Oxidative stress modulates the organization of erythrocyte membrane cytoskeleton

Postepy Higieny i Medycyny Doswiadczalnej

Volumn 66, Issue , 2012, Pages 534-542

  Olszewska, Maria ^a   Wiatrow, Jerzy ^a   Bober, Joanna ^a   Stachowska, Ewa ^a   Gołembiewska, Edyta ^a   Jakubowska, Katarzyna ^a   Stańczyk Dunaj, Małgorzata ^a   Pietrzak Nowacka, Maria ^a  

^a POMERANIAN MEDICAL UNIVERSITY   (Poland)

Author keywords

Cytoskeleton proteins; Erythrocytes; Oxidative stress

Indexed keywords

EID: 84867933468     PISSN: 00325449     EISSN: 17322693     Source Type: Journal    
DOI: 10.5604/17322693.1005677     Document Type: Article

References (61)

1. An X., Guo X., Sum H., Morrow J., Gratzer W., Mohandas N.: Phosphatidylserine binding sites in erythroid spectrin: location and implications for membrane stability. Biochemistry, 2004;43:310-315
2. Andrade J., Pearce S. T., Zhao H., Barroso M.: Interactions among p22, glyceraldehyde-3 phosphate dehydrogenase and microtubules. Biochem. J., 2004;384:327-336
3. Antonelou M. H., Papassideri I. S., Karababa F. J., Stravopodis D. J., Loutradi A., Margaritis L. H.: Defective organization of the erythroid cell membrane in a novel case of congenital anemia. Blood Cells Mol. Dis., 2003;30:43-54
4. Babusikova E., Jesenak M., Racay P., Dobrota D., Kaplan P.: Oxidative alternations in rat heart homogenate and mitochondria during ageing. Gen. Physiol. Biophys., 2008;27:115-120
5. Bennett V.: The spectrin-actin junction of erythrocyte membrane skeletons. Biochim. Biophys. Acta, 1989;988:107-121
6. Bennett V., Baines A. J.: Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues. Physiol. Rev., 2001;81:1353-1392
7. Bober J., Kedzierska K., Safranow K., Kwiatkowska E., Jakubowska K., Herdzik E., Dołegowska B., Domański L., Ciechanowski K.: Influence of glucose in dialyzing fluid on purine concentrations in hemodialyzed patients with chronic renal failure. Nephron. Clin. Pract., 2003;95:c31-c36
8. Bober J., Kwiatkowska E., Kedzierska K., Olszewska M., Dołegowska B., Domanski L., Herdzik E., Ciechanowski K., Chlubek D.: Does glucose present in the dialysate limit oxidative stress in patients undergoing regular hemodialysis? Blood Purif., 2005;23:219-225
9. Bober J., Kwiatkowska E., Kedzierska K., Olszewska M., Gołebiewska E., Stachowska E., Kucharska E., Ciechanowski K., Chlubek D.: Influence of glucose in the dialysate on the activity of erythrocyte-glutathione-peroxidase and blood selenium concentration in hemodialyzed patients. Arch. Med. Res., 2007;38:330-336
10. Bratosin D., Mazurier J., Tissier J. P., Estaquier J., Huart J. J., Ameisen J. C., Aminoff D., Montreuil J.: Cellular and molecular mechanisms of senescent erythrocyte phagocytosis by macrophages. A review. Biochimie, 1998;80:173-195
11. Caprari P., Bozzi A., Malorni W., Bottini A., Iosi F., Santini M. T., Salvati A. M.: Junctional sites of erythrocyte skeletal proteins are specific targets of tert-butylhydroperoxide oxidative damage. Chem. Biol. Interact., 1995;94:243-258
12. Celedón G., González G., Lissi E. A., Hidalgo G.: Free radical-induced protein degradation of erythrocyte membrane is influenced by the localization of radical generation. IUBMB Life, 2001;51:377-380
13. Chakrabarti A., Kelkar D. A., Chattopadhyay A.: Spectrin organization and dynamics: new insights. Biosci. Rep., 2006;26:369-386
14. Chattopadhyay A., Rawat S. S., Kelkar D. A., Ray S., Chakrabarti A.: Organization and dynamics of tryptophan residues in erythroid spectrin: novel structural features of denatured spectrin revealed by the wavelength-selective fluorescence approach. Protein Sci., 2003;12:2389-2403
15. Cibulka R., Racek J.: Metabolic disorders in patients with chronic kidney failure. J. Physiol. Res., 2007;56:697-705
16. Cooke M. S., Henderson P. T., Evans M. D.: Sources of extracellular, oxidatively-modified DNA lesions: implications for their measurement in urine. J. Clin. Biochem. Nutr., 2009;45:255-270
17. Daschner M., Lenhartz H., Bötticher D., Schaefer F., Wollschläger M., Mehls O., Leichsenring M.: Influence of dialisys on plasma lipid peroxidation products and antioxidant levels. Kidney Int., 1996;50:1268-1272
18. Dean R. T., Fu S., Stocker R., Davies M. J.: Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J., 1997;324:1-18
19. Delaunay J.: Molecular basis of red cell membrane disorders. Acta Haematol., 2002;108:210-218
20. Delaunay J., Alloisio N., Morle L., Baklouti F., Dalla Venezia N., Maillet P., Wilmotte R.: Molecular genetics of hereditary elliptocytosis and hereditary spherocytosis. Ann. Genet., 1996;39:209-221
21. Di Mascio P., Dewez B., Garcia C. R.: Ghost protein damage by peroxynitrite and its protection by melatonin. Braz. J. Med. Biol. Res., 2000;33:11-17
22. Dodge J. T., Mitchell C., Hanahan D.: The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Arch. Biochem. Biophys., 1963;100:119-130
23. Dołegowska B., Stepniewska J., Ciechanowski K., Safranow K., Millo B., Bober J., Chlubek D.: Does glucose in dialysis fluid protect erythrocytes in patients with chronic renal failure? Blood Purif., 2007;25:422-429
24. Dykens J. A., Sullivan S. G., Stern A.: Glucose metabolism and hemoglobin reactivity in human red blood cells exposed to the tryptophan metabolites 3-hydroxyanthranilate, quinolinate and picolinate. Biochem. Pharmacol., 1989;38:1555-1562
25. Esterbauer H., Schaur R. J., Zollner H.: Chemistry and biology of 4-hydroxynonenal, malonylaldehyde and related aldehydes. Free Radic. Biol. Med., 1991;11:81-128
26. Gallagher P. G.: Red cell membrane disorders. Hematology ASH Education Book, 2005;1:13-18
27. Gallagher P. G., Ferriera J. D.: Molecular basis of erythrocyte membrane disorders. Curr. Opin. Hematol., 1997;4:128-135
28. Galli F.: Protein damage and inflammation in uraemia and dialysis patients. Nephrol. Dial. Transplant., 2007;22(Suppl.5):20-36
29. Greenwalt T. J., Dumaswala U. J.: Effect of red cell age on vesiculation in vitro. Br. J. Haematol., 1988;68:465-467
30. Guedes S., Vitorino R., Domingues R., Amado F., Domingues P.: Oxidation of bovine serum albumin: identification of oxidation products and structural modifications. Rapid Commun. Mass Spectrom., 2009;23:2307-2315
31. Gwoździński K., Janicka M., Brzeszczyńska J., Luciak M.: Changes in red blood cell membrane structure in patients with chronic renal failure Acta Biochim. Pol., 1997;44:99-107
32. Himmelfarb J., McMonagle E., McMenamin E.: Plasma protein thiol oxidation and carbonyl formation in chronic renal failure. Kidney Int., 2000;58:2571-2578
33. Jollow D. J., McMillan D. C.: Oxidative stress, glucose-6-phosphate dehydrogenase and the red cell. Adv. Exp. Med. Biol., 2001;500:595-605
34. Kim K. M., Jung B. H., Paeng K. J., Kim S. W., Chung B. C.: Alteration of plasma total F2-isoprostanes before and after hemodialysis in end-stage renal disease patients. Prostaglandins Leukot. Essent. Fatty Acids, 2004;70:475-478
35. Kuypers F. A., Yuan J., Lewis R. A., Snyder L. M., Kiefer C. R., Bunyaratvej A., Funcharoen S., Ma L., Styles L., de Jong K., Schrier S. L.: Membrane phospholipid asymmetry in human thalassemia. Blood, 1998;91:3044-3051
36. Laemmli U. K.: Cleavage of structural proteins during the assembly of the head of acteriophage T4. Nature, 1970;227:680-685
37. Liu S. C., Yi S. J., Mehta J. R., Nichols P. E., Ballas S. K., Yacono P. W., Golan D. E., Palek J.: Red cell membrane remodeling in sickle cell anemia. Sequestration of membrane lipids and proteins in Heinz bodies. J. Clin. Invest., 1996;97:29-36
38. Low P. S., Rathinavelu P., Harrison M. L.: Regulation of glycolysis via reversible enzyme binding to the membrane protein, band 3. J. Biol. Chem., 1993;268:14627-14631
39. Low P. S., Waugh S. M., Zinke K., Drenckhahn D.: The role of hemoglobin denaturation and band 3 clustering in red blood cell aging. Science, 1985;227:531-533
40. Margetis P., Antonelou M., Karababa F., Loutradi A., Margaritis L., Papassideri I.: Cells physiologically important secondary modifications of red cell membrane in hereditary spherocytosis-evidence for in vivo oxidation and lipid rafits protein variations. Blood Cells Mol. Dis., 2007;38:210-220
41. Mazhul V., Shcherbin D., Zavodnik I., Rekawiecka K., Bryszewska M.: The effect of oxidative stress induced by t-butyl hydroperoxide on the structural dynamics of membrane proteins of Chinese hamster fibroblasts. Mol. Cell. Biol. Int., 1999;23:345-350
42. Mohandas N., An X.: New insights into function of red cell membrane proteins and their interaction with spectrin-based membrane skeleton. Transfus. Clin. Biol., 2006;13:29-30
43. Morrison M., Jackson C. W., Mueller T. J., Huang T., Dockter M. E., Walker W. S., Singer J. A., Edwards H. H.: Does cell density correlate with red cell age? Biomed. Biochim. Acta, 1983;42:S107-S111
44. Neumann, C. A., Krause D. S., Carman C. V., Das S., Dubey D. P., Abraham J. L., Bronson R. T., Fujiwara Y., Orkin S. H., Van Etten R. A.: Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression. Nature, 2003;424:561-565
45. Ohanian V., Wolfe L. C., John K. M., Pinder J. C., Lux S. E., Gratzer W. B.: Analysis of the ternary interaction of the red cell membrane skeletal proteins spectrin, actin, and 4.1. Biochemistry, 1984;23:4416-4420
46. Okamoto K., Maruyama T., Kaji Y., Harada M., Mawatari S., Fujino T., Uyesaka N.: Verapamil prevents impairment in filterability of human erythrocytes exposed to oxidative stress. Jpn. J. Physiol., 2004;54:39-46
47. Palek J., Liu S. C., Snyder L. M.: Metabolic dependence of protein arrangement in human erythrocyte membranes. I. Analysis of spectrin-rich complexes in ATP-depleted red cells. Blood, 1978;51:385-395
48. Pandolfi P. P., Sonati F., Rivi R., Mason P., Grosveld F., Luzzatto L.: Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress. EMBO J., 1995;14:5209-5215
49. Reliene R., Mariani M., Zanella A., Reinhart W. H., Ribeiro M. L., del Giudice E. M., Perrotta S., Iolascon A., Eber S., Lutz H. U.: Splenectomy prolongs in vivo survival of erythrocytes differently in spectrin/ankyrin-and band 3-deficient hereditary spherocytosis. Blood, 2002;100:2208-2215
50. Rocha S., Rebelo I., Costa E., Catarino C., Belo L., Castro E. M., Cabeda J. M., Barbot J., Quintanilha A., Santos-Silva A.: Protein deficiency balance as a predictor of clinical outcome in hereditary spherocytosis. Eur. J. Haematol., 2005;74:374-380
51. Rogalski A. A., Steck T. L., Waseem A.: Association of glyceraldehyde-3-phosphate dehydrogenase with the plasma membrane of the intact human red blood cell. J. Biol. Chem., 1989;264:6438-6446
52. Rybicki A. C., Heath R., Lubin B., Schwartz R. S.: Human erythrocyte protein 4.1 is a phosphatidylserine binding protein. J. Clin. Invest., 1988;81:255-260
53. Snyder L. M., Fairbanks G., Trainor J., Fortier N. L., Jacobs J. B., Leb L.: Properties and characterization of vesicles released by young and old human red cells. Br. J. Haematol., 1985;59:513-522
54. Srour M. A., Bilto Y. Y., Juma M.: Susceptibility of erythrocytes from non-insulin-dependent diabetes mellitus and hemodialysis patients, cigarette smokers and normal subject to in vitro oxidative stress and loss of deformability. Clin. Hemorheol. Microcirc., 2000;22:173-180
55. Tankiewicz A., Pawlak D., Pawlak K., Szewc D., Myśliwiec M., Buczko W.: Anthranilic acid-urae mic toxin damaged red cell's membrane. Int. Urol. Nephrol., 2005;37:621-627
56. Tanner M. J.: Band 3 anion exchanger and its involvement in erythrocyte and kidney disorders. Curr. Opin. Hematol., 2002;9:133-139
57. Turrini F., Arese P., Yuan J., Low P. S.: Clustering of integral membrane proteins of the human erythrocyte membrane stimulates autologous IgG binding, complement deposition, and phagocytosis. J. Biol. Chem., 1991;266:23611-23617
58. Waugh S. M., Walder J. A., Low P. S.: Partial characterization of the copolymerization reaction of erythrocyte membrane band 3 with hemichromes. Biochemistry, 1987;26:1777-1783
59. Weiss G., Schroecksnadel K., Mattle V., Winkler C., Konwalinka G., Fuchs D.: Possible role of cytokine-induced tryptophan degradation in anaemia of infammation. Eur. J. Haematol., 2004;72:130-134
60. Yawata Y., Jacob H. S.: Abnormal red cell metabolism in patients with chronic uremia: nature of the defect and its persistencedespite adequate hemodialysis. Blood, 1975;2:231-239
61. Zinkham W. H., Houtchens R. A., Caughey W. S.: Relation between variations in the phenotypic expression of an unstable hemoglobin disorder (hemoglobin Zurich) and carboxyhemoglobin levels. Am. J. Med., 1983;74:23-29