Possible Involvement of Glutathione <i>S</i>‐Transferases in the Cell Growth of C6 Astroglioma Cells

Senjo, Masanori; Ishibashi, Teruo

doi:10.1111/j.1471-4159.1988.tb13244.x

Cited by 11 publications

(3 citation statements)

References 18 publications

(7 reference statements)

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“…Appearance of GST-n is being employed as a marker protein in hepatocarcinogenesis [7], meningiomas [8], renal carcinoma [9], lung carcinoma [10] and gastric tumors [11]. In rat CNS, GSTs are localized exclusively in the astrocytes and ependymal cells, but not in the neurons and oligodendrocytes [12], while in mouse GST-rc occurs in myelin sheaths of the neuron and oligodendrocytes [13]. Sato [14] suggested a role for GST-n class of isozyme in detoxification of antineoplastic drugs and used as a biomarker to grade the gliomas.…”

Section: Introductionmentioning

confidence: 99%

Inhibition of cell proliferation and glutathione S-transferase by ascorbyl esters and interferon in mouse glioma

et al. 1993

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Mouse glioma-26 (G-26) cell line established in this laboratory was used in the study. The in vitro effect of ascorbyl esters, viz., ascorbyl-palmitate (As-P), -stearate (As-S) and mouse interferon-alpha/beta (MulFN-alpha/beta) on the glioma cell viability, proliferation and glutathione S-transferase (GST) activity was investigated. Cell viability and proliferation were examined by colorimetric MTT assay and [3H]-thymidine incorporation, respectively. Incubation (24h) of G-26 cells with As-S, As-P or MulFN-alpha/beta, resulted in a dose dependent decrease in cell viability (IC50 = 125 microM As-S; 175 microM As-P and 3.6 x 10(4) U/ml MulFN-alpha/beta) and proliferation (IC50 = 157 microM As-S; 185 microM As-P and 3.6 x 10(4) U/ml MulFN-alpha/beta). A combined exposure to 175 microM As-S and 800 U/ml of MulFN-alpha/beta resulted in a greater than an additive effect on cell viability and proliferation. The inhibition of cell proliferation/viability by interferon was species specific and was observed only with homologous MulFN-alpha/beta, but not with human interferon-alpha lymphoblastoid or human interferon-beta. Ascorbyl esters inhibited cytosolic GST activity (1-50 = 15.0 microM As-S and 28.5 microM As-P) towards 1-chloro-2,4-dinitrobenzene in a dose dependent manner. The apparent Ki values for affinity purified GST, deduced from Dixon plots were 0.95 microM and 2.0 microM for As-S and As-P, respectively. Significant inhibition of GST was also observed in the cytosol isolated from G-26 cells exposed to 300 microM As-S or 800 U/ml MulFN-alpha/beta.

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Section: Introductionmentioning

confidence: 99%

Inhibition of cell proliferation and glutathione S-transferase by ascorbyl esters and interferon in mouse glioma

et al. 1993

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“…GSTs are composed of a family of isoenzymes which are widely distributed in animal tissues (Mannervik, 1985). Their physiological function may be involved in the detoxification of xenobiotics (Jakoby, 1978;Berhane & Mannervik, 1990), synthesis of leukotriene C4 (Samuelsson, 1982), transport of haem (Havery & Beutler, 1982) and bilirubin (Kamisaka et al, 1975), and possibly in cell proliferation (Senjo & Ishibashi, 1988). Elevation of intracellular GST activities is frequently associated with acquired resistance to certain anti-cancer drugs (Batist et al, 1986;Robson et al, 1987;Lewis et al, 1988;Wang et al, 1989;Gupta et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

Glutathione S-transferase π in an arsenic-resistant Chinese hamster ovary cell line

Wang

Tam

et al. 1992

Biochemical Journal

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A glutathione S-transferase (GST) was purified from an arsenic-resistant Chinese hamster ovary cell line, SA7. The SA7 GST was shown to catalyse the conjugation of glutathione and ethacrynic acid, a specific substrate for Pi class GST. Its N-terminal amino-acid sequence has 80% identical residues to that of rat GST P and human GST pi. Thus, the GST purified from SA7 cells belongs to the Pi family. Treatment with Cibacron Blue or ethacrynic acid, which are GST inhibitors, significantly decreased the resistance of SA7 cells to sodium arsenite. On the other hand, pretreatment of SA7N cells, a partial revertant of SA7 cells, with sublethal doses of sodium arsenite, cadmium acetate or zinc sulphate resulted in re-elevation of GST activities and the cells regained the arsenic resistance. The regained arsenic resistance was well correlated with the levels of GST pi which were induced dose-dependently by zinc sulphate. Heat-shock treatment (45 degrees C for 10 min) did not increase GST pi expression or arsenic resistance of SA7N cells. The results indicate that GST pi is possibly involved in the mechanism of arsenic detoxification.

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“…The patterns of GST isoenzymes expressed in different tissues [56], in different cell types in the same tissue [57], and even during different phases of the cell cycle of one and the same cell [58] can differ considerably. Furthermore, the expressions of different GSTs in many different tissues have been shown to vary during development and aging [18,19,[59][60][61].…”

Section: Discussionmentioning

confidence: 99%

Growth hormone- and testosterone-dependent regulation of glutathione transferase subunit A5 in rat liver

Staffas

Ellis

Hayes

et al. 1998

Biochemical Journal

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The class Alpha glutathione S-transferase (GST) subunit A5 is expressed in the livers of young male and female rats. After sexual maturation, this protein is no longer detectable in the livers of male rats, but is still expressed in female rats. We have previously demonstrated that the sexually dimorphic secretion of growth hormone regulates the levels of certain class Mu GSTs in rat liver, and this study was designed to investigate the hormonal regulation of GSTA5. Control and hypophysectomized rats of both sexes were used to study the role of growth hormone in the regulation of hepatic GSTA5; and the influence of testosterone on the expression of this same subunit was investigated in intact females and castrated males. Liver cytosols were subjected to SDS/PAGE and immunoblotting using antibodies directed towards rat (r)GSTA5, and to affinity purification on glutathione-Sepharose followed by reverse-phase HPLC in order to quantify the relative levels of rGSTA1, A2, A3, A4, M1 and M2 subunits. These analyses revealed that the expression of rGSTA5 is, indeed, regulated by both growth hormone and testosterone.

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Possible Involvement of Glutathione S‐Transferases in the Cell Growth of C6 Astroglioma Cells

Cited by 11 publications

References 18 publications

Inhibition of cell proliferation and glutathione S-transferase by ascorbyl esters and interferon in mouse glioma

Inhibition of cell proliferation and glutathione S-transferase by ascorbyl esters and interferon in mouse glioma

Glutathione S-transferase π in an arsenic-resistant Chinese hamster ovary cell line

Growth hormone- and testosterone-dependent regulation of glutathione transferase subunit A5 in rat liver

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