Characterization of a class alpha glutathione-S-transferase with glutathione peroxidase activity in human liver microsomes

2004 ◽  
Vol 424 (1) ◽  
pp. 72-80 ◽  
Author(s):  
K Sandeep Prabhu ◽  
Padala V Reddy ◽  
Emily C Jones ◽  
Andrew D Liken ◽  
C Channa Reddy
Keyword(s):  
Glutathione Peroxidase ◽  
Peroxidase Activity ◽  
Human Liver ◽  
Liver Microsomes ◽  
Human Liver Microsomes ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase

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 Characterization of the basic glutathione S-transferase B1 and B2 subunits from human liver

1987 ◽  
Vol 244 (1) ◽  
pp. 55-61 ◽  
Author(s):  
P K Stockman ◽  
L I McLellan ◽  
J D Hayes
Keyword(s):  
Glutathione Peroxidase ◽  
Human Liver ◽  
Catalytic Properties ◽  
Peptide Mapping ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase ◽  
Tryptic Peptides ◽  
Glutathione S Transferases ◽  
Tributyltin Acetate

The basic glutathione S-transferases in human liver are composed of at least two immunochemically distinct polypeptides, designated B1 and B2. These subunits exist as homodimers, but can hybridize to form the B1B2 heterodimer [Stockman, Beckett & Hayes (1985) Biochem. J. 227, 457-465]. Although these basic glutathione S-transferases possess similar catalytic properties, the B2 subunit exhibits significantly greater selenium-independent glutathione peroxidase activity than subunit B1. The use of the ligands haematin, tributyltin acetate and Bromosulphophthalein as inhibitors of 1-chloro-2,4-dinitrobenzene-GSH-conjugating activity clearly discriminate between the B1 and B2 subunits and should help facilitate their identification. Peptide mapping experiments showed that B1 and B2 are structurally distinct, but related, subunits; subunit B1 yielded 43 tryptic peptides, seven of which were unique, whereas subunit B2 yielded 40 tryptic peptides, four of which were unique.

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.

Characterization of 1′-Hydroxymidazolam Glucuronidation in Human Liver Microsomes

2007 ◽  
Vol 36 (2) ◽  
pp. 331-338 ◽  
Author(s):  
Bing Zhu ◽  
David Bush ◽  
George A. Doss ◽  
Stella Vincent ◽  
Ronald B. Franklin ◽  
...  
Keyword(s):  
Human Liver ◽  
Liver Microsomes ◽  
Human Liver Microsomes

Isolation and characterization of a cytochrome P450 of the IIA subfamily from human liver microsomes

1991 ◽  
Vol 200 (2) ◽  
pp. 511-517 ◽  
Author(s):  
Manuelle MAURICE ◽  
Stephane EMILIANI ◽  
Isabelle DALET-BELUCHE ◽  
Jean DERANCOURT ◽  
Reinhard LANGE
Keyword(s):  
Cytochrome P450 ◽  
Human Liver ◽  
Liver Microsomes ◽  
Human Liver Microsomes ◽  
Isolation And Characterization
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