Purification and subunit-structural and immunological characterization of five glutathione S-transferases in human liver, and the acidic form as a hepatic tumor marker

Soma, Yuko; Satoh, Keisuke; Sato, Kei

doi:10.1016/0167-4838(86)90064-6

Cited by 112 publications

(43 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The supernatants obtained by centrifugation at 105 000 g for 45 min were subjected to S-hexyl-GSH-Sepharose affinity chromatography and the GST forms were eluted with 5 mM S-hexyl-GSH, as described by Guthenberg and Mannervik [25]. GST 3-3s from SD rat and HHR were further purified by chromatofocusing (pH 10.5-7.0), as described previously [26].…”

Section: Purification Of Gsts From Rat Liversmentioning

confidence: 99%

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

Kumano

Kimura

Hayakari

et al. 2000

Biochemical Journal

View full text Add to dashboard Cite

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

show abstract

Section: Purification Of Gsts From Rat Liversmentioning

confidence: 99%

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

Kumano

Kimura

Hayakari

et al. 2000

Biochemical Journal

View full text Add to dashboard Cite

show abstract

“…Anti-GST P1-1 antibody was prepared as reported previously. 29) The blots were then probed on an ECL western blotting detection system (Amersham).…”

Section: Gsh According To the Methods Of Hissin And Hilfmentioning

confidence: 99%

Characterization of cell death induced by ethacrynic acid in a human colon cancer cell line DLD‐1 and suppression by N‐acetyl‐l‐cysteine

et al. 2003

View full text Add to dashboard Cite

Since ethacrynic acid (EA), an SH modifier as well as glutathione S-transferase (GST) inhibitor, has been suggested to induce apoptosis in some cell lines, its effects on a human colon cancer cell line DLD-1 were examined. EA enhanced cell proliferation at 20-40 µ µ µ µM, while it caused cell death at 60-100 µ µ µ µM. Caspase inhibitors did not block cell death and DNA ladder formation was not detected. Poly(ADP-ribose) polymerase, however, was cleaved into an 82-kDa fragment, different from an 85-kDa fragment that is specific for apoptosisis. The 82-kDa fragment was not recognized by antibody against PARP fragment cleaved by caspase 3. N-Acetyl-L-cysteine (NAC) completely inhibited EA-induced cell death, but 3(2)-t-butyl-4-hydroxyanisole or pyrrolidinedithiocarbamate ammonium salt did not. Glutathione (GSH) levels were dose-dependently increased in cells treated with EA and this in-

show abstract

“…Human GST P1-1 was purified from placental tissue (120 units\mg of protein) and GST A1-1 and M1-1 from liver as reported previously [22]. Rat GST-P (7-7) and mouse GST-II, both Pi-class forms, were also purified from hyperplastic nodulebearing livers and normal liver respectively, as reported previously [4,23].…”

Section: Purification Of Gst Formsmentioning

confidence: 95%

Epitope mapping of a monoclonal antibody to human glutathione transferase P1–1 the binding of which is inhibited by glutathione

Takahata

Tsuchida

Oomura³

et al. 1997

Biochemical Journal

Self Cite

View full text Add to dashboard Cite

Although the three-dimensional structure of human glutathione transferase (GST) P1-1 crystallized with a GSH analogue has been reported, its structure in the non-complexed form has not been determined. Four monoclonal antibodies to GST P1-1 were produced to facilitate structural analysis. Of these, one, clone d-1 of IgG #a isotype, dose-dependently inhibited the activity of GST P1-1 but did not affect the activities of either GST A1-1 or M1-1. On immunoblotting, the antibody reacted strongly with GST P1-1 and weakly with rat GST-P and mouse GST-II, indicating cross-reactivity with Pi-class forms but preferential reactivity with GST P1-1. When GST P1-1 and the antibody were incubated in the presence of 60 µM GSH, no inhibition of activity was found, whereas 1-chloro-2,4-dinitrobenzene had no effect at concentrations up to 10 µM. The binding of GST P1-1

show abstract

Purification and subunit-structural and immunological characterization of five glutathione S-transferases in human liver, and the acidic form as a hepatic tumor marker

Cited by 112 publications

References 27 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

Characterization of cell death induced by ethacrynic acid in a human colon cancer cell line DLD‐1 and suppression by N‐acetyl‐l‐cysteine

Epitope mapping of a monoclonal antibody to human glutathione transferase P1–1 the binding of which is inhibited by glutathione

Contact Info

Product

Resources

About