Disease relevance of Cat

• The addition of Cat to the culture medium completely prevented the toxic effects of H2O2 and H/XO but had no significant effect on the toxicity of menadione or butylalloxan [1].
• Reduction in molecular synthesis or enzyme activity of superoxide dismutases and catalase contributes to oxidative stress and neurogenic hypertension in spontaneously hypertensive rats [2].
• We investigated the effects of polyethylene glycol-adsorbed superoxide dismutase (PEG-SOD), polyethylene glycol-adsorbed catalase (PEG-CAT), and DMSO on diaphragmatic contractility and malondialdehyde (MDA) concentrations in septic peritonitis in vitro [3].
• Prompted by this, we have generated herpes simplex virus-1 amplicon vectors over-expressing the genes for the antioxidant enzymes catalase (CAT) or glutathione peroxidase (GPX), both of which catalyze the degradation of hydrogen peroxide [4].
• To study the effects of altered food intake or dietary protein content on SOD and catalase in cardiac and skeletal muscles, young rats were fed ad libitum diets containing 3, 6 or 25% casein or were subjected to total or partial food restriction (resulting in similar body weight losses) [5].

Psychiatry related information on Cat

• Because of this SOD/catalase mimicry, EUK-8 and EUK-134 have been investigated as possible therapeutic agents in neurological disorders resulting from oxidative stress, including Alzheimer's disease, Parkinson's disease, stroke and multiple sclerosis [6].
• METHODS: In this study we examined the primary enzymatic defense mechanisms against the damage caused by reactive oxygen species (ROS): the superoxide dismutase (SOD) and catalase activities and glutathione content, as well as the levels of total thiobarbituric acid-reactant substances (TBARS), indicative of lipid peroxidation [7].
• We demonstrated an increase in catalase (CAT) and superoxide dismutase (SOD) activities at different time points after single and multiple electroconvulsive shock [8].
• The role of brain catalase in the mediation of ethanol's effects on motor activity was investigated [9].
• In conclusion, ethanol inhibits nitrite oxidation by catalase in the perfused rat liver at relatively low concentrations that can be realized in blood by daily alcohol consumption [10].

High impact information on Cat

• Toxicity was prevented by addition of pyruvate or catalase, which neutralize H2O2 produced by cysteine autoxidation [11].
• The endothelium-dependent relaxations to A23187 were significantly inhibited by catalase, and enhanced by superoxide dismutase, only in SHR; however, these enzymes had no effect in the presence of H4B [12].
• This decline in MnSOD activity occurred without a change in the lung activity of copper-zinc SOD, catalase, or glutathione peroxidase [13].
• GSH and catalase (but not DMTU, benzoate, or mannitol) decreased MDA concentrations, suggesting the Fe-driven lipid peroxidation was more H2O2 than .OH dependent [14].
• By determining H2O2-dependent inactivation of catalase in the presence of 3-amino-1,2,4-triazole (ATZ), we found increased H2O2 production in the forebrain after reoxygenation [15].

Chemical compound and disease context of Cat

• Hyperthyroidism elicited a calorigenic response and increased specific and molecular activities of NADPH-cytochrome P450 reductase, O2.- generation, and G-6PDH activity, concomitantly with diminution in liver SOD and catalase activities and in alpha-tocopherol, beta-carotene, and lycopene levels [16].
• Superoxide dismutase administered free in solution, or combined with catalase in liposomes, increased the normoxic pulmonary arterial pressure and enhanced vascular reactivity to angiotensin II and hypoxia [17].
• The animals were given subtherapeutical doses of insulin (Interdep 6 U. kg-1 body weight, s.c.). Considerably increased levels of malondialdehyde (MDA), as well as of superoxide dismutase (SOD) and catalase (CAT) activity were found in the myocardium of diabetic animals [18].
• AG administration did not affect body weight, blood glucose level and HbA1c content in diabetic rats but led to a decrease of MDA concentration and SOD and catalase activities after 12 weeks of treatment, with no significant effect after 6 weeks [19].
• Gene expression of glutathione peroxidase, catalase, cuprozinc superoxide dismutase, and manganese superoxide dismutase were not reduced in experimental diabetic neuropathy at either 3 or 12 months [20].

Biological context of Cat

• Thus, overexpression of Cat and Gpx, alone or in combination with SOD, by use of molecular biology techniques can protect insulin-producing cells against oxidative damage [1].
• The molecular weight of rat liver catalase was calculated to be 59,758 from the predicted amino acid sequence [21].
• Nucleotide sequencing was carried out on these five clones and the composite nucleotide sequence of catalase cDNA was determined [21].
• These results provided evidence that gene transfection of the activity-lacking mutant HO-1 protects cells against oxidative stress through multiple mechanisms involving up-regulation of catalase and glutathione contents [22].
• Identification of a functional peroxisome proliferator-activated receptor response element in the rat catalase promoter [23].

Anatomical context of Cat

• Rat liver catalase has no cleavable signal peptide for translocation of the enzyme into peroxisomes [21].
• Diabetes was associated with significantly increased activities of catalase (CAT), glutathione reductase (GSSG-RD), and CuZn-superoxide dismutase (SOD) in the pancreas and of CAT and GSSG-RD in the heart [24].
• HO-1- and mHO-1 U937 cells became more and less sensitive to H(2)O(2) than mock transfectants, respectively; such distinct susceptibility between the cells was ascribable to differences in the capacity to scavenge H(2)O(2) through catalase and to execute iron-mediated oxidant propagation [22].
• Treatment of microvascular endothelial cells with PPARgamma ligands led to increases in catalase mRNA and activity [23].
• During aging, the activity of catalase increase in cardiac muscle and, in contrast, decrease in other organs [25].

Associations of Cat with chemical compounds

• O2 plus endotoxin increased the concentration and stability of MnSOD, catalase, and GP mRNAs [26].
• The resistance of HO-1-U937 to hydroperoxides appeared to result from antioxidant properties of bilirubin, an HO-derived product, while that of mHO-1-U937 was ascribable to increased contents of catalase and glutathione [22].
• However, treatment with captopril resulted in a significant improvement in SOD, GSHPx and catalase activity in the 16-week PMI group [27].
• Catalase alone was able to increase the resistance of transfected RINm5F insulin-producing tissue culture cells against H(2)O(2) and HX/XO, but no protection was seen in the case of menadione [28].
• While a TCDD dose of 10 ng/kg/d resulted in significant increases in catalase and GSH-Px activities in Cc and H, doses of 22 and 46 ng/kg/d resulted in dose-dependent suppressions of these two enzymes in the same regions [29].

Physical interactions of Cat

• Oxidation of nitric oxide by oxomanganese-salen complexes: a new mechanism for cellular protection by superoxide dismutase/catalase mimetics [6].
• Implanted NGF-producing fibroblasts induce catalase and modify ATP levels but do not affect glutamate receptor binding or NMDA receptor expression in the rat striatum [30].

Enzymatic interactions of Cat

• The presence of manganese in the incubation mixture was found to increase the prooxidant role of catalase on autoxidation during one-electron reduction of aminochrome catalyzed by NADPH cytochrome P450 reductase [31].

Regulatory relationships of Cat

• Catalase was inhibited with aminotriazole while glutathione peroxidase activity was blocked by eliminating reduced glutathione after addition of either iodoacetamide diethylmaleate or phorone [32].
• 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 [33].
• These results suggest relatively small contribution of SOD, GSH-Px, and catalase in cadmium-induced lipid peroxidation in the testes [34].
• Catalase also decreased the activation induced with superoxide dismutase [35].
• In contrast, HXXO caused a marked amplification of the IL-1beta-induced steady-state tPA mRNA level and tPA enzyme activity that was blocked by catalase [36].

Other interactions of Cat

• Two of these proteins, heme oxygenase-1 and catalase, were expressed at relatively low levels until approximately the time of birth [37].
• Regarding changes in the enzyme activities accompanying development of iron epilepsy, the data showed that although SOD and G6P increased by approximately 60% and GR increased by approximately 40%, the increases in the enzyme GP and CA were much lower, less than 20% [38].
• Ovariectomy increases Na+, K+-ATPase, acetylcholinesterase and catalase in rat hippocampus [39].
• In terms of enzymatic activity, although we detected lower glutathione S-transferase activity in the crypt epithelium, there was a marginal increase of PHGPX activity, a twofold increase of GSHPx activity, and a three- to fivefold increase of catalase activity in the crypt relative to the distal villus [40].

Analytical, diagnostic and therapeutic context of Cat

• Cocultivation elevated AOA in EC (MnSOD, CuZnSOD, Cat, GPx), and AC (MnSOD, CuZnSOD, GPx) [41].
• Catalase and CuZn superoxide dismutase were localized by immunocytochemistry [33].
• Superoxide dismutases were detected by specific RIAs: catalase by polarography, and lipid peroxide by fluorimetry [42].
• Our results indicate that neither total SOD, GPx, nor catalase myocardial activities were changed whatever the perfusion protocol followed [43].
• Endotracheal bleomycin administration alone caused significant reductions in catalase activity at 2 days and 2 weeks after treatment, whereas glutathione peroxidase activity increased above control untreated animals at 2 and 4 weeks, respectively [44].

References