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At least 1,135 records · Page 63Linked to original sources
PubMed1999

A method for determining the cytoprotective effect of catalase in transiently transfected cell lines and in corneal tissue.

Both when developing gene constructs for therapeutic purposes and when testing the biological function of proteins, it would be convenient to use cells or tissues that have been transiently transfected with the gene of interest. However, determining the protective effects of transient gene expression is complicated by a low transfection efficiency, resulting in only a minority of the cells expressing the introduced gene and consequently a reduced sensitivity of assays measuring the death of transfected cells. In this study we have developed a convenient technique for determining cell death in transiently transfected vascular endothelial cell monolayers and in corneal tissue. Vascular endothelial cells were cotransfected with human catalase cDNA and the lacZ gene encoding beta-galactosidase, under conditions in which cells expressing beta-galactosidase also expressed catalase. By assaying release of beta-galactosidase upon cell death, it was possible to show that catalase transfection led to significant protection against the cytotoxic effect of increasing concentrations of hydrogen peroxide. The assay was adapted to demonstrate the protective effects of catalase transfection on hydrogen peroxide-mediated injury of intact corneal endothelium under ex vivo culture conditions. This assay should also be useful for characterizing the cytoprotective effects of other genes in transient transfection systems.

Animals↗
PubMed1995

A novel human catalase mutation (358 T-->del) causing Japanese-type acatalasemia.

Japanese-type acatalasemia is characterized by the almost total loss of catalase activity in red cells and is often associated with ulcerating oral lesions. A splicing mutation in intron 4 of catalase gene has so far been a sole disease-causing mutation found in Japanese-type acatalasemic patients. We report here a novel single base deletion in the catalase gene causing Japanese-type acatalasemia. The patient was a 72 year-old Japanese male. His maternal grandmother and his father were first cousins. Molecular analysis using non-RI PCR-SSCP analysis combined with direct sequencing revealed a deletion of the 358th thymine in exon 4 of the patient's catalase gene. The proband was a homozygote and his mother and his three children were heterozygotes for this mutation. The frame shift caused by the nucleotide deletion should alter the downstream amino acid sequence and introduce a new termination codon TGA 43 bp 3' to the mutation. Although the truncated peptide chain consisted of 133 amino acid residues might be translated in the patient's tissue, such an aberrant protein is expected to be extremely unstable and have no catalytic function at all. Our results suggest that Japanese-type acatalasemia is heterogeneous.

Acatalasia↗
PubMed1995

Superoxide dismutase and catalase enhance autoxidation during one-electron reduction of aminochrome by NADPH-cytochrome P-450 reductase.

NADPH-cytochrome P-450 reductase catalyzes one-electron reduction of aminochrome to the corresponding ortho-semiquinone, which was found to be unstable as indicated by the occurrence of NADPH oxidation and oxygen consumption. The addition of superoxide dismutase and catalase, alone or together, to the incubation mixture, during reduction of aminochrome catalyzed by NADPH-cytochrome P-450 reductase, did not prevent the autoxidation of ortho-semiquinone, but instead they increased NADPH oxidation. These results contrast with the almost complete inhibition of autoxidation (NADH oxidation) of ortho-hydroquinone during reduction of aminochrome catalyzed by DT-diaphorase in the presence of both superoxide dismutase and catalase. However, the effect of superoxide dismutase and catalase on oxygen consumption was found to differ from the effect on NADH or NADPH oxidation, since these enzymes, alone or together, inhibited the oxygen consumption during the reduction of aminochrome catalyzed by both NADPH-cytochrome P-450 reductase and DT-diaphorase. These results support the proposed role of NADPH-cytochrome P-450 reductase in neurodegeneration as a consequence of activation of aminochrome to reactive oxygen species. In addition, they also support the protective and antioxidant role of DT-diaphorase, together with superoxide dismutase and catalase, by competing with NADPH-cytochrome P-450 reductase to reduce aminochrome to ortho-hydroquinone and prevent the formation of reactive oxygen species. A possible mechanism is proposed.

Animals↗
PubMed1995

Effects of superoxide dismutase and catalase during reduction of adrenochrome by DT-diaphorase and NADPH-cytochrome P450 reductase.

NADPH-cytochrome1 P450 reductase and DT-diaphorase catalyze and one- and two-electron reduction of adrenochrome to its o-semiquinone and o-hydroquinone, respectively. Under aerobic conditions both adrenochrome o-semiquinone and o-hydroquinone proved to be unstable, undergoing autoxidation with concomitant oxygen consumption and continuous NADPH and NADH oxidation. Molecular oxygen was found to play a predominant role in autoxidation of o-semiquinone during reduction of adrenochrome catalyzed by NADPH-cytochrome P450 reductase. In addition, molecular oxygen, in the presence of manganese, was found to be responsible for the majority of autoxidation of o-semiquinone. However, the role of superoxide radicals in the autoxidation of leucoadrenochrome during the reduction of adrenochrome by DT-diaphorase was found to be predominant. Catalase different significantly with respect to NADPH and NADH oxidation during reduction of adrenochrome catalyzed by NADPH-cytochrome P450 reductase and DT-diaphorase. Catalase increased NADPH oxidation slightly, while NADH oxidation was inhibited during reduction of adrenochrome by NADPH cytochrome P450 reductase and DT-diaphorase, respectively. 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. A marked difference in the inhibitory effect of superoxide dismutase on oxygen consumption during adrenochrome reduction catalyzed by NADPH-cytochrome P450 reductase and DT-diaphorase was also observed. A possible mechanism for reduction of adrenochrome by NADPH-cytochrome P450 reductase and DT-diaphorase and a role for superoxide dismutase and catalase are proposed.

Adrenochrome↗
PubMed1994

Levels of expression of the genes for glutathione reductase, glutathione peroxidase, catalase and CuZn-superoxide dismutase in rat lens and liver.

Oxidative mechanisms are thought to play a major role in several biological phenomena, including cataract formation. In the following studies we determined the relative levels of expression of the genes for the mRNAs for glutathione peroxidase (GPx), glutathione reductase (GR), CuZn-superoxide dismutase (CuZn-SOD) and catalase, in both the rat lens and liver. Northern blot hybridization methods were used to determine the mRNA size. The RNase protection method was used to determine levels of expression for these mRNAs plus levels of expression for alpha A-crystallin and gamma-crystallin mRNAs in the lens, and gamma-actin mRNAs in both the lens and the liver; using [32P]-labeled specific cRNA probes transcribed from the various cDNA clones for the mRNAs being studied. The data was normalized relative to the level of expression of alpha A-crystallin and gamma-actin mRNAs in the lens, and to gamma-actin mRNA in the liver. We find the levels of the mRNAs in the lens fall in the following descending order: GPx > GR > CuZn-SOD > catalase, in the same order as has been reported for the activities of the enzymes in the lens. In the liver, levels of these mRNAs were as follows: GPx > CuZn-SOD > GR > catalase. In the liver, CuZn-SOD mRNA was expressed at about four times the level found in the lens, GPx at three times, catalase at three times and GR at about the same level.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1998

The effect of catalase amplification on immortal lens epithelial cell lines.

Utilizing a human beta-actin promoter, a catalase cDNA expression vector was constructed. This construct was used to transfect two immortal cell lines, mouse alpha TN4-1 and rabbit N/N 1003A. The catalase activity was increased about 3.4 fold in the alpha TN4-1 cells and 38 fold in the N/N 1003A cells. Some changes in other enzyme activities were also observed as a result of the transfections. Surprisingly, the ability to degrade H2O2 in the extracellular environment of the cells did not markedly change as a result of the catalase amplification. However, the ability to resist H2O2 stress was dramatically altered. Non-protein thiol (NP-SH) levels, choline uptake and glyceraldehyde phosphate dehydrogenase (GPD) activity were all markedly decreased in the non-transfected cells when they were subjected to 300 microM H2O2. However, in both transfected cell lines, these parameters remained in the normal range during H2O2 stress. The results obtained upon observing aspects of DNA metabolism were more complicated. While on H2O2 stress, non-transfected cell lines showed a marked decrease in thymidine incorporation, only the transfected alpha TN4-1 line remained in the normal range. Thymidine incorporation in transfected rabbit N/N 1003A cells was decreased compared to normal cells. In contrast, studies on single strand DNA breaks indicated that transfected rabbit cells had little damage compared to the significant DNA damage observed in the normal cells. The normal N/N 1003A cells were also much more susceptible to H2O2 induced damage than normal alpha TN4-1 cells, suggesting that the high GSH peroxidase activity observed in the rabbit cells may be detrimental since the low glutathione reductase activity in such cells results in an accelerated depletion of glutathione. The overall results suggest that augmenting lens catalase may prevent cataract development caused by H2O2 stress.

Animals↗
PubMed1993

Superoxide dismutase plus catalase therapy delays neither cell death nor the loss of the TTC reaction in experimental myocardial infarction in dogs.

Studies to test whether superoxide dismutase (SOD), with or without catalase, limits myocardial infarct size have produced conflicting results. Positive results following short periods of reperfusion vs negative results following longer periods of reperfusion could be explained if either: (1) myocytes, initially salvaged by SOD, are killed by continued production of free radicals after the administered SOD have been excreted, or (2) false positive results occur because SOD transiently preserves the TTC reaction, despite loss of cellular viability. To evaluate these two possibilities, we measured infarct size after 90 min of ischemia and 4 h of reperfusion in SOD+catalase treated and untreated dogs. Treated dogs received a 60 min intra-arterial infusion of SOD (15,000 U/kg) plus catalase (CAT) (55,000 U/kg) beginning 25 min before reperfusion. Infarct size was measured using triphenyl tetrazolium (TTC) macrochemistry and was compared with the extent of necrosis assessed semi-quantitatively by light microscopy. Mean infarct size was similar in the control and treated groups. In addition, there was a positive linear correlation (r = 0.95) between the extent of necrosis estimated by microscopy and that estimated by TTC in both groups, and treatment did not alter the regression line. These current results were compared with results from the control dogs from our previous study (Richard et al., 1988) in which 90 min of ischemia was followed by 4 days of reperfusion. TTC-based infarct size at 4 days of reperfusion was similar to that observed in both groups at 4 h. These data indicate that oxygen free radicals, accessible to intravascular SOD and catalase, are not a cause of myocyte death detectable by measurement of infarct size after 4 h of reperfusion. Moreover, neither an "early protection, delayed death" hypothesis nor a specific preservation of the TTC reaction explain the positive results of other studies. TTC macrochemistry provides reliable estimates of myocardial infarct size, provided that sufficient magnification is used to permit resolution of interdigitating peninsulas of viable and necrotic tissue.

Animals↗
PubMed1996

Chronic exposure of neonatal cardiac myocytes to hydrogen peroxide enhances the expression of catalase.

The adaptive response of antioxidant enzymes to oxidative stress in the heart has not been investigated. Because H2O2 is considered to play a major role in reperfusion injury to the heart, this study was undertaken to examine if H2O2 alters the expression of these enzymes in the rat neonatal myocytes. H2O2 was continuously generated by the addition of glucose oxidase to the culture medium. Both the activity and the mRNA for catalase were increased following incubation of neonatal myocytes with non-toxic concentrations of glucose oxidase. The induction of mRNA preceded the enhancement of activity, and both remained elevated after 24 h incubation. Nuclear run-on assay indicated that the transcriptional rate for catalase mRNA was increased. The same treatment did not alter the activities for total superoxide dismutase and Se-glutathione peroxidase. The results suggest that H2O2-induced expression of catalase was in part due to transcriptional activation. It further implies that the induction of catalase may play an important role in protecting hearts from ischemic/reperfusion injury.

Animals↗
PubMedDate not supplied

Human erythrocyte catalase: 2-D crystal nucleation and production of multiple crystal forms.

Negatively stained electron microscope images are presented, showing the nucleation of two-dimensional (2-D) crystals of human erythrocyte catalase produced on mica by the negative staining-carbon film technique. Examples of the formation of partially ordered 2-D arrays and more ordered 2-D crystals are shown and the conditions required for the production of large well-ordered 2-D crystals discussed. The structural transformation of one flexuous 2-D paracrystal into a p2 2-D crystal is considered. The crystallographic 2-D image average of this p2 crystal form is presented (lattice parameters a = 9.0 nm, b = 18.6 nm, gamma = 90.8 degrees). It is shown that transmission electron microscopy provides the possibility of defining 2-D crystal nucleation, growth of intermediate forms, and low-resolution crystallographic structural analysis of 2-D crystals of human erythrocyte catalase. Comparison of the various electron microscopical negatively stained images with the peptide backbone of the X-ray structure of bovine liver catalase at different tilt and rotation positions correlates with and emphasizes the multiple intermolecular contacts and orientations that can be adopted by human erythrocyte catalase, leading to various 2-D arrays and 2-D crystals. Alignment of the surface groups involved in the protein-protein interactions that occur during 2-D crystal nucleation and crystal growth may ultimately be determined. From this approach, when taken together with detailed consideration of protein-solvent and protein-solute electrostatic interactions in solution, and at the fluid-air interface, it is considered that a more general theory of crystal nucleation and growth may eventually emerge.

Aluminum Silicates↗
PubMed1996

Blood superoxide dismutase, catalase and glutathione peroxidase activities in familial and sporadic amyotrophic lateral sclerosis.

Recent studies have implicated free radicals in the pathogenesis of amyotrophic lateral sclerosis (ALS), a fatal, paralytic disorder of motor neurons. Herein we report on measurements of erythrocyte activity of the three main free radical scavenging enzymes: copper/zinc superoxide dismutase (Cu/Zn-SOD), catalase, and glutathione peroxidase. We studied 31 patients with sporadic ALS, 18 with familial ALS, and 24 controls, Mean Cu/Zn-SOD activity was reduced in eight familial ALS patients with mutations of Cu/Zn-SOD but was normal in patients with both familial ALS without identified Cu/Zn-SOD mutations and sporadic ALS. Glutathione peroxidase activity was significantly reduced only in sporadic ALS patients treated with insulin-like growth factor I (100 micrograms/kg). Catalase activity was normal in sporadic and familial ALS. Neither glutathione peroxidase nor catalase activities correlated significantly with duration of symptoms or age at onset. Vitamin E, vitamin C, and beta-carotene did not affect any of the three enzyme activities. These observations indicate that disturbances of catalase and glutathione peroxidase function are not likely to be central factors in the pathogenesis of ALS.

Age of Onset↗
PubMed1986

On the multiplicity of the enzyme catalase in mammalian liver.

The literature on the complex multiplicity of mammalian catalase and the nature of the epigenetic modifications undergone by this enzyme has been reviewed, along with relevant comment on the subcellular localization and biological role of the enzyme. The epigenetic causations of multiplicity are established as being multifactorial and include oxidoreductive conversions of sulphydryl groups, the covalent attachment of carbohydrate, and partial proteolysis of the enzyme. Each of these epigenetic transformations may give rise to sets of multiple forms, and overlaps between these separate sets may give rise to extremely complex multiplicity patterns. It is concluded that any interpretation of catalase multiplicity which places emphasis on a single epigenetic causation is not compatible with the scope and variety of the available data on this enzyme. Instead, a holistic approach is urged - one giving due emphasis to the multiple causation of catalase multiplicity, and the interrelationships of these causations in the cellular situation. Rather than viewing the multiplicity of this enzyme as merely a series of interesting chemical modifications, emphasis is directed towards the fact that catalase heterogeneity provides a sensitive indication of the functional variations which occur within separate compartments of the subcellular structure, and hence becomes an essential element in any satisfactory understanding of the role of this enzyme in cellular processes.

Animals↗
PubMed1996

An increase of acidic isoform of catalase in red blood cells from HIV(+) population.

A systemic oxidative stress of HIV (+) individuals has been recognized from a low glutathione level and a high level of inflammatory cytokines such as TNF alpha. Previously, we demonstrated that the catalase enzyme activity in HIV (+) population is significantly altered depending on the cell types; the level was significantly high in red blood cells while the enzymes in white blood cells were remarkably low (Res Commun Subs Abuse 16: 161-176, 1995). In this study, we further characterized the difference in RBC catalase molecules between HIV (+) and control population. We have found that RBC from HIV (+) population, whether they were asymptomatic or symptomatic, contained a significantly elevated catalase protein accompanied by the enzyme activities, and that the majority of the elevated protein were acidic pI of the molecules with an identical subunit mass of approximately 60 KDa. These results suggest that catalase is induced prior to and/or during erythroid differentiation lineage in HIV (+) population as a somatic defense to respond and compensate for a systemic oxidative stress and for an anemic condition.

Adult↗
PubMed1986

Use of catalase polymorphisms in the study of sporadic aniridia.

Catalase is known to map at chromosome 11p13. It is one of the closest known markers to the WAGR locus. Restriction fragment length polymorphisms (RFLP) of the catalase gene may be invaluable for studying rearrangements in somatic tumours, linkage in cases of familial Wilms tumour, and the relationship between sporadic and familial aniridia. We describe a catalase RFLP with two different enzymes and use these polymorphisms to exclude deletion of the catalase gene in patients with sporadic aniridia, including one who is known to have a deletion and another suspected of having a deletion.

Catalase↗
PubMed1993

Regulation of Saccharomyces cerevisiae catalase gene expression by copper.

Treatment of Saccharomyces cerevisiae cells with copper induces the activity of Cu/Zn superoxide dismutase (SOD) and catalase. To understand the level at which Cu regulates catalase, the expression of the S. cerevisiae CTA1 (encoding the peroxisomal catalase A) and CTT1 (encoding the cytosolic catalase T) genes was monitored as a function of Cu treatment. Copper was found to specifically induce transcription of CTT1, but not CTA1, mRNA. Moreover, genetic and biochemical studies demonstrate that this induction is independent of the ACE1 Cu trans-activator controlling the expression of yeast Cu/Zn SOD and metallothionein genes. Copper regulation of CTT1 thus appears to represent a novel metal regulatory pathway in S. cerevisiae cells.

Blotting, Northern↗
PubMed1979

A comparative immunological study of catalases from coagulase-positive staphylococci.

Protein homology studies with catalase as a reference point were carried out with coagulase-positive staphylococci belonging to Staphylococcus aureus, S. intermedius and S. hyicus. Antisera against catalases of S. aureus ATCC 12600 and S. aureus ATCC12601 reacted very weakly employing double immunodiffusion and quantitative microcomplement-fixation assay with cell-free extracts or catalase enriched preparations of S. intermedius or S. hyicus. The differences between coagulase-positive staphylococci could be confirmed by using the antiserum against S. intermedius H 11 catalase. Within the strains of the species S. intermedius immunological distances ranging up to 25 indicate a heterogeneity which justify the separation of the biotypes E and F on a subspecies level. Coagulase-positive strains of S. hyicus revealed neither a close relationship to S. aureus nor to S. intermedius.

Animals↗
PubMed1975

Cytochemical discrimination between catalases and peroxidases using diaminobenzidine.

The influence on diaminobenzidine staining of four variables: prefixation in aldehyde, temperature and pH of incubation, and H2O2 concentration, was investigated in catalase-, as well as in peroxydase-containing material. Catalase from five different sources and five types of peroxidase were examined. It is concluded: (a) when cells are incubated without prior fixation, in a DAB medium at room temperature and pH 7.3 with 0.003% H2O2, peroxidases produce a visible cytochemical stain, while catalases do not; (b) the cytochemical reaction elicited by catalases is stimulated by prior aldehyde fixation in specified conditions, and incubation at 45 degrees C and pH 9.7 with 0.06% H2O2; (c) under the latter circumstances several peroxidases also stain. Ultrastructural preservation is satisfactory in tissues incubated prior to fixation.

Aminobiphenyl Compounds↗
PubMed1976

Enzymic and morphological studies on catalase positive particles from brown fat of cold adapted rats.

Brown adipose tissue of normal and cold-adapted adult rats has been investigated morphologically and cytochemically. In thin-sections catalase-positive particles appear as circular, oval or elongated profiles lying either as single particles or forming groups. Biochemical studies on peroxisomal enzymes show an increase of catalase activity to the tenfold amount after cold adaptation. The tissue is devoid of D-aminoacid oxidase and glycolate oxidase, while low activities of middle-chain-alpha-hydroxyacid oxidases could be detected. The catalase-positive particles were purified by differential and is lower than that of the liver peroxisomes. Enzymic investigations of the fractions render it probably that particles contain carnitine acetyltransferase, whereas they are lacking NAD-dependent glycerophosphate dehydrogenase. The pellets derived from the gradient centrifugation have been checked morphologically for purity. After performing DAB-cytochemistry for identification of the peroxidatic activity of catalase, most of the particles were shown to be structurally intact and homogeneously filled with reaction product.

Adipose Tissue, Brown↗
PubMed1979

Cytochemical detection of catalase with 3,3'-diaminobenzidine. A quantitative reinvestigation of the optimal conditions.

The influence of various parameters of fixation and incubation upon the oxidation of DAB by catalase have been analyzed. Crystalline beef liver catalase was fixed with different concentrations of glutaraldehyde and peroxidatic activity was determined spectrophotometrically using DAB as hydrogen donor. Although aldehyde fixation appeared to be important in elicitation of the peroxidatic activity of catalase, the final pigment production after 60 min incubation was optimal with the lowest concentration of glutaraldehyde (1%), after the shortest fixation period (30 min), and at the lowest temperature (5 degrees C) tested. Similarly cytochemical studies with rat kidney sections incubated for 10 min confirmed that the staining of peroxisomes in proximal tubules was strongest after the "mildest" fixation conditions. The pH and the temperature of incubation were closely interrelated, so that at room temperature (25 degrees C) the maximal pigment production was obtained at pH 10.5, but incubation at 45 degrees C gave the strongest staining at pH 8.5. The production of pigment increased with higher DAB concentrations which required larger amounts of H2O2 in the incubation medium. Cytochemical studies on renal peroxisomes were in agreement with these biochemical findings. The observations indicate that there are several options for the localization of catalase depending on the fixation and incubation conditions. Hence, these conditions should be selected according to the tissue and the purpose of the study. Examples for such selective applications are presented.

3,3'-Diaminobenzidine↗