PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19302986-7 2009 Finally, the protection could be antagonized using the catalase inhibitor 3-aminotriazole. Amitrole 74-89 catalase Rattus norvegicus 55-63 21439021-1 2011 We previously reported that the inhibition of catalase and glutathione peroxidase activities by treatment with 3-amino-1,2,4-triazole (ATZ) and mercaptosuccinic acid evoked sustained increases in the levels of reactive oxygen species and apoptosis in rat primary hepatocytes. Amitrole 111-133 catalase Rattus norvegicus 46-54 21439021-1 2011 We previously reported that the inhibition of catalase and glutathione peroxidase activities by treatment with 3-amino-1,2,4-triazole (ATZ) and mercaptosuccinic acid evoked sustained increases in the levels of reactive oxygen species and apoptosis in rat primary hepatocytes. Amitrole 135-138 catalase Rattus norvegicus 46-54 21032900-4 2010 Aminotriazole also activated ADH and MEOS, but inhibited liver catalase. Amitrole 0-13 catalase Rattus norvegicus 63-71 21890522-8 2011 Microinjection into the PVN of the catalase inhibitor, aminotriazole, increased the RSNA and MAP and enhanced the CSAR. Amitrole 55-68 catalase Rattus norvegicus 35-43 18439665-3 2008 Further, DA-induced oxidative induction was potentiated (P<0.001) in the presence of iron (5 microM) and 3-amino triazole and mercaptosuccinate (P<0.001), known inhibitors of the peroxide metabolizing enzymes, catalase and glutathione peroxidase, respectively. Amitrole 108-124 catalase Rattus norvegicus 216-224 19607981-9 2009 This effect was reverted by concomitant bath application of the catalase inhibitor 3-aminotriazole (20mM), suggesting the involvement of catalase in mediating the neuroprotective effects of MS. Amitrole 83-98 catalase Rattus norvegicus 64-72 19607981-9 2009 This effect was reverted by concomitant bath application of the catalase inhibitor 3-aminotriazole (20mM), suggesting the involvement of catalase in mediating the neuroprotective effects of MS. Amitrole 83-98 catalase Rattus norvegicus 137-145 16527547-9 2006 Catalase attenuated acetylcholine-induced relaxations and this attenuation was prevented by 3-amino-1,2,4-triazole (catalase inhibitor). Amitrole 92-114 catalase Rattus norvegicus 0-8 17660523-5 2007 The addition of the catalase inhibitor, aminotriazole, (10 mM) to the perfusing fluid decreased ethanol elimination significantly. Amitrole 40-53 catalase Rattus norvegicus 20-28 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. Amitrole 194-207 catalase Rattus norvegicus 174-182 17320761-5 2007 The first, a pharmacological approach, used 3-amino-1,2,4-triazole, an irreversible inhibitor that reduced catalase enzymatic activity by 75%. Amitrole 44-66 catalase Rattus norvegicus 107-115 17961299-1 2007 We have previously shown that inhibition of catalase and glutathione peroxidase activities in rat primary hepatocytes by 3-amino-1,2,4-triazole (ATZ) and mercaptosuccinic acid (MS) results in sustained oxidative stress, followed by apoptosis. Amitrole 121-143 catalase Rattus norvegicus 44-52 17961299-1 2007 We have previously shown that inhibition of catalase and glutathione peroxidase activities in rat primary hepatocytes by 3-amino-1,2,4-triazole (ATZ) and mercaptosuccinic acid (MS) results in sustained oxidative stress, followed by apoptosis. Amitrole 145-148 catalase Rattus norvegicus 44-52 17961299-4 2007 Treatment with ATZ and MS reduced catalase (CAT) and glutathione peroxidase (GPx) activities, and decreased CAT and GPx activities recovered to normal values upon withdrawal. Amitrole 15-18 catalase Rattus norvegicus 34-42 17961299-4 2007 Treatment with ATZ and MS reduced catalase (CAT) and glutathione peroxidase (GPx) activities, and decreased CAT and GPx activities recovered to normal values upon withdrawal. Amitrole 15-18 catalase Rattus norvegicus 44-47 17961299-4 2007 Treatment with ATZ and MS reduced catalase (CAT) and glutathione peroxidase (GPx) activities, and decreased CAT and GPx activities recovered to normal values upon withdrawal. Amitrole 15-18 catalase Rattus norvegicus 108-111 16527547-9 2006 Catalase attenuated acetylcholine-induced relaxations and this attenuation was prevented by 3-amino-1,2,4-triazole (catalase inhibitor). Amitrole 92-114 catalase Rattus norvegicus 116-124 15763964-1 2005 We previously showed that inhibition of catalase and glutathione peroxidase activities in rat primary hepatocytes by 3-amino-1,2,4-triazole (ATZ) and mercaptosuccinic acid (MS) results in endogenous oxidative stress and apoptosis. Amitrole 117-139 catalase Rattus norvegicus 40-48 16407272-1 2006 We have previously shown that inhibition of catalase and glutathione peroxidase activities by 3-amino-1,2,4-triazole (ATZ) and mercaptosuccinic acid (MS), respectively, in rat primary hepatocytes caused sustained endogenous oxidative stress and apoptotic cell death without caspase-3 activation. Amitrole 94-116 catalase Rattus norvegicus 44-52 16407272-1 2006 We have previously shown that inhibition of catalase and glutathione peroxidase activities by 3-amino-1,2,4-triazole (ATZ) and mercaptosuccinic acid (MS), respectively, in rat primary hepatocytes caused sustained endogenous oxidative stress and apoptotic cell death without caspase-3 activation. Amitrole 118-121 catalase Rattus norvegicus 44-52 15857626-7 2005 In addition, the antidyskinetic property of vitamin E and vitamin C was abolished by a concomitant treatment with the catalase inhibitor aminotriazole. Amitrole 137-150 catalase Rattus norvegicus 118-126 15763964-1 2005 We previously showed that inhibition of catalase and glutathione peroxidase activities in rat primary hepatocytes by 3-amino-1,2,4-triazole (ATZ) and mercaptosuccinic acid (MS) results in endogenous oxidative stress and apoptosis. Amitrole 141-144 catalase Rattus norvegicus 40-48 15196668-3 2004 The rate of peroxide detoxification was significantly slowed by pre-incubating the cells with the glutathione synthesis inhibitor buthionine sulfoximine (BSO), or the catalase inhibitor 3-amino-1,2,4-triazole (3AT), and was retarded further when both treatments were combined. Amitrole 186-208 catalase Rattus norvegicus 167-175 15696052-7 2005 In the second set of experiments, a direct irreversible catalase inhibitor, 3-amino-1,2,4-triazole (AT), was administered intraperitoneally (1 mg/kg) daily to tamoxifen-treated (n = 6) and control rats (n = 6), starting on day 7 after elastase perfusion. Amitrole 76-98 catalase Rattus norvegicus 56-64 15696052-7 2005 In the second set of experiments, a direct irreversible catalase inhibitor, 3-amino-1,2,4-triazole (AT), was administered intraperitoneally (1 mg/kg) daily to tamoxifen-treated (n = 6) and control rats (n = 6), starting on day 7 after elastase perfusion. Amitrole 100-102 catalase Rattus norvegicus 56-64 12068249-3 2002 The catalase inhibitor 3-amino-1,2,4-triazole (AT) reduces the production of acetaldehyde, and AT administration can reduce a number of ethanol-induced behavioral effects; this suggests the involvement of acetaldehyde in these behaviors. Amitrole 23-45 catalase Rattus norvegicus 4-12 15528010-6 2004 In the presence of 3-amino-1,2,4-triazole, a catalase inhibitor that created conditions that were favorable to reactive oxygen species accumulation, trolox was able to counteract the deleterious effect of the inhibitor. Amitrole 19-41 catalase Rattus norvegicus 45-53 15042439-3 2004 It has been reported that when catalase activity is reduced by 3-amino-1,2,4-triazole (AT), rats reduce their intake and preference for ethanol. Amitrole 63-85 catalase Rattus norvegicus 31-39 13129829-9 2003 One group of rats that received the ethanol injection was pretreated with 3-amino-1,2,4-triazole (AT), a catalase inhibitor, and another group was pretreated with disulfiram, an aldehyde dehydrogenase inhibitor. Amitrole 98-100 catalase Rattus norvegicus 105-113 12423650-9 2002 Further co-incubation of TE either with mercaptosuccinate (a potent glutathione peroxidase inhibitor) or 3-aminotriazole (an irreversible catalase inhibitor) resulted in a marked increase in t-bHP-induced lipid peroxidation, clearly suggesting the importance of both of these enzymic antioxidants in rat testis in vitro. Amitrole 105-120 catalase Rattus norvegicus 138-146 12775721-6 2003 Treatment of H4IIE cells with the catalase inhibitor 3-amino-1,2,4-triazole rendered them resistant to exogenous TNF-alpha. Amitrole 53-75 catalase Rattus norvegicus 34-42 12068249-3 2002 The catalase inhibitor 3-amino-1,2,4-triazole (AT) reduces the production of acetaldehyde, and AT administration can reduce a number of ethanol-induced behavioral effects; this suggests the involvement of acetaldehyde in these behaviors. Amitrole 47-49 catalase Rattus norvegicus 4-12 11510883-7 2001 A catalase inhibitor, 3-amino-1,2,4-triazole, completely abolished the infarct-limiting effect of HBO pretreatment, which suggests that HBO-induced tolerance against ischemia-reperfusion injury is due to catalase induction. Amitrole 22-44 catalase Rattus norvegicus 2-10 12123625-9 2002 Though aminotriazole partially inhibited the catalase activity, it inhibited 5-HT-induced contractions significantly. Amitrole 7-20 catalase Rattus norvegicus 45-53 11812238-4 2001 The entrance of mitochondria into the nucleus was modeled in rats that were given ethanol and the catalase inhibitor aminotriazole for 12 weeks. Amitrole 117-130 catalase Rattus norvegicus 98-106 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. Amitrole 154-176 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. Amitrole 154-176 catalase Rattus norvegicus 126-134 11510883-7 2001 A catalase inhibitor, 3-amino-1,2,4-triazole, completely abolished the infarct-limiting effect of HBO pretreatment, which suggests that HBO-induced tolerance against ischemia-reperfusion injury is due to catalase induction. Amitrole 22-44 catalase Rattus norvegicus 204-212 10762670-7 2000 Pretreatment with 3-amino-1,2,4 triazole (5 mM), a catalase inhibitor, inhibited the peak relaxant response to acetylcholine in diabetic rings. Amitrole 18-40 catalase Rattus norvegicus 51-59 10967081-12 2000 Aminotriazole, L-buthionine sulfoximine, and sodium azide partly abrogated the RGC resistance to oxidative stress, suggesting that this resistance may be mediated by catalase and/or glutathione peroxidase. Amitrole 0-13 catalase Rattus norvegicus 166-174 10569634-2 1999 To produce endogenous oxidative stress, 3-amino-1,2,4-triazole (ATZ) and mercaptosuccinic acid (MS), which are known to inhibit catalase and glutathione peroxidase activities, respectively, were used. Amitrole 40-62 catalase Rattus norvegicus 128-136 10569634-2 1999 To produce endogenous oxidative stress, 3-amino-1,2,4-triazole (ATZ) and mercaptosuccinic acid (MS), which are known to inhibit catalase and glutathione peroxidase activities, respectively, were used. Amitrole 64-67 catalase Rattus norvegicus 128-136 10579652-4 1999 In both cell types, the presence of 3-aminotriazole (an inhibitor of catalase) did not decrease ROS production from ethanol. Amitrole 36-51 catalase Rattus norvegicus 69-77 9441834-8 1997 Catalase inhibition by 3-amino triazole (AT) abolished the antiarrhythmic effect of heat stress. Amitrole 23-39 catalase Rattus norvegicus 0-8 10457996-0 1999 [Features of the inhibition of catalase activity by 3-amino-1,2,4-triazole in erythrocytes and liver of rats with streptozotocin diabetes]. Amitrole 52-74 catalase Rattus norvegicus 31-39 10457996-4 1999 It was investigated liver- and erythrocyte catalase inhibition in the presence of 3-amino-1,2,4-triazole. Amitrole 82-104 catalase Rattus norvegicus 43-51 9835273-5 1998 Inhibition of this process by the catalase inhibitor, 3-amino-1,2,4-triazole (8 mM), was minimal in the brainstem (27%) and maximal (57%) in the cerebellum, despite nearly complete inhibition of catalase. Amitrole 54-76 catalase Rattus norvegicus 34-42 9835273-5 1998 Inhibition of this process by the catalase inhibitor, 3-amino-1,2,4-triazole (8 mM), was minimal in the brainstem (27%) and maximal (57%) in the cerebellum, despite nearly complete inhibition of catalase. Amitrole 54-76 catalase Rattus norvegicus 195-203 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. Amitrole 32-54 catalase Rattus norvegicus 20-28 9441834-8 1997 Catalase inhibition by 3-amino triazole (AT) abolished the antiarrhythmic effect of heat stress. Amitrole 41-43 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. Amitrole 57-72 catalase Rattus norvegicus 115-123 9309319-4 1997 When incubated with CAT inhibitors (sodium azide or 3-aminotriazole), AcHO formation was blocked, whereas neither the alcohol dehydrogenase inhibitor, 4-methylpyrazole, nor P-450 inhibitors decreased AcHO production. Amitrole 52-67 catalase Rattus norvegicus 20-23 9309319-10 1997 This was prevented by administration of a CAT inhibitor (3-amino-1,2,4-triazole). Amitrole 57-79 catalase Rattus norvegicus 42-45 9208153-6 1997 Incubation with 3-amino-1,2,4-triazole (50 mM, 90 min, followed by washout) to inhibit endogenous catalase had no effect by itself on subsequent phenylephrine-induced contraction. Amitrole 16-38 catalase Rattus norvegicus 98-106 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. Amitrole 31-53 catalase Rattus norvegicus 84-92 9140708-6 1997 On the other hand, administration of aminotriazole, an inhibitor of catalase, did not affect the brain pathology of SHRSP, in spite of a mild reduction in tissue uric acid content. Amitrole 37-50 catalase Rattus norvegicus 68-76 9254029-7 1997 The protective effect of IL-6 was attenuated by 3-amino-1,2,4-triazole, an inhibitor of catalase. Amitrole 48-70 catalase Rattus norvegicus 88-96 8892520-4 1996 Catalase inhibitors sodium azide (SA) and 3-amino-1,2,4-triazole (3-AT) had little effect on ADH activity but markedly decreased catalase activity and acetaldehyde formation (1 mM of SA to 56 +/- 13% of control, 5 mM of 3-AT to 67 +/- 3% of control; mean +/- SE). Amitrole 42-64 catalase Rattus norvegicus 0-8 8892520-4 1996 Catalase inhibitors sodium azide (SA) and 3-amino-1,2,4-triazole (3-AT) had little effect on ADH activity but markedly decreased catalase activity and acetaldehyde formation (1 mM of SA to 56 +/- 13% of control, 5 mM of 3-AT to 67 +/- 3% of control; mean +/- SE). Amitrole 42-64 catalase Rattus norvegicus 129-137 8892520-4 1996 Catalase inhibitors sodium azide (SA) and 3-amino-1,2,4-triazole (3-AT) had little effect on ADH activity but markedly decreased catalase activity and acetaldehyde formation (1 mM of SA to 56 +/- 13% of control, 5 mM of 3-AT to 67 +/- 3% of control; mean +/- SE). Amitrole 66-70 catalase Rattus norvegicus 0-8 8892520-4 1996 Catalase inhibitors sodium azide (SA) and 3-amino-1,2,4-triazole (3-AT) had little effect on ADH activity but markedly decreased catalase activity and acetaldehyde formation (1 mM of SA to 56 +/- 13% of control, 5 mM of 3-AT to 67 +/- 3% of control; mean +/- SE). Amitrole 66-70 catalase Rattus norvegicus 129-137 8892520-4 1996 Catalase inhibitors sodium azide (SA) and 3-amino-1,2,4-triazole (3-AT) had little effect on ADH activity but markedly decreased catalase activity and acetaldehyde formation (1 mM of SA to 56 +/- 13% of control, 5 mM of 3-AT to 67 +/- 3% of control; mean +/- SE). Amitrole 220-224 catalase Rattus norvegicus 0-8 9032791-2 1996 When weanling rabbits, guinea pigs, and rats we administered 3-AT for 8, 7, and 10 weeks, respectively, retinal catalase activity was reduced by approximately 50% in all these animals. Amitrole 61-65 catalase Rattus norvegicus 112-120 8614020-9 1996 Administered alone or in association with PMA, CAT inactivated by heat or 3-aminotriazole also caused severe lung damage. Amitrole 74-89 catalase Rattus norvegicus 47-50 8620569-6 1996 Treatment of rats with the catalase inhibitor aminotriazole increased the ubiquinone levels in kidney, heart and muscle but not in liver. Amitrole 46-59 catalase Rattus norvegicus 27-35 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. Amitrole 120-143 catalase Rattus norvegicus 15-23 7586320-0 1995 Catalase inhibition with 3-amino-1,2,4-triazole does not abolish infarct size reduction in heat-shocked rats. Amitrole 25-47 catalase Rattus norvegicus 0-8 7586320-3 1995 The aim of the present study was to determine whether catalase inhibition with 3-amino-1,2,4-triazole (3-AT) abolishes the reduction of infarct size conferred by heat-shock treatment in rats. Amitrole 79-101 catalase Rattus norvegicus 54-62 7586320-3 1995 The aim of the present study was to determine whether catalase inhibition with 3-amino-1,2,4-triazole (3-AT) abolishes the reduction of infarct size conferred by heat-shock treatment in rats. Amitrole 103-107 catalase Rattus norvegicus 54-62 7586320-8 1995 Treatment with 3-AT significantly reduced myocardial catalase activity in both heat-shocked and control animals (29.6 +/- 5.7, n = 5, and 36.4 +/- 15.3, n = 6, respectively). Amitrole 15-19 catalase Rattus norvegicus 53-61 7586320-10 1995 CONCLUSIONS: Catalase inhibition with 3-AT does not abolish the reduction of infarct size in heat-shocked rats. Amitrole 38-42 catalase Rattus norvegicus 13-21 7752092-6 1995 In contrast, suppression of rat red cell catalase activity by aminotriazole had no effect on the hemotoxicity of N-hydroxydapsone. Amitrole 62-75 catalase Rattus norvegicus 41-49 7546330-1 1995 Aminotriazole (AT), a catalase inhibitor, was administered to UChA (low ethanol consumer) and UChB (high ethanol consumer) rats. Amitrole 0-13 catalase Rattus norvegicus 22-30 7546330-1 1995 Aminotriazole (AT), a catalase inhibitor, was administered to UChA (low ethanol consumer) and UChB (high ethanol consumer) rats. Amitrole 15-17 catalase Rattus norvegicus 22-30 8181541-4 1993 However, addition of catalase or the catalase inhibitor aminotriazole did not influence the inhibition of gap junctional communication by 25-hydroxycholesterol. Amitrole 56-69 catalase Rattus norvegicus 37-45 8060524-3 1994 It has also been reported that when catalase activity is pharmacologically reduced, via 3-amino-1,2,4-triazole (AT), rats reduce their intake and preference for ethanol. Amitrole 88-110 catalase Rattus norvegicus 36-44 8280068-6 1993 Inhibition of catalase by 3-amino-1,2,4-triazole (0.2 mM) significantly increased the benzylamine-induced net K+ release as well as the benzylamine-induced release of GSSG into bile, but had no effect on benzylamine oxidation at monoamine oxidase. Amitrole 26-48 catalase Rattus norvegicus 14-22 8138192-5 1993 Additional controls included heart and kidney preparations from aminotriazole-treated (catalase-depleted) rats. Amitrole 64-77 catalase Rattus norvegicus 87-95 8400028-5 1993 Measurement of catalase activity showed significant inhibition in the 3-aminotriazole treated groups. Amitrole 70-85 catalase Rattus norvegicus 15-23 8168729-3 1993 Intracellular catalase was inhibited with 3-amino-1,2,4-triazole (ATZ, 1.5 g/kg body weight, two hours prior to heart perfusion). Amitrole 42-64 catalase Rattus norvegicus 14-22 8216172-8 1993 Combined treatment of myocytes with 3-amino-1,2,4-triazole, 1,3-bis(2-chloroethyl)-1-nitrosourea and diethyl maleate (to inactivate catalase, to inhibit glutathione reductase activity, and to deplete glutathione, respectively) enhanced the sensitivity of translocase to hydrogen peroxide, supporting the view that the cellular defense mechanism is a significant factor in determining the toxicity of hydrogen peroxide. Amitrole 36-58 catalase Rattus norvegicus 132-140 8380970-2 1993 Mitoplasts were prepared from hearts of aminotriazole-treated rats which displayed both an 80-90% reduction in matrix catalase activity and rate of H2O2 consumption. Amitrole 40-53 catalase Rattus norvegicus 118-126 8098954-3 1993 In combination with the catalase inhibitor aminotriazole, benzyl viologen again diminished, but markedly, the rat liver glutamine synthetase activity. Amitrole 43-56 catalase Rattus norvegicus 24-32 1627338-4 1992 To enable investigation of the glutathione redox cycle and catalase pathways, glutathione reductase was inactivated with 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU) and catalase was inactivated with aminotriazole. Amitrole 199-212 catalase Rattus norvegicus 169-177 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. Amitrole 45-58 catalase Rattus norvegicus 25-33 1407407-1 1992 The effects of the catalase inhibitor, 3-amino-1,2,4-triazole (AT), on maintenance of voluntary consumption of ethanol was tested in male Long-Evans rats. Amitrole 39-61 catalase Rattus norvegicus 19-27 1407407-1 1992 The effects of the catalase inhibitor, 3-amino-1,2,4-triazole (AT), on maintenance of voluntary consumption of ethanol was tested in male Long-Evans rats. Amitrole 63-65 catalase Rattus norvegicus 19-27 1767853-11 1991 However, inhibition of endogenous catalase activity by 3-amino-1,2,4-triazole did not significantly alter glucose oxidase- or nascent H2O2-induced 51Cr release. Amitrole 55-77 catalase Rattus norvegicus 34-42 1924513-3 1991 Rats were pretreated with the catalase inhibitor 3-amino-1,2,4-triazole (AT) or saline. Amitrole 49-71 catalase Rattus norvegicus 30-38 1757301-5 1991 In animals pretreated with ATZ, HBO inactivated 21-40% more catalase than air exposure in the six brain regions studied. Amitrole 27-30 catalase Rattus norvegicus 60-68 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. Amitrole 8-11 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. Amitrole 8-11 catalase Rattus norvegicus 82-90 1757301-7 1991 Pargyline, administered 30 min before HBO, inhibited MAO by greater than 90%, prevented ATZ inhibition of catalase activity during HBO, and reversed the augmentation of CNS O2 toxicity by ATZ. Amitrole 88-91 catalase Rattus norvegicus 106-114 1859472-0 1991 Dose- and time-dependent effect of an acute 3-amino-1,2,4-triazole injection on rat brain catalase activity. Amitrole 44-66 catalase Rattus norvegicus 90-98 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. Amitrole 0-13 catalase Rattus norvegicus 42-50 1872419-8 1991 Incubation of the cells with aminotriazole led to a rapid inhibition of catalase. Amitrole 29-42 catalase Rattus norvegicus 72-80 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. Amitrole 0-13 catalase Rattus norvegicus 37-45 1646749-3 1991 3-amino-1,2,4-triazole reacts with catalase to form irreversibly inactivated catalase only in the presence of hydrogen peroxide. Amitrole 0-22 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. Amitrole 0-22 catalase Rattus norvegicus 77-85 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. Amitrole 40-53 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. Amitrole 40-53 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. Amitrole 144-157 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. Amitrole 144-157 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. Amitrole 14-27 catalase Rattus norvegicus 87-95 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. Amitrole 31-46 catalase Rattus norvegicus 11-19 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. Amitrole 111-133 catalase Rattus norvegicus 0-8 1646749-9 1991 In control animals, aminotriazole caused a 53.4% decrease in catalase activity. Amitrole 20-33 catalase Rattus norvegicus 61-69 2285988-1 1990 3-Amino-1,2,4-triazole (aminotriazole) is an irreversible inhibitor of catalase which is a marker enzyme of peroxisomes. Amitrole 0-22 catalase Rattus norvegicus 71-79 2285988-1 1990 3-Amino-1,2,4-triazole (aminotriazole) is an irreversible inhibitor of catalase which is a marker enzyme of peroxisomes. Amitrole 24-37 catalase Rattus norvegicus 71-79 2285988-3 1990 When catalase activity of peroxisomes of rat liver was inhibited by aminotriazole treatment, bile acid content in the bile was significantly decreased to about 70% of the control, but that in the liver was not changed. Amitrole 68-81 catalase Rattus norvegicus 5-13 2285988-9 1990 These results indicate that when catalase activity of liver peroxisomes is suppressed by aminotriazole treatment, biosynthesis of bile acid from exogenous cholesterol is not inhibited, but a step in the pathway of biosynthesis of endogenous cholesterol from mevalonate is inhibited. Amitrole 89-102 catalase Rattus norvegicus 33-41 2325161-6 1990 NGF protection from hydrogen peroxide is partially abolished by aminotriazole (Az), a low molecular weight catalase inhibitor. Amitrole 64-77 catalase Rattus norvegicus 107-115 2325161-6 1990 NGF protection from hydrogen peroxide is partially abolished by aminotriazole (Az), a low molecular weight catalase inhibitor. Amitrole 79-81 catalase Rattus norvegicus 107-115 2782423-2 1989 Using this method, we found a significantly higher inhibition of renal catalase activity at various time points (30, 60, and 90 min) in glycerol-treated rats (a well-established model for myoglobinuric acute renal failure) compared with rats treated with aminotriazole alone. Amitrole 255-268 catalase Rattus norvegicus 71-79 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. Amitrole 43-56 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. Amitrole 43-56 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. Amitrole 43-56 catalase Rattus norvegicus 81-89 3355670-2 1988 The involvement of catalase was confirmed by its blocking by aminotriazole (AT) or methanol but not by pyrazole or butanol. Amitrole 61-74 catalase Rattus norvegicus 19-27 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. Amitrole 0-13 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. Amitrole 0-13 catalase Rattus norvegicus 165-173 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. Amitrole 128-141 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. Amitrole 128-141 catalase Rattus norvegicus 165-173 2912161-3 1989 Aminotriazole injected intraperitoneally caused a dose-dependent (0.1-1 g/kg) and a time-dependent (15, 30, 60, 90, 120 min) inhibition of the catalase activity in renal cortex. Amitrole 0-13 catalase Rattus norvegicus 143-151 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. Amitrole 43-56 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. Amitrole 43-56 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. Amitrole 43-56 catalase Rattus norvegicus 83-91 2912161-6 1989 The residual catalase activity (RCA) in the glomeruli (0.05 +/- 0.01 k/mg protein) was 19% of control values at 90 min after aminotriazole injection (1 g/kg). Amitrole 125-138 catalase Rattus norvegicus 13-21 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. Amitrole 0-13 catalase Rattus norvegicus 37-45 3416882-8 1988 The increase in 4-methylpyrazole-insensitive ethanol uptake by fatty acids was blocked by the catalase inhibitor, aminotriazole, indicating the involvement of catalase. Amitrole 114-127 catalase Rattus norvegicus 94-102 3416882-8 1988 The increase in 4-methylpyrazole-insensitive ethanol uptake by fatty acids was blocked by the catalase inhibitor, aminotriazole, indicating the involvement of catalase. Amitrole 114-127 catalase Rattus norvegicus 159-167 3355670-2 1988 The involvement of catalase was confirmed by its blocking by aminotriazole (AT) or methanol but not by pyrazole or butanol. Amitrole 76-78 catalase Rattus norvegicus 19-27 3169364-11 1988 Acute and chronic aminotriazole injections led to catalase inactivation and in the latter case also to inhibition of the liver superoxide dismutase and glutathione peroxidase activities. Amitrole 18-31 catalase Rattus norvegicus 50-58 3271871-6 1986 Aminotriazole (3-amino-1H-1,2,4-triazole) (50 mM) completely inhibited only mercury-oxidizing activity; some residual catalase activity was found in the aminotriazole-treated homogenate. Amitrole 0-13 catalase Rattus norvegicus 118-126 3720947-2 1986 Treatment of rats with aminotriazole in vivo inhibited heart catalase by 83% and shifted the dose-response curve for GSSG release toward lower H2O2 concentrations. Amitrole 23-36 catalase Rattus norvegicus 61-69 3445547-0 1987 [Effect of ethanol and the catalase inhibitor aminotriazole on the activity of antioxidative enzymes in the rat liver and heart]. Amitrole 46-59 catalase Rattus norvegicus 27-35 2887206-1 1987 Catalase activity was inhibited by aminotriazole administration to rats in order to evaluate the influence of catalase on the peroxisomal fatty acyl-CoA beta-oxidation system. Amitrole 35-48 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. Amitrole 235-257 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. Amitrole 207-229 catalase Rattus norvegicus 6-14 3567333-0 1987 [Effect of ethanol and the catalase inhibitor aminotriazole on lipid peroxidation in the rat myocardium]. Amitrole 46-59 catalase Rattus norvegicus 27-35 3567333-1 1987 The influence of chronic alcohol consumption and catalase inhibitor aminotriazole administration on the level of nonenzymatic lipid peroxidation has been studied in the rat myocardium. Amitrole 68-81 catalase Rattus norvegicus 49-57 3828063-3 1987 On the opposite, the presence of 3-amino-1,2,4-triazole (10 to 40 mM), a known catalase inhibitor, induced a concentration dependent reduction of the amount of AcH recovered during incubation even in presence of glucose oxidase. Amitrole 33-55 catalase Rattus norvegicus 79-87 3271871-6 1986 Aminotriazole (3-amino-1H-1,2,4-triazole) (50 mM) completely inhibited only mercury-oxidizing activity; some residual catalase activity was found in the aminotriazole-treated homogenate. Amitrole 153-166 catalase Rattus norvegicus 118-126 6846030-2 1983 Catalase activity was inhibited by aminotriazole either by intraperitoneal injections affecting catalase in most tissues of the animal or by intraventricular injections affecting catalase in the brain selectively. Amitrole 35-48 catalase Rattus norvegicus 0-8 2999539-0 1985 Blockade of ethanol induced conditioned taste aversion by 3-amino-1,2,4-triazole: evidence for catalase mediated synthesis of acetaldehyde in rat brain. Amitrole 58-80 catalase Rattus norvegicus 95-103 2999539-3 1985 Pretreatment with the catalase inhibitor, 3-amino-1,2,4-triazole (AT), shows an attenuation of this ethanol-induced CTA. Amitrole 42-64 catalase Rattus norvegicus 22-30 2999539-3 1985 Pretreatment with the catalase inhibitor, 3-amino-1,2,4-triazole (AT), shows an attenuation of this ethanol-induced CTA. Amitrole 66-68 catalase Rattus norvegicus 22-30 6530393-6 1984 When the catalase activity of liver peroxisomes was irreversibly inhibited by administration of 3-amino-1,2,4-triazole (amino-triazole), the biosynthesis of bile acids was suppressed to about one-third, and the serum cholesterol level was increased. Amitrole 96-118 catalase Rattus norvegicus 9-17 6530393-6 1984 When the catalase activity of liver peroxisomes was irreversibly inhibited by administration of 3-amino-1,2,4-triazole (amino-triazole), the biosynthesis of bile acids was suppressed to about one-third, and the serum cholesterol level was increased. Amitrole 120-134 catalase Rattus norvegicus 9-17 6846030-6 1983 Contrary to the intraventricular injection of aminotriazole, in animals receiving aminotriazole intraperitoneally prior to elemental mercury injection, we suggest that the lower activity of brain catalase is compensated by an increased supply of elemental mercury caused by the generally lower oxidation rate in the animal. Amitrole 82-95 catalase Rattus norvegicus 196-204 6846030-2 1983 Catalase activity was inhibited by aminotriazole either by intraperitoneal injections affecting catalase in most tissues of the animal or by intraventricular injections affecting catalase in the brain selectively. Amitrole 35-48 catalase Rattus norvegicus 96-104 7143231-6 1982 Studies in rats treated with 3-aminotriazole indicated that alcohol probably also acted by inhibition of catalase-mediated oxidation of mercury vapor. Amitrole 29-44 catalase Rattus norvegicus 105-113 6802838-9 1982 Inactivation of catalase by 3-amino-1,2,4-triazole was accompanied by loss of ferroactivator activity as well. Amitrole 28-50 catalase Rattus norvegicus 16-24 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. Amitrole 0-22 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. Amitrole 0-22 catalase Rattus norvegicus 280-288 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. Amitrole 75-90 catalase Rattus norvegicus 56-64 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. Amitrole 81-103 catalase Rattus norvegicus 61-69 7004234-4 1980 The irreversible inhibition of catalase by aminotriazole is known to proceed via the reaction of (catalase-H2O2) compound I with aminotriazole. Amitrole 43-56 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. Amitrole 43-56 catalase Rattus norvegicus 98-106 7004234-4 1980 The irreversible inhibition of catalase by aminotriazole is known to proceed via the reaction of (catalase-H2O2) compound I with aminotriazole. Amitrole 129-142 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. Amitrole 129-142 catalase Rattus norvegicus 98-106 4426896-0 1974 Synthesis of catalase in liver slices from aminotriazole-pretreated rats. Amitrole 43-56 catalase Rattus norvegicus 13-21 30981876-5 2019 Aminotriazole (a catalase inhibitor), however, completely inhibited the stimulation. Amitrole 0-13 catalase Rattus norvegicus 17-25 30157459-8 2018 Conversely, inhibition of catalase with aminotriazole decreased phenylephrine-induced contraction in aortas from ethanol-treated rats. Amitrole 40-53 catalase Rattus norvegicus 26-34 30269681-0 2018 Inhibition of catalase activity with 3-amino-1,2,4-triazole intensifies bisphenol A (BPA)-induced toxicity in granulosa cells of female albino rats. Amitrole 37-59 catalase Rattus norvegicus 14-22 30269681-3 2018 Eight-week-old female Wistar rats were treated with BPA (25 mg/kg BW/day for 9 days, intraperitonially) with or without pretreatment of the catalase-specific blocker 3-amino-1,2,4-triazole (ATZ; 1 g/kg BW/day for 5 days, intraperitonially). Amitrole 166-188 catalase Rattus norvegicus 140-148 30269681-10 2018 Results of Western blot analysis demonstrated decreased expression of catalase in the BPA-treated group and a further decrease in expression in the group treated with both BPA and ATZ. Amitrole 180-183 catalase Rattus norvegicus 70-78 28527616-7 2017 Conversely, aminotriazole, a catalase inhibitor, completely abolished the effect, pointing out that this enhanced ethanol oxidation is mediated by catalase activity. Amitrole 12-25 catalase Rattus norvegicus 29-37 28527616-7 2017 Conversely, aminotriazole, a catalase inhibitor, completely abolished the effect, pointing out that this enhanced ethanol oxidation is mediated by catalase activity. Amitrole 12-25 catalase Rattus norvegicus 147-155 240743-5 1975 4-Methylpyrazole and aminotriazole are specific inhibitors for alcohol dehydrogenase and catalase, respectively, under these conditions. Amitrole 21-34 catalase Rattus norvegicus 89-97 166481-5 1975 Sodium citrate and aminotriazole and feeding decrease also the activity of hepatic catalase in rats fed ASA. Amitrole 19-32 catalase Rattus norvegicus 83-91 4727356-0 1973 Differential effect of 3-amino-1,2,4-triazole on multiple forms of rat liver catalase. Amitrole 23-45 catalase Rattus norvegicus 77-85 5783872-6 1969 (11), the half-life of catalase derived from the rate of recovery from aminotriazole inhibition was about 11(1/2) days, as was the apparent half-life of the heme prosthetic groups measured with (14)C-alpha-aminolevulinic acid. Amitrole 71-84 catalase Rattus norvegicus 23-31 31545999-1 2019 Intracerebroventricular (icv) injection of hydrogen peroxide (H2O2), a reactive oxygen species, or the blockade of catalase (enzyme that degrades H2O2 into H2O and O2) with icv injection of 3-amino-1,2,4-triazole (ATZ) reduces the pressor effects of angiotensin II also injected icv. Amitrole 190-212 catalase Rattus norvegicus 115-123 31545999-1 2019 Intracerebroventricular (icv) injection of hydrogen peroxide (H2O2), a reactive oxygen species, or the blockade of catalase (enzyme that degrades H2O2 into H2O and O2) with icv injection of 3-amino-1,2,4-triazole (ATZ) reduces the pressor effects of angiotensin II also injected icv. Amitrole 214-217 catalase Rattus norvegicus 115-123 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. Amitrole 75-90 catalase Rattus norvegicus 151-159 25672632-8 2015 Furthermore, ATZ inhibited the activity of CAT, reduced hepatic levels of H2O2and MDA in alcohol exposed rats. Amitrole 13-16 catalase Rattus norvegicus 43-46 25672632-0 2015 [The catalase inhibitor aminotriazole alleviates acute alcoholic liver injury]. Amitrole 24-37 catalase Rattus norvegicus 5-13 25298180-3 2014 Thus, in the present work, we examined the effects of the daily administration of the CAT inhibitor, 3-amino-1,2,4-triazole (1 mg/g), on the hearts of streptozotocin (STZ)-induced diabetic rats. Amitrole 101-123 catalase Rattus norvegicus 86-89