Isolation and characterization of two mouse Pi-class glutathione S-transferase genes

Pi-class glutathione S-transferases (GSTs) play an important role in the detoxification of chemical toxins and mutagens and are implicated in neoplastic development and drug resistance. In all species characterized to date, only one functional Pi-class GST gene has been described. In this report we have identified two actively transcribed murine Pi-class GST genes, Gst p-1 and Gst p-2. The coding regions of Gst p-1 and the mouse Pi-class GST cDNA (GST-II) reported by Hatayama, Satoh and Satoh (1990) (Nucleic Acids Res. 18, 4606) are identical, whereas Gst p-2 encodes a protein that has not been described previously. The two genes are approximately 3 kb long and contain seven exons interrupted by six introns. In addition to a TATA box and a sequence motif matching the phorbol-ester-responsive element, the promoters of Gst p-1 and Gst p-2 exhibit one and two G+C boxes (GGGCGG) respectively. The cDNAs of the two genes were isolated from total liver RNA using reverse PCR. The peptide sequence deduced from the cDNAs share 97% identity and differ in six amino acids. Both genes are transcribed at significantly higher levels in male mouse liver than in female, and Gst p-1 mRNA is more abundant in both sexes than Gst p-2.

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Differential induction of class Alpha glutathione S-transferases in mouse liver by the anticarcinogenic antioxidant butylated hydroxyanisole. Purification and characterization of glutathione S-transferase Ya1Ya1

Biochemical Journal ◽

10.1042/bj2630393 ◽

1989 ◽

Vol 263 (2) ◽

pp. 393-402 ◽

Cited By ~ 42

Author(s):

L I McLellan ◽

J D Hayes

Keyword(s):

Female Mouse ◽

Mouse Liver ◽

Normal Mouse ◽

Butylated Hydroxyanisole ◽

Glutathione S Transferase ◽

Purification And Characterization ◽

Glutathione S Transferases ◽

Differential Induction ◽

Carcinogenic Compound

A novel cytosolic Alpha class glutathione S-transferase (GST) that is not normally expressed in mouse liver was found to be markedly induced (at least 20-fold) by the anti-carcinogenic compound butylated hydroxyanisole. This enzyme (designated GST Ya1 Ya1) did not bind to either the S-hexylglutathione-Sepharose or the glutathione-Sepharose affinity matrices, and purification was achieved by using bromosulphophthalein-glutathione-Sepharose. The purified isoenzyme, which comprises subunits of Mr 25,600, was characterized, and its catalytic, electrophoretic, immunochemical and structural properties are documented. GST Ya1 Ya1 was shown to be distinct from the Alpha class GST that is expressed in normal mouse liver and is composed of 25,800-Mr subunits; the Alpha class isoenzyme that is constitutively expressed in the liver is now designated GST Ya3 Ya3. Hepatic concentrations of GST Ya3 Ya3 were not significantly affected when mice were treated with butylated hydroxyanisole. Both Pi class GST (subunit Mr 24,800) and Mu class GST (subunit Mr 26,400) from female mouse liver were induced by dietary butylated hydroxyanisole. By contrast, hepatic concentrations of microsomal GST (subunit Mr 17,300) were unaffected.

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The structure of the human glutathione S-transferase π gene

Biochemical Journal ◽

10.1042/bj2550079 ◽

1988 ◽

Vol 255 (1) ◽

pp. 79-83 ◽

Cited By ~ 86

Author(s):

I G Cowell ◽

K H Dixon ◽

S E Pemble ◽

B Ketterer ◽

J B Taylor

Keyword(s):

Phorbol Ester ◽

Transcription Initiation ◽

Initiation Site ◽

Polyoma Virus ◽

Transcription Initiation Site ◽

Tata Box ◽

Cosmid Library ◽

Sequence Motif ◽

Glutathione S Transferase ◽

Responsive Element

The human glutathione S-transferase pi gene has been isolated from a cosmid library. The gene spans approximately 3 kb, is interrupted by six introns and the region around its 5′ end has the high G + C and CpG content typical of an HTF (HpaII tiny fragment) island. In addition to a TATA box at position -28 relative to the transcription initiation site and two G + C boxes (GGGCGG), the promoter contains a sequence motif matching the phorbol ester- and ras-responsive element from the polyoma virus enhancer.

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Isolation and characterization of GTP cyclohydrolase I from mouse liver. Comparison of normal and the hph-1 mutant

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)98895-2 ◽

1991 ◽

Vol 266 (19) ◽

pp. 12294-12300

Author(s):

K.W. Cha ◽

K.B. Jacobson ◽

J.J. Yim

Keyword(s):

Mouse Liver ◽

Gtp Cyclohydrolase I ◽

Gtp Cyclohydrolase ◽

Isolation And Characterization

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Isolation and Characterization of the Gene Encoding Rat Class θ Glutathione S-Transferase Subunit Yrs

Biochemical and Biophysical Research Communications ◽

10.1006/bbrc.1994.2799 ◽

1994 ◽

Vol 205 (2) ◽

pp. 1250-1256 ◽

Cited By ~ 10

Author(s):

K. Ogura ◽

T. Nishiyama ◽

A. Hiratsuka ◽

T. Watabe ◽

T. Watabe

Keyword(s):

Glutathione S Transferase ◽

Gene Encoding ◽

Isolation And Characterization

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Isolation and Characterization of Dehydration-Responsive Element-Binding Factor 2C (MsDREB2C) from Malus sieversii Roem.

Plant and Cell Physiology ◽

10.1093/pcp/pct087 ◽

2013 ◽

Vol 54 (9) ◽

pp. 1415-1430 ◽

Cited By ~ 20

Author(s):

Kai Zhao ◽

Xinjie Shen ◽

Huazhao Yuan ◽

Yun Liu ◽

Xiong Liao ◽

...

Keyword(s):

Malus Sieversii ◽

Isolation And Characterization ◽

Binding Factor ◽

Responsive Element

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Purification and characterization of prostaglandin-H E-isomerase, a sigma-class glutathione S-transferase, from Ascaridia galli

Biochemical Journal ◽

10.1042/bj3130223 ◽

1996 ◽

Vol 313 (1) ◽

pp. 223-227 ◽

Cited By ~ 41

Author(s):

David J. MEYER ◽

Richmond MUIMO ◽

Michael THOMAS ◽

David COATES ◽

R. Elwyn ISAAC

Keyword(s):

Parasitic Nematode ◽

Helminth Parasites ◽

Ascaridia Galli ◽

Glutathione S Transferase ◽

Purification And Characterization ◽

Parasitic Helminths ◽

Accessory Cells ◽

Glutathione S Transferases ◽

Prostaglandin H

Comparison of partial primary sequences of sigma-class glutathione S-transferases (GSH) of parasitic helminths and a GSH-dependent prostaglandin (PG)-H D-isomerase of rat immune accessory cells suggested that some of the helminth enzymes may also be involved in PG biosynthesis [Meyer and Thomas (1995) Biochem. J. 311, 739-742]. A soluble GSH transferase of the parasitic nematode Ascaridia galli has now been purified which shows high activity and specificity in the GSH-dependent isomerization of PGH to PGE, comparable to that of the rat spleen enzyme in its isomerization of PGH to PGD, and similarly stimulates the activity of prostaglandin H synthase. The enzyme subunit is structurally related to the rat spleen enzyme and sigma-class GSH transferases of helminths according to the partial primary sequence. The data support the hypothesis that some sigma-class GSH transferases of helminth parasites are involved in PG biosynthesis which, in the case of PGE, is likely to be associated with the subversion or suppression of host immunity. A PG-H E-isomerase of comparable specificity and activity has not previously been isolated.

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Characterization of glutathione S-transferases in rat kidney. Alteration of composition by cis-platinum

Biochemical Journal ◽

10.1042/bj2520127 ◽

1988 ◽

Vol 252 (1) ◽

pp. 127-136 ◽

Cited By ~ 26

Author(s):

G M Trakshel ◽

M D Maines

Keyword(s):

Specific Activity ◽

Rat Kidney ◽

Male Rats ◽

Glutathione S Transferase ◽

Aberrant Form ◽

Glutathione S Transferases ◽

Exchange Matrix ◽

Rat Kidney Cytosol

We have developed chromatographic and mathematical protocols that allowed the high resolution of glutathione S-transferase (GST) subunits, and the identification of a previously unresolved GST monomer in rat kidney cytosol; the monomer was identified tentatively as subunit 6. Also, an aberrant form of GST 7-7 dimer appeared to be present in the kidney. This development was utilized to illustrate the response of rat kidney GST following cis-platinum treatment in vivo. Rat kidney cytosol was separated into three ‘affinity families’ of GST activity after elution from a GSH-agarose matrix. The affinity peaks were characterized by quantitative differences in their subunit and dimeric compositions as determined by subsequent chromatography on a cation-exchange matrix and specific activity towards substrates. By use of these criteria, the major GST dimers of affinity peaks were tentatively identified. The major GST dimers in peak I were GST 1-1 and 1-2, in affinity peak II it was GST 2-2, and in peak III they were GST 3-3 and 7-7. GST 3-6 and/or 4-6, which have not been previously resolved in kidney cytosol, were also present in peak II. Alterations in the kidney cytosolic GST composition of male rats were detected subsequent to the administration of cis-platinum (7.0 mg/kg subcutaneously, 6 days). This treatment caused a pronounced alteration in the GST profile, and the pattern of alteration was markedly different from that reported for other chemicals in the kidney or in the liver. In general, the cellular contents of the GSTs of the Alpha and the Mu classes decreased and increased respectively. It is postulated that the decrease in the Alpha class of GSTs by cis-platinum treatment may be related to renal cortical damage and the loss of GSTs in the urine. The increase in the Mu class of GSTs could potentially stem from a lowered serum concentration of testosterone; the latter is a known effect of cis-platinum treatment.

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