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At least 1,171 records · Page 65Linked to original sources
PubMed2001

A polymorphism in the promoter region of catalase is associated with blood pressure levels.

Catalase is an important antioxidant enzyme that detoxifies H2O2 into oxygen and water and thus limits the deleterious effects of reactive oxygen species (ROS). Because chronic exposure to excess ROS may contribute to vascular damage, we investigated whether genetic variation in catalase was associated with susceptibility to essential hypertension (EHYT) in 324 individuals (at least 50 years old) who were randomly sampled from an isolated population living in Xiangchang, China. They were screened for genetic variation in the promoter of catalase by direct sequencing. In total, four single nucleotide polymorphisms (SNPs) were identified. The association between the SNPs and EHYT was investigated by a linear regression model under phenotypic selection; in our analyses, we used both SBP>150 mmHg and SBP>160 mmHg as thresholds. A SNP 844 bp upstream of the start codon (SNP-844) demonstrated strong evidence of association with EHYT (SBP>150 mmHg: F=5.09, P=0.008; SBP>160 mmHg: F=7.13, P=0.002). This is the first study to implicate genetic variation in catalase in susceptibility to EHYT and suggests that polymorphisms in promoter regions may be particularly relevant to the study of complex diseases.

Aged↗
PubMed2006

Parthenolide-induced apoptosis in multiple myeloma cells involves reactive oxygen species generation and cell sensitivity depends on catalase activity.

The sesquiterpene lactone, parthenolide (PTL), possesses strong anticancer activity against various cancer cells. We report that PTL strongly induced apoptosis in 4 multiple myeloma (MM) cell lines and primary MM cells (CD38(+) high), but barely induced death in normal lymphocytes (CD38(-/+)low). PTL-mediated apoptosis correlated well with ROS generation and was almost completely inhibited by L-N-acetylcysteine (L-NAC), indicating the crucial role of oxidative stress in the mechanism. Among 4 MM cell lines, there is considerable difference in susceptibility to PTL. KMM-1 and MM1S cells sensitive to PTL possess less catalase activity than the less sensitive KMS-5 and NCI-H929 cells as well as normal lymphocytes. A catalase inhibitor 3-amino-1,2,4-triazole enhanced their PTL-mediated ROS generation and cell death. The siRNA-mediated knockdown of catalase in KMS-5 cells decreased its activity and sensitized them to PTL. Our findings indicate that PTL induced apoptosis in MM cells depends on increased ROS and intracellular catalase activity is a crucial determinant of their sensitivity to PTL.

Acetylcysteine↗
PubMed1991

Effect of brief regional ischemia followed by reperfusion with or without superoxide dismutase and catalase administration on myocardial sarcoplasmic reticulum and contractile function.

The effect of reperfusion with and without free radical scavengers on sarcoplasmic reticulum and contractile function was examined in a canine model of 15-minute coronary artery occlusion followed by reperfusion. Dogs were reperfused with (n = 13) or without (n = 16) superoxide dismutase and catalase or were killed at 15 minutes of ischemia (n = 17). Superoxide dismutase and catalase were administered as a bolus (20,000 and 12,500 U/kg, respectively) beginning 1.25 minutes before reperfusion followed by infusion of 16,000 and 12,500 U/kg/hr, respectively. Sarcoplasmic reticulum function was evaluated from the rate of calcium uptake of unfractionated subepicardial, subendocardial, and transmural homogenates determined with and without ruthenium red to close the calcium release channel. Mechanical function was evaluated by means of sonomicrometry. Fifteen minutes of ischemia significantly (p less than 0.05) depressed the sarcoplasmic reticulum calcium uptake rate only in the subendocardium (from 25 +/- 2 to 14 +/- 1 nmol/min/mg without ruthenium red and from 60 +/- 3 to 49 +/- 3 nmol/min/mg with ruthenium red). Reperfusion with or without superoxide dismutase and catalase restored homogenate calcium uptake rates to normal, although severe contractile dysfunction persisted. This indicates that damage to the sarcoplasmic reticulum may not be the major cause of postreperfusion contractile dysfunction. Ischemia-reperfusion caused a decrease in systolic shortening from 19 +/- 2% to 1 +/- 2% with and from 18 +/- 1% to 4 +/- 1% without free radical scavengers (p = NS between groups). Thus administration of superoxide dismutase and catalase beginning shortly before reperfusion had no effect on postreperfusion contractile dysfunction or sarcoplasmic reticulum function.

Animals↗
PubMed1988

A spectrophotometric method for determination of catalase activity in small tissue samples.

A simple and rapid method for determination of catalase activity in small tissue samples is described. Using a new approach, we have exploited the peroxidatic function of catalase for the determination of enzyme activity. The method was based on the reaction of the enzyme with methanol in the presence of an optimal concentration of hydrogen peroxide. The formaldehyde produced was measured spectrophotometrically with 4-amino-3-hydrazino-5-mercapto-1,2,4-triazole (Purpald) as a chromogen. With this method, a detection limit of 12.5 ng of purified catalase from bovine liver was possible, and it was successfully applied to microgram amounts of mouse liver and pancreatic islet homogenates. The catalase activity in liver was about 50 times higher than that in pancreatic islets.

Animals↗
PubMed1989

Catalase activity measurement with the disk flotation method.

Activity measurements of catalase are usually performed with a spectrophotometric method by monitoring the decrease of H2O2 at 240 nm. A different method presented here uses an instrument named Catalase-meter and yields flotation time data which are expressed in tenth of seconds. For the first time, solutions of catalase of different concentrations were tested simultaneously with the two methods, and the Catalase-meter's flotation data were submitted to correlation with international units calculated from spectrophotometric data. The corresponding calibration curve correlates flotation time data to international units. The r2 values thus obtained for the two calibration curves were 0.960 and 0.929, for a range of activity varying from 9.3 to 144.5 international units/ml.

Animals↗
PubMed1987

Induction and inactivation of catalase and superoxide dismutase of Escherichia coli by ozone.

Oxyradicals have been implicated in ozone (O3) toxicity and in other oxidant stress. In this study, we investigated the effects of O3 on the biosynthesis of the antioxidant enzymes catalase and superoxide dismutase in Escherichia coli to determine their role in the defense against ozone toxicity. Inhibition of growth and loss of viability were observed in cultures exposed to ozone. Results also showed an increase in the activities of catalase and superoxide dismutase in cultures exposed to ozone, which was shown to be due to true induction rather than activation of preexisting apoproteins. Cessation of O3 exposure resulted in 30 min of continual high rate of catalase biosynthesis followed by a gradual decrease in the level of the enzyme approaching that of control cultures. This decrease was attributed to a concomitant cessation of de novo enzyme synthesis and dilution of preexisting enzyme by cellular growth. Ozonation of cell-free extracts showed that superoxide dismutase and catalase are subject to oxidative inactivation by ozone. In vivo induction of these enzymes may represent an adaptive response evolved to protect cells against ozone toxicity.

Catalase↗
PubMed1977

On the specific association of porcine erythrocyte catalase caused by formation of disulfide cross-links.

Porcine erythrocyte catalase (hydrogen-peroxide:hydrogen-peroxide oxidoreductase, EC 1.11.1.6) has been purified from porcine blood by DEAE-cellulose column chromatography, ammonium sulfate fractionation and CM-cellulose column chromatography. The purified enzyme was found to associate into larger molecules than the native one when it was stored at 4degrees C for more than one week. The associated molecules can be detected by gel filtration on a Bio-gel A-1.5 m column and disc gel electrophoresis as well as ultracentrifugal analysis. Molecular weights of the associated catalase molecules were about 500 000, 750 000, 1 000 000 and so forth estimated by gel filtration and disc gel electrophoresis, corresponding to dimer, trimer and tetramer respectively, of a native molecule (monomer) with a molecular weight of about 250 000. The association of catalase molecules is found to be time-dependent and to proceed seemingly from monomer through dimer as an intermediate. From the effects of several thiol reagents or reducing reagents on the association process and spectrophotometric titration of SH groups, it is inferred that this specific association of procine erythrocyte catalase is caused by formation of intermolecular disulfide cross-links due to air oxidation of SH groups in the protein moiety.

Animals↗
PubMed1982

The effects of clofibrate and 3-amino-1,2,4-triazole on liver catalase and lipid metabolism in mice.

Clofibrate-treated mice showed a significant decrease in plasma triacylglycerols and a parallel elevation of liver catalase. Repeated administration of aminotriazole to clofibrate-treated mice effectively abolished the elevated catalase activity, but had no significant effect on the reduced plasma triacylglycerol levels. In mice, the hypolipidemic effect of clofibrate may be dissociated from its capacity to elevate liver catalase. Repeated administration of aminotriazole to control mice resulted in significantly lowered carcass fat and plasma triacylglycerol levels even though the liver catalase activity was greatly depressed. The livers of clofibrate-treated mice showed an increase in phospholipid content. Livers of aminotriazole-treated mice showed a decrease in total lipid content, with a profound decrease in free fatty acids and triacylglycerols and a slight increase in phospholipids. The composition of the individual free fatty acids of the liver triacylglycerols showed a shift towards the shorter fatty acids and the nutritionally essential alpha-linolenic acid in clofibrate-treated mice.

Amitrole↗
PubMed1983

Correlation of H2O2 production and liver catalase during riboflavin deficiency and repletion in mammals.

A substantial decrease in liver peroxisomal catalase was found during riboflavin deficiency in rats. This decrease is greater than that found among other hemoproteins and seems to follow decrease in flavin-dependent peroxisomal oxidases. This is not due to a general depression of peroxisomal enzymes, since Cu-dependent urate oxidase activity was not changed. Furthermore, the level of catalase activity as well as flavin-dependent oxidases was restored by riboflavin repletion. These results suggest that hydrogen peroxide, the substrate for catalase produced by several flavoprotein oxidases, induces catalase in mammals as has been indicated for certain bacteria.

Animals↗
PubMed1989

Changes in the expression of superoxide dismutase and catalase as a function of age and dietary restriction.

The activities of superoxide dismutase (Cu/Zn) and catalase were observed to decrease significantly between 6 and 29 months of age in rat liver. The decrease in superoxide dismutase and catalase activity was paralleled by a decrease in the levels of the mRNA species coding for these enzymes and the nuclear transcription of the superoxide dismutase and catalase genes. Life-long dietary restriction was shown to increase the expression (i.e. activities, mRNA levels, and nuclear transcription) of superoxide dismutase and catalase in liver tissue from 18-month-old rats.

Aging↗
PubMed1989

Butyrate increases catalase activity and protects rat pulmonary artery smooth muscle cells against hyperoxia.

A protective effect of butyrate against hyperoxia was found with adult rat pulmonary artery smooth muscle cells. Butyrate (5mM) when added just prior to the hyperoxic exposure (95%) markedly decreased lactate dehydrogenase release from cells during 68 hours of exposure (22% release with butyrate versus 98% without). The uptake and reduction of a tetrazolium compound as another index of cell viability also showed similar improvement with butyrate. Butyrate was associated with a striking increase of catalase to three times the control in the air exposed group while GSH content and the activities of superoxide dismutase and glutathione peroxidase were not significantly changed. In the groups exposed to hyperoxia alone, both enzyme activities were decreased compared to the air exposed controls. When butyrate was present with hyperoxia, the superoxide dismutase was maintained closer to the air exposed control values and the catalase activity remained nearly twice as high as the air exposed control cells. These results suggest that butyrate protects rat pulmonary artery smooth muscle cells from hyperoxia by increasing catalase activity which may help to preserve superoxide dismutase activity. This may be a good model to determine the biological significance of catalase and its interrelationships with other antioxidant systems within the cell.

Animals↗
PubMed1989

Inactivation of low-Km rat liver mitochondrial aldehyde dehydrogenase by cyanamide in vitro. A catalase-mediated reaction.

The inactivation of the affinity chromatography purified low-Km rat liver mitochondrial aldehyde dehydrogenase (ALDH)--free of catalase activity--by the alcohol sensitizing agent cyanamide was studied in vitro. This ALDH-purified preparation was not susceptible to cyanamide inactivation at concentrations up to 2.5 mM. On the other hand, ALDH activity appears to be irreversibly inhibited when the incubation mixture contained ALDH, catalase, NAD+ and cyanamide. Influence of catalase, NAD+ and cyanamide concentrations in the incubation mixtures on the ALDH activity were also established. The time course of the concentration of cyanamide in an incubation mixture when ALDH activity was inhibited by cyanamide in the presence of catalase and NAD+, was evaluated by HPLC. No disappearance of cyanamide was observed for a period of time up to 24 hr. This result suggests that no metabolic conversion of cyanamide to an active inhibitory form takes place, as has been suggested recently.

Aldehyde Dehydrogenase↗
PubMed1990

Effects of hepatic peroxisome proliferators and 12-O-tetradecanoyl phorbol-13-acetate on catalase and other enzyme activities of embryonic cells in vitro.

The effects of the hepatic peroxisome proliferators (HPPs) clofibrate, di-(2-ethylhexyl)-phthalate (DEHP), mono-(2-ethylhexyl)phthalate (MEHP) and 2,4-dichlorophenoxy acetic acid (2,4-D) on the activities of some peroxisome-associated enzymes and marker enzymes for other organelles, have been studied in primary Syrian hamster embryo (SHE) cells and Wistar rat embryo (WRE) cells. The majority of the cells are fibroblast-like. 12-O-Tetradecanoyl phorbol-13-acetate (TPA) was included as it has been suggested that it may act as a peroxisome proliferator. The specific activities of catalase, fatty acyl-CoA oxidase (FAO) and peroxisomal beta-oxidation were approximately 100-fold lower in the embryonic cells than in rat hepatocytes. Other peroxisome-associated oxidases were not detected. The dihydroxyacetone-phosphate acyltransferase (DHAPAT) activity was comparable to that in rat liver. Marker enzymes for other organelles had specific activities comparable to rat hepatocytes. Catalase was shown by digitonin titration to be contained in a peroxisome-like compartment in both SHE and WRE cells. Clofibrate, DEHP and MEHP increased the catalase activity, which might suggest peroxisome proliferation. However, the findings that FAO and peroxisomal beta-oxidation did not increase or only very slightly, argue against peroxisome proliferation. 2,4-D and TPA induced no or only a very slight increase in the catalase activity.

2,4-Dichlorophenoxyacetic Acid↗
PubMed1994

Effect of hydrogen peroxide and catalase on rat cerebellum nitric oxide synthase.

The effect of H2O2 and catalase on isolated rat cerebellum nitric oxide (NO) synthase activity was determined by measuring the conversion of L-[3H]arginine to L-[3H]citrulline. H2O2 (1-5 mM) markedly increased NO synthase activity in the presence of endogenous catalase (72 +/- 4 U/mL). This effect of H2O2 was further increased by exogenous catalase (200 U/mL). Exogenous catalase (0.1 to 1000 U/mL) by itself had no significant effect on NO synthase activity. Nitroblue tetrazolium chloride, an electron acceptor, inhibited NO synthase activity in a concentration-dependent manner. This study suggests that H2O2 is not directly involved in NO synthesis and that the H2O2/catalase stimulation of NO synthase activity may be due to the excess oxygen produced by the H2O2/catalase system.

Amino Acid Oxidoreductases↗
PubMed1982

Determination of erythrocyte superoxide dismutase, catalase, glucose-6-phosphate dehydrogenase, reduced glutathione and malonyldialdehyde in uremia.

Erythrocyte superoxide dismutase (SOD: EC 1.15.1.1), catalase (EC 1.15.1.6), glucose-6-phosphate dehydrogenase (G-6-PD: EC 1.1.1.49), reduced glutathione (GSH) and malonyldialdehyde (MDA) were studied in 27 patients with chronic and 11 patients with acute renal failure. A comparison with 15 age- and sex-matched healthy subjects showed that patients with both acute and chronic renal failure had significantly low G-6-PD (p less than 0.05) values whereas SOD, catalase and MDA showed significantly elevated levels (p less than 0.05). After adequate dialysis or renal transplantation the SOD, G-6-PD, catalase and MDA values returned to normal. The findings suggest that the erythrocyte SOD, catalase, and G-6-PD can undergo an adaptive alteration which however appears reversible.

Acute Kidney Injury↗
PubMed1989

Origin of serum catalase activity in acute pancreatitis.

Serum catalase activity was examined in 96 patients with the oedematous form and in 15 patients with the necrotic form of acute pancreatitis. Total catalase release into plasma was estimated to be 2,140 +/- 947 kU and 4,764 +/- 1,505 kU, respectively. The g equivalents of pancreas were 163 +/- 72 g and 362 +/- 133 g, being 2.03-fold and 4.52-fold higher than the whole mass of pancreas indicating the nonpancreatic origin of the total increase of serum catalase. In both types of acute pancreatitis serum haemoglobin, haematin, haptoglobin and LDH values supported the presence of haemolysis. The volumes of blood were 22.6 +/- 10.1 ml and 50.4 +/- 15.9 ml which are only 0.41% and 0.91% of the total blood volume. Taking these findings into account, in acute pancreatitis the major part of increase of serum catalase can be explained by its release from the erythrocytes.

Acute Disease↗
PubMed1996

Spectrophotometric determination of hydrogen peroxide: catalase activity and rates of hydrogen peroxide removal by erythrocytes.

A new method of hydrogen peroxide determination for the measurement of catalase activity and rates of hydrogen peroxide removal by erythrocytes was described. Hydrogen peroxide was determined by converting it to the indamine dye with a water-soluble ironporphyrin and measuring the absorbance at 590 nm. This method was applied to the assay of catalase in hemolysates from human, rat and mouse blood. The activities obtained were in agreement with those obtained by other methods including UV method. The present method was also applied to the determination of rates of hydrogen peroxide removal by intact erythrocytes from human subjects, rats and mice. Data suggested that normal erythrocytes have substantial capacity to remove extracellular hydrogen peroxide. From the measurement of catalase activity in erythrocytes treated with 3-amino-1,2,4-triazole and rates of hydrogen peroxide removal by the erythrocytes, it is deduced that rate constants related to the hemoglobin content (k/g Hb) for hydrogen peroxide removal by catalase in normal and acatalasemic erythrocytes are 42.0 +/- 6.0 and 8.0 +/- 3.0, respectively.

Amitrole↗
PubMed1975

Blockade by metal complexing agents and by catalase of the effects of arachidonic acid on platelets: relevance to the study of anti-inflammatory mechanisms.

Metal-chelating agents inhibited platelet aggregation and the accompanying generation of rabbit aorta contracting and PG-like activities, when platelets were challenged with arachidonic acid. Inhibition required the presence of the chelating agents in the medium, and was insured by reagents avid for free or protein-bound copper. Catalase also prevented aggregation and generation of pharmacologically active substances; its activity was reversed by aminothiol agents and by Cu2+ and Zn2+, shown previously to potentiate the platelet effects of arachidonic acid. Inhibition by indomethacin was not prevented by amino-thiol drugs nor by Cu2+ or Zn2+. The catalase-induced inhibition was not affected by scavenging of thiol groups; this rules out, as a mechanism of action of catalase, the increased destruction of popoperoxides by glutathione peroxidase, which requires reduced glutathione as hydrogen donor. The results are compatible with the hypothesis that the agent that mediates platelet aggregation by arachidonic acid is a popoperoxide, requiring the presence either of H2O2 or of a similarly catalase-sensitive substance to be generated.

Adenosine Diphosphate↗