Plasma levels of total, free and protein bound thiols as well as sulfane sulfur in different age groups of rats

• Autorzy: Iciek M. , Chwatko G. , Lorenc-Koci E. , Bald E. , Wlodek L.
• Języki publikacji: EN

Abstrakty

EN

The redox status of plasma thiols can be a diagnostic indicator of different patho­logical states. The aim of this study was to identify the age dependent changes in the plasma levels of total, free and protein bound glutathione, cysteine and homocysteine. The determination was conducted in plasma of three groups of rats: 1) young (3-month-old), 2) middle aged (19-month-old), and 3) old (31-month-old). To­tal levels of glutathione, cysteine and homocysteine and their respective free and protein-bound fractions decreased with age. The only exception was a rise in free homocysteine concentration in the middle group, which indicates a different pattern of transformations of this thiol in plasma. The drop in the level of protein-bound thiols suggests that the antioxidant capacity of plasma diminishes with age, which, consequently, leads to impaired protection of -SH groups through irreversible oxida­tion. The plasma sulfane sulfur level also declines with age, which means that aging is accompanied by inhibition of anaerobic sulfur metabolism.

Słowa kluczowe

EN

plasma level; disulphide; thiol; sulphane sulphur; age group; rat

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2004
• Tom: 51
• Numer: 3
• Opis fizyczny: p.815-824,fig.,ref.

Twórcy

autor

Iciek M.

• Jagiellonian University, Kopernika 7, 31-034 Krakow, Poland

autor

Chwatko G.

autor

Lorenc-Koci E.

autor

Bald E.

autor

Wlodek L.

Bibliografia

• Anderson ME, Bridges RJ, Meister A. (1980) Direct evidence for inter-organ transport of glutathione and that the non­filtration renal mechanism for glutathione utilization involves gamma-glutamyl transpeptidase. Biochem Biophys Res Commun.; 96: 848-53.
• Bald E, Glowacki R. (2001) 2-Chloro-1-methylquinolinium tetrafluoroborate as an effective and thiol specific UV-tagging reagent for liquid chromatography. JLiq ChromatogrRel Technol.; 24: 1323-39.
• Cappiello M, Vilardo PG, Micheli V, Jacomelli G, Banditelli S, Leverenz V, Giblin FJ, del Corso A, Mura U. (2000) Thiol disulfide exchange modulates the activity of aldose reductase in intact bovine lens as a response to oxidative stress. Exp Eyre Res.; 70: 795-3.
• Choi J, Liu RM, Kundu RK, Sangiorgi F, Wu W, Maxson R, Forman HJ. (2000) Molecular mechanism of decreased glutathione content in human immunodeficiency virus type 1 Tat-transgenic mice. J Biol Chem.; 275: 3693-8.
• Chwatko G, Bald E. (2002) Determination of different species of homocysteine in human plasma by high-performance liquid chromatography with ultraviolet detection. J Chromatogr A.; 949: 141-51.
• Dafre AL, Sies H, Akerboom T. (1996) Protein S-thiolation and regulation of microsomal glutathione redox couple. Arch Biochem Biophys.; 332: 288-94.
• Everett SA, Folkes LK, Wardman P. (1994) Free radical repair by a novel perthiol: reversible hydrogen transfer and perthiyl radical formation. Free Radic Res.; 20: 387-400.
• Hadi Yasa M, Kacmaz M, Serda Ozturk M, Durak J. (1999) Antioxidant status of erythrocyte from patients with cirrhosis. Hepato-Gastroenterology.; 46: 2460-3.
• Harman D. (1981) The aging process. Proc Natl Acad Sci USA.; 78: 7124-8.
• Hernanz A, Fernandez-Vivancos E, Salazar RM, Arnalich F. (2000) Homocysteine and other thiol compounds in ageing. Biofactors.; 11: 47-9.
• Hogg N. (1999) The effect of cyst(e)ine on the auto-oxidation of homocysteine. Free Radic Biol Med. ; 27: 28-33.
• Iciek M, Wlodek L. (2001) Biosynthesis and biological properties of compounds containing highly reactive reduced sulfane sulfur. Pol J Pharmacol.; 53: 215-25.
• Jung CH, Thomas JA. (1996) S-glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase and glutathione. Arch Biochem Biophys.; 335: 61-72.
• Klatt P, Lamas S. (2000) Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress. Eur J Biochem.; 267: 4928-44.
• Kleinman WA, Richie JP Jr. (2000) Status of glutathione and other thiols and disulfides in human plasma. Biochem Pharmacol.; 60: 19-29.
• Lang CA, Naryshkin S, Schneider DL, Mills BJ, Lindeman RD. (1992) Low blood glutathione levels in healthy aging adults. J Lab Clin Med.; 120: 720-5.
• Lash LH, Jones DP. (1985) Distribution of oxidized and reduced forms of glutathione and cysteine in rat plasma. Arch Biochem Biophys.; 240: 583-92.
• Lou MF. (2000) Thiol regulation in the lens. J OculPharmacol Ther.; 16: 137-48.
• Mallis RJ, Hamann MJ, Zhao W, Zhang T, Hendrich S, Thomas JA. (2002) Irreversible thiol oxidation in carbonic anhydrase III: protection by S-glutathiolation and detection in aging rats. Biol Chem.; 383: 649-62.
• Mansoor MA, Svardal AM, Schneede J, Ueland PM. (1992) Dynamic relation between reduced, oxidzed and protein bound homocysteine and other thiol compounds in plasma during methionine loading in healthy men. Clin Chem.; 38: 1316-21.
• McCully KS. (1996) Homocysteine and vascular disease. Nat Med.; 2: 386-9.
• Mills BJ, Lang CA. (1996) Differential distribution of free and bound glutathione and cyst(e)ine in human blood. Biochem Pharmacol.; 52: 401-6.
• Padgett CM, Whorton AR. (1998) Cellular responses to nitric oxide: role of protein S-thiolation/dethiolation. Arch Biochem Biophys.; 358: 232-42.
• Percival MD, Quellet M, Campagnolo C, Claveau D, Li C. (1999) Inhibition of cathepsin K by nitric oxide donors: evidence for the formation of mixed disulfides and a sulfenic acid. Biochemistry.; 38: 13574-83.
• Pirmohamed M, Williams D, Tingle MD, Barry M, Khoo S, O'Mahony C, Wilkins EG, Breckenridge AM, Park BK. (1996) Intracellular glutathione in the peripheral blood cell of HIV-infected patients: failure to show a deficiency. AIDS.; 10: 501-7.
• Qiao F, Xing K, Lou MF. (2000) Modulation of lens glycolytic pathway by thioltransferase. Exp Eye Res.; 70: 745-53.
• Rea IM, McMaster D, Woodside JV, Young IS, Archbold GP, Linton T, Lennox S, McNulty H, Harmon DL, Whitehead AS. (2000) Community-living nonagenarians in Northern Ireland have lower plasma homocysteine but similar methylenetetrahydrofolate reductase thermolabile genotype prevalence compared to 70-89-year-old subjects. Atherosclerosis.; 149: 207-14.
• Rokutan K, Johnston RB Jr, Kawai K. (1994) Oxidative stress induces S-thiolation of specific proteins in cultured gastric mucosal cells. Am J Physiol. ; 266: G247-54.
• Samiec PS, Drews-Botsch C, Flagg EW, Kurtz JC, Sternberg P Jr, Reed RL, Jones DP. (1998) Glutathione in human plasma: decline in association with aging, age-related macular degeneration and diabetes. Free Radic Biol Med. ; 24: 699-704.
• Schuppe-Koistinen I, Moldeus P, Bergman T, Cotgreave IA. (1994) S-Thiolation of human endothelial cell glyceraldehyde- 3-phosphate dehydrogenase after hydrogen treatment. Eur J Biochem.; 221: 1033-7.
• Sengupta S, Chen H, Togawa T, DiBello PM, Majors AK, Budy B, Ketterer M, Jacobsen DW. (2001) Albumin thiolate anion is an intermediate in the formation of albumin-S-S-homocysteine. J Biol Chem.; 276: 30111-7.
• Sian J, Dexter DT, Lees AJ, Daniel S, Agid Y, Javoy-Agid F, Jenner P, Marsden CD. (1994) Alteration of glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia. Ann Neurol.; 36: 348-55.
• Speisky H. (1992) Age-dependent removal of circulating glutathione by rat liver: role of gamma-glutamyl transferase. Age.; 15: 104-7.
• Thomas JA, Mallis RJ. (2000) Aging and oxidation of reactive protein sulfhydryls. Exp Geront.; 36: 1519-26.
• Toohey JI. (1989) Sulphane sulphur in biological systems: a possible regulatory role. Biochem J.; 264: 625-32.
• Ueland PM. (1995) Homocysteine species as components of plasma redox thiol status. Clin Chem.; 41: 340-2.
• Ueland PM, Mansoor MA, Guttormsen AB, Muller F, Aukrust P, Refsum H, Svardal AM. (1996) Reduced, oxidized and protein-bound forms of homocysteine and other aminothiols in plasma comprise the redox thiol status - a possible element of the extracellular antioxidant defense system. JNutr.; 126: 1281S-4S.
• Vogt BL, Richie JP Jr. (1993) Fasting-induced depletion of glutathione in the aging mouse. Biochem Pharmacol.; 46: 257-63.
• Welch GN, Upchurch GR Jr, Loscalzo J. (1997) Homocysteine, oxidative stress and vascular disease. Hosp Pract.; 32: 81-92.
• Wlodek L. (2002) Causes of L-cysteine neurotoxicity. Acta Biol Cracoviensia.; 44: 15-24.
• Wlodek P, Sokolowska M, Smolenski O, Wlodek L. (2002) The gamma-glutamyltransferase activity and non-protein sulfhydryl compounds levels in rat kidney of different groups. Acta Biochim Polon.; 49: 501-7.
• Wood JL. (1987) Sulfane sulfur. Methods Enzymol.; 143: 25-9.