The γ-glutamyltransferase activity and non-protein sulfhydryl compounds levels in rat kidney of different age groups.

• Authors: Przemysław Włodek , Maria Sokołowska , Olgierd Smoleński , Lidia Włodek
• Languages of publication: EN

Abstracts

EN

The present work was aimed to obtain information about age-dependent changes of γ-glutamyltransferase (GGT) activity and the levels of non-protein sulfhydryl compounds (NPSH) in rat kidneys. In addition, protein-bound cysteine (PB-Cys), sulfane sulfur compounds and reactive oxygen species (ROS) were estimated The results indicate that the activity of GGT and NPSH levels in the kidneys are reduced with age. At the same time, a significant increase in the level of protein-bound cysteine was observed. Simultaneously, the content of sulfane sulfur compounds was increased in the group of the oldest animals. These findings indicate that the capacity for extracellular glutathione degradation and, in consequence, the availability of cysteine for intracellular glutathione biosynthesis may be impaired. The increased PB-Cys level indicates potentiation of the thiolation reaction, i.e. development of protein-mixed disulfides. These results reveal age dependent disturbances in the thiol-disulfide equilibrium in the kidneys which leads to an imbalance between pro- and antioxidatory processes.

Keywords

EN

L-cysteine; kidney; aging; γ-glutamyl transferase; reactive oxygen species; protein-bound cysteine; glutathione; sulfane sulfur compounds

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2002
• Volume: 49
• Issue: 2
• Pages: 501-507

Dates

published

2002

received

2002-01-2

revised

2002-02-20

accepted

2002-04-22

Contributors

author

Przemysław Włodek

• Department of Nephrology, Rydygier Hospital, Kraków, Poland

author

Maria Sokołowska

• Institute of Medical Biochemistry, Collegium Medicum, Jagiellonian University, Kraków, Poland

author

Olgierd Smoleński

• Department of Nephrology, Rydygier Hospital, Kraków, Poland

author

Lidia Włodek

• Institute of Medical Biochemistry, Collegium Medicum, Jagiellonian University, Kraków, Poland

References

• Aebi E, Lauterberg BH. (1992) Divergent effects of intravenous GSH and cysteine on renal and hepatic GSH. Am J Physiol.; 263: R348-52.
• Anderson ME, Bridges RJ, Meister A. (1980) Direct evidence for inter-organ transport of glutathione and that the non-filtration renal mechanism for glutathione utilization involves g-glutamyl transpeptidase. Biochem Biophys Res Commun.; 96: 848-53.
• Bondy SC, Guo SX. (1994) Effect of ethanol treatment on indices of cumulative oxidative stress. Eur J Pharmacol.; 270: 349-55.
• Choie DD, Longnecker DS., del Campo AA. (1981) Acute and chronic cisplatin nephropathy in rats. Lab Invest.; 44: 397-402.
• Clark A. (2000) Biology of renal aging in humans. Adv Ren Replace Ther.; 7: 11-21.
• Collison MW, Beidler D, Grimm LM, Thomas JA. (1986) A comparison of protein S-thiolation (protein mixed-disulfide formation) in heart cells treated with t-butylhydroperoxide or diamide. Biochem Biophys Acta.; 885: 58-67.
• Elfarra AA, Anders MW. (1984) Renal processing of glutathione conjugates: role in nephrotoxicity. Biochem Pharmacol.; 33: 3729-32.
• Everett SA. (1995) Antioxidant drug design: a comparison of thiol and perthiol antiradical and prooxidant radiation mechanism. In Biothiols in health and disease: Packer L, Cadens E. eds, pp 49-64. New York.
• Hazelton GA, Lang CA. (1985) Glutathione peroxidase and reductase activities in the aging mouse. Mech Ageing Dev.; 29: 71-81.
• Hinchman CA, Ballatori N. (1990) Glutathione-degradating capacities of liver and kidney in different species. Biochem Pharmacol.; 40: 1131-5.
• Iciek M, Włodek L. (2001) Biosynthesis and biological properties of compounds containing highly reactive, reduced sulfane sulfur. Pol J Pharmacol.; 53: 215-25.
• Jenkinson SG, Duncan CA, Bryan CL, Lawrence RA. (1991) Effects of age on rat glutathione metabolism. Am J Med Sci.; 302: 347-52.
• Kharasch ED, Thorning D, Garton K, Douglas C, Hankin MA, Kitty CE. (1997) Role of renal cysteine conjugate β-lyase in the mechanism of compound nephrotoxicity in rats. Anesthesiology.; 86: 160-71.
• Kugelman A, Choy HA, Liu R, Shi MM, Gozal E, Forman HJ. (1994) Gamma-glutamyltranspeptidase is increased by oxidative stress in rat alveolar L2 epithelial cells. Am J Respir Cell Mol Biol.; 11: 586-92.
• Lam YWE, Banerji S, Hatfield C, Talbert RL. (1997) Principles of drug administration in renal insufficiency. Clin Pharmacokinet.; 32: 30-57.
• Malloy MM, Rassin DC, Gaull GE. (1981) A method for measurement of free and bound plasma cysteine. Anal Biochem.; 113: 407-15.
• Meister A. (1983) Metabolism and transport of glutathione and other g-glutamyl compounds. In Functions of glutathione: biochemical, physiological, toxicological and clinical aspects. Larsson A, Orrenius S, Holmgren A, Mannervik B. eds, pp 1-22. Raven Press, New York.
• Mühlberg W, Platt D. (1999) Age-dependent changes of the kidneys: pharmacological implications. Gerontology.; 45: 243-53.
• Ogasawara Y, Isoda S, Tanabe S. (1994) Tissue and subcellular distribution of bound and acid-labile sulfur and the enzymatic capacity of sulfide production in the rat. Biol Pharm Bull.; 17: 1535-42.
• Orlowski M, Meister A. (1966) Isolation of g&-glutamyl transpeptidase from hog kidney. J Biol Chem.; 240: 338-40.
• Potter DW, Tran T. (1993) Apparent rates of glutathione turnover in rat tissues. Toxicol Appl Pharmacol.; 120: 186-92.
• Puka-Sundvall M, Eriksson P, Nilscon M, Sondberg M, Lehmann, A. (1995) Neurotoxicity of cysteine: interaction with glutamate. Brain Res.; 705: 65-70.
• Rodriguez-Puyol D. (1998) The aging kidney. Kidney Int.; 54: 2247-65.
• Sedlak J, Lindsay RH. (1968) Estimation of total protein bound and nonprotein sulfhydryl groups in tissues with Ellman's reagent. Anal Biochem.; 25: 192-205.
• Smolin LA, Laidlaw SA, Kopple JD. (1987) Altered plasma free and protein bound sulphur amino acid levels in patients undergoing maintenance hemodialysis. Am J Clin Nutr.; 45: 737-45.
• Speisky H. (1992) Age-dependent removal of circulating glutathione by rat liver: role of gamma-glutamyl transferase. Age.; 15: 104-7.
• Stipanuk MH, De La Rosa J, Hirschberger L. (1990) Catabolism of cysteine by rat renal cortical tubules. J Nutr.; 120: 450-8.
• Sturman JA, Rassin DK, Gaull GE (1970) Distribution of transsulphuration enzymes in various organs and species. Int J Biochem.; 1: 251-3.
• Toohey JJ. (1989) Sulphane sulphur in biological systems: a possible regulatory role. Biochem J.; 264: 625-32.
• Włodek P, Iciek MB, Miłkowski A, Smoleński OB. (2001) Various forms of plasma cysteine and its metabolites in patients undergoing hemodialysis. Clin Chim Acta.; 304: 9-18.
• Wood L. (1987) Sulfane sulfur. Methods Enzymol.; 143: 25-9.