Genetic heterogeneity of the human glutathione transfereses: A complex of gene families

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Abstract

The glutathione transferases (GSTs) are involved in the metabolism of a wide range of compounds of both exogenous and endogenous origin. There is evidence that deficiency of GST may increase sensitivity to certain environmentally derived carcinogens. In contrast, elevated expressoin has been implicated in resistance to therapeutic drugs. The GSTs are the products fo a several gene families. This review summarized the present knowledge of the genetic onterrelationships between the various isoenzymes, their deficiences and the physical locations of their genes.

References (88)

  • J.W. Harvey et al.

    Binding of heme by glutathione S-transferase: a possible role for the erythrocyte enzyme

    Blood

    (1982)
  • H. Jensson et al.

    Rat glutathione transferases 8-8, an enzyme efficiently detoxifying 4-hydroxyalk-2-enals

    FEBS Lett.

    (1986)
  • C.J. Marcus et al.

    Glutathione transferase form human erythrocytes. Non-identity with the enzymes from liver

    Archs Biochem. Biophys.

    (1978)
  • R. Morgenstern et al.

    Microsomal glutathione transferase: primary structure

    J. biol. Chem.

    (1985)
  • C.S. Morrow et al.

    Structure of the human genomic glutathione S-transferase-π gene

    Gene

    (1989)
  • K. Nakagawa et al.

    Glutathione S-transferase π as a determinant of drug resistance in transfectant cell lines

    J. biol. Chem.

    (1990)
  • D.M. Rhoads et al.

    The basic glutathione S-transferase from human livers are products of separate genes

    Biochem. biophys. Res. Commun.

    (1987)
  • J. Seidegard et al.

    Characterization of soluble glutathione transferase activity in ersting mononuclear leukocytes form human blood

    Biochem. Pharmac.

    (1984)
  • P.C. Simons et al.

    Bilirubin binding to human liver ligandin (glutathione S-transferase)

    J. biol. Chem.

    (1980)
  • S.V. Singh et al.

    Purification of unique glutathione S-transferases form human muscle

    Archs Biochem. Biophys.

    (1988)
  • Y. Soma et al.

    Purification and subunit-structural and immunological characterization of five glutathione transfereses in human liver and the acidic form as a hepatic tumour marker

    Biochem. biophys. Acta

    (1986)
  • S. Tsuchida et al.

    Sato K.

    Purification and characterization of glutathione transferases with an activity towards nitroglycerin from human aorta and heart. Multiplicity of human class mu forms

    J. biol. Chem.

    (1990)
  • C.-P.D. Tu et al.

    Human liver glutathione S-transferases: complete primary structure of an Ha subunit cDNA

    Biochem. biophys. Res. Commun.

    (1986)
  • C.-P.D. Tu et al.

    Immunological and sequence interrelationshiops between multiple human liver and rat glutathione transferases

    J. biol. Chem.

    (1986)
  • D.L. Vander Jagt et al.

    Isolation and characterization of the multiple glutathione S-transferases from human liver

    J. biol. Chem.

    (1985)
  • Y. Adachi et al.

    Partial defect in hepatic glutathione S-transferase activity in a case of Rotor's syndrome

    Gastroent. jap.

    (1987)
  • K. Akiyama et al.

    The gene frequencies of glutathione S-transferase isoenzymes in Japanese population

    Jap. J. hum. Genet.

    (1984)
  • e. Beutler et al.

    Erythrocyte glutathione synthetase deficiency leads not only to glutathione but also glutathione S-transferase deficiency

    J. clin. Invest.

    (1986)
  • P.G. Board

    Biochemical genetics of glutathione S-transferase in man

    Am. J. hum. Genet.

    (1981)
  • P.G. Board et al.

    Expression of human glutathione S-transferase 2 in Escherichia coli. Immunological comparison with the basic glutathione S-transferase isoenzymes from human liver

    Biochem. J.

    (1987)
  • P.G. Board et al.

    Isolation of a cDNA clone and localization of glutathione S-transferase 2 genes to chromosome band 6p12

  • P.G. Board et al.

    Isolation of a cDNA clone and localization of the human glutathione S-transferase 3 genes to bhromosome bands 11q13 and 12q13–14

    Ann. hum. Genet.

    (1989)
  • J. Booth et al.

    An enzyme form rat liver catalysin gconjugations with glutathione

    Biochem. J.

    (1961)
  • P.S. Bora et al.

    Metabolism of ethanol and carcinogens by glutathione transferases

  • E. Boyland et al.

    The role of glutathione and glutathione S-transferases in mercapturic acid biosynthesis

  • A.l. Buller et al.

    Glutathione S-transferase in nitrogen mustard-resistant and sensitive cell lines

    Molec. Pharmac.

    (1987)
  • I.G. Cowell et al.

    The structure of the human glutathione S-transferase π gene

    Biochem. J.

    (1988)
  • B. Dahlöf et al.

    Characterization of multidrug resistance in SEWA mouse tumor cells: increased glutatione transferase activity and reversal of resistance with verapamil

    Anticancer Res.

    (1987)
  • J.L. De Jong et al.

    The human liver glutathione S-transferase gene superfamily: expression and chromosome mapping of an Hb subunit cDNA

    Nucl. Acids Res.

    (1988)
  • G. Del Boccio et al.

    Identification of a novel glutathione transferase in human skin homologous with class alpha glutathione transferase 2-2 in the rat

    Biochem. J.

    (1987)
  • C. Di Ilio et al.

    Purification and characterization of five forms of glutathione transferase form human uterus

    Eur. J. Biochem.

    (1988)
  • C. Guthenberg et al.

    Purification of glutathione S-transferase from human placenta

    Acta chem. scand. Ser. B

    (1979)
  • W.H. Habig et al.

    The identity of glutathione S-transferase B with ligandin, a major binding protein of liver

  • S. Harada et al.

    Liver glutathione S-transferase polymorphism in Japanese and its pharmacogenetic importance

    Hum. Genet.

    (1987)
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