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PubMed1985

DNA homology studies of the catalase-negative campylobacters and "Campylobacter fecalis," an emended description of Campylobacter sputorum, and proposal of the neotype strain of Campylobacter sputorum.

Twenty-three strains of catalase-negative campylobacters and five strains of "Campylobacter fecalis," which is catalase-positive, were examined by DNA hybridization experiments. These organisms formed four distinct DNA homology groups corresponding to Campylobacter sputorum, Campylobacter mucosalis, Campylobacter concisus, and a currently unnamed group referred to as the "catalase-negative or weak" (CNW) strains. The strains were further characterized to determine which phenotypic characteristics provide the most reliable identification at the species level. Campylobacter sputorum ssp. sputorum, C. sputorum ssp. bubulus, and "C. fecalis" could not be distinguished by DNA homology; consequently, it is proposed that these three taxa be considered as biovars of C. sputorum. The description of C. sputorum is emended accordingly. ATCC strain 35980 is proposed as the neotype strain of C. sputorum.

Campylobacter↗
PubMed1990

Catalase activity in Campylobacter jejuni: comparison of a wild-type strain with an aerotolerant variant.

A comparison of Campylobacter jejuni VPI strain H840 (ATCC 29428), which can grow at O2 levels up to 15%, with variant strain MC711-01 (which can grow at O2 levels up to 21-26%) indicated that the specific activity of catalase in crude cell extracts was higher in the variant by a factor of 1.6 to 2.5, depending on cultural conditions. Smaller differences occurred with superoxide dismutase activity, while peroxidase activities were invariably lower in the variant strain. The variant strain was much more resistant than the wild type to the bactericidal effects of H2O2. The results suggest that catalase activity might be one of the factors associated with the greater tolerance of O2 by the variant strain. However, both strains became more susceptible to H2O2 when cultures were initially grown at 6% O2 and then shifted to 21% O2; thus the role of catalase in the oxygen tolerance of C. jejuni is probably minor.

Campylobacter fetus↗
PubMed1988

Catalase prevents prostanoid release and lung lipid peroxidation after endotoxemia in sheep.

We determined the effect of H2O2 on both the physiological and biochemical lung changes seen in the adult sheep after endotoxin. Fourteen unanesthetized adult sheep with chronic lung lymph fistula were given Escherichia coli endotoxin (1 microgram/kg) over 30 min. Seven sheep were given catalase (32,500 U/kg body wt) as an intravenous bolus 30 min before endotoxin. Four sheep were given catalase alone. Oxidant lung changes were measured using arterial plasma conjugated dienes and lung tissue malondialdehyde (MDA) content, both reflecting the lipid peroxidation process. Animals were killed 5 h after endotoxin. We found that endotoxin alone caused an early increase in pulmonary arterial pressure lung lymph flow (QL), plasma thromboxane B2, 6-keto-prostaglandin F1 alpha, and plasma conjugated dienes. A decrease in cardiac output and arterial PO2 was also seen. A three- to four-fold increase in protein-rich QL was noted at 3-4 h as well as a continued increase in arterial conjugated dienes. Lung MDA and water content were also significantly increased from base line. Catalase pretreatment significantly attenuated both the physiological changes and the prostanoid and conjugated diene release. Lung MDA and water content also remained at base line. We conclude that H2O2 plays a major role in endotoxin-induced lung injury as well as the resulting lipid peroxidation process.

Animals↗
PubMed1991

Human serum catalase decreases endothelial cell injury from hydrogen peroxide.

Serum from normal human subjects contained variable amounts of catalase activity, which was inhibitable by heat, azide, trichloroacetic acid (TCA), or aminotriazole treatment. Serum also decreased hydrogen peroxide (H2O2) concentrations in vitro and H2O2-mediated injury to cultured endothelial cells. By comparison, heat-, azide-, TCA-, or aminotriazole-treated serum neither decreased H2O2 concentrations in vitro nor reduced H2O2-mediated damage to endothelial cells. We conclude that serum catalase activity can alter H2O2-dependent reactions. We speculate that variations in serum catalase activity may alter individual susceptibility to oxidant-mediated vascular disease or be a factor when added to test systems in vitro.

Animals↗
PubMed1992

Changes in catalase activity and its thermolability in liver and kidneys of ageing male garden lizard.

Catalase activity in liver and kidneys of male garden lizards remained unchanged during maturation, but showed an increase during ageing. Instead of inactivating catalase, thermal treatment at 60 +/- 1 degree C caused a marginal increase in enzyme activity in the liver of middle-aged and kidneys of young lizards with no significant effect in old counterparts. Increase in basal enzyme activity during ageing and the maintenance of resistance against thermal inactivation of the enzyme throughout the life-span support the contention that catalase molecules in lizard tissues are not altered as a function of age, a deviation from the predictions of Orgel's error catastrophe hypothesis.

Aging↗
PubMed1986

Antiphlogistic effect of catalase on experimental phacoanaphylactic endophthalmitis.

Oxygen-derived free radicals generated by polymorphonuclear leukocytes have recently been implicated as important pathogenic mediators of tissue damage in immune complex-mediated acute inflammatory reactions. In order to study the role of oxygen radicals in experimentally induced phacoanaphylactic endophthalmitis, rats were immunized with soluble bovine lens protein and, following surgical disruption of the anterior lens capsule, subjected to treatment with catalase. Our data show that phacoanaphylactic endophthalmitis, as determined morphologically and by measurements of retinal edema, choroidal inflammation, retinal hemorrhage and necrotizing vasculitis, is greatly diminished in catalase-treated animals. This protective effect of catalase indicates that hydrogen peroxide (H2O2) and/or conversion products of H2O2 (e.g., hydroxyl radical, hypochlorous acid) may play an important role in the development of experimental phacoanaphylactic endophthalmitis.

Animals↗
PubMed1991

Roles of catalase and the glutathione redox cycle in the regulation of anterior-chamber hydrogen peroxide.

The effects of inhibition of both glutathione synthesis and of glutathione reductase and catalase activities have been determined in the regulation of hydrogen peroxide (H2O2) in the anterior chamber of pigmented rabbits. Glutathione reductase inhibition using intravitreal 1,3-bis-(2-chloroethyl)-1-nitrosourea (BCNU) did not significantly alter either total glutathione or the percent oxidized glutathione fraction in the iris-ciliary body. Intravitreal buthionine sulfoximine (BSO) significantly reduced the total glutathione content of iris-ciliary body and corneal endothelium, while not altering the oxidized fraction. BCNU increased the oxidized fraction of glutathione in the aqueous humor from 22 to 63% without significantly altering total glutathione levels. BSO, however, reduced total glutathione by 70% in the aqueous humor, and the oxidized fraction doubled. Decreases in the reduced glutathione concentration caused by BSO correlate with increases in the normally stable ratio of H2O2 to ascorbate concentrations in the aqueous humor, strongly suggesting that glutathione metabolism is correlated with H2O2 regulation at endogenous levels of this oxidant. Both BSO and 3-aminotriazole (3AT) separately increased the half-time for the loss of exogenously added H2O2 from the anterior chamber. BSO increased the half-time by 77% after 10 microliters of 10 mM H2O2 was injected intracamerally, while suppression of catalase activity with 3AT increased it by only 40%. With intracameral injections of 10 microliters of either 25 or 50 mM H2O2, however, 3AT had a greater effect than BSO. The half-time values after 3AT pretreatment were 61 and 135% greater than control values at the concentrations of 25 and 50 mM H2O2, respectively; those after BSO pretreatment were at 14 and 78%. From these data we conclude that the glutathione redox system protects the anterior segment tissues from hydrogen peroxide at low concentrations of this oxidant, while catalase assumes a greater role at higher concentrations of hydrogen peroxide.

Amitrole↗
PubMed1975

Properties of leukocyte catalase in Swiss type acatalasemia: a comparative study of normals, heterozygotes and homozygotes.

Properties of leukocyte catalase from individuals heterozygous and homozygous for Swiss type acatalasemia were found to differ from those of the normal enzyme as well as interindividually in regard to heat stability and electrophoretic mobility. Molecular hybridization is discussed as a possible explanation for the presence of intermediate catalase species. Antigenic identity of catalase from all sources is confirmed.

Animals↗
PubMed1986

Superoxide dismutase plus catalase improve contractile function in the canine model of the "stunned myocardium".

Fifteen minutes of coronary occlusion followed by reperfusion does not result in myocardial necrosis; however, the contractile function and high energy phosphate content of the previously ischemic myocardium remains depressed or "stunned" for several hours to days after reperfusion. Oxygen-derived free radicals have been implicated in ischemia and reperfusion-induced injury in a variety of tissues. We wished to determine whether administration of free radical scavengers superoxide dismutase plus catalase before and during occlusion, and throughout reperfusion, could attenuate the "stunning" produced by 15 minutes of left anterior descending coronary artery occlusion in anesthetized, open-chest dogs. Segment shortening in the previously ischemic zone recovered to within only +/- 10% of preinfusion values in the control group during 3 hours of reperfusion, while, in the treated dogs, segment shortening returned to a maximum of 56 +/- 16% of preinfusion at 1 1/2 hours post-reperfusion (P less than 0.0003 compared to controls). Similarly, superoxide dismutase + catalase-treated dogs exhibited improved wall thickening during reperfusion (+30% to +70% of preinfusion values), compared to controls (0% to +10%). However, this improvement in contractile function in the treated group was not accompanied by increased adenosine triphosphate stores in the previously ischemic zone (31.8 +/- 0.8 vs. 28.2 +/- 2.2 nmol/mg protein for control vs. treated groups). Infusion of superoxide dismutase + catalase did not influence blood flow during occlusion or reperfusion. However, the treated group did exhibit a significant decrease in blood pressure during reperfusion.(ABSTRACT TRUNCATED AT 250 WORDS)

Adenosine Triphosphate↗
PubMed1992

Individual differences in activity of glutathione peroxidase and catalase studied in monozygotic twins discordant for smoking.

1. Cigarette smoke contains free radicals. The enzymes glutathione peroxidase (GSH-px) and catalase are important parts of the anti-oxidative protecting system. 2. Ten pairs of monozygotic twins, who were discordant for smoking, were analysed in order to determine their erythrocyte glutathione peroxidase and catalase activities and their plasma concentrations of selenium. 3. Analysis of variance (ANOVA) revealed that the difference in activities of catalase and glutathione peroxidase was much less within pairs than between pairs, indicating a large individual variation due to genetic expression or shared environment and no major effect from smoking. 4. The plasma selenium levels of the investigated twins revealed sufficient intake of selenium to maintain maximal activity of GSH-px in erythrocytes. The mean +/- s.d. selenium concentration in plasma for smokers was 98 +/- 16 micrograms l-1 and for non-smokers 111 +/- 16 micrograms l-1. There was no correlation between plasma selenium and glutathione peroxidase in erythrocytes.

Adult↗
PubMed1976

Ultrastructural localization of catalase and L-alpha-hydroxy acid oxidase in microperoxisomes of Hydra.

The ultrastructural localization of catalase and L-alpha-hydroxy acid oxidase (LalphaHAO) was studied in two species of Hydra. Diaminobenzidine reaction product of catalase activity was present in small round or elongated bodies resembling microperoxisomes in the epitheliomuscular, digestive and gland cells. They were closely related to the endoplasmic reticulum, and were often found in proximity to deposits of lipid and glycogen. Reaction product of LalphaHAO activity was also associated with the microperoxisomes. With rapidly oxidized substrates, such as L-lactic acid, reaction product diffused into the cytoplasm around the microperoxisomes. With slowly oxidized substrates, such as DL-alpha-hydroxyisovaleric acid, reaction product was restricted to the matrix of the microperoxisomes. No reaction product was present in the microperoxisomes in the absence of substrate or with D-lactic acid. The rate of substrate oxidation measured biochemically roughly paralleled the amount of cytochemical reaction product deposited with different substrates. Microperoxisome-like bodies reactive for LalphaHAO were also found in the epidermal cnidoblasts; however, catalase could not be demonstrated in them. This study provides the first cytochemical evidence for the presence of an H2O2-producing oxidase in microperoxisomes.

Alcohol Oxidoreductases↗
PubMed1988

Catalase-positive microperoxisomes in rat soleus and extensor digitorum longus muscle fiber types.

The size, distribution, and content of catalase-reactive microperoxisomes were studied cytochemically in slow-twitch oxidative (SO), fast-twitch oxidative glycolytic (FOG), and fast-twitch glycolytic (FG) fibers of soleus and extensor digitorum longus (EDL) rat muscles. Fiber types were classified on the basis of mitochondrial content and distribution, Z-band widths, and myofibril size and shape. Microperoxisomes were generally located between myofibrils at the I-bands. The absence of crystalloid inclusions prevented positive identification of microperoxisomes in nonreacted and aminotriazole-inhibited muscles. EDL and soleus SO fibers possessed the largest microperoxisomes, whereas FOG and FG fibers of the EDL contained small- to medium-sized microperoxisomes. Comparing either microperoxisome number per muscle fiber area or microperoxisome area per fiber area revealed significant differences between fiber types with this ranking: soleus SO greater than EDL SO greater than EDL FOG greater than EDL FG. The present observations demonstrate that the content of catalase-positive microperoxisomes is greatest in the oxidative muscle fiber types. These cytochemical findings account for the higher catalase activity in homogenates of soleus muscles as compared to that of EDL muscles, because the soleus contains more oxidative fibers than EDL.

Animals↗
PubMed2003

Escherichia coli deltafur mutant displays low HPII catalase activity in stationary phase.

Iron is among the most important micronutrients used by bacteria. As a partner of the Fenton reaction, however, iron potentiates oxygen toxicity. Strict regulation of iron metabolism, and its coupling with regulation of defenses against oxidative stress, is an essential factor for life in the presence of oxygen. In Escherichia coli, iron metabolism is regulated by the Fur protein. A Fur-deficient mutant, in stationary phase, displayed about 30y-fold lower HPII activity than the respective, Fur-proficient parental strain. Deletion of fur seems to affect HPII catalase specifically, since the mutant was capable of inducing HPI catalase when challenged with H(2)O(2). Low HPII catalase activity appears to be among the reasons for hydrogen peroxide hypersensitivity of the deltafur mutant.

Bacterial Proteins↗
PubMed1985

The development of antioxidant enzymatic defense in the perinatal rat lung: activities of superoxide dismutase, glutathione peroxidase, and catalase.

This report describes the development of superoxide dismutase, glutathione peroxidase, and catalase activities in fetal (days 16-22) and neonatal (day 2 postpartum) lungs of normal rats. Each of the enzymes showed an individual pattern of development in the perinatal period. Glutathione peroxidase activity increased by 135% (p less than 0.001) during the last 3 days before birth, catalase activity by 105% (p less than 0.01) during the first 2 postnatal days, and the activity of superoxide dismutase by 52% (p less than 0.05) from gestational day 19 to 2 days after birth. Contamination by superoxide dismutase from blood in the lung samples accounted for less than 2% of the activity. In contrast, not less than 10-30% of glutathione peroxidase and catalase originated from the blood; and corrections were made for this source of error in each sample.

Animals↗
PubMed1989

Changes in lipid peroxidation and activities of xanthine oxidase, superoxide dismutase and catalase in kidneys of cephaloridine-administered rats.

To elucidate the toxic and protective mechanisms responsible for cephaloridine (CER)-induced nephrotoxicity, changes in renal formation of malondialdehyde and renal activities of xanthine oxidase, superoxide dismutase and catalase were mainly investigated for 15 days in rats that received single intravenous injections of CER in doses of 100 and 1,000 mg/kg body weight. In the 100 mg/kg group, the above items determined remained within the control levels. In the 1,000 mg/kg group, renal formation of malondialdehyde was observed to be accelerated with the following two stages: highly in the early stage (the 3rd hour to the 2nd day, especially at the 3rd hour) and more highly in the late stage (the 2nd to the 7th day). Concerning the other items determined, significantly different changes were hardly observed in the 1,000 mg/kg group within the 12th hour of the early stage, while the rises in renal activities of xanthine oxidase and falls in renal activities of superoxide dismutase and catalase were observed in the late stage. These results suggested that the increment in malondialdehyde formation in the late stage might be explained enzymatically by both the rises in the activities of xanthine oxidase and the declines in the activities of superoxide dismutase and catalase and that those in the early stage did not relate directly to the above renal enzymatic systems.

Animals↗
PubMed2004

The effects of the sulfonylurea glyburide on glutathione peroxidase, superoxide dismutase and catalase activities in the heart tissue of streptozotocin-induced diabetic rat.

Oxygen free radicals have been suggested to be a contributory factor in diabetes complications. The aim of this study was to examine the effects of glyburide on the antioxidant enzyme activities in the heart tissue of diabetic rats. We investigated the activities of antioxidant enzymes (superoxide dismutase, catalase and glutathione peroxidase) in the hearts of both control and streptozotocin-induced diabetic rats. In the heart of diabetic rats, the activity of total superoxide dismutase decreased significantly (p < 0.005), whereas the activity of catalase and glutathione peroxidase increased to a large extent (p < 0.0001 and p = 0.05, respectively) at the end of the fourth week compared with the control group. Glyburide treatment of diabetic rats for 4 weeks corrected the changes observed in diabetic heart. In addition, blood glucose levels of untreated diabetic rats decreased following the glyburide treatment. These results demonstrate that the sulfonylurea glyburide is capable of exerting direct insulin-like effect on heart superoxide dismutase, catalase and glutathione peroxidase activities of diabetic rats in vivo.

Animals↗
PubMed1980

Superoxide dismutase, catalase and glutathione peroxidase activities in maternal and cord blood erythrocytes.

The "antioxidant" enzymes superoxide dismutase, catalase and glutathione peroxidase were assayed in a biological model with low oxygen tension (red cells from cord blood of newborn infants). Catalase and glutathione peroxidase activities in red cells of newborns were significantly lower when compared with their mothers and with normal controls. In contrast, superoxide dismutase activity was unchanged. Thus, normal activities of superoxide dismutase seem to be necessary in order to protect red blood cells from superoxide radicals during foetal life, while even low activities of catalase and glutathione peroxidase are sufficient to protect red blood cells from hydrogen peroxide. No correlation was found between the "antioxidant" enzyme activities present in cord blood erythrocytes and the bilirubin concentrations during the first days of life.

Adult↗
PubMed1994

Control of superoxide dismutase, catalase and glutathione peroxidase activities in rat lymphoid organs by thyroid hormones.

This study examined the effect of experimental hyper- and hypothyroidism on the superoxide dismutase, catalase and glutathione peroxidase activities of rat lymphoid organs (mesenteric lymph nodes, spleen and thymus) and muscles (soleus and gastrocnemius-white portion) for comparison. The capacity for the generation of reducing equivalents was also investigated: activities of glucose-6-phosphate dehydrogenase (pentose-phosphate pathway) and citrate synthase (Krebs cycle). Hyperthyroidism tended to enhance lipid peroxide content in all tissues. This effect may result from (1) a high capacity for the generation of reducing equivalents in cytosol and mitochondria and (2) a reduced activity of catalase in the lymphoid organs and of glutathione peroxidase in the muscles. The process of lipid peroxidation in these tissues caused by hyperthyroidism was probably slowed down by the augmentation of CuZn- and Mn-superoxide dismutase (Mn-SOD) activities observed under this condition. Hypothyroidism tended to diminish lipid peroxidation and did not affect citrate synthase and glucose-6-phosphate dehydrogenase activities in the lymphoid organs and muscles. Low levels of thyroid hormones tended to diminish Mn-SOD and glutathione peroxidase activities. These findings show that the thyroid hormones might be able to regulate the activities of CuZn- and Mn-SOD, and catalase and glutathione peroxidase in the lymphoid organs and skeletal muscles.

Animals↗