Specific inactivation of glutathione S-transferases in Class Pi by SH-modifiers

Tamai, Katsuto; Satoh, Keisuke; Tsuchida, Shigeki; Hatayama, Ichiro; Maki, Takako; Sato, Kei

doi:10.1016/0006-291x(90)91769-o

Cited by 102 publications

(55 citation statements)

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“…A previous sitedirected mutagenesis study revealed that the three cysteine residues of the lysine\serine form were not involved in enzyme activity [9]. The presence of reactive cysteine residues has been reported in the Pi class GST forms [6,46]. Both GST-P (7-7) and GST 3-3 are increased in rat pre-neoplastic hepatic lesions [47], but whereas the Pi class are inactivated by H # O # through disulphide bond formation between two cysteine residues [7], this is not the case for either the asparagine\cysteine or lysine\serine forms of GST 3-3.…”

Section: Discussionmentioning

confidence: 97%

“…In order to identify the reactive cysteine residue of HHR GST subunit 3, the enzyme (300 µg protein) was treated with 1 mM DDPM, as reported previously [6]. After digestion with DPCCtreated trypsin, peptides were separated by HPLC and DDPMlabelled peptides were detected by absorbance at 320 nm.…”

Section: Ddpm Treatment and Trypsin Digestionmentioning

confidence: 99%

“…The forms in the Alpha class possess high glutathione peroxidase activity towards lipid hydroperoxides [4]. Conjugation reactions of the Mu-class forms are activated by active oxygen species [5], whereas the Pi class is inactivated by SH reagents and H # O # ; modification of cysteine residues being responsible [6,7]. The GST forms have been suggested to play important roles in the prevention of tissue damage by oxidative stress [3,8].…”

Section: Introductionmentioning

confidence: 99%

“…Although cysteine residues of GSTs are not directly involved in enzyme activity [6,9], those of other enzymes and proteins play important roles in processes, such as catalysis [10], protein folding [11] and DNA binding [12]. Modification of cysteine residues with GSH has been reported for many enzymes, such as carbonic anhydrase [13] and fatty acid synthetase [14], and the amounts of glutathionylated forms may be increased in response Abbreviations used : HHR, Hirosaki hairless rat ; SD, Sprague-Dawley ; GST, glutathione transferase ; NEM, N-ethylmaleimide ; CDNB, 1-chloro-2,4-dinitrobenzene ; DDPM, N- (4-dimethylamino-3,5-dinitrophenyl)maleimide ; DPCC, diphenylcarbamyl chloride ; TFA, trifluoroacetic acid ; MALDI-TOF, matrix-assisted laser desorption-ionization-time-of-flight ; DTT, dithiothreitol, RT-PCR, reverse transcriptase PCR.…”

Section: Introductionmentioning

confidence: 99%

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Polymorphism of the glutathione transferase subunit 3 in Sprague–Dawley rats involves a reactive cysteine residue

Kumano

Kimura

Hayakari

et al. 2000

Biochemical Journal

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Comparison of Hirosaki hairless rat (HHR) and SpragueDawley (SD) rat liver glutathione transferase (GST) subunits by HPLC revealed differences in subunit 3 ; a new peak was detected in HHR GSTs and this was tentatively named X. By chromatofocusing, the HHR GST form composed of peak X and SD rat GST 3-3 were eluted at pH 8.8 and 9.1 respectively. The former was more sensitive to the SH reagent N-ethylmaleimide (NEM) than the latter. GSSG treatment of peak X resulted in a shift of retention time (peak Y) by HPLC analysis. However, such conversion was not observed for the SD rat GST 3-3 following GSSG or dithiothreitol (DTT) treatment. Peak Y exhibited m\z values of 26091.9 and 26125.4 by matrix-assisted laser-desorption ionization-time-of-flight MS, higher than those of peak X by 304-307, equivalent to the molecular-mass value of GSH. On treatment with DTT, peak Y was converted into peak X, with release of a substance with HPLC-characteristics of GSH. This substance was confirmed to be GSH by liquid chromatography\ MS. These results thus indicated peak Y to be a glutathionylated form of peak X. Quantification revealed the release of

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Section: Discussionmentioning

confidence: 97%

Section: Ddpm Treatment and Trypsin Digestionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Polymorphism of the glutathione transferase subunit 3 in Sprague–Dawley rats involves a reactive cysteine residue

Kumano

Kimura

Hayakari

et al. 2000

Biochemical Journal

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“…Enzymatic properties of GSTs in the Pi class GST-P and other GSTs in the Pi class have unique enzymatic properties ; low sensitivity to organic anion inhibitors ) and high sensitivity to sulfhydryl-modifiers and active oxygen species (Tamai et al 1990.…”

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confidence: 99%

Specific Expression of Glutathione S-transferase Pi Forms in (Pre)neoplastic Tissues: Their Properties and Functions.

Sato

Satoh

Tsuchida

et al. 1992

Tohoku J. Exp. Med.

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The detection of preneoplastic cells is very important for the analysis of carcinogenic processes and for developing strategies for prevention and treatment of cancer. We have been investigating enzyme alterations occurring during rat chemical hepatocarcinogenesis, especially to find more specific enzyme markers for preneoplastic hepatic lesions. We identified the placental form of glutathione S-transferese (GST-P ; GST 7-7) as a new marker enzyme for preneoplastic hepatocytes. We also found human placental form, GST-7c, to be a possible tumor marker for various human tissues except liver. In this article, their properties and possible functions are reviewed on basis of our recent investigations. A peroxisomal enzyme, enoyl CoA hydratese, in also described as a possible negative marker for rat preneoplastic hepatic foci/nodules and hepatomas induced by peroxisome proliferators.(pre)neoplastic marker ; glutathione S-transferase ; peroxisome proliferator ; enoyl CoA hydratase Chemical carcinogenesis is thought to proceed through initiation and promotion stages. During the latter, in rat hepatocarcinogenesis, preneoplastic cells such as enzyme-altered foci and hyperplastic nodules appear, which express specific marker enzymes (see a review by Sato 1989). We thought chemical carcinogenesis depends on the balance between activation and inactivation of carcinogens and have focused our investigations on drug-metabolizing enzymes, and in particular on isoenzyme alteration of glutathione S-transferase ( GST ), one of the detoxicating enzymes, in rat preneoplastic hepatic lesions.GST has multi-functions performed by multi-molecular forms (isoenzymes) (Sato 1989;Sato and Tsuchida 1991). So far, a large number of isoenzymes have been identified from many species and grouped into Class Alpha, Mu, Pi, Theta

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Monoclonal antibodies to glutathione S‐Transferase π–immunohistochemical analysis of human tissues and cancers

Kantor

Giardina

Bartolazzi³

et al. 1991

Intl Journal of Cancer

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Mouse monoclonal antibodies (MAb) have been generated against the anionic isozyme of human glutathione S-transferase (GST pi). MAb AGST I can inhibit 50-70% of GST pi enzymatic activity and reacts with a 3-dimensional epitope which includes a putative glutathione binding site on GST pi. A sandwich enzyme-immunoassay established using MAb AGST I and a polyclonal antibody displayed a sensitivity of 0.5 ng/ml. Immunohistochemical analysis of human tissues demonstrated marked increases in GST pi levels in cancers of the brain, cervix, endometrium, colon, rectum and testis and in fibro- and chondrosarcomas.

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Specific inactivation of glutathione S-transferases in Class Pi by SH-modifiers

Cited by 102 publications

References 10 publications

Polymorphism of the glutathione transferase subunit 3 in Sprague–Dawley rats involves a reactive cysteine residue

Polymorphism of the glutathione transferase subunit 3 in Sprague–Dawley rats involves a reactive cysteine residue

Specific Expression of Glutathione S-transferase Pi Forms in (Pre)neoplastic Tissues: Their Properties and Functions.

Monoclonal antibodies to glutathione S‐Transferase π–immunohistochemical analysis of human tissues and cancers

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