Disease relevance of catalase

• We can also obtain information on previously reported genes involved in nematode infection (e.g., multicystatin, peroxidase, catalase, pectin esterase, and S-adenosylmethionine transferase) [1].
• We have validated this assay by examining survival during acute heat stress and protection against oxidative stress with the superoxide dismutase/catalase mimetic Euk-134 [2].
• Characterization of a pathogen-induced potato catalase and its systemic expression upon nematode and bacterial infection [3].
• A two-stage dose-response was apparent, with catalase activities increasing as the peroxide levels increased, before a return to control levels at higher peroxide concentrations, most likely reflecting a balance between induction and toxicity of the inducing agent itself [4].
• (type strain VKM Ac-1804T=UCM Ac-620T) is proposed to accommodate aerobic, oxidase- and catalase-positive, weakly motile, coryneform actinobacteria isolated from leaf galls induced by the plant-parasitic nematode Heteroanguina graminophila in narrow reed grass, Calamagrostis neglecta [5].

High impact information on catalase

• Malate synthase and isocitrate lyase, key enzymes of the glyoxylate cycle, consistently sedimented with mitochondrial enzymes in differential pellets while catalase, a major peroxisomal enzyme, was always soluble [6].
• The activities of catalase, superoxide dismutase, isocitrate dehydrogenase, isocitrate lyase, and malate synthase are all higher relative to those in worms that are wild type for these genes, but acid phosphatase is down-regulated and alkaline phosphatase activity is lowered to 10% of the activity measured in age-1(+) and daf-2(+) worms [7].
• Hydrogen peroxide-mediated killing might represent a common mechanism by which gram-positive, catalase-negative pathogens kill C. elegans [8].
• We have isolated a cDNA encoding a catalase (Cat2St) by differential screening of a cDNA library constructed from potato roots infected with the cyst nematode Globodera pallida [3].
• The response of Haemonchus contortus to oxidative stress in vitro was examined by measuring catalase activities in adult and L4 stage worms exposed to hydrogen peroxide generated by a glucose/glucose oxidase system [4].

Chemical compound and disease context of catalase

• These experiments demonstrate the toxicity of intracellular O2- and H2O2 in nematodes and the importance of superoxide dismutase and catalase in providing a defense against these toxic molecules in vivo [9].

Biological context of catalase

• The results indicate that the three nematodes can protect themselves against possible host-immune initiated lipid peroxidation of their membranes at the level of the hydroperoxide and at the level of cytotoxic carbonyl, although other protective enzymatic mechanisms are also likely to exist (superoxide dismutase and catalase) [10].

Anatomical context of catalase

• The ability of H contortus to increase its catalase activity may be crucial in allowing it to respond to the production of reactive oxygen species by host phagocytes in vivo [4].

Associations of catalase with chemical compounds

• 3-Amino-1,2,4-triazole (20 mM) eliminated greater than or equal to 80% of the catalase activity in vivo and diethyldithiocarbamate (5 mM) decreased the level of CuZn superoxide dismutase by greater than or equal to 70% [9].
• Levels of defensive enzymes such as superoxide dismutase, catalase, glutathione peroxidase, and dianisidine peroxidase were measured in the two species [9].

Other interactions of catalase

• Axenic culture also caused higher activities of the antioxidant enzymes superoxide dismutase and catalase, and led to increased resistance to high temperature, which was further exacerbated by mutation in eat-2 [11].
• The Ginkgo biloba extract EGb761 reduces stress sensitivity, ROS accumulation and expression of catalase and glutathione S-transferase 4 in Caenorhabditis elegans [12].

References