Modulation of plasma antioxidant levels, glutathione S -transferase activity and DNA damage in smokers following a single portion of broccoli: a pilot study

2013 ◽  
Vol 94 (3) ◽  
pp. 522-528 ◽  
Author(s):  
Patrizia Riso ◽  
Cristian Del Bo' ◽  
Stefano Vendrame ◽  
Antonella Brusamolino ◽  
Daniela Martini ◽  
...  
Keyword(s):  
Dna Damage ◽  
Pilot Study ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
Plasma Antioxidant

DNA damage and effects on glutathione-S-transferase activity induced by atrazine exposure in zebrafish (Danio rerio)

2010 ◽  
Vol 26 (5) ◽  
pp. 480-488 ◽  
Author(s):  
Lusheng Zhu ◽  
Xiaoli Dong ◽  
Hui Xie ◽  
Jun Wang ◽  
Jinhua Wang ◽  
...  
Keyword(s):  
Dna Damage ◽  
Danio Rerio ◽  
Transferase Activity ◽  
Glutathione S Transferase

scholarly journals Effects of a radio frequency electromagnetic field on honey bee larvae (Apis mellifera) differ in relation to the experimental study design

2021 ◽  
Vol 91 (4) ◽  
pp. 427-435
Author(s):  
Marinko Vilić ◽  
◽  
Ivona Žura Žaja ◽  
Mirta Tkalec ◽  
Anamaria Štambuk ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Dna Damage ◽  
Apis Mellifera ◽  
Honey Bee ◽  
Biological Effects ◽  
Control Group ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
Communication Devices ◽  
Honey Bee Larvae

Exposure to radiofrequency electromagnetic fields (RF-EMF) at the operating frequencies of different communication devices can cause various biological effects. However, there is a lack of studies on the oxidative stress response and genotoxicity in the honey bee (Apis mellifera) after exposure to RF-EMF. In this study, we investigated the oxidative stress and DNA damage in honey bee larvae situated in waxcomb cells, exposed to modulated RF-EMF 23 Vm-1. The glutathione S-transferase activity decreased, whereas the catalase activity increased significantly in the honey bee larvae upon RF-EMF exposure. Superoxide dismutase activity, the level of lipid peroxidation, and DNA damage were not statistically altered in exposed honey bee larvae when compared to the control group. These results suggest that the biological effects of modulated RF-EMF in honey bee larvae depend on the exposure design.

Overexpression of Stably Transfected Human Glutathione S-Transferase P1–1 Protects against DNA Damage by Benzo[a]pyrene Diol-Epoxide in Human T47D Cells

1998 ◽  
Vol 54 (2) ◽  
pp. 298-304 ◽  
Author(s):  
Wanda R. Fields ◽  
Charles S. Morrow ◽  
Amanda J. Doss ◽  
Kathrin Sundberg ◽  
Bengt Jernström ◽  
...  
Keyword(s):  
Dna Damage ◽  
Glutathione S Transferase ◽  
T47d Cells ◽  
Diol Epoxide

Glutathione S-Transferase Activity in Nontreated and CGA-154281- Treated Maize Shoots

1991 ◽  
Vol 46 (9-10) ◽  
pp. 850-855 ◽  
Author(s):  
John V. Dean ◽  
John W. Gronwald ◽  
Michael P. Anderson
Keyword(s):  
Liquid Chromatography ◽  
Anion Exchange ◽  
Cinnamic Acid ◽  
Fast Protein Liquid Chromatography ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
Selective Enhancement

Abstract Fast protein liquid chromatography (anion exchange) was used to separate glutathione S-transferase isozymes in nontreated etiolated maize shoots and those treated with the herbi­cide safener CGA -1542814-(dichloroacetyl)-3,4-dihydro-3-methyl-2 H-1 ,4-benzoxazine. Non­treated shoots contained isozymes active with the following substrates: trans-cinnamic acid (1 isozyme), atrazine (3 isozymes), 1-chloro-2,4-dinitrobenzene (1 isozyme), metolachlor (2 isozymes) and the sulfoxide derivative of S-ethyl dipropylcarbamothioate (2 isozymes). Pre­treatment of shoots with the safener CGA -154281 (1 μM) had no effect on the activity of the isozymes selective for trans-cinnamic acid and atrazine but increased the activity of the constitutively-expressed isozymes that exhibit activity with 1-chloro-2,4-dinitrobenzene, metola­chlor and the sulfoxide derivative of S-ethyl dipropylcarbamothioate. The safener pretreat­ment also caused the appearance of one new isozyme active with 1-chloro-2,4-dinitrobenzene and one new isozyme active with metolachlor. The results illustrate the complexity of gluta­thione S-transferase activity in etiolated maize shoots, and the selective enhancement of gluta­thione S-transferase isozymes by the safener CGA -154281.

scholarly journals The distribution, induction and isoenzyme profile of glutathione S-transferase and glutathione peroxidase in isolated rat liver parenchymal, Kupffer and endothelial cells

1989 ◽  
Vol 264 (3) ◽  
pp. 737-744 ◽  
Author(s):  
P Steinberg ◽  
H Schramm ◽  
L Schladt ◽  
L W Robertson ◽  
H Thomas ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Glutathione Peroxidase ◽  
Rat Liver ◽  
Peroxidase Activity ◽  
Cell Types ◽  
Transferase Activity ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase ◽  
Liver Parenchymal ◽  
Parenchymal Cells

The distribution and inducibility of cytosolic glutathione S-transferase (EC 2.5.1.18) and glutathione peroxidase (EC 1.11.1.19) activities in rat liver parenchymal, Kupffer and endothelial cells were studied. In untreated rats glutathione S-transferase activity with 1-chloro-2,4-dinitrobenzene and 4-hydroxynon-2-trans-enal as substrates was 1.7-2.2-fold higher in parenchymal cells than in Kupffer and endothelial cells, whereas total, selenium-dependent and non-selenium-dependent glutathione peroxidase activities were similar in all three cell types. Glutathione S-transferase isoenzymes in parenchymal and non-parenchymal cells isolated from untreated rats were separated by chromatofocusing in an f.p.l.c. system: all glutathione S-transferase isoenzymes observed in the sinusoidal lining cells were also detected in the parenchymal cells, whereas Kupffer and endothelial cells lacked several glutathione S-transferase isoenzymes present in parenchymal cells. At 5 days after administration of Arocolor 1254 glutathione S-transferase activity was only enhanced in parenchymal cells; furthermore, selenium-dependent glutathione peroxidase activity decreased in parenchymal and non-parenchymal cells. At 13 days after a single injection of Aroclor 1254 a strong induction of glutathione S-transferase had taken place in all three cell types, whereas selenium-dependent glutathione peroxidase activity remained unchanged (endothelial cells) or was depressed (parenchymal and Kupffer cells). Hence these results clearly establish that glutathione S-transferase and glutathione peroxidase are differentially regulated in rat liver parenchymal as well as non-parenchymal cells. The presence of glutathione peroxidase and several glutathione S-transferase isoenzymes capable of detoxifying a variety of compounds in Kupffer and endothelial cells might be crucial to protect the liver from damage by potentially hepatotoxic substances.

Expression of Glutathione S-Transferase Activity and Glutathione Content in Squamous Cell Carcinoma of Bladder Associated with Schistosomiasis in a Population in Egypt

1997 ◽  
Vol 31 (1) ◽  
pp. 43-47 ◽  
Author(s):  
Galal E. M. D. Ghazaly ◽  
Madeha M. Zakahary ◽  
Mohamed A. A. El-aziz ◽  
Ahmed A. E. M. Mahmoud ◽  
Pablo Carretero ◽  
...  
Keyword(s):  
Squamous Cell Carcinoma ◽  
Cell Carcinoma ◽  
Squamous Cell ◽  
Transferase Activity ◽  
Glutathione S Transferase
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