scholarly journals A glutathione S-transferase with glutathione-peroxidase activity from Arabidopsis thaliana. Molecular cloning and functional characterization

1993 ◽  
Vol 216 (2) ◽  
pp. 579-586 ◽  
Author(s):  
Dieter BARTLING ◽  
Renate RADZIO ◽  
Ulrike STEINER ◽  
Elmar W. WEILER
Keyword(s):  
Arabidopsis Thaliana ◽  
Glutathione Peroxidase ◽  
Molecular Cloning ◽  
Peroxidase Activity ◽  
Functional Characterization ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase

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.

Glutathione S-transferase isoenzymes and glutathione peroxidase activity in normal and tumour samples from human lung

1988 ◽  
Vol 9 (9) ◽  
pp. 1617-1621 ◽  
Author(s):  
James Carmichael ◽  
Lesley M. Forrester ◽  
Alexander D. Lewis ◽  
John D. Hayes ◽  
Peter C. Hayes ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Peroxidase Activity ◽  
Human Lung ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase

scholarly journals Glutathione S-transferases of the bovine retina. Evidence that glutathione peroxidase activity is the result of glutathione S-transferase

1982 ◽  
Vol 205 (1) ◽  
pp. 213-217 ◽  
Author(s):  
R P Saneto ◽  
Y C Awasthi ◽  
S K Srivastava
Keyword(s):  
Glutathione Peroxidase ◽  
Peroxidase Activity ◽  
Structural Parameters ◽  
Gel Filtration ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase ◽  
Ph Optimum ◽  
Bovine Retina ◽  
Apparent Homogeneity ◽  
Glutathione S Transferases

We have purified two isoenzymes of glutathione S-transferase from bovine retina to apparent homogeneity through a combination of gel-filtration chromatography, affinity chromatography and isoelectric focusing. The more anionic (pI = 6.34) and less anionic (pI = 6.87) isoenzymes were comparable with respect to kinetic and structural parameters. The Km for both substrates, reduced glutathione and 1-chloro-2,4-dinitrobenzene, bilirubin inhibition of glutathione conjugation to 1-chloro-2,4-dinitrobenzene, 1-chloro-2,4-dinitrobenzene inactivation of enzyme activity and molecular weight were similar. However, pH optimum and energy of activation were found to differ considerably. Retina was found to have no selenium-dependent glutathione peroxidase activity. The total glutathione peroxidase activity fractionated with the transferases in the gel-filtration range of mol.wt. 49000 and expressed activity with only organic hydroperoxides as substrate. Only the more anionic isoenzyme expressed both transferase and peroxidase activity.

Microsomal glutathione S-transferase A1-1 with glutathione peroxidase activity from sheep liver: molecular cloning, expression and characterization

2001 ◽  
Vol 360 (2) ◽  
pp. 345-354 ◽  
Author(s):  
K. Sandeep PRABHU ◽  
Padala V. REDDY ◽  
Eric GUMPRICHT ◽  
George R. HILDENBRANDT ◽  
Richard W. SCHOLZ ◽  
...  
Keyword(s):  
Amino Acid ◽  
Glutathione Peroxidase ◽  
Molecular Mass ◽  
Peroxidase Activity ◽  
Sequence Similarity ◽  
Liver Microsomes ◽  
Amino Acid Residues ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase ◽  
Sheep Liver

A 25kDa subunit of glutathione S-transferase (GST) from sheep liver microsomes (microsomal GSTA1-1) with a significant selenium-independent glutathione peroxidase activity has been isolated and characterized. Several analytical criteria, including EDTA stripping, protease protection assay and extraction with alkaline Na2CO3, indicate that the microsomal GSTA1-1 is associated with the inner microsomal membrane. The specific cDNA nucleotide sequence reveals that the enzyme is made up of 222 amino acid residues and shares approx. 73–83% sequence similarity to Alpha-class GSTs from different species. The molecular mass, as determined by electrospray mass ionization, is 25611.3Da. The enzyme is distinct from the previously reported rat liver microsomal GST in both amino acid sequence and catalytic properties [Morgenstern, Guthenberg and DePierre (1982) Eur. J. Biochem. 128, 243–248]. The microsomal GSTA1-1 differs from the sheep liver cytosolic GSTs, reported previously from this laboratory, in its substrate specificity profile and molecular mass [Reddy, Burgess, Gong, Massaro and Tu (1983) Arch. Biochem. Biophys. 224, 87–101]. In addition to catalysing the conjugation of 4-hydroxynonenal with GSH, the enzyme also exhibits significant glutathione peroxidase activity towards physiologically relevant fatty acid hydroperoxides, such as linoleic and arachidonic acid hydroperoxides, as well as phosphatidylcholine hydroperoxide, but not with H2O2. Thus the microsomal GSTA1-1 isoenzyme might have an important role in the protection of biological membranes against oxidative damage.

scholarly journals Two immunologically distinct Yc-type subunits are present in rat lung glutathione S-transferases

1984 ◽  
Vol 224 (1) ◽  
pp. 335-338 ◽  
Author(s):  
S V Singh ◽  
Y C Awasthi
Keyword(s):  
Glutathione Peroxidase ◽  
Rat Liver ◽  
Peroxidase Activity ◽  
Gel Electrophoresis ◽  
Rat Lung ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase ◽  
Two Dimensional Gel Electrophoresis ◽  
Glutathione S Transferases

Two types of 25 000-Mr subunits are present in rat lung glutathione S-transferase I (pI 8.8). These subunits, designated Yc and Yc', are immunologically and functionally distinct from each other. The homodimers YcYc (pI 10.4) and Yc'Yc' (pI 7.6) obtained by hybridization in vitro of the two subunits of glutathione S-transferase I (pI 8.8) were isolated and characterized. Results of these studies indicate that only the Yc subunits express glutathione peroxidase activity and cross-react with the antibodies raised against glutathione S-transferase B (YaYc) or rat liver. The Yc' subunits do not express glutathione peroxidase activity and do not cross-react with the antibodies raised against glutathione S-transferase B of rat liver. The amino acid compositions of these two subunits are also different. These two subunits can also be separated by the two-dimensional gel electrophoresis of glutathione S-transferase I (pI 8.8) of rat lung.

scholarly journals The influence of melatonin on the state of the glutathione system of the rat liver under the conditions of subacute alcoholic intoxication

2014 ◽  
Vol 18 (3 (71)) ◽  
Author(s):  
N. V. Davydova
Keyword(s):  
Glutathione Peroxidase ◽  
Oral Administration ◽  
Rat Liver ◽  
Peroxidase Activity ◽  
Reduced Glutathione ◽  
Alcohol Intoxication ◽  
Transferase Activity ◽  
Glutathione System ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase

The investigations of certain parameters of glutathione system in the liver of rats under the conditions of subacute alcohol intoxication revealed a decreased content of reduced glutathione and glutathione peroxidase activity as well as an activation of glutathione-S-transferase activity. An oral administration of “Vita-melatonin” against a background of subacute alcohol intoxication in a dose 5 mg/kg during 10 days prevented the changes of the parameters under study.

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