Publication Cover
Xenobiotica
the fate of foreign compounds in biological systems
Volume 23, 1993 - Issue 8
16
Views
41
CrossRef citations to date
0
Altmetric
Original Article

Glutathione transferases of classes α, μ and π show selective expression in different regions of rat kidney

, , , &
Pages 835-849 | Received 05 May 1993, Accepted 14 Jun 1993, Published online: 23 Apr 2010

References

  • Abramovitz M., Ishigak S., Felix A. M., Listowsky I. Expression of an enzymatically active Yb3 glutathioneS-transferase inEscherichia coli and identification of its natural form in rat brain. Journal of Biological Chemistry 1988; 263: 17627–17631
  • Ådlin P., Jensson H., Cederlund E., Jörnvall H., Mannervik B. Cytosolic GSH transferases from rat liver. Primary structure of class alpha transferase 8–8 and characterization of low abundance class mu transferases. Biochemical Journal 1989; 261: 531–539
  • ÅLin P., Jensson H., Guthenberg C., Danielson U. H., Tahir M. K., Mannervik B. Purification of major basic glutathione transferase isoenzymes from rat liver by use of affinity chromatography and fast protein liquid chromatofocusing. Analytical Biochemistry 1985; 146: 313–320
  • BÅCkman L., Appelkvist E. L., Ringden O., Dallner G. Glutathione transferase in the urine: a marker for post-transplant tubular lesions. Kidney International 1988; 33: 571–577
  • Bannikov G. A., Tchipyseva T. A. Ligandin in steroidogenically active cells of rat gonads. British Journal of Cancer 1978; 38: 350–354
  • Bennett C. F., Spector D. L., Yeoman L. C. Nonhistone protein BA is a glutathioneS-transferase localized to interchromatinic regions of the cell nucleus. Journal of Cell Biology 1986; 102: 600–609
  • Blake M. S., Johnston K. H., Russel-Jones B. J., Gotschliech E. C. Analytical Biochemistry 1984; 136: 175–187
  • Boyce S. J., McBennett S. M., Mantle T. J., Hayes J. D. Tissue distribution of glutathioneS-transferase subunits in rodents: an immunocytochemical study. Glutathione S-transferases and Carcinogenesis, T. J. Mantle, C. B. Pickett, J. D. Hayes. Taylor & Francis, London 1987; 69–72
  • Danielson U. H., Mannervik B. Kinetic independence of the subunits of cytosolic glutathione transferases from rat liver. Biochemical Journal 1985; 231: 263–267
  • Editorial. A standard nomenclature for structures of the kidney. European Journal of Physiology 1988; 411: 113–120
  • Feinfeld D. A., Bourgoinie J. J., Fleischner G., Goldstein E. J., Biampica L., Arias I. M. Ligandinuria in nephrotoxic acute tubular necrosis. Kidney International 1977; 12: 387–392
  • Fleischner G. M., Robbins J. B., Arias I. M. Cellular localization of ligandin in rat, hamster and man. Biochemical and Biophysical Research Communication 1977; 74: 992–1000
  • Guthenberg C., Jensson H., Nyström L., Österlund E., Tahir M. K., Mannervik B. Isoenzymes of glutathione transferase in rat kidney cytosol. Biochemical Journal 1985; 230: 609–615
  • Hiley C., Bell J., Hume R., Strange R. Differential expression of alpha and pi isoenzymes of glutathioneS-transferase in developing human kidney. Biochimica et Biophysica Acta 1989; 990: 321–324
  • Jakoby W. B., Ketterer B., Mannervik B. Glutathione transferases: nomenclature. Biochemical Pharmacology 1984; 33: 2539–2540
  • Jensson H., Guthenberg C., ÅLin P., Mannervik B. Rat glutathione transferase 8–8, an enzyme efficiently detoxifying 4-hydroxyalk-2-enals. Federations of the European Biochemical Society Letters 1986; 203: 207–209
  • Johnson G. D., Davidson R. S., McNamee K. C., Russel G., Goodwin D., Holborrow E. J. Fading of immunofluorescence during microscopy: a study of the phenomenon and its remedy. Journal of Immunological Methods 1982; 55: 231–235
  • Kalb V. F., Jr, Bernlohr R. W. A new spectrophotometric assay for protein in cell extracts. Analytical Biochemistry 1977; 82: 362–371
  • Ketterer B., Carne T., Tipping E. Ligandin and protein A: intracellular binding proteins. Transport of Proteins, G. Blauer, H. Sund. Walter de Gruyter, Berlin 1978; 69–94
  • Ketterer B., Meyer D. J., Clark A. G. Soluble glutathione transferases. Glutathione Conjugation. Mechanisms and Biological Significance, M. Sies, B. Ketterer. Academic, London 1988; 73–135
  • Kotanko P., Keiler R., Knabl L., Aulitzky W., Margreiter R., Gstraunthaler Pfaller W. Urinary enzyme analysis in renal allograft transplantation. Clinica Chimica Acta 1986; 160: 137–144
  • Laemmli U. K. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 1970; 277: 680–685
  • Mannervik B. The isoenzymes of glutathione transferase. Advances in Enzymology and Related Areas of Molecular Biology 1985; 57: 357–417
  • Mannervik B., Daneilson U. H. Glutathione transferases—structure and catalytic activity. CRC Critical Reviews in Biochemistry 1988; 23: 283–377
  • Mannervik B., Jensson H. Binary combinations of four protein subunits with different catalytic specificities explain the relationship between six basic glutathioneS-transferase in rat liver cytosol. Journal of Biological Chemistry 1982; 257: 9909–9912
  • Mannervik B., Guthenberg C., Jensson H., Warholm M., ÅLin P. Isoenzymes of glutathioneS-transferases in rat and human tissues. Functions of Glutathione: Biochemical, Physiological, Toxicological and Clinical Aspects, A. Larsson, S. Orrenius, A. Holmgren, B. Mannervik. Raven Press, New York 1983; 75–88
  • Mannervik B., ÅLin P., Guthenberg C., Jensson H., Tahir M. K., Warholm M., Jörnvall H. Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties. Proceedings of the National Academy of Sciences, USA 1985; 82: 7202–7206
  • Meyer D. J., Lalor E., Coles B., Kispert A., Ålin P., Mannervik B., Ketterer B. Single step purification and h.p.l.c. analysis of glutathione transferase 8–8 in rat tissues. Biochemical Journal 1989; 260: 785–788
  • Persson B., Jörnvall H., Ålin P., Mannervik B. Structural classes of glutathione transferase: distinctions between isoenzymes and enzymes. Protein Sequences Data Analyses 1988; 1: 183–186
  • Redick J. A., Jakoby W. B., Baron J. Immunohistochemical localization of glutathioneS-transferases in livers of untreated rats. Journal of Biological Chemistry 1982; 257: 15200–15203
  • Rozell B., Hansson H.-A., Luthman M., Holmgren A. Immunohistochemical localization of thioredoxin and thioredoxin reductase in adult rats. European Journal of Cell Biology 1985; 38: 79–86
  • Senjo M., Ishibashi T., Terashima T., Inoue Y. Successive appearance of glutathioneS-transferase-positive cells in developing rat brain: choroid plexus, pia mater, ventricular zone and astrocytes. Neuroscience Letters 1986; 66: 131–134
  • Sies H., Ketterer B. Glutathione Conjugation. Mechanisms and Biological Significance. Academic, London 1988
  • Singh S. V., Leal T., Ansari G. A., Awasthi Y. C. Purification and characterization of glutathioneS-transferase of human kidney. Biochemical Journal 1987; 246: 179–186
  • Tahir M. K., Mannervik B. Simple inhibition studies for distinction between homodimeric and heterodimeric isoenzymes of glutathione transferase. Journal of Biological Chemistry 1986; 261: 1048–1051
  • Tateoka N., Tsuchida S., Soma Y., Sato K. Purification and characterization of glutathioneS-transferases in human kidney. Clinica Chimica Acta 1987; 166: 207–218
  • Tokuyasu K. T. Immunocryoultramicrotomy. Immunolabelling for Electron Microscop, J. M. Polak, I. M. Varndall. Elsevier, London 1984
  • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proceedings of the National Academy of Sciences, USA 1979; 76: 4350–4354
  • Trakshel G. M., Maines M. D. Characterization of glutathioneS-transferases in rat kidney. Alteration of composition by cisplatinum. Biochemical Journal 1988; 252: 127–136
  • Tsuda H., Moore M. A., Asamoto M., Satoh K., Tsuchida S., Sato K., Ichihara A., Ito N. Comparison of the various forms of glutathioneS-transferase with glucose 6-phosphate dehydrogenase and gamma-glutamyltranspeptidase as markers of preneoplastic and neoplastic lesions in rat kidney induced byN-ethyl-N-hydroxy-ethylnitrosamine. Japanese Journal of Cancer Research (Gann) 1985; 76: 919–929
  • Venkatachalam M. A., Bernard D. B., Donohoe J. F., Levinsky N. G. Ischemic damage and repair in the rat proximal tubule: differences among the S1, S2 and S3 segments. Kidney International 1978; 14: 31–49

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.