HUGO ID Detailed Result 1516

HUGO ID 1516
Symbol CAT
Name catalase
#Occurrence 82
#Paper 30

 

PMID Match String Actual String Score Flanking text Edited by Edit
16681429CATCAT1.0following ADEs copper-zinc superoxide dismutase (CuZn CuZn SOD catalase (CAT), CAT glutathione peroxidase (GSH-Px) GSH-Px and glutathione reductase (GR) GR in 
16681429CATCAT1.0The disease also influenced CAT and GR activity 
17191135CATCAT0.1other main antioxidant enzymatic activities such as GPx GSSG reductase CAT and SOD1 were also found elevated in several regions of 
18308427CATCAT1.0Antioxidant defense enzymes superoxide dismutase (SOD), SOD catalase (CAT), CAT glutathione peroxidase (GSHPx), GSHPx glutathione reductase (GR) GR and glucose-6-phosphate 
18308427CATCAT1.0Catalase (CAT) CAT (E.C E.C No 1.11.1.6 catalyzes the conversion of hydrogen peroxide 
18308427CATCAT1.0other sulfydryl groups of a cell and the antioxidant enzyme CAT in its active form ( Kletzien et al. 1994 and 
18308427CATCAT1.0correlation if any between the lipid peroxidation (LPO), LPO SOD CAT GSH GSHPx GR and G-6-PDH levels and the progression of 
18308427CATCAT1.0CAT was estimated by the method of Aebi (1984) 1984 
18308427CATCAT1.0found that LPO ( Fig 6 started to increase and CAT GSH GR and G-6-PDH levels ( Fig 7 Fig 8 
18308427CATCAT1.0In the present study CAT was found to exhibit significantly reduced activity when compared to 
9856861catalasecatalase1.0iron iii /ascorbate toxicity was completely prevented with the hydrogen peroxide detoxifying enzyme catalase and partially prevented with the antioxidant vitamin e. sod1 the enzyme that removes superoxide did not protect against iron iii /ascorbate toxicity.  
10593879catalasecatalase1.0h 2 o 2 produced from o 2 is converted to h 2 o by catalase and glutathione peroxidase gsh px the normal detoxification pathway of h 2 o 2 although some h 2 o 2 may be converted to oh by sod1.  
10593879catalasecatalase1.0this is probably due to efficient h 2 o 2 removal which is the normal catalytic function of gsh px and catalase. msod1 mice had significantly higher levels of h 2 o 2 and oh than did the sod1 and nc mice and significantly lower levels of o 2 than the nc mice.  
10593879catalasecatalase1.0it may work together with the detoxification enzymes such as catalase and gsh px to remove the h 2 o 2 produced from o 2 .  
10643818catalasecatalase1.0peroxidase and catalase activities are reduced in the substantia nigra caudate and putamen in parkinson's disease [ 43 ].  
10930589catalasecatalase1.0further cells incubated with vitamin c catalase or the flavinoid quercetin significantly reduced ros in all groups.  
10930589catalasecatalase1.0the catalase inhibitor 3 amino 1 2 4 triazole resulted in a ten fold increase of ros in all groups.  
10930589catalasecatalase1.0lactate dehydrogenase ldh activity was used to calculate the specific fluorescence. nitroarginine aldrich catalase boehringer mannheim and other chemicals sigma studied were added 15 min before loading of the cells with c dcdhf da am table 1 .  
10930589catalasecatalase1.0sod1 is a major source of h 2 o 2 in cells [ 20 ] and catalase and glutathione peroxidase are the primary enzymes responsible for decomposition of h 2 o 2 [ 21 ].  
10930589catalasecatalase1.0catalase reduced the c dcf fluorescence in resting or menadione stimulated cells in all three groups of cells tested.  
10930589catalasecatalase1.0however the reduction was more pronounced in menadione stimulated cells. 3 amino 1 2 4 triazole 3 at an inhibitor of catalase [ 22 and 23 ] increased the c dcf fluorescence of all three types of cells.  
10930589catalasecatalase1.0reduction of c dcf fluorescence by catalase and other antioxidants vitamin c and the flavinoid quercetin but not inhibitor of nos supports the conclusion that c dcdhf was oxidized by h 2 o 2 table 2 .  
11050436catalasecatalase1.0thus transgenic drosophila with increased expression of cuznsod did not show increased life span unless accompanied by increased expression of catalase to remove the hydrogen peroxide.  
11050436catalasecatalase1.0hydrogen peroxide is converted to water by either catalase or glutathione peroxidase.  
11679167catalasecatalase1.0in agreement s. cerevisiae mutants deficient in antioxidant defences such as catalase superoxide dismutase and cytochrome c peroxidase are sensitive to a lethal heat shock and the overexpression of genes encoding catalase and superoxide dismutase increase the resistance to the severe  
11679167catalasecatalase1.0 superoxide dismutase and cytochrome c peroxidase are sensitive to a lethal heat shock and the overexpression of genes encoding catalase and superoxide dismutase increase the resistance to the severe heat shock davidson et al. 1996 .  
11679167catalasecatalase1.0hap1p regulates the transcriptional activation of the antioxidant genes such as sod2 mitochondrial superoxide dismutase cta1 peroxisomal catalase ctt1 cytosolic catalase and ubi4 polyubiquitin .  
12392777catalasecatalase1.0h 2 o 2 is then converted to h 2 o by either catalase or glutathione peroxidase gsh px .  
12614931catalasecatalase1.0ecause of its high level of polyunsaturated fatty acids as substrates for lipid peroxidation high rate of oxygen consumption and low or moderate levels of the antioxidant enzymes superoxide dismutase catalase and gpx compared with kidney or liver [ 1 ].  
12614931catalasecatalase1.0ease in dcfh da oxidation after treatment with ea indicates the presence of increased levels of h 2 o 2 and could be a direct consequence of gsh deficiency since in mitochondria_amp_#x2014;which lack catalase activity_amp_#x2014;h 2 o 2 is metabolized by gsh peroxidase using the reducing equivalents of gsh.  
12614931catalasecatalase1.0in addition levels of catalase are very low in the nervous system [ 1 ].  
12614931catalasecatalase1.0interestingly treatment with catalase was beneficial in a mouse model of als [ 28 ].  
12654515catalasecatalase1.0based on our previous study showing that the anti oxidants catalase n acetyl cysteine n ac and the spin trapping molecule 5_amp_#x2032; 5_amp_#x2032; dimethylpryrroline n oxide dmpo were all protective fig 1d and ref [ 32 ] we assume that oxidative stress is at least 
12663085catalasecatalase1.0sod and catalase activities were not changed suggesting that specific defects of the gsh system are more important in als.  
12684448catalasecatalase1.0xposed for 15 min to sham wash or to kainate [100 micro m plus + 5 methyl 10 11 dihydro 5h dibenzo [a d] cyclohepten 5 10 imine maleate mk 801 ] alone or in the presence of antioxidants sod 100 u/ml; catalase 400 u/ml followed after another 10 min by incubation in [ h]glutamate 2 microci/ml in hss for 5 min.  
12684448catalasecatalase1.0a spinal cultures were exposed to sham wash or to kainate ka ; 100 micro m plus 10 micro m mk 801 alone or with addition of the antioxidants sod 100 u/ml and catalase 400 u/ml to the bath ka+ao before [ h]glutamate uptake assays as described.  
12684448catalasecatalase1.0furthermore this local decrease in uptake was prevented by addition of cell impermeant antioxidant enzymes sod 100 u/ml; catalase 400 u/ml to the bath.  
12718737catalasecatalase1.0antioxidant enzymes such as superoxide dismutase sod catalase and glutathione peroxidase gpx have demonstrated therapeutic efficacy in models of neurodegeneration.  
12893007catalasecatalase1.0nding ubiquitous antioxidative enzyme that catalyses the conversion of the toxic superoxide radical to hydrogen peroxide which in turn is converted to h 2 o by the action of glutathione peroxidase or catalase [ fridovich 1986 ] .  
12909279catalasecatalase1.0these include enzymatic activities superoxide dismutase catalase peroxidase and peroxiredoxin low molecular weight antioxidant species vitamin e ascorbate glutathione plus more complex forms of protection such as systems for metal transport and buffering and induc 
12909279catalasecatalase1.0the central nervous system cns is particularly sensitive to this kind of damage for a number of reasons including a low level of some antioxidant enzymes catalase and gsh peroxidase a high content of easily oxidised substrates e.g membrane polyunsaturated lipids and an inherently high flux of ros generated during neurochemical reactions such as dopamine oxidat 
14648077catalasecatalase1.0in the second enzyme group the peroxiredoxin prx and glutathione peroxidase gpx families as well as catalase localized within peroxisomes have been identified.  
14648077catalasecatalase1.0unlike sod and catalase enzymes of the prx and gpx families require secondary enzymes and cofactors to function at high efficiency.  
14690536catalasecatalase1.0the hsod1 induced decline in glt 1 protein and [3h]d aspartate uptake was not blocked by the antioxidant trolox nor potentiated by antioxidant depletion using catalase and glutathione peroxidase inhibitors.  
15031734catalasecatalase1.0in the ad brain the activity of the antioxidant proteins catalase superoxide dismutase sod glutathione peroxidase and glutathione reductase are increased in the hippocampus and amygdala 9 10 .  
15031734catalasecatalase1.0synthetic a beta is toxic to cells in the presence of cu 2+ but this toxicity is inhibited by extracellular catalase which implicates h 2 o 2 in the toxic pathway 50 51 .  
15031734catalasecatalase1.0beta actin catalase creatine kinase frataxin glucose transporter type 3 glutathione peroxidase glutathione reductase mitogen activated protein kinase 1 sod alpha synuclein xanthine dehydrogenase  
15266948catalasecatalase1.0melatonin has been shown to either stimulate gene expression for the antioxidant enzymes superoxide dismutase catalase glutathione peroxidase glutathione reductase or to increase their activity.  
15896810catalasecatalase1.0ble substrates such as polyunsaturated fatty acids and catecholamines; b relatively low levels of antioxidants such as glutathione and vitamin e and antioxidant enzymes such as glutathione peroxidase catalase and superoxide dismutase ; c the endogenous generation of reactive oxygen free radicals via several specific reactions; d the elevated content of iron in specific areas of the human brain such as glo 
15896810catalasecatalase1.0other heme protein targets for no are catalase cytochrome c hemoglobin and peroxidase.  
16188953catalasecatalase1.0in further conditions ppx 300 microm malonate malo 10 mm the sod catalase mimic euk 134 melov et al. 2001 euk 30 microm or atp 1 mm was added.  
16188953catalasecatalase1.0therefore we reevaluated the antioxidative properties of ppx and snd targeted toward different reactive species and compartments; obtained efficacies were compared with euk 134 a potent sod catalase mimetic jung et al. 2001 ; melov et al. 2001 .  
16188953catalasecatalase1.0after demonstrating entry of ppx into brain cells and mitochondria we reevaluated the antioxidative properties of ppx and snd and compared the obtained efficacy with euk 134 a potent sod catalase mimetic melov et al. 2001 .  
16194581catalasecatalase1.0moreover the brain is not particularly endowed with antioxidant defenses: it has a very low level of catalase activity and only moderate amounts of the endogenous antioxidant enzymes superoxide dismutase and glutathione peroxidase.  
16681429catalasecatalase1.0methods: we determined activity of the following ades: copper zinc superoxide dismutase cuzn sod catalase cat glutathione peroxidase gsh px and glutathione reductase gr in erythrocytes from sporadic als patients [sals /+ ] familial als patients with the leu144phe mutation in the sod1 gene [fals +/+ ] asy 
16877542catalasecatalase1.0to conditioned medium containing 0.1 milliunits/ml glucose oxidase generating an average stable concentration of 75 _amp_#x003bc;m h 2 o 2 fig 5 e ; this effect was abolished by adding 1 000 units/ml catalase to the medium data not shown .  
17150307catalasecatalase1.0more significantly treatment of als like transgenic mice with antioxidants such as sod and catalase mimetics jung et al. 2001 dmpo liu et al. 2002 iron porphyrin wu et al. 2003 or manganese porphyrin crow et al. 2005 delays disease onset and extends survival.  
17174478catalasecatalase1.0the catalase protein completes the process of eliminating ros by converting hydrogen peroxide into water and oxygen.  
17174478catalasecatalase1.0in addition to this defense against oxidative damage human catalase has roles in ethanol metabolism zimatkin et al. 1998 inflammation halliwell and gutteridge 1984 apoptosis yabuki et al. 1999 aging and cancer miyamoto et al. 1996 .  
17174478catalasecatalase1.0several catalase crystal structures have been determined aiding our understanding of reactive oxygen control by defining the reaction and inhibition mechanisms goth 1997 .  
17174478catalasecatalase1.0these studies include the definition of the chemistry of the human catalase through structures of the resting state enzyme and complexes of a catalase bound to cyanide and 3at inhibitors putnam et al. 2000 .  
17174478catalasecatalase1.0human catalase forms a tetrameric assembly and this may be important to ensure that the active site is sequestered and that the enzyme is competent to complete the reaction.  
17174478catalasecatalase1.0interestingly an unstable catalase isolated from patients homozygous for a swiss type acatalasemia a hereditary catalase deficiency disorder rapidly disassociates into inactive dimers with reduced heme content.  
17174478catalasecatalase1.0this suggests that catalase assembly variants may play roles in disease susceptibility aebi et al. 1974 in addition to nonsense and splicing mutations hirono et al. 1995 .  
17174478catalasecatalase1.0from the structural data a mechanism for the recognition and removal of peroxide by catalase has been proposed putnam et al. 2000 .  
17174478catalasecatalase1.0catalase uses these two asymmetric interactions with the substrate to prime the otherwise symmetric peroxide bond for heterolytic bond cleavage; good geometry for both iron coordination and hydrogen bond form 
17368952catalasecatalase1.0superoxide dismutase sod is a major antioxidative defense enzyme converting superoxide anion o 2 _amp_#xb7; _amp_#x2212; to hydrogen peroxide h 2 o 2 which is reduced to h 2 o by catalase and selenium dependent glutathione peroxidase.  
17496232catalasecatalase1.0because peroxisomes contain the highest concentration of catabolizing catalase mitochondria with very low levels of degrading enzymes are accepted as the main source of o 2 species 17 33 .  
17496232catalasecatalase1.0otherwise enzymes that catabolize h 2 o 2 catalase gluthatione peroxidase gpx; reactions 6 and 7 and thioredoxin peroxidase trx; reaction 8 are preferentially distributed in cytosol and peroxisomes.  
17496232catalasecatalase1.0considering the reduction to h 2 o by liver cytosolic gpx and catalase at the respective concentrations of 2.7 x 10 m and 1.2 x 10 m and the rate constants for reactions 7 and 8 the no dependent [h 2 o 2 ] ss could be calculated as follows 17 :  
17496232catalasecatalase1.0lation of [h 2 o 2 ] ss implies an effective regulation of the different pathways participating in the process including the concentration and activities of mtnos cytosolic classic nos isoforms mnsod catalase and peroxidases.  
17496232catalasecatalase1.0in this study cells were reverted to a normal phenotype by cotransfection with catalase and the authors concluded that a major role of h 2 o 2 is to activate genes related to the proliferating cascade.  
17496232catalasecatalase1.0isolated neonatal hepatocytes supplemented with h 2 o 2 catalase inhibitor 3 amino 1 2 4 triazole or l arginine invariably determined a dose dependent negative modulation of cell proliferation.  
18210200catalasecatalase1.0based on this our laboratories developed cell mediated delivery of catalase nanozyme to the brain to mitigate production of ros and induce neuroprotection batrakova et al 2007 .  
18210200catalasecatalase1.0to preclude bmm mediated enzyme degradation catalase was packaged into a block ionomer complex with a cationic block copolymer pei peg.  
18210200catalasecatalase1.0the self assembled catalase/pei peg complexes were ca. 60 to 100 nm in size stable in ph and ionic strength and retained antioxidant activities.  
18308427catalasecatalase1.0antioxidant defense enzymes: superoxide dismutase sod catalase cat glutathione peroxidase gshpx glutathione reductase gr and glucose 6 phosphate dehydrogenase g 6 pdh in the erythrocytes are capable of detoxifying reactive oxygen species produced endogenously or 
18308427catalasecatalase1.0on the other hand catalase activity was found to be significantly lower p _amp_#x3c; 0.001 .  
18308427catalasecatalase1.0it was further observed that lipid peroxidation started to increase and catalase glutathione reductase glucose 6 phosphate dehydrogenase enzyme activities and glutathione levels started to decrease as amyotrophic lateral sclerosis progressed from 6 to 24 months suggesting a corre 
18308427catalasecatalase1.0catalase cat e.c no 1.11.1.6 catalyzes the conversion of hydrogen peroxide h 2 o 2 to water and molecular oxygen thereby protecting cells from the toxic effects of hydrogen peroxide.  
18308427catalasecatalase1.0the rate of lpo in the erythrocytes of als patients was significantly increased with respect to control subjects p _amp_#x3c; 0.001 fig 1 whereas catalase activity in the rbc of als patients was significantly lower than the controls p _amp_#x3c; 0.01 fig 2 .  
18308427catalasecatalase1.0fig. 7._amp_#xa0;second degree polynomial regression plot showing the activity of catalase in the erythrocytes of als vs. duration of illness n = 10 at 6 months 5 at 12 months and 5 at 24 months .