Glutathione transferases in primary rat hepatomas: the isolation of a form with GSH peroxidase activity

Meyer, David J.; Beale, Denis; Tan, K. Hong; Coles, Brian; Ketterer, Brian

doi:10.1016/0014-5793(85)80670-0

Cited by 121 publications

(66 citation statements)

References 8 publications

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“…The finding that in culture [32], as well as in preneoplastic nodules [33] the appearance of GST 7 is correlated with expression of oneogenes, suggests this may be an underlying factor. Secondly, the question a~ises as to whether some relation exists between the de novo expression of subunit 7 and its high peroxidase activity [34], especially since it has been found that DMSO, being a free radical scavenger, inhibits its expression. Sato [35] suggested that the expression of GST rt may be related to the prevention of lipid peroxidation since this latter orocess has been considered to play an important role during tumor promotion.…”

Section: Discussionmentioning

confidence: 99%

Transcriptional‐ and post‐transcriptional‐dependent regulation of glutathione S‐transferase expression in rat hepatocytes as a function of culture conditions

et al. 1992

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Transcriptional activity of the glutathlone S-transfemse (GST) ~t (subumt~ 1 and 2),/~ (.~ubunit~ 3 and 4) :rod rt (~ubumt 7) gent fam~hes has been analyzed u~mg the nuclear "run-on' technique on adult rat hepatoeyte~ ,naintained for 4 days m convenuonal culture and for 4 and 12 days in co-culture with rat liver epithehal cells. Several medium conditions are included m tlus utudy, namely with or without fetal calf ~rum and with meotmamide or dlmethylnulphoxlde. Hepatocyte~ co-cultured for 4 days maintain approximatdy 30-70% of the a t~ene family transcriptional acuvity, whatever the medium conditions, when compared to freshly isolated hepatocytes. A marked decrease is observed after 12 days ofeo-culture or when hepatoeytes are maintained in convenuonal culture. The tmn~npuonal activity of the/~ gene family is saammiugd at 40-160% when hepatocytes are cultured with or without fetal calf serum, and is inducible by nicotinamidc (approximately 4-fold) and d:meth]llsulphoxlde (approximately 2-fold) m conventional culture and/or in co-culture. In contrast to freshly ~solated hepatocyte.% GST ~ gene transcriptional activity is observed in eouventLonal and go-cultured hepatoeytes, trrespeetive of the medium conditions. Dlmcthylsulphoxidc treatment however, represses the expression of GST 7 in vitro. These rehultn demonbtrate that the expression of GST 0~,/~ and rt genes m conventional and eo.eultured rat hepatoeytgs is controlled primarily at the level of transerq)tion. It cannot be excluded, however, that dimethylsulphoxide ntablllze~ the GST mRNA levels m vitro,

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Section: Discussionmentioning

confidence: 99%

Transcriptional‐ and post‐transcriptional‐dependent regulation of glutathione S‐transferase expression in rat hepatocytes as a function of culture conditions

et al. 1992

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“…Rat GSH transferases 1-1, 2-2, 3-3, 4-4 and 7-7 were purified by the procedures of Beale et al (1983) andMeyer et al (1985). GSH transferase 6-6 was purified from rat testis by a modification of the method of Beale et al (1983) in which a fraction ofisoelectric point pH 5.8 was further purified on hydroxyapatite.…”

Section: Materials and Methods Purified Enzymesmentioning

confidence: 99%

The separation of glutathione transferase subunits by using reverse-phase high-pressure liquid chromatography

Farrants

Meyer

Coles

et al. 1987

Biochemical Journal

177

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A simple method is described for the separation and quantification of the subunits of GSH transferases present in rat tissue extracts. This method, involving GSH-agarose affinity chromatography followed by reverse-phase h.p.l.c., is rapid and sufficiently sensitive to measure 5 micrograms of each subunit in a mixture. Examples are given of its application to extracts of rat kidney, adrenal, testicular interstitial cells and seminiferous tubules. The analysis of seminiferous tubules indicates that the technique may be of value for the identification of novel subunits. Preliminary separations of subunits from human GSH transferases are also described.

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“…GSH peroxidase.activity Data for Lin OOH, HO-nonenal and BPDE are from [9], [171 and [19] respectively; n.d., not determined was assayed [12] using 0.5 mM Thy" OOH and GSH transferase activities were measured according to [13]. GSH transferase isoenzymes were isolated from rat liver, kidney and testis according to [14][15][16]. Se-dependent and Se-independent GSH peroxidase activities in rat liver soluble supernatant fraction were separated by chromatography on Sephadex G-100.…”

Section: Methodsmentioning

confidence: 99%

Thymine hydroperoxide, a substrate for rat Se‐dependent glutathione peroxidase and glutathione transferase isoenzymes

et al. 1986

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The thymine hydroperoxide, 5‐hydroperoxymethyluracil, is a substrate for Se‐dependent glutathione (GSH) peroxidase and the Se‐independent GSH peroxidase activity associated with the GSH transferase fraction. These enzymes may contribute to repair mechanisms for damage caused by oxygen radicals. GSH transferases 1‐1, 2‐2, 3‐3, 4‐4, 6‐6 and 7‐7 [(1984) Biochem. Pharmacol. 33, 2539–2540] are shown to differ considerably in their ability to utilize this substrate. For example, high activity is found in GSH transferase 6‐6 which is the major isoenzyme in spermatogenic tubules where DNA synthesis is so active and faithful DNA replication so important. The activity of the purified GSH transferase isoenzymes towards 5‐hydroperoxymethyluracil is comparable with their activity towards other endogenous substrates related to cellular peroxidation such as linoleate hydroperoxide and 4‐hydroxynon‐2‐enal or biologically important xenobiotic metabolites such as benzo(a)pyrene‐7,8‐diol‐9,10‐oxide.

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Glutathione transferases in primary rat hepatomas: the isolation of a form with GSH peroxidase activity

Cited by 121 publications

References 8 publications

Transcriptional‐ and post‐transcriptional‐dependent regulation of glutathione S‐transferase expression in rat hepatocytes as a function of culture conditions

Transcriptional‐ and post‐transcriptional‐dependent regulation of glutathione S‐transferase expression in rat hepatocytes as a function of culture conditions

The separation of glutathione transferase subunits by using reverse-phase high-pressure liquid chromatography

Thymine hydroperoxide, a substrate for rat Se‐dependent glutathione peroxidase and glutathione transferase isoenzymes

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