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Tytuł artykułu

Glutathione conjugation in male reproductive system: studies on glutathione-S-transferase of bull and boar epididymis

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Male reproductive organs are extremely sensitive to the negative influence of toxic environmental factors as well as drugs, and until now not many attempts have been made at studying the detoxication enzymes and the relationship between the activity of those enzymes and spermatozoa fertility. In the present work we studied cytosolic glutathione-S-transferases (GST, EC 2.5.1.18) from different parts (head, corpus and tail) of bull and boar epididymis. We isolated two molecular forms of GST from each part of epididymis, characterized their biochemical properties and examined the mechanism of the catalyzed reaction. On the basis of their substrate specificity and isoelectric point, the isoforms were found to belong to the near neutral GST class mi. All examined GST forms exhibited higher affinity towards GSH than towards 1-chloro-2,4-dinitrobenzene (CDNB) and bull epididymis GST forms showed biphasic Lineweaver-Burk double reciprocal curves in the presence of GSH as a variable substrate. Boar epididymis anionic GST had the -SH groups both in the GSH and the CDNB binding place, whereas the cationic GST form arginine residues in the CDNB binding place. Bull epididymis GST forms contained neither thiol nor arginine residues essential for catalytic activity.

Wydawca

-

Rocznik

Tom

47

Numer

1

Opis fizyczny

p.223-231,fig.

Twórcy

  • The Medical University of Warsaw, S.Banacha 1, 02-097 Warsaw, Poland

Bibliografia

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  • 2. Glover, T.D. & Nicander, L. (1971) Some aspects of structure and function in mammalian epididymis. J. Reprod. Fert. (Suppl.) 13, 39- 50.
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  • 4. Jakoby, W.B. (1978) The glutathione-S-transferases: A group of multifunctional detoxication proteins. Adv. Enzymol. 46, 383-414.
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  • 6. Mannervik, B. & Danielson, U.H. (1988) Glutathione transferases: Structure and catalytic activity. CRC Crit. Rev. Biochem. 23, 283-337.
  • 7. Armstrong, R. (1994) Glutathione-S-transferase: Structure and mechanism of an archetypical detoxication enzyme. Adv. Enzymol. 69, 1-44.
  • 8. Pickett, C.B. & Lu, A.Y.H. (1989) Glutathione- S-transferases: Gene structure, regulation and biological function. Annu. Rev. Biochem. 58, 743-764.
  • 9. Adang, A.E.P., Brussee, J., van der Gen, A. & Mulder, G.J. (1990) The glutathione-binding site in glutathione-S-transferases. Biochem. J. 269, 47-54.
  • 10. D'Silva, C. (1990) Inhibition and recognition studies on the glutathione-binding site of equine liver glutathione-S-transferase. Biochem. J. 271, 161-165.
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  • 13. Boyland, E. & Chasseaud, L.F. (1967) Enzyme-catalysed conjugation of glutathione with unsaturated compounds. Biochem. J. 104, 95-102.
  • 14. Habig, W.B., Pabst, M.J. & Jakoby, W.B. (1974) Glutathione-S-transferases: The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249, 7130-7139.
  • 15. Listowsky, I., Abramowitz, M., Homma, H. & Niitsu, Y. (1988) Intracellular binding of hormones and xenobiotics by glutathione-S-transferases. DrugMetab. Rev. 19, 305-318.
  • 16. Morrow, S. & Cowan, K.H. (1990) Glutathione-S-transferase and drug resistance. Cancer Cells. 2, 15-22.
  • 17. Hayes, J.D. & 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 (Review). Crit. Rev. Biochem. Mol. Biol. 30, 445-600.
  • 18. Ciszewska-Pilczynska, A. & Baranczyk- Kuzma, A. (1992) Glutathione-S-transferase from boar testis: Properties of the cytosolic and microsomal forms. Acta Biochim. Polon. 39, 139-145.
  • 19. Fujita, E., Kitagawa, H., Ishizawa, H., Suzuki, T. & Kitani, K. (1985) Age associated alterations in hepatic glutathione-S-transferase activity. Biochem. Pharmacol. 34, 3891-3894.
  • 20. Lowry, O.H., Rosebrough, N.J., Farr, A.L. & Randall, R.J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265-275.
  • 21. Eisenthal, R. & Cornish-Bowden, A. (1974) The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters. Biochem. J. 139, 715-720.
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  • 25. Meyer, L.G., Christodoulides, O., Nyan, R., Schuster, B. & Ketterer, B. (1983) A comparison of the glutathione transferases (GST) of three extrahepatic organs with different functions the adrenal, the lactating mammary gland and the male reproductive system; in Extrahepatic Drug Metabolism and Chemical Carcinogenesis (Rydstrom, I., Montelius, J. & Bengtsson, M., eds.) pp. 198-200, Elsevier, Amsterdam.
  • 26. Boggards, J.J.P., van Ommen, B. & van Bladderen, P.J. (1992) Purification and characterization of eight glutathione-S-transferase isoenzymes of hamster. Biochem. J. 286, 383-388.
  • 27. Aceto, A., Ilio di, C., Angelucci, S., Felaco, M. & Federici, G. (1989) Glutathione transferase isoenzymes from human testis. Biochem. Pharmacol. 38, 3653-3660.
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Bibliografia

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