Oxidative stress, erythrocyte ageing and plasma non-protein-bound iron in diabetic patients

References

• Signorini C, Ferrali M, Ciccoli L, Sugherini L, Magnani A, Comporti M. Iron release, membrane protein oxidation and erythrocyte ageing. FEBS Lett 1995; 362: 165–170
   PubMed Web of Science ®Google Scholar
• Comporti M, Signorini C, Buonocore G, Ciccoli L. Iron release, oxidative stress and erythrocyte ageing. Free Radic Biol Med 2002; 32: 568–576
   PubMed Web of Science ®Google Scholar
• Turrini F, Mannu F, Cappadoro M, Ulliers D, Giribaldi G, Arese P. Binding of naturally occurring antibodies to oxidatively and nonoxidatively modified erythrocyte band 3. Biochim Biophys Acta 1994; 1190: 297–303
   PubMed Web of Science ®Google Scholar
• Ferrali M, Ciccoli L, Comporti M. Allyl alcohol-induced hemolysis and its relation to iron release and lipid peroxidation. Biochem Pharmacol 1989; 38: 1819–1825
   PubMed Web of Science ®Google Scholar
• Ferrali M, Signorini C, Ciccoli L, Comporti M. Iron release and membrane damage in erythrocytes exposed to oxidizing agents, phenylhydrazine, divicine and isouramil. Biochem J 1992; 285: 295–301
   PubMed Web of Science ®Google Scholar
• Ciccoli L, Signorini C, Scarano C, Rossi V, Bambagioni S, Ferrali M, Comporti M. Iron release in erythrocytes from patients with beta-thalassemia. Free Radic Res 1999; 30: 407–413
   PubMed Web of Science ®Google Scholar
• Ciccoli L, Rossi V, Leoncini S, Signorini C, Paffetti P, Bracci R, Buonocore G, Comporti M. Iron release in erythrocytes and plasma non protein-bound iron in hypoxic and non hypoxic newborns. Free Radic Res 2003; 37: 51–58
   PubMed Web of Science ®Google Scholar
• Pearson HA. Life-span of the fetal red blood cell. J Pediatr 1967; 70: 166–171
   PubMed Web of Science ®Google Scholar
• Rossi V, Leoncini S, Signorini C, Buonocore G, Paffetti P, Tanganelli D, Ciccoli L, Comporti M. Oxidative stress and autologous immunoglobulin G binding to band 3 dimers in newborn erythrocytes. Free Radic Biol Med 2006; 40: 907–915
   PubMed Web of Science ®Google Scholar
• Milne GL, Musiek ES, Morrow JD. F2-isoprostanes as markers of oxidative stress in vivo: an overview. Biomarkers 2005; 10: S10–S23
   Web of Science ®Google Scholar
• Comporti M, Signorini C, Leoncini S, Buonocore G, Rossi V, Ciccoli L. Plasma F2- isoprostanes are elevated in newborns and inversely correlated to gestational age. Free Radic Biol Med 2004; 37: 724–732
   PubMed Web of Science ®Google Scholar
• Jay D, Hitomi H, Griendling KK. Oxidative stress and diabetic cardiovascular complications. Free Radic Biol Med 2006; 40: 183–192
   PubMedGoogle Scholar
• Davì G, Falco A, Patrono C. Lipid peroxidation in diabetes mellitus. Antiox Redox Signals 2005; 7: 256–268
   PubMed Web of Science ®Google Scholar
• Halliwell B, Gutteridge JMC. Free radicals, other reactive species and disease. Free radicals in biology and medicine, B Halliwell, JMC Gutteridge. Clarendon Press, Oxford 1999; 617–783
   Google Scholar
• Sailaja YR, Baskar R, Saralakumari D. The antioxidant status during maturation of reticulocytes to erythrocytes in type 2 diabetics. Free Radic Biol Med 2003; 35: 133–139
   PubMed Web of Science ®Google Scholar
• Babu N, Singh M. Influence of hyperglycemia on aggregation, deformability and shape parameters of erythrocytes. Clin Hemorheol Microcirc 2004; 31: 273–280
   PubMed Web of Science ®Google Scholar
• Wautier JL, Wautier MP, Schmidt M, Anderson GM, Hori O, Zoukourian C, Capron L, Chappey O, Yan SD, Brett J, Guillausseau PJ, Stern D. Advanced glycation end products (AGEs) on the surface of diabetic erythrocytes bind to the vessel wall via a specific receptor inducing oxidant stress in the vasculature: a link between surface-associated AGEs and diabetic complications. Proc Natl Acad Sci USA 1994; 91: 7742–7746
   PubMed Web of Science ®Google Scholar
• Berger HM, Mumby S, Gutteridge JMC. Ferrous ions detected in iron-overloaded cord blood plasma from preterm and term babies: implications for oxidative stress. Free Radic Res 1995; 22: 555–559
   PubMed Web of Science ®Google Scholar
• Loréal O, Gosriwatana I, Guyader D, Porter J, Brissot P, Hider RC. Determination of non-transferrin-bound iron in genetic hemochromatosis using a new HPLC-based method. J Hepatol 2000; 32: 727–733
   PubMed Web of Science ®Google Scholar
• Gosriwatana I, Loréal O, Lu S, Brissot P, Porter J, Hider RC. Quantification of non-transferrin-bound iron in the presence of unsaturated transferrin. Anal Biochem 1999; 273: 212–220
   PubMed Web of Science ®Google Scholar
• Fernández-Real JM, López-Bermejo A, Ricart W. Cross-talk between iron metabolism and diabetes. Diabetes 2002; 51: 2348–2354
   PubMed Web of Science ®Google Scholar
• Swaminathan S, Fonseca VA, Alam MG, Shah SV. The role of iron in diabetes and its complications. Diabetes Care 2007; 30: 1926–1933
   PubMed Web of Science ®Google Scholar
• Sulieman M, Asleh R, Cabantchik ZI, Breuer W, Aronson D, Sulieman A, Miller-Lotan R, Hammerman H, Levy AP. Serum chelatable redox-active iron is an independent predictor of mortality after myocardial infarction in individuals with diabetes. Diabetes Care 2004; 27: 2730–2732
   Google Scholar
• Lee DH, Liu DY, Jacobs DR, Jr, Shin HR, Song K, Lee IK, Kim B, Hider RC. Common presence of non-transferrin-bound iron among patients with type 2 diabetes. Diabetes Care 2006; 29: 1090–1095
   PubMedGoogle Scholar
• Witko-Sarsat V, Friedlander M, Capeillere-Blandin C, Nguyen-Khoa T, Thu Nguyen A, Zingraff J, Jungers P, Descamps-Latsca B. Advanced oxidation protein products as a novel marker of oxidative stress in uremia. Kidney Int 1996; 49: 1304–1313
   PubMed Web of Science ®Google Scholar
• American Diabetes Association. Nutrition recommendations and interventions for diabetes-2006: A position statement of the American Diabetes Association. Diabetes Care 2006;29:2140–2157.
   PubMed Web of Science ®Google Scholar
• Evelyn KA, Malloy HT. Microdetermination of oxyhemoglobin, methemoglobin and sulfhemoglobin in a single sample of blood. J Biol Chem 1938; 26: 655–662
   Google Scholar
• Dodge TG, Mitchell RG, Hanahan DJ. The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Arch Biochem Biophys 1963; 100: 119–130
   PubMed Web of Science ®Google Scholar
• Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. J Biol Chem 1951; 193: 265–275
   PubMed Web of Science ®Google Scholar
• Laemmli UK. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 1970; 227: 680–685
   PubMed Web of Science ®Google Scholar
• Towbin H, Staehlin R, Fordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 1979; 6: 4350–4354
   Google Scholar
• Nourooz-Zadeh J, Gopaul NK, Barrow S, Mallet AI, Anggård EE. Analysis of F2-isoprostanes as indicators of non-enzymatic lipid peroxidation in vivo by gas chromatography-mass spectrometry: development of a solid-phase extraction procedure. J Chromatogr B Biomed Appl 1995; 667: 199–208
   PubMed Web of Science ®Google Scholar
• Signorini C, Comporti M, Giorgi G. Ion trap tandem mass spectrometric determination of F2-isoprostanes. J Mass Spectrom 2003; 38: 1067–1074
   PubMed Web of Science ®Google Scholar
• Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72: 248–254
   PubMed Web of Science ®Google Scholar
• Kay MMB, Goodman SR, Sorensen K, Whitfield CF, Wong P, Zaki L, Rudloff V. Senescent cell antigen is immunologically related to band 3. Proc Natl Acad Sci USA 1983; 80: 1631–1635
   PubMed Web of Science ®Google Scholar
• Hornig R, Lutz HU. Band 3 protein clustering on human erythrocytes promotes binding of naturally occurring anti-band 3 and anti-spectrin antibodies. Exp Gerontol 2000; 35: 1025–1044
   Google Scholar
• Low PS. Role of hemoglobin denaturation and band 3 clustering in initiating red cell removal. Adv Exp Med Biol 1991; 307: 173–183
   PubMedGoogle Scholar
• Arese P, Turrini F, Schwarzer E. Band 3/complement-mediated recognition and removal of normally senescent and pathological human erythrocytes. Cell Physiol Biochem 2005; 16: 133–146
   PubMed Web of Science ®Google Scholar
• Ciccoli L, Rossi V, Leoncini S, Signorini C, Blanco-Garcia J, Aldinucci C, Buonocore G, Comporti M. Iron release, superoxide production and binding of autologous IgG to band 3 dimers in newborn and adult erythrocytes exposed to hypoxia and hypoxia-reoxygenation. Biochim Biophys Acta 2004; 1672: 203–213
   PubMed Web of Science ®Google Scholar
• Nagababu E, Ramasamy S, Rifkind JM. Site-specific cross-linking of human and bovine hemoglobins differentially alters oxygen binding and redox side reactions producing rhombic heme and heme degradation. Biochemistry 2002; 41: 7407–7415
   PubMed Web of Science ®Google Scholar
• Repka T, Shalev O, Reddy R, Yuan J, Abrahmov A, Rachmilewitz EA, Low PS, Hebbel RP. Nonrandom association of free iron with membranes of sickle and β-thalassemic erythrocytes. Blood 1993; 82: 3204–3210
   PubMed Web of Science ®Google Scholar
• Browne P, Shalev O, Hebbel RB. The molecular pathobiology of cell membrane iron: the sickle red cell as a model. Free Radic Biol Med 1998; 24: 1040–1048
   PubMed Web of Science ®Google Scholar
• Kar M, Chakraborti AS. Release of iron from haemoglobin—a possible source of free radicals in diabetes mellitus. Indian J Exp Biol 1999; 37: 190–192
   PubMedGoogle Scholar
• Sen S, Kar M, Roy A, Chakraborti AS. Effect of nonenzymatic glycation on functional and structural properties of hemoglobin. Biophys Chem 2005; 113: 289–298
   PubMed Web of Science ®Google Scholar
• Cussimanio BL, Booth AA, Todd P, Hudson BG, Kahlifah RG. Unusual susceptibility of heme proteins to damage by glucose during non-enzymatic glycation. Biophys Chem 2003; 105: 743–755
   PubMed Web of Science ®Google Scholar
• Gutteridge JM, Rowley DA, Halliwell B. Superoxide-dependent formation of hydroxyl radicals in the presence of iron salts. Detection of ‘free’ iron in biological systems by using bleomycin-dependent degradation of DNA. Biochem J 1981; 199: 263–265
   PubMed Web of Science ®Google Scholar
• Yuan XM, Li W. The iron hypothesis of atherosclerosis and its clinical impact. Ann Med 2003; 35: 578–591
   PubMed Web of Science ®Google Scholar
• Gopaul NK, Anggård EE, Mallet AI, Betteridge DJ, Wolff SP, Nourooz-Zadeh J. Plasma 8-epi-PGF2 alpha levels are elevated in individuals with non-insulin dependent diabetes mellitus. FEBS Lett 1995; 368: 225–229
   PubMed Web of Science ®Google Scholar
• Salahudeen AK, Oliver B, Bower JD, Roberts LJ II. Increase in plasma esterified F2-isoprostanes following intravenous iron infusion in patients on hemodialysis. Kidney Int 2001; 60: 1525–1531
   PubMed Web of Science ®Google Scholar
• Signorini C, Perrone S, Sgherri C, Ciccoli L, Buonocore G, Leoncini S, Rossi V, Vecchio D, Comporti M. Plasma esterified F2-Isoprostanes and oxidative stress in newborns. Role of non protein bound iron. Pediat Res 2008; 63: 287–291
   PubMed Web of Science ®Google Scholar
• Devaraj S, Hirany SV, Burk RF, Jialal I. Divergence between LDL oxidative susceptibility and urinary F(2)-isoprostanes as measures of oxidative stress in type 2 diabetes. Clin Chem 2001; 47: 1974–1979
   PubMed Web of Science ®Google Scholar
• Feillet-Coudray C, Choné F, Michel F, Rock E, Thiéblot P, Rayssiguier Y, Tauveron I, Mazur A. Divergence in plasmatic and urinary isoprostane levels in type 2 diabetes. Clin Chim Acta 2002; 324: 25–30
   Google Scholar
• Selmeci L, Seres L, Antal M, Lukacs J, Regoly-Merei A, Acsady G. Advanced oxidation protein products (AOPP) for monitoring oxidative stress in critically ill patients: a simple, fast and inexpensive automated technique. Clin Chem Lab Med 2005; 43: 294–297
   PubMed Web of Science ®Google Scholar
• Kalousova M, Skrha J, Zima T. Advanced glycation end-products and advanced oxidation protein products in patients with diabetes mellitus. Physiol Res 2002; 51: 597–604
   PubMed Web of Science ®Google Scholar