Abstract
Cellular detoxification of exogenous toxins, antibiotics, carcinogens, and anticancer agents involves detoxifying enzymes, such as superoxide dismutase, catalase, glutathione peroxidase, and glutathione S-transferase. Glutathione S-transferases (GST; enzymal code (EC) 2.5.1.18) compromise a group of abundant and widely distributed catalytic and binding proteins that facilitate the conjugation of glutathione (GSH) with the electrophilic center of a large spectrum of hydrophobic molecules. Multiple GST isozymes in mammalian tissues arise from dimeric combinations of a number of distinct subunits grouped into three major classes, α, µ, and π [1], GST, a π-class enzyme, has been found overexpressed in human malignant tumor tissues [2], suggesting that it may be a good tumor marker. GST is also reported to be elevated in an Adriamycin-induced multidrug resistant human breast cancer cell line (MCF-7) [3] as well as in some alkylating agent resistant cell lines [4]. Despite these reports indicating GST to possibly have a critical role in carcinogenesis and anticancer drug resistance, little is known of the role of GST in brain tumors. We report the GST activities of human brain tumors, C6 rat glioma cells, and drug resistant cells.
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References
Mannervik B, Alin P, Guthenberg C (1985) Identification of three classes of cytosolic glutathione transferase common to several mammalian species: Correlation between structural data and enzymatic properties. Proc Natl Acad Sci USA 82: 7292–7206
Niitsu Y, Takahasi Y, Saito T (1989) Serum glutathione S-transferase-rc as a tumor marker for gastrointestinal malignancies. Cancer 63: 317–323
Sinha BK, Katki AG, Batist G (1987) Differential formation of hydroxyl radicals by Adriamycin in sensitive and resistant MCF-7 human breast tumor cells: Implications for the mechanism of action. Biochemistry 26: 3776–3781
Margie L, Kenneth D (1987) Identification of a glutathione S-transferase associated with microsomes of tumor cells resistant to nitrogen mustards. Biochem Pharmacol 38: 1915–1921
Sasaoka N (1990) Chemosensitivity assays for malignant gliomas (in Japanese). Gan To Kagaku Ryoho (Jpn J Cancer Chemotherap) 17: 2247–2252
Habig W, Pabst M, Jakoby W (1974) Glutathione S-transferases. J Biol Chem 249: 7130–7139
Kudo H, Mio T, Kokunai T (1990) Quantitative analysis of glutathione in human brain tumors. J Neurosurg 72: 610–615
Russo A, Carmichael J, Friedman N, DeGraff W (1986) The role of intracellular glutathione in antineoplastic chemotherapy. Int J Radiat Oncol Biol Phys 12: 1347–1354
Lewis AD, Hickson ID, Robson CN (1988) Amplification and increased expression of alpha class glutathione S-transferase encoding genes associated with resistance to nitrogen mustard. Proc Natl Acad Sci USA 85: 8511–8515
Buller AL, Clapper ML, Tew KD (1987) Glutathione S-transferases in nitrogen mustard-resistant and -sensitive cell lines. Mol Phamacol 31: 575–578
Evans CG, Bodell WJ, Tokuda K (1987) Glutathione and related enzymes in rat brain tumor cell resistance to l,3-bis(2-chloroethyl)-l-nitrosourea and nitrogen mustard. Cancer Res 47: 2525–2530
Smith MT, Evance CG, Mannervik B (1989) Denitrosation of l,3-bis(2- chloroethyl)-l-nitrosourea by class mu glutathione transferase and its role in cellular resistance in rat brain tumor cells. Cancer Res 49: 2621–2625
Pearce HL, Safa AR, Bach NJ (1989) Essential features of the P-glycoprotein pharmacophore as defined by a series of reserpine analogs that modulate multidrug resistance. Proc Natl Acad Sci USA 86: 5128–5132
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© 1991 Springer-Verlag Tokyo
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Matsumoto, Y., Sasaoka, N., Tsuchida, T., Fujiwara, T., Ohmoto, T. (1991). Quantitative Analysis of Glutathione S-Transferase in Human Brain Tumors, C6 Rat Glioma Cells, and Drug Resistant C6 Cells. In: Tabuchi, K. (eds) Biological Aspects of Brain Tumors. Springer, Tokyo. https://doi.org/10.1007/978-4-431-68150-2_36
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DOI: https://doi.org/10.1007/978-4-431-68150-2_36
Publisher Name: Springer, Tokyo
Print ISBN: 978-4-431-68152-6
Online ISBN: 978-4-431-68150-2
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