Wszystkie pola: glutathione reductase - Katalog OPAC zbiorów

Skocz do pozycji: 1.

Tytuł:: In vitro effects of compounds isolated from Sideritis brevibracteata on bovine kidney cortex glutathione reductase
Autorzy:: Tandogan, Berivan
Güvenç, Ayşegül
Çalış, İhsan
Ulusu, Nuriye
Powiązania:: https://bibliotekanauki.pl/articles/1039826.pdf
Data publikacji:: 2011
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: inhibition
glutathione reductase
Sideritis brevibracteata
kinetic
8-hydroxyflavone glycosides
Opis:: Glutathione reductase (GR, E.C 1.6.4.2) is a flavoprotein that catalyzes NADPH-dependent reduction of oxidized glutathione (GSSG) to reduced glutathione (GSH). The aim of this study was to investigate in vitro effects of phenolic compounds isolated from Sideritis brevibracteata on bovine kidney GR. The Sideritis species are widely found in nature and commonly used as medicinal plants. 7-O-glycosides of 8-OH-flavones (hypolaetin, isoscutellarein and 3'-hydroxy-4'-O-methylisoscutellarein) were isolated from aerial parts of Sideritis brevibracteata. These compounds inhibited bovine kidney cortex GR in a concentration-dependent manner. Kinetic characterization of the inhibition was also performed.
Źródło:: Acta Biochimica Polonica; 2011, 58, 4; 471-475
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 2.

Tytuł:: Glutathione reductase activity correlates with concentration of extracellular matrix degradation products in synovial fluid from patients with joint diseases
Autorzy:: Średzińska, Krystyna
Galicka, Anna
Porowska, Halina
Średziński, Łukasz
Porowski, Tadeusz
Popko, Janusz
Powiązania:: https://bibliotekanauki.pl/articles/1040477.pdf
Data publikacji:: 2009
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: glutathione reductase
collagen
glycosaminoglycans
synovial fluid
Opis:: The mechanisms underlying cartilage matrix degradation in joint diseases is not fully understood but reactive oxygen species are implicated as main causative factors. Comparative studies of glutathione reductase (GR) activity in synovial fluid from patients with rheumatoid arthritis (RA), reactive arthritis (ReA) and osteoarthritis (OA) as well as correlations between GR activity and concentration of the major cartilage components in synovial fluid are presented in this study. We found significantly higher activity of GR in RA (about three-fold) and ReA (about two-fold) than in OA. In RA and ReA patients, GR activity in synovial fluid correlates negatively with the concentrations of collagen and degradation products of sulfated glycosaminoglycans. In OA patients the activity of GR was significantly lower than in RA and ReA, which positively correlated with the concentration of collagen and showed a tendency for positive correlation with the degradation products of sulfated glycosaminoglycans. Our results suggest that in RA and ReA patients increased activity of GR does not prevent the increased degradation of collagen and proteoglycans by ROS.
Źródło:: Acta Biochimica Polonica; 2009, 56, 4; 635-640
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 3.

Tytuł:: Changes in GSH-antioxidant system induced by daunorubicin in human normal and diabetic fibroblasts.
Autorzy:: Zatorska, Agnieszka
Maszewski, Janusz
Jóźwiak, Zofia
Powiązania:: https://bibliotekanauki.pl/articles/1043460.pdf
Data publikacji:: 2003
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: glutathione S-transferase
glutathione reductase
glutathione peroxidase
daunorubicin
apoptosis
glutathione
oxidative stress
Opis:: We investigated the effect of daunorubicin on glutathione content and activity of GSH-related enzymes in cultured normal and diabetic human fibroblasts. Cells were incubated with 4 μM daunorubicin (DNR) for 2 h followed by culture in drug-free medium for up to 72 h. Treatment of diabetic cells with the drug caused a time-dependent depletion of intracellular GSH and a decrease of the GSH to total glutathione ratio. GSH depletion was accompanied by apoptotic changes in morphology of the nucleus. Analysis of GSH-related enzymes showed a significant increase of the activities of Se-dependent and Se-independent peroxidases and glutathione S-transferase. In contrast, glutathione reductase activity was reduced by 50%. Significant differences between normal and diabetic cells exposed to DNR were observed in the level of GST and Se-dependent glutathione peroxidase activities. These findings indicated that daunorubicin efficiently affects the GSH antioxidant defense system both in normal and diabetic fibroblasts leading to disturbances in glutathione content as well as in the activity of GSH-related enzymes.
Źródło:: Acta Biochimica Polonica; 2003, 50, 3; 825-835
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 4.

Tytuł:: Glutathione and GSH-dependent enzymes in patients with liver cirrhosis and hepatocellular carcinoma
Autorzy:: Czeczot, Hanna
Ścibior, Dorota
Skrzycki, Michał
Podsiad, Małgorzata
Powiązania:: https://bibliotekanauki.pl/articles/1041298.pdf
Data publikacji:: 2006
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: malondialdehyde
glutathione S-transferase
glutathione reductase
liver cirrhosis
glutathione peroxidase
glutathione
hepatocellular carcinoma
Opis:: We investigated glutathione level, activities of selenium independent GSH peroxidase, selenium dependent GSH peroxidase, GSH S-transferase, GSH reductase and the rate of lipid peroxidation expressed as the level of malondialdehyde in liver tissues obtained from patients diagnosed with cirrhosis or hepatocellular carcinoma. GSH level was found to be lower in malignant tissues compared to adjacent normal tissues and it was higher in cancer than in cirrhotic tissue. Non-Se-GSH-Px activity was lower in cancer tissue compared with adjacent normal liver or cirrhotic tissue, while Se-GSH-Px activity in cancer was found to be similar to its activity in cirrhotic tissue and lower compared to control tissue. An increase in GST activity was observed in cirrhotic tissue compared with cancer tissue, whereas the GST activity in cancer was lower than in adjacent normal tissue. The activity of GSH-R was similar in cirrhotic and cancer tissues, but higher in cancer tissue compared to control liver tissue. An increased level of MDA was found in cancer tissue in comparison with control tissue, besides its level was higher in cancer tissue than in cirrhotic tissue. Our results show that the antioxidant system of cirrhosis and hepatocellular carcinoma is severely impaired. This is associated with changes of glutathione level and activities of GSH-dependent enzymes in liver tissue. GSH and enzymes cooperating with it are important factors in the process of liver diseases development.
Źródło:: Acta Biochimica Polonica; 2006, 53, 1; 237-242
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 5.

Tytuł:: Tocopherol esters inhibit human glutathione S-transferase omega
Autorzy:: Sampayo-Reyes, Adriana
Zakharyan, Robert
Powiązania:: https://bibliotekanauki.pl/articles/1041213.pdf
Data publikacji:: 2006
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: glutathione S-transferase
human
hGSTO1-1
MMA(V) reductase
Vitamin E
Opis:: Human glutathione S-transferase omega 1-1 (hGSTO1-1) is a newly identified member of the glutathione S-transferase (GST) family of genes, which also contains alpha, mu, pi, sigma, theta, and zeta members. hGSTO1-1 catalyzes the reduction of arsenate, monomethylarsenate (MMA(V)), and dimethylarsenate (DMA(V)) and exhibits thioltransferase and dehydroascorbate reductase activities. Recent evidence has show that cytokine release inhibitory drugs, which specifically inhibit interleukin-1b (IL-1b), directly target hGSTO1-1. We found that (+)-α-tocopherol phosphate and (+)-α-tocopherol succinate inhibit hGSTO1-1 in a concentration-dependent manner with IC50 values of 2 µM and 4 µM, respectively. A Lineweaver-Burk plot demonstrated the uncompetitive nature of this inhibition. The molecular mechanism behind the inhibition of hGSTO1-1 by α-tocopherol esters (vitamin E) is important for understanding neurodegenerative diseases, which are also influenced by vitamin E.
Źródło:: Acta Biochimica Polonica; 2006, 53, 3; 547-552
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

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