Disease relevance of RCJMB04_1j22

• Catalase depression in malignant liver from chickens with myeloblastosis and Marek's disease [1].
• The L-glutamate toxicity could to a large extent by prevented by NMDA receptor antagonists and to a lesser extent by catalase, superoxide dismutase or glutathione ethyl ester added 30 min before the glutamate [2].
• The isolates could be distinguished from other Arcobacter species by the following biochemical tests: catalase, oxidase and urease activities; reduction of nitrate; growth at 25 and 37 degrees C under aerobic conditions; growth on 2-4 % (w/v) NaCl media; and susceptibility to cephalothin [3].
• Decrease in catalase activity of cultured cells by Mycoplasma gallisepticum infection [4].
• Vitamin E, catalase, manganous or cobaltous ions and dithiothreitol protect against Tween 20-induced hemolysis of vitamin E-deficient chick and kid erythrocytes [5].

High impact information on RCJMB04_1j22

• Furthermore, it was found that when the PAM and red blood cell targets were cross-linked with PHA, catalase still completely eliminated IIC-DCC and had no effect on ADCC, which suggests that catalase is able to penetrate the lytic site when the effector and targets are cross-linked as in ADCC [6].
• The presence of cytochalasin B, which inhibits internalization of immune complexes by PAM and presumably prevents intracellular killing, also had no effect on the differential susceptibility of IIC-DCC and ADCC to catalase [6].
• Superoxide dismutase and catalase activities in the growth cartilage: relationship between oxidoreductase activity and chondrocyte maturation [7].
• Endogenous superoxide dismutase (SOD), catalase, and glutathione peroxidase (GP) activities were determined for the macrophages during intermediate and late inflammatory stages [8].
• For antioxidant enzymes, chicks of pullets given 120 mg/kg supplemental vitamin E had higher (P < 0.05) activities of liver catalase than those given 0-80 mg/kg [9].

Chemical compound and disease context of RCJMB04_1j22

• Addition of catalase, MnCl2, CoCl2 or dithiothreitol in vitro showed significant protection against the hemolysis induced by Tween 20 in vitamin E-deficient chick and kid erythrocytes [5].

Biological context of RCJMB04_1j22

• Tetrasomic macrophages had reduced SOD activity at the late stage, no significant difference was observed in catalase activity among genotypes at either time point, and trisomic macrophages had enhanced GP activity compared to disomic cells at both time points [8].
• The rate of transformation of catalase to catalase-formate in liver was studied by freeze-clamping liver in anaesthetised chickens, then warming to 37 degrees for 1 or 2 minutes anaerobiosis, and then refreezing [1].
• The culture response to oxidative stress, produced either by addition of exogenous hydrogen peroxide or by high-dissolved oxygen tensions, was examined in terms of the activities of two key defensive enzymes: catalase (CAT) and superoxide dismutase (SOD) [10].
• In the presence of catalase, superoxide dismutase, or vitamin E, the SVMF enhanced cell proliferation was reduced by 79, 67, and 82%, respectively [11].
• There was a negative correlation (r= -0.397, P < 0.05) between catalase-like activity in sperm cells and the rate of sperm lipid peroxidation [12].

Anatomical context of RCJMB04_1j22

• 1. Tissue-specific profiles of the expression of the antioxidant enzymes superoxide dismutase (SOD), glutathione peroxidase (GSH-Px) and catalase (CAT) and the concentrations of reduced glutathione (GSH) during the development of the chick embryo were investigated [13].
• The distributions of these organelles are characterized after density gradient centrifugation in sucrose or Percoll by urate oxidase and catalase activities [14].
• Additionally, the reversing action of Mg2+ re-added to 1.0 mM and the partial reversing action of dimethylthiourea suggested that (i) [Mg2+]e deficiency induced the increase of H2O2 production, (ii) [Mg2+]e deficiency decreased catalase activity in chick embryo hepatocyte in vitro, subsequently causing oxidative stress and cell peroxidative damage [15].
• The effect of Mycoplasma gallisepticum infection on the host cell catalase activity was histochemically examined in cultured chicken embryo fibroblasts (CEF) and kidney cells [4].
• In addition, free radical scavengers, catalase and glutathione, were tested with DCFH fluorescent imaging for their ability to quench the production of reactive oxygen species in hair cells after drug exposure [16].

Associations of RCJMB04_1j22 with chemical compounds

• Hepatic glutathione content, hepatic catalase and superoxide dismutase were unchanged by the dietary treatments [17].
• Paraquat significantly stimulated the rate of NADPH-supported consumption of oxygen by the microsomal fractions of chick liver and lung, and this stimulation was decreased by addition of superoxide dismutase and/or catalase [18].
• Cu-Zn superoxide dismutase, Mn superoxide dismutase, catalase, glutathione peroxidase, and glutathione reductase activities and thiobarbituric acid-reactive products were assayed in the superficial pectoral muscles of genetically dystrophic chickens (line 413) and their controls (line 412) 1, 2, and 4 weeks, and 4 months after hatching [19].
• Dopamine was also cytotoxic, and the cytotoxicity was reduced by the combination of catalase and glutathione ethyl ester but not by the MAO inhibitors clorgyline or L-deprenyl, or by the selective dopamine uptake inhibitor GBR 12783 [2].
• The only difference of significance in this transformation between diseased and normal livers was the greater percentage of total catalase present as catalase-formate (approximately + 15%) in aerobic diseased liver, which may indicate a lowered production of hydrogen peroxide, relative to formate, in these livers [1].

Physical interactions of RCJMB04_1j22

• Lysyl oxidase coupled with catalase in egg shell membrane [20].

Other interactions of RCJMB04_1j22

• Moreover, the H(2)O(2) released by lysyl oxidase in ESM was completely decomposed by coexisting catalase activity [20].
• Further, the effect of Se on some of the antioxidant enzymes like glutathione peroxidase (GPx), glutathione transferase (GST), glutathione reductase (GR), superoxide dismutase (SOD) and catalase were studied [21].

Analytical, diagnostic and therapeutic context of RCJMB04_1j22

• Immobilization of catalase by entrapment of permeabilized yeast cells in hen egg white using glutaraldehyde [22].
• Effect of oral administration of aluminum sulphate (200 and 400 mg/kg body wt/day) without or with citric acid (62 mg/kg body wt/day) to day-old White Leghorn male chicks (n = 5 per group) for 30 days was studied on the activities of superoxide dismutase (SOD) and catalase, and level of lipid peroxidation in cerebral hemisphere and liver [23].
• Using routine transmission electron microscopy and light and electron microscopic techniques for the histologic demonstration (localization) of catalase (a peroxisomal enzyme), peroxisomes in chick duodenal epithelial cells were identified and studied [24].
• At 16 days, cervical, thoracic, and lumbar regions of the spinal cord were fixed in gluteraldehyde and processed for electron microscopy, either directly or following incubation in media containing 3,3-diaminobenzidine and hydrogen peroxide for the histochemical detection of catalase-reactive peroxisomes [25].

References