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 protective effect of heat stress against mechanical dysfunction and myocardial necrosis after prolonged ischemia is well known. We have investigated whether the protective effect of heat stress extends to reperfusion arrhythmias in the isolated perfused rat heart. Rats were exposed to 20 min of 42 degrees C hyperthermia. Twenty-four h later their hearts were isolated, perfused and subjected to a 5-min period of occlusion of the left coronary artery. The incidence and duration of reperfusion arrhythmias were assessed in the 30-min reperfusion period. Prior heat stress led to a reduction in the incidence (from 100 to 60%, P</=0.05) and duration (from 611+/-251 to 62+/-51 s, P</=0.05) of ventricular tachycardia and/or fibrillation, upon reperfusion following a 5-min ischemic period. This prevention of reperfusion arrhythmias was associated with a two-fold increase in endogenous catalase activity and an enhanced heat stress protein hsp 72 and 27 expression. Catalase inhibition by 3-amino triazole (AT) abolished the antiarrhythmic effect of heat stress. The incidence (80 v 100%) and duration (691+/-238 v 989+/-242 s) of reperfusion arrhythmias were not different between the group heat shocked + AT and the group treated only with AT. On the other hand, in the presence of AT, myocardial noradrenaline release was attenuated by prior heat stress (upon stabilization: 3.9+/-0.8 compared to 9.4+/-2.1 pg/ml/g tissue, P</=0.05; upon reperfusion: 42.7+/-7.3 compared to 69.8+/-9.5 pg/ml/g tissue, P</=0.05). In conclusion, heat stress leads to protection against reperfusion arrhythmias occurring after a short ischemic insult, in the isolated rat heart. Heat stress proteins and catalase seem to be implicated in this protective effect. Finally, we have shown that in presence of AT, heat stress decreases myocardial noradrenaline release.
J Mol Cell Cardiol 1997 Dec
PMID:In vitro antiarrhythmic effect of prior whole body hyperthermia: implication of catalase. 944 34

Oxygen-derived free radical injury has been associated with several cytopathic conditions. Oxygen radicals produced by chondrocytes is an important mechanism by which chondrocytes induce matrix degradation. In the present study, we extend these observations by studying oxidative processes against osteoblasts. Osteoblasts were mixed in in vitro culture with 200 microM menadione. The cytotoxic effect of menadione-induced oxidative stress was monitored by lucigenin- or luminol-amplified chemiluminescence, tetrazolium assay and immunocytochemical study. Results showed that adding menadione induces an oxidative stress on osteoblasts, via superoxide and hydrogen peroxide production, that can be eradicated by superoxide dismutase (SOD) and catalase in a dose-dependent manner. Catalase and the appropriate concentration of dimethyl sulfoxide have a protective effect on cytotoxicity induced by menadione, whereas SOD does not. Menadione-treated osteoblasts have a strong affinity for annexin V, and the nuclei are strongly stained by TUNEL (TdT-mediated dUTP nick-end labelling). The results suggest that menadione-triggered production of reactive oxygen species leads to apoptosis of osteoblasts.
Cell Mol Life Sci 1997 Dec
PMID:Menadione-induced cytotoxicity to rat osteoblasts. 944 50

In aqueous solutions containing Cu(II) ions and ascorbic acid, thiamine was observed to be oxidized to the fluorescent products thiochrome and oxodihydrothiochrome in neutral and acid media. At high initial concentrations of thiamine, thiochrome was practically the only product of thiamine oxidation. Catalase inhibited the oxidation rate approximately by 30-fold, whereas superoxide dismutase reduced the rate by only 2.5-fold. Aliphatic alcohols, glucose, and high concentrations of ascorbic acid effectively inhibited the production of thiochrome. The yield of thiochrome was also decreased in the presence of aliphatic amino acids, histidine, and particularly human serum albumin (HSA). With complete binding of copper ions by HSA, no formation of fluorescent products was observed. In neutral and acidic media under the action of hydroxyl radicals, thiamine formed a tricyclic semiquinone form which was then oxidized to thiochrome by superoxide anion or H2O2. Ascorbic acid played the main role in the reduction of Cu(II), whereas the contribution of superoxide anions was less significant. Cu(I) interacted with H2O2 to form hydroxyl radicals. The addition of H2O2 both to thiamine and to the mixture of thiamine and Cu(II) ions did not lead to significant production of thiochrome in neutral and acidic media.
Biochemistry (Mosc) 1997 Dec
PMID:Thiamine oxidative transformations catalyzed by copper ions and ascorbic acid. 948 73

Reactive oxygen species such as superoxides, hydrogen peroxide (H2O2) and hydroxyl radicals have been suggested to be involved in the catalytic action of nitric oxide synthase (NOS) to produce NO from L-arginine. An examination was conducted on the effects of oxygen radical scavengers and oxygen radical-generating systems on the activity of neuronal NOS and guanylate cyclase (GC) in rat brains and NOS from the activated murine macrophage cell line J774. Catalase and superoxide dismutase (SOD) showed no significant effects on NOS or GC activity. Nitroblue tetrazolium (NBT, known as a superoxide radical scavenger) and peroxidase (POD) inhibited NOS, but their inhibitory actions were removed by increasing the concentration of arginine or NADPH respectively, in the reaction mixture. NOS and NO-dependent GC were inactivated by ascorbate/FeSO4 (a metal-catalyzed oxidation system), 2'2'-azobis-amidinopropane (a peroxy radical producer), and xanthine/xanthine oxidase (a superoxide generating system). The effects of oxygen radicals or antioxidants on the two isoforms of NOS were almost similar. However, H2O2 activated GC in a dose-dependent manner from 100 microM to 1 mM without significant effects on NOS. H2O2-induced GC activation was blocked by catalase. These results suggested that oxygen radicals inhibited NOS and GC, but H2O2 could activate GC directly.
Exp Mol Med 1998 Dec 31
PMID:The effects of oxygen radicals on the activity of nitric oxide synthase and guanylate cyclase. 989 52

Chronic inflammation induced by Helicobacter pylori infection has been associated with an increased risk of stomach cancer. We have analysed 167 stomach biopsies from 99 patients for H. pylori infection and immunohistochemically for the expression of inducible nitric oxide synthase (iNOS), catalase and superoxide dismutases (SODs) as markers of oxidative stress. Biopsies were graded as follows on the basis of histology: normal, superficial gastritis, variable severity of atrophic gastritis with or without intestinal metaplasia, and dysplasia. iNOS was detected in inflammatory cells in all types of gastritis with or without H. pylori infection and independently of its severity. In foveolar cells, iNOS was observed in approximately 25% of all biopsies showing any type of gastritis, but in a markedly higher proportion of dysplastic samples. Catalase and Mn-type SOD in inflammatory cells and catalase in foveolar cells were more frequently observed in marked atrophic gastritis biopsies than in less severe gastritis. Individual differences were found in the expression of these enzymes within groups with the same severity of gastritis. Prolonged oxidative stress in severe gastritis and dysplasia may play an important role in gastric carcinogenesis, through increased damage of DNA and tissue by reactive oxygen and nitrogen species.
Eur J Cancer Prev 1998 Dec
PMID:Inducible nitric oxide synthase, anti-oxidant enzymes and Helicobacter pylori infection in gastritis and gastric precancerous lesions in humans. 992 91

There are some suggestions that free radicals are involved in some dysfunctions observed in preeclampsia. In this study we have examined the antioxidant status of preeclamptic placentas. We have used placentas obtained from normal pregnant women and women with preeclampsia. Lipoperoxidative process was measured by means of Okhawa method. Sedlak method was used to measured the total thiol groups. The catalase activity was measured by means of Pffeifer method. The results show that the catalase activity decreases, the amount of MDA increases and the total amount of thiol groups is smaller in preeclamptic placentas. The level of lipid peroxides in preeclamptic placentas is about 1.8 times higher in comparison with normal placentas. The decreased level of total thiol groups in preeclamptic placentas can be caused by a more intensive process of protein peroxidation. Catalase is less active in preeclamptic placentas. It can be due to lower activity of antioxidant systems or the destruction of antioxidant systems by reactive oxygen species. The results of our experiments confirm lower antioxidant status in preeclamptic placentas and suggest that peroxidative reaction may cause many dysfunctions associated with preeclampsia.
Ginekol Pol 1998 Dec
PMID:[Lipid and protein peroxidation process and catalase activity in pre-eclamptic placenta]. 1022 49

1. We report opposite inotropic effects of NO donors in frog cardiac fibres. The negative effect, elicited by either 3-morpholino-sydnonimine (SIN-1) or S-nitroso-N-acetyl-penicillamine (SNAP), involved cyclic GMP (cGMP) production. However, SIN-1, unlike SNAP, could elicit a positive effect, in a superoxide dismutase (SOD)-sensitive manner. SIN-1, unlike SNAP, can release both NO and superoxide anion, the precursors of peroxynitrite (OONO-). The role of these messengers was examined. 2. Catalase did not reduce the positive inotropic effect of SIN-1. Thus, a conversion of superoxide anion into hydrogen peroxide was not involved in this effect. In addition, catalase did not modify the negative effects of SIN-1 plus SOD, or SNAP plus SOD. 3. LY 83583, a superoxide anion generator, elicited a positive inotropic effect, like SIN-1. The effect of LY 83583 was additive to the negative effects of SIN-1 or SNAP, and to the positive effect of SIN-1. Thus, superoxide anion generation, per se, did not account for the positive effect of SIN-1. 4. Authentic peroxynitrite (OONO-), but not mock-OONO- (negative control plus decomposed OONO-), exerted a dramatic positive inotropic effect in cardiac fibres. The effect of OONO- was larger in atrial fibres, as compared with ventricular fibres. 5. The positive effect of OONO- was not additive with that of SIN-1, suggesting a common mechanism of action. In contrast, the effects of either OONO- or SIN-1 were additive with the negative inotropic effect of SNAP. Furthermore, the effect of OONO-, like that of SIN-1, was not antagonized by 1H-[1,2,4]xidiazolo[4, 3-a]quinoxaline-1-one (ODQ; 10 microM), the guanylyl cyclase inhibitor. 6. The positive inotropic effects of SIN-1 and OONO- were not modified by hydroxyl radical scavengers, such as dimethyl-thio-urea (DMTU; 10 mM). 7. The positive inotropic effect of SIN-1 (100 microM) was abolished in sodium-free solutions, a treatment that eliminates the activity of the sodium-calcium exchanger. In contrast, the effect of SIN-1 was unchanged by a potassium channel inhibitor (tetraethyl-ammonium, 20 mM), or a sodium-potassium pump inhibitor (ouabain 10 microM). 8. We conclude that OONO- is a positive inotropic agent in frog cardiac fibres. The generation of OONO- accounts for the positive inotropic effect of SIN-1. OONO- itself was responsible for the positive inotropic effect, and appeared to modulate the activity of the sodium-calcium exchanger.
J Physiol 1999 Dec 01
PMID:Peroxynitrite is a positive inotropic agent in atrial and ventricular fibres of the frog heart. 1058 9

There is considerable interest in the role of the 1-hydroxyethyl radical (HER) in the toxic effects of ethanol. The goal of this study was to evaluate the effects of HER on classical antioxidant enzymes. The interaction of acetaldehyde with hydroxylamine-o-sulfonic acid has been shown to produce 1, 1'-dihydroxyazoethane (DHAE); this compound appears to be highly unstable, and its decomposition leads to the generation of HER. Addition of DHAE into a solution of PBN led to the appearance of the typical EPR spectra of PBN/HER adduct. No PBN/HER spin adduct was detected when DHAE was incubated with 0.1 M PBN in the presence of GSH. In the absence of PBN, DHAE oxidized ascorbic acid to semidehydroascorbyl radical, presumably via an ascorbate-dependent one-electron reduction of HER back to ethanol. Catalase was progressively inactivated by exposure to DHAE-generated HER in a time and HER concentration-dependent manner. Ascorbic acid and PBN gave full protection to catalase against HER-dependent inactivation. The antioxidants 2-tert-butyl-4-methylphenol, propylgallate, and alpha-tocopherol-protected catalase against inactivation by 84, 88, and 39%, respectively. Other antioxidant enzymes were also sensitive to exposure to HER. Glutathione reductase, glutathione peroxidase, and superoxide dismutase were inactivated by 46, 36, and 39%, respectively, by HER. The results reported here plus previous results showing HER interacts with GSH, ascorbate, and alpha-tocopherol suggest that prolonged generation of HER in cells from animals chronically exposed to ethanol may lower the antioxidant defense status, thereby contributing to mechanisms by which ethanol produces a state of oxidative stress and produces toxicity.
Arch Biochem Biophys 1999 Dec 15
PMID:Interaction of 1-hydroxyethyl radical with antioxidant enzymes. 1060 Jan 75

Catalases are oxidized by singlet oxygen giving rise to more acidic conformers detected in zymograms after electrophoresis in polyacrylamide gels. This shift in catalase mobility can be indicative of singlet oxygen production in vivo. Catalase from human cells, as from many organisms, is susceptible to in vitro modification by singlet oxygen. Human myeloid leukemia (U937) cells were treated under different stress conditions and catalase activity and its electrophoretic mobility was monitored. The U937 cells were found to have high levels of catalase activity, as compared to cultured fibroblasts, and to be very resistant to oxidative stress. Hydrogen peroxide did not modify the electrophoretic mobility of catalase, even at doses that produced cell damage. Conditions that primarily generate superoxide, such as treatment with paraquat or heat shock, also failed to modify the enzyme. In contrast, photosensitization reactions using rose Bengal gave rise to a more acidic conformer of catalase. Singlet oxygen quenchers prevented catalase modification by rose Bengal and light. The growth medium had a photosensitizing activity. Catalase was not modified in cells illuminated in phosphate buffer but was modified in cells illuminated in phosphate buffer containing riboflavin. Intense light per se also generated a slight shift in the electrophoretic mobility of catalase. Ultraviolet light (350 or 366 nm) did cause a change in catalase, but to a less acidic catalase conformer, indicating other modifications of the enzyme. The main effect of photosensitization with methylene blue was crosslinking of the enzyme, although some shift to acidic conformers was observed at a low concentration of the photoactive compound. Results indicate that catalase can be modified by singlet oxygen generated intracellularly, even though the enzyme is predominantly inside peroxisomes. Under some photosensitization conditions, catalase modification can be used as a marker to detect intracellular singlet oxygen.
Photochem Photobiol 1999 Dec
PMID:Oxidation of human catalase by singlet oxygen in myeloid leukemia cells. 1062

In the last two decades, a variety of fungal antioxidants have attracted considerable interest, largely arising from their hypothetical role as virulence determinants. Melanin is a potent free radical scavenger and in Cryptococcus neoformans, there is now good evidence that the production of melanin is a significant virulence determinant. There is also recent evidence linking melanin biosynthesis to the virulence of Aspergillus fumigatus conidia. Superoxide dismutases are important housekeeping antioxidants and have an additional hypothetical role in virulence; however, although these enzymes have been biochemically characterized from Aspergillus and Cryptococcus, there is as yet no firm evidence that these enzymes are involved in pathogenicity. Catalase production may play some role in the virulence of Candida albicans but this enzyme has not been shown, as yet, to influence the virulence of A. fumigatus. There are some data supporting an antioxidant function for the acyclic hexitol mannitol in C. neoformans, but further investigations are required in this area. Research into the putative antioxidant activities of a range of other fungal enzymes, such as acid phosphatases, remains limited at this time.
Med Mycol 1999 Dec
PMID:Antioxidant systems in the pathogenic fungi of man and their role in virulence. 1064 18


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