Cellular redox potential and hemoglobin S-glutathionylation in human and rat erythrocytes: A comparative study

Blood Cells, Molecules, and Diseases

Volumn 44, Issue 3, 2010, Pages 133-139

  Colombo, Graziano ^a   Dalle Donne, Isabella ^a   Giustarini, Daniela ^b   Gagliano, Nicoletta ^a   Portinaro, Nicola ^c   Colombo, Roberto ^a   Rossi, Ranieri ^b   Milzani, Aldo ^a  

^a UNIVERSITY OF MILAN   (Italy)

^b UNIVERSITY OF SIENA   (Italy)

^c HUMANITAS CLINICAL AND RESEARCH CENTER   (Italy)

Author keywords

Erythrocytes; Glutathione redox potential; Nernst equation potential; S glutathionylated hemoglobin; tert butylhydroperoxide

Indexed keywords

BETA GLOBIN; CYSTEINE; DISULFIDE; GLUTATHIONE; GLUTATHIONE DISULFIDE; HEMOGLOBIN; HEMOGLOBIN S; TERT BUTYL HYDROPEROXIDE; THIOL;

ADULT; ANIMAL CELL; ARTICLE; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ERYTHROCYTE; EXPERIMENTAL MODEL; GLUTATHIONE METABOLISM; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; HUMAN CELL; NONHUMAN; NORMAL HUMAN; OXIDATION REDUCTION POTENTIAL; OXIDATIVE STRESS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PREDICTION; PRIORITY JOURNAL; PROTEIN LOCALIZATION; RAT; SPECIES DIFFERENCE;

ADULT; ANIMALS; ERYTHROCYTES; GLUTATHIONE; GLUTATHIONE DISULFIDE; HEMOGLOBIN, SICKLE; HUMANS; MIDDLE AGED; OXIDATION-REDUCTION; OXIDATIVE STRESS; RATS; RATS, SPRAGUE-DAWLEY; TERT-BUTYLHYDROPEROXIDE;

RATTUS;

EID: 76849098861     PISSN: 10799796     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcmd.2009.11.005     Document Type: Article

References (48)

1. Kemp M., Go Y.-M., and Jones J.P. Nonequilibrium thermodynamics of thiol/disulfide redox systems: a perspective on redox systems biology. Free Radic. Biol. Med. 44 (2008) 921-937
2. Jones D.P. Radical-free biology of oxidative stress. Am. J. Physiol. Cell Physiol. 295 (2008) C849-C868
3. Schafer F.Q., and Buettner G.R. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic. Biol. Med. 30 (2001) 1191-1212
4. Nemeth I., Orvos H., and Boda D. Blood glutathione redox status in gestational hypertension. Free Radic. Biol. Med. 30 (2001) 715-721
5. Rossi R., Giustarini D., Milzani A., and Dalle-Donne I. Membrane skeletal protein S-glutathionylation and haemolysis in human red blood cells. Blood Cells Mol. Dis. 37 (2006) 180-187
6. Giustarini D., Milzani A., Dalle-Donne I., and Rossi R. Red blood cells as a physiological source of glutathione for extracellular fluids. Blood Cells Mol. Dis. 40 (2008) 174-179
7. Jones D.P. Redox potential of [GSH]/[GSSG] couple: assay and biological significance. Methods Enzymol. 348 (2002) 93-112
8. Samiec P.S., Drews-Botsch C., and Flagg E.W. Glutathione in human plasma: decline in association with aging, age-related macular degeneration, and diabetes. Free Radic. Biol. Med. 24 (1998) 699-704
9. Dalle-Donne I., Rossi R., Giustarini D., et al. S-Glutathionylation in protein redox regulation. Free Radic. Biol. Med. 43 (2007) 883-898
10. Dalle-Donne I., Milzani A., Gagliano N., et al. Molecular mechanisms and potential clinical significance of S-glutathionylation. Antioxid. Redox Signal. 10 (2008) 445-473
11. Mieyal J.J., Gallogly M.M., Qanungo S., Sabens E.A., and Shelton M.D. Molecular mechanisms and clinical implications of reversible protein S-glutathionylation. Antioxid. Redox Signal. 10 (2008) 1941-1988
12. Kleinman W.A., Komninou D., Leutzinger Y., et al. Protein glutathiolation in human blood. Biochem. Pharmacol. 65 (2003) 741-746
13. Hoffmann P., Woon J., and Rowley K.G. Glutathionyl haemoglobin is not increased in diabetes nor related to glycaemia, complications, dyslipidaemia, inflammation or other measures of oxidative stress. Diabetes Res. Clin. Pract. 80 (2008) e1-3
14. Bursell S.E., and King G.L. The potential use of glutathionyl hemoglobin as a clinical marker of oxidative stress. Clin. Chem. 46 (2000) 145-146
15. Muscat J.E., Kleinman W., and Colosimo S. Enhanced protein glutathiolation and oxidative stress in cigarette smokers. Free Radic. Biol. Med. 36 (2004) 464-470
16. Sampathkumar R., Balasubramanyam M., Sudarslal S., et al. Increased glutathionylated hemoglobin (HbSSG) in type 2 diabetes subjects with microangiopathy. Clin. Biochem. 38 (2005) 892-899
17. Niwa T. Protein glutathionylation and oxidative stress. J. Chromatogr. B 855 (2007) 59-65
18. Lii C.K., and Hung C.N. Protein thiol modifications of human red blood cells treated with t-butyl hydroperoxide. Biochim. Biophys. Acta 1336 (1997) 147-156
19. Giustarini D., Dalle-Donne I., Colombo R., et al. Protein glutathionylation in erythrocytes. Clin. Chem. 49 (2003) 327-330
20. Giannerini F., Giustarini D., Lusini L., et al. Responses of thiols to an oxidant challenge: differences between blood and tissues in the rat. Chem. Biol. Interact. 134 (2001) 73-85
21. Mawatari K., and Murakami K. Different types of glutathionylation of hemoglobin can exist in intact erythrocytes. Arch. Biochem. Biophys. 421 (2004) 108-114
22. Rossi R., Milzani A., Dalle-Donne I., et al. Different metabolizing ability toward thiolic reagents in human and rat blood. J. Biol. Chem. 276 (2001) 7004-7010
23. Giustarini D., Dalle-Donne I., Colombo R., et al. An improved HPLC measurement for GSH and GSSG in human blood. Free Radic. Biol. Med. 35 (2003) 1356-1372
24. Rossi R., Dalle-Donne I., Milzani A., and Giustarini D. Oxidized forms of glutathione in peripheral blood as biomarkers of oxidative stress. Clin. Chem. 52 (2006) 1406-1414
25. Dalle-Donne I., Giustarini D., Colombo R., et al. S-glutathionylation in human platelets by a thiol-disulphide exchange-independent mechanism. Free Radic. Biol. Med. 38 (2005) 1501-1510
26. Kirlin W.G., Cai J., and Thompson S.A. Glutathione redox potential in response to differentiation and enzyme inducers. Free Radic. Biol. Med. 27 (1999) 1208-1218
27. Nkabyo Y.S., Ziegler T.R., and Gu H.H. Glutathione and thioredoxin redox during differentiation in human colon epithelial (Caco-2) cells. Am. J. Physiol. Gastrointest. Liver Physiol. 283 (2002) G1352-G1359
28. Nkabyo Y.S., Gu L.H., Jones D.P., and Ziegler T.R. Thiol/Disulfide redox status is oxidized in plasma and small intestinal and colonic mucosa of rats with inadequate sulfur amino acid intake. J. Nutr. 136 (2006) 1242-1248
29. Dalle-Donne I., Rossi R., Colombo R., et al. Biomarkers of oxidative damage in human disease. Clin. Chem. 52 2006 (2006) 601-623
30. Dalle-Donne I., Rossi R., Colombo G., et al. Protein S-glutathionylation: a regulatory device from bacteria to humans,. Trends Biochem. Sci. 34 (2009) 85-96
31. Dickerson R.E., Geis I., and Hemoglobins I. Structure, Function, Evolution, and Pathology (1983), Benjamin/Cummings, Menlo Park, CA
32. Jia L., Bonaventura C., Bonaventura J., and Stamler J.S. S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control. Nature 380 (1996) 221-226
33. Stamler J.S., Jia L., Eu J.P., et al. Blood flow regulation by S-nitrosohemoglobin in the physiological oxygen gradient. Science 276 (1997) 2034-2037
34. Singel D.J., and Stamler J.S. Chemical physiology of blood flow regulation by red blood cells: the role of nitric oxide and S-nitrosohemoglobin. Annu. Rev. Physiol. 67 (2005) 99-145
35. Garel M.C., Domenget C., Caburi-Martin J., et al. Covalent binding of glutathione to hemoglobin I. Inhibition of hemoglobin S polymerization. J. Biol. Chem. 261 (1986) 14704-14709
36. Craescu C.T., Poyart C., Schaeffer C., et al. Covalent binding of glutathione to hemoglobin. II. Functional consequences and structural changes reflected in NMR spectra. J. Biol. Chem. 261 (1986) 14710-14716
37. Thomas J.A., Mallis R.J., and Sies H. Protein S-thiolation, S-nitrosylation, and irreversible sulfhydryl oxidation: roles in redox regulation. In: Gitler C., and Danon A. (Eds). Cellular Implications of Redox Signaling (2003), Imperial College Press, London 141-174
38. Naito C., and Niwa T. Analysis of glutathionyl hemoglobin levels in diabetic patients by electrospray ionization liquid chromatography-mass spectrometry: effect of vitamin E administration. J. Chromatogr. B 746 (2000) 91-94
39. Al-Abed Y., VanPatten S., Li H., et al. Characterization of a novel hemoglobin-glutathione adduct that is elevated in diabetic patients. Mol. Med. 7 (2001) 619-623
40. Piemonte F., Pastore A., Tozzi G., et al. Glutathione in blood of patients with Friedreich's ataxia. Eur. J. Clin. Invest. 31 (2001) 1007-1011
41. Niwa T., Naito C., Mawjood A.H., and Imai K. Increased glutathionyl hemoglobin in diabetes mellitus and hyperlipidemia demonstrated by liquid chromatography/electrospray ionization-mass spectrometry. Clin. Chem. 46 (2000) 82-88
42. Naito C., Kajita M., and Niwa T. Determination of glutathionyl haemoglobin in hemodialysis patients using electrospray ionization liquid chromatography-mass spectrometry. J. Chromatogr. B 731 (1999) 121-124
43. Takayama F., Tsutsui S., Horie M., et al. Glutathionyl hemoglobin in uremic patients undergoing hemodialysis and continuous ambulatory peritoneal dialysis. Kidney Int. Suppl. 78 (2001) S155-S158
44. Ferranti P., Carbone V., Sannolo N., et al. Mass spectrometric analysis of rat hemoglobin by FAB-overlapping. Primary structure of the alpha-major and of four beta constitutive chains, Int. J. Biochem. 25 (1993) 1943-1950
45. Rossi R., Barra D., Bellelli A., et al. Fast-reacting thiols in rat hemoglobins can intercept damaging species in erythrocytes more efficiently than glutathione. J. Biol. Chem. 273 (1998) 19198-19206
46. Miranda J.J. Highly reactive cysteine residues in rodent hemoglobins. Biochem. Biophys. Res. Commun. 275 (2000) 517-523
47. Hempe J.M., Ory-Ascani J., and Hsia D. Genetic variation in mouse beta globin cysteine content modifies glutathione metabolism: implications for the use of mouse models. Exp. Biol. Med. (Maywood) 232 (2007) 437-444
48. Giustarini D., Dalle-Donne I., Cavarra E., et al. Metabolism of oxidants by blood from different mouse strains. Biochem. Pharmacol. 71 (2006) 1753-1764