acatalasia/peroxidase

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Activities of superoxide dismutase and glutathione peroxidase in the red cells of Japanese acatalasemia blood.

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The activities of superoxide dismutase and glutathione peroxidase in the red cells of normal and acatalasemia bloods were compared. Superoxide dismutase activity in the red cells of Japanese acatalasemia blood was higher than in normal control, while glutathione peroxidase activity remained within

Defense of mouse red blood cells against oxidative damage by phenylhydrazine. Glutathione peroxidase and catalase deficiency.

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Acatalasemia sensitizes renal tubular epithelial cells to apoptosis and exacerbates renal fibrosis after unilateral ureteral obstruction.

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Tissue homeostasis is determined by the balance between oxidants and antioxidants. Catalase is an important antioxidant enzyme regulating the level of intracellular hydrogen peroxide and hydroxyl radicals. The effect of catalase deficiency on renal tubulointerstitial injury induced by unilateral

Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes.

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Genetic deficiencies of glucose-6-phosphate dehydrogenase (G6PD) and NADPH predispose affected erythrocytes to destruction from peroxides. Conversely, genetic deficiencies of catalase do not predispose affected erythrocytes to peroxide-induced destruction. These observations have served to

Determination of glutathione peroxidase activity and its contribution to hydrogen peroxide removal in erythrocytes.

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A new method for the determination of glutathione peroxidase activity in erythrocytes was developed. The present method was applied to the measurement of hydrogen peroxide removal rates by glutathione peroxidase in erythrocytes at 70 microM hydrogen peroxide under simulated in vivo conditions. The

Catalase deficiency renders remnant kidneys more susceptible to oxidant tissue injury and renal fibrosis in mice.

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BACKGROUND Catalase is one of the important antioxidant enzymes regulating the levels of intracellular hydrogen peroxide and hydroxyl radical. The effect of catalase deficiency on progressive renal fibrosis has not been fully elucidated. METHODS Homozygous acatalasemic mutant mice

Acatalasemia and diabetes mellitus.

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The enzyme catalase catalyzes the breakdown of hydrogen peroxide into oxygen and water. It is the main regulator of hydrogen peroxide metabolism. Hydrogen peroxide is a highly reactive small molecule formed as a natural byproducts of energy metabolism. Excessive concentrations may cause significant

Molecular defect in human acatalasia fibroblasts.

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The human hereditary disease Acatalasia (AC) is characterized by low or no catalase activity in all body tissues. We have studied the molecular basis of AC. In order to assess their antioxidant defense status we measured the enzyme activities, protein levels and m-RNA concentrations of catalase,

Inherited catalase deficiency: is it benign or a factor in various age related disorders?

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Hydrogen peroxide was - and is still - considered toxic for a wide range of living organisms. Oxidative stress occurs when there is an excess of pro-oxidants over antioxidants and it has been implicated in several diseases. Catalase is involved in hydrogen peroxide catabolism and is important in

Lipid hydroperoxides induce apoptosis in T cells displaying a HIV-associated glutathione peroxidase deficiency.

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8E5 is a chronically human immunodeficiency virus (HIV)-infected human T cell line, which we have previously shown to be extremely susceptible to hydrogen peroxide (H2O2)-induced apoptosis due to a HIV-associated catalase deficiency. Here we report that HIV gene expression additionally renders 8E5

Peroxisomal catalase deficiency modulates yeast lifespan depending on growth conditions.

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We studied the role of peroxisomal catalase in chronological aging of the yeastHansenula polymorpha in relation to various growth substrates. Catalase-deficient (cat) cells showed a similar chronological life span (CLS) relative to the wild-type control upon growth on carbon and nitrogen sources

Hungarian hereditary acatalasemia and hypocatalasemia are not associated with chronic hemolysis.

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Two Hungarian acatalasemic and eight hypocatalasemic patients revealed normal erythropoesis. Contrary to their decreased defence system against the toxic hydrogen peroxide, the biochemical tests (serum catalase, serum hemoglobin, serum lactate dehydrogenase (LDH) ratio of LDH1 and LDH2 isoenzymes

Importance of catalase in the disposal of hydrogen peroxide within human erythrocytes.

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The catalase within normal, intact human erythrocytes was completely inactivated with amino triazole. The rate of 14CO2 evolution, when the cells were subsequently incubated with 14C-labeled glucose, provided a measure of the rate at which NADPH was being oxidized by the glutathione

The peroxidatic and catalatic activity of catalase in normal and acatalasemic mouse liver.

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Monomeric, dimeric and tetrameric forms of mouse liver catalase have been shown to express peroxidatic activity while the tetrameric form expresses the catalatic activity. Autosomally inherited acatalasemia, produced by X-ray irradiation of mice results in almost complete loss of catalatic activity

Protection of Bacillus larvae from Oxygen Toxicity with Emphasis on the Role of Catalase.

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Sporulation of Bacillus larvae NRRL B-3650 occurred only at aeration rates lower than those used for cultivation of most Bacillus species. One possible explanation for the requirement for a low level of aeration in B. larvae is that toxic forms of oxygen such as H(2)O(2) and superoxide are involved.

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