Possible accumulation of non-active molecules of catalase and superoxide dismutase in S. cerevisiae cells under hydrogen peroxide induced stress

2007 ◽  
Vol 2 (3) ◽  
pp. 326-336 ◽  
Author(s):  
Maria Bayliak ◽  
Halyna Semchyshyn ◽  
Volodymyr Lushchak
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Experimental Conditions ◽  
Sod Activity ◽  
Sublethal Doses ◽  
Cell Densities ◽  
Enzyme Molecules ◽  
High Level ◽  
Inhibitor Of Protein Synthesis ◽  
Stress Protectant

AbstractThe effect of hydrogen peroxide on the activities of catalase and superoxide dismutase (SOD) in S. cerevisiae has been studied under different experimental conditions: various H2O2 concentrations, time exposures, yeast cell densities and media for stress induction. The yeast treatment with 0.25–0.50 mM H2O2 led to an increase in catalase activity by 2–3-fold. At the same time, hydrogen peroxide caused an elevation by 1.6-fold or no increase in SOD activity dependently on conditions used. This effect was cancelled by cycloheximide, an inhibitor of protein synthesis in eukaryotes. Weak elevation of catalase and SOD activities in cells treated with 0.25–0.50 mM H2O2 found in this study does not correspond to high level of synthesis of the respective enzyme molecules observed earlier by others. It is well known that exposure of microorganisms to low sublethal concentrations of hydrogen peroxide leads to the acquisition of cellular resistance to a subsequent lethal oxidative stress. Hence, it makes possible to suggest that S. cerevisiae cells treated with low sublethal doses of hydrogen peroxide accumulate non-active stress-protectant molecules of catalase and SOD to survive further lethal oxidant concentrations.

Further investigation of the mechanism of Vitreoscilla hemoglobin (VHb) protection from oxidative stress in Escherichia coli

Biologia ◽  
2011 ◽  
Vol 66 (5) ◽  
Author(s):  
Meltem Akbas ◽  
Tugrul Doruk ◽  
Serhat Ozdemir ◽  
Benjamin Stark
Keyword(s):  
Oxidative Stress ◽  
Escherichia Coli ◽  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Stationary Phase ◽  
Exponential Phase ◽  
Vitreoscilla Hemoglobin ◽  
Sod Activity ◽  
E Coli ◽  
Hydrogen Peroxide Treatment

AbstractIn Escherichia coli, Vitreoscilla hemoglobin (VHb) protects against oxidative stress, perhaps, in part, by oxidizing OxyR. Here this protection, specifically VHb-associated effects on superoxide dismutase (SOD) and catalase levels, was examined. Exponential or stationary phase cultures of SOD+ or SOD− E. coli strains with or without VHb and oxyR antisense were treated with 2 mM hydrogen peroxide without sublethal peroxide induction, and compared to untreated control cultures. The hydrogen peroxide treatment was toxic to both SOD+ and SOD− cells, but much more to SOD− cells; expression of VHb in SOD+ strains enhanced this toxicity. In contrast, the presence of VHb was generally associated in the SOD+ background with a modest increase in SOD activity that was not greatly affected by oxyR antisense or peroxide treatment. In both SOD+ and SOD− backgrounds, VHb was associated with higher catalase activity both in the presence and absence of peroxide. Contrary to its stimulatory effects in stationary phase, in exponential phase oxyR antisense generally decreased VHb levels.

Superoxide dismutase isoelectric focusing patterns as a tool to differentiate pathotypes of Globodera spp.

Nematology ◽  
2010 ◽  
Vol 12 (5) ◽  
pp. 751-758 ◽  
Author(s):  
Sergio Molinari ◽  
Nicola Greco ◽  
Miloslav Zouhar
Keyword(s):  
Cluster Analysis ◽  
Superoxide Dismutase ◽  
Isoelectric Focusing ◽  
Cyst Nematode ◽  
Globodera Pallida ◽  
Data Matrix ◽  
Sod Activity ◽  
Isozyme Electrophoresis ◽  
Fourth Group ◽  
High Level

Abstract Isoelectric focusing was used to separate proteins from cyst extracts of potato cyst nematode (PCN) populations. In a first set of assays, cyst extracts from standard populations of Globodera rostochiensis pathotypes Ro1, Ro2, Ro3, Ro2/3, Ro4, and Ro5, and G. pallida pathotypes Pa2 and Pa3, were loaded on isoelectric focusing gels. Gels were stained for superoxide dismutase (SOD), esterase, and glucose-6-phosphate isomerase (GPI). Twelve bands of SOD activity were detected, six (B1-B6) migrating towards the basic zone and the other six (A1-A6) migrating towards the acidic zone, starting from the loading point. A cluster analysis was carried out based on a data matrix that reported the presence or absence of SOD bands on the isozyme electrophoresis patterns (IEPs). Globodera spp. were clearly distinguished and, within G. rostochiensis, Ro2 and Ro4 shared a high level of similarity, respectively, with Ro3 and Ro5; moreover, Ro1 could be clearly distinguished from Ro2/3 and Ro4/5. Globodera pallida Pa2 and Pa3 also shared a high level of similarity. In contrast, esterase and GPI IEPs did not discriminate among G. rostochiensis standard pathotypes. Subsequently, 14 field populations of G. rostochiensis, five from Italy and nine from Venezuela, and three field populations of G. pallida, two from Italy and one from Chile, were assayed to obtain SOD IEPs. Italian populations had previously been identified at pathotype level by bioassays according to the generally accepted international test using different resistant potato cultivars and clones. The cluster analysis carried out on the SOD IEPs of all the populations tested formed four distinct groups within G. rostochiensis and only one within G. pallida. Pathotype identification of Globodera populations by SOD IEPs was not able to discriminate between bioassay standard couples Ro2/Ro3, Ro4/Ro5 and Pa2/Pa3. Therefore, three groups were assigned to Ro1, Ro2/3 and Ro4/5, and a fourth group to Pa2/Pa3. Four Venezuelan populations, not identified at pathotype level by bioassays, formed a distinct fifth group. By means of the method described herein, four additional unknown Venezuelan populations could be assigned to Ro1 group and one to Ro2/Ro3 group; one G. pallida population from Chile was assigned to Pa2/Pa3 group.

Superoxide dismutase mimetic drug tempol aggravates anti-GBM antibody-induced glomerulonephritis in mice

2010 ◽  
Vol 299 (2) ◽  
pp. F445-F452 ◽  
Author(s):  
Hua Lu ◽  
Junhui Zhen ◽  
Tianfu Wu ◽  
Ai Peng ◽  
Ting Ye ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Basement Membrane ◽  
Glomerular Basement Membrane ◽  
Immunohistochemical Staining ◽  
Treated Group ◽  
First Line ◽  
Sod Activity ◽  
Leukocyte Influx

Oxidative stress plays an important role in the pathogenesis of anti-glomerular basement membrane antibody-induced glomerulonephritis (anti-GBM-GN). Superoxide dismutase (SOD) is the first line of defense against oxidative stress by converting superoxide to hydrogen peroxide (H2O2). We investigated the effect of the SOD mimetic drug tempol on anti-GBM-GN in mice. 129/svJ mice were challenged with rabbit anti-mouse-GBM sera to induce GN and subsequently divided into tempol (200 mg·kg−1·day−1, orally) and vehicle-treated groups. Routine histology, SOD and catalase activities, malondialdehyde (MDA), H2O2, and immunohistochemical staining for neutrophils, lymphocytes, macrophages, p65-NF-κB, and osteopontin were performed. Mice with anti-GBM-GN had significantly reduced renal SOD and catalase activities and increased H2O2 and MDA levels. Unexpectedly, tempol administration exacerbated anti-GBM-GN as evidenced by intensification of proteinuria, the presence of severe crescentic GN with leukocyte influx, and accelerated mortality in the treated group. Tempol treatment raised SOD activity and H2O2 level in urine, upregulated p65-NF-κB and osteopontin in the kidney, but had no effect on renal catalase activity. Thus tempol aggravates anti-GBM-GN by increasing production of H2O2 which is a potent NF-κB activator and as such can intensify inflammation and renal injury. This supposition is supported by increases seen in p65-NF-κB, osteopontin, and leukocyte influx in the kidneys of the tempol-treated group.

scholarly journals NFAT is required for spontaneous pulmonary hypertension in superoxide dismutase 1 knockout mice

2013 ◽  
Vol 304 (9) ◽  
pp. L613-L625 ◽  
Author(s):  
Juan Manuel Ramiro-Diaz ◽  
Carlos H. Nitta ◽  
Levi D. Maston ◽  
Simon Codianni ◽  
Wieslawa Giermakowska ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Pulmonary Hypertension ◽  
Superoxide Dismutase ◽  
Nuclear Localization ◽  
Vascular Reactivity ◽  
Arterial Wall ◽  
Pulmonary Arteries ◽  
Systolic Pressure ◽  
Sod Activity ◽  
Pulmonary Arterial

Elevated reactive oxygen species are implicated in pulmonary hypertension (PH). Superoxide dismutase (SOD) limits superoxide bioavailability, and decreased SOD activity is associated with PH. A decrease in SOD activity is expected to increase superoxide and reduce hydrogen peroxide levels. Such an imbalance of superoxide/hydrogen peroxide has been implicated as a mediator of nuclear factor of activated T cells (NFAT) activation in epidermal cells. We have shown that NFATc3 is required for chronic hypoxia-induced PH. However, it is unknown whether NFATc3 is activated in the pulmonary circulation in a mouse model of decreased SOD1 activity and whether this leads to PH. Therefore, we hypothesized that an elevated pulmonary arterial superoxide/hydrogen peroxide ratio activates NFATc3, leading to PH. We found that SOD1 knockout (KO) mice have elevated pulmonary arterial wall superoxide and decreased hydrogen peroxide levels compared with wild-type (WT) littermates. Right ventricular systolic pressure (RVSP) was elevated in SOD1 KO and was associated with pulmonary arterial remodeling. Vasoreactivity to endothelin-1 was also greater in SOD1 KO vs. WT mice. NFAT activity and NFATc3 nuclear localization were increased in pulmonary arteries from SOD1 KO vs. WT mice. Administration of A-285222 (selective NFAT inhibitor) decreased RVSP, arterial wall thickness, vasoreactivity, and NFAT activity in SOD1 KO mice to WT levels. The SOD mimetic, tempol, also reduced NFAT activity, NFATc3 nuclear localization, and RVSP to WT levels. These findings suggest that an elevated superoxide/hydrogen peroxide ratio activates NFAT in pulmonary arteries, which induces vascular remodeling and increases vascular reactivity leading to PH.

Superoxide dismutase (SOD) activity ofDictyocaulus viviparusand its inhibition by antibody from infected and vaccinated bovine hosts

Parasitology ◽  
1994 ◽  
Vol 109 (2) ◽  
pp. 257-263 ◽  
Author(s):  
C. Britton ◽  
D. P. Knox ◽  
M. W. Kennedy
Keyword(s):  
Superoxide Dismutase ◽  
Protective Immunity ◽  
Igg Antibody ◽  
Sod Activity ◽  
Dictyocaulus Viviparus ◽  
Chemical Assay ◽  
Parasite Stage ◽  
Copper Zinc ◽  
High Level ◽  
Antibody Inhibition

SUMMARYThe presence of superoxide dismutase (SOD) activity in the bovine lungwormDictyocaulus viviparuswas examined using the xanthine–xanthine oxidase assay system and by non-denaturing PAGE followed by specific enzyme staining. High levels of activity were detected in excretory–secretory (ES) products of adult worms and in soluble extracts of both the L3 and adult stages of the parasite. Stage-specific and ES-specific activities were indicated by differences in SOD isoenzyme profiles between adult and larval parasite extracts and between adult extract and ES products, with a fast migrating activity being specific to ES products. All isoenzymes were sensitive to cyanide, indicating copper/zinc dependency. The antigenicity of ES SOD was demonstrated by a reduction in SOD activity in both the chemical assay and non-denaturing PAGE following incubation of parasite ES products with IgG antibody purified from serum of infected or vaccinated bovine hosts. The high level of SOD activity released by adultD. viviparusmay be a reflection of the problems faced by a parasite occupying an oxygen-rich environment. Antibody inhibition of SOD may, therefore, be an important target of protective immunity.

Mechanism of oxidative stress in skeletal muscle atrophied by immobilization

1993 ◽  
Vol 265 (6) ◽  
pp. E839-E844 ◽  
Author(s):  
H. Kondo ◽  
I. Nakagaki ◽  
S. Sasaki ◽  
S. Hori ◽  
Y. Itokawa
Keyword(s):  
Oxidative Stress ◽  
Skeletal Muscle ◽  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
High Performance ◽  
Superoxide Anions ◽  
Glutathione S Transferase ◽  
Sod Activity ◽  
Cytochemical Study ◽  
Male Wistar Rats

To clarify the mechanism of oxidative stress in skeletal muscle atrophied by immobilization, we measured the activities of antioxidant enzymes and xanthine oxidase (XOD) and carried out the cytochemical study of hydrogen peroxide in a typical slow red muscle, the soleus. Male Wistar rats (15 wk old), of which ankle joints of one hindlimb were immobilized in the fully extended position, were killed after 4, 8, or 12 days. The activities of Mn-containing superoxide dismutase (Mn-SOD), Cu-Zn-containing superoxide dismutase (Cu-Zn-SOD), Se-dependent glutathione peroxidase (Se-GSHPx), glutathione S-transferase, catalase, and glutathione reductase were measured spectrophotometrically. The XOD activity and the concentrations of hypoxanthine, xanthine, and urate were measured using a high-performance liquid chromatography. The cytochemical study of hydrogen peroxide in short-term organ culture was performed using an electron microscope. Increased Cu-Zn-SOD and decreased Mn-SOD in atrophy might reflect increased generation of superoxide anions in the cytoplasm rather than in the mitochondria. The source of superoxide anions in the cytoplasm might be the increased superoxide-producing XOD. Enhanced generation of superoxide anions and increased Cu-Zn-SOD activity in atrophy suggested the enhanced generation of hydrogen peroxide in the cytoplasm. Due to the unchanged activity of Se-GSHPx and the unchanged or slightly increased activity of catalase in atrophy, the ability to degrade hydrogen peroxide might not increase so much. Hence, hydrogen peroxide is expected to be increased in atrophy. The cytochemical study supported this expectation.(ABSTRACT TRUNCATED AT 250 WORDS)

Stabilization of electroluminescence and photoluminescence of porous n-silicon by chemical oxidation in H2O2

1994 ◽  
Vol 358 ◽  
Author(s):  
F. Kozlowski ◽  
W. Wagenseil ◽  
P. Steiner ◽  
W. Lang
Keyword(s):  
Hydrogen Peroxide ◽  
Porous Silicon ◽  
Chemical Oxidation ◽  
Time Stability ◽  
Initial Value ◽  
Experimental Conditions ◽  
Long Time ◽  
Pl Intensity ◽  
High Level ◽  
Long Time Stability

ABSTRACTWe have oxidized porous (n-)silicon samples in solutions of H202 and have found that PL can be stabilized at a high level. The PL intensity of as prepared samples (PL quantum efficiencies in the range of 5 %) degrades to about 1/3 of the initial value in some ten minutes (the exact value depends on the experimental conditions). After having treated the samples for about 30 - 45 minutes in hydrogen peroxide it can be observed that bright PL remains stable for hours. These results confirm similar experiments performed with porous silicon made from p-substrates1. While red electroluminescing samples have shown long time stability for about 100 hours2, samples with blue-green electroluminescence have a lifetime of about 20 - 40 minutes. Oxidizing electroluminescent samples as described above results in a stabilization of electroluminescence for more than 7 hours.

scholarly journals Antioxidant enzymes activity in ‘Castel Gala’ apple trees after the budbreak inducers application

2021 ◽  
pp. 1051-1057
Author(s):  
Léo Omar Duarte Marques ◽  
Caroline Hernke Thiel ◽  
Gabrielle Leivas de Leivas ◽  
Sidnei Deuner ◽  
Mateus da Silveira Pasa ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Antioxidant Enzymes ◽  
Calcium Nitrate ◽  
Fruit Trees ◽  
Mineral Oil ◽  
Apple Trees ◽  
Sod Activity ◽  
Efficient Treatment ◽  
Enzymes Activity

Since antioxidant enzymes activity affects the end of dormancy stage, it is important to understand the responses given by antioxidant enzymes and their roles in budbreak induction in temperate fruit trees. This research aimed at evaluating the antioxidant enzymes activity at the end of budbreak stage after the inducers application to ‘Castel Gala’ apple trees and their performance in budbreak and blooming. Seven treatments were carried out: Erger® 3% + calcium nitrate 5%; Erger® 5% + calcium nitrate 5%; Erger® 7% + calcium nitrate 5%; garlic extract (GE) 5% + mineral oil (MO) 2%; GE 10% + MO 2%; GE 15% + MO 2%; and the control. Buds were collected one, four and seven days after the application (DAA) of budbreak inducers, and activity of the following enzymes was determined by: superoxide dismutase (SOD), catalase (CAT) and ascorbate peroxidase (APX). Besides that, hydrogen peroxide was quantified. Percentages of budbreak and blooming were evaluated at 32th, 40 th, 45 th and 52 th DAA. The results showed that SOD activity had increased as the dormancy stage reached its end. CAT activity was influenced by the application of budbreak inducers. It decreased significantly throughout the experiment in the most efficient treatment. Percentages of budbreak (61.85%) and blooming (25.44%) showed the highest efficiency in the treatment with Erger® 7% + calcium nitrate 5%, which was the inducer with the highest potential in ‘Castel Gala’ apple trees

Superoxide dismutase and catalase in Frankia

1986 ◽  
Vol 32 (5) ◽  
pp. 409-413 ◽  
Author(s):  
D. Bernie Steele ◽  
Mark D. Stowers
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Nitrogen Fixation ◽  
Methyl Viologen ◽  
Nitrogenase Activity ◽  
Nitrogen Fixing ◽  
Additional Mechanism ◽  
Sod Activity ◽  
Cell Extracts ◽  
Cell Components

Superoxide dismutase (SOD) and catalase (CAT) are important enzymes in the protection of cell components from oxidation via superoxide free radicals [Formula: see text] and hydrogen peroxide (H2O2). SOD and CAT activities in Frankia, under non-nitrogen fixing conditions, are among the highest reported in prokaryotes. A sixfold increase in SOD activity (2150 units/mg of protein) and a twofold increase in CAT activity (413 units/mg of protein) was seen in cultures derepressed for nitrogen fixation compared with ammonium-grown cultures. Frankia possesses a manganese-containing SOD (MnSOD) when grown with ammonium as the nitrogen source. An additional SOD isozyme containing iron (FeSOD) was detected in cell extracts when grown with dinitrogen. Methyl viologen induced higher activity of the MnSOD in ammonium-grown cultures but failed to induce the FeSOD. During derepression of nitrogenase activity, the simultaneous induction of SOD and CAT was detected. The presence of a new iron-containing SOD under nitrogen-fixing conditions could provide an additional mechanism for protection from O2 toxicity.

Superoxide, Xanthine Oxidase and Platelet Reactions: Further Studies on Mechanisms by which Oxidants Influence Platelets

1981 ◽  
Vol 45 (03) ◽  
pp. 290-293 ◽  
Author(s):  
Peter H Levine ◽  
Danielle G Sladdin ◽  
Norman I Krinsky
Keyword(s):  
Superoxide Dismutase ◽  
Cytochrome C ◽  
Xanthine Oxidase ◽  
Direct Effect ◽  
Platelet Function ◽  
Experimental Conditions ◽  
Release Reaction

SummaryIn the course of studying the effects on platelets of the oxidant species superoxide (O- 2), Of was generated by the interaction of xanthine oxidase plus xanthine. Surprisingly, gel-filtered platelets, when exposed to xanthine oxidase in the absence of xanthine substrate, were found to generate superoxide (O- 2), as determined by the reduction of added cytochrome c and by the inhibition of this reduction in the presence of superoxide dismutase.In addition to generating Of, the xanthine oxidase-treated platelets display both aggregation and evidence of the release reaction. This xanthine oxidase induced aggreagtion is not inhibited by the addition of either superoxide dismutase or cytochrome c, suggesting that it is due to either a further metabolite of O- 2, or that O- 2 itself exerts no important direct effect on platelet function under these experimental conditions. The ability of Of to modulate platelet reactions in vivo or in vitro remains in doubt, and xanthine oxidase is an unsuitable source of O- 2 in platelet studies because of its own effects on platelets.

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