scholarly journals Galectin-3 Deficiency Reduces Cardiac and Renal Antioxidant Capacity in Mice

2020 ◽  
Vol 68 (2) ◽  
pp. 73-80
Author(s):  
Danijela B. Vučević ◽  
Sunčica Z. Borozan ◽  
Ana S. Radenković ◽  
Milica I. Radosavljević ◽  
Dušan R. Mladenović ◽  
...  
Keyword(s):  
Antioxidant Capacity ◽  
Nitrosative Stress ◽  
Renal Tissue ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
Tissue Samples ◽  
Galectin 3 ◽  
Overnight Fasting ◽  
Binding Lectin ◽  
Total Superoxide Dismutase

Galectin-3 (Gal-3) has increasingly been recognized as a modulator of inflammation, oxidative/nitrosative stress, fibrogenesis, and tissue remodeling. The objective of the current pilot study was to investigate the influence of Gal-3 on cardiac and renal antioxidant capacity using biochemical and histopathological examinations. Two groups (n=7 each) of male mice were tested: 1. control (CON) group (wild type of C57BL/6 mice) and 2. GAL-3-/- group (galectin-3-/- knockout mice). After overnight fasting, mice were sacrificed by exsanguination in ketamine (100mg/kg intraperitoneally). Then, cardiac and renal tissue samples were taken to determine the parameters of oxidative/nitrosative stress and antioxidant capacity. The levels of malondialdehyde and nitrites+nitrates was not significantly different in the GAL-3-/- group vs. the CON group. The total superoxide dismutase activity in the renal tissue of the GAL-3-/- mice was significantly lower compared to the CON group. Cardiac and renal catalase and glutathione S-transferase activity was significantly reduced in the GAL-3-/- group vs. the CON group, respectively. A significant decrease in glutathione level was also registered in hearts of the GAL-3-/- group vs. the CON group. Our findings indicate that Gal-3 deficiency does not lead to lipid peroxidation and nitrosative stress in cardiac and renal tissue in mice. However, the lack of this beta-galactoside-binding lectin does reduce antioxidant capacity in both of the investigated tissues.

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

Effect of Mn2+ on Glutathione-S-Transferase Activity of Human Ejaculated Spermatozoa

2015 ◽  
Vol 10 (3) ◽  
pp. 117-124
Author(s):  
Kuldeep Kaushik ◽  
Pawan Kumar Mittal ◽  
Natwar Raj Kalla
Keyword(s):  
Transferase Activity ◽  
Glutathione S Transferase

scholarly journals Glutathione S-Transferases and Cytochrome P450 Enzyme Expression in Patients with Intracranial Tumors: Preliminary Report of 55 Patients

2018 ◽  
Vol 28 (1) ◽  
pp. 56-62
Author(s):  
Cahit Kural ◽  
Arzu Kaya Kocdogan ◽  
Gulcin Güler Şimşek ◽  
Serpil Oğuztüzün ◽  
Pınar Kaygın ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Brain Tissue ◽  
Pituitary Adenomas ◽  
Normal Brain ◽  
Cytochrome P450 Enzyme ◽  
Intracranial Tumors ◽  
Glutathione S Transferase ◽  
Normal Brain Tissue ◽  
Tissue Samples ◽  
P450 Enzyme

Objective: Intracranial tumors are one of the most frightening and difficult-to-treat tumor types. In addition to surgery, protocols such as chemotherapy and radiotherapy also take place in the treatment. Glutathione S-transferase (GST) and cytochrome P450 (CYP) enzymes are prominent drug-metabolizing enzymes in the human body. The aim of this study is to show the expression of GSTP1, GSTM1, CYP1A1, and CYP1B1 in different types of brain tumors and compare our results with those in the literature. Subjects and Methods: The expression of GSTP1, GSTM1, CYP1A1, and CYP1B1 was analyzed using immunostaining in 55 patients with intracranial tumors in 2016–2017. For GST and CYP expression in normal brain tissue, samples of a portion of surrounding normal brain tissue as well as a matched far neighbor of tumor tissue were used. The demographic features of the patients were documented and the expression results compared. Results: The mean age of the patients was 46.72 years; 29 patients were female and 26 were male. Fifty-seven specimens were obtained from 55 patients. Among them, meningioma was diagnosed in 12, metastases in 12, glioblastoma in 9, and pituitary adenoma in 5. The highest GSTP1, GSTM1, and CYP­1A1 expressions were observed in pituitary adenomas. The lowest GSTP1 expression was detected in glioblastomas and the lowest CYP1B1 expression in pituitary adenomas. Conclusion: GSTP1 and CYP expression is increased in intracranial tumors. These results should be confirmed with a larger series and different enzyme subtypes.

Glutathione-S-transferase activity from rat placenta

Placenta ◽  
1986 ◽  
Vol 7 (2) ◽  
pp. 155-162 ◽  
Author(s):  
C. Di Ilio ◽  
P. Sacchetta ◽  
G. Del Boccio ◽  
E. Casalone ◽  
G. Polidoro
Keyword(s):  
Transferase Activity ◽  
Glutathione S Transferase
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