scholarly journals Regulation of aortic CuZn-superoxide dismutase with copper. Effects in vivo

1987 ◽  
Vol 248 (3) ◽  
pp. 663-668 ◽  
Author(s):  
C T Dameron ◽  
E D Harris
Keyword(s):  
Superoxide Dismutase ◽  
Liver Enzyme ◽  
Matched Control ◽  
Gel Filtration ◽  
Sod Activity ◽  
Dietary Copper ◽  
A Subunit ◽  
Cuzn Superoxide Dismutase ◽  
Chick Tissue

Cu2Zn2-superoxide dismutase (CuZn-SOD) was purified from chicken liver. The liver enzyme had a subunit Mr of 16900 and contained equimolar amounts of copper and zinc [0.26% (w/w) for each]. Aortic CuZn-SOD had the same Mr as estimated by gel filtration and cross-reacted with antibodies to the liver enzyme. Both enzymes were inhibited by 1.0 mM-NaCN. Within 24-72 h after hatching, total SOD activity in aorta rose 3-fold over the day-1 level and stayed elevated for 10 days. With low dietary copper, the total SOD activity rose as before, but then decayed progressively to non-detectable levels in 10 days. Both the cyanide-sensitive (CuZn-SOD) and insensitive (mangano-SOD) activities fell, but not at the same rate. When the 10-day-old deficient chicks were injected with 0.5 mumol of CuSO4 intraperitoneally, SOD activity in aorta was restored to control levels in about 8 h. Despite non-measurable SOD activity in aorta, extracts from the 15-day-old-deficient-chick tissue contained as much, or slightly more, immunoreactive CuZn-SOD protein as age-matched control tissue. The data show clearly that dietary copper regulates SOD activity in the aortas of young developing animals. They further suggest that a copper deficiency suppresses CuZn-SOD activity without inhibiting synthesis or accumulation of the CuZn protein in this tissue.

scholarly journals The activity of superoxide-dismutase in animal cell culture CHO-K1 after treatment with fullerenol and mytomicine C

2009 ◽  
Vol 63 (3) ◽  
pp. 143-149 ◽  
Author(s):  
Visnja Bogdanovic ◽  
Marija Slavic ◽  
Jasminka Mrdjanovic ◽  
Slavica Solajic ◽  
Aleksandar Djordjevic
Keyword(s):  
Superoxide Dismutase ◽  
Mammalian Cells ◽  
Animal Cell ◽  
Water Soluble ◽  
Cytotoxic Agents ◽  
Antioxidant Defenses ◽  
Free Radical Scavengers ◽  
Sod Activity

Eukaryotic cell survives in predominantly reduced conditions. Homeostasis of cellular redox system is an imperative of cell surviving and its normal metabolism. ROS are well recognized for playing a dual role as both deleterious and beneficial species, since they can be either harmful or beneficial to living systems. These species are mutagenic compounds known to lead to DNA damage, favor cell transformation, and contribute to the development of a variety of malignant diseases. All the effects of oxidants are influenced by the cellular antioxidant defenses. This multilayer system consists of low molecular weight components and several antioxidant enzymes. Superoxide dismutases (SODs) are the only enzymes dismuting superoxide radicals. Mitomycin C, a cross-linking agent, demonstrated genotoxicity in all in vitro and in vivo test systems in mammalian cells and animals. Water-soluble fullerenes are well known as cytotoxic agents for many cell lines in vitro. At the other side, fullerenols are good free radical scavengers and antioxidants both in vitro and in vivo. This paper investigates the effects of fullerenol on survival and fullerenol/ /mytomicine (MMC) treatment on superoxide-dismutase (SOD) activity in CHO-K1 cells. Samples were treated 3 and 24 h with fullerenol (C60(OH)24) at concentration range 0.01-0.5 mg/mL and survival was monitored with dye exclusion test (DET). The activity of total SOD was estimated in samples treated with chosen concentrations of fullerenol and MMC (0.5 and 0.1 mg/mL) after 3 and 24 h of cell incubation. Increasing of C60(OH)24 concentration leads to decreasing of percent of surviving cells 3 and 24 h after incubation. The activity of total SOD enhanced with higher concentration of fullerenol, while decreased in the highest concentration at both experimental points. In samples treated with MMC, as well as in samples treated with fullerenol (0.0625 mg/mL) + MMC was noticed boost in total SOD activity in comparison with controls. Treatment with fullerenol decreased SOD activity in rest of samples treated with MMC. Decreased activity of superoxide-dismutase in almost all samples treated with fullerenol and MMC might be contributed to antioxidative properties of fullerenol. Increased enzyme level at concentration of 0.0625 mg/mL may be due to its prooxidative activity.

scholarly journals Molecular immunocytochemistry of the CuZn superoxide dismutase in rat hepatocytes.

1988 ◽  
Vol 107 (6) ◽  
pp. 2169-2179 ◽  
Author(s):  
L Y Chang ◽  
J W Slot ◽  
H J Geuze ◽  
J D Crapo
Keyword(s):  
Superoxide Dismutase ◽  
Rat Liver ◽  
Oxidant Stress ◽  
Rat Hepatocytes ◽  
Reaction Rates ◽  
Cytoplasmic Matrix ◽  
Cytosolic Proteins ◽  
Cuzn Superoxide Dismutase ◽  
O2 Production

The distribution of CuZn superoxide dismutase (SOD) molecules in subcellular organelles in rat liver hepatocytes was studied using integrated biochemical, stereological, and quantitative immunocytochemical techniques. A known concentration of purified CuZn SOD in 10% gelatin was embedded alongside the liver tissue for the calculation of CuZn SOD concentrations in hepatocyte organelles and total CuZn SOD in the rat liver. Most of the CuZn SOD was located in the cytoplasmic matrix (73.1%) and in the nucleus (11.9%) with concentrations of 1.36 and 0.71 mg/cm3, respectively. Lysosomes contained the highest concentration (5.81 mg/cm3). Only low concentrations were measured in mitochondria (0.21 mg/cm3). Membrane-bound spaces of rough endoplasmic reticulum (ER), smooth ER, and the Golgi system did not contain significant concentrations of the enzyme. By adding up the concentrations in all subcellular compartments, a total liver content of CuZn SOD was established from the immunocytochemical measurements (0.386 +/- 0.028 mg/gm liver) that agreed closely with those obtained by biochemical assays (0.380 +/- 0.058 mg/gm liver). The average distances between two CuZn SOD molecules can be calculated from enzyme concentrations. It was determined that CuZn SOD molecules in the cytoplasmic matrix and nucleus were 34 and 42 nm apart, respectively. In peroxisomes and mitochondria, average intermolecular distance increased to approximately 60 nm and increased to 136 nm in smooth ER. CuZn SOD is a relatively abundant protein in the cytosol of hepatocytes and its distribution overlaps with major sites of O2- production. The efficiency of protection CuZn SOD can provide to cytosolic proteins from attacks by superoxide anion depends on the rate of O2- production, distribution of CuZn SOD relative to cytosolic proteins, and the relative reaction rates between O2- with both cytosolic proteins and CuZn SOD. Future studies of these substrate-enzyme relationships in vivo can lead to a greater understanding of how cells handle oxidant stress.

scholarly journals Skeletal muscle weakness due to deficiency of CuZn-superoxide dismutase is associated with loss of functional innervation

2011 ◽  
Vol 301 (5) ◽  
pp. R1400-R1407 ◽  
Author(s):  
Lisa M. Larkin ◽  
Carol S. Davis ◽  
Catrina Sims-Robinson ◽  
Tatiana Y. Kostrominova ◽  
Holly Van Remmen ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Muscle Weakness ◽  
Muscle Atrophy ◽  
Muscle Stimulation ◽  
Wild Type ◽  
Functional Changes ◽  
Fiber Number ◽  
Cuzn Superoxide Dismutase

An association between oxidative stress and muscle atrophy and weakness in vivo is supported by elevated oxidative damage and accelerated loss of muscle mass and force with aging in CuZn-superoxide dismutase-deficient ( Sod1−/−) mice. The purpose was to determine the basis for low specific force (N/cm2) of gastrocnemius muscles in Sod1−/− mice and establish the extent to which structural and functional changes in muscles of Sod1−/− mice resemble those associated with normal aging. We tested the hypothesis that muscle weakness in Sod1−/− mice is due to functionally denervated fibers by comparing forces during nerve and direct muscle stimulation. No differences were observed for wild-type mice at any age in the forces generated in response to nerve and muscle stimulation. Nerve- and muscle-stimulated forces were also not different for 4-wk-old Sod1−/− mice, whereas, for 8- and 20-mo-old mice, forces during muscle stimulation were 16 and 30% greater, respectively, than those obtained using nerve stimulation. In addition to functional evidence of denervation with aging, fiber number was not different for Sod1−/− and wild-type mice at 4 wk, but 50% lower for Sod1−/− mice by 20 mo, and denervated motor end plates were prevalent in Sod1−/− mice at both 8 and 20 mo and in WT mice by 28 mo. The data suggest ongoing denervation in muscles of Sod1−/− mice that results in fiber loss and muscle atrophy. Moreover, the findings support using Sod1−/− mice to explore mechanistic links between oxidative stress and the progression of deficits in muscle structure and function.

Effects of Nonylphenol on the Enzyme Activity of SOD in Shrimp (Neocaridina heteropoda)

2014 ◽  
Vol 1073-1076 ◽  
pp. 256-258
Author(s):  
Hong Wei Wang ◽  
Qing Chao Xing ◽  
Jie Zhang ◽  
Rui Yin ◽  
Duan Bo Cai ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Enzyme Activity ◽  
Sod Activity ◽  
Physiological Indicators ◽  
Relationship Of ◽  
The Relationship

The effects of different concentrations of nonylphenol on Neocaridina heteropoda were studied through testing the Superoxide Dismutase (SOD) activity in the muscle of N. heteropoda under the nonylphenol stress, then explored the relationship of the time that was N. heteropoda exposed nonylphenol and the in vivo physiological indicators. Results showed the following conclusion: in a certain range, higher concentrations of nonylphenol had heavier influence on SOD activity of shrimps; shrimps were infected significantly when they were exposed to the same concentration of nonylphenol in 2 days; the influence was reduced to the shrimp with the prolonging of time.

No effect of superoxide dismutase on spontaneous development of diabetes in db/db mice

1988 ◽  
Vol 117 (1) ◽  
pp. 99-102
Author(s):  
Ove Berglund ◽  
Kjell Grankvist ◽  
Carina Albiin ◽  
Stefan L. Marklund
Keyword(s):  
Superoxide Dismutase ◽  
B Cells ◽  
Superoxide Radical ◽  
Superoxide Radicals ◽  
Cuzn Superoxide Dismutase

Abstract. B-cells have previously been shown to be very susceptible to damage induced by superoxide radicals, and protection against such damage has been achieved both in vitro and in vivo with superoxide dismutase. During maturation, db/db mice develop diabetes and accumulation of potentially superoxide radical-producing leucocytes can be demonstrated in the islets during the process. To test for the possibility that superoxide radical-induced damage contributes to the development of diabetes, db/db mice were given daily ip injections of 200 mg/kg polyethylene glycolsubstituted CuZn superoxide dismutase. No effect of the treatment could be demonstrated.

scholarly journals Purification and partial characterization of superoxide dismutase from the thermophilic bacteria Thermothrix sp

2004 ◽  
Vol 69 (1) ◽  
pp. 9-16 ◽  
Author(s):  
Svetlana Seatovic ◽  
Ljubinka Gligic ◽  
Zeljka Radulovic ◽  
Ratko Jankov
Keyword(s):  
Molecular Weight ◽  
Superoxide Dismutase ◽  
Specific Activity ◽  
Thermophilic Bacteria ◽  
Noncovalent Interactions ◽  
Gel Filtration ◽  
Antioxidant Defense System ◽  
Exchange Chromatography ◽  
Gel Chromatography ◽  
Sod Activity

Superoxide dismutase (SOD; EC 1.15.1.1), a high molecular weight component of the antioxidant defense system, provided promising results in the treatment of oxidative damage. Thermothrix sp., isolated from thermal spa water in Serbia, showed high superoxide dismutase activity. The SOD, from cell free extract, was purified to homogenity by ammonium sulfate precipitation, Sephadex G 75 gel filtration chromatography and QAE Sephadex ion exchange chromatography. The specific activity of the purified enzyme was 9191 U/mg. The purified enzyme was analyzed and partially characterized. SOD was localized in polyacrylamide gel by activity staining, based on the reduction of nitroblue tetrazolium (NBT) by superoxide. The enzyme molecular weight determined by gel chromatography is 37 kD. According to SDS PAGE it is composed of two subunits of equal size, joined by noncovalent interactions. The isoelectric point, assessed by isoelectric focusing is 5.3. The optimum pH for enzyme activity was in the range of 8 to 10. The optimum temperature for SOD activity was 60 ?C. After one hour of incubation at 40, 50 and 60 ?C the SOD activity increases, but at 80 ?C, the SOD is denaturated. After 24 hours of incubation at 25 ?C SO Dactivity only slightly decreases.

scholarly journals Biochemical Properties and Regulated Gene Expression of the Superoxide Dismutase from the Facultatively Aerobic Hyperthermophile Pyrobaculum calidifontis

2003 ◽  
Vol 185 (21) ◽  
pp. 6340-6347 ◽  
Author(s):  
Taku Amo ◽  
Haruyuki Atomi ◽  
Tadayuki Imanaka
Keyword(s):  
Superoxide Dismutase ◽  
Biochemical Properties ◽  
Activity Measurement ◽  
Gene Encoding ◽  
Sod Activity ◽  
Pyrobaculum Calidifontis ◽  
Highly Active ◽  
Regulated Gene Expression

ABSTRACT Superoxide dismutase (SOD) was purified from a facultatively aerobic hyperthermophilic archaeon, Pyrobaculum calidifontis VA1. The purified native protein from aerobically grown cells exhibited 1,960 U of SOD activity/mg and contained 0.86 ± 0.04 manganese and <0.01 iron atoms per subunit. The gene encoding SOD was cloned and expressed in Escherichia coli. Although the recombinant protein was soluble, little activity was observed due to the lack of metal incorporation. Reconstitution of the enzyme by heat treatment with either Mn or Fe yielded a highly active protein with specific activities of 1,970 and 434 U/mg, respectively. This indicated that the SOD from P. calidifontis was a cambialistic SOD with a preference toward Mn in terms of activity. Interestingly, reconstitution experiments in vitro indicated a higher tendency of the enzyme to incorporate Fe than Mn. When P. calidifontis was grown under anaerobic conditions, a majority of the native SOD was incorporated with Fe, indicating the cambialistic property of this enzyme in vivo. We further examined the expression levels of SOD and a previously characterized Mn catalase from this strain in the presence or absence of oxygen. Northern blot, Western blot, and activity measurement analyses revealed that both genes are expressed at much higher levels under aerobic conditions. We also detected a rapid response in the biosynthesis of these enzymes once the cells were exposed to oxygen.

Isolation of a Wild Morchella spp. Strain and the Effects of its Extract on Ethanol-Induced Gastric Mucosal Lesions in Rats

2011 ◽  
Vol 66 (1-2) ◽  
pp. 55-62
Author(s):  
Wei Wei ◽  
Xia Luo ◽  
Linyong Zheng ◽  
Mengyao Yu ◽  
Nan Jiang ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Sequence Analysis ◽  
Phylogenetic Tree ◽  
Internal Transcribed Spacer ◽  
Protective Effects ◽  
Gastric Lesions ◽  
Sod Activity ◽  
Gastric Mucosal Lesions ◽  
Mucosal Lesions

A Morchella spp. strain was isolated from a wild morel mushroom, and the effects of its mycelia extract on the ethanol-induced gastric mucosal lesions of rats were investigated in vivo. Sequence analysis of internal transcribed spacer suggested that this Morchella spp. strain (strain No. M1) was clustered together with M. conica in the phylogenetic tree. The superoxide dismutase (SOD) activity increased significantly compared to the control. However, the malondialdehyde (MDA) level and myeloperoxidase (MPO) activity decreased significantly compared to the control. These results indicated that M1 is one member of M. conica and the protective effects of M1 extract against the ethanol-induced gastric lesions may be related to the increased SOD activity and decreased MDA level and MPO activity in rats.

scholarly journals Erythrocytic antioxidant system in the administration of new coordination compounds thiosemicarbazide derivatives

2021 ◽  
Vol 64 (5) ◽  
pp. 70-75
Author(s):  
Valeriana Pantea ◽  
◽  
Marina Gamaniuc ◽  
Veaceslav Popa ◽  
◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Antioxidant System ◽  
Coordination Compounds ◽  
Control Level ◽  
Control Group ◽  
Cytotoxic Action ◽  
Sod Activity ◽  
White Rats ◽  
Thiosemicarbazide Derivatives

Background: Currently, there is a growing interest in new local coordination compounds (CC), which demonstrated antitumor properties, but their influence on the erythrocyte antioxidant system has not been studied. The aim of the study: to study the effects of CC, thiosemicarbazide derivatives –TIA-160, CMT-67 and CMJ-33 on indices of the antioxidant system indicators in erythrocytes peripheral blood in vivo experiments. Material and methods: The action of CC on superoxide dismutase, catalase, total antioxidant capacity was evaluated on a group of 34 white rats, randomly divided into 4 groups: the first control group was injected subcutaneously with saline. The other groups (2 – TIA-160, 3 – CMT-67 and 4 – CMJ-33) were given subcutaneously 3 times a week for 30 days, 0.1µM / kg CC. Results: It was established that the TIA-160 compound demonstrated the highest capacity to induce the expression of erythrocyte catalase that exceeded the control level of 1.8, which did not correlate with the enzymatic superoxide dismutase (SOD) activity. Thus, this study showed that there are differences in the mechanisms of action of thiosemicarbazone derivatives. Conclusions: The influence of tested CC on the indices of the antioxidant system is selective. This selectivity may be the base to their strong selective antiproliferative and cytotoxic action on tumor cells, but not on healthy ones.

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