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Volumn 372, Issue 2, 2003, Pages 611-616

Polymorphic glutathione S-transferase subunit 3 of rat liver exhibits different susceptibilities to carbon tetrachloride: Differences in their interactions with heat-shock protein 90

Author keywords

Glutathiolation; Glyoxalase I; Mitogen activated protein kinase; Oxidative stress

Indexed keywords

AMINO ACIDS; GENES; HALOGEN COMPOUNDS; OXIDATION;

EID: 0038338320     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021788     Document Type: Article
Times cited : (5)

References (33)
  • 2
    • 0000107746 scopus 로고
    • Identification of three classes of cytosolic glutathione transferase common to several mammalian species: Correlation between structural data and enzymatic properties
    • 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. U.S.A. 82, 7202-7206
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 7202-7206
    • Mannervik, B.1    Ålin, P.2    Guthenberg, C.3    Jensson, H.4    Tahir, M.K.5    Warholm, M.6    Jörnvall, H.7
  • 3
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • Hayes, J. D. and Pulford, D. J. (1995) The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit. Rev. Biochem. Mol. Biol. 30, 445-600
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 6
    • 0034283556 scopus 로고    scopus 로고
    • Polymorphism of the glutathione transferase subunit 3 in Sprague-Dawley rats involves a reactive cysteine residue
    • Kumano, T., Kimura, J., Hayakari, M., Yamazaki, T., Sawamura, D. and Tsuchida, S. (2000) Polymorphism of the glutathione transferase subunit 3 in Sprague-Dawley rats involves a reactive cysteine residue. Biochem. J. 350, 405-412
    • (2000) Biochem. J. , vol.350 , pp. 405-412
    • Kumano, T.1    Kimura, J.2    Hayakari, M.3    Yamazaki, T.4    Sawamura, D.5    Tsuchida, S.6
  • 8
    • 0027433644 scopus 로고
    • Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system
    • Stancato, L. F., Chow, Y.-H., Hutchison, K. A., Perdew, G. H., Jove, R. and Pratt, W. B. (1993) Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system. J. Biol. Chem. 268, 21711-21716
    • (1993) J. Biol. Chem. , vol.268 , pp. 21711-21716
    • Stancato, L.F.1    Chow, Y.-H.2    Hutchison, K.A.3    Perdew, G.H.4    Jove, R.5    Pratt, W.B.6
  • 9
    • 0022342203 scopus 로고
    • Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein
    • Sanchez, E. R., Toft, D. O., Schlesinger, M. J. and Pratt, W. B. (1985) Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein. J. Biol. Chem. 260, 12398-12401
    • (1985) J. Biol. Chem. , vol.260 , pp. 12398-12401
    • Sanchez, E.R.1    Toft, D.O.2    Schlesinger, M.J.3    Pratt, W.B.4
  • 10
    • 0029737509 scopus 로고    scopus 로고
    • Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90
    • Blagosklonny, M. V., Toretsky, J., Bohen, S. and Neckers, L. (1996) Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90. Proc. Natl. Acad. Sci. U.S.A. 93, 8379-8383
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 8379-8383
    • Blagosklonny, M.V.1    Toretsky, J.2    Bohen, S.3    Neckers, L.4
  • 11
    • 0026669310 scopus 로고
    • The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity
    • Miyata, Y. and Yahara, I. (1992) The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity. J. Biol. Chem. 267, 7042-7047
    • (1992) J. Biol. Chem. , vol.267 , pp. 7042-7047
    • Miyata, Y.1    Yahara, I.2
  • 15
    • 0031873765 scopus 로고    scopus 로고
    • Increase of lipid hydroperoxides in liver mitochondria and inhibition of cytochrome oxidase by carbon tetrachloride intoxication in rats
    • Ikeda, K., Toda, M., Tanaka, K., Tokumaru, S. and Kojo, S. (1998) Increase of lipid hydroperoxides in liver mitochondria and inhibition of cytochrome oxidase by carbon tetrachloride intoxication in rats. Free Radic. Res. 28, 403-410
    • (1998) Free Radic. Res. , vol.28 , pp. 403-410
    • Ikeda, K.1    Toda, M.2    Tanaka, K.3    Tokumaru, S.4    Kojo, S.5
  • 16
    • 0025859931 scopus 로고
    • Intralobular heterogeneity of carbon tetrachloride-induced oxidative stress in perfused rat liver visualized by digital imaging fluorescence microscopy
    • Suematsu, M., Kato, S., Ishii, H., Asako, H., Yanagisawa, T., Suzuki, H., Oshio, C. and Tsuchiya, M. (1991) Intralobular heterogeneity of carbon tetrachloride-induced oxidative stress in perfused rat liver visualized by digital imaging fluorescence microscopy. Lab. Invest. 64, 167-173
    • (1991) Lab. Invest. , vol.64 , pp. 167-173
    • Suematsu, M.1    Kato, S.2    Ishii, H.3    Asako, H.4    Yanagisawa, T.5    Suzuki, H.6    Oshio, C.7    Tsuchiya, M.8
  • 17
    • 0017100110 scopus 로고
    • The resistance of putative premalignant liver cell populations, hyperplastic nodules, to the acute cytotoxic effects of some hepatocarcinogens
    • Farber, E., Parker, S. and Gruenstein, M. (1976) The resistance of putative premalignant liver cell populations, hyperplastic nodules, to the acute cytotoxic effects of some hepatocarcinogens. Cancer Res. 36, 3879-3887
    • (1976) Cancer Res. , vol.36 , pp. 3879-3887
    • Farber, E.1    Parker, S.2    Gruenstein, M.3
  • 18
    • 0018395676 scopus 로고
    • Purification of glutathione S-transferases from rat lung by affinity chromatography. Evidence for an enzyme form absent in rat liver
    • Guthenberg, C. and Mannervik, B. (1979) Purification of glutathione S-transferases from rat lung by affinity chromatography. Evidence for an enzyme form absent in rat liver. Biochem. Biophys. Res. Commun. 86, 1304-1310
    • (1979) Biochem. Biophys. Res. Commun. , vol.86 , pp. 1304-1310
    • Guthenberg, C.1    Mannervik, B.2
  • 19
    • 0016275313 scopus 로고
    • Glutathione S-transferases. The first enzymatic step in mercapturic acid formation
    • 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. 249, 7130-7139
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76, 4350-4354
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 22
    • 0023655586 scopus 로고
    • The separation of glutathione transferase subunits by using reverse-phase high-pressure liquid chromatography
    • Ostlund-Farrants, A.-K., Meyer, D. J., Coles, B., Southan, C., Aitken, A., Johnson, P. J. and Ketterer, B. (1987) The separation of glutathione transferase subunits by using reverse-phase high-pressure liquid chromatography. Biochem. J. 245, 423-428
    • (1987) Biochem. J. , vol.245 , pp. 423-428
    • Ostlund-Farrants, A.-K.1    Meyer, D.J.2    Coles, B.3    Southan, C.4    Aitken, A.5    Johnson, P.J.6    Ketterer, B.7
  • 23
    • 0014348411 scopus 로고
    • Selective enzyme purification by affinity chromatography
    • Cuatrecasas, P., Wilchek, M. and Anfinsen, C.B. (1968) Selective enzyme purification by affinity chromatography. Biochemistry 61, 636-643
    • (1968) Biochemistry , vol.61 , pp. 636-643
    • Cuatrecasas, P.1    Wilchek, M.2    Anfinsen, C.B.3
  • 24
    • 0030722402 scopus 로고    scopus 로고
    • Characterization of S-hexylglutathione-binding proteins of human hepatocellular carcinoma: Separation of enoyl-CoA isomerase from an Alpha class glutathione transferase form
    • Kajihara-Kano, H., Hayakari, M., Satoh, K., Tomioka, Y., Mizugaki, M. and Tsuchida, S. (1997) Characterization of S-hexylglutathione-binding proteins of human hepatocellular carcinoma: separation of enoyl-CoA isomerase from an Alpha class glutathione transferase form. Biochem. J. 328, 473-478
    • (1997) Biochem. J. , vol.328 , pp. 473-478
    • Kajihara-Kano, H.1    Hayakari, M.2    Satoh, K.3    Tomioka, Y.4    Mizugaki, M.5    Tsuchida, S.6
  • 25
    • 0023719098 scopus 로고
    • r 90,000 heat shock protein
    • r 90,000 heat shock protein. Anal. Biochem. 173, 405-411
    • (1988) Anal. Biochem. , vol.173 , pp. 405-411
    • Denis, M.1
  • 26
    • 0035918227 scopus 로고    scopus 로고
    • Glutathione S-transferase Mu modulates the stress-activated signals by suppressing apoptosis signal-regulating kinase 1
    • Cho, S.-G., Lee, Y. H., Park, H.-S., Ryoo, K., Kang, K. W., Park, J., Eom, S.-J., Kim, M. J., Chang, T.-S., Choi, S.-Y. et al. (2001) Glutathione S-transferase Mu modulates the stress-activated signals by suppressing apoptosis signal-regulating kinase 1. J. Biol. Chem. 276, 12749-12755
    • (2001) J. Biol. Chem. , vol.276 , pp. 12749-12755
    • Cho, S.-G.1    Lee, Y.H.2    Park, H.-S.3    Ryoo, K.4    Kang, K.W.5    Park, J.6    Eom, S.-J.7    Kim, M.J.8    Chang, T.-S.9    Choi, S.-Y.10
  • 27
    • 0028940309 scopus 로고
    • Transient interaction of hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo
    • Jakob, U., Lille, H., Meyer, I. and Buchner, J. (1995) Transient interaction of hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo. J. Biol. Chem. 270, 7288-7294
    • (1995) J. Biol. Chem. , vol.270 , pp. 7288-7294
    • Jakob, U.1    Lille, H.2    Meyer, I.3    Buchner, J.4
  • 28
    • 0030176306 scopus 로고    scopus 로고
    • Pharmacology of methylglyoxal: Formation, modification of proteins and nucleic acids, and enzymatic detoxification. A role in pathogenesis and antiproliferative chemotherapy
    • Thornalley, P. J. (1996) Pharmacology of methylglyoxal: formation, modification of proteins and nucleic acids, and enzymatic detoxification. A role in pathogenesis and antiproliferative chemotherapy. Gen. Pharmacol. 27, 565-573
    • (1996) Gen. Pharmacol. , vol.27 , pp. 565-573
    • Thornalley, P.J.1
  • 29
    • 0028605299 scopus 로고
    • Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with N-α-acetylarginine, N-α-acetylcysteine, and N-α-acetyllysine, and bovine serum albumin
    • Lo, T. W. C., Westwood, M. E., McLellan, A. C., Selwood, T. and Thornalley, P. J. (1994) Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with N-α-acetylarginine, N-α-acetylcysteine, and N-α-acetyllysine, and bovine serum albumin. J. Biol. Chem. 269, 32299-32305
    • (1994) J. Biol. Chem. , vol.269 , pp. 32299-32305
    • Lo, T.W.C.1    Westwood, M.E.2    McLellan, A.C.3    Selwood, T.4    Thornalley, P.J.5
  • 30
    • 0032510747 scopus 로고    scopus 로고
    • Evidence of high levels of methylglyoxal in cultured Chinese hamster ovary cells
    • Chaplen, F. W. R., Fahl, W. E. and Cameron, D. C. (1998) Evidence of high levels of methylglyoxal in cultured Chinese hamster ovary cells. Proc. Natl. Acad. Sci. U.S.A. 95, 5533-5538
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 5533-5538
    • Chaplen, F.W.R.1    Fahl, W.E.2    Cameron, D.C.3
  • 31
    • 0029165873 scopus 로고
    • Molecular characteristics of methylglyoxal-modified bovine and human serum albumins. Comparison with glucose-derived advanced glycation endproduct-modified serum albumins
    • Westwood, M. E. and Thornalley, P. J. (1995) Molecular characteristics of methylglyoxal-modified bovine and human serum albumins. Comparison with glucose-derived advanced glycation endproduct-modified serum albumins. J. Protein Chem. 14, 359-372
    • (1995) J. Protein Chem. , vol.14 , pp. 359-372
    • Westwood, M.E.1    Thornalley, P.J.2
  • 33
    • 0032544309 scopus 로고    scopus 로고
    • Activation of apoptosis signal-regulating kinase 1 (ASK1) by the adapter protein Daxx
    • Chang, H. Y., Nishitoh, H., Yang, X., Ichijo, H. and Baltimore, D. (1998) Activation of apoptosis signal-regulating kinase 1 (ASK1) by the adapter protein Daxx. Science 281, 1860-1863
    • (1998) Science , vol.281 , pp. 1860-1863
    • Chang, H.Y.1    Nishitoh, H.2    Yang, X.3    Ichijo, H.4    Baltimore, D.5


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