2O2, Fe(II) NTA but not Fe(III)NTA caused similar but slight BSA fragmentation, which depended on the molecular oxygen. Fe(II)citrate also showed O2-dependent BSA fragmentation to a comparable degree, however, Fe(II)ADP showed no detectable BSA damage. BSA fragmentation by Fe(II)NTA+O2 and by Fe(III)NTA+H2O2 resulted in the appearance of the new alpha-amino groups. Electron spin resonance study using 5,5-dimethyl-1-pyrroline N-oxide (DMPO) as a spin trapping reagent showed DMPO-OH spin adduct, which suggests the presence of hydroxyl radical, in Fe(III)NTA+H2O2, but not in Fe(II)NTA+O2 system. Fe(II)NTA inactivated G-6-PD and GSSGRase in a O2-dependent manner, however, G-6-PD was more susceptible to the damage. This enzyme inactivation also accompanied the protein fragmentation and was not due to simple sulfhydryl oxidation. Catalase was not significantly inactivated nor fragmented by Fe(II)NTA+O2. These findings suggest that the interaction between proteins and iron-chelate complexes is important in iron catalyzed oxidative damage, and that the structure of the chelating agent may determine the target molecules.
Biochim Biophys Acta 1995 Dec 14
PMID:Oxidative damage of bovine serum albumin and other enzyme proteins by iron-chelate complexes. 854 12

Iron-containing proteins catalyze lipid peroxidation when combined with either H2O2 or ascorbic acid (ASC). Microsomal membranes were prepared from Day 13 endometrial and conceptus tissues (5 pigs) and from Day 30 endometrial, placental, fetal liver, and fetus minus fetal liver tissues (5 pigs). Microsomal membranes were subjected to the following in vitro treatments: 1) no treatment, 2) 50 microM ASC, 3) 100 microM uteroferrin (UF), 4) 50 microM ASC + 100 microM UF, 5) 50 microM ASC + 100 microM UF + 10 microM apotransferrin (transferrin with no iron bound; ATF), and 6) 50 microM ASC + 100 microM UF + 10 microM holotransferrin (transferrin saturated with iron; HTF). For treatments 7 through 10, membranes were preincubated (0 degrees C, 3 h) with either 7) no treatment, 8) 50 microM fetuin, 9) 50 microM holoretinol binding protein (holoRBP: retinol binding protein [HoloRBP] with retinol bound), or 10) 50 microM apoRBP (RBP with no retinol bound) followed by incubation with 50 microM ASC + 100 microM UF. Lipid peroxidation was measured in the samples as thiobarbituric acid reactive substances (TBARS). Endogenous TBARS were greater (p < 0.05) in Day 13 conceptus than in Day 13 endometrium and were highest (p < 0.05) on Day 30 in fetal liver. Combined ASC and UF caused a large increase (p < 0.05) in TBARS in all membranes except Day 30 placental membranes. Addition of ATF, but not HTF, decreased TBARS production in all membrane preparations. HoloRBP, but not fetuin or apoRBP, decreased (p < 0.05) TBARS production in all but Day 30 endometrial membranes. In other experiments, when combined with ASC, UF/UF-associated protein complex induced less (p < 0.01) lipid peroxidation in fetal liver microsomal membranes than did free UF. Catalase and superoxide dismutase had no effect on UF-induced lipid peroxidation in fetal liver membranes. These results indicate that 1) UF combined with ASC induces lipid peroxidation in Day 13 endometrial and conceptus and Day 30 endometrial, fetal liver, and fetus minus liver microsomal membranes, and 2) ATF, holoRBP, and the UF-associated proteins, but not catalase or superoxide dismutase, inhibit this reaction.
Biol Reprod 1995 Dec
PMID:Uteroferrin induces lipid peroxidation in endometrial and conceptus microsomal membranes and is inhibited by apotransferrin, retinol binding protein, and the uteroferrin-associated proteins. 856 1

Endrin, a poly-halogenated cyclic hydrocarbon, induces hepatic lipid peroxidation, modulates calcium homeostasis, decreases membrane fluidity, and increases nuclear DNA damage. Little information is available on the neurotoxicity of endrin. The effects of endrin on lipid peroxidation, DNA damage, and regional distribution of catalase activity were assessed in rat brain and liver 24 h following an acute oral dose of 4.5 mg endrin/kg. Lipid peroxidation associated with whole brain mitochondria increased 2.4-fold, whereas microsomal lipid peroxidation increased 2.8-fold following endrin administration. Lipid peroxidation also increased 2.0-fold both in hepatic mitochondria and microsomes. Catalase activity decreased 24% in the hypothalamus, 23% in the cortex, 38% in the cerebellum, and 11% in the brain stem in response to endrin. A 4.3-fold increase in brain nuclear DNA-single strand breaks (SSB) was observed in endrin-treated rats. Pretreatment of rats intraperitoneally with the lazaroid U74389F (16-desmethyl tirilazad) (10 mg/kg in two doses) attenuated the biochemical consequences of endrin-induced oxidative stress. The administration of U74389F in citrate buffer (pH 3.8) provided better protection than administering the lazaroid in corn oil, decreasing endrin-induced lipid peroxidation by 50-80% and DNA-SSB by approximately 72% in liver and 85% in brain, while ameliorating the suppressed catalase activity. The data suggest an involvement of an oxidative stress in the neurotoxicity and hepatotoxicity induced by endrin, which can be attenuated by the lazaroid U74389F.
Free Radic Biol Med 1995 Dec
PMID:Protective effects of lazaroid U74389F (16-desmethyl tirilazad) on endrin-induced lipid peroxidation and DNA damage in brain and liver and regional distribution of catalase activity in rat brain. 858 61


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