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Identification of thetrans-stilbene oxide-active glutathione transferase in human mononuclear leukocytes and in liver as GST1

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Abstract

A glutathione transferase from human mononuclear leukocytes with a high activity towardtrans-stilbene oxide (GT-tSBO) has been studied in liver and blood from fetus and adults and in blood from neonates. Using starch gel electrophoresis, different phenotypes of GST1 have been determined, GST1 0, GST1 1, and GST1 2. As judged from activity measurements and the fact that only those individuals who express the null allele of GST1, the GST1 0, which has a low activity towardtrans-stilbene oxide, it is concluded that the hepatic transferase GST1 is identical to GT-tSBO, as well as to hepatic transferase μ. In addition, it has been shown that the different genotypes of GST1 1 (GST1 1-1, GST1 1-0) and GST1 2 (GST1 2-2, GST1 2-0) can be separated by measuring the GT-tSBO activity in whole blood from the same individual. It is also demonstrated that GT-tSBO activity is much lower in fetal liver, approximately 10 times, compared with adult liver, while this activity seems to be unchanged in the blood from fetus and adults, as well as in neonates.

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References

  • Awasthi, Y. C., Dao, D. D., and Saneto, R. P. (1980). Interrelationship between anionic and cationic forms of glutathione S-transferases of human liver.Biochem. J. 1911.

    Google Scholar 

  • Board, P. G. (1980). A method for the localization of glutathione S-transferase isozymes after starch gel electrophoresis.Anal. Biochem. 105147.

    Google Scholar 

  • Board, P. G. (1981). Biochemical genetics of glutathione S-transferase in man.Am. J. Hum. Genet. 3336.

    Google Scholar 

  • Board, P. G., Suzuki, T., and Shaw, D. C. (1988). Human muscle glutathione S-transferase (GST-4) shows close homology to human liver GST-1.Biochim. Biophys. Acta 953214.

    Google Scholar 

  • De Pierre, J. W., Seidegård, J., Morgenstern, R., Balk, L., Meijer, J., Åström, J., Norelius, I., and Ernster, L. (1984). Induction of cytosolic glutathione transferase and microsomal epoxide hydrolase activities in extrahepatic organs of the rat by phenobarbital, 3-methylcholanthrene andtrans-stilbene oxide.Xenobiotica 14295.

    Google Scholar 

  • Faulder, C. G., Hirrell, P. A., Hume, R., and Strange, R. C. (1987). Studies of the development of basic, neutral and acidic isoenzymes of glutathione S-transferase in human liver, adrenal, kidney and spleen.Biochem. J. 241221.

    Google Scholar 

  • Gill, S., Ota, K., and Hammock, B. D. (1983). Radiometric assay for mammalian epoxide hydrolase and glutathione S-transferase.Anal. Biochem. 131273.

    Google Scholar 

  • Habig, W. H., Pabst, M. J., and Jakoby, W. B. (1974). Glutathione S-transferases: The first enzymatic step in mercapturic acid formation.J. Biol. Chem. 2497130.

    Google Scholar 

  • Harada, S., Abai, M., Tanaka, N., Agarwal, D., and Goedde, H. W. (1987). Liver glutathione S-transferase polymorphism in Japanese and its pharmacogenetic importance.Hum. Genet. 75322.

    Google Scholar 

  • Jakoby, W. B., and Habig, W. H. (1980). Glutathione transferases. In Jacoby, W. B. (ed.),Enzymatic Basis of Detoxication, Vol. 2 Academic Press, New York, p. 63.

    Google Scholar 

  • Laisney, V., Van Cong, N., Gross, M. S., and Frezal, J. (1984). Human genes for glutathione S-transferases.Hum. Genet. 68221.

    Google Scholar 

  • Mannervik, B. (1985). The isoenzymes of glutathione transferase.Adv. Enzymol. Relat. Areas Mol. Biol. 57357.

    Google Scholar 

  • Mannervik, B., Ålin, P., Guthenberg, C., Jensson, H., Tahir, M. K., Warholm, M., and Jörnvall, H. (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 827202.

    Google Scholar 

  • Seidegård, J., and Pero, R. W. (1985). The hereditary transmission of high glutathione transferase activity towardstrans-stilbene oxide in human mononuclear leukocytes.Hum. Genet. 6966.

    Google Scholar 

  • Seidegård, J., DePierre, J. W., Birberg, W., Pilotti, Å., and Pero, R. W. (1984). Characterization of soluble glutathione transferase activity in resting mononuclear leukocytes from human blood.Biochem. Pharmacol. 333053.

    Google Scholar 

  • Seidegård, J., DePierre, J. W., and Pero, R. W. (1985). Hereditary interindividual differences in the glutathione transferase activity towardstrans-stilbene oxide in resting human mononuclear cells are due to a particular isozyme(s).Carcinogenesis 61211.

    Google Scholar 

  • Seidegård, J., Pero, R. W., Miller, D. G., and Beattie, E. J. (1986). A glutathione transferase in human leukocytes as a marker for the susceptibility to lung cancer.Carcinogenesis 7751.

    Google Scholar 

  • Seidegård, J., Guthenberg, C., Pero, R. W., and Mannervik, B. (1987a). The trans-stilbene oxide active glutathione transferase in human mononuclear leukocytes is identical with the hepatic glutathione transferase μ.Biochem. J. 246783.

    Google Scholar 

  • Seidegård, J., Pero, R. W., Jonsson, G. G., Olsson, S.-Å., Stavenow, L., and Aronsen, K.-F. (1987b). A human isozyme of glutathione transferase activity in different organs and its relation to lung cancer. In Benford, B., Bridges, J. W., and Gibson, G. G. (eds.),Drug Metabolism—from Molecules to Man Taylor and Francis, London, p. 106.

    Google Scholar 

  • Seidegård, J., Pero, R. W., and Pearson, W. R. (1988). Hereditary differences in human glutathione transferase GT-tSBO expression are due to a gene deletion.Proc. Natl. Acad. Sci. 857293.

    Google Scholar 

  • Singh, S. V., Kurosky, A., and Awasthi, Y. C. (1987). Human liver glutathione S-transferase ω. Chemical characterization and secondary-structure comparison with other mammalian glutathione transferases.Biochem. J. 24361.

    Google Scholar 

  • Strange, R. C., Faulder, C. G., David, B. A., Hume, R., Brown, J. A. H., Cotton, W., and Hopkinson, D. A. (1984). The human glutathione S-transferases. Studies on the tissue distribution and genetic variation of the GST1, GST2, and GST3 isozymes.Ann. Hum. Genet. 4811.

    Google Scholar 

  • Strange, R. C., Davis, B. A., Faulder, C. G., Cotton, W., Bain, A. D., Hopkinson, D. A., and Hume, R. (1985). The human glutathione S-transferases: Development aspects of the GST1, GST2, and GST3 loci.Biochem. Genet. 231011.

    Google Scholar 

  • Suzuki, T., Coggan, M., Shaw, D. C., and Board, P. G. (1987). Electrophoretic and immunological analysis of human glutathione S-transferase isoenzymes.Ann. Hum. Genet. 5195.

    Google Scholar 

  • Vander Jagt, D. L., Hunsaker, L. A., Garcia, K. B., and Royer, R. E. (1985). Isolation and characterization of the multiple glutathione S-transferases from human liver.J. Biol. Chem. 26011603.

    Google Scholar 

  • Warholm, M., Guthenberg, C., and Mannervik, B. (1983). Molecular and catalytic properties of glutathione transferase μ from human liver: An enzyme efficiently conjugating epoxides.Biochemistry 223610.

    Google Scholar 

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This study was supported by Svenska Tobaks AB, Grant 8617, Magnus Bergvalls Stiftelse, Marcus Borgströms fond, Greta och Johan Kocks Stiftelse, John och Augusta Perssons Stiftelse för vetenskaplig medicinsk forskning, och Direktör Albert Påhlssons stiftelse för forskning och välgörenhet.

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Seidegård, J., Pero, R.W. & Stille, B. Identification of thetrans-stilbene oxide-active glutathione transferase in human mononuclear leukocytes and in liver as GST1. Biochem Genet 27, 253–261 (1989). https://doi.org/10.1007/PL00020159

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  • DOI: https://doi.org/10.1007/PL00020159

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