scholarly journals Toxic effects of ozone on murine L929 fibroblasts. Enzyme inactivation and glutathione depletion

1987 ◽  
Vol 242 (3) ◽  
pp. 707-712 ◽  
Author(s):  
J Van der Zee ◽  
T M A R Dubbelman ◽  
T K Raap ◽  
J Van Steveninck
Keyword(s):  
Lysosomal Enzymes ◽  
Prolonged Exposure ◽  
Enzyme Inactivation ◽  
Ozone Exposure ◽  
Glutathione Depletion ◽  
Mitochondrial Enzymes ◽  
Oxidized Glutathione ◽  
Atp Content ◽  
Murine Fibroblasts ◽  
Reduced And Oxidized Glutathione

Exposure of L929 murine fibroblasts to ozone resulted in K+ leakage and inhibition of several enzymes. Most sensitive to ozone exposure were glyceraldehyde-3-phosphate dehydrogenase and pyruvate kinase. The activities of another cytosolic enzyme, lactate dehydrogenase, the mitochondrial enzymes glutamate dehydrogenase, succinate dehydrogenase, cytochrome c oxidase and the activity of the lysosomal enzymes acid phosphatase and beta-glucuronidase were, initially, not or only slightly affected. The localization of the lysosomal enzymes did not change during ozone exposure. After prolonged exposure complete deterioration of the cells was observed and all enzyme activities declined. The activity of the enzymes was also monitored during ozone exposure of a sonicated cell suspension and it was shown that all these enzymes are in fact susceptible to ozone. These observations clearly demonstrate that, besides the structure and amino acid composition of an enzyme, the localization in the cell plays an important role in its susceptibility to ozone. The intracellular levels of reduced and oxidized glutathione were affected as well. The ATP content, however, proved to be insensitive to ozone exposure.

scholarly journals Coordination chemistry of glutathione.

1999 ◽  
Vol 46 (3) ◽  
pp. 567-580 ◽  
Author(s):  
A Krezel ◽  
W Bal
Keyword(s):  
Glutamic Acid ◽  
Metal Ions ◽  
Metal Ion ◽  
Reduced Glutathione ◽  
Transition Metal Ions ◽  
Oxidized Glutathione ◽  
Binding Modes ◽  
Glutamic Acid Residue ◽  
Reduced And Oxidized Glutathione ◽  
Soft Metal

The metal ion coordination abilities of reduced and oxidized glutathione are reviewed. Reduced glutathione (GSH) is a very versatile ligand, forming stable complexes with both hard and soft metal ions. Several general binding modes of GSH are described. Soft metal ions coordinate exclusively or primarily through thiol sulfur. Hard ones prefer the amino acid-like moiety of the glutamic acid residue. Several transition metal ions can additionally coordinate to the peptide nitrogen of the gamma-Glu-Cys bond. Oxidized glutathione lacks the thiol function. Nevertheless, it proves to be a surprisingly efficient ligand for a range of metal ions, coordinating them primarily through the donors of the glutamic acid residue.

Development and Validation of HPLC Method for Simultaneous Estimation of Reduced and Oxidized Glutathione in Bulk Pharmaceutical Formulation

2021 ◽  
Vol 8 (1) ◽  
Author(s):  
Singh N ◽  
◽  
Akhtar MJ ◽  
Anchliya A ◽  
◽  
...  
Keyword(s):  
Detection Limit ◽  
Limit Of Detection ◽  
Reduced Glutathione ◽  
Pharmaceutical Formulations ◽  
Hplc Method ◽  
Simultaneous Estimation ◽  
Oxidized Glutathione ◽  
Range Limit ◽  
Limit Of Quantification ◽  
Reduced And Oxidized Glutathione

The objective of this study was the development, optimization, and validation of a RP-HPLC method for the quantification of reduced glutathione (GSH) and oxidized glutathione (GSSG) in pharmaceutical formulations The separation utilized a C18 column at room temperature with absorption wavelength 210nm. The mobile phase was an isocratic flow of a 95:5 (v/v) mixture of 25mM phosphate buffer (pH 2.7) and methanol with flow rate at 1.0 mL/min. Validation of the method assessed with the methods ability in seven categories: linearity, range, limit of detection, limit of quantification, accuracy, precision, and selectivity. The method show an acceptable degree of linearity with r²=0.9994 and 0.999 over a concentration range of 10-200 μg/mL for GSH and GSSG respectively. The detection limit and quantification limit for GSH 20.7μg/mL and 69.24μg/mL and for GSSG 17.22μg/mL and 57.42μg/mL respectively. The percent recovery of the method was 99.98-100.93 %. Following validation, the method was employed in the determination of glutathione in pharmaceutical formulations in the form of a liposome. The proposed method offers a simple, accurate, and inexpensive way to quantify reduced glutathione.

Arbutin prevents alterations in mitochondrial and lysosomal enzymes in isoproterenol-induced myocardial infarction: An in vivo study

2020 ◽  
Vol 40 (1) ◽  
pp. 100-112
Author(s):  
S Sivasangari ◽  
L Asaikumar ◽  
L Vennila
Keyword(s):  
Myocardial Infarction ◽  
Lysosomal Enzymes ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Heart Tissue ◽  
Lipoprotein Cholesterol ◽  
Tissue Homogenate ◽  
Mitochondrial Enzymes ◽  
Low Density ◽  
Low Density Lipoprotein Cholesterol

The present study demonstrated the protective effects of arbutin (ARB) on hyperlipidemia, mitochondrial, and lysosomal membrane damage and on the DNA damage in rats with isoproterenol (ISO)-induced myocardial infarction (MI). Rats were pretreated with ARB (25 and 50 mg/kg body weight (bw)) for 21 days. After pretreatment with ARB, MI was induced by subcutaneous injection of ISO (60 mg/kg bw) for two consecutive days at an interval of 24 h. The levels of TC, TG, and FFA were increased and decreased the level of PL in the heart tissue of ISO-induced MI rats. Very-low-density lipoprotein cholesterol and low-density lipoprotein cholesterol were increased while high-density lipoprotein cholesterol was decreased in the plasma of ISO-administered rats. A heart mitochondrial fraction of the ISO rats showed a significant decrease in the activities of mitochondrial enzymes isocitrate dehydrogenase, α-ketoglutarate dehydrogenase, succinate dehydrogenase, and malate dehydrogenase. The activities of lysosomal enzymes (β-glucosidase, β-glucuronidase, α-galactosidase, β-galactosidase, cathepsin-B, and cathepsin-D) were increased significantly in the heart tissue homogenate of disease control rats. In ISO-induced MI, rat’s significant increase in the percentage of tail DNA and tail length, and a decrease in the level of head DNA were also observed. ARB administration to MI rats brought all these parameters to near normality, showing the protective effect of ARB against MI in rats. The results of this study demonstrated that the 50 mg/kg bw of ARB shows higher protection than 25 mg/kg bw against ISO-induced damage.

scholarly journals The role of metal ion binding in the antioxidant mechanisms of reduced and oxidized glutathione in metal-mediated oxidative DNA damage

Metallomics ◽  
2020 ◽  
Vol 12 (1) ◽  
pp. 79-91 ◽  
Author(s):  
Elias O. U. Eteshola ◽  
Devin A. Haupt ◽  
Stephen I. Koos ◽  
Lee A. Siemer ◽  
Daniel L. Morris
Keyword(s):  
Dna Damage ◽  
Metal Ion ◽  
Oxidative Dna Damage ◽  
Ion Binding ◽  
Oxidized Glutathione ◽  
Metal Ion Binding ◽  
Reduced And Oxidized Glutathione ◽  
Antioxidant Mechanisms

GSH and GSSG appear to function as antioxidants against metal-mediated oxidative DNA damage by coordinating Fe(ii) and Cu(ii).

scholarly journals Determination of Blood Total, Reduced, and Oxidized Glutathione in Pediatric Subjects

2001 ◽  
Vol 47 (8) ◽  
pp. 1467-1469 ◽  
Author(s):  
Anna Pastore ◽  
Fiorella Piemonte ◽  
Mattia Locatelli ◽  
Anna Lo Russo ◽  
Laura Maria Gaeta ◽  
...  
Keyword(s):  
Oxidized Glutathione ◽  
Reduced And Oxidized Glutathione

scholarly journals Characterization of Oxidative Stress in Various Tissues of Diabetic and Galactose-fed Rats

2001 ◽  
Vol 2 (3) ◽  
pp. 211-216 ◽  
Author(s):  
Robert M. Strother ◽  
Tonya G. Thomas ◽  
Mary Otsyula ◽  
Ruth A. Sanders ◽  
John B. Watkins III
Keyword(s):  
Oxidative Stress ◽  
Lipid Peroxidation ◽  
Superoxide Dismutase ◽  
Glutathione Peroxidase ◽  
Rat Model ◽  
Catalase Activity ◽  
Diabetic Rats ◽  
Oxidized Glutathione ◽  
Hepatic Glutathione ◽  
Reduced And Oxidized Glutathione

Rats fed a galactose-rich diet have been used for several years as a model for diabetes to study, particularly in the eye, the effects of excess blood hexoses. This study sought to determine the utility of galactosemia as a model for oxidative stress in extraocular tissues by examining biomarkers of oxidative stress in galactose-fed rats and experimentally-induced diabetic rats. Sprague-Dawley rats were divided into four groups: experimental control; streptozotocin-induced diabetic; insulin-treated diabetic; and galactose-fed. The rats were maintained on these regimens for 30 days, at which point the activities of catalase, glutathione peroxidase, glutathione reductase, and superoxide dismutase, as well as levels of lipid peroxidation and reduced and oxidized glutathione were determined in heart, liver, and kidney. This study indicates that while there are some similarities between galactosemic and diabetic rats in these measured indices of oxidative stress (hepatic catalase activity levels and hepatic and renal levels of oxidized glutathione in both diabetic and galactosemic rats were significantly decreased when compared to normal), overall the galactosemic rat model is not closely parallel to the diabetic rat model in extra-ocular tissues. In addition, several effects of diabetes (increased hepatic glutathione peroxidase activity, increased superoxide dismutase activity in kidney and heart, decreased renal and increased cardiac catalase activity) were not mimicked in galactosemic rats, and glutathione concentration in both liver and heart was affected in opposite ways in diabetic rats and galactose- fed rats. Insulin treatment reversed/prevented the activity changes in renal and cardiac superoxide dismutase, renal and cardiac catalase, and hepatic glutathione peroxidase as well as the hepatic changes in lipid peroxidation and reduced and oxidized glutathione, and the increase in cardiac glutathione. Thus, prudence should be exercised in the use of experimentally galactosemic rats as a model for diabetes until the correspondence of the models has been more fully characterized.

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