PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset
20837563-10 2010 Administration of ethanol and AFB1 separately resulted in significant decrease in both non-enzymatic antioxidant glutathione (GSH) level and enzymatic antioxidant catalase (CAT) and glutathione-S-transferase (GST) activities, whereas lipid peroxidation was markedly elevated. Ethanol 18-25 catalase Mus musculus 163-171
21457746-6 2011 Moreover, CISE treatment with ethanol decreased CYP2E1 expression and increased activities of catalase and superoxide dismutase, which were significantly inhibited by treatment with ethanol alone. Ethanol 30-37 catalase Mus musculus 94-102
21457746-6 2011 Moreover, CISE treatment with ethanol decreased CYP2E1 expression and increased activities of catalase and superoxide dismutase, which were significantly inhibited by treatment with ethanol alone. Ethanol 182-189 catalase Mus musculus 94-102
22554647-5 2012 In addition, taraxerone prevented catalase, superoxide dismutase, and reduced glutathione concentrations from the decrease induced by ethanol administration with the concentration dependent manner. Ethanol 134-141 catalase Mus musculus 34-42
20837563-10 2010 Administration of ethanol and AFB1 separately resulted in significant decrease in both non-enzymatic antioxidant glutathione (GSH) level and enzymatic antioxidant catalase (CAT) and glutathione-S-transferase (GST) activities, whereas lipid peroxidation was markedly elevated. Ethanol 18-25 catalase Mus musculus 173-176
20837563-12 2010 Co-exposure of animals to ethanol and AFB1 showed additive effects on the activities of GST and CAT as well as on the GSH level. Ethanol 26-33 catalase Mus musculus 96-99
20347918-5 2010 When compared to the ethanol-alone treated group, the mice receiving ethanol plus TOH exhibited significant increases in hepatic antioxidant activities, including catalase, glutathione-S-transferase, glutathione peroxidase, glutathione reductase, and glutathione. Ethanol 69-76 catalase Mus musculus 163-171
21086752-3 2010 Ethanol (1.6 g/kg body wt/day) exposure for 12 wks significantly increased TBARS and nitrite levels and GST activity, and significantly decreased GSH content and the activities of SOD, CAT, GR and GPx in whole blood hemolyzate of 8-10 wks-old male BALB/c mice (weighing 20-30 g). Ethanol 0-7 catalase Mus musculus 185-188
20397104-6 2010 Besides this, the ethanol extracts from the DMCB treatment significantly increased catalase, superoxide dismutase and glutathione peroxidase activities, except for decreasing the maleic dialdehyde level in diabetic mice. Ethanol 18-25 catalase Mus musculus 83-91
18975145-4 2008 The cultured lichen extract also showed hepatoprotection against ethanol-induced toxicity in the mice liver slice culture model by a significant decrease in the antioxidant enzymes, glutathione peroxidase, catalase, and superoxide dismutase, along with a decrease in lipid peroxidation and lactate dehydrogenase release. Ethanol 65-72 catalase Mus musculus 206-214
19386791-8 2009 Examples include significant inductions of catalase and glutathione transferase activity in ethanol-fed KO and TG mice, along with elevated levels of glutathione peroxidase activity. Ethanol 92-99 catalase Mus musculus 43-51
19398231-3 2009 METHODS: Ethanol (5 g/kg) was administered orally to the wild-type and the Gpx-1(-/-)/Cat(-/-) mice every 12 h for a total of three doses. Ethanol 9-16 catalase Mus musculus 86-89
19398231-7 2009 Ethanol administration to the Gpx-1(-/-)/Cat(-/-) mice increased the elevation of serum alanine aminotransferase activity, plasma homocysteine levels, hepatic fat accumulation and lipid peroxidation compared with the wild-type animals challenged with ethanol. Ethanol 0-7 catalase Mus musculus 41-44
19398231-7 2009 Ethanol administration to the Gpx-1(-/-)/Cat(-/-) mice increased the elevation of serum alanine aminotransferase activity, plasma homocysteine levels, hepatic fat accumulation and lipid peroxidation compared with the wild-type animals challenged with ethanol. Ethanol 251-258 catalase Mus musculus 41-44
19398231-9 2009 CONCLUSIONS: The results indicate that Gpx-1 and Cat have critical roles in the protection of liver against binge ethanol exposure. Ethanol 114-121 catalase Mus musculus 49-52
19398231-10 2009 Augmentation of ethanol-induced oxidative stress may be responsible for the impairment of the transsulfuration reactions and the aggravation of acute liver injury in the Gpx-1(-/-)/Cat(-/-) mice. Ethanol 16-23 catalase Mus musculus 181-184
19177030-2 2009 Catalase has been proposed as the main enzyme responsible for the synthesis of acetaldehyde from ethanol in the brain. Ethanol 97-104 catalase Mus musculus 0-8
18222027-4 2008 Ethanol treatment increased malondialdehyde (MDA) level, decreased glutathione (GSH) content and catalase and glutathione peroxidase (GPX) activities, and increased cytochrome P450 2E1 (CYP2E1) activity in liver (P<0.05). Ethanol 0-7 catalase Mus musculus 97-105
18222027-7 2008 Ethanol treatment caused down-regulation in both catalase and GPX mRNA expression, and up-regulated both IL-6 and TNF-alpha mRNA expression (P<0.05). Ethanol 0-7 catalase Mus musculus 49-57
18761051-10 2008 The activities of some antioxidant enzymes (such as SOD, GPx and Catalase) were modified by ethanol, MDMA and their joint action. Ethanol 92-99 catalase Mus musculus 65-73
19706976-4 2008 Ethanol also enhanced the formation of malondialdehyde (MDA) and protein carbonyls in the liver, whereas ethanol treatment resulted in significantly lower activity of hepatic glutathione peroxidase (GPx), catalase and superoxide dismutase (SOD). Ethanol 105-112 catalase Mus musculus 205-213
18155096-0 2008 Involvement of brain catalase activity in the acquisition of ethanol-induced conditioned place preference. Ethanol 61-68 catalase Mus musculus 21-29
18155096-2 2008 The present research addressed the hypothesis that catalase-dependent metabolism of ethanol to acetaldehyde in the brain is an important step in the production of ethanol-related affective properties. Ethanol 84-91 catalase Mus musculus 51-59
18155096-2 2008 The present research addressed the hypothesis that catalase-dependent metabolism of ethanol to acetaldehyde in the brain is an important step in the production of ethanol-related affective properties. Ethanol 163-170 catalase Mus musculus 51-59
18155096-3 2008 Firstly, we investigated the contribution of brain catalase in the acquisition of ethanol-induced conditioned place preference (CPP). Ethanol 82-89 catalase Mus musculus 51-59
18155096-9 2008 Taken together, the results of the present study indicate that the brain catalase-H(2)O(2) system contributes to the acquisition of affective-dependent learning induced by ethanol, and support the involvement of centrally-formed acetaldehyde in the formation of positive affective memories produced by ethanol. Ethanol 172-179 catalase Mus musculus 73-81
18155096-9 2008 Taken together, the results of the present study indicate that the brain catalase-H(2)O(2) system contributes to the acquisition of affective-dependent learning induced by ethanol, and support the involvement of centrally-formed acetaldehyde in the formation of positive affective memories produced by ethanol. Ethanol 302-309 catalase Mus musculus 73-81
12474118-0 2002 Ethanol-stimulated behaviour in mice is modulated by brain catalase activity and H2O2 rate of production. Ethanol 0-7 catalase Mus musculus 59-67
16344722-10 2006 CONCLUSIONS: Although the contribution of CYP2E1 and catalase in ethanol oxidation may be of little significance, these enzymes appear to play a significant role in ethanol sensitivity in the brain. Ethanol 65-72 catalase Mus musculus 53-61
16109828-0 2005 Cardiac overexpression of catalase antagonizes ADH-associated contractile depression and stress signaling after acute ethanol exposure in murine myocytes. Ethanol 118-125 catalase Mus musculus 26-34
16109828-2 2005 This study was designed to examine the impact of antioxidant catalase (CAT) on cardiac contractile response to ethanol and activation of stress signaling. Ethanol 111-118 catalase Mus musculus 61-69
16109828-2 2005 This study was designed to examine the impact of antioxidant catalase (CAT) on cardiac contractile response to ethanol and activation of stress signaling. Ethanol 111-118 catalase Mus musculus 71-74
16109828-9 2005 Interestingly, myocytes from CAT-ADH mice displayed normal ethanol response with maximal inhibitions of 46.0 and 47.2% for cell shortening and intracellular Ca(2+), respectively. Ethanol 59-66 catalase Mus musculus 29-32
16109828-10 2005 CAT transgene lessened ethanol-induced inhibition on cell shortening (maximal inhibition of 30.3%) but not intracellular Ca(2+). Ethanol 23-30 catalase Mus musculus 0-3
16109828-11 2005 ADH amplified ethanol-induced reactive oxygen species generation, which was nullified by the CAT transgene. Ethanol 14-21 catalase Mus musculus 93-96
16109828-15 2005 These data suggest that antioxidant CAT may effectively antagonize ADH-induced enhanced cardiac depression in response to ethanol. Ethanol 122-129 catalase Mus musculus 36-39
16102377-0 2005 Brain catalase mediates potentiation of social recognition memory produced by ethanol in mice. Ethanol 78-85 catalase Mus musculus 6-14
16102377-1 2005 The involvement of catalase in ethanol-induced locomotion has been clearly proven. Ethanol 31-38 catalase Mus musculus 19-27
16102377-12 2005 The present results suggest that brain catalase activity could mediate the memory-enhancing capacity of ethanol and add further support to the idea that this enzyme mediates some of the psychopharmacological effects produced by ethanol. Ethanol 104-111 catalase Mus musculus 39-47
16102377-12 2005 The present results suggest that brain catalase activity could mediate the memory-enhancing capacity of ethanol and add further support to the idea that this enzyme mediates some of the psychopharmacological effects produced by ethanol. Ethanol 228-235 catalase Mus musculus 39-47
14519943-2 2003 Pretreatment (quercetin 25, 50 and 75 mg/kg body weight for 15 d+co-treatment of ethanol 18%+quercetin for 15 d and ethanol 18% for the 15 d) increased the activities of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), glutathione reductase (GR), and glutathione (GSH) in comparison to the ethanol group. Ethanol 81-88 catalase Mus musculus 198-206
14519943-2 2003 Pretreatment (quercetin 25, 50 and 75 mg/kg body weight for 15 d+co-treatment of ethanol 18%+quercetin for 15 d and ethanol 18% for the 15 d) increased the activities of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), glutathione reductase (GR), and glutathione (GSH) in comparison to the ethanol group. Ethanol 81-88 catalase Mus musculus 208-211
14519943-2 2003 Pretreatment (quercetin 25, 50 and 75 mg/kg body weight for 15 d+co-treatment of ethanol 18%+quercetin for 15 d and ethanol 18% for the 15 d) increased the activities of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), glutathione reductase (GR), and glutathione (GSH) in comparison to the ethanol group. Ethanol 116-123 catalase Mus musculus 198-206
14519943-2 2003 Pretreatment (quercetin 25, 50 and 75 mg/kg body weight for 15 d+co-treatment of ethanol 18%+quercetin for 15 d and ethanol 18% for the 15 d) increased the activities of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), glutathione reductase (GR), and glutathione (GSH) in comparison to the ethanol group. Ethanol 116-123 catalase Mus musculus 208-211
14519943-2 2003 Pretreatment (quercetin 25, 50 and 75 mg/kg body weight for 15 d+co-treatment of ethanol 18%+quercetin for 15 d and ethanol 18% for the 15 d) increased the activities of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), glutathione reductase (GR), and glutathione (GSH) in comparison to the ethanol group. Ethanol 116-123 catalase Mus musculus 198-206
14519943-2 2003 Pretreatment (quercetin 25, 50 and 75 mg/kg body weight for 15 d+co-treatment of ethanol 18%+quercetin for 15 d and ethanol 18% for the 15 d) increased the activities of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), glutathione reductase (GR), and glutathione (GSH) in comparison to the ethanol group. Ethanol 116-123 catalase Mus musculus 208-211
16930212-10 2006 The highest levels of ethanol oxidation were found in microsomal and peroxisomal subcellular brain fractions, where CYP2E1 and catalase are located, respectively. Ethanol 22-29 catalase Mus musculus 127-135
16930212-11 2006 CONCLUSIONS: Catalase is the key enzyme of ethanol oxidation in the brain of rodents: it may be responsible for about 60% of the process. Ethanol 43-50 catalase Mus musculus 13-21
16344722-0 2006 CYP2E1 and catalase influence ethanol sensitivity in the central nervous system. Ethanol 30-37 catalase Mus musculus 11-19
16344722-2 2006 Ethanol is metabolized to acetaldehyde mainly by the alcohol dehydrogenase pathway (ADHs) and, to a lesser extent, by microsomal oxidization (CYP2E1) and the catalase-H2O2 system. Ethanol 0-7 catalase Mus musculus 158-166
16269173-3 2005 In mice, catalase is involved in ethanol and methanol metabolism, but not in the metabolism of other alcohols such as 1-propanol or tert-butanol. Ethanol 33-40 catalase Mus musculus 9-17
16269173-12 2005 These results support the hypothesis that the effects of lead treatment on ethanol-induced behaviors are related to changes in catalase activity, rather than some nonspecific effect that generalizes to all alcohols. Ethanol 75-82 catalase Mus musculus 127-135
15608607-0 2004 Brain catalase activity inhibition as well as opioid receptor antagonism increases ethanol-induced HPA axis activation. Ethanol 83-90 catalase Mus musculus 6-14
15608607-1 2004 BACKGROUND: Growing evidence indicates that brain catalase activity is involved in the psychopharmacological actions of ethanol. Ethanol 120-127 catalase Mus musculus 50-58
15608607-3 2004 The present study assessed whether brain catalase has a role in ethanol-induced activation of the HPA axis, a neuroendocrine system modulated by the endogenous opioid neurotransmission. Ethanol 64-71 catalase Mus musculus 41-49
15608607-6 2004 In addition, we tested the effects of 45 mg/kg of cyanamide (another catalase inhibitor) and 0 to 2 mg/kg of naltrexone (nonselective opioid receptor antagonist) on ethanol-induced enhancement in plasma corticosterone values. Ethanol 165-172 catalase Mus musculus 69-77
15608607-9 2004 The catalase inhibitor cyanamide (45 mg/kg, intraperitoneally) also increased ethanol-related plasma corticosterone levels. Ethanol 78-85 catalase Mus musculus 4-12
15608607-10 2004 These effects of AT and cyanamide on ethanol-induced corticosterone values were observed under treatment conditions that decreased significantly brain catalase activity. Ethanol 37-44 catalase Mus musculus 151-159
15608607-13 2004 CONCLUSIONS: This study shows that the inhibition of brain catalase increases ethanol-induced plasma corticosterone levels. Ethanol 78-85 catalase Mus musculus 59-67
14703737-8 2003 Chronic ethanol administration to young mice produced an increase in lipid peroxidation, and a decline in forebrain total glutathione (GSH), SOD and catalase levels, which was significantly reversed by the co-administration of quercetin (10, 25 and 50 mg/kg). Ethanol 8-15 catalase Mus musculus 149-157
12788382-0 2003 Cardiac-specific overexpression of catalase rescues ventricular myocytes from ethanol-induced cardiac contractile defect. Ethanol 78-85 catalase Mus musculus 35-43
12788382-2 2003 Catalase is responsible for detoxification of hydrogen peroxide (H(2)O(2)) and may interfere with ethanol-induced cardiac toxicity. Ethanol 98-105 catalase Mus musculus 0-8
12788382-12 2003 In conclusion, our data suggest that catalase overexpression may protect cardiac myocytes from ethanol-induced contractile defect, partially through improved intracellular Ca(2+) handling and Akt signaling. Ethanol 95-102 catalase Mus musculus 37-45
12474118-1 2002 RATIONALE: Over the last few years, a role for the brain catalase-H(2)O(2) enzymatic system has been suggested in the behavioural effects observed in rodents after ethanol administration. Ethanol 164-171 catalase Mus musculus 57-65
12474118-2 2002 This role seems to be related to the ability of cerebral catalase to metabolise ethanol to acetaldehyde using H(2)O(2)as a co-substrate. Ethanol 80-87 catalase Mus musculus 57-65
12474118-4 2002 Thus, substrate-level changes could regulate brain catalase activity, thereby modulating the behavioural effects of ethanol. Ethanol 116-123 catalase Mus musculus 51-59
12474118-11 2002 Therefore, this study provides further support for the notion that the brain catalase-H(2)O(2) system, and by implication centrally formed acetaldehyde, plays a key role in the mediation of ethanol"s psychopharmacological effects. Ethanol 190-197 catalase Mus musculus 77-85
11821648-0 2002 Gene coding variant in Cas1 between the C57BL/6J and DBA/2J inbred mouse strains: linkage to a QTL for ethanol-induced locomotor activation. Ethanol 103-110 catalase Mus musculus 23-27
10487386-0 1999 The catalase inhibitor sodium azide reduces ethanol-induced locomotor activity. Ethanol 44-51 catalase Mus musculus 4-12
11495670-0 2001 Brain catalase activity is highly correlated with ethanol-induced locomotor activity in mice. Ethanol 50-57 catalase Mus musculus 6-14
11495670-3 2001 In the present study, in an attempt to further evaluate the relation between brain catalase activity and lead-induced changes in ethanol-stimulated locomotion, the interaction between lead acetate and 3-amino-1H,2,4-triazole (AT), a well-known catalase inhibitor, was assessed. Ethanol 129-136 catalase Mus musculus 83-91
11495670-12 2001 The results show that brain catalase activity is involved in the effects of lead acetate on ethanol-induced locomotion in mice. Ethanol 92-99 catalase Mus musculus 28-36
11495670-13 2001 Thus, this study confirms the notion that brain catalase provides the molecular basis for understanding some of the mechanisms of the action of ethanol in the central nervous system. Ethanol 144-151 catalase Mus musculus 48-56
10837853-2 2000 Other reports have shown a role of brain catalase in ethanol-induced behaviors. Ethanol 53-60 catalase Mus musculus 41-49
10837853-10 2000 The fact that brain catalase and ethanol-induced locomotor activity followed a similar pattern could suggest a relationship between both lead acetate effects and also a role for brain catalase in ethanol-induced behaviors. Ethanol 33-40 catalase Mus musculus 184-192
10837853-10 2000 The fact that brain catalase and ethanol-induced locomotor activity followed a similar pattern could suggest a relationship between both lead acetate effects and also a role for brain catalase in ethanol-induced behaviors. Ethanol 196-203 catalase Mus musculus 20-28
10837853-10 2000 The fact that brain catalase and ethanol-induced locomotor activity followed a similar pattern could suggest a relationship between both lead acetate effects and also a role for brain catalase in ethanol-induced behaviors. Ethanol 196-203 catalase Mus musculus 184-192
10780252-1 1999 A role for brain catalase in the mediation of some psychopharmacological effects of ethanol has been proposed. Ethanol 84-91 catalase Mus musculus 17-25
10780252-12 1999 Furthermore, the present study provides further support for the notion that brain catalase activity may be a factor mediating some of the psychopharmacological effects of ethanol. Ethanol 171-178 catalase Mus musculus 82-90
11714585-0 2001 Influence of brain catalase on ethanol-induced loss of righting reflex in mice. Ethanol 31-38 catalase Mus musculus 19-27
11714585-8 2001 These results suggest that brain catalase activity, and by implication centrally formed acetaldehyde, may modulate ethanol-induced LORR. Ethanol 115-122 catalase Mus musculus 33-41
10487386-1 1999 The involvement of brain catalase in modulating the psychopharmacological effects of ethanol was investigated by examining ethanol-induced locomotor activity in sodium azide-treated mice. Ethanol 85-92 catalase Mus musculus 25-33
10487386-9 1999 However, this catalase inhibitor significantly reduced ethanol-induced locomotor activity when it was injected simultaneously or 30 min before ethanol injections. Ethanol 55-62 catalase Mus musculus 14-22
10487386-9 1999 However, this catalase inhibitor significantly reduced ethanol-induced locomotor activity when it was injected simultaneously or 30 min before ethanol injections. Ethanol 143-150 catalase Mus musculus 14-22
10487386-14 1999 These results provide further support for the involvement of brain catalase in ethanol-induced behavioral effects. Ethanol 79-86 catalase Mus musculus 67-75
10487387-0 1999 Effects of chronic lead administration on ethanol-induced locomotor and brain catalase activity. Ethanol 42-49 catalase Mus musculus 78-86
10487387-2 1999 Other reports have shown a role of brain catalase on ethanol-induced behaviors. Ethanol 53-60 catalase Mus musculus 41-49
10487387-12 1999 The fact that brain catalase and ethanol-induced locomotor activity followed a similar pattern could suggest a relationship between both lead acetate effects and also a role for brain catalase in ethanol-induced behaviors. Ethanol 33-40 catalase Mus musculus 184-192
10487387-12 1999 The fact that brain catalase and ethanol-induced locomotor activity followed a similar pattern could suggest a relationship between both lead acetate effects and also a role for brain catalase in ethanol-induced behaviors. Ethanol 196-203 catalase Mus musculus 20-28
10487387-12 1999 The fact that brain catalase and ethanol-induced locomotor activity followed a similar pattern could suggest a relationship between both lead acetate effects and also a role for brain catalase in ethanol-induced behaviors. Ethanol 196-203 catalase Mus musculus 184-192
10379628-1 1999 The present study was designed in an attempt to assess a previously suggested role of brain catalase activity in ethanol-induced behaviour by examining ethanol-induced locomotor activity in cyanamide-treated mice. Ethanol 113-120 catalase Mus musculus 92-100
10371398-1 1999 It has been proposed that brain catalase plays a role in the modulation of some psychopharmacological effects of ethanol. Ethanol 113-120 catalase Mus musculus 32-40
10371398-12 1999 These data suggest that brain catalase is involved in ethanol"s effects. Ethanol 54-61 catalase Mus musculus 30-38
10379628-1 1999 The present study was designed in an attempt to assess a previously suggested role of brain catalase activity in ethanol-induced behaviour by examining ethanol-induced locomotor activity in cyanamide-treated mice. Ethanol 152-159 catalase Mus musculus 92-100
10379628-7 1999 Moreover, an additive effect of cyanamide and another brain catalase inhibitor, 3-amino-1,2,4-triazole (AT), on the reduction of ethanol-induced locomotor activity was observed. Ethanol 129-136 catalase Mus musculus 60-68
10379628-10 1999 These results suggest that cyanamide could reduce locomotor activity through its inhibition of brain catalase, giving further support to the notion that brain catalase may be an important regulator of some ethanol-induced behavioural effects. Ethanol 206-213 catalase Mus musculus 101-109
10379628-10 1999 These results suggest that cyanamide could reduce locomotor activity through its inhibition of brain catalase, giving further support to the notion that brain catalase may be an important regulator of some ethanol-induced behavioural effects. Ethanol 206-213 catalase Mus musculus 159-167
9167939-1 1997 Multiplicity of catalase activity has been observed in crude homogenates from the tissue and cell lines of mouse liver by ethanol/Triton X-100/heat treatment. Ethanol 122-129 catalase Mus musculus 16-24
21528208-0 1997 Peroxisome proliferators increase ethanol catabolism through utilization of the catalase pathway. Ethanol 34-41 catalase Mus musculus 80-88
21528208-5 1997 Our study suggests that peroxisome proliferators increase ethanol catabolism through hydrogen peroxide production, thus allowing utilization of the catalase pathway. Ethanol 58-65 catalase Mus musculus 148-156
21528208-6 1997 These findings indicate that catalase has the potential to provide a significant pathway for ethanol metabolism under conditions of peroxisome proliferation. Ethanol 93-100 catalase Mus musculus 29-37
9167939-3 1997 Cultured mouse liver cell lines, mouse liver tissue homogenate, and pure mouse liver catalase showed only one catalase band (CAT1) after ethanol/Triton X-100 treatment at 4 degrees C for 72 hr. Ethanol 137-144 catalase Mus musculus 85-93
9167939-3 1997 Cultured mouse liver cell lines, mouse liver tissue homogenate, and pure mouse liver catalase showed only one catalase band (CAT1) after ethanol/Triton X-100 treatment at 4 degrees C for 72 hr. Ethanol 137-144 catalase Mus musculus 110-118
8060524-0 1994 Effects of 3-amino-1,2,4-triazole on brain catalase in the mediation of ethanol consumption in mice. Ethanol 72-79 catalase Mus musculus 43-51
8060524-1 1994 Research has suggested that catalase plays a role in mediating ethanol"s psychopharmacological effects. Ethanol 63-70 catalase Mus musculus 28-36
8060524-10 1994 These results suggest a role for brain catalase in ethanol consumption across a variety of strains and species and further support the involvement of centrally formed acetaldehyde in the mediation of ethanol"s psychopharmacological effects. Ethanol 51-58 catalase Mus musculus 39-47
8060524-10 1994 These results suggest a role for brain catalase in ethanol consumption across a variety of strains and species and further support the involvement of centrally formed acetaldehyde in the mediation of ethanol"s psychopharmacological effects. Ethanol 200-207 catalase Mus musculus 39-47
8279661-9 1993 In addition, MAIDS infection inhibited an ETOH-induced increase in catalase and GT activities. Ethanol 42-46 catalase Mus musculus 67-75
8489262-6 1993 In this study, methanol, a selective substrate for catalase in rodents, was compared with ethanol. Ethanol 16-23 catalase Mus musculus 51-59
8489262-0 1993 Evidence that catalase is a major pathway of ethanol oxidation in vivo: dose-response studies in deer mice using methanol as a selective substrate. Ethanol 45-52 catalase Mus musculus 14-22
8489262-12 1993 The catalase inhibitor aminotriazole decreased ethanol and methanol metabolism 75% in ADH- deer mice. Ethanol 47-54 catalase Mus musculus 4-12
8489262-17 1993 The contribution of catalase was about 50% in the ADH+ mutant at low doses of ethanol and approached 100% as the alcohol concentration was elevated. Ethanol 78-85 catalase Mus musculus 20-28
8451258-1 1993 In studies designed to further examine the previously reported involvement of catalase in ethanol-induced effects, we attempted to confirm earlier observations by using normal (C3H-N) and acatalasemic (C3H-A) mice. Ethanol 90-97 catalase Mus musculus 78-86
8451258-12 1993 Together, these results provide strong support for the involvement of brain catalase in a variety of ethanol-induced behavioral effects. Ethanol 101-108 catalase Mus musculus 76-84
34182490-5 2021 RESULTS: Ethanol increased the production of reactive oxygen species and nitric oxide, decreased glutathione content, and lowered the activity of glutathione peroxide, glutathione reductase and catalase. Ethanol 9-16 catalase Mus musculus 194-202
8471082-3 1993 Ethanol is oxidized to acetaldehyde by alcohol dehydrogenase, catalase and the microsomal ethanol oxidizing system (MEOS). Ethanol 0-7 catalase Mus musculus 62-70
1898039-1 1991 The purpose of this work was to compare the roles of a newly described mitochondrial dehydrogenase and catalase in ethanol elimination in deer mice deficient in alcohol dehydrogenase (ADH-). Ethanol 115-122 catalase Mus musculus 103-111
1898039-4 1991 In addition, rates of metabolism of methanol, a selective substrate for catalase in rodents, were similar to rates of ethanol elimination and were decreased from 6.9 +/- 1.0 to 1.7 +/- 0.5 mmol/kg/h by fructose, supporting the hypothesis that catalase and not a mitochondrial dehydrogenase predominates in ethanol oxidation in ADH-deer mice. Ethanol 37-44 catalase Mus musculus 72-80
1898039-7 1991 These data are consistent with the hypothesis that fructose decreases catalase-dependent ethanol metabolism in vivo by inhibiting hepatic H2O2 generation. Ethanol 89-96 catalase Mus musculus 70-78
33290154-5 2021 Chronic ethanol consumption increased SBP, creatinine levels, O2.- and H2O2 levels, lipid peroxidation, catalase activity, Nox4, IL-6 and TNF-alpha levels, and MMP-9/TIMP-1 ratio. Ethanol 8-15 catalase Mus musculus 159-167
34755883-3 2022 We hypothesized that catalase depletion would exacerbate ethanol effects. Ethanol 57-64 catalase Mus musculus 21-29
35062902-10 2022 RESULTS: Ethanol induced oxidative stress injury and cell apoptosis on HCKs, and Tbeta4 can alleviate it by up-regulating the expression of Bcl-2, catalase, and CuZnSOD, and inhibiting the expression of Caspase-3. Ethanol 9-16 catalase Mus musculus 147-155
33892114-9 2021 Ethanol is mainly metabolized by alcohol dehydrogenase (ADH), cytochrome P450 2E1 (CYP2E1) and catalase. Ethanol 0-7 catalase Mus musculus 95-103
33892114-11 2021 What is more, injection of catalase inhibitor increased serum ethanol. Ethanol 62-69 catalase Mus musculus 27-35
29023845-11 2017 Ethanol depleted glutathione content, increased CYP2E1 activity and reactive oxygen species production, and reduced the activity of glutathione peroxide, glutathione reductase and catalase in liver. Ethanol 0-7 catalase Mus musculus 180-188
32710977-4 2020 Here, we reported that chronic unpredictable stress increased the sensitivity to the acute ethanol intoxication in mice via impairing nuclear factor (erythroid-derived 2)-like 2 (Nrf2)-catalase signaling. Ethanol 91-98 catalase Mus musculus 185-193
32710977-5 2020 Nrf2 activity regulates the expression of catalase, a key antioxidant enzyme that mediates ethanol oxidation in the brain. Ethanol 91-98 catalase Mus musculus 42-50
32710977-6 2020 Pharmacological blockade of catalase or Nrf2 activity significantly aggravated acute ethanol intoxication. Ethanol 85-92 catalase Mus musculus 28-36
28943104-6 2017 The mechanism analysis showed that FDP prevented ethanol-induced decrease of mouse antioxidant capability through inhibiting the reducion of the level of glutathione (GSH) and activities of superoxide dismutase (SOD), catalase (CAT), glutathione reductase (GR) and glutathione peroxidase (GSH-PX) in mouse livers, and suppressing the reducion of GSH level and SOD activity in L02 cells. Ethanol 49-56 catalase Mus musculus 218-226
28943104-6 2017 The mechanism analysis showed that FDP prevented ethanol-induced decrease of mouse antioxidant capability through inhibiting the reducion of the level of glutathione (GSH) and activities of superoxide dismutase (SOD), catalase (CAT), glutathione reductase (GR) and glutathione peroxidase (GSH-PX) in mouse livers, and suppressing the reducion of GSH level and SOD activity in L02 cells. Ethanol 49-56 catalase Mus musculus 228-231
28708332-4 2017 Our results demonstrated significantly reduced Catalase abundance and activity and increased glutathione content in the embryos of ethanol-treated females. Ethanol 131-138 catalase Mus musculus 47-55
28599809-5 2017 The antioxidant-enzyme activities in the liver tissue, including those of superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GPx), were significantly decreased by a chronic ethanol administration, whereas the hepatic lipid-peroxidation level was increased. Ethanol 194-201 catalase Mus musculus 102-110
28599809-5 2017 The antioxidant-enzyme activities in the liver tissue, including those of superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GPx), were significantly decreased by a chronic ethanol administration, whereas the hepatic lipid-peroxidation level was increased. Ethanol 194-201 catalase Mus musculus 112-115
28797835-5 2017 Ethanol increased superoxide anion (O2-) generation, thiobarbituric acid reactive substance concentration, and the activity of superoxide dismutase and catalase in aortas (PVAT- and PVAT+) from WT mice, but not TNFR1-/-. Ethanol 0-7 catalase Mus musculus 152-160
24065054-7 2014 Marked decreases in the expression of catalase and superoxide dismutases and ensuing increases in lipid peroxides were also observed in the livers of mice with middle- and high-dose ethanol treatment, suggesting the association between the suppression of hepatic CST expression and enhancement of oxidative stress. Ethanol 182-189 catalase Mus musculus 38-46
26074427-0 2015 Embryonic catalase protects against ethanol embryopathies in acatalasemic mice and transgenic human catalase-expressing mice in embryo culture. Ethanol 36-43 catalase Mus musculus 10-18
26074427-5 2015 Maternal pretreatment of C57BL/6 WT dams with 50kU/kg PEG-catalase (PEG-cat) 8h prior to embryo culture, which increases embryonic catalase activity, blocked all EtOH embryopathies (p<0.001). Ethanol 162-166 catalase Mus musculus 58-66
25352249-4 2015 This study presents a simple method for the purification of mouse liver catalase using ethanol-chloroform treatment, sodium sulfate fractionation, dialysis and Sephadex G-200 gel filtration chromatography. Ethanol 87-94 catalase Mus musculus 72-80
25427919-2 2015 The primary enzymes involved in ethanol metabolism include alcohol dehydrogenase (ADH), cytochrome P450 isoform 2E1, (CYP2E1), catalase (CAT), and aldehyde dehydrogenases (ALDH). Ethanol 32-39 catalase Mus musculus 127-135
25427919-2 2015 The primary enzymes involved in ethanol metabolism include alcohol dehydrogenase (ADH), cytochrome P450 isoform 2E1, (CYP2E1), catalase (CAT), and aldehyde dehydrogenases (ALDH). Ethanol 32-39 catalase Mus musculus 137-140
24103023-3 2015 Evidence indicates that catalase-mediated conversion of ethanol into acetaldehyde in pVTA plays a critical role in this effect. Ethanol 56-63 catalase Mus musculus 24-32
24103023-9 2015 This effect requires ethanol oxidation into acetaldehyde given that, when H2 O2 -catalase system was impaired by either 3-amino-1,2,4-triazole or in vivo administration of alpha-lipoic acid, ethanol did not enhance DA cell activity. Ethanol 21-28 catalase Mus musculus 81-89
24103023-9 2015 This effect requires ethanol oxidation into acetaldehyde given that, when H2 O2 -catalase system was impaired by either 3-amino-1,2,4-triazole or in vivo administration of alpha-lipoic acid, ethanol did not enhance DA cell activity. Ethanol 191-198 catalase Mus musculus 81-89
23733920-9 2013 Plasma concentrations of EtOH in catalase-altered mice were similar to controls, precluding a pharmacokinetic basis for altered EtOH teratogenesis. Ethanol 25-29 catalase Mus musculus 33-41