Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “CATALASE”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,495 records · Page 83Linked to original sources
PubMed1998

The protective effect of 17 beta-estradiol on vasomotor responses of aorta from cholesterol-fed rabbit is reduced by inhibitors of superoxide dismutase and catalase.

The involvement of endogenous antioxidant enzymes in the protective effect of 17 beta-estradiol against hypercholesterolemia was evaluated on aorta from cholesterol-fed rabbits treated with estradiol. 17 beta-Estradiol, more potent than alpha-tocopherol, restored the acetylcholine-induced relaxation, which was impaired by cholesterol chow, and enhanced the vasorelaxation induced by sodium nitroprusside. Diethyldithiocarbamate (5 mM), a superoxide dismutase (SOD) inhibitor, reduced relaxation to acetylcholine down to the level obtained in cholesterol-fed rabbits not treated with estrogen. This inhibition was dose-dependently reversed by addition of exogenous SOD. Aminotriazole (5 mM), a catalase inhibitor, reduced slightly this response, which was not reversed by exogenous catalase. A similar concentration of diethyldithiocarbamate prevented the potentiation of response to sodium nitroprusside induced by estrogen, whereas aminotriazole had no effect. These results suggest that, on aorta from cholesterol-fed rabbit, superoxide dismutase and catalase are involved in the protective effect of estrogen on the vasomotor response to acetylcholine, but only superoxide dismutase participates in response to sodium nitroprusside.

Acetylcholine↗
PubMed2000

Anovel catalase mutation (a GA insertion) causes the Hungarian type of acatalasemia.

Acatalasemia, a deficiency of enzyme catalase, is an autosomal recessive syndrome with an incidence of 5:106 in Hungary. We have examined the first Hungarian acatalasemic family for the disease-causing mutation. All exons of the catalase gene were screened by PCR-SSCP, PCR-heteroduplex, and nucleotide sequence analysis. The heteroduplex formation detected in exon 2 was verified by nucleotide sequence analysis. We found a GA insertion at nucleotide position 138, increasing the GA repeat number from 4 to 5. This GA insertion caused a frameshift in the amino acid sequence from position 68 to 133 and generated a TGA terminating codon at amino acid position 134. This truncated protein lacks the essential amino acid (histidine 74) in the active center. This finding can explain the decreased blood catalase activity in the Hungarian acatalasemic family.

Acatalasia↗
PubMed1998

Toxic responses and catalase activity of Lemna minor L. Exposed to folpet, copper, and their combination.

Toxicity of copper and folpet--two fungicides widely used on grape--was evaluated on Lemna minor L., a sensitive aquatic weed regularly used for (eco)toxicological studies. Toxicity assessments were based on inhibition of growth and chlorophyll content of L. minor cultures after 7 days. IC10, IC50, and IC90 were determined for both compounds alone and were respectively, 0.03, 0.16, and 0.95 mg liter-1 for copper and 1.20, 7.50, and > 40 mg liter-1 for folpet. When both compounds were combined, the response of L. minor depended on the initial folpet concentration. Indeed, a slight synergy was observed for 5 mg liter-1 folpet, while at folpet concentrations of 20 to 35 mg liter-1, the two fungicides were antagonists. The antagonism was positively correlated with folpet concentration. Antagonism between Cu and folpet could not be explained by a reduced bioavailability of Cu since concentration of free copper in the mixture did not depend on the presence of folpet. One physiological defense response elicited by copper in plants is an increase in catalase activity. Copper and folpet stimulated catalase activity and changes in the activity of the enzyme could not account for the synergy but possibly for the antagonism. Nevertheless, catalase activity increase significantly after a 24-h exposure to 25 micrograms liter-1 of copper. The use of this property as a rapid and sensitive biomarker to monitor the toxicity of xenobiotics alone or in combination and of environmental water is discussed.

Catalase↗
PubMed1994

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.

Neurotrophic factors, in particular NGF, have been shown to potently protect against glutamate-receptor-mediated toxicity. In order to further investigate the mechanism of this protection, we investigated the in vivo effects of fibroblasts, genetically modified to secrete NGF and implanted near the striatum, on striatal excitatory amino acid binding and receptor expression, on the induction of the peroxidative enzyme catalase, and on cellular energy metabolism in the striatum. Seven days after implantation into the corpus callosum of either a genetically altered NGF-producing (NGF[+]) or unaltered parental (NGF[-]) fibroblast cell-line, there is a time point at which NGF[+] cells have been shown to prevent excitotoxic insults. At that time point after implantation, we found that NGF[+] grafts caused a marked increase in catalase mRNA expression in and around the NGF[+] grafts. The NGF[+] grafts also reduced basal levels of striatal ATP when compared to the effects of NGF[-] grafts. No changes were observed in [3H]glutamate binding and NMDA receptor mRNA expression. We conclude that effects of NGF[+] fibroblast grafts on glutamate receptor mediated toxicity are not by direct effects on glutamate receptors or glutamate binding, but rather appear to be a process involving enzymatic induction and modification of cellular energy stores. The observed increase in catalase mRNA suggests that peroxidative metabolism may be involved in these NGF-mediated effects.

Adenosine Triphosphate↗
PubMed1997

Transforming growth factor-betas block cytokine induction of catalase and xanthine oxidase mRNA levels in cultured rat cardiac cells.

We examined the effects of transforming growth factor-beta (TGF-beta) on the mRNA expression of the antioxidative enzymes, catalase, manganese superoxide dismutase (MnSOD), and copper-zinc superoxide dismutase (CuZnSOD), as well as the oxidative enzyme, xanthine oxidase (XO), in cultures of cardiomyocytes, cardiac non-myocytes, and fetal bovine heart endothelial cells. TGF-betas alone had little effect on expression of these enzymes, but treatment with a combination of interleukin-1beta, interferon-gamma, and tumor necrosis factor-alpha increased expression of MnSOD, catalase, and XO in some cell types with little effect on CuZnSOD expression. When TGF-betas were added along with these inflammatory cytokines there was a return to control levels of catalase expression, as well as a dramatic reduction in XO expression. In fetal bovine heart endothelial cells, treatment with inflammatory cytokines increased XO mRNA expression 11.5-fold and inclusion of TGF-betas reduced this 4-5-fold: effects on XO enzyme activity paralleled those seen on mRNA expression. Similar changes in XO expression were seen in cardiomyocytes. In contrast, TGF-betas did not change cytokine-induced MnSOD expression. All three mammalian isoforms of TGF-beta showed similar effects. In summary, TGF-betas may be able to decrease superoxide anion production and subsequent tissue damage by decreasing levels of XO.

Animals↗
PubMed1997

In vitro antiarrhythmic effect of prior whole body hyperthermia: implication of catalase.

The protective effect of heat stress against mechanical dysfunction and myocardial necrosis after prolonged ischemia is well known. We have investigated whether the protective effect of heat stress extends to reperfusion arrhythmias in the isolated perfused rat heart. Rats were exposed to 20 min of 42 degrees C hyperthermia. Twenty-four h later their hearts were isolated, perfused and subjected to a 5-min period of occlusion of the left coronary artery. The incidence and duration of reperfusion arrhythmias were assessed in the 30-min reperfusion period. Prior heat stress led to a reduction in the incidence (from 100 to 60%, P</=0.05) and duration (from 611+/-251 to 62+/-51 s, P</=0.05) of ventricular tachycardia and/or fibrillation, upon reperfusion following a 5-min ischemic period. This prevention of reperfusion arrhythmias was associated with a two-fold increase in endogenous catalase activity and an enhanced heat stress protein hsp 72 and 27 expression. Catalase inhibition by 3-amino triazole (AT) abolished the antiarrhythmic effect of heat stress. The incidence (80 v 100%) and duration (691+/-238 v 989+/-242 s) of reperfusion arrhythmias were not different between the group heat shocked + AT and the group treated only with AT. On the other hand, in the presence of AT, myocardial noradrenaline release was attenuated by prior heat stress (upon stabilization: 3.9+/-0.8 compared to 9.4+/-2.1 pg/ml/g tissue, P</=0.05; upon reperfusion: 42.7+/-7.3 compared to 69.8+/-9.5 pg/ml/g tissue, P</=0.05). In conclusion, heat stress leads to protection against reperfusion arrhythmias occurring after a short ischemic insult, in the isolated rat heart. Heat stress proteins and catalase seem to be implicated in this protective effect. Finally, we have shown that in presence of AT, heat stress decreases myocardial noradrenaline release.

Animals↗
PubMed1998

Rapid one-step isolation of mouse liver catalase by immobilized metal ion affinity chromatography.

A novel and rapid procedure for the isolation of catalase from mouse liver, after prior treatment with the peroxisome proliferator perfluorooctanoic acid was developed using immobilized metal ion affinity chromatography involving chelation with zinc ions. The purification developed is simple, rapid (requiring 3 hours from cytosol or peroxisomal matrix to homogeneous proteins), reproducible, and yields virtually complete overall recovery of catalase activity. This procedure makes catalase from a variety of tissues and physiological and environmental conditions more readily available for study.

Animals↗
PubMed1996

Retinal nitro blue tetrazolium staining and catalase activity in rat models of diabetes.

BACKGROUND: Recent studies have suggested that reactive oxygen species may be involved in the development of diabetic retinopathy. METHODS: Nitro blue tetrazolium (NBT) staining, a marker of reductants which may be induced by free radicals such as superoxide, and catalase activity, as an indirect measure of hydrogen peroxide (H2O2) generation, were studied in the rat retina in three conditions known to cause diabetes-like retinopathy, i.e. rats with spontaneous diabetes (the BB Wistar rat), rats with streptozotocin-induced diabetes mellitus, and rats fed on galactose. Male Wistar BB rats were studied 4-10 weeks after diagnosis of diabetes. Streptozotocin (60 mg/kg) was injected i.p. at 8 weeks of age and the experiments were performed after 8 weeks of diabetes. Young Sprague-Dawley rats were fed a 50% galactose diet for 9, 12 or 22 months. RESULTS: In trypsinized vessel preparations, more intense NBT staining was observed only in rats fed a galactose diet for 22 months. In cross sections, the number of stained vessels were increased in BB rats (p < 0.01), but not in rats with streptozotocin-induced diabetes. Catalase activity did not differ between any of the experimental groups and their matched controls. CONCLUSIONS: Increased amount of NBT reductants in retinal vessels occurred in BB Wistar rats and to some extent in galactose-fed rats, indicating a possible role for free radicals in the development of diabetic retinopathy. There was no evidence of increased retinal H2O2 production or activation of catalase, indicating that this particular enzyme was not affected during the conditions studied.

Animals↗
PubMed1985

Gene order on the short arm of human chromosome 11: regional assignment of the LDH A gene distal to catalase in two translocations.

Leukemic cells with reciprocal translocations involving 11p13 and 14q13 were obtained from two patients with T-cell acute lymphoblastic leukemia and fused with mouse Ltk- cells. DNA from independent hybrid clones was screened by Southern blot and hybridization to molecular probes for the human catalase and Ha-ras-1 genes. Several clones showed segregation of these two genes, indicating the presence of either the der11 or der14 human chromosomes. When DNA from these hybrid clones was examined for the presence of the human genes for calcitonin and gamma-globin, both genes were found to segregate with the Ha-ras-1 gene and the der14 chromosome indicating that they lie distal to catalase. When the hybrid clones were examined for the presence of human lactate dehydrogenase A (LDH A) activity, only those clones containing the der14 chromosome expressed activity indicating that the LDH A gene is also distal to catalase on the short arm of chromosome 11.

Animals↗
PubMed1993

The effect of supplementing hypothermic crystalloid cardioplegia with catalase plus allopurinol in the isolated rabbit heart.

The effect of adding allopurinol and catalase to hypothermic cardioplegia for ischemic-reperfusion injury was investigated in the isolated rabbit heart. Hearts were divided into two groups, namely: Group C (n = 7), which received a hypothermic crystalloid cardioplegic solution alone (4 degrees C), and group T (n = 7), which received the hypothermic cardioplegic solution with allopurinol (148 mumol/L)13 and catalase (37 nmol/L).12 The cardioplegic solution was infused continuously into the isolated hearts, which had been placed in ice-cold saline, during a 12 h preservation. Subsequently, the hearts were mounted on a noncirculating, nonpulsatile perfusion circuit using Krebs-Henseleit buffer solution at 37 degrees C for 1 h at a constant perfusion pressure of 75 mm Hg. The left ventricular developed pressure (LVDP), maximum rate of pressure change (max dp/dt), and percent recovery of coronary flow were higher, while the creatine phosphokinase concentration and left ventricular end diastolic pressure (LVEDP) were lower in group T. The tissue malondialdehyde concentration and water content were similar in both groups. Thus, cardiac function after a 12 h preservation was enhanced by the added combination of allopurinol and catalase to the cardioplegic solution, supporting its role in the prevention of free radical reperfusion injury in cardiac preservation.

Allopurinol↗
PubMed1993

Induction of glucose oxidase, catalase, and lactonase in Aspergillus niger.

The induction of glucose oxidase, catalase, and lactonase activities was studied both in wild-type and in glucose oxidase regulatory and structural mutants of Aspergillus niger. The structural gene for glucose oxidase was isolated and used for Northern analysis and in transformation experiments using various gox mutations. Wild-type phenotype could be restored in the glucose oxidase-negative mutant (goxC) by transformation with the structural gene. We conclude, therefore, that the goxC marker which is located on chromosome 2 represents the structural gene of glucose oxidase. Glucose and a high oxygen level are necessary for the induction of all three enzyme activities in the wild-type strain and it was shown that both glucose and oxygen effects reflect regulation at the transcriptional level. The goxB mutation results in constitutive expression of all three activities although modulated to some extent by the carbon source. The goxE mutation only has an effect on lactonase and glucose oxidase expression and does not relieve the necessity for a high oxygen level. Catalase and lactonase could not be induced in the glucose oxidase-negative strain (goxC). Addition of H2O2 resulted in the induction of all three enzymes in the wild-type without glucose being present. The H2O2 induction is probably mediated by the goxB product. Besides the H2O2 induction there is still an effect of the carbon source on the induction. A model for induction of glucose oxidase, catalase, and lactonase in A. niger is discussed.(ABSTRACT TRUNCATED AT 250 WORDS)

Aspergillus↗
PubMed1980

Comparative investigations of catalase activity in different ocular tissues of cattle and man.

As previously published, ocular catalase activity was measured by Warburg's respirometer, the examined material being taken from the local slaughterhouse and keratoplasty-donor eyes. The results were given in microliter O2 per mg soluble protein (Biuret's solution) and showed an extensive parallelism between human and bovine eyes: They were in a decreasing order of catalase activity, i.e., conjunctiva > retina > vitreous > sclera > iris > choroid > cornea > aqueous humor > serum > lens. In the latter, catalase activity was a sensitive indicator of aerobic metabolism. Oxidative processes in the vitreous merit more consideration.

Animals↗
PubMed1978

Catalase positive particles from pig lung. Biochemical preparations and morphological studies.

In pig lung tissue catalase positive particles (CPs) are abundant especially in type II pneumocytes and in Clara cells. In both cell types they occur as circular, oval or elongated membrane profiles surrounding a moderately electron dense matrix lacking a crystalline core. In Clara cells and in part of type II pneumocytes they are located as individual particles without any evident morphological relation to other cell organelles. In part of type II pneumocytes 5-8 particles are forming a group and their close relation to agranular endoplasmic reticulum cisterns is evident. The particles can be purified from lung homogenates by fractionated pelleting and subsequent rate sedimentation in a sucrose gradient using a zonal rotor. The catalase rich fraction bands in the middle of the gradient whereas cytochrome oxidase and part of the acid phosphatase sediments at its heavy end. A second part of acid phosphatase stays at the light end of the gradient and--according to morphological control--seems to correspond to lamellar bodies of the type II pneumocytes. The purified catalase positive particles do not contain hydroxyacid and D-aminoacid oxidases thought to be characteristic H2O2 producing enzymes of peroxisomal systems. The buoyant density of the particles (d = 1.195 g/cm3) is lower than that of liver peroxisomes. Cytochemical controls of the peroxisomal pellets exhibit the particles partly uniformly filled with reaction product, partly irregularly stained.

Acid Phosphatase↗
PubMed1981

Quantitation of catalase activity by microspectrophotometry after diaminobenzidine staining.

The absorbance of the reaction product of catalase staining with diaminobenzidine is linearly proportional to enzyme activity. This is shown in semithin Epon sections of model systems containing serum albumin and catalase from bovine or guinea pig liver. Absorbance measurements were also performed on semithin sections of guinea pig liver, and from these, the activity of cytoplasmic (extraperoxisomal) catalase has been derived.

3,3'-Diaminobenzidine↗
PubMed1982

Chromosome abnormalities involving 11p13 and low erythrocyte catalase activity.

Two unrelated patients with clinical features of 11p13 deletion syndrome, 3 years old and 3 months old, are reported. The clinical features of the patients included mental retardation, aniridia, nystagmus, blepharophimosis, and genitourinary abnormalities. Both patients were apparently free from Wilms' tumor and gonadoblastoma. Prometaphase banding analyses revealed a 46,XY,del(11)(p1300p1500) karyotype in one patient and 46,XX,dir ins(11;2)(p13;q12q23) in the other. Catalase activities in the erythrocytes in the two patients were respectively 65% and 56% of those of normal controls, close to the expected values in hemizygosity of the catalase gene. These findings confirmed a close linkage of the gene for catalase and those for the aniridia--Wilm's tumor or gonadoblastoma complex.

Catalase↗
PubMed1981

Selective cytochemical localization of peroxidase, cytochrome oxidase and catalase in rat liver with 3,3'-diaminobenzidine.

In rat liver, three different enzymes with peroxidatic activity are demonstrated with modifications of the DAB-technique: peroxidase in the endoplasmic reticulum of Kupffer cells, catalase in peroxisomes and cytochrome oxidase in mitochondria. The major problem of the DAB-methods is their limited specificity so that often in tissues incubated for one enzyme the other two proteins are also stained simultaneously. We have studied the conditions for selective staining of each of these three enzymes in rat liver fixed either by perfusion with glutaraldehyde or by immersion in a modified Karnovsky's glutaraldehyde-formaldehyde fixative. The observations indicate that in perfusion fixed material selective staining can be obtained by reduction of the incubation time (5 min) and the use of optimal conditions for each enzyme. In livers fixed by immersion the distribution of the staining is patchy and irregular and usually longer incubation times (15-30 min) are required. Selective staining of peroxidase in Kupffer cells was obtained by brief incubation at room temperature in a medium containing 2.5 mM DAB in cacodylte buffer pH 6.5 and 0.02% H2O2. The exclusive staining for cytochrome oxidase in cristae of mitochondria was achieved after short incubation in 2.5 mM DAB in phosphate buffer pH 7.2 containing 0.05% cytochrome c. For selective demonstration of catalase in peroxisomes the tissue was incubated in 5 mM DAB in Teorell-Stenhagen (or glycine-NaOH) buffer at pH 10.5 and 0.15% H2O2. The prolongation of the incubation time in peroxidase medium caused marked staining of both mitochondria and peroxisomes. In the cytochrome oxidase medium longer incubations led to slight staining of peroxisomes. The catalase medium was quite selective for this enzyme so that even after incubation for 120 min only peroxisomes stained.

3,3'-Diaminobenzidine↗
PubMed1985

Human vascular smooth muscle cells and endothelial cells lack catalase activity and are susceptible to hydrogen peroxide.

51Cr release as lytic and cell detachment as nonlytic injury were employed to estimate neutrophil-mediated injury of cultured human vascular smooth muscle cells and endothelial cells. The reagents hydrogen peroxide or hypoxanthine-xanthine oxidase produced dose-dependent killing and nonlytic cell detachment, which were specifically inhibited by catalase but not by superoxide dismutase. The concentration of hydrogen peroxide or xanthine oxidase to induce cell detachment was less than lytic dose, suggesting that cell detachment was a much more sensitive assay of injury. Neutrophil-mediated cell lysis averaged 15% at most and was mostly dependent on hydrogen peroxide, while neutrophil-mediated cell detachment was nearly 100% and its dependency on hydrogen peroxide varied from 46% to 60%. These results suggest that vascular smooth muscle cells and endothelial cells in neutrophil-mediated events are destroyed by a hydrogen peroxide-dependent process, mainly via a nonlytic cell detachment mechanism. There was no striking difference of sensitivity to hydrogen peroxide between vascular smooth muscle cells and endothelial cells. Vascular smooth muscle cells and endothelial cells contained fairly high concentrations of superoxide dismutase, but not catalase, activity. The sensitivity of these cells to hydrogen peroxide but not to superoxide may arise from the fact that these cells lack intracellular catalase activity. The injury of vascular cells, which constitute important components of blood vessels, may lead to vascular injury and subsequent tissue damage.

Blood Vessels↗
PubMed1994

Superoxide dismutase, catalase, and U78517F attenuate neuronal damage in gerbils with repeated brief ischemic insults.

Repeated ischemic insults at one hour intervals result in more severe neuronal damage than a single similar duration insult. The mechanism for the more severe damage with repetitive ischemia is not fully understood. We hypothesized that the prolonged reperfusion periods between the relatively short ischemic insults may result in a pronounced generation of oxygen free radicals (OFRs). In this study, we tested the protective effects of superoxide dismutase (SOD) and catalase (alone or in combination), and U78517F in a gerbil model of repetitive ischemia. Three episodes (two min each) of bilateral carotid occlusion were used at one hour intervals to produce repetitive ischemia. Superoxide dismutase and catalase were infused via osmotic pumps into the lateral ventricles. Two doses of U78517F were given three times per animal, one half hour prior to each occlusion. Neuronal damage was assessed 7 days later in several brain regions using the silver staining technique. The Mann-Whitney U test was used for statistical comparison. Superoxide dismutase showed significant protection in the hippocampus (CA4), striatum, thalamus and the medial geniculate nucleus (MGN). Catalase showed significant protection in the striatum, hippocampus, thalamus, and MGN and the substantia nigra reticulata. Combination of the two resulted in additional protection in the cerebral cortex. Compared to the controls, there was little protection in a dose of 3 mg/kg of U78517F. There was significant protection with a dose of 10 mg/kg in the hippocampus (CA4), striatum, thalamus, medial geniculate nucleus and the substantia nigra reticulata.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗