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    Wyświetlanie 1-14 z 14
    Tytuł:
    Cadmium-induced changes in antioxidant enzymes in suspension culture of soybean cells.
    Autorzy:
    Sobkowiak, Robert
    Rymer, Katarzyna
    Rucińska, Renata
    Deckert, Joanna
    Powiązania:
    https://bibliotekanauki.pl/articles/1043349.pdf
    Data publikacji:
    2004
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    ascorbate peroxidase
    superoxide dismutase
    peroxidase
    soybean cell suspension culture
    catalase
    cadmium
    Opis:
    Cadmium (Cd), similarly to other heavy metals, inhibits plant growth. We have recently showed that Cd2+ either stimulates (1-4 μM) or inhibits (ł 6 μM) growth of soybean (Glycine max L.) cells in suspension culture (Sobkowiak & Deckert, 2003, Plant Physiol Biochem. 41: 767-72). Here, soybean cell suspension cultures were treated with various concentrations of Cd2+ (1-10 μM) and the following enzymes were analyzed by native electrophoresis: superoxide dismutase (SOD), catalase (CAT), peroxidase (POX) and ascorbate peroxidase (APOX). We found a significant correlation between the cadmium-induced changes of soybean cell culture growth and the isoenzyme pattern of the antioxidant enzymes. The results suggest that inhibition of growth and modification of antioxidant defense reactions appear in soybean cells when Cd2+ concentration in culture medium increases only slightly, from 4 to 6 μM.
    Źródło:
    Acta Biochimica Polonica; 2004, 51, 1; 219-222
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Differential response of antioxidant enzymes to cadmium stress in tolerant and sensitive cell line of cucumber (Cucumis sativus L.)
    Autorzy:
    Gzyl, Jarosław
    Rymer, Katarzyna
    Gwóźdź, Edward
    Powiązania:
    https://bibliotekanauki.pl/articles/1040497.pdf
    Data publikacji:
    2009
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    cell suspension
    cadmium
    tolerance
    superoxide dismutase
    catalase
    ascorbate peroxidase
    guaiacol peroxidase
    Opis:
    Previously, a stable cell suspension of cucumber tolerant to 100 µM CdCl2 was obtained (Gzyl & Gwóźdź, 2005, Plant Cell Tissue Organ Cult 80: 59-67). In this study, the relationship between the activity of antioxidant enzymes and cadmium tolerance of cucumber cells was analyzed. A cadmium-sensitive and the cadmium-tolerant cell lines were exposed to 100 µM and 200 µM CdCl2 and the activities of superoxide dismutase (SOD), catalase (CAT), ascorbate peroxidase (APOX) and guaiacol peroxidase (POX) were determined. In the sensitive cell line, a decrease of total activity of SOD and POX was observed, whereas the activity of CAT and APOX significantly increased in metal-supplemented medium. By contrast, in the tolerant cells, the total activity of antioxidant enzymes decreased (SOD, CAT) or was maintained at approximately the same level (APOX, POX). Moreover, a different pattern of isoenzyme activity was observed in the tolerant and sensitive cells. These results suggest that an enhanced activity of antioxidant enzymes is not directly involved in the increased tolerance to cadmium of the selected cucumber cell line.
    Źródło:
    Acta Biochimica Polonica; 2009, 56, 4; 723-727
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Kinetic studies on the oxidation of nitrite by horseradish peroxidase and lactoperoxidase
    Autorzy:
    Gębicka, Lidia
    Powiązania:
    https://bibliotekanauki.pl/articles/1044450.pdf
    Data publikacji:
    1999
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    lactoperoxidase
    nitrite
    stopped-flow
    horseradish peroxidase
    Opis:
    The reaction of nitrite (NO-_2) with horseradish peroxidase and lactoperoxidase was studied. Sequential mixing sopped-flow measeruments gave the following values for the rate constants of the reaction of nitrite with compounds II (oxoferryl heme intermediates) of horseradish peroxidase and lactoperoxidase at pH 7.0, 13.3 ± 0.07 mol^{-1}dm^3s^{-1} and 3.5 ± 0.05 · 10^4mol^{-1}dm^3s^{-1}, respectively. Nitrite, at neutral pH, influenced measurements of activity of lactoperoxidase with typical substrates like 2,2'-azino-bis[ethyl-benzothiazoline-(6)-sulphonic acid] (ABTS), guaiacol or thiocyanate (SCN-). The rate of ABTS and guaiacol oxidation increased linearly with nitrite concentration up to 2.5-5 mmol dm^{-3}. On the other hand, two-electron SCN- oxidation was inhibited in the presence od nitrite. Thus, nitrite competed with the investigated substrates of lactoperoxidase. The intermediate, most probably nitrogen dioxide (*NO_2), reacted more rapidly with ABTS or guaiacol than did lactoperoxidase compound II. It did not, however, effectively oxidize SCN- to OSCN-. NO-_2 did not influence the activity measurements of horseradish peroxidase by ABTS or guaiacol method.
    Źródło:
    Acta Biochimica Polonica; 1999, 46, 4; 919-927
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    pH Profile of cytochrome c-catalyzed tyrosine nitration
    Autorzy:
    Kambayashi, Yasuhiro
    Hitomi, Yoshiaki
    Kodama, Norio
    Kubo, Masayuki
    Okuda, Junna
    Takemoto, Kei
    Shibamori, Masafumi
    Takigawa, Tomoko
    Ogino, Keiki
    Powiązania:
    https://bibliotekanauki.pl/articles/1041220.pdf
    Data publikacji:
    2006
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    pseudo-peroxidase
    pH
    cytochrome c
    nitrite
    nitrotyrosine
    Opis:
    In the present study, we investigated how cytochrome c catalyzed the nitration of tyrosine at various pHs. The cytochrome c-catalyzed nitration of tyrosine occurred in proportion to the concentration of hydrogen peroxide, nitrite or cytochrome c. Thecytochromec-catalyzed nitration of tyrosine was inhibited by catalase, sodium azide, cystein, and uric acid. These results show that the cytochrome c-catalyzednitrotyrosine formation was due to peroxidase activity. The rate constant between cytochrome c and hydrogen peroxide within the pH range of 3 - 8 was the largest at pH 6 (37°C). The amount of nitrotyrosine formed was the greatest at pH 5. At pH 3, onlycytochromec-independent nitration of tyrosine occurred in the presence of nitrite. At this pH, the UV as well as visible spectrum of cytochrome c was changed by nitrite, even in the presence of hydrogen peroxide, probably via the formation of a heme iron - nitric oxide complex. Due to this change, the peroxidase activity of cytochrome c was lost.
    Źródło:
    Acta Biochimica Polonica; 2006, 53, 3; 577-584
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Double-edged sword behaviour of gallic acid and its interaction with peroxidases in human microvascular endothelial cell culture (HMEC-1). Antioxidant and pro-oxidant effects
    Autorzy:
    Serrano, José
    Cipak, Ana
    Boada, Jordi
    Gonzalo, Hugo
    Cacabelos, Daniel
    Cassanye, Anna
    Pamplona, Reinald
    Zarkovic, Neven
    Portero-Otin, Manuel
    Powiązania:
    https://bibliotekanauki.pl/articles/1040403.pdf
    Data publikacji:
    2010
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    gallic acid
    peroxidase
    pro-oxidant
    antioxidant
    HMEC-1
    Opis:
    A previous report from our group had shown in vitro a direct interaction between peroxidases and dietary antioxidants at physiological concentrations, where in the absence of H2O2, the antioxidants could serve as oxidizing substrates for the peroxidases. However, the physiological relevance of those findings had not been evaluated. The main objective of this study was to determine whether the oxidizing products produced in the interaction between peroxidase and gallic acid at a physiological concentration of 1 µM may promote cell death or survival in a human microvascular endothelial cell line (HMEC-1). Our findings suggested that gallic acid may show a double-edged sword behaviour, since in the absence of H2O2 it may have a pro-oxidant effect which may promote cell injury (evidenced by LDH, Crystal Violet and calcein AM viability/citotoxicity assays), while in the presence of H2O2, gallic acid may act as an antioxidant inhibiting oxidative species produced in the peroxidase cycle of peroxidases. These observations were confirmed with several oxidative stress biomarkers and the evaluation of the activation of cell survival pathways like AKT and MAPK/ERK.
    Źródło:
    Acta Biochimica Polonica; 2010, 57, 2; 193-198
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Selenium supplementation to chronic kidney disease patients on hemodialysis does not induce the synthesis of plasma glutathione peroxidase
    Autorzy:
    Zachara, Bronislaw
    Gromadzinska, Jolanta
    Zbrog, Zbigniew
    Swiech, Rafal
    Wasowicz, Wojciech
    Twardowska, Ewa
    Jablonska, Ewa
    Sobala, Wojciech
    Powiązania:
    https://bibliotekanauki.pl/articles/1040656.pdf
    Data publikacji:
    2009
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    hemodialysis
    selenium supplementation
    glutathione peroxidase
    chronic kidney disease
    plasma
    Opis:
    Background: Numerous authors have shown that selenium (Se) concentration and glutathione peroxidase (GSH-Px) activity in plasma of chronic kidney disease (CKD) patients are lower than in healthy subjects, but there are only few publications on the level of GSH-Px protein in those patients and no reports on the effect of Se supplementation to HD patients on the level of this enzyme. Subjects and Methods: Se concentration and GSH-Px protein level in plasma were measured in a group of 30 CKD patients on hemodialysis (HD) supplemented with 200 µg Se/day for 3 months, and 28 patients on HD administered with placebo. Se concentration was measured by graphite furnace atomic absorption spectrometry and plasma GSH-Px protein level by the sandwich ELISA method using polyclonal antibody specific for human plasma GSH-Px. Results: Se concentration in patients on placebo did not change throughout the 3-month study period, but increased significantly in Se supplemented group. Se supplementation to CKD patients on HD had no effect on the level of GSH-Px protein. Conclusions: The lack of GSH-Px protein in CKD patients on HD is not linked to Se deficiency since the level of this element increased after Se supplementation while enzyme protein level did not change. The damaged kidney of HD patients is unable to synthesize GSH-Px, even after induction with selenium.
    Źródło:
    Acta Biochimica Polonica; 2009, 56, 1; 183-187
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Selenium, glutathione and glutathione peroxidases in blood of patients with chronic liver diseases.
    Autorzy:
    Czuczejko, Jolanta
    Zachara, Bronisław
    Staubach-Topczewska, Ewa
    Halota, Waldemar
    Kędziora, Józef
    Powiązania:
    https://bibliotekanauki.pl/articles/1043405.pdf
    Data publikacji:
    2003
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    selenium
    glutathione peroxidase
    chronic liver disease
    glutathione
    oxidative stress
    Opis:
    Disturbances in the antioxidant system could play a role in pathogenesis of chronic liver disease. The aim of our study was to evaluate the levels/activities of antioxidants in blood of patients with chronic liver disease. We estimated selenium and glutathione concentrations and glutathione peroxidase activities in blood of 59 patients with chronic hepatitis B or C virus infection (group 1) and 64 patients with alcoholic, autoimmune or cryptogenic chronic liver disease (group 2). The results were compared with 50 healthy controls. Whole blood and plasma selenium and red cell glutathione concentrations were significantly lower in the patients compared with the controls. Red cell glutathione peroxidase activity was slightly reduced in both subgroups of group 1 and in group 2 with normal alanine aminotransferase values. Plasma glutathione peroxidase activity was slightly but significantly higher in patients with elevated aminotransferase values. The findings suggest that disturbances in antioxidant parameters in blood of patients with chronic liver disease may be the cause of the peroxidative damage of cells.
    Źródło:
    Acta Biochimica Polonica; 2003, 50, 4; 1147-1154
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Antioxidant status in erythrocytes of cystic fibrosis children.
    Autorzy:
    Laskowska-Klita, Teresa
    Chełchowska, Magdalena
    Powiązania:
    https://bibliotekanauki.pl/articles/1044199.pdf
    Data publikacji:
    2001
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    superoxide dismutase
    catalase
    glutathione peroxidase
    vitamin E
    erythrocytes
    cystic fibrosis
    Opis:
    Activities of superoxide dismutase, catalase and glutathione peroxidase in erythrocytes of cystic fibrosis children were studied in order to estimate the severity of their deficiency. Our results point to increased susceptibility of erythrocytes of cystic fibrosis subjects to oxidative injury and indicate that the antioxidant status of patients should be carefully monitored.
    Źródło:
    Acta Biochimica Polonica; 2001, 48, 1; 283-285
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Salivary aldehyde dehydrogenase - temporal and population variability, correlations with drinking and smoking habits and activity towards aldehydes contained in food
    Autorzy:
    Giebułtowicz, Joanna
    Dziadek, Marta
    Wroczyński, Piotr
    Woźnicka, Katarzyna
    Wojno, Barbara
    Pietrzak, Monika
    Wierzchowski, Jacek
    Powiązania:
    https://bibliotekanauki.pl/articles/1040385.pdf
    Data publikacji:
    2010
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    superoxide dismutase
    fluorescence
    aldehyde dehydrogenase
    aldehydes
    nutrition safety
    saliva
    salivary peroxidase
    Opis:
    Fluorimetric method based on oxidation of the fluorogenic 6-methoxy-2-naphthaldehyde was applied to evaluate temporal and population variability of the specific activity of salivary aldehyde dehydrogenase (ALDH) and the degree of its inactivation in healthy human population. Analyzed was also its dependence on drinking and smoking habits, coffee consumption, and its sensitivity to N-acetylcysteine. Both the specific activity of salivary ALDH and the degree of its inactivation were highly variable during the day, with the highest activities recorded in the morning hours. The activities were also highly variable both intra- and interpersonally, and negatively correlated with age, and this correlation was stronger for the subgroup of volunteers declaring abstinence from alcohol and tobacco. Moderately positive correlations of salivary ALDH specific activity with alcohol consumption and tobacco smoking were also recorded (rs ~0.27; p=0.004 and rs =0.30; p=0.001, respectively). Moderate coffee consumption correlated positively with the inactivation of salivary ALDH, particularly in the subgroup of non-drinking and non-smoking volunteers. It was found that mechanical stimulation of the saliva flow increases the specific activity of salivary ALDH. The specific activity of the salivary ALDH was strongly and positively correlated with that of superoxide dismutase, and somewhat less with salivary peroxidase. The antioxidant-containing drug N-acetylcysteine increased activity of salivary ALDH presumably by preventing its inactivation in the oral cavity. Some food-related aldehydes, mainly cinnamic aldehyde and anisaldehyde, were excellent substrates of the salivary ALDH3A1 enzyme, while alkenals, particularly those with short chain, were characterized by lower affinity towards this enzyme but high catalytic constants. The protective role of salivary ALDH against aldehydes in food and those found in the cigarette smoke is discussed, as well as its participation in diminishing the effects of alcohol- and smoking-related oxidative stress.
    Źródło:
    Acta Biochimica Polonica; 2010, 57, 3; 361-368
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Red blood cell and plasma glutathione peroxidase activities and selenium concentration in patients with chronic kidney disease: A review
    Autorzy:
    Zachara, Bronisław
    Gromadzińska, Jolanta
    Wąsowicz, Wojciech
    Zbróg, Zbigniew
    Powiązania:
    https://bibliotekanauki.pl/articles/1041155.pdf
    Data publikacji:
    2006
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    hemodialysis
    selenium
    kidney transplantation
    glutathione peroxidase
    chronic kidney disease
    antioxidants
    plasma
    Opis:
    The metabolism of oxygen in aerobic organisms leads to generation of reactive oxygen species (ROS). These entities are able to oxidize almost all classes of macromolecules, including proteins, lipids and nucleic acids. The physiological level of ROS is usually regulated by antioxidant defense mechanisms. There are at least three groups of antioxidant enzymes: superoxide dismutases, catalases and glutathione peroxidases (GSH-Pxs) which neutralize ROS. The trace elements (copper, zinc and selenium) bound to the active sites of the above listed enzymes play an important role in the antioxidant defense system. In mammals, a major function of selenium (Se) and Se-dependent GSH-Pxs is to protect cells from oxidative stress. Selenium concentrations and GSH-Px activities are altered in blood components of chronic kidney disease (CKD) patients. The Se level is frequently lower than in healthy subjects and the concentration very often decreases gradually with advancing stage of the disease. Studies on red cell GSH-Px activity in CKD patients reported its values significantly lower, significantly higher and lower or higher, but not significantly as compared with healthy subjects. On the other hand, all authors who studied plasma GSH-Px activity have shown significantly lower values than in healthy subjects. The degree of the reduction decreases gradually with the progression of the disease. High inverse correlations were seen between plasma GSH-Px activity and creatinine level. A gradual decrease in plasma GSH-Px activity in CKD patients is due to the fact that this enzyme is synthesized predominantly in the kidney and thus the impairment of this organ is the cause of the enzyme's lower activity. Se supplementation to CKD patients has a slightly positive effect in the incipient stage of the disease, but usually no effect was observed in end-stage CKD. Presently, kidney transplantation is the only treatment that may restore plasma Se level and GSH-Px activity in patients suffering from end-stage CKD. A few studies have shown that in kidney recipients, plasma Se concentration and GSH-Px activity are restored to normal values within a period of 2 weeks to 3 months following surgery and thus it can be acknowledged that Se supplementation to those patients has a positive effect on plasma GSH-Px activity.
    Źródło:
    Acta Biochimica Polonica; 2006, 53, 4; 663-677
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Similarity between enzymatic and electrochemical oxidation of 2-hydroxyacridinone, the reference compound of antitumor imidazoacridinones.
    Autorzy:
    Mazerska, Zofia
    Powiązania:
    https://bibliotekanauki.pl/articles/1043630.pdf
    Data publikacji:
    2003
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    peroxidase-mediated oxidation
    antitumor acridinones
    enzymatic activation
    enzymatic and electrochemical transformations
    Opis:
    The present work is part of a wide research project aimed to elucidate the mechanism of the metabolic activation of the antitumor imidazoacridinone agent C-1311 selected for clinical trials. The objectives of the investigations presented here were: (i) to examine the enzymatic transformation of the reference compound 2-hydroxyacridinone and (ii) to test the similarity between enzymatic and electrochemical oxidation of acridinone compounds. This similarity was searched with respect to the usefulness of the electrochemical results for further studies on the metabolic oxidation of imidazoacridinone antitumor drugs. The enzymatic oxidation of 2-hydroxyacridinone was performed with a model system containing various amounts of horseradish peroxidase and hydrogen peroxide and was followed by UV-VIS spectroscopy and by HPLC. One product of the reaction was isolated and its chemical structure was identified. It was shown that 2-hydroxyacridinone was transformed by the studied system in a manner dependent on the amount of the enzyme and on the compound/H2O2 ratio. While under mild reaction conditions the transformation ran slowly to yield only one product, p1, independently of the reaction time, higher enzyme concentration resulted in several steps of transformation. Product p1 turned out to be a dimer: 1,1-bi(2-hydroxyacridinone). A comparison of the results of the enzymatic transformations of 2-hydroxyacridinone presented here with studies on the electrochemical oxidation reported earlier allowed us to show both transformations to be similar as far as the reaction pathway and two reaction products are concerned.
    Źródło:
    Acta Biochimica Polonica; 2003, 50, 2; 515-525
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    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
    Artykuł
    Tytuł:
    Effect of Medicago sativa Mhb1gene expression on defense response of Arabidopsis thaliana plants
    Autorzy:
    Maassen, Anna
    Hennig, Jacek
    Powiązania:
    https://bibliotekanauki.pl/articles/1039900.pdf
    Data publikacji:
    2011
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Arabidopsis thaliana
    pathogen infection
    nitrotyrosine
    nitric oxide
    peroxidase activity
    non-symbiotic hemoglobin
    Opis:
    Besides the previously described nitric oxide-detoxification activity we identified new features of class-1 non-symbiotic hemoglobin from Medicago sativa (Mhb1). Under in vitro conditions, using peroxidase in-gel activity assay, the Mhb1 protein was shown to possess also peroxidase-like activity. Due to this activity, in the presence of nitrite and hydrogen peroxide, the protein can mediate autonitration and nitration of other proteins at tyrosine residues, as revealed by tandem mass spectrometry and immune assay approaches. Mhb1 through its multifunctional activities can affect different components of signal transduction cascades operating during plant response to infections. This influence is manifested by Mhb1-mediated selective up-regulation of expression of certain pathogen inducible genes in Pseudomonas syringae infected Arabidopsis thaliana plants which overproduce Mhb1, as revealed by reverse transcription-quantitative real-time PCR analysis. Changes in expression level of these genes can influence such processes as synthesis of secondary metabolites, protein degradation and biosynthesis of ethylene. They can also result in alteration of pathogen-induced defense response of Mhb1 transgenic plants.
    Źródło:
    Acta Biochimica Polonica; 2011, 58, 3; 427-432
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    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
    Artykuł
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