Difference in the effects of phenobarbital and 3-methylcholanthrene treatment on subunit composition of hepatic glutathione<i>S</i>-transferase in male and female rats

Isobe, Takashi; Irokawa, Nobuo; Ono, Shoichiro; Ohmori, Shigeru; Ueno, Koichi; Kitagawa, Haruo; Satoh, Tetsuo

doi:10.3109/00498258709043923

Cited by 54 publications

(15 citation statements)

References 26 publications

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“…On adding GSTs 1 and 1', the class-Alpha GSTs constituted 54-56% of the GSTs in female rat livers. These results are consistent with the finding of Igarashi et al [34] that liver class-Mu proteins are more abundant in male compared with female rats, while the GST 2 level is higher in females.…”

Section: Discussionsupporting

confidence: 93%

Mass spectrometric analysis of rat liver cytosolic glutathione S-transferases: modifications are limited to N-terminal processing

Yeh

Hsieh

Wang

et al. 1995

Biochemical Journal

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Cytosolic glutathione S-transferases (GSTs) from rat livers were purified using an S-hexylglutathione affinity column. The GST subunits were resolved by reverse-phase HPLC and their molecular masses were determined by electrospray mass spectrometry. The major hepatic GSTs detected were subunits 1, 1′, 2, 3 and 4, with molecular mass of 25,520, 25,473, 25,188, 25,782 and 25,571 Da respectively. Subunits 6, 7 and 10 are minor components, with molecular mass of 25,551, 23,308 and 25,211 Da respectively. Alternatively, the hepatic GSTs were purified using a glutathione affinity column. Subunits 1, 1′, 2, 8 and 10 were eluted from this column with GSSG, the oxidized form of glutathione. Subunit 8 has a molecular mass of 25,553 Da. The remaining proteins on the glutathione affinity column were removed with glutathione and S-hexylglutathione. Subunits 2, 3, 4 and 6 could be detected in the eluate. We could not detect any significant difference in molecular mass between GSTs isolated from male and female rat livers. Cytosolic GSTs were isolated from livers of buthionine sulphoximine-treated female rats for MS analysis. The molecular masses obtained were identical to those determined for the controls.

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Section: Discussionsupporting

confidence: 93%

Mass spectrometric analysis of rat liver cytosolic glutathione S-transferases: modifications are limited to N-terminal processing

Yeh

Hsieh

Wang

et al. 1995

Biochemical Journal

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“…The overall magnitude of the effect of each of the inducers, studied in terms of total amount of GST protein, is in accord with reports of the increases in GST activity induced respectively, by EQ (Benson et al, 1978;Kensler et al, 1985Kensler et al, , 1986, by PB (Igarishi et al, 1987;Vos et al, 1988;Di Simplicio et al, 1989) and by ,-NF (McLellan et al, 1991), notwithstanding the range of different experimental conditions represented in those papers.…”

Section: Constitutive Expression Of Gst Subunits In Becsupporting

confidence: 87%

Constitutive and inducible profile of glutathione S-transferase subunits in biliary epithelial cells and hepatocytes isolated from rat liver

Parola

Biocca

Leonarduzzi

et al. 1993

Biochemical Journal

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The constitutive and inducible cytosolic glutathione S-transferase (EC 2.5.1.18) subunit compositions of parenchymal cells (hepatocytes) and biliary epithelial cells (BEC) from rat liver have been quantitatively analysed using reverse-phase h.p.l.c. Hepatocytes, analysed in the absence of non-parenchymal cells, expressed constitutively the following subunits, in order of their concentration: 3, 4, 2, 1a, 1b, 8, 6 and 10. BEC express constitutively only four of the GST subunits expressed by hepatocytes and these are, in order of their concentration: subunits 2, 7, 4 and 3. Notable differences from hepatocytes are that BEC completely lack the Alpha-class subunits 1a and 1b that are major subunits in hepatocytes, Mu-class subunits make up a very low proportion of the total, and the Pi-class subunit 7 is a major subunit in BEC, whereas it is essentially absent from hepatocytes. For the first time, the effects of the inducing agents phenobarbitone (PB), beta-naphthoflavone (beta-NF) and ethoxyquin (EQ) have been characterized in a comprehensive and quantitative manner in both cell types. PB, beta-NF and EQ increased total GST protein in hepatocytes by approx. 2-fold, 3-fold and 4-fold respectively. Subunits significantly induced in hepatocytes were (in order of fold-induction): by PB, 1b > 8 > 3 > 2 > 4; by beta-NF, 1b > 8 > 2 > 3 > 4; and by EQ, 7 > 1b > 10 > 8 > 3 > 2 > 1a > 4. In BEC, neither PB nor beta-NF had significant effects on the total amount of GST protein, although PB did significantly induce subunit 3 at the expense of other subunits. EQ increased total GST protein nearly 5-fold in BEC, subunits 7 and 3 being induced dramatically above constitutive levels.

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“…This similarity may also be apparent in bilirubin binding as a nonsubstrate ligand by GSTA and GSTM classes in the hepatocyte [7,13].…”

Section: Discussionmentioning

confidence: 88%

Are glutathione S-transferase gene polymorphisms linked to neonatal jaundice?

et al. 2007

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Glutathione S-transferases (GSTs) are a major group of phase II detoxification enzymes involved in the metabolism of both endogenous and xenobiotic compounds. In addition to their catalytic function in detoxification, GSTs participate in binding to nonsubstrate ligands such as bilirubin. Ligandin, which is one of the principal hepatic-binding proteins, is also a member of the GST family. The aim of the present study was to investigate the possible relationship between neonatal jaundice and the GST gene polymorphisms. The study cohort consisted of a patient group of 116 newborns (plasma bilirubin levels > or = 15 mg/dl) and a control group of 54 newborns (plasma bilirubin levels <13 mg/dl). In the patient group, the null genotype frequencies in GSTM1 and GSTT1 were 52.6 and 19%, respectively; in the control group, these were 63 and 27.8%, respectively. The frequencies of GSTM1 and GSTT1 were similar in the patient and control groups (p > 0.05). Total bilirubin levels were found to be significantly higher in patients with the GSTM1 null genotype than in patients with the GSTM1 wild genotype (p = 0.042). There was no statistically significant difference in total bilirubin levels between patients with the null GSTT1 genotype and those with the wild GSTT1 genotype. It is conceivable that there is a relation between GSTM1 gene polymorphism and total bilirubin levels in neonatal jaundice. We suggest that GSTM1 gene polymorphisms may affect ligandin functions in hepatocytes, which are important in bilirubin transportation. Consequently, patients with the GSTM1 null genotype may have higher total levels of bilirubin.

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Difference in the effects of phenobarbital and 3-methylcholanthrene treatment on subunit composition of hepatic glutathioneS-transferase in male and female rats

Cited by 54 publications

References 26 publications

Mass spectrometric analysis of rat liver cytosolic glutathione S-transferases: modifications are limited to N-terminal processing

Mass spectrometric analysis of rat liver cytosolic glutathione S-transferases: modifications are limited to N-terminal processing

Constitutive and inducible profile of glutathione S-transferase subunits in biliary epithelial cells and hepatocytes isolated from rat liver

Are glutathione S-transferase gene polymorphisms linked to neonatal jaundice?

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