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

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.

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

The Scientific World JOURNAL ◽

10.1155/2014/874824 ◽

2014 ◽

Vol 2014 ◽

pp. 1-6 ◽

Cited By ~ 8

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.

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

The Journal of Cell Biology ◽

10.1083/jcb.66.3.609 ◽

1975 ◽

Vol 66 (3) ◽

pp. 609-620 ◽

Cited By ~ 36

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.

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Genotoxic and Antigenotoxic Activities of Thai Bee Pollen and Its Extracts in Human Lymphocytes by in Vitro Sister Chromatid Exchange Assay

Natural Product Communications ◽

10.1177/1934578x1701200728 ◽

2017 ◽

Vol 12 (7) ◽

pp. 1934578X1701200

Author(s):

Treetip Ratanavalachai ◽

Sumon Thitiorul ◽

Chalerm Jansom ◽

Wantha Jenkhetkan ◽

Arunporn Itharat

Keyword(s):

Sister Chromatid ◽

Sister Chromatid Exchange ◽

Chemotherapeutic Agent ◽

Human Lymphocytes ◽

Food Supplement ◽

Pollen Extract ◽

Protective Mechanisms ◽

Bee Pollen ◽

Phenolic Contents

Bee pollen has been used as a food supplement and as a traditional medicine for thousands of years. Our study demonstrated that by in vitro sister chromatid exchange assay, Mimosa pudica crude bee pollen extract (0.005-5.0 μg/mL CE) from Chiangmai, Northern Thailand, increased genotoxicity in human lymphocytes at concentrations of 0.005 and 0.5 μg/mL by 20% and 24% respectively, compared to the RPMI control. Its defatted extract (DE) at 0.005-5.0 μg/mL increased the activities by 24–32% whereas the lipid extract (LE) at 0.00125 μg/mL but not at 0.0125–1.25 μg/mL increased the activities by 25%. Only CE at 5.0 μg/mL induced cytotoxicity. Pretreatments of CE, DE, and LE at 0.5, 5, and 0.00125 μg/mL induced antigenotoxicities against doxorubicin, a potent genotoxic chemotherapeutic agent by 24%, 28%, and 16%, respectively. Their protective mechanisms are feasibly involved with α-tocopherol and phenolic contents such as gallic acid and ferulic acid.

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