PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24831254-1 2015 In the adult heart, catalase (CAT) activity increases appropriately with increasing levels of hydrogen peroxide, conferring cardioprotection. Hydrogen Peroxide 94-111 catalase Oryctolagus cuniculus 20-28 24831254-1 2015 In the adult heart, catalase (CAT) activity increases appropriately with increasing levels of hydrogen peroxide, conferring cardioprotection. Hydrogen Peroxide 94-111 catalase Oryctolagus cuniculus 30-33 9071927-6 1997 RESULTS: Of the free radical scavengers tested, superoxide dismutase, which reacts with the superoxide anion, significantly reduced oesophagitis, whereas catalase, which reacts with hydrogen peroxide, had only a mild effect and dimethylsulphoxide had no effect. Hydrogen Peroxide 182-199 catalase Oryctolagus cuniculus 154-162 17610981-0 2007 Efficient protection by cationized catalase against H2O2 injury in primary cultured alveolar epithelial cells. Hydrogen Peroxide 52-56 catalase Oryctolagus cuniculus 35-43 17610981-2 2007 In this study, the successful prevention of hydrogen peroxide (H(2)O(2))-induced injury in primary cultured rabbit alveolar epithelial cells by cationized catalase is described. Hydrogen Peroxide 44-61 catalase Oryctolagus cuniculus 155-163 17610981-2 2007 In this study, the successful prevention of hydrogen peroxide (H(2)O(2))-induced injury in primary cultured rabbit alveolar epithelial cells by cationized catalase is described. Hydrogen Peroxide 63-71 catalase Oryctolagus cuniculus 155-163 17610981-5 2007 Cationized catalase markedly suppressed H(2)O(2)-induced cell injury. Hydrogen Peroxide 40-48 catalase Oryctolagus cuniculus 11-19 17610981-6 2007 In addition, electron spin resonance spectrometry analysis revealed that cationized catalase effectively eliminated H(2)O(2) produced in the medium by glucose plus glucose oxidase. Hydrogen Peroxide 116-124 catalase Oryctolagus cuniculus 84-92 14645719-5 2003 By contrast, the enzyme catalase, which destroys H2O2, attenuated A23187-induced relaxations over a broad range of concentrations, but only minimally depressed the maximum response to ACh. Hydrogen Peroxide 49-53 catalase Oryctolagus cuniculus 24-32 12097831-4 2002 In OK cells subjected to chemical hypoxia, the generation of ROS was increased, and this was prevented by the H(2)O(2) scavenger catalase, but not by the hydroxyl radical scavenger dimethylthiourea (DMTU). Hydrogen Peroxide 110-118 catalase Oryctolagus cuniculus 129-137 11250878-14 2001 Aminotriazole (an inhibitor of catalase; 50 mM) significantly potentiated the H(2)O(2)-induced inhibition of ACh-contractions in epithelium-intact strips but not in epithelium-denuded strips. Hydrogen Peroxide 78-86 catalase Oryctolagus cuniculus 31-39 11250878-19 2001 It is suggested that the epithelium may act as a powerful biochemical barrier via both the action of catalase (scavenging H(2)O(2)) and the release of bronchoconstrictor prostaglandins, thus attenuating the H(2)O(2)-induced modulation of ACh-contractions. Hydrogen Peroxide 122-131 catalase Oryctolagus cuniculus 101-109 11250878-19 2001 It is suggested that the epithelium may act as a powerful biochemical barrier via both the action of catalase (scavenging H(2)O(2)) and the release of bronchoconstrictor prostaglandins, thus attenuating the H(2)O(2)-induced modulation of ACh-contractions. Hydrogen Peroxide 122-130 catalase Oryctolagus cuniculus 101-109 9990330-14 1998 The overall results suggest that augmenting lens catalase may prevent cataract development caused by H2O2 stress. Hydrogen Peroxide 101-105 catalase Oryctolagus cuniculus 49-57 9763225-9 1998 These results indicate that intact proximal tubules are more resistant to H2O2 than are cultured proximal tubular cells, and the resistance is due to a higher specific activity of catalase resulting from the increased expression of its mRNA. Hydrogen Peroxide 74-78 catalase Oryctolagus cuniculus 180-188 9418724-8 1997 RESULTS: H2O2 converted DCFH to DCF in a dose-dependent manner, which was inhibited by catalase dose dependently. Hydrogen Peroxide 9-13 catalase Oryctolagus cuniculus 87-95 11250878-11 2001 Catalase (500 u ml(-1)) completely blocked both H(2)O(2)-induced effects on ACh-contractions (enhancement and inhibition). Hydrogen Peroxide 48-56 catalase Oryctolagus cuniculus 0-8 9932891-8 1999 Both ebselen and catalase inhibited the contractile response to hydroxyl radical generated by ferrous ion (10(-3) mol/L) plus hydrogen peroxide (10(-2) mol/L). Hydrogen Peroxide 126-143 catalase Oryctolagus cuniculus 17-25 8992503-14 1996 Such inhibition of catalase by near-UV would enhance H2O2 toxicity and stimulate SH oxidation so as to damage the lens. Hydrogen Peroxide 53-57 catalase Oryctolagus cuniculus 19-27 8975786-3 1996 Catalase prevented the effect of H2O2 but not that of t-BHP, suggesting that lower potency of H2O2 is attributed to the endogenous catalase activity. Hydrogen Peroxide 33-37 catalase Oryctolagus cuniculus 0-8 8975786-3 1996 Catalase prevented the effect of H2O2 but not that of t-BHP, suggesting that lower potency of H2O2 is attributed to the endogenous catalase activity. Hydrogen Peroxide 33-37 catalase Oryctolagus cuniculus 131-139 8975786-3 1996 Catalase prevented the effect of H2O2 but not that of t-BHP, suggesting that lower potency of H2O2 is attributed to the endogenous catalase activity. Hydrogen Peroxide 94-98 catalase Oryctolagus cuniculus 0-8 8975786-3 1996 Catalase prevented the effect of H2O2 but not that of t-BHP, suggesting that lower potency of H2O2 is attributed to the endogenous catalase activity. Hydrogen Peroxide 94-98 catalase Oryctolagus cuniculus 131-139 8696257-6 1996 Here we investigate the histochemical and immunoperoxidase distributions of catalase, an enzyme which detoxifies H2O2, in cells from the peripheral and central regions of the epithelium on flat mount preparations of the epithelium. Hydrogen Peroxide 113-117 catalase Oryctolagus cuniculus 76-84 8696257-11 1996 The decreased level of catalase throughout the central epithelium may account for the increased susceptibility of these cells to H2O2-induced cell death. Hydrogen Peroxide 129-133 catalase Oryctolagus cuniculus 23-31 8193214-5 1994 INTERVENTIONS: Four groups according to pretreatment: group I: superoxide dismutase-superoxide scavenger; group II: catalase-hydrogen peroxide scavenger; group III: superoxide dismutase and catalase; group IV: mannitol-hydroxyl scavenger. Hydrogen Peroxide 125-142 catalase Oryctolagus cuniculus 116-124 9054188-3 1996 Application of catalase, a scavenger of hydrogen peroxide, to the eye surface during the irradiation diminished the increase of xanthine oxidase activity. Hydrogen Peroxide 40-57 catalase Oryctolagus cuniculus 15-23 8135870-2 1994 Since the oxidation of cyanamide by catalase/H2O2 had been shown previously to lead to nitroxyl (HNO) generation via the intermediate N-hydroxycyanamide, and aortic ring relaxation was inhibited by the catalase inhibitor, 3-aminotriazole, HNO appears to be responsible for the vasorelaxation mediated by cyanamide. Hydrogen Peroxide 45-49 catalase Oryctolagus cuniculus 202-210 7930939-1 1994 The production of H2O2 by cells in cold paraformaldehyde-fixed frozen sections of inflammatory lesions was histochemically demonstrated by incubating them with diaminobenzidine (DAB) for 2 to 6 h. Catalase (150 micrograms/ml, about 1400 U/ml) inhibited the reaction, indicating that H2O2 was required to produce the chromogenic DAB product. Hydrogen Peroxide 18-22 catalase Oryctolagus cuniculus 197-205 2395064-5 1990 The two mechanisms available to metabolize H2O2, catalase and the glutathione cycle, were significantly lower in both proximal and distal small bowel from fasted animals than in those from fed animals. Hydrogen Peroxide 43-47 catalase Oryctolagus cuniculus 49-57 1335702-7 1992 Catalase completely inhibited the H2O2-induced relaxation of ACh-precontracted tracheal smooth muscle. Hydrogen Peroxide 34-38 catalase Oryctolagus cuniculus 0-8 1280902-7 1992 The antioxidant, catalase, inhibited chemiluminescence but superoxide dismutase had no effect, suggesting that luminol-dependent chemiluminescence in chondrocytes mostly measured hydrogen peroxide. Hydrogen Peroxide 179-196 catalase Oryctolagus cuniculus 17-25 1321075-3 1992 Catalase (100 U/ml), but not SOD (100 Uml), deferoxamine (100 microM) or mannitol (20 mM), protected CK from inactivation; suggesting that H2O2 was responsible for inactivation. Hydrogen Peroxide 139-143 catalase Oryctolagus cuniculus 0-8 1784460-11 1991 From these data we conclude that the glutathione redox system protects the anterior segment tissues from hydrogen peroxide at low concentrations of this oxidant, while catalase assumes a greater role at higher concentrations of hydrogen peroxide. Hydrogen Peroxide 228-245 catalase Oryctolagus cuniculus 168-176 1672675-2 1991 Intraperitoneal superoxide dismutase (SOD) and catalase were used to block the toxic effects of superoxide anion (O2) and hydrogen peroxide (H2O2), associated with the production of endometriosis and inflammation in a rabbit model. Hydrogen Peroxide 122-139 catalase Oryctolagus cuniculus 47-55 1672675-2 1991 Intraperitoneal superoxide dismutase (SOD) and catalase were used to block the toxic effects of superoxide anion (O2) and hydrogen peroxide (H2O2), associated with the production of endometriosis and inflammation in a rabbit model. Hydrogen Peroxide 141-145 catalase Oryctolagus cuniculus 47-55 1784460-0 1991 Roles of catalase and the glutathione redox cycle in the regulation of anterior-chamber hydrogen peroxide. Hydrogen Peroxide 88-105 catalase Oryctolagus cuniculus 9-17 1784460-1 1991 The effects of inhibition of both glutathione synthesis and of glutathione reductase and catalase activities have been determined in the regulation of hydrogen peroxide (H2O2) in the anterior chamber of pigmented rabbits. Hydrogen Peroxide 151-168 catalase Oryctolagus cuniculus 89-97 1784460-1 1991 The effects of inhibition of both glutathione synthesis and of glutathione reductase and catalase activities have been determined in the regulation of hydrogen peroxide (H2O2) in the anterior chamber of pigmented rabbits. Hydrogen Peroxide 170-174 catalase Oryctolagus cuniculus 89-97 2373171-0 1990 The relative roles of the glutathione redox cycle and catalase in the detoxification of H2O2 by cultured rabbit lens epithelial cells. Hydrogen Peroxide 88-92 catalase Oryctolagus cuniculus 54-62 2114447-8 1990 Fluorescent dichlorofluorescin oxidation by chondrocytes was inhibited by the addition of catalase, an enzyme that detoxifies hydrogen peroxide. Hydrogen Peroxide 126-143 catalase Oryctolagus cuniculus 90-98 2373171-1 1990 The relative roles of the glutathione redox cycle and catalase in the detoxification of H2O2 were investigated in cultured rabbit lens epithelial cells. Hydrogen Peroxide 88-92 catalase Oryctolagus cuniculus 54-62 2373171-8 1990 In contrast, cells with completely inhibited catalase but with an unimpaired glutathione redox cycle suffered few damaging effects from a 3-hr exposure to 0.025 mM H2O2. Hydrogen Peroxide 164-168 catalase Oryctolagus cuniculus 45-53 2373171-9 1990 When lens cells were pulsed with a single challenge of 0.5 mM H2O2, both the glutathione redox cycle and catalase were found to be essential for survival of the cells. Hydrogen Peroxide 62-66 catalase Oryctolagus cuniculus 105-113 2373171-12 1990 The cause of cell death following inhibition of catalase appeared to be related to an inability of the cells to remove peroxide from the culture medium, at a rapid rate, following the H2O2-pulse. Hydrogen Peroxide 184-188 catalase Oryctolagus cuniculus 48-56 2560663-7 1989 Experiments with superoxide dismutase and catalase suggest that release of H2O2 may partly explain the stimulatory activity of leukocytes in the presence of chemoattractants. Hydrogen Peroxide 75-79 catalase Oryctolagus cuniculus 42-50 2562169-3 1989 Enzymatically generated superoxide anion produced endothelial damage which could not be blocked with superoxide dismutase (which removes superoxide anion from the system), but could it be blocked with catalase which removes hydrogen peroxide from the system. Hydrogen Peroxide 224-241 catalase Oryctolagus cuniculus 201-209 2486936-1 1989 Hydrogen peroxide injected into the anterior chamber of adult rabbits causes a sequence of events that is not seen in young normal rabbits, yet is replicated in young rabbits receiving a catalase inhibitor. Hydrogen Peroxide 0-17 catalase Oryctolagus cuniculus 187-195 3427989-3 1987 The more rapid disappearance of H2O2 correlated with greater catalase levels in iris (35%) and corneal endothelium (50%) in young as compared to adult animals. Hydrogen Peroxide 32-36 catalase Oryctolagus cuniculus 61-69 3182500-4 1988 Pretreatment with catalase (1,000 U/ml), a scavenger of H2O2, significantly (P less than 0.05, Friedman"s) attenuated the increases in lung weight (50.4 +/- 13.9 vs. 15.1 +/- 4.9 g), airway pressure, and pulmonary arterial pressure. Hydrogen Peroxide 56-60 catalase Oryctolagus cuniculus 18-26 3143279-8 1988 or H2O2 (derived from O2-) contribute to the well-documented increase in lung permeability in RPE because dimethylthiourea, dimethylthiourea plus catalase, or catalase alone inhibited the edema to various degrees. Hydrogen Peroxide 3-7 catalase Oryctolagus cuniculus 159-167 3427989-9 1987 Considering the sum total of all tissues of the anterior segment, specific incremental decreases of catalase generated by intravenous 3AT caused the t1/2 of H2O2 clearance from the anterior chamber to become longer, while the reducing power of anterior segment tissues excluding lens epithelium is related clearly to the systemic dose of 3AT. Hydrogen Peroxide 157-161 catalase Oryctolagus cuniculus 100-108 4018164-6 1985 These observations indicate that catalase within the iris-ciliary body enables the tissue to detoxify hydrogen peroxide from solution. Hydrogen Peroxide 102-119 catalase Oryctolagus cuniculus 33-41 4018164-7 1985 Catalase might protect the iris-ciliary body from damage by hydrogen peroxide generated by normal physiological or pathophysiological conditions. Hydrogen Peroxide 60-77 catalase Oryctolagus cuniculus 0-8 6317286-7 1984 and H2O2 provided by superoxide dismutase, catalase and glutathione peroxidase were impaired in cataracts. Hydrogen Peroxide 4-8 catalase Oryctolagus cuniculus 43-51 6414352-3 1983 We found that either dimethyl thiourea, a scavenger of hydroxyl radical, or catalase, a scavenger of H2O2, protected cultured rabbit AM against hyperoxic damage, which suggests that H2O2 or an H2O2-derived product, such as hydroxyl radical, contribute to damage to AM from hyperoxia. Hydrogen Peroxide 101-105 catalase Oryctolagus cuniculus 76-84 6414352-3 1983 We found that either dimethyl thiourea, a scavenger of hydroxyl radical, or catalase, a scavenger of H2O2, protected cultured rabbit AM against hyperoxic damage, which suggests that H2O2 or an H2O2-derived product, such as hydroxyl radical, contribute to damage to AM from hyperoxia. Hydrogen Peroxide 182-186 catalase Oryctolagus cuniculus 76-84 6414352-3 1983 We found that either dimethyl thiourea, a scavenger of hydroxyl radical, or catalase, a scavenger of H2O2, protected cultured rabbit AM against hyperoxic damage, which suggests that H2O2 or an H2O2-derived product, such as hydroxyl radical, contribute to damage to AM from hyperoxia. Hydrogen Peroxide 182-186 catalase Oryctolagus cuniculus 76-84 211851-3 1978 CL is inhibited by superoxide dismutase, an enzyme which catalyzes the conversion of O2- to hydrogen peroxide (H2O2), by catalase, an enzyme which destroys H2O2, and by the hydroxyl radical (.OH) scavengers, benzoate and ethanol. Hydrogen Peroxide 156-160 catalase Oryctolagus cuniculus 121-129 208649-10 1978 Thus endogenous catalase of lens affords protection to the lens superoxide dismutase from inactivation by H2O2. Hydrogen Peroxide 106-110 catalase Oryctolagus cuniculus 16-24 208649-13 1978 We conclude that catalase of eye affords protection to the lens from H2O2 and it also protects superoxide dismutase of lens from inactivation by H2O2. Hydrogen Peroxide 69-73 catalase Oryctolagus cuniculus 17-25 208649-13 1978 We conclude that catalase of eye affords protection to the lens from H2O2 and it also protects superoxide dismutase of lens from inactivation by H2O2. Hydrogen Peroxide 145-149 catalase Oryctolagus cuniculus 17-25 208649-8 1978 H2O2 caused inhibition of superoxide dismutase activity of lens extract, and this inhibition was potentiated by the catalase inhibitor 3-amino-1H-1,2,4-triazole (3-aminotriazole) or NaN3. Hydrogen Peroxide 0-4 catalase Oryctolagus cuniculus 116-124 889879-8 1977 Based on these findings our conclusion is that catalase of eye tissues regulates the endogenous H2O2 in eye humors to the physiological level. Hydrogen Peroxide 96-100 catalase Oryctolagus cuniculus 47-55