Vanadium effect on the activity of horseradish peroxidase, catalase, glutathione peroxidase, and superoxide dismutase in vitro

1992 ◽  
Vol 46 (3) ◽  
pp. 161-174 ◽  
Author(s):  
Miguel Ángel Serra ◽  
Enrico Sabbioni ◽  
Alessandro Pintar ◽  
Luigi Casella
Keyword(s):  
Superoxide Dismutase ◽  
Horseradish Peroxidase ◽  
Glutathione Peroxidase

Indole-3-Carbinol Inhibits Nasopharyngeal Carcinoma

2010 ◽  
Vol 29 (2) ◽  
pp. 185-192 ◽  
Author(s):  
Wei Zhu ◽  
Wenxue Li ◽  
Guangyu Yang ◽  
Quanxin Zhang ◽  
Ming Li ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Nasopharyngeal Carcinoma ◽  
Glutathione Peroxidase ◽  
Tumor Growth ◽  
Caspase 3 ◽  
Caspase 9 ◽  
Human Nasopharyngeal Carcinoma ◽  
Induced Apoptosis

This study explored the effects of indole-3-carbinol on the proliferation of human nasopharyngeal carcinoma, both in vitro and in vivo, and the underlying mechanisms in inducing apoptosis of CNE1 cells. Proliferation, apoptosis, malondialdehyde, superoxide dismutase, glutathione peroxidase, expressions of caspase-9, and caspase-3 in human nasopharyngeal carcinoma cells CNE1 were examined. Indole-3-carbinol suppressed proliferation, induced apoptosis, decreased malondialdehyde level, increased the activity of superoxide dismutase and glutathione peroxidase, and up-regulated the expression of active fragments of caspase-9 and caspase-3 both in vitro and in vivo. It was concluded that indole-3-carbinol could inhibit proliferation and induce apoptosis of CNE1 cells and inhibit tumor growth in mice. Increased activity of superoxide dismutase and glutathione peroxidase and activated expression of caspase-9 and caspase-3 were also observed in indole-3-carbinol–treated tumors or tumor cells, suggesting that stress- and apoptosis-related molecules are involved in the indole-3-carbinol–induced apoptosis and inhibition of tumor growth.

Liquid storage of ram semen in the absence or presence of some antioxidants

1996 ◽  
Vol 8 (6) ◽  
pp. 1013 ◽  
Author(s):  
WM Maxwell ◽  
T Stojanov
Keyword(s):  
Superoxide Dismutase ◽  
Glutathione Peroxidase ◽  
Intrauterine Insemination ◽  
Fertilization Rates ◽  
Liquid Storage ◽  
Semen Storage ◽  
Acrosome Integrity ◽  
Improvement In Survival ◽  
Fresh Semen

The antioxidants superoxide dismutase (SOD), catalase (CAT), cytochrome c (CHc) and glutathione peroxidase (GP) were added at various concentrations to Tris-glucose-yolk diluent (TGY), and their effects on motility, acrosome integrity and fertility of ram spermatozoa were assessed after extension and liquid storage. All the antioxidants improved the motility and acrosome integrity of spermatozoa, and a combination of SOD and CAT had an additive effect on the survival of spermatozoa stored at 5 degrees C but not at 25 degrees C. There was a linear improvement in survival of spermatozoa with increasing dose of antioxidants except for CAT for which doses higher than 200 U mL-1 were toxic. The proportion of oocytes fertilized in vitro declined with time of semen storage (P < 0.001), and was better for semen diluted with TGY containing SOD or CAT than TGY without antioxidants when stored for 7 days (116/246, 47% v. 25/79, 32%; P < 0.05) but not for 14 days (23/174, 13% v. 8/66, 12%). Fertilization rates were unaffected by the presence or absence in the diluent of CHc or GP. The proportions of ewes with fertilized ova and of recovered ova fertilized were better after insemination with semen diluted in TGY containing SOD and CAT than TGY without antioxidants when stored for 14 days (9/18, 50% and 20/40, 50% v. 2/13, 15% and 5/32, 16%; P < 0.05) but not for 7 days (9/20, 45% and 16/48, 33% v. 8/16, 50% and 24/41, 59%). Pregnancy rates were better after intrauterine insemination of ewes with fresh semen than stored semen (11/18, 61% v. 21/75, 28%; P < 0.01), and with semen stored in TGY containing SOD and CAT than in TGY without antioxidants (15/37, 41% v. 6/38, 16%; P < 0.05).

Infiluence of Lindane and Paraquat on Oxidative Stress-Related Parameters of Erythrocytes In Vitro

1994 ◽  
Vol 13 (7) ◽  
pp. 461-465 ◽  
Author(s):  
Afonso C.D. Bainy ◽  
Marcia A.S. Silva ◽  
Mariza Kogake ◽  
Luis A. Videlal ◽  
V.B.C. Junqueira
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Glutathione Peroxidase ◽  
Blood Cell ◽  
Red Blood Cell ◽  
Butyl Hydroperoxide ◽  
Anti Oxidant ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Oxidant Status

1 The influence of lindane and paraquat on oxidative stress-related parameters of the red blood cell was studied in vitro. 2 Lindane addition did not modify either the t-butyl hydroperoxide-induced oxygen uptake of the erythrocytes and the induction time preceding it, or the activity of catalase, superoxide dismutase, glutathione peroxidase and glucose 6-phosphate dehydrogenase, in conditions of comparable levels of haemoglobin and methaemoglobin. 3 Red blood cells exposed to paraquat exhibited a concentration-dependent decrease in the t-butyl hydroperoxide-induced oxygen consumption and increments in either the induction period or in the activity of catalase and glucose 6-phosphate dehydrogenase, with no changes in superoxide dismutase activity and a small decrement in that of glutathione peroxidase. 4 These data indicate that lindane does not interfere with the oxidant status of the erythrocyte, while paraquat addition leads to an increment in the anti-oxidant capacity of the red blood cell.

scholarly journals CuZn-superoxide dismutase, Mn-superoxide dismutase, catalase and glutathione peroxidase in pancreatic islets and other tissues in the mouse

1981 ◽  
Vol 199 (2) ◽  
pp. 393-398 ◽  
Author(s):  
K Grankvist ◽  
S L Marklund ◽  
I B Täljedal
Keyword(s):  
Superoxide Dismutase ◽  
Glutathione Peroxidase ◽  
Pancreatic Islets ◽  
Islet Cells ◽  
Blood Contamination ◽  
Tissue Samples ◽  
Mouse Islets ◽  
Cuzn Superoxide Dismutase ◽  
Endogenous Enzymes

Exogenous superoxide dismutase, catalase and scavengers of the hydroxyl radical protect pancreatic-islet cells against the toxic actions of alloxan in vitro [Grankvist et al. (1979) Biochem. J. 182, 17--25]. To test whether the extraordinary sensitivity of islet cells to alloxan is due to a deficiency of endogenous enzymes protecting against oxygen-reduction products, we assayed CuZn-superoxide dismutase, Mn-superoxide dismutase, catalase and glutathione peroxidase in mouse islets and other tissues. To correct for any blood contamination, haemoglobin was also measured in the tissue samples. Pancreatic islets were found to belong to tissues with relatively little activity of the protective enzymes. However, the deviation from other tissues in this respect is probably not large enough to explain the especially great susceptibility of islet cells to alloxan.

Silver Nanoparticle-Mediated Cellular Responses in Human Keratinocyte Cell Line HaCaT in Vitro

2019 ◽  
Vol 2 (2) ◽  
pp. 1-9 ◽  
Author(s):  
Khaled Habas ◽  
Lijun Shang
Keyword(s):  
Superoxide Dismutase ◽  
Antioxidant Enzymes ◽  
Glutathione Peroxidase ◽  
Superoxide Anion ◽  
Hacat Cells ◽  
Lactate Dehydrogenase Release ◽  
Skin Cell ◽  
Keratinocyte Cell Line Hacat ◽  
Endogenous Antioxidant

The interactions between cells and nanoparticles has been the focus of recent research in the area. The effects of AgNPs on skin cell lines for further potential biological applications are highlighted. This study aimed to investigate the mechanism of cytotoxic and genotoxic effects of AgNPs nanoparticles on human skin keratinocytes (HaCaT). Genocytotoxic effects of AgNPs was assessed using changes in various cellular parameters of HaCaT cells involving viability, superoxide anion radical production, lactate dehydrogenase release and the levels of the antioxidant enzymes, namely, Catalase, Glutathione peroxidase (GPX) and Superoxide Dismutase (SOD). Superoxide anion was detected using nitroblue tetrazolium NBT reduction assay. LDH levels was evaluated using the standard kit, and activity of antioxidant enzymes such as catalase (CAT), glutathione peroxidase 1 (GPX-1) and superoxide dismutase 1 (SOD-1) were quantified using qPCR. Our results indicated that AgNPs caused severe HaCaT oxidative damage, accompanied by increased the production of superoxide anion levels as well as significant decrease in endogenous antioxidant enzyme of SOD, CAT, GPX expression involved in HaCat cells in vitro. Our study suggests that AgNPs exposure increased oxidative stress levels. Moreover; the low cytotoxic effect observed on human HaCaT keratinocytes suggested that these nano-compounds have a potential toxic effect at the skin level only after long-term exposure.

scholarly journals Role of oxidative stress in cardiac dysfunction of PPARα−/− mice

2007 ◽  
Vol 293 (1) ◽  
pp. H93-H102 ◽  
Author(s):  
Aziz Guellich ◽  
Thibaud Damy ◽  
Yves Lecarpentier ◽  
Marc Conti ◽  
Victor Claes ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Glutathione Peroxidase ◽  
Papillary Muscle ◽  
Ex Vivo ◽  
Left Ventricular ◽  
Protein Adducts ◽  
Contractile Dysfunction ◽  
Wild Type ◽  
Copper Zinc

This study was designed to determine the effects of PPARα lack on cardiac mechanical performance and to identify potential intracellular mechanisms linking PPARα pathway deficiency to cardiac contractile dysfunction. Echocardiography, ex vivo papillary muscle assays, and in vitro motility assays were used to assess global, intrinsic ventricular muscle performance and myosin mechanical properties, respectively, in PPARα−/− and age-matched wild-type mice. Three-nitrotyrosine formation and 4-hydroxy-2-nonenal protein-adducts, both markers of oxidative damage, were analyzed by Western blot analysis and immunolabeling. Radical scavenging capacity was analyzed by measuring protein levels and/or activities of the main antioxidant enzymes, including catalase, glutathione peroxidase, and manganese and copper-zinc superoxide dismutases. Echocardiographic left ventricular fractional shortening in PPARα−/− was 16% lower than that in wild-type. Ex vivo left ventricular papillary muscle exhibited reduced shortening velocity and isometric tension (three- and twofold, respectively). In vitro myosin-based velocity was ≈20% slower in PPARα−/−, indicating that myosin itself was involved in the contractile dysfunction. Staining of 3-nitrotyrosine was more pronounced in PPARα−/−, and myosin heavy chain was the main nitrated protein. Formation of 3-nitrotyrosine myosin heavy chain was twofold higher in PPARα−/− and 4-hydroxy-2-nonenal protein-adducts were threefold higher. The expression and activity of manganese superoxide dismutase were respectively 33% and 50% lower in PPARα−/−, with no changes in copper-zinc superoxide dismutase, catalase, or glutathione peroxidase. These findings demonstrate that PPARα pathway deficiency impairs cardiac function and also identify oxidative damage to myosin as a link between PPARα deficiency and contractile dysfunction.

scholarly journals Study on the ageing method and antioxidant activity of black garlic residues

2018 ◽  
Vol 36 (No. 1) ◽  
pp. 88-97 ◽  
Author(s):  
Feng Xiong ◽  
Chunhua Dai ◽  
Furong Hou ◽  
Peipei Zhu ◽  
Ronghai He ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Superoxide Dismutase ◽  
Glutathione Peroxidase ◽  
Antioxidant Capacity ◽  
Inhibitory Concentration ◽  
Oil Extraction ◽  
Garlic Oil ◽  
Ic50 Values

Garlic residue (GR), a co-product of garlic oil extraction, contains most of the nutrients of raw garlic (RG). Preparation of black garlic residue (BGR) is considered to be an effective method of processing GR. The main objective of this study was to optimise the ageing conditions of GR based on moisture, polyphenol and 5-hydroxymethyl-2-furaldehyde (HMF) levels. In addition, the antioxidant capacity of BGR was also evaluated in vitro and in vivo and compared with black garlic (BR) and RG. The results indicate that optimum ageing resulting in polyphenol and HMF contents of 25.80 mg/g and 3.84 mg/g, respectively, were achieved using a temperature of 90°C and humidity of 95% for four days. Both BGR and BR had stronger capacities to scavenge α,α-diphenyl-β-picrylhydrazyl (DPPH) than RG with half maximal inhibitory concentration (IC50) values of 0.454, 0.514 and 4.236 mg/ml, respectively. Experiments on mice demonstrated that there was no obvious difference in antioxidant activity between BGR and BR in vivo. BGR and BR consumption significantly decreased malondialdehyde (MDA) levels in serum and liver, in addition to markedly increasing superoxide dismutase (SOD) and glutathione peroxidase (GSH-Px) activities.

scholarly journals In Vitro Effect of Sodium Fluoride on Malondialdehyde Concentration and on Superoxide Dismutase, Catalase, and Glutathione Peroxidase in Human Erythrocytes

2013 ◽  
Vol 2013 ◽  
pp. 1-7 ◽  
Author(s):  
José Gutiérrez-Salinas ◽  
Liliana García-Ortíz ◽  
José A. Morales González ◽  
Sergio Hernández-Rodríguez ◽  
Sotero Ramírez-García ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Antioxidant Enzymes ◽  
Vitamin E ◽  
Glutathione Peroxidase ◽  
Sodium Fluoride ◽  
Specific Activity ◽  
Human Erythrocytes ◽  
Vitro Effect

The aim of this paper was to describe the in vitro effect of sodium fluoride (NaF) on the specific activity of the major erythrocyte antioxidant enzymes, as well as on the membrane malondialdehyde concentration, as indicators of oxidative stress. For this purpose, human erythrocytes were incubated with NaF (0, 7, 28, 56, and 100 μg/mL) or NaF (100 μg/mL) + vitamin E (1, 2.5, 5 and 10 μg/mL). The malondialdehyde (MDA) concentration on the surface of the erythrocytes was determined, as were the enzymatic activities of superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GlPx). Our results demonstrated that erythrocytes incubated with increasing NaF concentrations had an increased MDA concentration, along with decreased activity of antioxidant enzymes. The presence of vitamin E partially reversed the toxic effects of NaF on erythrocytes. These findings suggest that NaF induces oxidative stress in erythrocytes in vitro, and this stress is partially reversed by the presence of vitamin E.

Eugenol influences the expression of messenger RNAs for superoxide dismutase and glutathione peroxidase 1 in bovine secondary follicles cultured in vitro

Zygote ◽  
2021 ◽  
pp. 1-6
Author(s):  
E.M. Vasconcelos ◽  
F.C. Costa ◽  
A.V.N. Azevedo ◽  
P.A.A. Barroso ◽  
E.I.T. de Assis ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Glutathione Peroxidase ◽  
Mrna Expression ◽  
Progressive Increase ◽  
Control Group ◽  
Mrna Levels ◽  
Messenger Rnas ◽  
Glutathione Peroxidase 1 ◽  
Viability Analysis

Summary This study aimed to investigate the effects of eugenol on growth, viability, antrum formation and mRNA expression of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase 1 (GPX1) and peroxiredoxin 6 (PRDX6) in bovine secondary follicles cultured in vitro. To this end, bovine ovaries were collected from a local slaughterhouse and in the laboratory the follicles were isolated from the ovarian cortex. The follicles were then cultured in TCM-199+ alone or supplemented with different concentrations of eugenol (0.5, 5.0 and 50.0 μM). Follicular diameters and antrum formation were evaluated on days 0, 6, 12 and 18. Viability analysis was performed using calcein and ethidium homodimer. Real-time PCR was used to quantify mRNA levels for SOD, CAT, GPX1 and PRDX6 in cultured follicles. Follicular diameters and mRNA levels in follicles cultured in vitro were compared using analysis of variance and Kruskal–Wallis tests, while follicular survival and antrum formation were compared using the chi-squared test (P < 0.05). The results showed that secondary follicles cultured with eugenol maintained similar morphology and viability to follicles cultured in the control group. A progressive increase in follicular diameter was observed between days 0 and 12 for all treatments, except for follicles cultured with 50 µM eugenol. Eugenol (5.0 and 50.0 μM) increased mRNA levels for GPX1 in cultured follicles, but 0.5 μM eugenol reduced mRNA levels for SOD. The addition of eugenol did not influence mRNA expression for CAT and PRDX6. In conclusion, eugenol supplementation reduces mRNA levels for SOD and increases mRNA levels of GPX1 in bovine secondary follicles cultured in vitro.

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