PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12622181-5 2002 The activities of antioxidant enzymes, superoxide dismutase (SOD), catalase and glutathione peroxidase (GPx) were enhanced, which might be to eliminate the superoxide radical and H2O2 and accompanied by a fall in glutathione-s-transferase (GST) and glutathione reductase (GR) activity. Hydrogen Peroxide 179-183 catalase Rattus norvegicus 67-75 11792395-6 2002 The phenol red method of eosinophil identification was disrupted by co-incubation with resorcinol, an EPO inhibitor, or catalase, a hydrogen peroxide scavenger. Hydrogen Peroxide 132-149 catalase Rattus norvegicus 120-128 11376598-9 2001 In contrast, the antioxidant catalase (1000 U/ml) significantly attenuated methylmercury-induced inhibition of 3H-aspartate uptake, suggesting that excess reactive oxygen species, specifically H2O2, inhibit the function of an astrocytic excitatory amino acid transporter (EAAT1). Hydrogen Peroxide 193-197 catalase Rattus norvegicus 29-37 11557603-6 2001 Increased H(2)O(2), inhibitable by catalase, was detected in the vascular space at 1-2 s after the onset of ischemia. Hydrogen Peroxide 10-18 catalase Rattus norvegicus 35-43 11454704-6 2001 In addition, overexpression of catalase inhibited radiation-induced increases in PAI-1 expression, suggesting a mechanistic role for hydrogen peroxide (H2O2) in regulating PAI-1 expression after oxidative insult. Hydrogen Peroxide 133-150 catalase Rattus norvegicus 31-39 11454704-6 2001 In addition, overexpression of catalase inhibited radiation-induced increases in PAI-1 expression, suggesting a mechanistic role for hydrogen peroxide (H2O2) in regulating PAI-1 expression after oxidative insult. Hydrogen Peroxide 152-156 catalase Rattus norvegicus 31-39 11182294-1 2001 Pheochromocytoma (PC12) cell cultures exhibited a loss of cells and increase in intracellular oxidative stress when exposed to ethanol (EtOH) for 24 h. Catalase, an enzyme that hydrolyzes hydrogen peroxide (H(2)O(2)) to O(2) and H(2)O can attenuate EtOH-induced cell loss and oxidative stress in PC12 cells. Hydrogen Peroxide 188-205 catalase Rattus norvegicus 152-160 11325355-7 2001 Transient transfection of primary astroglial cells with a reporter plasmid containing the upstream region of the catalase gene showed a decrease in reporter gene activity after exposure of transfected cells to either H2O2 or paraquat. Hydrogen Peroxide 217-221 catalase Rattus norvegicus 113-121 11259492-3 2001 We examined H(2)O(2)-induced toxicity in neuronal PC12 cells and the effects of inducible overexpression of the H(2)O(2)-scavenging enzyme catalase on this process. Hydrogen Peroxide 112-120 catalase Rattus norvegicus 139-147 11134000-0 2001 Scavenging of extracellular H2O2 by catalase inhibits the proliferation of HER-2/Neu-transformed rat-1 fibroblasts through the induction of a stress response. Hydrogen Peroxide 28-32 catalase Rattus norvegicus 36-44 11392115-2 2001 The important role in AOS belongs to catalase and glutathione peroxidase which perform H2O2 to nontoxic products. Hydrogen Peroxide 87-91 catalase Rattus norvegicus 37-45 11121887-0 2001 Catalase in astroglia-rich primary cultures from rat brain: immunocytochemical localization and inactivation during the disposal of hydrogen peroxide. Hydrogen Peroxide 132-149 catalase Rattus norvegicus 0-8 11121887-4 2001 In contrast, after inhibition of glutathione peroxidases by mercaptosuccinate the rate of the catalase-dependent disposal of H(2)O(2) declined with time and after about 10 min the extracellular concentration of H(2)O(2) remained almost constant at a concentration of about 100 microM. Hydrogen Peroxide 125-133 catalase Rattus norvegicus 94-102 11121887-4 2001 In contrast, after inhibition of glutathione peroxidases by mercaptosuccinate the rate of the catalase-dependent disposal of H(2)O(2) declined with time and after about 10 min the extracellular concentration of H(2)O(2) remained almost constant at a concentration of about 100 microM. Hydrogen Peroxide 211-219 catalase Rattus norvegicus 94-102 11125030-10 2001 Ang II stimulated the H2O2 synthesis by cultured cells, and the presence of CAT in the extracellular compartment significantly diminished the Ang II-dependent increased intracellular H2O2 concentration. Hydrogen Peroxide 22-26 catalase Rattus norvegicus 76-79 11216869-1 2001 Regulation of catalase (CAT) expression, a major antioxidant enzyme that detoxifies H2O2, is very complex. Hydrogen Peroxide 84-88 catalase Rattus norvegicus 24-27 11216869-12 2001 Our data strongly suggest that the diminished renal and hepatic CAT expression in garlic-fed rats is mediated by post-transcriptional changes (mainly low translational efficiency) which could be an adaptation to the low H2O2. Hydrogen Peroxide 220-224 catalase Rattus norvegicus 64-67 11125030-10 2001 Ang II stimulated the H2O2 synthesis by cultured cells, and the presence of CAT in the extracellular compartment significantly diminished the Ang II-dependent increased intracellular H2O2 concentration. Hydrogen Peroxide 183-187 catalase Rattus norvegicus 76-79 10967081-11 2000 Catalase counteracted the effect of each ROS-generating system on retinal cells, consistent with damage occurring via a hydrogen peroxide intermediate. Hydrogen Peroxide 120-137 catalase Rattus norvegicus 0-8 10801894-5 2000 Catalase blocked ERK activation by H(2)O(2), but not by ONOO(-), demonstrating that the effect of ONOO(-) was not due to the generation of H(2)O(2). Hydrogen Peroxide 35-43 catalase Rattus norvegicus 0-8 10963730-6 2000 H(2)O(2) (30 microM)-induced phasic contraction could be abolished by catalase (800 U/ml), but not affected by SOD (150 U/ml), DMSO (5 mM) and apyrase (5 U/ml), suggesting no involvement of O(2)(-), hydroxyl free radicals and ATP release. Hydrogen Peroxide 0-8 catalase Rattus norvegicus 70-78 10788420-5 2000 The ROS produced appears to be H(2)O(2), because the introduction of catalase into the cells abolished NGF-induced neurite outgrowth, ROS production, and tyrosine phosphorylation. Hydrogen Peroxide 31-39 catalase Rattus norvegicus 69-77 10792963-1 2000 This study was conducted to quantify the effect of systemic Catalase, a hydrogen peroxide scavenger, on villous microcirculation in the inflamed small intestine of the rat. Hydrogen Peroxide 72-89 catalase Rattus norvegicus 60-68 11324438-3 2000 Superoxide dismutases (SOD) and catalase (CAT) activities were measured based on their abilities to inhibit the oxidation of epinephrine by the xanthine-xanthine oxidase system or to decompose H2O2 respectively. Hydrogen Peroxide 193-197 catalase Rattus norvegicus 32-40 11324438-3 2000 Superoxide dismutases (SOD) and catalase (CAT) activities were measured based on their abilities to inhibit the oxidation of epinephrine by the xanthine-xanthine oxidase system or to decompose H2O2 respectively. Hydrogen Peroxide 193-197 catalase Rattus norvegicus 42-45 10792963-12 2000 Hyperemia and the vascular diameter of the main arteriole were significantly reduced by H(2)O(2)-scavenger Catalase, suggesting that endogenous H(2)O(2) may be one of the mediators of hyperemia in the mucosa in this animal model of intestinal inflammation. Hydrogen Peroxide 88-96 catalase Rattus norvegicus 107-115 10792963-12 2000 Hyperemia and the vascular diameter of the main arteriole were significantly reduced by H(2)O(2)-scavenger Catalase, suggesting that endogenous H(2)O(2) may be one of the mediators of hyperemia in the mucosa in this animal model of intestinal inflammation. Hydrogen Peroxide 144-152 catalase Rattus norvegicus 107-115 10823352-2 2000 In these preparations, H2O2 (30 microM) induced a fast and transient contraction, which could be abolished by pretreatment of catalase (800 U/ml), but not affected by superoxide anion scavenger, superoxide dismutase (SOD; 150 U/ml) or the hydroxyl free radical scavenger, DMSO/mannitol (each 3 mM). Hydrogen Peroxide 23-27 catalase Rattus norvegicus 126-134 11723541-3 2000 We measured the activity of superoxide dismutase (SOD) and the hydrogen peroxide removing activity (mainly due to catalase (CAT) and glutathione peroxidase (GSH -Px) and found significant activity of these enzymes already at day 9.5 in the embryos and their yolk sac, both in vivo and in vitro. Hydrogen Peroxide 63-80 catalase Rattus norvegicus 114-122 11723541-3 2000 We measured the activity of superoxide dismutase (SOD) and the hydrogen peroxide removing activity (mainly due to catalase (CAT) and glutathione peroxidase (GSH -Px) and found significant activity of these enzymes already at day 9.5 in the embryos and their yolk sac, both in vivo and in vitro. Hydrogen Peroxide 63-80 catalase Rattus norvegicus 124-127 10574385-0 1999 Microinjection of catalase cDNA prevents hydrogen peroxide-induced motoneuron death. Hydrogen Peroxide 41-58 catalase Rattus norvegicus 18-26 10727540-8 2000 At 3 months, renal activity of Cu/Zn SOD was higher, and activities of catalase and GPx lower in ZO than in ZL rats, leading to an accumulation of hydrogen peroxide (H(2)O(2)). Hydrogen Peroxide 147-164 catalase Rattus norvegicus 71-79 10469365-9 1999 Both desferrioxamine and catalase reduced H2O2-mediated cellular injury and death. Hydrogen Peroxide 42-46 catalase Rattus norvegicus 25-33 10635343-3 1999 The mutagenesis by low doses of CYS, CYSGLY and GSH + GGT detected in IC203 was abolished by rat liver S9, through the activity of catalase, as well as by the metal chelator diethyldithiocarbamate (DETC), supporting the dependence of this mutagenesis on H2O2 production, probably in thiol autoxidation reactions in which transition metals are involved. Hydrogen Peroxide 254-258 catalase Rattus norvegicus 131-139 10650917-8 1999 This increase was inhibited by EDTA, butylated hydroxytoluene (BHT), and catalase (CAT), suggesting that some metal, most likely the accumulated Cu, and ROSs derived from hydrogen peroxide (H2O2) are involved in the increased levels of LPO in the livers of hepatitic LEC rats. Hydrogen Peroxide 171-188 catalase Rattus norvegicus 73-81 10650917-8 1999 This increase was inhibited by EDTA, butylated hydroxytoluene (BHT), and catalase (CAT), suggesting that some metal, most likely the accumulated Cu, and ROSs derived from hydrogen peroxide (H2O2) are involved in the increased levels of LPO in the livers of hepatitic LEC rats. Hydrogen Peroxide 171-188 catalase Rattus norvegicus 83-86 10650917-8 1999 This increase was inhibited by EDTA, butylated hydroxytoluene (BHT), and catalase (CAT), suggesting that some metal, most likely the accumulated Cu, and ROSs derived from hydrogen peroxide (H2O2) are involved in the increased levels of LPO in the livers of hepatitic LEC rats. Hydrogen Peroxide 190-194 catalase Rattus norvegicus 73-81 10650917-8 1999 This increase was inhibited by EDTA, butylated hydroxytoluene (BHT), and catalase (CAT), suggesting that some metal, most likely the accumulated Cu, and ROSs derived from hydrogen peroxide (H2O2) are involved in the increased levels of LPO in the livers of hepatitic LEC rats. Hydrogen Peroxide 190-194 catalase Rattus norvegicus 83-86 10650917-14 1999 The increased generation of H2O2 with reduced activities of GPX and CAT may result in cellular accumulation of H2O2 in the liver of hepatitic LEC rats. Hydrogen Peroxide 28-32 catalase Rattus norvegicus 68-71 10650917-14 1999 The increased generation of H2O2 with reduced activities of GPX and CAT may result in cellular accumulation of H2O2 in the liver of hepatitic LEC rats. Hydrogen Peroxide 111-115 catalase Rattus norvegicus 68-71 10574385-2 1999 We investigated the protective effects of overexpression of catalase in primary cultures of rat spinal motoneurons against the oxidative stress of hydrogen peroxide. Hydrogen Peroxide 147-164 catalase Rattus norvegicus 60-68 10691293-4 1999 Hydrogen peroxide (H2O2) concentrations were calculated from catalase-sensitive chemiluminescence, the difference between total and catalase-resistant chemiluminescence. Hydrogen Peroxide 0-17 catalase Rattus norvegicus 61-69 10468195-2 1999 The role of H2O2 in these rats may be studied modulating the amount or activity of catalase, which breakdowns H2O2 to water and oxygen. Hydrogen Peroxide 12-16 catalase Rattus norvegicus 83-91 10468195-2 1999 The role of H2O2 in these rats may be studied modulating the amount or activity of catalase, which breakdowns H2O2 to water and oxygen. Hydrogen Peroxide 110-114 catalase Rattus norvegicus 83-91 10468195-8 1999 These data indicate that the in vivo catalase inhibition magnifies PAN-nephrosis, suggesting that H2O2 is produced in vivo and involved in the renal damage in this experimental disease. Hydrogen Peroxide 98-102 catalase Rattus norvegicus 37-45 10691293-4 1999 Hydrogen peroxide (H2O2) concentrations were calculated from catalase-sensitive chemiluminescence, the difference between total and catalase-resistant chemiluminescence. Hydrogen Peroxide 0-17 catalase Rattus norvegicus 132-140 10691293-4 1999 Hydrogen peroxide (H2O2) concentrations were calculated from catalase-sensitive chemiluminescence, the difference between total and catalase-resistant chemiluminescence. Hydrogen Peroxide 19-23 catalase Rattus norvegicus 61-69 9806814-3 1998 We have demonstrated the ability of two oxygen-free radical scavengers, superoxide dismutase (SOD), a superoxide anion scavenger, and catalase, a hydrogen peroxide scavenger, to reduce thrombus growth. Hydrogen Peroxide 146-163 catalase Rattus norvegicus 134-142 10349863-9 1999 The clearance rate by neurons for H2O2 was strongly reduced in the presence of the catalase inhibitor 3-aminotriazol, a situation contrasting with that in astroglial cultures. Hydrogen Peroxide 34-38 catalase Rattus norvegicus 83-91 10349863-10 1999 This indicates that for the rapid clearance of H2O2 by neurons, both glutathione peroxidase and catalase are essential and that the glutathione system cannot functionally compensate for the loss of the catalase reaction. Hydrogen Peroxide 47-51 catalase Rattus norvegicus 96-104 10220589-3 1999 Catalase but not superoxide dismutase (SOD) nor a NO scavenger protected PC12 cells from death, indicating that H2O2 is the main effector responsible for this cell death. Hydrogen Peroxide 112-116 catalase Rattus norvegicus 0-8 10051504-7 1999 While the addition of H2O2 to HSC induced the expression of alpha1(I) procollagen mRNA, catalase, an H2O2 enzyme scavenger, abrogated TGF-beta-mediated col1a1 gene up-regulation. Hydrogen Peroxide 22-26 catalase Rattus norvegicus 60-96 10051504-7 1999 While the addition of H2O2 to HSC induced the expression of alpha1(I) procollagen mRNA, catalase, an H2O2 enzyme scavenger, abrogated TGF-beta-mediated col1a1 gene up-regulation. Hydrogen Peroxide 101-105 catalase Rattus norvegicus 60-96 10420989-2 1999 LPA increased intracellular H2O2, with a maximal increase at 30 min, which was blocked by the catalase from Aspergillus niger. Hydrogen Peroxide 28-32 catalase Rattus norvegicus 94-102 10420989-4 1999 Purified phosphatidic acid (PA) also increased intracellular H2O2 and the increase was inhibited by the catalase. Hydrogen Peroxide 61-65 catalase Rattus norvegicus 104-112 10420989-8 1999 In addition, catalase inhibited actin polymerization activated by LPA, PA, or H2O2, indicated the role of H2O2 in actin polymerization. Hydrogen Peroxide 78-82 catalase Rattus norvegicus 13-21 10420989-8 1999 In addition, catalase inhibited actin polymerization activated by LPA, PA, or H2O2, indicated the role of H2O2 in actin polymerization. Hydrogen Peroxide 106-110 catalase Rattus norvegicus 13-21 10217353-9 1999 In the presence of catalase or superoxide dismutase (SOD), LDL oxidation was completely blocked, suggesting that hydrogen peroxide and superoxide are involved in P450 2E1-induced LDL oxidation. Hydrogen Peroxide 113-130 catalase Rattus norvegicus 19-27 10333085-5 1999 Consequently, this study was undertaken to evaluate the effect of sustained high serum insulin levels on the activity of hepatic catalase, a peroxisomal antioxidant enzyme involved in the decomposition of H2O2. Hydrogen Peroxide 205-209 catalase Rattus norvegicus 129-137 10436710-1 1999 BACKGROUND: Glutathione peroxidase (GSHPx) and catalase are two important cellular antioxidant enzymes involved in H2O2 and lipid-peroxide metabolism. Hydrogen Peroxide 115-119 catalase Rattus norvegicus 47-55 10684523-8 1999 Catalase attenuated the H(2)O(2)-induced increase in [Ca(2+)](i) significantly, whereas mannitol showed no effect. Hydrogen Peroxide 24-32 catalase Rattus norvegicus 0-8 9894152-8 1998 H2O2-induced GC activation was blocked by catalase. Hydrogen Peroxide 0-4 catalase Rattus norvegicus 42-50 9815067-4 1998 Cerebral vasodilator responses to arachidonate, but not papaverine, were abolished during topical application of indomethacin (10 microM, an inhibitor of cyclooxygenase) or catalase (100 U/ml, which inactivates hydrogen peroxide). Hydrogen Peroxide 211-228 catalase Rattus norvegicus 173-181 10402649-3 1998 It is followed from the result that the activity of catalase livers can be explained by the participation of catalases in other reactions, which were connected with forming a hydrogen peroxide. Hydrogen Peroxide 175-192 catalase Rattus norvegicus 52-60 9356019-2 1997 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. Hydrogen Peroxide 108-125 catalase Rattus norvegicus 147-155 9755114-12 1998 Both MAb 9B9-catalase and MAb 1A29-catalase significantly attenuated the H2O2-induced elevation in 1) angiotensin-converting enzyme release to the perfusate (215 +/- 14 and 217 +/- 38 mU, respectively), 2) lung wet-to-dry ratio (6.25 +/- 0.1 and 6.3 +/- 0.3, respectively), 3) tracheal pressure (94 +/- 4 and 101 +/- 4%, respectively, of the control level), and 4) pulmonary arterial pressure (103 +/- 3 and 104 +/- 7%, respectively, of the control level). Hydrogen Peroxide 73-77 catalase Rattus norvegicus 13-21 9755114-12 1998 Both MAb 9B9-catalase and MAb 1A29-catalase significantly attenuated the H2O2-induced elevation in 1) angiotensin-converting enzyme release to the perfusate (215 +/- 14 and 217 +/- 38 mU, respectively), 2) lung wet-to-dry ratio (6.25 +/- 0.1 and 6.3 +/- 0.3, respectively), 3) tracheal pressure (94 +/- 4 and 101 +/- 4%, respectively, of the control level), and 4) pulmonary arterial pressure (103 +/- 3 and 104 +/- 7%, respectively, of the control level). Hydrogen Peroxide 73-77 catalase Rattus norvegicus 35-43 9622158-7 1998 Catalase, but not superoxide dismutase, completely inhibited MAP kinase activation by H2O2. Hydrogen Peroxide 86-90 catalase Rattus norvegicus 0-8 9717456-3 1998 An inverse relationship was found between catalase activity and hydrogen peroxide production. Hydrogen Peroxide 64-81 catalase Rattus norvegicus 42-50 9436611-10 1998 In rat hepatoma H4IIE cells the induction of catalase mRNA by H2O2 was prevented by the addition of actinomycin D or cycloheximide. Hydrogen Peroxide 62-66 catalase Rattus norvegicus 45-53 9436611-11 1998 Although induction of catalase mRNA by H2O2 was found in rat hepatocytes and H4IIE cells, gene expression of catalase does not appear to be regulated in both cell types in the same manner. Hydrogen Peroxide 39-43 catalase Rattus norvegicus 22-30 9753295-5 1998 The addition of Cat to the culture medium completely prevented the toxic effects of H2O2 and H/XO but had no significant effect on the toxicity of menadione or butylalloxan. Hydrogen Peroxide 84-88 catalase Rattus norvegicus 16-19 9659819-8 1998 Pretreatment by intraperitoneal injection of catalase attenuated H2O2 generation significantly. Hydrogen Peroxide 65-69 catalase Rattus norvegicus 45-53 9585474-9 1998 Catalase inhibited the EPR signal of the DMPO-OH adduct, indicating that H2O2 is the precursor of the hydroxyl radical spin adduct. Hydrogen Peroxide 73-77 catalase Rattus norvegicus 0-8 9438559-7 1998 Sensitivity to catalase indicates the critical role of H2O2 in the inactivation. Hydrogen Peroxide 55-59 catalase Rattus norvegicus 15-23 9436611-3 1998 Exposure of hepatocytes to H2O2 prevented this decrease in catalase mRNA expression, catalase expression was induced 2-fold. Hydrogen Peroxide 27-31 catalase Rattus norvegicus 59-67 9436611-3 1998 Exposure of hepatocytes to H2O2 prevented this decrease in catalase mRNA expression, catalase expression was induced 2-fold. Hydrogen Peroxide 27-31 catalase Rattus norvegicus 85-93 9436611-7 1998 In confluent hepatoma H4IIE cells catalase mRNA expression was lower than in early hepatocyte cultures and could be induced 2-fold upon treatment with H2O2. Hydrogen Peroxide 151-155 catalase Rattus norvegicus 34-42 9435555-0 1997 Role of glutathione and catalase in H2O2 detoxification in LPS-activated hepatic endothelial and Kupffer cells. Hydrogen Peroxide 36-40 catalase Rattus norvegicus 24-32 9435555-9 1997 After inhibition of catalase by 3-amino-1,2,4-triazole, the presence of 0.2 mM H2O2 depleted GSH content by 75% and 40% in Kupffer cells from saline- or LPS-injected rats, respectively. Hydrogen Peroxide 79-83 catalase Rattus norvegicus 20-28 9435555-13 1997 These data show that in activated Kupffer cells the elevated level of cellular glutathione plays an augmented role in the protection against reactive oxygen species, whereas the contribution of catalase to H2O2 detoxification is attenuated. Hydrogen Peroxide 206-210 catalase Rattus norvegicus 194-202 9356019-8 1997 Catalase-transfected RINm5F cells showed a 10-fold greater resistance toward hydrogen peroxide toxicity, whereas glutathione peroxidase overexpression was much less effective. Hydrogen Peroxide 77-94 catalase Rattus norvegicus 0-8 9356019-9 1997 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. Hydrogen Peroxide 21-38 catalase Rattus norvegicus 47-55 9219864-0 1997 Involvement of glutathione peroxidase and catalase in the disposal of exogenous hydrogen peroxide by cultured astroglial cells. Hydrogen Peroxide 80-97 catalase Rattus norvegicus 42-50 9365024-7 1997 PUT-SOD administered in combination with PUT-CAT may eliminate both the superoxide radical and the H2O2 produced from the dismutation of superoxide, respectively, and thus prevent the formation of hydroxyl radicals. Hydrogen Peroxide 99-103 catalase Rattus norvegicus 45-48 9430440-4 1997 Activities of three enzymes related to the metabolism of superoxide radical (SOD) and hydrogen peroxide (CAT and GPx) of testis, were found to be significantly decreased in response to TP treatment. Hydrogen Peroxide 86-103 catalase Rattus norvegicus 105-108 23604323-6 1997 One must be careful in the interpretation of such data, however, since catalase is rapidly inactivated by its substrate (H2O2), thus displaying abnormal enzyme kinetics. Hydrogen Peroxide 121-125 catalase Rattus norvegicus 71-79 23604323-8 1997 Using this method we found a significant increase in catalase activity in DR animals at several H2O2 concentrations during the light span. Hydrogen Peroxide 96-100 catalase Rattus norvegicus 53-61 9400726-4 1997 Catalase prevented this effect, which suggested that it was mediated by quartz-generated hydrogen peroxide. Hydrogen Peroxide 89-106 catalase Rattus norvegicus 0-8 9219864-8 1997 Incubation of astroglial cells with mercaptosuccinate or 3-aminotriazole, inhibitors of glutathione peroxidase and catalase, respectively, only marginally reduced the rate of disappearance of H2O2 from the incubation buffer. Hydrogen Peroxide 192-196 catalase Rattus norvegicus 115-123 9219864-10 1997 These results demonstrate that glutathione peroxidase and catalase are involved in the detoxification of H2O2 by astroglial cells and that both enzymes are able to substitute for each other in the detoxification of H2O2. Hydrogen Peroxide 105-109 catalase Rattus norvegicus 58-66 9219864-10 1997 These results demonstrate that glutathione peroxidase and catalase are involved in the detoxification of H2O2 by astroglial cells and that both enzymes are able to substitute for each other in the detoxification of H2O2. Hydrogen Peroxide 215-219 catalase Rattus norvegicus 58-66 9208153-15 1997 On the basis of the actions of 3-amino-1,2,4-triazole, it is likely that endogenous catalase plays an important role in the protection of vascular reactivity of rat aorta against oxidant damage by high (1 mM) but not lower (0.1 mM) concentrations of hydrogen peroxide. Hydrogen Peroxide 250-267 catalase Rattus norvegicus 84-92 9212351-8 1997 Hydrogen peroxide and superoxide anions were also involved, as DNA damage was partially inhibited by catalase and, to a lesser extent, by superoxide dismutase. Hydrogen Peroxide 0-17 catalase Rattus norvegicus 101-109 9197278-1 1997 The activity of catalase, the main enzyme responsible for detoxification against hydrogen peroxide, decreases in specific brain areas of aged rats. Hydrogen Peroxide 81-98 catalase Rattus norvegicus 16-24 9042155-6 1997 Superoxide dismutase treatment did not reduce granuloma formation, whereas catalase treatment resulted in decreased granuloma size, suggesting that H2O2 plays an important role in this process. Hydrogen Peroxide 148-152 catalase Rattus norvegicus 75-83 9250541-10 1997 The data indicate that the combination of exercise and ethanol ingestion resulted in an enhanced hepatic CAT and GR activity to eliminate H2O2 and to maintain endogenous GSH levels. Hydrogen Peroxide 138-142 catalase Rattus norvegicus 105-108 9130244-3 1997 Previously we have shown that NGF treatment enhances the activity of GSH-Px and catalase which catalyze the degradation of H2O2. Hydrogen Peroxide 123-127 catalase Rattus norvegicus 80-88 9119073-4 1997 Administration of catalase, superoxide dismutase and deferoxamine revealed that H2O2 was the major reactive oxygen species causing cell death, and H2O2O exerted its effect by formation of hydroxyl radical (.OH). Hydrogen Peroxide 80-84 catalase Rattus norvegicus 18-26 9042155-10 1997 These in vivo data, coupled with in vitro data that indicate that both catalase-sensitive reagent H2O2 and neutrophil-derived reactive oxygen intermediates (ie, H2O2) can induce MCP-1 secretion by human umbilical vein endothelial cells, support the hypothesis that neutrophils and neutrophil-derived products (H2O2) influence granuloma formation through induction of local MCP-1 expression. Hydrogen Peroxide 98-102 catalase Rattus norvegicus 71-79 8733824-4 1996 On the other hand, mRNA levels of catalase were higher than normal between 40 and 60 hr in the presence of H2O2. Hydrogen Peroxide 107-111 catalase Rattus norvegicus 34-42 9040030-12 1997 These questions pertain especially to: (a) quantitative aspects with regard to the possible effectiveness of an increase in catalase activity by two-, three-, or four-fold enhanced peroxisome numbers; (b) the role of cytoplasmic catalase; (c) the existence and importance of a myocardial mitochondrial catalase; and (d) the co-operation between the two H2O2-destroying enzymes catalase and glutathione peroxidase. Hydrogen Peroxide 353-357 catalase Rattus norvegicus 124-132 8986210-9 1996 From foregoing results, bezafibrate induced in the organism beta-oxidation by peroxisomes and increased H2O2 production, which led to augmented ethanol metabolism by catalase. Hydrogen Peroxide 104-108 catalase Rattus norvegicus 166-174 8690093-8 1996 Addition of catalase antagonized the actions of H2O2 completely. Hydrogen Peroxide 48-52 catalase Rattus norvegicus 12-20 8889859-4 1996 The enzymatic antioxidant catalase was used as a marker of endogenous cell antioxidant activity, especially to hydrogen peroxide. Hydrogen Peroxide 111-128 catalase Rattus norvegicus 26-34 8869666-8 1996 Catalase and thiourea both inhibited the H2O2-induced effects, but catalase inhibition was more complete. Hydrogen Peroxide 41-45 catalase Rattus norvegicus 0-8 8844524-3 1996 Catalase activity is determined by measuring residual hydrogen peroxide after incubation with the enzyme. Hydrogen Peroxide 54-71 catalase Rattus norvegicus 0-8 8762051-0 1996 Chronic exposure of neonatal cardiac myocytes to hydrogen peroxide enhances the expression of catalase. Hydrogen Peroxide 49-66 catalase Rattus norvegicus 94-102 8762051-8 1996 The results suggest that H2O2-induced expression of catalase was in part due to transcriptional activation. Hydrogen Peroxide 25-29 catalase Rattus norvegicus 52-60 8614020-4 1996 While CAT (50,000 IU/rat) significantly reduced the biochemical changes induced by hydrogen peroxide produced by a glucose/glucose oxidase system, it markedly exacerbated the lesions induced by phorbol myristate acetate (PMA). Hydrogen Peroxide 83-100 catalase Rattus norvegicus 6-9 7723246-6 1995 Catalase was partially protective in this model, thereby indicating hydrogen peroxide-dependent toxicity. Hydrogen Peroxide 68-85 catalase Rattus norvegicus 0-8 7491977-11 1995 Addition of 700 microM H2O2 also activated AP-1, and catalase at 500 U/ml prevented this activation. Hydrogen Peroxide 23-27 catalase Rattus norvegicus 53-61 8884889-5 1995 Catalase (but not superoxide dismutase or deferoxamine) eliminated the reduction in twitch tension, indicating that hydrogen peroxide played a role in the reduction. Hydrogen Peroxide 116-133 catalase Rattus norvegicus 0-8 7543016-14 1995 When Wt3A cells were treated with catalase, a cellular enzyme that inactivates H2O2, CAPE-induced apoptosis in Wt3A cells was reduced, further proving that Wt3A cells were more sensitive than CREF cells to oxidative stress. Hydrogen Peroxide 79-83 catalase Rattus norvegicus 34-42 7621992-8 1995 This increase in catalase in diabetic vascular tissue suggests increased oxidative stress due to chronic exposure to H2O2 in vivo. Hydrogen Peroxide 117-121 catalase Rattus norvegicus 17-25 8788950-12 1995 Catalase catalyses H2O2. Hydrogen Peroxide 19-23 catalase Rattus norvegicus 0-8 8719811-2 1995 In this study we investigated the role of catalase in relaxation induced by hydroxylamine, sodium azide, glyceryl trinitrate and hydrogen peroxide in isolated rings of rat aorta. Hydrogen Peroxide 129-146 catalase Rattus norvegicus 42-50 8719811-9 1995 Pretreatment of endothelium-denuded rings with catalase (1000 u ml-1) blocked relaxation induced by hydrogen peroxide (10 microM-1 mM). Hydrogen Peroxide 100-117 catalase Rattus norvegicus 47-55 8719811-10 1995 The ability of catalase to inhibit hydrogen peroxide-induced relaxation was partially blocked following incubation with 3-amino-1,2, 4-triazole (AT, 50 mM) for 30 min and completely blocked at 90 min. Hydrogen Peroxide 35-52 catalase Rattus norvegicus 15-23 8719811-14 1995 Pretreatment of endothelium-denuded rings with AT (1-50 mM, 90 min) to inhibit endogenous catalase blocked relaxation induced by sodium azide (1-300 nM) and hydroxylamine (1-300 nM) but had no effect on relaxation induced by hydrogen peroxide (10 microM-1 mM) or glyceryl trinitrate (1-100 nM). Hydrogen Peroxide 225-242 catalase Rattus norvegicus 90-98 8537642-3 1995 Catalase is an important scavenging enzyme against reactive oxygen species, as it removes H2O2 produced during metabolic processes. Hydrogen Peroxide 90-94 catalase Rattus norvegicus 0-8 8557531-2 1995 Incubations in the presence of 5 mM diaminobenzidine, 44 mM hydrogen peroxide and 2% polyvinyl alcohol performed on fixed cryostat sections resulted in the highest amounts of final reaction product precipitated in a fine granular form which was specific for catalase activity. Hydrogen Peroxide 60-77 catalase Rattus norvegicus 258-266 8557531-6 1995 Catalase in rat liver showed a Km value of 2.0 mM for its substrate hydrogen peroxide when the diaminobenzidine concentration was 5 mM. Hydrogen Peroxide 68-85 catalase Rattus norvegicus 0-8 7616120-11 1995 A positive correlation was also seen between catalase mRNA and H2O2 (r = 0.95, P < 0.001). Hydrogen Peroxide 63-67 catalase Rattus norvegicus 45-53 7976574-3 1994 The concentration of malondialdehyde (MDA; free radical) in cerebral cortex of aminotriazol (an H2O2-dependent inhibitor of catalase) treated rats 2 h after stroke was 6.33 times the level before infarction, while the concentration of MDA in h-r SOD (free radical-scavenging enzyme) treated rats 2 h after stroke was significantly lower than in untreated rats. Hydrogen Peroxide 96-100 catalase Rattus norvegicus 124-132 7986095-1 1994 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. Hydrogen Peroxide 69-73 catalase Rattus norvegicus 16-24 7986095-4 1994 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. Hydrogen Peroxide 165-169 catalase Rattus norvegicus 39-47 7519855-2 1994 H2O2 (1-5 mM) markedly increased NO synthase activity in the presence of endogenous catalase (72 +/- 4 U/mL). Hydrogen Peroxide 0-4 catalase Rattus norvegicus 84-92 7519855-3 1994 This effect of H2O2 was further increased by exogenous catalase (200 U/mL). Hydrogen Peroxide 15-19 catalase Rattus norvegicus 55-63 7519855-6 1994 This study suggests that H2O2 is not directly involved in NO synthesis and that the H2O2/catalase stimulation of NO synthase activity may be due to the excess oxygen produced by the H2O2/catalase system. Hydrogen Peroxide 84-88 catalase Rattus norvegicus 89-97 7496602-4 1995 Therefore, peroxisomal catalase also acts as an antioxidant defence mechanism by removing H2O2 and preventing the formation of hydroxyl radicals in the cell. Hydrogen Peroxide 90-94 catalase Rattus norvegicus 23-31 7524478-8 1994 After the pervanadate from 3 mM H2O2 and 1 mM Vi was treated with catalase, it was able to induce the [Ca2+]i increase and histamine secretion as much as the antigen did. Hydrogen Peroxide 32-36 catalase Rattus norvegicus 66-74 7954597-1 1994 OBJECTIVE: The aim was to investigate the potential for the enhancement of endogenous catalase activity after heat stress to protect the isolated rat myocardium from the injurious effects of exogenous hydrogen peroxide. Hydrogen Peroxide 201-218 catalase Rattus norvegicus 86-94 7768207-4 1994 The degradation of one such species, H2O2, is catalyzed by catalase and glutathione peroxidase (GSH Px). Hydrogen Peroxide 37-41 catalase Rattus norvegicus 59-67 8137175-3 1994 The catecholamine toxicity, reproduced by equimolar concentrations of H2O2, could be completely prevented by simultaneous treatment of OLs with the H2O2-decomposing enzyme catalase. Hydrogen Peroxide 70-74 catalase Rattus norvegicus 172-180 8137175-3 1994 The catecholamine toxicity, reproduced by equimolar concentrations of H2O2, could be completely prevented by simultaneous treatment of OLs with the H2O2-decomposing enzyme catalase. Hydrogen Peroxide 148-152 catalase Rattus norvegicus 172-180 7802591-10 1994 A comparison of the activity of enzymes involved in the detoxification of hydrogen peroxide showed that catalase and glutathione-S-transferase activity is 2.9-fold higher in monkey hepatocytes than in rat liver cells, while glutathione peroxidase activity was 1.6-fold higher in rat cells. Hydrogen Peroxide 74-91 catalase Rattus norvegicus 104-112 7606214-6 1994 The results suggest that enzymes are asynchronously incorporated into pre-existing peroxisomes; that this import is faster in smaller organelles than in the larger, adult ones; that catalase increases after the H2O2-producing oxidases; and that the abrupt rise of beta-oxidation capacity and DH-APAT is related to the increased renal work immediately after birth. Hydrogen Peroxide 211-215 catalase Rattus norvegicus 182-190 8280068-10 1993 Net K+ efflux under these conditions is enhanced when catalase is inhibited, suggesting that the rate of both intracellular H2O2 generation and degradation can modulate cellular K+ balance and cellular volume. Hydrogen Peroxide 124-128 catalase Rattus norvegicus 54-62 8226515-4 1993 Fiber bundles from rat diaphragm were incubated with exogenous catalase (an antioxidant enzyme that dehydrates hydrogen peroxide to molecular oxygen and water) to decrease the tissue concentration of reactive oxygen intermediates. Hydrogen Peroxide 111-128 catalase Rattus norvegicus 63-71 8214103-6 1993 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. Hydrogen Peroxide 27-44 catalase Rattus norvegicus 0-8 8138192-0 1993 Roles of catalase and cytochrome c in hydroperoxide-dependent lipid peroxidation and chemiluminescence in rat heart and kidney mitochondria. Hydrogen Peroxide 38-51 catalase Rattus norvegicus 9-17 8138192-7 1993 In catalase-containing preparations, H2O2 lipid peroxidation increased by only 40 to 96% over controls. Hydrogen Peroxide 37-41 catalase Rattus norvegicus 3-11 8283971-6 1993 Hydrogen peroxide inhibited creatine kinase activity in a concentration-dependent manner; this inhibition was prevented by the addition of catalase. Hydrogen Peroxide 0-17 catalase Rattus norvegicus 139-147 8395452-6 1993 Catalase (200 U/ml, n = 6) added to the perfusate attenuated all parameters of myocardial injury by eliminating H2O2 from the perfusate, and thus .OH was not detected in the effluent. Hydrogen Peroxide 112-116 catalase Rattus norvegicus 0-8 8394614-7 1993 The biphasic effect of H2O2 was blocked totally by 5-200 micrograms/l of catalase. Hydrogen Peroxide 23-27 catalase Rattus norvegicus 73-81 8366617-8 1993 Catalase (1000 U/ml), a H2O2 scavenger, completely inhibited the response of the isolated ring (without endothelium) to H2O2. Hydrogen Peroxide 24-28 catalase Rattus norvegicus 0-8 8366617-8 1993 Catalase (1000 U/ml), a H2O2 scavenger, completely inhibited the response of the isolated ring (without endothelium) to H2O2. Hydrogen Peroxide 120-124 catalase Rattus norvegicus 0-8 1431262-2 1992 To obtain information on the nature of the reactive oxygen species involved, the effect of catalase, a hydrogen peroxide scavenger, was tested. Hydrogen Peroxide 103-120 catalase Rattus norvegicus 91-99 8491514-2 1993 Serum H2O2 scavenging activity was inhibited by addition of sodium azide, a catalase inhibitor. Hydrogen Peroxide 6-10 catalase Rattus norvegicus 76-84 8491514-4 1993 We conclude that increased serum catalase activity is a consequence of thermal skin injury and that increased serum catalase activity may be a mechanism that modulates H2O2-dependent processes following skin burn. Hydrogen Peroxide 168-172 catalase Rattus norvegicus 116-124 8380162-6 1993 Attempts to counter the toxicity of SOD involved the covalent conjugation of SOD to catalase in an effort to lower the available free H2O2 and thus minimize the extent of the Fenton reaction. Hydrogen Peroxide 134-138 catalase Rattus norvegicus 84-92 8515989-0 1993 Catalase protection against hydrogen peroxide-induced injury in rat oral mucosa. Hydrogen Peroxide 28-45 catalase Rattus norvegicus 0-8 8515989-2 1993 This study assesses the protective effect of catalase against the hydrogen peroxide insult in the rat tongue mucosa. Hydrogen Peroxide 66-83 catalase Rattus norvegicus 45-53 8515989-7 1993 Catalase applied to the tongue before the hydrogen peroxide fully prevented the pathologic tissue reaction. Hydrogen Peroxide 42-59 catalase Rattus norvegicus 0-8 8515989-8 1993 Thus testing of the clinical feasibility of catalase in protecting the oral mucosa against hydrogen peroxide-induced injury is strongly indicated. Hydrogen Peroxide 91-108 catalase Rattus norvegicus 44-52 8098954-5 1993 This inactivation was prevented by catalase, which suggests that the NAD(P)H/BV2+/O2-dependent system has a role in H2O2 production. Hydrogen Peroxide 116-120 catalase Rattus norvegicus 35-43 8380970-0 1993 The role of cytochrome c and mitochondrial catalase in hydroperoxide-induced heart mitochondrial lipid peroxidation. Hydrogen Peroxide 55-68 catalase Rattus norvegicus 43-51 8380970-3 1993 Catalase-depleted mitochondria were more susceptible to H2O2-dependent lipid peroxidation and had similar extents of tert-butyl hydroperoxide (t-BuOOH)-induced lipid peroxidation compared with control mitochondria. Hydrogen Peroxide 56-60 catalase Rattus norvegicus 0-8 8380970-7 1993 These data show a critical role for cytochrome c3+ in hydroperoxide-induced mitochondrial lipid peroxidation and demonstrate the importance of matrix catalase in protecting heart mitochondria from the toxicity of H2O2. Hydrogen Peroxide 213-217 catalase Rattus norvegicus 150-158 8168729-1 1993 The objective of this study was to determine whether inhibition of intracellular catalase would decrease the tolerance of the heart to ischemia-reperfusion and hydrogen peroxide-induced injuries. Hydrogen Peroxide 160-177 catalase Rattus norvegicus 81-89 1337274-4 1992 Activation was inhibited by the antioxidants, vitamin E and nordihydroguaiaretic acid, and by superoxide dismutase and catalase, which metabolize SOR and H2O2 to remove reactive oxygen species from the cell. Hydrogen Peroxide 154-158 catalase Rattus norvegicus 119-127 1329980-4 1992 Hydrogen peroxide inhibited creatine kinase activity in a dose-dependent manner, this inhibition was protected by the addition of catalase. Hydrogen Peroxide 0-17 catalase Rattus norvegicus 130-138 1329980-6 1992 Mitochondrial sulfhydryl groups contents were decreased by xanthine plus xanthine oxidase or hydrogen peroxide; this depression in sulfhydryl groups contents was prevented by the addition of superoxide dismutase or catalase. Hydrogen Peroxide 93-110 catalase Rattus norvegicus 215-223 1627338-6 1992 When the cells were exposed to a high (0.25 mM) H2O2 concentration, H2O2-scavenging capacity decreased remarkably when catalase was inactivated. Hydrogen Peroxide 48-52 catalase Rattus norvegicus 119-127 1328230-1 1992 The successful prevention of hydrogen peroxide-induced damage to the rat jejunal mucosa by cationized catalase is described in this study. Hydrogen Peroxide 29-46 catalase Rattus norvegicus 102-110 1524418-7 1992 Oxidation of 1,2-propanediol to formaldehyde plus acetaldehyde involved interaction with an oxidant derived from H2O2 plus nonheme iron, since production of the two aldehydic products was completely prevented by catalase or glutathione plus glutathione peroxidase and by chelators such as desferrioxamine or EDTA. Hydrogen Peroxide 113-117 catalase Rattus norvegicus 212-220 1443417-3 1992 Rates of hydrogen peroxide production, assessed from the oxidation of methanol to formaldehyde by catalase-H2O2, were similar in tissue cylinders isolated from periportal regions in control and ethanol-treated rats. Hydrogen Peroxide 9-26 catalase Rattus norvegicus 98-106 1443417-3 1992 Rates of hydrogen peroxide production, assessed from the oxidation of methanol to formaldehyde by catalase-H2O2, were similar in tissue cylinders isolated from periportal regions in control and ethanol-treated rats. Hydrogen Peroxide 107-111 catalase Rattus norvegicus 98-106 1627338-6 1992 When the cells were exposed to a high (0.25 mM) H2O2 concentration, H2O2-scavenging capacity decreased remarkably when catalase was inactivated. Hydrogen Peroxide 68-72 catalase Rattus norvegicus 119-127 1627338-7 1992 When the cells were exposed to 0.1 to 0.5 mM H2O2, cell cytotoxicity (lactate dehydrogenase release) increased significantly if glutathione reductase was inactivated; catalase inactivation resulted in a significant cytotoxicity only at high (greater than or equal to 0.25 mM) H2O2 concentrations. Hydrogen Peroxide 45-49 catalase Rattus norvegicus 167-175 1627338-7 1992 When the cells were exposed to 0.1 to 0.5 mM H2O2, cell cytotoxicity (lactate dehydrogenase release) increased significantly if glutathione reductase was inactivated; catalase inactivation resulted in a significant cytotoxicity only at high (greater than or equal to 0.25 mM) H2O2 concentrations. Hydrogen Peroxide 276-280 catalase Rattus norvegicus 167-175 1627338-11 1992 When intact cells were treated with different antioxidants and exposed to 0.5 mM H2O2, both catalase and 3-aminobenzamide protected the cells completely. Hydrogen Peroxide 81-85 catalase Rattus norvegicus 92-100 1326736-9 1992 This increase in 51Cr release was inhibited by catalase, a scavenger of hydrogen peroxide, or dimethyl sulfoxide, a scavenger of hydroxyl radicals, but not by superoxide dismutase, a scavenger of superoxide, nor deferoxamine, an inhibitor of hydroxyl radical generation. Hydrogen Peroxide 72-89 catalase Rattus norvegicus 47-55 1405036-3 1992 Hydrogen peroxide also caused a significant decrease in the enzyme activity; and this effect of hydrogen peroxide was counteracted by catalase and dithiothreitol, but not by mannitol, dimethyl sulfoxide and reduced glutathione. Hydrogen Peroxide 0-17 catalase Rattus norvegicus 134-142 1405036-3 1992 Hydrogen peroxide also caused a significant decrease in the enzyme activity; and this effect of hydrogen peroxide was counteracted by catalase and dithiothreitol, but not by mannitol, dimethyl sulfoxide and reduced glutathione. Hydrogen Peroxide 96-113 catalase Rattus norvegicus 134-142 1733283-5 1992 Addition of the specific catalase inhibitor, aminotriazole, decreased the rate of consumption of exogenously added H2O2 in freshly isolated cells but not in cultured cells. Hydrogen Peroxide 115-119 catalase Rattus norvegicus 25-33 1559931-7 1992 Glutathione peroxidase, glutathione reductase, superoxide dismutase, and catalase activities were significantly elevated after exhaustive exercise with or without hydroperoxide injection in muscle but not in liver. Hydrogen Peroxide 163-176 catalase Rattus norvegicus 73-81 1663741-5 1991 Catalase inhibited both Fe(2+)-H2O2 induced oxalate binding and lipid peroxidation reactions, suggesting that the induced oxalate binding in mitochondria was mediated through the hydroxyl radical reaction mechanism. Hydrogen Peroxide 31-35 catalase Rattus norvegicus 0-8 1657986-8 1991 Thus catalase, representing 0.025% of heart mitochondrial protein, is important for detoxifying mitochondrial derived H2O2 and represents a key antioxidant defense mechanism for myocardial tissue. Hydrogen Peroxide 118-122 catalase Rattus norvegicus 5-13 1757301-3 1991 We investigated the relationship between regional generation of hydrogen peroxide (H2O2) in the brain in the presence of an irreversible inhibitor of catalase, aminotriazole (ATZ), and protection from CNS O2 toxicity by a monoamine oxidase (MAO) inhibitor, pargyline. Hydrogen Peroxide 64-81 catalase Rattus norvegicus 150-158 1757301-3 1991 We investigated the relationship between regional generation of hydrogen peroxide (H2O2) in the brain in the presence of an irreversible inhibitor of catalase, aminotriazole (ATZ), and protection from CNS O2 toxicity by a monoamine oxidase (MAO) inhibitor, pargyline. Hydrogen Peroxide 83-87 catalase Rattus norvegicus 150-158 1757301-6 1991 Because ATZ-mediated inactivation of catalase was H2O2 dependent, the decrease in catalase activity during hyperoxia was proportional to the intracellular production of H2O2. Hydrogen Peroxide 50-54 catalase Rattus norvegicus 37-45 1757301-6 1991 Because ATZ-mediated inactivation of catalase was H2O2 dependent, the decrease in catalase activity during hyperoxia was proportional to the intracellular production of H2O2. Hydrogen Peroxide 169-173 catalase Rattus norvegicus 37-45 1757301-6 1991 Because ATZ-mediated inactivation of catalase was H2O2 dependent, the decrease in catalase activity during hyperoxia was proportional to the intracellular production of H2O2. Hydrogen Peroxide 169-173 catalase Rattus norvegicus 82-90 1687018-7 1991 H2O2 itself did not oxidize ethylene glycol to formaldehyde; however, the microsomal reaction was inhibited by catalase or glutathione plus glutathione peroxidase and was stimulated by added H2O2 in the presence of NADPH. Hydrogen Peroxide 0-4 catalase Rattus norvegicus 111-119 1687018-7 1991 H2O2 itself did not oxidize ethylene glycol to formaldehyde; however, the microsomal reaction was inhibited by catalase or glutathione plus glutathione peroxidase and was stimulated by added H2O2 in the presence of NADPH. Hydrogen Peroxide 191-195 catalase Rattus norvegicus 111-119 12106245-5 1991 This toxicity involved the production by brain macrophages of reactive oxygen intermediates, as shown by the protective effect of catalase, a scavenger of H2O2. Hydrogen Peroxide 155-159 catalase Rattus norvegicus 130-138 1872419-7 1991 Aminotriazole is a compound that inhibits catalase in the presence of H2O2 at a rate that is proportional to the rate of intracellular H2O2 production in or near peroxisomes. Hydrogen Peroxide 70-74 catalase Rattus norvegicus 42-50 1872419-7 1991 Aminotriazole is a compound that inhibits catalase in the presence of H2O2 at a rate that is proportional to the rate of intracellular H2O2 production in or near peroxisomes. Hydrogen Peroxide 135-139 catalase Rattus norvegicus 42-50 1859472-2 1991 Furthermore, the inhibition of brain catalase by AT demonstrates the presence of hydrogen peroxide in brain, since AT inhibits catalase in the presence of this compound. Hydrogen Peroxide 81-98 catalase Rattus norvegicus 37-45 1859472-2 1991 Furthermore, the inhibition of brain catalase by AT demonstrates the presence of hydrogen peroxide in brain, since AT inhibits catalase in the presence of this compound. Hydrogen Peroxide 81-98 catalase Rattus norvegicus 127-135 1859472-3 1991 The rate of inhibition of catalase seems to be dependent upon the rate by which H2O2 is generated. Hydrogen Peroxide 80-84 catalase Rattus norvegicus 26-34 1646749-0 1991 Hydrogen peroxide and ischemic renal injury: effect of catalase inhibition. Hydrogen Peroxide 0-17 catalase Rattus norvegicus 55-63 1708332-10 1991 Since catalase reversed the effects of xanthine oxidase, we conclude that superoxide was rapidly dismuted to hydrogen peroxide and mediated the antigonadotropic and antisteroidogenic actions of xanthine oxidase in luteal cells. Hydrogen Peroxide 109-126 catalase Rattus norvegicus 6-14 2018152-0 1991 Injury of rat pulmonary alveolar epithelial cells by H2O2: dependence on phenotype and catalase. Hydrogen Peroxide 53-57 catalase Rattus norvegicus 87-95 1646033-2 1991 Xanthine plus xanthine oxidase (X + XO) which is known to generate superoxide anions (O2-) and hydrogen peroxide (H2O2), an activated species of oxygen, was found to decrease Ca(2+)-stimulated ATPase activity, increase Mg(2+)-ATPase activity and reduce sulfhydryl (SH) group contents in myofibrils; these effects were completely prevented by superoxide dismutase (SOD) plus catalase (CAT). Hydrogen Peroxide 95-112 catalase Rattus norvegicus 374-382 1646033-2 1991 Xanthine plus xanthine oxidase (X + XO) which is known to generate superoxide anions (O2-) and hydrogen peroxide (H2O2), an activated species of oxygen, was found to decrease Ca(2+)-stimulated ATPase activity, increase Mg(2+)-ATPase activity and reduce sulfhydryl (SH) group contents in myofibrils; these effects were completely prevented by superoxide dismutase (SOD) plus catalase (CAT). Hydrogen Peroxide 95-112 catalase Rattus norvegicus 384-387 1646033-2 1991 Xanthine plus xanthine oxidase (X + XO) which is known to generate superoxide anions (O2-) and hydrogen peroxide (H2O2), an activated species of oxygen, was found to decrease Ca(2+)-stimulated ATPase activity, increase Mg(2+)-ATPase activity and reduce sulfhydryl (SH) group contents in myofibrils; these effects were completely prevented by superoxide dismutase (SOD) plus catalase (CAT). Hydrogen Peroxide 114-118 catalase Rattus norvegicus 374-382 1646033-2 1991 Xanthine plus xanthine oxidase (X + XO) which is known to generate superoxide anions (O2-) and hydrogen peroxide (H2O2), an activated species of oxygen, was found to decrease Ca(2+)-stimulated ATPase activity, increase Mg(2+)-ATPase activity and reduce sulfhydryl (SH) group contents in myofibrils; these effects were completely prevented by superoxide dismutase (SOD) plus catalase (CAT). Hydrogen Peroxide 114-118 catalase Rattus norvegicus 384-387 1646033-4 1991 The effects of H2O2 and HOCl were prevented by CAT and L-methionine, respectively. Hydrogen Peroxide 15-19 catalase Rattus norvegicus 47-50 1916946-7 1991 Incubation with zymosan resulted in rapid decline in catalase levels, facilitating evolution of H2O2. Hydrogen Peroxide 96-100 catalase Rattus norvegicus 53-61 1901719-5 1991 Exposure to H2O2 led to reduced cytotoxicity in cells pretreated with PEG-catalase than in controls. Hydrogen Peroxide 12-16 catalase Rattus norvegicus 74-82 1984785-5 1991 The lesion was abolished by catalase, superoxide dismutase (both enzymes inhibit delta-aminolevulinic acid autoxidation) and ortho-phenanthroline, but not by mannitol; added H2O2 induces damage poorly. Hydrogen Peroxide 174-178 catalase Rattus norvegicus 28-36 1818795-4 1991 As an indication of free radical production, catalase activity was measured, reflecting the production of hydrogen peroxide (H2O2). Hydrogen Peroxide 106-123 catalase Rattus norvegicus 45-53 1818795-4 1991 As an indication of free radical production, catalase activity was measured, reflecting the production of hydrogen peroxide (H2O2). Hydrogen Peroxide 125-129 catalase Rattus norvegicus 45-53 1646749-3 1991 3-amino-1,2,4-triazole reacts with catalase to form irreversibly inactivated catalase only in the presence of hydrogen peroxide. Hydrogen Peroxide 110-127 catalase Rattus norvegicus 35-43 1646749-3 1991 3-amino-1,2,4-triazole reacts with catalase to form irreversibly inactivated catalase only in the presence of hydrogen peroxide. Hydrogen Peroxide 110-127 catalase Rattus norvegicus 77-85 1646749-4 1991 We made use of this chemical reaction both to determine whether inhibition of the hydrogen peroxide-scavenging enzyme catalase would influence ischemic renal injury and to measure hydrogen peroxide production rates after ischemia. Hydrogen Peroxide 82-99 catalase Rattus norvegicus 118-126 2058415-11 1991 This method is based on the notion that aminotriazole interacts with H2O2 to inactivate catalase; thus, the rate of inactivation of catalase in aminotriazole treated animals reflects H2O2 production. Hydrogen Peroxide 69-73 catalase Rattus norvegicus 88-96 1962845-4 1990 Both the Ca2(+)-pump and Na(+)-Ca2+ exchange activities in control heart sarcolemmal preparations were depressed by activated oxygen-generating systems containing xanthine plus xanthine oxidase and H2O2; these changes were prevented by the inclusion of superoxide dismutase and catalase in the incubation medium. Hydrogen Peroxide 198-202 catalase Rattus norvegicus 278-286 2058415-11 1991 This method is based on the notion that aminotriazole interacts with H2O2 to inactivate catalase; thus, the rate of inactivation of catalase in aminotriazole treated animals reflects H2O2 production. Hydrogen Peroxide 69-73 catalase Rattus norvegicus 132-140 2058415-11 1991 This method is based on the notion that aminotriazole interacts with H2O2 to inactivate catalase; thus, the rate of inactivation of catalase in aminotriazole treated animals reflects H2O2 production. Hydrogen Peroxide 183-187 catalase Rattus norvegicus 88-96 2058415-11 1991 This method is based on the notion that aminotriazole interacts with H2O2 to inactivate catalase; thus, the rate of inactivation of catalase in aminotriazole treated animals reflects H2O2 production. Hydrogen Peroxide 183-187 catalase Rattus norvegicus 132-140 2058415-13 1991 Animals given aminotriazole, whether rendered ischemic or not, showed a reduced tissue catalase activity, reflecting H2O2 production in the brain. Hydrogen Peroxide 117-121 catalase Rattus norvegicus 87-95 2241155-2 1990 Since H2O2 can be produced by autooxidation of the tetrahydropterin cofactor required for the hydroxylation reaction, in vitro assays are usually carried out in the presence of added catalase. Hydrogen Peroxide 6-10 catalase Rattus norvegicus 183-191 2090584-5 1990 Hydrogen peroxide-stimulated 6-keto-PGF1 alpha release was completely blocked by indomethacin, significantly blocked (69%) by nordihydroguiaretic acid, and completely blocked by catalase. Hydrogen Peroxide 0-17 catalase Rattus norvegicus 178-186 2090584-7 1990 Endogenous catalase inhibitors 3-aminotriazole and sodium azide further enhanced the release of 6-keto-PGF1 alpha stimulated by H2O2 by 29% and 73%, respectively. Hydrogen Peroxide 128-132 catalase Rattus norvegicus 11-19 2090584-10 1990 These studies suggest a direct effect of H2O2 on colonic fragments leading to submicroscopic cellular membrane damage and excess prostanoid production utilizing a PLA2/cyclooxygenase and catalase-sensitive pathway without the formation of toxic hydroxyl ions. Hydrogen Peroxide 41-45 catalase Rattus norvegicus 187-195 2311188-7 1990 However hepatic capacities of H2O2-degrading enzymes, catalase and GSH-Px, apparently exceeded the H2O2-generating levels obtained on the basis of peroxisomal beta-oxidation activities in the livers of control and treated rats throughout the experimental period. Hydrogen Peroxide 30-34 catalase Rattus norvegicus 54-62 2277034-0 1990 Significance of catalase in peroxisomal fatty acyl-CoA beta-oxidation: NADH oxidation by acetoacetyl-CoA and H2O2. Hydrogen Peroxide 109-113 catalase Rattus norvegicus 16-24 2277034-11 1990 Acta 921, 142-150] suggest that the role of catalase in peroxisomes is at least in part to protect the fatty acyl-CoA beta-oxidation system from the deleterious action of H2O2. Hydrogen Peroxide 171-175 catalase Rattus norvegicus 44-52 2164334-5 1990 This injury was ameliorated by the addition of catalase, which neutralizes hydrogen peroxide produced during the respiratory burst. Hydrogen Peroxide 75-92 catalase Rattus norvegicus 47-55 2382268-1 1990 The decomposition of H2O2 by catalase (CAT) was measured in a cell-free in vitro system in the presence of 0-24 mM Ni(II) or Mg(II) as well as in red blood cells (RBCs), and in post-mitochondrial fractions of liver and kidney of rats injected i.p. Hydrogen Peroxide 21-25 catalase Rattus norvegicus 29-37 2382268-1 1990 The decomposition of H2O2 by catalase (CAT) was measured in a cell-free in vitro system in the presence of 0-24 mM Ni(II) or Mg(II) as well as in red blood cells (RBCs), and in post-mitochondrial fractions of liver and kidney of rats injected i.p. Hydrogen Peroxide 21-25 catalase Rattus norvegicus 39-42 2155813-3 1990 As superoxide dismutase and catalase reduced the ulcerogenesis induced by diethyldithiocarbamate, the superoxide radical and hydrogen peroxide were considered to play a pathogenic role in this ulcer model. Hydrogen Peroxide 125-142 catalase Rattus norvegicus 28-36 2311188-9 1990 Our results suggest that a large part of H2O2 produced by peroxisomal beta-oxidation could be rapidly scavenged by catalase and GSH-Px in the liver of rats treated with peroxisome proliferators. Hydrogen Peroxide 41-45 catalase Rattus norvegicus 115-123 34309037-9 2022 However, pre-treatment with the hydrolysates in PC12 cells, which were then injured by H2 O2 , markedly attenuated ROS generation and enhanced the activities and mRNA expression of the endogenous antioxidant enzymes (catalase (CAT), glutathione peroxidase (GPx), and superoxide dismutase (SOD)), leading to a 26.68% increase in cell viability. Hydrogen Peroxide 87-92 catalase Rattus norvegicus 217-225 2295642-4 1990 Both effects of butanol were blocked by an inhibitor of ADH, 4-methylpyrazole, consistent with the hypothesis that elevation of the NADH redox state by butanol inhibited H2O2 production via NAD+-requiring peroxisomal beta-oxidation, leading indirectly to diminished rates of catalase-dependent methanol uptake. Hydrogen Peroxide 170-174 catalase Rattus norvegicus 275-283 2295642-8 1990 Taken together, these data indicate that generation of reducing equivalents from ADH in the cytosol inhibits H2O2 generation leading to significantly diminished rates of peroxidation of alcohols via catalase. Hydrogen Peroxide 109-113 catalase Rattus norvegicus 199-207 2386536-7 1990 3) The significant reduction in catalase activity denotes the decreased formation of hydrogenperoxides during exercise; and 4) The pattern of changes in the activity level of GPxI indicate its least participation during exercise. Hydrogen Peroxide 85-102 catalase Rattus norvegicus 32-40 34968071-2 2022 To tackle this limitation, previous studies adopted a cascade reaction between the degradation of uric acid (UA) and timely elimination of H2O2 using complicated composites of uricase and catalase (CAT)/CAT-like nanozyme. Hydrogen Peroxide 139-143 catalase Rattus norvegicus 188-196 34968071-2 2022 To tackle this limitation, previous studies adopted a cascade reaction between the degradation of uric acid (UA) and timely elimination of H2O2 using complicated composites of uricase and catalase (CAT)/CAT-like nanozyme. Hydrogen Peroxide 139-143 catalase Rattus norvegicus 198-201 34968071-2 2022 To tackle this limitation, previous studies adopted a cascade reaction between the degradation of uric acid (UA) and timely elimination of H2O2 using complicated composites of uricase and catalase (CAT)/CAT-like nanozyme. Hydrogen Peroxide 139-143 catalase Rattus norvegicus 203-206 34968071-3 2022 Herein, the self-cascade nanozyme Pt/CeO2 with high efficiency toward simultaneous UA degradation and H2O2 elimination is demonstrated on the basis of both uricase- and CAT-like activities in Pt, Ir, Rh, and Pd platinum-group metals. Hydrogen Peroxide 102-106 catalase Rattus norvegicus 169-172 34887995-3 2021 The results showed that salidroside significantly alleviated cell growth inhibition induced by H2O2 treatment in H9C2 cells, decreased the levels of intracellular ROS and malondialdehyde (MDA), and increased the activity of superoxide dismutase (SOD) and catalase (CAT); meanwhile, salidroside upregulated the expression of Bcl-2 while downregulated the expression of Bax, p53, and caspase-3 in H2O2-treated H9C2 cells. Hydrogen Peroxide 95-99 catalase Rattus norvegicus 265-268 2325161-6 1990 NGF protection from hydrogen peroxide is partially abolished by aminotriazole (Az), a low molecular weight catalase inhibitor. Hydrogen Peroxide 20-37 catalase Rattus norvegicus 107-115 18215347-11 2008 The activity of catalase was reduced in the arteries with endothelium of 1-year-old rats, indicating that hydrogen peroxide is the likely mediator of increased oxidative stress in the aging endothelium. Hydrogen Peroxide 106-123 catalase Rattus norvegicus 16-24 34775236-9 2022 The results demonstrated that D1M significantly decreased the release of nitric oxide (NO), formation of intracellular reactive oxygen species (ROS), and the level of malondialdehyde (MDA), whereas it enhanced the content of glutathione (GSH), and activity of heme oxygenase 1 (HO-1), NAD(P)H: quinone oxidoreductase 1 (NQO1), and catalase (CAT) in PC12 cells exposed to H2O2. Hydrogen Peroxide 371-375 catalase Rattus norvegicus 331-339 34775236-9 2022 The results demonstrated that D1M significantly decreased the release of nitric oxide (NO), formation of intracellular reactive oxygen species (ROS), and the level of malondialdehyde (MDA), whereas it enhanced the content of glutathione (GSH), and activity of heme oxygenase 1 (HO-1), NAD(P)H: quinone oxidoreductase 1 (NQO1), and catalase (CAT) in PC12 cells exposed to H2O2. Hydrogen Peroxide 371-375 catalase Rattus norvegicus 341-344 34900030-10 2021 By detecting the supernatant, it was found that the contents of LDH were significantly increased, and the contents of SOD and CAT in the H2O2 group were significantly decreased. Hydrogen Peroxide 137-141 catalase Rattus norvegicus 126-129 34500721-6 2021 The MMP integrity, as well as the SOD, CAT, and GPx activity, of F3 and F6 were also increased significantly compared to the H2O2 in Clone-9 cells. Hydrogen Peroxide 125-129 catalase Rattus norvegicus 39-42 34309037-9 2022 However, pre-treatment with the hydrolysates in PC12 cells, which were then injured by H2 O2 , markedly attenuated ROS generation and enhanced the activities and mRNA expression of the endogenous antioxidant enzymes (catalase (CAT), glutathione peroxidase (GPx), and superoxide dismutase (SOD)), leading to a 26.68% increase in cell viability. Hydrogen Peroxide 87-92 catalase Rattus norvegicus 227-230 34257805-4 2021 Compared with the control group, the activities of superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GSH-Px) were significantly decreased, and the content of malondialdehyde (MDA) was significantly increased in the H2O2 group. Hydrogen Peroxide 237-241 catalase Rattus norvegicus 79-87 34121192-7 2021 In addition, PP-S4-1 could significantly inhibit the decrease of superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GSH-Px) activity as well as the increase of MDA content in H9c2 cells induced by H2 O2 . Hydrogen Peroxide 218-223 catalase Rattus norvegicus 93-101 34121192-7 2021 In addition, PP-S4-1 could significantly inhibit the decrease of superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GSH-Px) activity as well as the increase of MDA content in H9c2 cells induced by H2 O2 . Hydrogen Peroxide 218-223 catalase Rattus norvegicus 103-106 34257805-4 2021 Compared with the control group, the activities of superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GSH-Px) were significantly decreased, and the content of malondialdehyde (MDA) was significantly increased in the H2O2 group. Hydrogen Peroxide 237-241 catalase Rattus norvegicus 89-92 34257805-5 2021 By AEE pretreatment, the level of MDA was reduced and the levels of SOD, CAT, and GSH-Px were increased in H2O2-stimulated PC12 cells. Hydrogen Peroxide 107-111 catalase Rattus norvegicus 73-76 34067571-4 2021 Compared with H2O2 alone, PCs enhanced antioxidant activities (e.g., GSH-Px, CAT, and SOD), decreased levels of ROS and MDA, and enhanced Nrf2/ antioxidant response element (ARE) activation and raised expression levels of NQO1, HO-1, GCLM, and GCLC. Hydrogen Peroxide 14-18 catalase Rattus norvegicus 77-80 35447320-7 2022 Site-specific expression of catalase in cytosol, mitochondria, and ER attenuated lipid peroxidation, indicating the contribution of metabolically generated H2O2 from all three subcellular compartments. Hydrogen Peroxide 156-160 catalase Rattus norvegicus 28-36 35390465-6 2022 Pretreatment with catalase, a H2O2-scavenging enzyme, blocked the effects of PD toxins on NOX2-dependent H2O2 production, AMPK/Akt/mTOR signaling and apoptosis in the cells. Hydrogen Peroxide 105-109 catalase Rattus norvegicus 18-26 2624761-2 1989 In the present study, we investigated the roles of intracellular catalase and glutathione-dependent reactions in providing protection against cytotoxic concentrations of H2O2 and stimulated neutrophils. Hydrogen Peroxide 170-174 catalase Rattus norvegicus 65-73 35473521-4 2022 MATERIALS AND METHODS: PC12 cells were simultaneously treated with 400 muM H2O2 and sesquiterpenoid compounds or vitamin E (used as a positive control) for 24 h. The activities of GSH-Px, LDH, CAT, and SOD were detected by ELISA kits. Hydrogen Peroxide 75-79 catalase Rattus norvegicus 193-196 2551190-7 1989 Superoxide dismutase, catalase, and D-mannitol showed protective effects on the sulfhydryl group depression by O2-., H2O2, and .OH, respectively. Hydrogen Peroxide 117-121 catalase Rattus norvegicus 22-30 2774554-4 1989 Inhibition of .OH production by catalase implicates H2O2 as the precursor of .OH generated by the nuclei, whereas superoxide dismutase had only a partially inhibitory effect. Hydrogen Peroxide 52-56 catalase Rattus norvegicus 32-40 35390465-6 2022 Pretreatment with catalase, a H2O2-scavenging enzyme, blocked the effects of PD toxins on NOX2-dependent H2O2 production, AMPK/Akt/mTOR signaling and apoptosis in the cells. Hydrogen Peroxide 30-34 catalase Rattus norvegicus 18-26 2550081-6 1989 Perfusion with catalase (550 U/ml) completely suppressed the OH signal both in the presence and absence of the drugs, thus suggesting the intermediacy of hydrogen peroxide. Hydrogen Peroxide 154-171 catalase Rattus norvegicus 15-23 2782423-1 1989 Aminotriazole-mediated inhibition of catalase has been used in previous studies as a measure of in vivo changes in the hydrogen peroxide generation. Hydrogen Peroxide 119-136 catalase Rattus norvegicus 37-45 2782423-4 1989 We confirmed that catalase inactivation by aminotriazole was due to formation of catalase-hydrogen peroxide intermediate (compound I) because catalase inactivation was prevented by ethanol, a competitive substrate for compound I. Hydrogen Peroxide 90-107 catalase Rattus norvegicus 18-26 2782423-4 1989 We confirmed that catalase inactivation by aminotriazole was due to formation of catalase-hydrogen peroxide intermediate (compound I) because catalase inactivation was prevented by ethanol, a competitive substrate for compound I. Hydrogen Peroxide 90-107 catalase Rattus norvegicus 81-89 2782423-4 1989 We confirmed that catalase inactivation by aminotriazole was due to formation of catalase-hydrogen peroxide intermediate (compound I) because catalase inactivation was prevented by ethanol, a competitive substrate for compound I. Hydrogen Peroxide 90-107 catalase Rattus norvegicus 81-89 2476132-5 1989 The hydroxyl radical generation was inhibited by catalase and superoxide dismutase, suggesting a mechanism in which the phenols oxidize to produce superoxide radical, which then assists .OH generation from H2O2 in the presence of Fe3+-EDTA. Hydrogen Peroxide 206-210 catalase Rattus norvegicus 49-57 2624761-3 1989 Catalase was found to be instrumental in protecting epithelial cells because when inhibited by either azide or 3-amino-1,2,4-triazole, there was an increase in the cytotoxic effect of exogenous H2O2 and stimulated neutrophils. Hydrogen Peroxide 194-198 catalase Rattus norvegicus 0-8 2788883-2 1989 Our results show that pigmented tissue is lacking in manganese superoxide dismutase activity and that the main enzymatic activity utilized in the cytosol by pigmented cells to reduce the hydrogen peroxide to water is represented by catalase; on the contrary, for the same reaction, the cells of albino rat liver primarily utilize the glutathione peroxidase activity. Hydrogen Peroxide 187-204 catalase Rattus norvegicus 232-240 2928952-1 1989 To investigate the specific nature and timing of oxygen (O2) metabolite reperfusion injury, we used a rat-heart model (Langendorff"s solution, 37 degrees C) and hydrogen peroxide (H2O2)-dependent aminotriazole inactivation of catalase as a measure of myocardial H2O2 before, during, and after ischemia. Hydrogen Peroxide 180-184 catalase Rattus norvegicus 226-234 2492771-1 1989 Superoxide dismutase and catalase enzymatically scavenge superoxide and hydrogen peroxide, respectively. Hydrogen Peroxide 72-89 catalase Rattus norvegicus 25-33 2537662-1 1989 Bovine liver catalase (hydrogen-peroxide:hydrogen peroxide oxidoreductase, EC 1.11.1.6) was derivatized by 9"(10")-[4"-(2-(4,6-dichloro-1,3,5-triazinyl) oxy)butoxy] stearic acid and the fatty acyl-coated enzyme was separated from native catalase and excess reagent by hydroxyapatite chromatography. Hydrogen Peroxide 23-40 catalase Rattus norvegicus 13-21 2537662-1 1989 Bovine liver catalase (hydrogen-peroxide:hydrogen peroxide oxidoreductase, EC 1.11.1.6) was derivatized by 9"(10")-[4"-(2-(4,6-dichloro-1,3,5-triazinyl) oxy)butoxy] stearic acid and the fatty acyl-coated enzyme was separated from native catalase and excess reagent by hydroxyapatite chromatography. Hydrogen Peroxide 23-40 catalase Rattus norvegicus 237-245 2537032-6 1989 Superoxide dismutase showed a protective effect on depression in Ca2+-pump activities caused by O2-.H2O2 inhibited Ca2+-pump activities in a dose-dependent manner; this inhibition was protected by the addition of catalase. Hydrogen Peroxide 100-104 catalase Rattus norvegicus 213-221 2550151-6 1989 Catalase can be stimulatory, inhibitory or without affect because H2O2 may oxidize some Fe2+ to form the required Fe3+, or, alternatively, excess H2O2 may inhibit by excessive oxidation of the Fe2+. Hydrogen Peroxide 66-70 catalase Rattus norvegicus 0-8 2918717-4 1989 In another experimental group, the role of hydrogen peroxide was evaluated by the infusion of catalase at the time of reperfusion. Hydrogen Peroxide 43-60 catalase Rattus norvegicus 94-102 2550151-6 1989 Catalase can be stimulatory, inhibitory or without affect because H2O2 may oxidize some Fe2+ to form the required Fe3+, or, alternatively, excess H2O2 may inhibit by excessive oxidation of the Fe2+. Hydrogen Peroxide 146-150 catalase Rattus norvegicus 0-8 3169246-0 1988 Hepatic ethanol metabolism is mediated predominantly by catalase-H2O2 in the fasted state. Hydrogen Peroxide 65-69 catalase Rattus norvegicus 56-64 2912161-2 1989 Aminotriazole irreversibly inactivates catalase only in the presence of hydrogen peroxide, and previous studies have shown that aminotriazole-mediated inhibition of catalase is a measure of in vivo changes in the hydrogen peroxide generation. Hydrogen Peroxide 72-89 catalase Rattus norvegicus 39-47 2912161-2 1989 Aminotriazole irreversibly inactivates catalase only in the presence of hydrogen peroxide, and previous studies have shown that aminotriazole-mediated inhibition of catalase is a measure of in vivo changes in the hydrogen peroxide generation. Hydrogen Peroxide 213-230 catalase Rattus norvegicus 39-47 2912161-2 1989 Aminotriazole irreversibly inactivates catalase only in the presence of hydrogen peroxide, and previous studies have shown that aminotriazole-mediated inhibition of catalase is a measure of in vivo changes in the hydrogen peroxide generation. Hydrogen Peroxide 213-230 catalase Rattus norvegicus 165-173 2912161-4 1989 We confirmed that catalase inactivation by aminotriazole was due to formation of a catalase-hydrogen peroxide intermediate (compound I) because catalase inactivation was prevented by ethanol (2 g/kg), a competitive substrate for compound I. Hydrogen Peroxide 92-109 catalase Rattus norvegicus 18-26 2912161-4 1989 We confirmed that catalase inactivation by aminotriazole was due to formation of a catalase-hydrogen peroxide intermediate (compound I) because catalase inactivation was prevented by ethanol (2 g/kg), a competitive substrate for compound I. Hydrogen Peroxide 92-109 catalase Rattus norvegicus 83-91 2912161-4 1989 We confirmed that catalase inactivation by aminotriazole was due to formation of a catalase-hydrogen peroxide intermediate (compound I) because catalase inactivation was prevented by ethanol (2 g/kg), a competitive substrate for compound I. Hydrogen Peroxide 92-109 catalase Rattus norvegicus 83-91 2912161-8 1989 Aminotriazole-mediated inhibition of catalase has been used in previous studies as a measure of in vivo changes in the hydrogen peroxide generation. Hydrogen Peroxide 119-136 catalase Rattus norvegicus 37-45 2540265-8 1989 Experiments in vitro with .OH-scavengers (dimethylsulfoxide, ethanol) and with the enzyme, catalase, confirmed both the presence of .OH and its dependence upon generated hydrogen peroxide during the oxidation of ferrous salt by molecular oxygen. Hydrogen Peroxide 170-187 catalase Rattus norvegicus 91-99 3192184-10 1988 The toxicity of glucose oxidase was suppressed by the addition of catalase, indicating that it was actually mediated by H2O2. Hydrogen Peroxide 120-124 catalase Rattus norvegicus 66-74 3169246-1 1988 Methanol and butanol were employed as selective substrates for catalase-H2O2 and alcohol dehydrogenase (ADH), respectively, in the perfused rat liver. Hydrogen Peroxide 72-76 catalase Rattus norvegicus 63-71 3169246-5 1988 These data demonstrate that catalase-H2O2 is the predominant pathway of alcohol oxidation in the fasted state in the presence of fatty acids. Hydrogen Peroxide 37-41 catalase Rattus norvegicus 28-36 3127425-4 1988 Third, myocardial H2O2-dependent inactivation of catalase occurred after reperfusion following ischemia, but not after ischemia without reperfusion or perfusion without ischemia. Hydrogen Peroxide 18-22 catalase Rattus norvegicus 49-57 3416882-11 1988 H2O2 generation was determined from the time necessary for steady-state level of catalase-H2O2, measured spectrophotometrically (660-640 nm) through a lobe of the liver, to return to basal values after the addition of a known quantity of methanol, which is not metabolized by ADH in the rat. Hydrogen Peroxide 0-4 catalase Rattus norvegicus 81-89 3416882-11 1988 H2O2 generation was determined from the time necessary for steady-state level of catalase-H2O2, measured spectrophotometrically (660-640 nm) through a lobe of the liver, to return to basal values after the addition of a known quantity of methanol, which is not metabolized by ADH in the rat. Hydrogen Peroxide 90-94 catalase Rattus norvegicus 81-89 2833658-5 1988 To demonstrate that oxygen metabolites were responsible for the toxicity, we assessed the protective effects of catalase and superoxide dismutase, scavengers of hydrogen peroxide and the superoxide anion, respectively. Hydrogen Peroxide 161-178 catalase Rattus norvegicus 112-120 3661692-11 1987 The gentamicin-induced change in fluorescence was completely inhibited by catalase (but not by heat-inactivated catalase), indicating that the decrease in fluorescence was due to hydrogen peroxide. Hydrogen Peroxide 179-196 catalase Rattus norvegicus 74-82 2821829-3 1987 We found that addition of glucose oxidase (GO) or H2O2 to isolated perfused rat kidneys caused injury that was manifested by decreases in glomerular filtration rate, perfusion flow rate, and sodium reabsorption and that was prevented by addition of catalase (CAT) (but not inactivated CAT) or large doses of DMTU (15 mM), but not urea (15 mM). Hydrogen Peroxide 50-54 catalase Rattus norvegicus 285-288 3190361-3 1988 Catalase and glutathione peroxidase are the two enzymes that protect against oxidative damage by hydrogen peroxide. Hydrogen Peroxide 97-114 catalase Rattus norvegicus 0-8 3061793-3 1988 Antioxidant enzymes, superoxide dismutase, catalase, and glutathione peroxidase are responsible for the detoxification of partially reduced oxygen species, superoxide and hydrogen peroxide, to less reactive states. Hydrogen Peroxide 171-188 catalase Rattus norvegicus 43-51 2821829-3 1987 We found that addition of glucose oxidase (GO) or H2O2 to isolated perfused rat kidneys caused injury that was manifested by decreases in glomerular filtration rate, perfusion flow rate, and sodium reabsorption and that was prevented by addition of catalase (CAT) (but not inactivated CAT) or large doses of DMTU (15 mM), but not urea (15 mM). Hydrogen Peroxide 50-54 catalase Rattus norvegicus 249-257 2821829-3 1987 We found that addition of glucose oxidase (GO) or H2O2 to isolated perfused rat kidneys caused injury that was manifested by decreases in glomerular filtration rate, perfusion flow rate, and sodium reabsorption and that was prevented by addition of catalase (CAT) (but not inactivated CAT) or large doses of DMTU (15 mM), but not urea (15 mM). Hydrogen Peroxide 50-54 catalase Rattus norvegicus 259-262 3040661-11 1987 Catalase liposome-treated cells also exhibited an enhanced ability to scavenge enzymatically generated H2O2 from the culture medium. Hydrogen Peroxide 103-107 catalase Rattus norvegicus 0-8 2887206-13 1987 Therefore, catalase may protect thiolase and its substrate, 3-ketoacyl-CoA, by removing H2O2, which is abundantly produced during peroxisomal enzyme reactions. Hydrogen Peroxide 88-92 catalase Rattus norvegicus 11-19 3500016-6 1987 These findings thus suggest that catalase, along with other antioxidant enzymes, may offer protection against the damaging effects of hydrogen peroxide. Hydrogen Peroxide 134-151 catalase Rattus norvegicus 33-41 3111274-6 1987 Catalase (an enzyme that reduces hydrogen peroxide) diminished xanthine-xanthine oxidase-induced 51Cr release in a dose-dependent manner. Hydrogen Peroxide 33-50 catalase Rattus norvegicus 0-8 3624137-1 1987 Hyperoxia and hyperbaric hyperoxia increased the rate of cerebral hydrogen peroxide (H2O2) production in unanesthetized rats in vivo, as measured by the H2O2-mediated inactivation of endogenous catalase activity following injection of 3-amino-1,2,4-triazole. Hydrogen Peroxide 66-83 catalase Rattus norvegicus 194-202 3624137-1 1987 Hyperoxia and hyperbaric hyperoxia increased the rate of cerebral hydrogen peroxide (H2O2) production in unanesthetized rats in vivo, as measured by the H2O2-mediated inactivation of endogenous catalase activity following injection of 3-amino-1,2,4-triazole. Hydrogen Peroxide 85-89 catalase Rattus norvegicus 194-202 3647757-7 1987 Vanadate-dependent oxidation of either pyridine nucleotide was inhibited by the addition of either superoxide dismutase or catalase, indicating that both superoxide and hydrogen peroxide may be intermediates in the process. Hydrogen Peroxide 169-186 catalase Rattus norvegicus 123-131 3624137-1 1987 Hyperoxia and hyperbaric hyperoxia increased the rate of cerebral hydrogen peroxide (H2O2) production in unanesthetized rats in vivo, as measured by the H2O2-mediated inactivation of endogenous catalase activity following injection of 3-amino-1,2,4-triazole. Hydrogen Peroxide 153-157 catalase Rattus norvegicus 194-202 3624137-2 1987 Brain catalase activity in rats breathing air (0.2 ATA O2) decreased to 75, 61, and 40% of controls due to endogenous H2O2 production at 30, 60, and 120 min, respectively, after intraperitoneal injection of 3-amino-1,2,4-triazole. Hydrogen Peroxide 118-122 catalase Rattus norvegicus 6-14 2435174-6 1987 In contrast, the glomerular response to supernatants obtained from neutrophils stimulated in the presence of catalase, a scavenger of hydrogen peroxide, or in the presence of methionine or taurine, scavengers of hypochlorous acid, was significantly reduced (P less than 0.001). Hydrogen Peroxide 134-151 catalase Rattus norvegicus 109-117 3105332-6 1987 This effect was reversed by addition of catalase to the ROS generating system but not by superoxide dismutase or mannitol, which suggested that H2O2 was the responsible metabolite. Hydrogen Peroxide 144-148 catalase Rattus norvegicus 40-48 3580135-1 1987 Fatty acids generate H2O2 via peroxisomal beta-oxidation and increase ethanol metabolism markedly in a system that involves catalase-H2O2. Hydrogen Peroxide 21-25 catalase Rattus norvegicus 124-132 3580135-1 1987 Fatty acids generate H2O2 via peroxisomal beta-oxidation and increase ethanol metabolism markedly in a system that involves catalase-H2O2. Hydrogen Peroxide 133-137 catalase Rattus norvegicus 124-132 3580135-3 1987 A new method was developed to measure rates of H2O2 generation based on the fact that methanol is oxidized only by catalase in rat liver. Hydrogen Peroxide 47-51 catalase Rattus norvegicus 115-123 3580135-4 1987 Rates of H2O2 generation were estimated from the time necessary for the steady-state level of catalase-H2O2 measured spectrophotometrically (660-640 nm) through a lobe of the liver to return to basal values following the addition of a known quantity of methanol in a closed perfusion system containing 4% bovine serum albumin. Hydrogen Peroxide 9-13 catalase Rattus norvegicus 94-102 3580135-4 1987 Rates of H2O2 generation were estimated from the time necessary for the steady-state level of catalase-H2O2 measured spectrophotometrically (660-640 nm) through a lobe of the liver to return to basal values following the addition of a known quantity of methanol in a closed perfusion system containing 4% bovine serum albumin. Hydrogen Peroxide 103-107 catalase Rattus norvegicus 94-102 3580135-9 1987 It is concluded, therefore, that rates of H2O2 generation are sufficient to account for rates of fatty acid-stimulated ethanol metabolism via catalase-H2O2. Hydrogen Peroxide 42-46 catalase Rattus norvegicus 142-150 3580135-9 1987 It is concluded, therefore, that rates of H2O2 generation are sufficient to account for rates of fatty acid-stimulated ethanol metabolism via catalase-H2O2. Hydrogen Peroxide 151-155 catalase Rattus norvegicus 142-150 3575330-3 1987 Catalase and GPx levels showed different trends; in particular, GPx, which appears to play a key role in detoxification of hydrogen peroxide, after an initial fall increases steadily with age. Hydrogen Peroxide 123-140 catalase Rattus norvegicus 0-8 2833323-7 1987 These data suggest that catalase, hydroxyl radical scavengers, and iron chelators protect chemotactically stimulated neutrophils from autotoxicity caused by neutrophil-derived hydrogen peroxide and its iron-catalyzed conversion product, hydroxyl radical. Hydrogen Peroxide 176-193 catalase Rattus norvegicus 24-32 3758300-4 1986 H2O2 intake decreased activity of catalase in rat skeletal muscle. Hydrogen Peroxide 0-4 catalase Rattus norvegicus 34-42 3508430-3 1987 Addition of superoxide dismutase or catalase clearly suppressed the ethanol-induced release of GPT and SDH, suggesting that .O2- and H2O2 are involved in this process. Hydrogen Peroxide 133-137 catalase Rattus norvegicus 36-44 3769136-3 1986 Activities of enzymes responsible for the production [peroxisomal palmitoyl CoA oxidase (PCO)] and degradation [catalase (Cat) and glutathione peroxidase (GSHPx)] of H2O2 were assayed in liver homogenates prepared from treated animals. Hydrogen Peroxide 166-170 catalase Rattus norvegicus 112-120 3769136-6 1986 A kinetic treatment of the rates of formation of hydrogen peroxide by PCO, and of degradation of hydrogen peroxide by catalase was used to estimate steady-state hydrogen peroxide concentrations ([H2O2]) during peroxisomal oxidation of palmitoyl CoA. Hydrogen Peroxide 97-114 catalase Rattus norvegicus 118-126 3769136-6 1986 A kinetic treatment of the rates of formation of hydrogen peroxide by PCO, and of degradation of hydrogen peroxide by catalase was used to estimate steady-state hydrogen peroxide concentrations ([H2O2]) during peroxisomal oxidation of palmitoyl CoA. Hydrogen Peroxide 97-114 catalase Rattus norvegicus 118-126 3769136-6 1986 A kinetic treatment of the rates of formation of hydrogen peroxide by PCO, and of degradation of hydrogen peroxide by catalase was used to estimate steady-state hydrogen peroxide concentrations ([H2O2]) during peroxisomal oxidation of palmitoyl CoA. Hydrogen Peroxide 196-200 catalase Rattus norvegicus 118-126 4049433-3 1985 Toxicity from modes of O3 exposure favoring stable free radicals (stationary cultures or added O3-exposed medium) was prevented by the H2O2 scavenger, catalase. Hydrogen Peroxide 135-139 catalase Rattus norvegicus 151-159 3720947-0 1986 Role of catalase in metabolism of hydrogen peroxide by the perfused rat heart. Hydrogen Peroxide 34-51 catalase Rattus norvegicus 8-16 3720947-4 1986 The results show that catalase, although present at low levels of activity in the heart compared to other organs, functions as a major route for detoxication of H2O2 in the myocardium. Hydrogen Peroxide 161-165 catalase Rattus norvegicus 22-30 3489212-4 1986 This protective effect of catalase indicates that hydrogen peroxide (H2O2) and/or conversion products of H2O2 (e.g., hydroxyl radical, hypochlorous acid) may play an important role in the development of experimental phacoanaphylactic endophthalmitis. Hydrogen Peroxide 50-67 catalase Rattus norvegicus 26-34 3489212-4 1986 This protective effect of catalase indicates that hydrogen peroxide (H2O2) and/or conversion products of H2O2 (e.g., hydroxyl radical, hypochlorous acid) may play an important role in the development of experimental phacoanaphylactic endophthalmitis. Hydrogen Peroxide 69-73 catalase Rattus norvegicus 26-34 3489212-4 1986 This protective effect of catalase indicates that hydrogen peroxide (H2O2) and/or conversion products of H2O2 (e.g., hydroxyl radical, hypochlorous acid) may play an important role in the development of experimental phacoanaphylactic endophthalmitis. Hydrogen Peroxide 105-109 catalase Rattus norvegicus 26-34 2865135-10 1985 Catalase, a hydrogen peroxide (H2O2) scavenger, almost completely prevented inactivation of the enzyme by AsA plus Cu2+. Hydrogen Peroxide 31-35 catalase Rattus norvegicus 0-8 2865135-10 1985 Catalase, a hydrogen peroxide (H2O2) scavenger, almost completely prevented inactivation of the enzyme by AsA plus Cu2+. Hydrogen Peroxide 12-29 catalase Rattus norvegicus 0-8 3965466-9 1985 Catalase added with menadione did not prevent the cell killing at 1 h but did prevent it at 3 h. These data indicate that catalase and the GSH-GSSG cycle are active in the defense of hepatocytes against the toxicity of H2O2. Hydrogen Peroxide 219-223 catalase Rattus norvegicus 0-8 3965466-9 1985 Catalase added with menadione did not prevent the cell killing at 1 h but did prevent it at 3 h. These data indicate that catalase and the GSH-GSSG cycle are active in the defense of hepatocytes against the toxicity of H2O2. Hydrogen Peroxide 219-223 catalase Rattus norvegicus 122-130 6502267-1 1984 In cells the level of potentially toxic superoxide radical (O2-) is controlled by superoxide dismutase (SOD); the level of hydrogen peroxide (H2O2), also potentially toxic, is controlled by catalase and glutathione peroxidase. Hydrogen Peroxide 123-140 catalase Rattus norvegicus 190-198 6502267-1 1984 In cells the level of potentially toxic superoxide radical (O2-) is controlled by superoxide dismutase (SOD); the level of hydrogen peroxide (H2O2), also potentially toxic, is controlled by catalase and glutathione peroxidase. Hydrogen Peroxide 142-146 catalase Rattus norvegicus 190-198 6233906-1 1984 Previously it was shown that tissue injury occurring in acute immune-complex-induced vasculitis, which is complement and neutrophil-dependent, is significantly attenuated by the presence of catalase, suggesting the pathogenic role of H2O2 generated from activated neutrophils. Hydrogen Peroxide 234-238 catalase Rattus norvegicus 190-198 6331321-7 1984 Catalase inhibited potently the oxidation of scavengers under all conditions, suggesting that H2O2 was the precursor of the hydroxyl radical in these systems. Hydrogen Peroxide 94-98 catalase Rattus norvegicus 0-8 6511542-1 1984 Enzymes specific for O-2 and H2O2 metabolism [superoxide dismutase (SOD) and catalase] can be delivered to the rat brain following entrapment in liposomes and intravenous injection and will protect against hyperbaric O2-induced convulsions in rats. Hydrogen Peroxide 29-33 catalase Rattus norvegicus 77-85 6280725-3 1982 Inhibition of H2O2 production should therefore decrease methanol oxidation by either a hydroxyl radical-dependent pathway or a catalase-dependent pathway. Hydrogen Peroxide 14-18 catalase Rattus norvegicus 127-135 6427146-6 1984 Pretreatment with catalase, a specific scavenger of hydrogen peroxide, preserved pulmonary vasoreactivity, inhibited the increase of the concentration of the measured prostaglandins, and prevented edema formation. Hydrogen Peroxide 52-69 catalase Rattus norvegicus 18-26 6882798-5 1983 Catalase (20 U/ml) abolished the stimulatory effect of H2O2, but did not affect diamide- or vitamin K-5-stimulated transport. Hydrogen Peroxide 55-59 catalase Rattus norvegicus 0-8 6280725-11 1982 The stimulation by iron-EDTA was blocked by the competing hydroxyl radical scavengers even in the absence of azide, suggesting that the added iron-EDTA favorably with microsomal catalase for H2O2 to produce hydroxyl radicals (or a species with the oxidizing power of the hydroxyl radical). Hydrogen Peroxide 191-195 catalase Rattus norvegicus 178-186 6696441-9 1984 The cell killing between 1 and 3 h in the presence of DPPD was prevented by catalase indicating its dependence upon continued generation of H2O2. Hydrogen Peroxide 140-144 catalase Rattus norvegicus 76-84 6667273-5 1983 These results suggest that hydrogen peroxide, the substrate for catalase produced by several flavoprotein oxidases, induces catalase in mammals as has been indicated for certain bacteria. Hydrogen Peroxide 27-44 catalase Rattus norvegicus 64-72 6667273-5 1983 These results suggest that hydrogen peroxide, the substrate for catalase produced by several flavoprotein oxidases, induces catalase in mammals as has been indicated for certain bacteria. Hydrogen Peroxide 27-44 catalase Rattus norvegicus 124-132 6196337-4 1983 The reaction was inhibited by pCMB (surface sulfhydryl group specific reagent), by heating, by anaerobic incubation and by catalase (H2O2 scavenger), but it was not inhibited by KCN or NaN3. Hydrogen Peroxide 133-137 catalase Rattus norvegicus 123-131 7150345-17 1982 3-Amino-1,2,4-triazole (50 mM), which irreversibly decomposes the peroxidatic compound II of the catalase: H2O2 complex, inhibited formate oxidation to a greater extent in the hormone-treated cells than in the control cells, whereas sodium azide, an inhibitor of the hemoprotein, catalase, completely inhibited it. Hydrogen Peroxide 107-111 catalase Rattus norvegicus 97-105 7150345-17 1982 3-Amino-1,2,4-triazole (50 mM), which irreversibly decomposes the peroxidatic compound II of the catalase: H2O2 complex, inhibited formate oxidation to a greater extent in the hormone-treated cells than in the control cells, whereas sodium azide, an inhibitor of the hemoprotein, catalase, completely inhibited it. Hydrogen Peroxide 107-111 catalase Rattus norvegicus 280-288 7288441-5 1981 Indeed, when heat-denatured microsomes were employed, incubation with H2O2 and the iron complex led to formation of lipid hydroperoxides; however, no production of MDA was observed, unless exogenous catalase was added together with H2O2 and hematin to the reaction mixture. Hydrogen Peroxide 70-74 catalase Rattus norvegicus 199-207 7262815-5 1981 Since the enzyme activity is markedly stimulated by phosphatidyl choline or catalase in the enzyme system obtained by DEAE-cellulose chromatography, it is presumed that the enzyme activity is markedly reduced because of removing the H2O2-scavenging system as well as the lipids, which are necessary to activate or stabilize the enzyme, from the microsomal enzyme system. Hydrogen Peroxide 233-237 catalase Rattus norvegicus 76-84 7288441-8 1981 Catalase is necessary to remove H2O2, which, after starting the peroxidation process, blocks the decomposition of lipid hydroperoxides, apparently by binding to the iron complex. Hydrogen Peroxide 32-36 catalase Rattus norvegicus 0-8 7300122-5 1981 This effect was inhibited by catalase, slightly stimulated by superoxide dismutase, unaffected by hydroxyl radical scavengers, thus suggesting that hydrogen peroxide was the by-product responsible. Hydrogen Peroxide 148-165 catalase Rattus norvegicus 29-37 7463055-6 1981 Catalase may function as one of the systems detoxifying H2O2 formed in CNS amine metabolism. Hydrogen Peroxide 56-60 catalase Rattus norvegicus 0-8 7004234-3 1980 The method is based on an H2O2-dependent inhibition of brain catalase in vivo by 3-amino-1,2,4-triazole and its prevention by ethanol. Hydrogen Peroxide 26-30 catalase Rattus norvegicus 61-69 7439185-7 1980 The major site for metabolic branching of H2O2 via different routes was found to be the mitochondrial catalase. Hydrogen Peroxide 42-46 catalase Rattus norvegicus 102-110 7439185-13 1980 Catalase was shown to protect rat-heart mitochondria from upsetting redox states of GSH and pyridine nucleotides following H2O2 decomposition by GSH peroxidase. Hydrogen Peroxide 123-127 catalase Rattus norvegicus 0-8 7429608-6 1980 Negative results obtained with scavengers of hydroxyl radicals and singlet molecular oxygen suggest that protection of superoxide dismutase by catalase from inactivation by hydrogen peroxide, is a likely explanation for the observed potentiation. Hydrogen Peroxide 173-190 catalase Rattus norvegicus 143-151 7004234-4 1980 The irreversible inhibition of catalase by aminotriazole is known to proceed via the reaction of (catalase-H2O2) compound I with aminotriazole. Hydrogen Peroxide 107-111 catalase Rattus norvegicus 31-39 7004234-4 1980 The irreversible inhibition of catalase by aminotriazole is known to proceed via the reaction of (catalase-H2O2) compound I with aminotriazole. Hydrogen Peroxide 107-111 catalase Rattus norvegicus 98-106 552903-6 1979 (3) H2O2 was shown to be the only relevant oxygen derivative in the production of cell damage: catalase was the only externally added agent that protected sensitive cells, and H2O2 (congruent to 10(-3) M) had the same effects as the photochemical treatment. Hydrogen Peroxide 4-8 catalase Rattus norvegicus 95-103 513850-6 1979 Both the relatively high and unchanged levels of reduced glutathione and kinetic considerations suggest that glutathione peroxidase is preferentially involved in lipid peroxide metabolism, while catalase predominantly metabolizes mitochondrial H2O2. Hydrogen Peroxide 244-248 catalase Rattus norvegicus 195-203 7394859-3 1980 The reaction was inhibited by catalase and also occurred with lactoperoxidase in the presence of H2O2 but 2-hydroxyestradiol was not detected in any of these experiments. Hydrogen Peroxide 97-101 catalase Rattus norvegicus 30-38 368807-1 1978 The intracellular site of synthesis of two peroxisomal enzymes of rat liver, uricase (urate:oxygen oxidoreductase, EC 1.7.3.3) and catalase (hydrogen peroxide:hydrogen peroxide oxidoreductase, EC 1.11.1.6), has been localized on free ribosomes and not membrane-bound ribosomes. Hydrogen Peroxide 141-158 catalase Rattus norvegicus 131-139 361418-5 1978 Addition of catalase suppresses 65% of the CL, suggesting that H2O2 generation may be its major source. Hydrogen Peroxide 63-67 catalase Rattus norvegicus 12-20 333049-4 1977 Experiments with catalase, superoxide dismutase, and methional showed that H(2)O(2) was the primary extracellular source of oxidant stress. Hydrogen Peroxide 75-83 catalase Rattus norvegicus 17-25 590442-1 1977 In rats receiving a dilute aqueous solution of hydrogen peroxide for a prolonged period, the activity of the peroxide metabolising enzymes, i.e. superoxide dismutase, peroxidase and catalase, is significantly increased in most tissues. Hydrogen Peroxide 47-64 catalase Rattus norvegicus 182-190 22327-3 1977 The mean value of 2.52 obtained for rat liver catalase at 37 degrees C and pH 6.3-7.7 was independent of both ethanol concentration and the rate of H2O2 generation over a wide range. Hydrogen Peroxide 148-152 catalase Rattus norvegicus 46-54 240743-4 1975 Direct read-out techniques for pyridine nucleotides, the catalase-H2O2 complex, and cytochrome P-450 were utilized to evaluate the specificity of inhibitors of alcohol dehydrogenase (4-methylpyrazole; 4 mM) and catalase (aminotriazole; 1.0 g/kg) qualitatively in perfused rat livers. Hydrogen Peroxide 66-70 catalase Rattus norvegicus 57-65 17386-7 1977 Spectrophotometric analysis of the steady-state concentration of the catalase-H2O2 intermediate with simultaneous measurement of the rate of release of GSSG leads to the conclusion that intracellular compartmentation of catalase in the peroxisomes and glutathione peroxidase in the cytosol and mitochondria distinguishes the reactivities of these enzymes one from the other, and facilitates their effective cooperation in hydroperoxide metabolism in the liver. Hydrogen Peroxide 78-82 catalase Rattus norvegicus 69-77 17386-7 1977 Spectrophotometric analysis of the steady-state concentration of the catalase-H2O2 intermediate with simultaneous measurement of the rate of release of GSSG leads to the conclusion that intracellular compartmentation of catalase in the peroxisomes and glutathione peroxidase in the cytosol and mitochondria distinguishes the reactivities of these enzymes one from the other, and facilitates their effective cooperation in hydroperoxide metabolism in the liver. Hydrogen Peroxide 78-82 catalase Rattus norvegicus 220-228 17386-7 1977 Spectrophotometric analysis of the steady-state concentration of the catalase-H2O2 intermediate with simultaneous measurement of the rate of release of GSSG leads to the conclusion that intracellular compartmentation of catalase in the peroxisomes and glutathione peroxidase in the cytosol and mitochondria distinguishes the reactivities of these enzymes one from the other, and facilitates their effective cooperation in hydroperoxide metabolism in the liver. Hydrogen Peroxide 422-435 catalase Rattus norvegicus 220-228 1009100-3 1976 Catalase functions to protect the enzyme from inactivation by H2O2 in addition to its documented ability to retard the noenzymatic oxidation of the pterin cofactor. Hydrogen Peroxide 62-66 catalase Rattus norvegicus 0-8 1009100-4 1976 The protective effect of catalase on alkylglycerol monooxygenase and on the aromatic amino acid hydroxylase systems indicates that H2O2 sensitivity is a general feature of pterin-dependent hydroxylases. Hydrogen Peroxide 131-135 catalase Rattus norvegicus 25-33 4418-7 1976 The optimal concentration of H2O2 for lacrimal gland peroxidase is at 10(-3)M and for peroxidatic activity of catalase at 10(-1)M. These optimal conditions obtained biochemically were applied to tissue sections of rat lacrimal gland. Hydrogen Peroxide 29-33 catalase Rattus norvegicus 110-118 240743-11 1975 The data indicate that alcohol dehydrogenase and catalase-H2O2 are responsible for hepatic ethanol oxidation. Hydrogen Peroxide 58-62 catalase Rattus norvegicus 49-57 240743-12 1975 At low ethanol concentrations (less than 20 mM), alcohol dehydrogenase is predominant; however, at higher ethanol concentrations (up to 80 mM), the contribution of catalase-H2O2 to overall ethanol utilization is significant. Hydrogen Peroxide 173-177 catalase Rattus norvegicus 164-172 1096557-7 1975 Quantitative assessments indicate that the predominant ethanol oxidase at low ethanol concentrations (less than 20 mM) is a alcohol dehydrogenase; however, at higher ethanol concentrations, a significant portion of total ethanol metabolism (up to 50%) is mediated by catalase-hydrogen peroxide complex. Hydrogen Peroxide 276-293 catalase Rattus norvegicus 267-275 240827-4 1975 The activity of the microsomal alcohol-oxidizing system could be dissociated from the alcohol peroxidation via catalase-H2O2 by differences in substrate specificity, since higher aliphatic alcohols react only with the microsomal system, but not with catalase-H2O2. Hydrogen Peroxide 120-124 catalase Rattus norvegicus 111-119 240827-4 1975 The activity of the microsomal alcohol-oxidizing system could be dissociated from the alcohol peroxidation via catalase-H2O2 by differences in substrate specificity, since higher aliphatic alcohols react only with the microsomal system, but not with catalase-H2O2. Hydrogen Peroxide 259-263 catalase Rattus norvegicus 111-119 1096557-9 1975 Considerable evidence implicates catalase-hydrogen peroxide complex in the mechanism of NADPH-dependent microsomal ethanol oxidation. Hydrogen Peroxide 42-59 catalase Rattus norvegicus 33-41 1224006-2 1975 Hydrogen peroxide is formed during this process, and the amount formed can be calculated from the amount of oxygen produced upon the addition of catalase. Hydrogen Peroxide 0-17 catalase Rattus norvegicus 145-153 167718-4 1975 When H2O2 production was stimulated by urate infusion, almost all of the H2O2 produced by the uricase reaction was decomposed by the catalase reaction. Hydrogen Peroxide 5-9 catalase Rattus norvegicus 133-141 167718-4 1975 When H2O2 production was stimulated by urate infusion, almost all of the H2O2 produced by the uricase reaction was decomposed by the catalase reaction. Hydrogen Peroxide 73-77 catalase Rattus norvegicus 133-141 14374012-0 1955 [Liver catalase-hydrogen peroxide system in DAB-fed rats]. Hydrogen Peroxide 16-33 catalase Rattus norvegicus 7-15 4854920-13 1974 Catalase or peroxidase enhanced enzymic activity fivefold; it is postulated that catalase (or other peroxidase) plays a part in the hydroxylation reaction independent of the protection by catalase of enzyme and cofactor from inactivation by a hydroperoxide. Hydrogen Peroxide 243-256 catalase Rattus norvegicus 0-8 4854920-13 1974 Catalase or peroxidase enhanced enzymic activity fivefold; it is postulated that catalase (or other peroxidase) plays a part in the hydroxylation reaction independent of the protection by catalase of enzyme and cofactor from inactivation by a hydroperoxide. Hydrogen Peroxide 243-256 catalase Rattus norvegicus 81-89 5725575-0 1968 Hydrogen peroxide detoxication by glutathione peroxidase and catalase in rat liver homogenates. Hydrogen Peroxide 0-17 catalase Rattus norvegicus 61-69 32031418-9 2020 Testicular levels of hydrogen peroxide and lipid peroxidation were significantly elevated with a decline in superoxide dismutase, catalase, glutathione peroxidase activities, and total thiol levels. Hydrogen Peroxide 21-38 catalase Rattus norvegicus 130-138 33947399-9 2021 Meanwhile, in vitro, hypoxia promoted the imbalance of SOD2 and CAT in AECs, leading to increased ROS and hydrogen peroxide (H2O2) production in the AECs culture medium. Hydrogen Peroxide 106-123 catalase Rattus norvegicus 64-67 33497181-9 2021 Concentrations of 2.5 x 1010 to 80 x 1010 CAT-SiNPs/mL not only proved to be nontoxic in cell cultures using the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay but also conferred cell protection when cells were exposed to 1 mM hydrogen peroxide (H2O2). Hydrogen Peroxide 253-270 catalase Rattus norvegicus 42-45 33497181-9 2021 Concentrations of 2.5 x 1010 to 80 x 1010 CAT-SiNPs/mL not only proved to be nontoxic in cell cultures using the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay but also conferred cell protection when cells were exposed to 1 mM hydrogen peroxide (H2O2). Hydrogen Peroxide 272-276 catalase Rattus norvegicus 42-45 33497181-10 2021 Finally, the ability of CAT-SiNPs to release oxygen (O2) when exposed to H2O2 was demonstrated in vivo using a rat model. Hydrogen Peroxide 73-77 catalase Rattus norvegicus 24-27 33497181-11 2021 Following the direct injection of CAT-SiNPs in the left kidney, partial pressure of oxygen (pO2) increased by more than 30 mmHg compared to the contralateral control kidney during the systemic infusion of safe levels of H2O2. Hydrogen Peroxide 220-224 catalase Rattus norvegicus 34-37 32954801-7 2021 An elevation in intracellular ROS, MDA, SOD, GSH-Px, and CAT level was observed in H2O2-induced granulosa cells; however, this effect was abrogated by morroniside treatment. Hydrogen Peroxide 83-87 catalase Rattus norvegicus 57-60 33425208-4 2020 Here, we report that a Chinese familial AD pedigree with E22K mutation was associated with higher levels of serum hydrogen peroxide (H2O2) and lower activity of catalase (a H2O2 degrading enzyme) than controls. Hydrogen Peroxide 173-177 catalase Rattus norvegicus 161-169 33425208-5 2020 Further, we found that E22K binding with catalase caused more severe H2O2 accumulation in the brains of E22K-injected rats than Abeta-injected rats. Hydrogen Peroxide 69-73 catalase Rattus norvegicus 41-49 33144915-5 2020 Both catalase (43%) and acetylated cytochrome c (19%) significantly decreased oxygen consumption that had been stimulated by doxorubicin; furthermore, extracellular hydrogen peroxide production was increased from undetectable control levels to 1.30 +- 0.02 nmol/min/107 myocytes (n = 4, P < 0.01) in the presence of 400 muM doxorubicin. Hydrogen Peroxide 165-182 catalase Rattus norvegicus 5-13 32390429-2 2020 Catalase-based (CAT) biomimetic complexes are emerging as promising therapeutic candidates that are expected to act as neuroprotectants for ischemic stroke by decreasing the damaging effects from H2O2. Hydrogen Peroxide 196-200 catalase Rattus norvegicus 16-19 32617047-7 2020 The expression levels of catalase and SOD2 increased significantly after treatment with ginsenoside Mc1, resulting in a decrease in the production of H2O2-mediated reactive oxygen species. Hydrogen Peroxide 150-154 catalase Rattus norvegicus 25-33 30981876-9 2019 In conclusion, the H2O2 necessary to boost the catalase-dependent oxidation of ethanol appears to come from cytoplasm and peroxisomes, and is produced by the enzyme lactate oxidase. Hydrogen Peroxide 19-23 catalase Rattus norvegicus 47-55 32128102-7 2019 Catalase (CAT) activity was assayed by the rate of decomposition of hydrogen peroxide. Hydrogen Peroxide 68-85 catalase Rattus norvegicus 0-8 32128102-7 2019 Catalase (CAT) activity was assayed by the rate of decomposition of hydrogen peroxide. Hydrogen Peroxide 68-85 catalase Rattus norvegicus 10-13 30615921-14 2019 SMI could also restore the mRNA expression and activities of SOD, GSR, and CAT suppressed by H2O2. Hydrogen Peroxide 93-97 catalase Rattus norvegicus 75-78 30697276-13 2019 In normal and diabetic rat sperm incubated with H2O2, a further increase in MDA and further decreases in SOD, CAT and GPx were observed, and these were ameliorated by quercetin treatment. Hydrogen Peroxide 48-52 catalase Rattus norvegicus 110-113 29565166-6 2017 Superoxide dismutase activity was assayed by measuring the inhibition of adrenaline auto-oxidation, catalase by the decrease rate in hydrogen peroxide and glutathione peroxidase by monitoring the oxidation of nicotinamide adenine dinucleotide phosphate. Hydrogen Peroxide 133-150 catalase Rattus norvegicus 100-108 29716865-4 2018 After one week, the animals were sacrificed and the catalase activity was measured from liver homogenate by the decomposition of H2O2 and followed directly by the decrease in absorbance at 240 nm. Hydrogen Peroxide 129-133 catalase Rattus norvegicus 52-60 29878401-4 2018 Additionally, inhibition of BRD4 using small interfering RNA or JQ1 (a selective potent chemical inhibitor) led to repression of H2 O2 -induced oxidative stress, as revealed by a decrease in the reactive oxygen species production accompanied by a decreased malondialdehyde content, along with increased activities of antioxidant markers superoxide dismutase, catalase, and glutathione peroxidase on exposure of chondrocytes to H2 O2 . Hydrogen Peroxide 129-134 catalase Rattus norvegicus 359-367 29971448-8 2018 Results: Cellular injury and oxidant damage were induced after exposure to H2O2 in HCE cells and rat corneas, such as increases of cell death and production of ROS; upregulation of a ROS generation enzyme, NOX4; and downregulation of degradation factors of ROS, superoxide dismutase, catalase, and glutathione S-transferase P. Hydrogen Peroxide 75-79 catalase Rattus norvegicus 284-292 29692247-5 2018 Compounds 1, 6b, 3c and 6r displayed significant decrease in MDA, SOD and CAT enzyme levels in H2O2 treated rats. Hydrogen Peroxide 95-99 catalase Rattus norvegicus 74-77 28683591-7 2017 The in vitro study, performed on PC12 cells, indicated that betaOHB inhibited H2O2-induced ROS production, decreased NOX2 and NOX4 protein levels, and upregulated FOXO3a, MnSOD, and catalase levels in a dose-dependent manner, which was consistent with the in vivo results. Hydrogen Peroxide 78-82 catalase Rattus norvegicus 182-190 28946188-8 2017 The exposure of IEC-6 cells to 40muM H2O2 during 4h resulted in oxidative stress manifested by (i) over 70% cell mortality, (ii) over-activity of CAT (246%), (iii) decrease in GSH level (10.4nmol/mg), (iv) excess in MDA content (18.4nmol/mg), and (v) a trigger of JNK phosphorylation. Hydrogen Peroxide 37-41 catalase Rattus norvegicus 146-149 27804049-8 2017 Expression levels of Forkhead box protein O1 (FoxO-1), MnSOD, catalase, pAKT, and p-mTOR were significantly (p < 0.05) reduced in the H2O2 group (p < 0.05). Hydrogen Peroxide 137-141 catalase Rattus norvegicus 62-70 28527616-8 2017 It is concluded that the H2O2 needed for catalase activity is derived from the oxidation of (hypo)xanthine by xanthine oxidase and the oxidation of urate by uricase. Hydrogen Peroxide 25-29 catalase Rattus norvegicus 41-49 27817140-7 2017 The 20 microM of H2O2 treatment induced OS by elevating total ROS level, reduced catalase and Bcl-2 expression levels with overexpression of Bax and cytochrome c and induced DNA fragmentation in denuded eggs cultured in vitro. Hydrogen Peroxide 17-21 catalase Rattus norvegicus 81-89 24872430-4 2014 Catalase (CAT) mimic activity was measured based on the decomposition of hydrogen peroxide. Hydrogen Peroxide 73-90 catalase Rattus norvegicus 0-8 27740870-4 2016 We hypothesized that hydrogen peroxide (H2O2), a relatively stable form of ROS, acts as a sensor of neuronal glucose consumption and availability and that lowering brain H2O2 with the enzyme catalase would lead to systemic responses increasing blood glucose. Hydrogen Peroxide 21-38 catalase Rattus norvegicus 191-199 27740870-4 2016 We hypothesized that hydrogen peroxide (H2O2), a relatively stable form of ROS, acts as a sensor of neuronal glucose consumption and availability and that lowering brain H2O2 with the enzyme catalase would lead to systemic responses increasing blood glucose. Hydrogen Peroxide 40-44 catalase Rattus norvegicus 191-199 27740870-4 2016 We hypothesized that hydrogen peroxide (H2O2), a relatively stable form of ROS, acts as a sensor of neuronal glucose consumption and availability and that lowering brain H2O2 with the enzyme catalase would lead to systemic responses increasing blood glucose. Hydrogen Peroxide 170-174 catalase Rattus norvegicus 191-199 28163957-8 2017 However, hepatic catalase (CAT) activities were significantly higher in H2O2, geraniol, and geraniol+H2O2 groups than control group. Hydrogen Peroxide 72-76 catalase Rattus norvegicus 27-30 28163957-8 2017 However, hepatic catalase (CAT) activities were significantly higher in H2O2, geraniol, and geraniol+H2O2 groups than control group. Hydrogen Peroxide 101-105 catalase Rattus norvegicus 27-30 27317948-6 2016 Cytosolic overexpression of catalase, a hydrogen peroxide detoxifying enzyme, provided a significant protection against viability loss and hydrogen peroxide generation, while mitochondrial overexpression of catalase did not protect against HC toxicity. Hydrogen Peroxide 40-57 catalase Rattus norvegicus 28-36 27317948-6 2016 Cytosolic overexpression of catalase, a hydrogen peroxide detoxifying enzyme, provided a significant protection against viability loss and hydrogen peroxide generation, while mitochondrial overexpression of catalase did not protect against HC toxicity. Hydrogen Peroxide 139-156 catalase Rattus norvegicus 28-36 27320188-8 2016 This was reduced by catalase, and was enhanced when 1microM H2O2 was present in the bath. Hydrogen Peroxide 60-64 catalase Rattus norvegicus 20-28 26827645-6 2016 The resistance of neonates to H2O2 inhibition was associated with higher catalase and glutathione peroxidase activities in skeletal muscle. Hydrogen Peroxide 30-34 catalase Rattus norvegicus 73-81 26717921-10 2015 In conclusion, our results suggest Adv-CAT gene transfer counteracts H2O2-induced ischemia/reperfusion injury through preserving p-Akt/p-eNOS/NO pathway in the rat kidney. Hydrogen Peroxide 69-73 catalase Rattus norvegicus 39-42 25324461-6 2015 RESULTS: The contents of hydrogen peroxide (H2O2) and malondialdehyde (MDA) were significantly reduced by MECO and vitamin C, while there were significant enhancements of the activities of superoxide dismutase (SOD), glutathione peroxidase (GPX), catalase (CAT), as well as the content of reduced glutathione (GSH) in pre-treated rats compared to IR-treated rats. Hydrogen Peroxide 25-42 catalase Rattus norvegicus 247-255 25324461-6 2015 RESULTS: The contents of hydrogen peroxide (H2O2) and malondialdehyde (MDA) were significantly reduced by MECO and vitamin C, while there were significant enhancements of the activities of superoxide dismutase (SOD), glutathione peroxidase (GPX), catalase (CAT), as well as the content of reduced glutathione (GSH) in pre-treated rats compared to IR-treated rats. Hydrogen Peroxide 25-42 catalase Rattus norvegicus 257-260 25324461-6 2015 RESULTS: The contents of hydrogen peroxide (H2O2) and malondialdehyde (MDA) were significantly reduced by MECO and vitamin C, while there were significant enhancements of the activities of superoxide dismutase (SOD), glutathione peroxidase (GPX), catalase (CAT), as well as the content of reduced glutathione (GSH) in pre-treated rats compared to IR-treated rats. Hydrogen Peroxide 44-48 catalase Rattus norvegicus 247-255 25324461-6 2015 RESULTS: The contents of hydrogen peroxide (H2O2) and malondialdehyde (MDA) were significantly reduced by MECO and vitamin C, while there were significant enhancements of the activities of superoxide dismutase (SOD), glutathione peroxidase (GPX), catalase (CAT), as well as the content of reduced glutathione (GSH) in pre-treated rats compared to IR-treated rats. Hydrogen Peroxide 44-48 catalase Rattus norvegicus 257-260 26991551-8 2016 In the presence of H2 O2 , the SOD blocker NaCN and the catalase inhibitor 3-aminotriazole, both suppressed the protective effects of PACAP on SOD and catalase activities, mitochondrial function, and cell survival. Hydrogen Peroxide 19-24 catalase Rattus norvegicus 56-64 26991551-8 2016 In the presence of H2 O2 , the SOD blocker NaCN and the catalase inhibitor 3-aminotriazole, both suppressed the protective effects of PACAP on SOD and catalase activities, mitochondrial function, and cell survival. Hydrogen Peroxide 19-24 catalase Rattus norvegicus 151-159 26925769-6 2016 The activity levels of superoxide dismutase and catalase were decreased with an increase in the levels of lipid peroxidation and H2O2 generation in the testis and epididymis of cisplatin treated rats, suggesting the cisplatin-induced oxidative stress. Hydrogen Peroxide 129-133 catalase Rattus norvegicus 48-56 27095206-2 2016 Starting out from a catalase-dominated thinking in the middle of the last century, Sies first demonstrated, by whole organ spectroscopy, that H2O2 is generated in rat liver and metabolized by catalase. Hydrogen Peroxide 142-146 catalase Rattus norvegicus 20-28 27095206-2 2016 Starting out from a catalase-dominated thinking in the middle of the last century, Sies first demonstrated, by whole organ spectroscopy, that H2O2 is generated in rat liver and metabolized by catalase. Hydrogen Peroxide 142-146 catalase Rattus norvegicus 192-200 25676582-3 2015 Introduction of catalase at a concentration as low as 7.5 U/mL counteracted the cytotoxic effect of H2O2 and enhanced the viability and proliferation rate of fibroblasts. Hydrogen Peroxide 100-104 catalase Rattus norvegicus 16-24 25304210-4 2015 Pretreatment with catalase (CAT), a hydrogen peroxide-scavenging enzyme, attenuated rotenone-induced ROS and neuronal apoptosis, implying hydrogen peroxide (H2O2) involved, which was further verified by imaging intracellular H2O2 using a peroxide-selective probe H2DCFDA. Hydrogen Peroxide 36-53 catalase Rattus norvegicus 18-26 25304210-4 2015 Pretreatment with catalase (CAT), a hydrogen peroxide-scavenging enzyme, attenuated rotenone-induced ROS and neuronal apoptosis, implying hydrogen peroxide (H2O2) involved, which was further verified by imaging intracellular H2O2 using a peroxide-selective probe H2DCFDA. Hydrogen Peroxide 36-53 catalase Rattus norvegicus 28-31 25304210-4 2015 Pretreatment with catalase (CAT), a hydrogen peroxide-scavenging enzyme, attenuated rotenone-induced ROS and neuronal apoptosis, implying hydrogen peroxide (H2O2) involved, which was further verified by imaging intracellular H2O2 using a peroxide-selective probe H2DCFDA. Hydrogen Peroxide 138-155 catalase Rattus norvegicus 18-26 25304210-4 2015 Pretreatment with catalase (CAT), a hydrogen peroxide-scavenging enzyme, attenuated rotenone-induced ROS and neuronal apoptosis, implying hydrogen peroxide (H2O2) involved, which was further verified by imaging intracellular H2O2 using a peroxide-selective probe H2DCFDA. Hydrogen Peroxide 138-155 catalase Rattus norvegicus 28-31 25304210-4 2015 Pretreatment with catalase (CAT), a hydrogen peroxide-scavenging enzyme, attenuated rotenone-induced ROS and neuronal apoptosis, implying hydrogen peroxide (H2O2) involved, which was further verified by imaging intracellular H2O2 using a peroxide-selective probe H2DCFDA. Hydrogen Peroxide 157-161 catalase Rattus norvegicus 18-26 25304210-4 2015 Pretreatment with catalase (CAT), a hydrogen peroxide-scavenging enzyme, attenuated rotenone-induced ROS and neuronal apoptosis, implying hydrogen peroxide (H2O2) involved, which was further verified by imaging intracellular H2O2 using a peroxide-selective probe H2DCFDA. Hydrogen Peroxide 157-161 catalase Rattus norvegicus 28-31 25304210-4 2015 Pretreatment with catalase (CAT), a hydrogen peroxide-scavenging enzyme, attenuated rotenone-induced ROS and neuronal apoptosis, implying hydrogen peroxide (H2O2) involved, which was further verified by imaging intracellular H2O2 using a peroxide-selective probe H2DCFDA. Hydrogen Peroxide 225-229 catalase Rattus norvegicus 18-26 25304210-4 2015 Pretreatment with catalase (CAT), a hydrogen peroxide-scavenging enzyme, attenuated rotenone-induced ROS and neuronal apoptosis, implying hydrogen peroxide (H2O2) involved, which was further verified by imaging intracellular H2O2 using a peroxide-selective probe H2DCFDA. Hydrogen Peroxide 225-229 catalase Rattus norvegicus 28-31 24872430-4 2014 Catalase (CAT) mimic activity was measured based on the decomposition of hydrogen peroxide. Hydrogen Peroxide 73-90 catalase Rattus norvegicus 10-13 24388786-6 2014 Co-expression of SOD1 + CAT rescued the effects of SOD1 expression on learning, redox measures, and synaptic function suggesting the effects were mediated by excess hydrogen peroxide. Hydrogen Peroxide 165-182 catalase Rattus norvegicus 24-27 23632742-3 2013 In the study, the expression of CAT, GPx, SOD1, and SOD2 and their activities in rat cardiomyocytes in infrasound exposure groups were significantly decreased compared to those in the various time controls, along with significantly higher levels of O2 (-) and H2O2. Hydrogen Peroxide 260-264 catalase Rattus norvegicus 32-35 24699274-6 2014 The potentiating effect of H2O2 on the apneic responses to these VLCF stimulants was prevented by catalase (an enzyme that degrades H2O2) and by dimethylthiourea (a hydroxyl radical scavenger). Hydrogen Peroxide 27-31 catalase Rattus norvegicus 98-106 24699274-6 2014 The potentiating effect of H2O2 on the apneic responses to these VLCF stimulants was prevented by catalase (an enzyme that degrades H2O2) and by dimethylthiourea (a hydroxyl radical scavenger). Hydrogen Peroxide 132-136 catalase Rattus norvegicus 98-106 24669281-0 2014 Catalase influence in the regulation of coronary resistance by estrogen: joint action of nitric oxide and hydrogen peroxide. Hydrogen Peroxide 106-123 catalase Rattus norvegicus 0-8 24669281-6 2014 Taken together, our data suggest that, in the absence of estrogen influence and, therefore, reduced NO bioavailability, coronary resistance regulation seems to be more dependent on the H2O2 that is maintained at low levels by increased catalase activity. Hydrogen Peroxide 185-189 catalase Rattus norvegicus 236-244 23871839-13 2013 Inhibition of catalase or GPx significantly increased hydrogen peroxide-induced apoptosis, which was not reversed by GSH-MEE. Hydrogen Peroxide 54-71 catalase Rattus norvegicus 14-22 23181054-4 2012 We have recently shown that ODN is a potent protective agent that prevents hydrogen peroxide (H(2)O(2))-induced inhibition of SOD and catalase activities and stimulation of cell apoptosis in astrocytes. Hydrogen Peroxide 94-103 catalase Rattus norvegicus 134-142 23181054-4 2012 We have recently shown that ODN is a potent protective agent that prevents hydrogen peroxide (H(2)O(2))-induced inhibition of SOD and catalase activities and stimulation of cell apoptosis in astrocytes. Hydrogen Peroxide 75-92 catalase Rattus norvegicus 134-142 23987456-5 2013 Compared with the H2O2 group, the total-antioxidant capacity, activities of superoxide dismutase and catalase were enhanced by 65.81%, 41.34% and 59.05%, respectively. Hydrogen Peroxide 18-22 catalase Rattus norvegicus 101-109 23352507-4 2013 Upregulation of antioxidant enzymes such as manganese superoxide dismutase and catalase accompanied the protective effect of 5-AIQ on H2O2-induced cell death. Hydrogen Peroxide 134-138 catalase Rattus norvegicus 79-87 23096233-11 2013 The raised CAT activity perhaps contributes to the higher TAS and lower H2O2 levels in SHR. Hydrogen Peroxide 72-76 catalase Rattus norvegicus 11-14 22082827-6 2013 Activities of the antioxidant enzymes of erythrocytes such as superoxide dismutase, catalase, glutathione S-transferase and glutathione peroxidase increased significantly in a dose-dependent manner with significant elevation in hydrogen peroxide and malondialdehyde levels, whereas glutathione level was not significantly decreased in BLCO-treated animals. Hydrogen Peroxide 228-245 catalase Rattus norvegicus 84-92 23181054-7 2012 In addition, 0.1 nM ODN blocked H(2)O(2)-evoked reduction of both mRNA levels and activities of SOD and catalase. Hydrogen Peroxide 32-40 catalase Rattus norvegicus 104-112 22213368-7 2012 A similar impact on hepatic peroxidase activity has also been observed, indicating a partial detoxication of hydrogen peroxide by both catalase and peroxidase. Hydrogen Peroxide 109-126 catalase Rattus norvegicus 135-143 22817944-1 2012 Amperometric flow injection method of hydrogen peroxide analysis was developed based on catalase enzyme (CAT) immobilization on a glassy carbon electrode (GC) modified with electrochemically deposited gold nanoparticles on a multiwalled carbon nanotubes/chitosan film. Hydrogen Peroxide 38-55 catalase Rattus norvegicus 88-103 22817944-1 2012 Amperometric flow injection method of hydrogen peroxide analysis was developed based on catalase enzyme (CAT) immobilization on a glassy carbon electrode (GC) modified with electrochemically deposited gold nanoparticles on a multiwalled carbon nanotubes/chitosan film. Hydrogen Peroxide 38-55 catalase Rattus norvegicus 105-108 21402136-8 2011 CAT activity remained high, possibly as a compensatory mechanism to eliminate hydroperoxides during lead poisoning. Hydrogen Peroxide 78-92 catalase Rattus norvegicus 0-3 21618048-4 2011 Pretreatment of cells with 2-cyclopropylimino-3-methyl-1,3-thiazoline hydrochloride prior to H2O2 exposure attenuated the H2O2-induced reductions in cell survival and superoxide dismutase, catalase, glutathione, and glutathione peroxidase activities. Hydrogen Peroxide 122-126 catalase Rattus norvegicus 189-197 21276205-0 2011 Vascular endothelial growth factor protects post-ganglionic sympathetic neurones from the detrimental effects of hydrogen peroxide by increasing catalase. Hydrogen Peroxide 113-130 catalase Rattus norvegicus 145-153 21487676-6 2011 Expression of the H(2)O(2)-inactivating enzyme catalase in mitochondria protected against cytokine toxicity by preventing hydroxyl radical formation. Hydrogen Peroxide 18-26 catalase Rattus norvegicus 47-55 21714805-5 2012 DCF and MDA levels were significantly lower, while SOD, CAT and GSH were significantly higher in the sperm of rats supplemented with RPO in combination with hydroperoxide treatment when compared to those receiving hydroperoxide and no RPO supplementation (P < 0.05). Hydrogen Peroxide 157-170 catalase Rattus norvegicus 56-59 21599667-6 2011 H(2) O(2) -treated cells exhibited high level of ROS associated with a reduction of both superoxide dismutases (SOD) and catalase activities. Hydrogen Peroxide 0-9 catalase Rattus norvegicus 121-129 21599667-9 2011 ODN stimulated SOD and catalase activities in a concentration-dependent manner, and blocked H(2) O(2) -evoked inhibition of SOD and catalase activities. Hydrogen Peroxide 92-101 catalase Rattus norvegicus 132-140 19698781-3 2009 Therefore we investigated the toxicity of dexamethasone in RINm5F insulin-producing cells and its dependence on the expression level of the antioxidant enzyme catalase, which inactivates hydrogen peroxide. Hydrogen Peroxide 187-204 catalase Rattus norvegicus 159-167 21472897-6 2011 The activities of pancreatic superoxide dismutase and catalase were significantly decreased with a concomitant increase in the levels of H2O2 and lipid peroxidation. Hydrogen Peroxide 137-141 catalase Rattus norvegicus 54-62 20971967-8 2011 Overexpression of catalase in the peroxisomes and in the cytosol, but not in the mitochondria, significantly reduced H2O2 formation and protected the cells against palmitic acid-induced toxicity. Hydrogen Peroxide 117-121 catalase Rattus norvegicus 18-26 20109102-5 2010 6-OHDA could induce the elevation of Grp58 and CHOP in the presence of catalase, a hydrogen peroxide-removing enzyme, suggesting that the elevation of Grp58 and CHOP are induced by both hydrogen peroxide and p-quinone generated by 6-OHDA. Hydrogen Peroxide 83-100 catalase Rattus norvegicus 71-79 20109102-5 2010 6-OHDA could induce the elevation of Grp58 and CHOP in the presence of catalase, a hydrogen peroxide-removing enzyme, suggesting that the elevation of Grp58 and CHOP are induced by both hydrogen peroxide and p-quinone generated by 6-OHDA. Hydrogen Peroxide 186-203 catalase Rattus norvegicus 71-79 19954424-5 2010 Tiron [O2- (superoxide anion) scavenger, 1 mmol/l] and catalase (H2O2 scavenger, 300 units/ml) reduced ethanol-induced contraction to a similar extent in both endothelium-intact and denuded rings. Hydrogen Peroxide 65-69 catalase Rattus norvegicus 55-63 19698781-10 2009 Increased ROS scavenging capacity in insulin-producing cells, through overexpression of catalase, prevents a deleterious increase in hydrogen peroxide generation and thus prevents dexamethasone-induced apoptosis. Hydrogen Peroxide 133-150 catalase Rattus norvegicus 88-96 19786260-6 2009 Catalase, an antioxidative enzyme that can decompose hydrogen peroxide (H(2)O(2)), significantly attenuated the increase in [Ca(2+)](i) and completely inhibited hypercontracture. Hydrogen Peroxide 53-70 catalase Rattus norvegicus 0-8 19924083-6 2009 Significantly enhanced catalase activity that was observed in all groups compared to the control indicates that the primary reactive oxygen species (ROS) metabolite is hydrogen peroxide, which decomposes very rapidly (very high catalase activity), thus hindering formation of OH radicals as the most toxic ROS. Hydrogen Peroxide 168-185 catalase Rattus norvegicus 23-31 19924083-6 2009 Significantly enhanced catalase activity that was observed in all groups compared to the control indicates that the primary reactive oxygen species (ROS) metabolite is hydrogen peroxide, which decomposes very rapidly (very high catalase activity), thus hindering formation of OH radicals as the most toxic ROS. Hydrogen Peroxide 168-185 catalase Rattus norvegicus 228-236 19679169-2 2009 In this study, we measured the activities of two enzymes that catalyze the removal of hydrogen peroxide (H(2)O(2)), catalase and glutathione peroxidase (Gpx), in 3- and 24-month-old Fisher-344 rats, and reduced and oxidized glutathione in 3-, 12-, and 24-month-old rats. Hydrogen Peroxide 86-103 catalase Rattus norvegicus 116-124 19786260-6 2009 Catalase, an antioxidative enzyme that can decompose hydrogen peroxide (H(2)O(2)), significantly attenuated the increase in [Ca(2+)](i) and completely inhibited hypercontracture. Hydrogen Peroxide 72-80 catalase Rattus norvegicus 0-8 19366358-7 2009 The intracellular formation of the active catalase mimic thus renders TAA-1 an attractive compound for protection against iron- and/or hydrogen peroxide-dependent cell injuries. Hydrogen Peroxide 135-152 catalase Rattus norvegicus 42-50 19394330-6 2009 The blockade of EDHF produced by ascorbate in the presence of CuSO4 (0.5 microM) was abolished by the hydrogen peroxide scavenger, catalase, but unaffected by the scavengers of hydroxyl radical or superoxide anion, mannitol and superoxide dismutase (SOD), respectively. Hydrogen Peroxide 102-119 catalase Rattus norvegicus 131-139 17557920-7 2007 Tiron (a superoxide anion scavenger), catalase (an enzyme that degrades H(2)O(2)), and deferoxamine (a hydroxyl radical scavenger) augmented the L-NAME-induced contractions in arteries of mature SHR. Hydrogen Peroxide 72-80 catalase Rattus norvegicus 38-46 18955588-9 2009 The increased ROS levels were abolished by L-NAME or by catalase, which degrades extracellular hydrogen peroxide. Hydrogen Peroxide 95-112 catalase Rattus norvegicus 56-64 18499325-7 2008 Catalase, the H2O2-decomposing enzyme, can prevent the reduction in ATP level and protect hepatocytes from toosendanin-induced death. Hydrogen Peroxide 14-18 catalase Rattus norvegicus 0-8 19266051-5 2008 The CL responses were completely abolished in the presence of superoxide dismutase and catalase, suggesting the primary involvement of superoxide and hydrogen peroxide (H2O2). Hydrogen Peroxide 150-167 catalase Rattus norvegicus 87-95 19266051-5 2008 The CL responses were completely abolished in the presence of superoxide dismutase and catalase, suggesting the primary involvement of superoxide and hydrogen peroxide (H2O2). Hydrogen Peroxide 169-173 catalase Rattus norvegicus 87-95 17311075-4 2007 Compared to wild-type D39 pneumococci, the increase of rCBF was diminished in meningitis induced by the H(2)O(2) defective SpxB(-) mutant (maximum increase, 135% +/- 17% versus 217% +/- 23% of the individual baseline; P<0.01) or after treatment of D39-induced meningitis with H(2)O(2)-degrading catalase or with tetraethylammonium (TEA), a blocker of calcium-sensitive potassium channels, which mediate H(2)O(2)-induced vasodilation. Hydrogen Peroxide 104-112 catalase Rattus norvegicus 298-306 19188683-4 2009 Furthermore, we show that attenuating mitochondrial H(2)O(2) emission, either by treating rats with a mitochondrial-targeted antioxidant or by genetically engineering the overexpression of catalase in mitochondria of muscle in mice, completely preserves insulin sensitivity despite a high-fat diet. Hydrogen Peroxide 52-60 catalase Rattus norvegicus 189-197 19114648-8 2009 We conclude that O(2)(.-)- and H(2)O(2)-dependent feedforward impairment of mitochondrial ETC complexes because of predisposed downregulation of superoxide dismutase or catalase and a cross-talk between NADPH oxidase-derived O(2)(.-) and ETC enzymes contribute to chronic oxidative stress in the RVLM of spontaneously hypertensive rats, leading to augmented sympathetic vasomotor tone and hypertension. Hydrogen Peroxide 31-39 catalase Rattus norvegicus 169-177 19607981-2 2009 Superoxide anion is converted by superoxide dismutase into hydrogen peroxide (H2O2), and the latter is then transformed into the toxic hydroxyl radical, through the Haber-Weiss reaction, converted to water by glutathione peroxidase (GPx) or dismuted to water and oxygen through catalase. Hydrogen Peroxide 59-76 catalase Rattus norvegicus 278-286 19607981-2 2009 Superoxide anion is converted by superoxide dismutase into hydrogen peroxide (H2O2), and the latter is then transformed into the toxic hydroxyl radical, through the Haber-Weiss reaction, converted to water by glutathione peroxidase (GPx) or dismuted to water and oxygen through catalase. Hydrogen Peroxide 78-82 catalase Rattus norvegicus 278-286 19607981-10 2009 Thus, our findings demonstrate that MS is neuroprotective in both in vivo and in vitro ischemic conditions, through a mechanism which may involve increased endogenous levels of H2O2 and its consequent conversion to molecular oxygen by catalase. Hydrogen Peroxide 177-181 catalase Rattus norvegicus 235-243 18303121-5 2008 Catalase treatment, but not SOD, completely inhibited the increase in Hx/XO-stimulated 2-deoxyglucose (2-DG) uptake, suggesting that H2O2 is an intermediary leading to Hx/XO-stimulated glucose uptake with incubation. Hydrogen Peroxide 133-137 catalase Rattus norvegicus 0-8 18260005-5 2008 Catalase-sensitive 2",7"-dichlorofluorescein (DCF) fluorescence also was measured as an index of H2O2 formation, and arteriolar dilation to exogenous H2O2 was pharmacologically probed in each age group. Hydrogen Peroxide 97-101 catalase Rattus norvegicus 0-8 18260005-5 2008 Catalase-sensitive 2",7"-dichlorofluorescein (DCF) fluorescence also was measured as an index of H2O2 formation, and arteriolar dilation to exogenous H2O2 was pharmacologically probed in each age group. Hydrogen Peroxide 150-154 catalase Rattus norvegicus 0-8 17934963-4 2007 Catalase-sensitive 2",7"-dichlorofluorescein (DCF) fluorescence was measured as an index of H2O2 formation, and the mechanism of arteriolar dilation to H2O2 was probed in each group using pharmacological inhibitors. Hydrogen Peroxide 92-96 catalase Rattus norvegicus 0-8 17934963-4 2007 Catalase-sensitive 2",7"-dichlorofluorescein (DCF) fluorescence was measured as an index of H2O2 formation, and the mechanism of arteriolar dilation to H2O2 was probed in each group using pharmacological inhibitors. Hydrogen Peroxide 152-156 catalase Rattus norvegicus 0-8 17673185-7 2007 Acutely, both therapeutic and excessive vitamin A doses induced a 1.8- to 2.2-fold decrease of catalase (CAT) activity, as determined through the rate of decrease of hydrogen peroxide (H(2)O(2)). Hydrogen Peroxide 166-183 catalase Rattus norvegicus 95-103 17673185-7 2007 Acutely, both therapeutic and excessive vitamin A doses induced a 1.8- to 2.2-fold decrease of catalase (CAT) activity, as determined through the rate of decrease of hydrogen peroxide (H(2)O(2)). Hydrogen Peroxide 166-183 catalase Rattus norvegicus 105-108 17175150-4 2007 Following exposure of cells to H2O2 (150 microM), a marked decrease in cell survival and activities of superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GSH-Px), as well as increased levels of malondialdehyde (MDA) production and lactate dehydrogenase (LDH) release were observed. Hydrogen Peroxide 31-35 catalase Rattus norvegicus 131-139 17934344-9 2007 Our results suggest that, in preconditioned rats, while hydrogen peroxide is generated from severe ischemia, the activity of catalase and glutathione peroxidase-1 is correspondingly increased to eliminate the excessive hydrogen peroxide. Hydrogen Peroxide 219-236 catalase Rattus norvegicus 125-133 17576767-3 2007 In addition, the block of respiration by antimycin A added to RLM respiring in state 4 conditions, or the addition of H2O2, results in O2 generation, which is blocked by the catalase inhibitors aminotriazole or KCN. Hydrogen Peroxide 118-122 catalase Rattus norvegicus 174-182 17576767-7 2007 All these observations are compatible with the presence of endogenous heme-containing catalase with an activity of 825 +/- 15 units, which contributes to mitochondrial protection against endogenous or exogenous H2O2. Hydrogen Peroxide 211-215 catalase Rattus norvegicus 86-94 17175150-4 2007 Following exposure of cells to H2O2 (150 microM), a marked decrease in cell survival and activities of superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GSH-Px), as well as increased levels of malondialdehyde (MDA) production and lactate dehydrogenase (LDH) release were observed. Hydrogen Peroxide 31-35 catalase Rattus norvegicus 141-144 16361258-5 2006 Neurotoxicity is completely attenuated by preincubation with catalase, suggesting that hydrogen peroxide, at least in part, evokes neuronal cell death in this model. Hydrogen Peroxide 87-104 catalase Rattus norvegicus 61-69 17439411-14 2007 The increased CAT activity and unchanged Se-GSH-Px activity observed in kidney suggest that H2O2 may be primarily scavenged by CAT. Hydrogen Peroxide 92-96 catalase Rattus norvegicus 14-17 17439411-14 2007 The increased CAT activity and unchanged Se-GSH-Px activity observed in kidney suggest that H2O2 may be primarily scavenged by CAT. Hydrogen Peroxide 92-96 catalase Rattus norvegicus 127-130 17126611-5 2007 Superoxide dismutase (SOD; converts superoxide to H(2)O(2)) significantly reduced the contraction in both types of arteries -- an effect abolished by catalase (H(2)O(2) scavenger), suggesting that the SOD effect was mediated by H(2)O(2). Hydrogen Peroxide 50-58 catalase Rattus norvegicus 150-158 17685003-6 2007 On the contrary to the massive increase of the Palmitoyl CoA oxidase--a marker enzyme for peroxisomal proliferation, there was only a limited increase of catalase (which inactivates hydrogen peroxide) activity. Hydrogen Peroxide 182-199 catalase Rattus norvegicus 154-162 17198197-7 2007 Notably, excess catalase (100 microg/mL) in the buffer, although sufficient to remove homocysteine-derived H2O2, did not alleviate the detrimental effects of homocysteine. Hydrogen Peroxide 107-111 catalase Rattus norvegicus 16-24 16716903-2 2006 The present study assessed the hypothesis that O2*- or H2O2 levels augmented by the reduced molecular synthesis or enzyme activity of superoxide dismutase (SOD), catalase (CAT), or glutathione peroxidase (GPx) in the rostral ventrolateral medulla (RVLM), where sympathetic premotor neurons that generate tonic vasomotor tone are located, contribute to the pathogenesis of hypertension. Hydrogen Peroxide 55-59 catalase Rattus norvegicus 162-170 16716903-2 2006 The present study assessed the hypothesis that O2*- or H2O2 levels augmented by the reduced molecular synthesis or enzyme activity of superoxide dismutase (SOD), catalase (CAT), or glutathione peroxidase (GPx) in the rostral ventrolateral medulla (RVLM), where sympathetic premotor neurons that generate tonic vasomotor tone are located, contribute to the pathogenesis of hypertension. Hydrogen Peroxide 55-59 catalase Rattus norvegicus 172-175 16716903-4 2006 A causative relationship between these biochemical correlates of oxidative stress and neurogenic hypertension was established when gene transfer by microinjection of adenovirus encoding SOD1, SOD2, or CAT into the bilateral RVLM promoted a long-lasting reduction in arterial pressure in SHR, but not WKY rats, accompanied by an enhanced SOD1, SOD2, or CAT protein expression or enzyme activity and reduced O2*- or H2O2 level in the RVLM. Hydrogen Peroxide 414-418 catalase Rattus norvegicus 201-204 16716903-5 2006 These results together suggest that downregulation of gene expression and enzyme activity of the antioxidant SOD1, SOD2, or CAT may underlie the augmented levels of O2*- and H2O2 in the RVLM, leading to oxidative stress and hypertension in SHR. Hydrogen Peroxide 174-178 catalase Rattus norvegicus 124-127 16527547-12 2006 Exogenous H2O2 caused endothelium-independent relaxation that was slightly inhibited by iberiotoxin, ODQ or significantly reduced by elevated KCl, and abolished by catalase. Hydrogen Peroxide 10-14 catalase Rattus norvegicus 164-172 16403660-5 2006 However, the NO synthase activity is abolished by the addition of catalase, suggesting that H(2)O(2) is involved in NO synthesis in a posttranslation state. Hydrogen Peroxide 92-100 catalase Rattus norvegicus 66-74 16337160-9 2006 Moreover, forced overexpression of catalase inhibited H(2)O(2)-triggered apoptosis, as evidenced by annexin-V labeling. Hydrogen Peroxide 54-62 catalase Rattus norvegicus 35-43 16393992-3 2006 We found that basal proliferation of microglia was stimulated by proinflammatory cytokines IL-1beta or TNF-alpha, and this proliferation was completely inhibited by catalase, implicating hydrogen peroxide as a mediator of proliferation. Hydrogen Peroxide 187-204 catalase Rattus norvegicus 165-173 16311918-2 2005 The antioxidant enzyme catalase, a heme protein that degrades hydrogen peroxide, is found at high concentrations in peroxisomes. Hydrogen Peroxide 62-79 catalase Rattus norvegicus 23-31 16393992-6 2006 Low concentrations of PMA or arachidonic acid (known activators of NADPH oxidase) or xanthine/xanthine oxidase or glucose oxidase (generating hydrogen peroxide) also increased microglia proliferation and this was blocked by catalase, showing that NADPH oxidase activation or hydrogen peroxide was sufficient to stimulate microglia proliferation. Hydrogen Peroxide 142-159 catalase Rattus norvegicus 224-232 16393992-6 2006 Low concentrations of PMA or arachidonic acid (known activators of NADPH oxidase) or xanthine/xanthine oxidase or glucose oxidase (generating hydrogen peroxide) also increased microglia proliferation and this was blocked by catalase, showing that NADPH oxidase activation or hydrogen peroxide was sufficient to stimulate microglia proliferation. Hydrogen Peroxide 275-292 catalase Rattus norvegicus 224-232 16106039-8 2006 However, coinfusion of catalase reduced H2O2 excretion in both ANG II-treated (41 +/- 6%) and nontreated rats (28 +/- 5%). Hydrogen Peroxide 40-44 catalase Rattus norvegicus 23-31 16231001-11 2005 The peak concentration of H2O2 was 5.1 x 10(-4) M at 3 min and was prevented by catalase. Hydrogen Peroxide 26-30 catalase Rattus norvegicus 80-88 15913578-4 2005 Catalase, a scavenger of H2O2, inhibited the hypoxia-induced ROS generation and PAI-1 gene expression. Hydrogen Peroxide 25-29 catalase Rattus norvegicus 0-8 15962377-7 2005 CAT activity was determined by the breakdown of hydrogen peroxide. Hydrogen Peroxide 48-65 catalase Rattus norvegicus 0-3 15878237-3 2005 The endogenous antioxidant defense systems, catalase and glutathione peroxidase, were enhanced quickly by the pretreatment of low doses of H2O2. Hydrogen Peroxide 139-143 catalase Rattus norvegicus 44-52 16006739-10 2005 Meanwhile, catalase at a concentration sufficient to inhibit H(2)O(2)-induced relaxation did not exert definite inhibition of the CCh-induced relaxation. Hydrogen Peroxide 61-69 catalase Rattus norvegicus 11-19 15637121-10 2005 Catalase inhibited ANG II-increased H2O2 production but not Akt phosphorylation. Hydrogen Peroxide 36-40 catalase Rattus norvegicus 0-8 15607232-7 2005 Following a 1-h exposure of the cells to H2O2, a significant reduction in cell survival and activities of glutathione peroxidase (GSH-Px) and catalase (CAT), as well as increased levels in malondialdehyde (MDA) production and lactate dehydrogenase (LDH) release were observed. Hydrogen Peroxide 41-45 catalase Rattus norvegicus 142-150 15683716-3 2005 We found that interleukin-1beta (IL-1beta) stimulated the production of hydrogen peroxide (H2O2) which could be inhibited by loading the cells with the H2O2-scavenging enzyme catalase. Hydrogen Peroxide 72-89 catalase Rattus norvegicus 175-183 15683716-3 2005 We found that interleukin-1beta (IL-1beta) stimulated the production of hydrogen peroxide (H2O2) which could be inhibited by loading the cells with the H2O2-scavenging enzyme catalase. Hydrogen Peroxide 91-95 catalase Rattus norvegicus 175-183 15683716-3 2005 We found that interleukin-1beta (IL-1beta) stimulated the production of hydrogen peroxide (H2O2) which could be inhibited by loading the cells with the H2O2-scavenging enzyme catalase. Hydrogen Peroxide 152-156 catalase Rattus norvegicus 175-183 15804435-6 2005 ROS levels were decreased by added superoxide dismutase and catalase, suggesting that both superoxide and hydrogen peroxide contribute to the ROS signal. Hydrogen Peroxide 106-123 catalase Rattus norvegicus 60-68 15763464-11 2005 The Michaelis constant for hydrogen peroxide was evaluated to be 28 mM at pH 6.5 and 30 degrees C. rCAT was suggested to be a member of the typical catalase family. Hydrogen Peroxide 27-44 catalase Rattus norvegicus 99-103 15777843-2 2005 The present study was undertaken to investigate in renal insufficiency the expression of catalase and glutathione peroxidase, which play a critical role in antioxidant defense system by catalyzing detoxification of hydrogen peroxide (H2O2) and organic hydroperoxides. Hydrogen Peroxide 215-232 catalase Rattus norvegicus 89-97 15777843-2 2005 The present study was undertaken to investigate in renal insufficiency the expression of catalase and glutathione peroxidase, which play a critical role in antioxidant defense system by catalyzing detoxification of hydrogen peroxide (H2O2) and organic hydroperoxides. Hydrogen Peroxide 234-238 catalase Rattus norvegicus 89-97 15777843-2 2005 The present study was undertaken to investigate in renal insufficiency the expression of catalase and glutathione peroxidase, which play a critical role in antioxidant defense system by catalyzing detoxification of hydrogen peroxide (H2O2) and organic hydroperoxides. Hydrogen Peroxide 252-266 catalase Rattus norvegicus 89-97 15607232-7 2005 Following a 1-h exposure of the cells to H2O2, a significant reduction in cell survival and activities of glutathione peroxidase (GSH-Px) and catalase (CAT), as well as increased levels in malondialdehyde (MDA) production and lactate dehydrogenase (LDH) release were observed. Hydrogen Peroxide 41-45 catalase Rattus norvegicus 152-155 15607232-8 2005 However, preincubation of the cells with EPS2 prior to H2O2 exposure elevated the cell survival and GSH-Px and CAT activities, and decreased the level of MDA and LDH activity in a dose-dependent manner. Hydrogen Peroxide 55-59 catalase Rattus norvegicus 111-114 15331536-4 2004 On the other hand, the cytoplasmic catalase overexpression provided better protection against H(2)O(2) toxicity. Hydrogen Peroxide 94-102 catalase Rattus norvegicus 35-43 15313952-8 2004 The augmentation of ROS levels in cardiomyocytes treated with both leptin and ET-1 was reversed by a selective ET(A) receptor antagonist, ABT-627, and catalase, a hydrogen peroxide-decomposing enzyme. Hydrogen Peroxide 163-180 catalase Rattus norvegicus 111-159 15621053-8 2005 In addition, cotreatment with catalase, but not superoxide dismutase or mannitol, reversed the cardioprotective effect of baicalein, suggesting the involvement of hydrogen peroxide in the cardioprotective mechanism. Hydrogen Peroxide 163-180 catalase Rattus norvegicus 30-38 15451066-10 2004 From these results, it is concluded that both the glutathione system and catalase can be enhanced by H2O2 stimulation, but increased glutathione content rather than catalase activity was operative in the tolerance of lethal oxidative stress. Hydrogen Peroxide 101-105 catalase Rattus norvegicus 73-81 15350833-7 2004 Following a 30 min exposure of the cells to H2O2 (150 microM), a marked decrease in cell survival, activities of glutathione peroxidase and catalase as well as increased production of malondialdehyde (MDA) were found. Hydrogen Peroxide 44-48 catalase Rattus norvegicus 140-148 15460450-5 2004 SOD removes superoxide anions by converting them to H2O2, which can be rapidly converted to water by CAT and GPx. Hydrogen Peroxide 52-56 catalase Rattus norvegicus 101-104 15177642-3 2004 The expression rates of mRNA for catalase, Cu/Zn-superoxide dismutase (Cu/Zn-SOD) and Mn-superoxide dismutase (Mn-SOD) remains constant during culture and were not modulated by hydrogen peroxide or paraquat. Hydrogen Peroxide 177-194 catalase Rattus norvegicus 33-41 15196668-0 2004 Endogenous glutathione and catalase protect cultured rat astrocytes from the iron-mediated toxicity of hydrogen peroxide. Hydrogen Peroxide 103-120 catalase Rattus norvegicus 27-35 15027813-13 2004 While catalase, glutathione reductase (GR), and superoxide dismutase (SOD) levels were found to be significantly decreased (P < 0.001), malondialdehyde (MDA) (P < 0.05) and hydrogen peroxide (H2O2) (P < 0.001) levels were significantly increased in the cisplatin group when compared to the controls. Hydrogen Peroxide 179-196 catalase Rattus norvegicus 6-14 15287076-3 2004 After a 30 min exposure of the cells to H2O2 (150 microM), a marked decrease in cell survival, activities of glutathione peroxidase and catalase as well as an increased production of malondialdehyde (MDA) were found. Hydrogen Peroxide 40-44 catalase Rattus norvegicus 136-144 14973232-0 2004 Glutathione peroxidase-catalase cooperativity is required for resistance to hydrogen peroxide by mature rat oligodendrocytes. Hydrogen Peroxide 76-93 catalase Rattus norvegicus 23-31 14973232-8 2004 To test the relative roles of catalase and GPx in the setting of oxidative stress, we measured enzyme activity in cells exposed to H2O2 and found that H2O2 induced a decrease in catalase activity in developing but not in mature OLs. Hydrogen Peroxide 151-155 catalase Rattus norvegicus 30-38 14973232-8 2004 To test the relative roles of catalase and GPx in the setting of oxidative stress, we measured enzyme activity in cells exposed to H2O2 and found that H2O2 induced a decrease in catalase activity in developing but not in mature OLs. Hydrogen Peroxide 151-155 catalase Rattus norvegicus 178-186 14973232-10 2004 Finally, H2O2-dependent inactivation of catalase in developing OLs was prevented by the GPx mimic ebselen. Hydrogen Peroxide 9-13 catalase Rattus norvegicus 40-48 14973232-11 2004 These data provide evidence for a key role for GPx-catalase cooperativity in the resistance of mature OLs to H2O2-induced cell death. Hydrogen Peroxide 109-113 catalase Rattus norvegicus 51-59 15027813-13 2004 While catalase, glutathione reductase (GR), and superoxide dismutase (SOD) levels were found to be significantly decreased (P < 0.001), malondialdehyde (MDA) (P < 0.05) and hydrogen peroxide (H2O2) (P < 0.001) levels were significantly increased in the cisplatin group when compared to the controls. Hydrogen Peroxide 198-202 catalase Rattus norvegicus 6-14 12826251-7 2003 In contrast, catalase and glutathione peroxidase, antioxidant enzymes that remove hydroperoxides, were significantly reduced in the soleus with hindlimb unloading by 54.5 and 16.1%, respectively. Hydrogen Peroxide 82-96 catalase Rattus norvegicus 13-21 12775721-4 2003 Catalase expression and activity were lower in Yv2-12 and Yv13-44 cells than in H4IIE cells; furthermore, the transfectants were more susceptible to H2O2. Hydrogen Peroxide 149-153 catalase Rattus norvegicus 0-8 14647150-4 2003 Since catalase is an essential enzyme in detoxifying hydrogen peroxide, the aim of the present study was to investigate the protective effect of catalase as delivered by an adenovirus vector against doxorubicin-induced cardiotoxicity in cultured neonatal rat cardiac myocytes (NeRCaMs). Hydrogen Peroxide 53-70 catalase Rattus norvegicus 6-14 14647150-4 2003 Since catalase is an essential enzyme in detoxifying hydrogen peroxide, the aim of the present study was to investigate the protective effect of catalase as delivered by an adenovirus vector against doxorubicin-induced cardiotoxicity in cultured neonatal rat cardiac myocytes (NeRCaMs). Hydrogen Peroxide 53-70 catalase Rattus norvegicus 145-153 14556849-4 2003 V2O5-induced STAT-1 activation was blocked by catalase and N-acetyl-L-cysteine (NAC), suggesting vanadium-induced generation of H2O2. Hydrogen Peroxide 128-132 catalase Rattus norvegicus 46-54 12840017-9 2003 Catalase scavenged H2O2. Hydrogen Peroxide 19-23 catalase Rattus norvegicus 0-8 14766088-1 2003 OBJECTIVE: To investigate the effect of antioxidants N-acetyl-L-cysteine and catalase on H(2)O(2)-induced apoptosis of lens epithelial cells and the activity of caspase-3. Hydrogen Peroxide 89-97 catalase Rattus norvegicus 77-85 12398934-1 2002 This study was aimed at assessing the relative contributions to H(2)O(2) detoxification by glutathione peroxidase and catalase in the mitochondrial matrix of heart. Hydrogen Peroxide 64-72 catalase Rattus norvegicus 118-126 12781331-6 2003 The half-life of HP in the RINmHP cell culture medium was about 2.5 times lower than that of the parental cells, corresponding to the increased level of catalase expression and activity in selected cells. Hydrogen Peroxide 17-19 catalase Rattus norvegicus 153-161 12629987-3 2003 We aimed to study: 1) the detailed histopathological changes induced by free oxygen radicals in pancreas; and 2) the preventive effect of intraductal catalase in H2O2-induced acute pancreatitis. Hydrogen Peroxide 162-166 catalase Rattus norvegicus 150-158 14568024-7 2003 The pressor effects of intrathecal H(2)O(2) (1000 nmol) were attenuated by pretreatment with intrathecal administration of catalase (500 units), or N-acetyl-cysteine (1000 nmol). Hydrogen Peroxide 35-43 catalase Rattus norvegicus 123-131 12456800-3 2002 Because generation of the reactive oxygen species hydrogen peroxide (H(2)O(2)) plays a role in the inflammatory process and activation of proinflammatory transcription factors, we wanted to determine whether the antioxidant enzyme catalase might be a PPARgamma target gene. Hydrogen Peroxide 50-67 catalase Rattus norvegicus 231-239 12456800-3 2002 Because generation of the reactive oxygen species hydrogen peroxide (H(2)O(2)) plays a role in the inflammatory process and activation of proinflammatory transcription factors, we wanted to determine whether the antioxidant enzyme catalase might be a PPARgamma target gene. Hydrogen Peroxide 69-77 catalase Rattus norvegicus 231-239 12523659-0 2002 Pharmacokinetics and preventive effects of targeted catalase derivatives on hydrogen peroxide-induced injury in perfused rat liver. Hydrogen Peroxide 76-93 catalase Rattus norvegicus 52-60 12523659-8 2002 CONCLUSIONS: Internalized CAT derivatives are also effective in degrading hydrogen peroxide and targeted delivery of CAT to liver nonparenchymal cells by mannosylation or succinylation is a useful method for the prevention of hepatic injury caused by reactive oxygen species. Hydrogen Peroxide 74-91 catalase Rattus norvegicus 26-29 12385774-7 2002 These data indicate that the most important H(2)O(2) scavenger system in the islets is CAT and that this system can be modulated by metabolic substrates. Hydrogen Peroxide 44-52 catalase Rattus norvegicus 87-90 12398934-3 2002 Results show that the contribution of catalase to H(2)O(2) removal in heart mitochondria is not significant, even under strong oxidative conditions, such as those achieved in ischemia-reperfusion and involving extensive glutathione depletion and high H(2)O(2) concentrations. Hydrogen Peroxide 50-58 catalase Rattus norvegicus 38-46 12386149-8 2002 Catalase overexpression attenuated hypoxia-induced increases in [Ca2+]i, suggesting that H2O2 acts upstream from calcium increases during hypoxia. Hydrogen Peroxide 89-93 catalase Rattus norvegicus 0-8 12204541-5 2002 As for cadmium"s inhibitory mechanism on catalase activity, our data, obtained in the pH range 6.0-8.0, are a preliminary indication that the negative effect of this metal is probably due to imidazole residue binding of His-74 which is essential in the decomposition of hydrogen peroxide. Hydrogen Peroxide 270-287 catalase Rattus norvegicus 41-49 12130563-7 2002 Hydrogen peroxide (>/=10(-5) M) also stimulated p38 MAPK phosphorylation, ANG secretion, and ANG mRNA gene expression, but its stimulatory effect was blocked by catalase and SB 203580. Hydrogen Peroxide 0-17 catalase Rattus norvegicus 164-172 12051720-8 2002 Catalase, an enzyme which scavenges hydrogen peroxide, also inhibited the relaxation by LIF. Hydrogen Peroxide 36-53 catalase Rattus norvegicus 0-8 12150543-9 2002 Catalase and bathocuproine inhibited DNA damage, indicating the involvement of H2O2 and Cu(I). Hydrogen Peroxide 79-83 catalase Rattus norvegicus 0-8 16120297-0 2002 Catalase-dependent measurement of H2O2 in intact mitochondria. Hydrogen Peroxide 34-38 catalase Rattus norvegicus 0-8 16120297-3 2002 To measure H2O2 within mitochondria that contain catalase, we have developed an assay based on the ability of H2O2 to inhibit catalase in the presence of 3-amino-1,2,4-triazole. Hydrogen Peroxide 11-15 catalase Rattus norvegicus 49-57 16120297-3 2002 To measure H2O2 within mitochondria that contain catalase, we have developed an assay based on the ability of H2O2 to inhibit catalase in the presence of 3-amino-1,2,4-triazole. Hydrogen Peroxide 11-15 catalase Rattus norvegicus 126-134 16120297-3 2002 To measure H2O2 within mitochondria that contain catalase, we have developed an assay based on the ability of H2O2 to inhibit catalase in the presence of 3-amino-1,2,4-triazole. Hydrogen Peroxide 110-114 catalase Rattus norvegicus 49-57 16120297-3 2002 To measure H2O2 within mitochondria that contain catalase, we have developed an assay based on the ability of H2O2 to inhibit catalase in the presence of 3-amino-1,2,4-triazole. Hydrogen Peroxide 110-114 catalase Rattus norvegicus 126-134 16120297-9 2002 The assay should be useful for study of both superoxide-dependent H2O2 generation in situ, and the role of endogenous mitochondrial catalase in H2O2 removal. Hydrogen Peroxide 144-148 catalase Rattus norvegicus 132-140 12364975-6 2002 Although the level of H2O2 content increased in response to HCH in both groups, a totally different trend was observed for the activity of the principal H2O2-metabolising enzyme, catalase. Hydrogen Peroxide 153-157 catalase Rattus norvegicus 179-187 12172644-3 2002 The observed partial protective effect exerted by catalase indicates the involvement of both MAO-derived hydrogen peroxide and aldehyde. Hydrogen Peroxide 105-122 catalase Rattus norvegicus 50-58