Molecular changes in erythrocyte membranes induced by nitroimidazoles and radiation

Polish Journal of Pharmacology

Volumn 48, Issue 3, 1996, Pages 269-280

  Rybczyńska, Maria ^a   Hoffmann, Stanisław K ^b   Goslar, Janina ^b  

^a POZNAN UNIVERSITY OF MEDICAL SCIENCES   (Poland)

^b INSTITUTE OF MOLECULAR PHYSICS   (Poland)

Author keywords

Band 3 protein; Electron spin resonance (ESR); Erythrocyte membrane; Gamma irradiation; Nitroimidazoles

Indexed keywords

3 MALEIMIDOMETHYL 2,2,5,5 TETRAMETHYLPYRROLIDINE 1 OXYL; 4 MALEIMIDO 2,2,6,6 TETRAMETHYLPIPERIDINE 1 OXYL; MALEIMIDE DERIVATIVE; MISONIDAZOLE; NITROIMIDAZOLE DERIVATIVE; PROTEIN; THIOL GROUP; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; ERYTHROCYTE MEMBRANE; GAMMA IRRADIATION; HUMAN; HUMAN TISSUE; LIPID PEROXIDATION; MEMBRANE DAMAGE; MOLECULAR WEIGHT; OXIDATIVE STRESS; POLYACRYLAMIDE GEL ELECTROPHORESIS; RADIOSENSITIVITY; SPIN LABELING;

CYCLIC N-OXIDES; DENSITOMETRY; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; ERYTHROCYTE MEMBRANE; GAMMA RAYS; HUMANS; LIPID PEROXIDATION; NITROIMIDAZOLES; SPIN LABELS;

EID: 0029811375     PISSN: 12306002     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (33)

1. Barber M. J., Rosen G., Rauckman E. J.: Studies of the mobility of maleimide spin labels within the erytlirocyte membrane. Biochim. Biophys. Acta, 1983, 732, 126-132.
2. Beppu M., Inoue M., Ishikawa T., Kikugawa K.: Presence of membrane-bound proteinases that preferentially degrade oxidatively damaged erythrocyte membrane proteins as secondary oxidant defence. Biochim. Biophys. Acta, 1994, 1196, 81-87.
3. Berliner I. J.: Spin Labeling Theory and Application, Academic Press, New York, 1979, vol. I, II.
4. Butterfield D. A., Roses A. D., Appel S. H., Chesnut D. B.: Electron spin resonance studies of membrane proteins in erythrocytes in myotonic muscular dystrophy. Arch. Biochem. Biophys., 1976, 177, 226-234.
5. Butterfield D. A.: Electron spin resonance investigations of membrane proteins in erythrocytes in muscle diseases: duchenne and myotonic muscular dystrophy and congenital myotonia. Biochim. Biophys. Acta, 1977, 470, 1-7.
6. Butterfield D. A., Braden M. L., Markesbery W. R.: Erythrocyte membrane alterations in Huntington disease: effects of γ-aminobutyric acid. J. Supramol. Struct., 1987, 9, 125-130.
7. Cohen C. H., Dotimas E., Korsgren C.: Human erythrocyte membrane protein band 4.2 (Palladin). Semin. Hematol., 1993, 30, 119-137.
8. Erriu G., Onnis S., Randaccio P., Gori C., Schianchi G.: EPR and DSC comparative study of phase separation in γ-irradiated lipid membranes. Lett. Nuovo Cimento, 1985, 44, 51-57.
9. Fairbanks G., Steck T. L., Wallach D. F. H.: Electrophoretic analysis of major polipeptides of the human erythrocyte membrane. Biochemistry, 1971, 10, 2602-2617.
10. Farmer B. T., Nicholas M. M., Butterfield D. A.: The alteration of membrane protein in human erythrocyte membranes induced by quinolinic acid, an endogenous neurotoxin. Correlation of effect with structure. Biochim. Biophys. Acta, 1984, 778, 260-268.
11. Farmer B. T., Harmon T. M., Butterfield D. A.: ESR studies of erythrocyte membrane skeletal protein network: influence of the state of aggregation of spectrin on the physical state of membrane proteins, bilayer lipids and cell surface carbohydrates. Biochim. Biophys. Acta, 1985, 821, 420-430.
12. Gilligan D. M., Bennett V.: The junctional complex of the membrane skeleton. Semin. Hematol., 1993, 30, 74-83.
13. Girroti A., Thomas J. P.: Damaging effect of oxygen radicals on resealed erythrocytes ghosts. J. Biol. Chem., 1984, 259, 1744-1752.
14. Guille J., Raison J. K., Gebicki J. M.: Radiation-induced lipid peroxidation and the fluidity of erythrocyte membrane lipids. Free Radical Biol. Med., 1987, 3, 147-152.
15. Kondo T., Fukushima Y., Kon H., Riesz P.: Effect of shear stress and free radicals induced by ultrasound on erythrocyte. Arch. Biochem. Biophys., 1989, 269, 381-389.
16. Kraemer D., Koog R., Friedrischs B., Drenckhahn D.: Two novel peripheral membrane proteins, pasin 1 and pasin 2, associated with NaK-ATPase in various cells and tissues. J. Cell Biol., 1989,111, 2375-2383.
17. 2+-mediated crosslinking of erythrocyte proteins. Proc. Nat. Acad. Sci. USA, 1976, 73, 4479-4481.
18. Lowry O. H., Rosenbrough N., Farr A., Randal J.: Protein measurement with the folin phenol reagent. J. Biol. Chem., 1951, 193, 156-257.
19. Mattayoshi E. D., Sawyer W. H., Jovin T. H.: Rotational diffusion of band 3 in erythrocyte membranes. 2. Binding of cytoplasmic enzymes. Biochemistry, 1991, 30, 3538-3543.
20. Miller G., Raleich J. A.: Action of some radical scavengers on radiation-induced haemolysis. Int. J. Radiât. Biol., 1983, 43, 911-919.
21. O'Neil P., Jenkins T. C.: Electron-transfer reactions of nitroxyl radicals with one-electron reduced quinones and viologens. J. Chem. Soc., Faraday Transactions I, 1977, 1912-1918.
22. Palmieri D. A., Butterfield D. A.: Structure activity investigation of the alteration of the physical state of skeletal network of proteins in human erythrocyte membranes induced by 9-amino-l,2,3,4-tetrahydroacridine. Biochim. Biophys. Acta, 1990, 1024, 285-288.
23. Parasassi T., Sapora O., Giust I. A. M., De Stasio G., Ravagnan G.: Alterations in erythrocyte membrane lipids induced by low doses of ionizing radiation as revealed by 1,6-dipheny1-1,3,5-hexatriene fluorescence lifetime. Int. J. Radiat. Biol, 1991, 59, 59-69.
24. Rybczyńska M.: The evaluation of erythrocyte membrane response to combined treatment of radiation and nitroimidazoles. Int. J. Radiat. Biol., 1990, 58, 2, 313-323.
25. Rybczyńska M., Csordas A.: Interaction of free fatty acids with erythrocyte membrane as affected by hyperthermia and ionizing radiation. Biosci. Rep., 1990, 10, 155-163.
26. Rybczyńska M., Feo C., Marden M., Poyart C.: Abnormal rheological response of erythrocytes caused by nitroimidazoles and hyperthermia. Int. J. Hyperther., 1993, 9, 313-323.
27. Rybczyńska M., Szczepaniak L.: Effect of nitroimidazoles and irradiation on the membrane proteins of human erythrocytes: a spin label study. Stud. Biophys., 1986,116, 133-134.
28. Rybczyńska M., Pawlak A. L., Hoffmann S. K., Ignatowicz R.: Carrier of ataxia-telangiectasia (A-T) gene displays additional protein fraction changes in the environment of SH groups in erythrocyte membrane. Biochim. Biophys. Acta, 1990, 1022, 260-264.
29. Rybicki A. C., Oiu J. H., Musto S., Rosen N. L., Nagel R, L., Schwartz R.: Human erythrocyte protein 4.2 deficiency associated with hemolytic anemia and homozygous glutamic acid → lysine substraction in the cytoplasmic domain of band 3. Blood, 1993, 81, 2155-2165.
30. Saltzer U., Ahorn H., Prohaska, R.: Identification of the phosphorylation site on human erythrocyte band 7 integral membrane protein: implications for a monotopic protein structure. Biochim. Biophys. Acta, 1993, 1115, 149-152.
31. Schneider D. J., Freed J. H.: Calculating slow motional magnetic resonance spectra. In: A User's Guide. Spin Labeling. Theory and Applications. Eds. Berliner L. J., Reuben J., Plenum Press, New York, 1989, Vol. 8, 1-76.
32. Watanabe H., Kobayashi A., Yamamoto T., Suzuki S., Hayashi H., Yamazaki N.: Alteration of human erythrocyte membrane fluidity by oxygen-derived free radicals and calcium. Free Radical Biol. Med., 1990, 9, 507-514.
33. Yonei S., Akasaka S., Kato M.: Studies on the mechanism of radiation-induced structural disorganization of human erythrocyte membrane. Int. J. Radiat. Biol., 1984, 46, 464-471.