scholarly journals Protective Role of Catechin and Quercetin in Sodium Benzoate-Induced Lipid Peroxidation and the Antioxidant System in Human ErythrocytesIn Vitro

2014 ◽  
Vol 2014 ◽  
pp. 1-6 ◽  
Author(s):  
Gamze Yetuk ◽  
Dilek Pandir ◽  
Hatice Bas
Keyword(s):  
Oxidative Stress ◽  
Lipid Peroxidation ◽  
Sodium Benzoate ◽  
Protective Role ◽  
Food Additive ◽  
Human Erythrocytes ◽  
Low Concentrations ◽  
High Concentrations

The aim of this study was to evaluate the protective effect of catechin and quercetin in sodium benzoate- (SB-) induced oxidative stress in human erythrocytesin vitro. For this, the effects of SB (6.25, 12.5, 25, 50, and 100 μg/mL), catechin (10 μM), and quercetin (10 μM) on lipid peroxidation (LPO) and the activities of SOD, CAT, GPx, and GST were studied. Significantly higher LPO and lower activities of antioxidant enzymes were observed with the increasing concentrations of SB. Catechin or quercetin protected the erythrocytes against SB-induced toxicity only at low concentrations of SB. The presence of catechin or quercetin at 10 μM have no effect on SB-induced toxicity at high concentrations of SB (50 and 100 μg/mL). In conclusion, SB may cause oxidative stress as food additive in human erythrocytesin vitro. So, it appears that our findings provide evidence for the protection of erythrocytes from SB that could be considered for further studies.

Protective effects of selenium against sister chromatid exchange induced by AFG 1 in human lymphocytes in vitro

2010 ◽  
Vol 30 (6) ◽  
pp. 515-519
Author(s):  
Lokman Alpsoy ◽  
Elif Kotan ◽  
Abdulgani Tatar ◽  
Guleray Agar
Keyword(s):  
Sister Chromatid ◽  
Sister Chromatid Exchange ◽  
Human Lymphocytes ◽  
Protective Role ◽  
Blood Cultures ◽  
Protective Effects ◽  
Low Concentrations ◽  
High Concentrations

Aflatoxins have been shown to be hepatotoxic, carcinogenic, mutagenic and teratogenic to different species of animals. Besides, at low concentrations, Selenium (Se4+) is antimutagenic and anticarcinogenic while it is toxic, mutagenic and carcinogenic at high concentrations. In this study, we aimed to evaluate the effect of Se4+ against aflatoxin GAFG1 (AFG1) on blood cultures in relation to induction of sister chromatid exchange (SCE). The results showed that at 0.4 and 0.8 parts per million (ppm) concentration of AFG1, the frequency of SCE increased in cultured human lymphocytes. When different concentration of Se4+ (0.08 and 8 ppm) were added to AFG1, the frequencies of SCE decreased. Howewer, when 800 ppm concentration of Se4+ together with 0.08 ppm AFG1 were added to cell division inhibited in the cultures. Results suggested that Se4+ could effectively inhibit AFG1-induced SCE. Besides, the protective role of Se4+ against AFG1-induced SCE is probably related to its doses.

scholarly journals Protective role of vitamins C and E in diclorvos-induced oxidative stress in human erythrocytes in vitro

2013 ◽  
Vol 46 (1) ◽  
pp. 33-38 ◽  
Author(s):  
Sema Eroglu ◽  
Dilek Pandir ◽  
Fatma G Uzun ◽  
Hatice Bas
Keyword(s):  
Oxidative Stress ◽  
Protective Role ◽  
Human Erythrocytes

Acrylamide-induced oxidative stress in human erythrocytes

2009 ◽  
Vol 28 (10) ◽  
pp. 611-617 ◽  
Author(s):  
Betul Catalgol ◽  
Gül Özhan ◽  
Buket Alpertunga
Keyword(s):  
Oxidative Stress ◽  
Reduced Glutathione ◽  
Human Erythrocytes ◽  
Antioxidant Enzyme Activities ◽  
Total Glutathione ◽  
Sod Activity ◽  
Spectrophotometric Methods ◽  
Low Concentrations ◽  
Different Doses

Acrylamide (AA), a widely used industrial chemical, is shown to be neurotoxic, mutagenic and carcinogenic. This study was carried out to investigate the effects of different doses of AA on lipid peroxidation (LPO), haemolysis, methaemoglobin (MetHb) and antioxidant system in human erythrocytes in vitro. Erythrocyte solutions were incubated with 0.10, 0.25, 0.50 and 1.00 mM of AA at 37°C for 1 hour. At the end of the incubation, malondialdehyde (MDA), an end product of LPO, was determined by liquid chromatography (LC) while total glutathione, reduced glutathione (GSH) levels, activities of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px) enzymes and the rates of haemolysis and MetHb were determined by spectrophotometric methods. All of the studied concentrations of AA increased MetHb formation and SOD activity, and induced MDA formation and haemolysis due to the destruction of erythrocyte cell membrane. AA caused a decrease in the activities of GSH-Px, CAT and GSH levels. However, these effects of AA were seen only at higher concentrations than AA intake estimated for populations in many countries. We suggest that LPO process may not be involved in the toxic effects of AA in low concentrations, although the present results showed that the studied concentrations of AA exert deteriorating effects on antioxidant enzyme activities, LPO process and haemolysis.

scholarly journals Colchicine-binding protein of the liver. Its characterization and relation to microtubules.

1975 ◽  
Vol 66 (3) ◽  
pp. 609-620 ◽  
Author(s):  
C Patzelt ◽  
A Singh ◽  
Y L Marchand ◽  
L Orci ◽  
B Jeanrenaud
Keyword(s):  
High Speed ◽  
Specific Binding ◽  
Electrophoretic Analysis ◽  
Binding Activity ◽  
Low Concentrations ◽  
Electrophoretic Behavior ◽  
High Affinity Binding Site ◽  
High Concentrations

Colchicine-binding activity of mouse liver high-speed supernate has been investigated. It has been found to be time and temperature dependent. Two binding activities with different affinities for colchicine seem to be present in this high-speed supernate, of which only the high-affinity binding site (half maximal binding at 5 x 10(-6) M colchicine) can be attributed to microtubular protein by comparison with purified tubulin. Vinblastine interacted with this binding activity by precipitating it when used at high concentrations (2 x 10(-3) M), and by stabilizing it at low concentrations (10(-5) M). Lumicolchicine was found not to compete with colchicine. The colchicine-binding activity was purified from liver and compared with that of microtubular protein from brain. The specific binding activity of the resulting preparation, its electrophoretic behavior, and the electron microscope appearance of the paracrystals obtained upon its precipitation with vinblastine permitted its identification as microtubular protein (tubulin). Electrophoretic analysis of the proteins from liver supernate that were precipitated by vinblastine indicated that this drug was not specific for liver tubulin. Preincubation of liver supernate with 5 mM EGTA resulted in a time-dependent decrease of colchicine-binding activity, which was partly reversed by the addition of Ca++. However, an in vitro formation of microtubules upon lowering the Ca++ concentration could not be detected. Finally, a method was developed enabling that portion of microtubular protein which was present as free tubulin to be measured and to be compared with the total amount of this protein in the tissue. This procedure permitted demonstration of the fact that, under normal conditions, only about 40% of the tubulin of the liver was assemled as microtubules. It is suggested that, in the liver, rapid polymerization and depolymerization of microtubules occur and may be an important facet of the functional role of the microtubular system.

scholarly journals A Protective Role of Paeoniflorin in Fluctuant Hyperglycemia-Induced Vascular Endothelial Injuries through Antioxidative and Anti-Inflammatory Effects and Reduction of PKCβ1

2019 ◽  
Vol 2019 ◽  
pp. 1-11 ◽  
Author(s):  
Jing-Shang Wang ◽  
Ye Huang ◽  
Shuping Zhang ◽  
Hui-Jun Yin ◽  
Lei Zhang ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Protein Level ◽  
Umbilical Vein ◽  
Protective Role ◽  
Vascular Endothelial ◽  
Glucose Levels ◽  
Umbilical Vein Endothelial Cells

Hyperglycemia fluctuation is associated with diabetes mellitus (DM) complications when compared to persistent hyperglycemia. Previous studies have shown that paeoniflorin (PF), through its antiapoptosis, anti-inflammation, and antithrombotic properties, effectively protects against cardiovascular and cerebrovascular disease. However, the mechanism underlying the protection from PF against vascular injuries induced by hyperglycemia fluctuations remains poorly understood. Herein, we investigated the potential protective role of PF on human umbilical vein endothelial cells (HUVECs) subjected to intermittent glucose levels in vitro and in DM rats with fluctuating hyperglycemia in vivo. A remarkable increased apoptosis associated with elevated inflammation, increased oxidative stress, and high protein level of PKCβ1 was induced in HUVECs by intermittently changing glucose for 8 days, and PF recovered those detrimental changes. LY333531, a potent PKCβ1 inhibitor, and metformin manifested similar effects. Additionally, in DM rats with fluctuating hyperglycemia, PF protected against vascular damage as what has been observed in vitro. Taken together, PF attenuates the vascular injury induced by fluctuant hyperglycemia through oxidative stress inhibition, inflammatory reaction reduction, and PKCβ1 protein level repression, suggesting its perspective clinical usage.

scholarly journals Manganese Induces Oxidative Stress, Redox State Unbalance and Disrupts Membrane Bound ATPases on Murine Neuroblastoma Cells In Vitro: Protective Role of Silymarin

2011 ◽  
Vol 36 (8) ◽  
pp. 1546-1557 ◽  
Author(s):  
Yassine Chtourou ◽  
Khaled Trabelsi ◽  
Hamadi Fetoui ◽  
Ghada Mkannez ◽  
Héla Kallel ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Redox State ◽  
Neuroblastoma Cells ◽  
Protective Role ◽  
Murine Neuroblastoma ◽  
Membrane Bound

scholarly journals Pyridoxine Decreases Oxidative Stress on Human Erythrocyte Membrane Protein in vitro

2019 ◽  
Vol 13 (1) ◽  
pp. 37-44 ◽  
Author(s):  
Margarita Velásquez ◽  
Darío Méndez ◽  
Carlos Moneriz
Keyword(s):  
Oxidative Stress ◽  
Lipid Peroxidation ◽  
Membrane Protein ◽  
Oxidative Damage ◽  
Erythrocyte Membrane ◽  
Cumene Hydroperoxide ◽  
Protein Carbonylation ◽  
Human Erythrocytes ◽  
Red Cell Membrane

Background: Pyridoxine has reduction and prevention against the levels of reactive oxygen species in in vitro studies. However, the biochemical mechanism that explains this behavior has not yet been fully clarified. Objective: To evaluate the effect of pyridoxine against oxidative damage on the membrane of human erythrocytes. Methods: Cumene hydroperoxide was used to induce oxidative stress in protein and lipid. Human erythrocytes were incubated with pyridoxine and cumene hydroperoxide, either alone or together for 8 h. Oxidative damage was determined by measuring lipid peroxidation and membrane protein carbonylation. Results: The results indicate that the malondialdehyde concentration decreased with increasing concentration of pyridoxine. The membrane protein content also decreased with increasing concentration of vitamin B6, which was confirmed by the decreased signal intensity in the western blot when compared to control without pyridoxine. Results demonstrate that pyridoxine can significantly decrease lipid peroxidation and protein carbonylation in red cell membrane exposed to high concentrations of oxidant agent. Conclusion: Pyridoxine showed a protective effect against the oxidative stress in human erythrocytes in vitro, inhibiting the carbonylation and the oxidative damage of erythrocyte membrane proteins. To date, such an effect has not yet been reported in terms of protein oxidation.

scholarly journals Protective Role of Myricetin on Markers of Oxidative Stress in Human Erythrocytes Subjected to Oxidative Stress

2009 ◽  
Vol 4 (2) ◽  
pp. 1934578X0900400 ◽  
Author(s):  
Kanti Bhooshan Pandey ◽  
Neetu Mishra ◽  
Syed Ibrahim Rizvi
Keyword(s):  
Oxidative Stress ◽  
Protective Role ◽  
Protein Carbonyl ◽  
Human Erythrocytes ◽  
The Body ◽  
Protein Carbonyl Content ◽  
Tert Butylhydroperoxide ◽  
Markers Of Oxidative Stress ◽  
Dose Dependent

The protective effect of myricetin against tert-butylhydroperoxide (t-BHP) induced oxidative stress in human erythrocytes was investigated. Incubating erythrocytes with t-BHP (10−5M) caused development of oxidative stress, as evidenced by significant ( p < 0.05) increase in erythrocyte malondialdedyde (MDA) and protein carbonyl content, and decrease in intracellular reduced glutathione (GSH), membrane sulphydryl (-SH) groups. Incubation of erythrocytes with myricetin, simultaneously with t-BHP, protected the erythrocytes from oxidative stress, an effect which was dose-dependent. The results demonstrate that myricetin attenuates t-BHP induced oxidative damage, suggesting that supplementation of diet with myricetin/myricetin rich food may be beneficial in all pathological conditions where the antioxidant system of the body is overwhelmed.

Effect of toluene on erythrocyte membrane stability under in vivo and in vitro conditions with assessment of oxidant/antioxidant status

2009 ◽  
Vol 25 (8) ◽  
pp. 545-550 ◽  
Author(s):  
Ismail Karabulut ◽  
Z. Dicle Balkanci ◽  
Bilge Pehlivanoglu ◽  
Aysen Erdem ◽  
Ersin Fadillioglu
Keyword(s):  
Oxidative Stress ◽  
Lipid Peroxidation ◽  
Unsaturated Fatty Acids ◽  
Osmotic Fragility ◽  
Human Erythrocytes ◽  
Antioxidant Enzyme Activities ◽  
Oxidative Stress Parameters ◽  
Stress Parameters

Toluene, an organic solvent used widely in the industry, is highly lipophilic and accumulates in the cell membrane impeding transport through it. Its metabolites cause oxygen radical formation that react with unsaturated fatty acids and proteins in erythrocytes leading to lipid peroxidation and protein breakdown. In this study, we aimed to investigate the membrane stabilizing and the oxidative stress—inducing effects of toluene in human erythrocytes. Measurements of osmotic fragility, mean corpuscular volume (MCV), oxidative stress parameters and antioxidant enzyme activities were performed simultaneously both in individuals exposed to toluene professionally (in vivo) and human erythrocytes treated with toluene (in vitro). To measure osmotic fragility, erythrocytes were placed in NaCl solutions at various concentrations (0.1% [blank], 0.38%, 0.40%, 0.42%, 0.44%, 0.46%, 0.48% and 1% [stock]). Percentage of haemolysis in each solution was calculated with respect to the 100% haemolysis in the blank solution. The erythrocyte packs prepared at the day of the above-mentioned measurements were kept at —80°C until the time for determination of malonyldialdehyde and protein carbonyl levels, and catalase (CAT) and glutathione peroxidase activities as indicators of oxidative stress. Toluene increased oxidative stress parameters significantly both in vivo and in vitro; it also caused a significant decrease in the activities of antioxidant enzymes. Osmotic fragility was altered only in the case of in vitro exposure. In conclusion, toluene exposure resulted in increased lipid peroxidation and protein damage both in vivo and in vitro. Although, it is natural to expect increased osmotic fragility due to oxidative properties of toluene, its membrane-stabilizing effect overcame the oxidative properties leading to decreased osmotic fragility or preventing its deterioration in vitro and in vivo toluene exposures, respectively, in the present study.

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