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dc.contributor.authorPieniazek, Anna
dc.contributor.authorGwozdzinski, Krzysztof
dc.description.abstractThe aim of this study was to evaluate the properties of internal components of erythrocytes in chronic renal failure (CRF) patients undergoing hemodialysis (HD) in comparison to control subjects. For investigation of conformational state of hemoglobin and nonheme proteins (NHP) the maleimide spin label (MSL) in electron paramagnetic resonance (EPR) was applied. The studies were performed using MSL in whole cells and hemolysate as well as proteins separated by ion exchange chromatography and checked by electrophoresis. Additionally the level of –SH groups in hemolysate and isolated internal proteins of CRF erythrocytes was determined using 4,4′-dithiodipyridine. All measurements were performed before and after hemodialysis. Oxidative stress accompanying CRF/hemodialysed patients caused a significant decrease in the mobility of internal components inside erythrocytes indicated by MSL (P < 0.02). The significant decrease in mobility of spin labeled HbA1c and HbA both before and after HD (P < 0.0002) as well as in nonheme proteins before hemodialysis (P < 0.05) versus control was indicated. Decrease in mobility of internal components of erythrocytes was accompanied by loss of thiols before and after hemodialysis versus control in NHP (P < 0.05), HbA1c (P < 0.0002), and HbA (P < 0.0005). These findings showed oxidative influence of hemodialysis on hemoglobins and internal nonheme proteins in erythrocytes of CRF patients.pl_PL
dc.publisherHindawi Publishing Corporationpl_PL
dc.relation.ispartofseriesOxidative Medicine and Cellular Longevity;Volume 2015 (2015), Article ID 783073
dc.rightsUznanie autorstwa 3.0 Polska*
dc.titleChanges in the Conformational State of Hemoglobin in Hemodialysed Patients with Chronic Renal Failurepl_PL
dc.contributor.authorAffiliationUniversity of Lodz, Faculty of Biology and Environmental Protectionpl_PL
dc.referencesZ. Hambali, Z. Ahmad, S. Arab, and H. Khazaai, “Oxidative stress and its association with cardiovascular disease in chronic renal failure patients,” Indian Journal of Nephrology, vol. 21, no. 1, pp. 21–25, 2011.pl_PL
dc.referencesA. Popolo, G. Autore, A. Pinto, and S. Marzocco, “Oxidative stress in patients with cardiovascular disease and chronic renal failure,” Free Radical Research, vol. 47, no. 5, pp. 346–356, 2013pl_PL
dc.referencesJ. Himmelfarb, J. M. Lazarus, and R. Hakim, “Reactive oxygen species production by monocytes and polymorphonuclear leukocytes during dialysis,” American Journal of Kidney Diseases, vol. 17, no. 3, pp. 271–276, 1991.pl_PL
dc.referencesK. N. Ekdahl, J. D. Lambris, H. Elwing et al., “Innate immunity activation on biomaterial surfaces: a mechanistic model and coping strategies,” Advanced Drug Delivery Reviews, vol. 63, no. 12, pp. 1042–1050, 2011.pl_PL
dc.referencesF. Antolini, F. Valente, D. Ricciardi, M. Baroni, and R. M. Fagugli, “Principal component analysis of some oxidative stress parameters and their relationships in hemodialytic and transplanted patients,” Clinica Chimica Acta, vol. 358, no. 1-2, pp. 87– 94, 2005.pl_PL
dc.referencesJ. Valentini, D. Grotto, C. Paniz, M. Roehrs, G. Burg, and S. C. Garcia, “The influence of the hemodialysis treatment time under oxidative stress biomarkers in chronic renal failure patients,” Biomedicine and Pharmacotherapy, vol. 62, no. 6, pp. 378–382, 2008.pl_PL
dc.referencesA. Pieniazek, J. Brzeszczynska, I.Kruszynska, andK.Gwozdzinski, “Investigation of albumin properties in patients with chronic renal failure,” Free Radical Research, vol. 43, no. 10, pp. 1008–1018, 2009.pl_PL
dc.referencesT. Nguyen-Khoa, Z. A. Massy, J. Pascal De Bandt et al., “Oxidative stress and haemodialysis: role of inflammation and duration of dialysis treatment,” Nephrology Dialysis Transplantation, vol. 16, no. 2, pp. 335–340, 2001pl_PL
dc.referencesG. Cao and R. L. Prior, “Measurement of oxygen radical absorbance capacity in biological samples,” Methods in Enzymology, vol. 299, pp. 50–62, 1998.pl_PL
dc.referencesM. G. Rico, M. J. Puchades, R. G. Ram´on, G. S´aez, M. C. Tormos, and A. Miguel, “Effect of oxidative stress in patients with chronic renal failure,” Nefrologia, vol. 26, no. 2, pp. 218– 225, 2006pl_PL
dc.referencesC. Libetta, V. Sepe, P. Esposito, F. Galli, and A. Dal Canton, “Oxidative stress and inflammation: implications in uremia and hemodialysis,” Clinical Biochemistry, vol. 44, no. 14-15, pp. 1189– 1198, 2011.pl_PL
dc.referencesJ. Stepniewska, B. Dolegowska, K. Ciechanowski, E. Kwiatkowska, B.Millo, and D. Chlubek, “Erythrocyte antioxidant defense system in patients with chronic renal failure according to the hemodialysis conditions,” Archives of Medical Research, vol. 37, no. 3, pp. 353–359, 2006.pl_PL
dc.referencesJ. Witkowska, J. Bober, and D. Chlubek, “Changes in the lipid content of erythrocytes in patients with chronic renal failure,” Annales Academiae Medicae Stetinensis, vol. 53, no. 2, pp. 46– 51, 2007.pl_PL
dc.referencesJ. Brzeszczynska, M. Luciak, and K. Gwozdzinski, “Alterations of erythrocyte structure and cellular susceptibility in patients with chronic renal failure: effect of haemodialysis and oxidative stress,” Free Radical Research, vol. 42, no. 1, pp. 40–48, 2008.pl_PL
dc.referencesM.Olszewska, J.Wiatrow, J. Bober et al., “Oxidative stress modulates the organization of erythrocyte membrane cytoskeleton,” Postepy Higieny i Medycyny Doswiadczalnej, vol. 66, pp. 534– 542, 2012.pl_PL
dc.referencesG. Stoya, A. Klemm, E. Baumann et al., “Determination of autofluorescence of red blood cells (RBCs) in uremic patients as a marker of oxidative damage,” Clinical Nephrology, vol. 58, no. 3, pp. 198–204, 2002.pl_PL
dc.referencesN. Srivastava, R. K. Sharma, N. Singh, and B. Sharma, “Acetylcholinesterase from human erythrocytes membrane: a screen for evaluating the activity of some traditional plant extracts,” Cellular and Molecular Biology, vol. 58, no. 1, pp. 160–169, 2012.pl_PL
dc.referencesE.Costa, S. Rocha, P. Rocha-Pereira et al., “Changes in red blood cells membrane protein composition during hemodialysis procedure,” Renal Failure, vol. 30, no. 10, pp. 971–975, 2008.pl_PL
dc.referencesM. H. Antonelou, A. G. Kriebardis, A. D. Velentzas, A. C. Kokkalis, S.-C. Georgakopoulou, and I. S. Papassideri, “Oxidative stress-associated shape transformation and membrane proteome remodeling in erythrocytes of end stage renal disease patients on hemodialysis,” Journal of Proteomics, vol. 74, no. 11, pp. 2441–2452, 2011.pl_PL
dc.referencesR. B. Bhogade, A. N. Suryakar, N. G. Joshi, and R. Y. Patil, “Effect of vitamin E supplementation on oxidative stress in hemodialysis patients,” Indian Journal of Clinical Biochemistry, vol. 23, no. 3, pp. 233–237, 2008.pl_PL
dc.referencesD. Kivelson, “Theory of ESR linewidths of free radicals,” The Journal of Chemical Physics, vol. 33, no. 4, pp. 1094–1106, 1960.pl_PL
dc.referencesA. Keith, G. Bulfield, and W. Snipes, “Spin-labeled neurospora mitochondria,” Biophysical Journal, vol. 10, no. 7, pp. 618–629, 1970.pl_PL
dc.referencesD. L. Drabkin, “Spectrophotometric studies; the crystallographic and optical properties of the hemoglobin of man in comparison with those of other species,” The Journal of Biological Chemistry, vol. 164, no. 2, pp. 703–723, 1946.pl_PL
dc.referencesT. H. J. Huisman, E. A. Martis, and A. Dozy, “Chromatography of hemoglobin types on carboxymethylcellulose,” The Journal of Laboratory and Clinical Medicine, vol. 52, no. 2, pp. 312–327, 1958.pl_PL
dc.referencesO. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall, “Protein measurement with the Folin phenol reagent,” The Journal of Biological Chemistry, vol. 193, no. 1, pp. 265–275, 1951.pl_PL
dc.referencesK. Gwozdzinski, “A spin label study of the action of cupric and mercuric ions on human red blood cells,” Toxicology, vol. 65,no. 3, pp. 315–323, 1991.pl_PL
dc.referencesL. J. Berliner, “The spin-label approach to labeling membrane protein sulfhydryl groups,” Annals of the New York Academy of Sciences, vol. 414, pp. 153–161, 1983.pl_PL
dc.referencesS. Ogawa and H. M. McConnell, “Spin-label study of hemoglobin conformations in solution,” Proceedings of the National Academy of Sciences of the United States of America, vol. 58, no. 1, pp. 19–26, 1967.pl_PL
dc.referencesS. Jaisson, C. Pietrement, and P. Gillery, “Carbamylationderived products: bioactive compounds and potential biomarkers in chronic renal failure and atherosclerosis,” Clinical Chemistry, vol. 57, no. 11, pp. 1499–1505, 2011.pl_PL
dc.referencesD. Sakota, R. Sakamoto, H. Sobajima et al., “Mechanical damage of red blood cells by rotary blood pumps: selective destruction of aged red blood cells and subhemolytic trauma,” Artificial Organs, vol. 32, no. 10, pp. 785–791, 2008.pl_PL
dc.referencesH.-D. Polaschegg, “Red blood cell damage from extracorporeal circulation in hemodialysis,” Seminars in Dialysis, vol. 22, no. 5, pp. 524–531, 2009.pl_PL
dc.referencesJ. P. Cristol, B. Canaud,H. Rabesandratana, I. Gaillard, A. Serre, and C.Mion, “Enhancement of reactive oxygen species production and cell surface markers expression due to haemodialysis,” Nephrology Dialysis Transplantation, vol. 9, no. 4, pp. 389–394, 1994pl_PL
dc.referencesM. Bonomini, S. Stuard, M. P. Carreno et al., “Neutrophil reactive oxygen species production during hemodialysis: role of activated platelet adhesion to neutrophils through P-selectin,” Nephron, vol. 75, no. 4, pp. 402–411, 1997.pl_PL
dc.referencesK. Gwozdzinski and M. Janicka, “Oxygen free radicals and red blood cell damage in acute renal failure,” Biochemical Society Transactions, vol. 23, no. 4, p. 635S, 1995.pl_PL
dc.referencesK. Gwo´zdzi´nski, M. Janicka, J. Brzeszczy´nska, and M. Luciak, “Changes in red blood cell membrane structure in patients with chronic renal failure,” Acta Biochimica Polonica, vol. 44, no. 1, pp. 99–108, 1997.pl_PL
dc.referencesV. Jeney, J. W. Eaton, G. Balla, and J. Balla, “Natural history of the bruise: formation, elimination, and biological effects of oxidized hemoglobin,” Oxidative Medicine and Cellular Longevity, vol. 2013, Article ID703571, 9 pages, 2013.pl_PL
dc.referencesD. Daveloose, G. Fabre, F. Berleur, G. Testylier, and F. Leterrier, “A new spin label method for the measurement of erythrocyte internal microviscosity,” Biochimica et Biophysica Acta, vol. 763, no. 1, pp. 41–49, 1983.pl_PL
dc.referencesR. Sharma and B. R. Premachandra, “Membrane-bound hemoglobin as a marker of oxidative injury in adult and neonatal red blood cells,” Biochemical Medicine and Metabolic Biology, vol. 46, no. 1, pp. 33–44, 1991.pl_PL
dc.referencesS. Ohnishi, J. C. Boeyens, and H. M. McConnell, “Spin-labeled hemoglobin crystals,” Proceedings of the National Academy of Sciences of the United States of America, vol. 56, no. 3, pp. 809– 813, 1966.pl_PL
dc.referencesJ. C. Boeyens and H. M.McConnell, “Spin-labeled hemoglobin,” Proceedings of the National Academy of Sciences of the United States of America, vol. 56, no. 1, pp. 23–25, 1966.pl_PL
dc.referencesP. W. Jia, R. A. Buehler, R. M. Boykins, R. M. Venable, and I. Alayash, “Structural basis of peroxide mediated changes in human hemoglobin: a novel oxidative pathwa,” The Journal of Biological Chemistry, vol. 282, pp. 4894–4907, 2007.pl_PL
dc.referencesS. Harel and J. Kanner, “The generation of ferryl or hydroxyl radicals during interaction of haemproteins with hydrogen peroxide,” Free Radical Research Communications, vol. 5, no. 1, pp. 21–33, 1988.pl_PL
dc.referencesN. B. J. Vollaard, B. J. Reeder, J. P. Shearman, P. Menu, M. T. Wilson, and C. E. Cooper, “A new sensitive assay reveals that hemoglobin is oxidatively modified in vivo,” Free Radical Biology and Medicine, vol. 39, no. 9, pp. 1216–1228, 2005.pl_PL
dc.referencesF. Xu, K. S. Quandt, and D. E. Hultquist, “Characterization of NADPH-dependent methemoglobin reductase as a hemebinding protein present in erythrocytes and liver,” Proceedings of the National Academy of Sciences of the United States of America, vol. 89, no. 6, pp. 2130–2134, 1992.pl_PL
dc.referencesR. Shainkin-Kestenbaum, C. Caruso, and G. M. Berlyne, “Reduced superoxide dismutase activity in erythrocytes of dialysis patients: a possible factor in the etiology of uremic anemia,” Nephron, vol. 55, no. 3, pp. 251–253, 1990.pl_PL
dc.referencesB. Knap, M. Prezelj, J. Buturovi´c-Ponikvar, R. Ponikvar, and A. F. Bren, “Antioxidant enzymes show adaptation to oxidative stress in athletes and increased stress in hemodialysis patients,” Therapeutic Apheresis and Dialysis, vol. 13, no. 4, pp. 300–305, 2009pl_PL
dc.referencesB. J. Reeder and M. T. Wilson, “Hemoglobin and myoglobin associated oxidative stress: from molecular mechanisms to disease states,” Current Medicinal Chemistry, vol. 12, no. 23, pp. 2741–2751, 2005.pl_PL
dc.referencesB. J. Reeder, M. A. Sharpe, A. D. Kay, M. Kerr, K. Moore, and M. T.Wilson, “Toxicity of myoglobin and haemoglobin: oxidative stress in patients with rhabdomyolysis and subarachnoid haemorrhage,” Biochemical Society Transactions, vol. 30, no. 4, pp. 745–748, 2002.pl_PL
dc.referencesK.Goswami andD. Ray, “Putative pathogenic effect of oxidative stress in sickle cell disorder,” Biomedical Research, vol. 22, no. 1, pp. 23–27, 2011.pl_PL
dc.referencesJ. Himmelfarb, E. McMonagle, and E. McMenamin, “Plasma protein thiol oxidation and carbonyl formation in chronic renal failure,” Kidney International, vol. 58,no. 6, pp. 2571–2578, 2000.pl_PL
dc.referencesW.H. F. Sutherland, S. A. de Jong, andR. J.Walker, “Hypochlorous acid and low serum paraoxonase activity in haemodialysis patients: an in vitro study,” Nephrology Dialysis Transplantation, vol. 19, no. 1, pp. 75–82, 2004.pl_PL
dc.referencesA. Amore, R. Bonaudo, D. Ghigo et al., “Enhanced production of nitric oxide by blood-dialysismembrane interaction,” Journal of the American Society of Nephrology, vol. 6, no. 4, pp. 1278– 1283, 1995.pl_PL
dc.referencesR. Radi, G. Peluffo, M. N. Alvarez, M. Naviliat, and A. Cayota, “Unraveling peroxynitrite formation in biological systems,” Free Radical Biology and Medicine, vol. 30, no. 5, pp. 463–488, 2001.pl_PL
dc.referencesZ.Mitrogianni, A. Barbouti,D.Galaris, andK. C. Siamopoulos, “Tyrosine nitration in plasma proteins from patients undergoing hemodialysis,” American Journal of Kidney Diseases, vol. 44, no. 2, pp. 286–292, 2004.pl_PL
dc.referencesI. O. C. Egwim and H. J. Gruber, “Spectrophotometric measurement of mercaptans with 4,4’ -dithiodipyridine,” Analytical Biochemistry, vol. 288, no. 2, pp. 188–194, 2001pl_PL

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Uznanie autorstwa 3.0 Polska
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