Protective effects of N-acetylcysteine and vitamin E derivative U83836E on proteins modifications induced by methanol intoxication

Toxicology Mechanisms and Methods

Volumn 15, Issue 4, 2005, Pages 263-270

  Skrzydlewska, Elzbieta ^a   Elas, Martyna ^b   Ostrowska, Justyna ^a  

^a MEDICAL UNIVERSITY OF BIALYSTOK   (Poland)

^b JAGIELLONIAN UNIVERSITY   (Poland)

Author keywords

Liver; Methanol Intoxication; N acetylocysteine; Proteins; Rat; Vitamin E Derivative

Indexed keywords

2 [[4 [2,6 BIS(1 PYRROLIDINYL) 4 PYRIMIDINYL] 1 PIPERAZINYL]METHYL] 3,4 DIHYDRO 2,5,7,8 TETRAMETHYL 2H 1 BENZOPYRAN 6 OL; ACETYLCYSTEINE; ALPHA TOCOPHEROL; CATHEPSIN B; FREE RADICAL; GLUTATHIONE; MALONALDEHYDE; METHANOL; TRYPTOPHAN;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ANTIOXIDANT ACTIVITY; ARTICLE; CONTROLLED STUDY; DRUG MECHANISM; ERYTHROCYTE SEDIMENTATION RATE; FLUORESCENCE; LIPID PEROXIDATION; LIVER; MALE; METHANOL POISONING; NONHUMAN; OXIDATIVE STRESS; PEROXIDATION; PRIORITY JOURNAL; PROTEIN MODIFICATION;

EID: 23444452231     PISSN: 15376516     EISSN: 15376524     Source Type: Journal    
DOI: 10.1080/15376520590968815     Document Type: Article

References (32)

1. Baker, J. E., Felix, C. C., Olinger, G. N., and Kalyanaraman, B. 1980. Myocardial ischemia and reperfusion: Direct evidence for free radical generation by electron spin resonance spectroscopy. Proc. Natl. Acad. Sci. USA. 85:2786-2789.
2. Barclay, L. R., and Vinqvist, M. R. 1994. Membrane peroxidation: Inhibiting effects of water-soluble antioxidants on phospholipids of different cgarde types. Free Radic. Biol. Med. 16:779-788.
3. Davies, K. J., Delsignore, M. E., and Lin, S. W. 1987. Protein damage and degradation by oxygen radicals. II Modification of amino acids. J. Biol. Chem. 262:9902-9907.
4. Davies, M. J., Fu, S., Wang, H., and Dean, R. T. 1999. Stable markers of oxidant damage to proteins and their application in the study of human disease. Free Radic. Biol. Med. 27:1151-1163.
5. Devenyi, T., and Gregely, J. 1968. Analytische Methoden zur Untersuchung von Aminosauren. In Peptiden und Proteinen. (T. Devenyi, and J. Gregely), pp. 115-117. Akademiai Kiado, Budapest.
6. Ellman, G. L. 1959. Tissue sulfhydryl groups. Archiv. Biochem. Biophys. 82:70-77.
7. Esterbauer, H., Lang, J., Zadravec, and Slater, S. T. F. 1984. Detection of malonaldehyde by high-performance liquid chromatography. Methods Enzymol. 105:319-328.
8. Esterbauer, H., Schaur, R. J., and Zollner, J. 1991. Chemistry and biochemistry of 4-hydroxynonenal, malondialdehyde and related aldehydes. Free Radic. Biol. Med. 11:81-128.
9. Fu, S., Gebicki, S., Jessup, W., Gebicki, J. M., and Dean, R. T. 1995. Biological fate of amino acid, peptide and protein hydroperoxides. Biochem. J. 311:821-827.
10. Galembeck, F., Ryan, J. R., and Feeney, R. E. 1977. Reaction of proteins with formaldehyde in the presence and absence of sodium borohydride. J. Agric. Food Chem. 25:238-245.
11. Gutteridge, J. M. 1995. Lipid peroxidation and antioxidants as biomarkers of tissue damage. Clin. Chem. 41:1819-1828.
12. Jain, S. K., McVie, R., Smith, T. 2000 Vitamin E supplementation Restores glutathione and malondialdehyde to normal concentrations in ertyhrocytes of type 1 diabetic children. Diabetes Care 23:1389-1394.
13. Kehrer, J. P. 1993. Free radicals as mediators of tissue injury and disease. Crit. Rev. Toxicol. 23:21-48.
14. Levine, R. L., Garaland, D., Oliver, C. N., Amici, A., Climent, I., Lenz, A. G., Ahn, B., Shatiel, S., and Stadtman, E. R. 1990. Determination of carbonyl content in oxidatively modified proteins. Methods Enzymol. 186:464-478.
15. Liesivuori, J., and Savolainen, H. 1991. Methanol and formic acid toxicity: Biochemical mechanisms. Pharmacol. Toxicol. 69:157-163.
16. McMartin, K. E., Martin-Amat, G., Noker, P. E., and Tephly, T. R. 1979. Lack of a role for formaldehyde in methanol poisoning in the monkey. Biochem. Pharmacol. 28:645-649.
17. Mertsch, K., Grune, T., Kunstmann, S., Wiesner, B., Ladhoff, A. M., Siems, W. G., Haseloff, R. F., and Blasig, I. E. 1998. Protective effects of the thiophosphate amifostine (WR 2721) and a lazaroid (U83836E) on lipid peroxidation in endothelial cells during hypoxia/reoxygenation. Biochem. Pharmacol. 56:945-54.
18. Mickle, D. A. 1993. Efficacy of water-soluble analogs of vitamin E in the prevention of myocardial ischemia-reperfusion injury. Methods Toxicol. In vitro Toxicity Indicators 16:309-322.
19. Nahano, H., Boudjema, K., Alexandre, E., Imbs, P., Chenard, M. P., and Wolf, P. 1995. Protective effects of N-acetylcysteine on hypothermic is chemioreperfusion injury of rat liver, Hepatology 22:539-545.
20. O'Neil, J., Hoppe, G., Sayre, L. M., and Hoff, H. F. 1997. Inactivation of cathepsin B by oxidized LDL involves complex formation induced by binding of putative reactive sites exposed at low pH to thiols on the enztme. Free Radic. Biol. Med. 23:215-225.
21. Poli, G. 1993. Liver damage due to free radicals. Br. Med. Bull. 49:604-609.
22. Rice-Evans, C. A., Diplock, A. T., and Symons, M. C. 1991. Techniques in free radical research. In Laboratory Techniques in Biochemistry and Molecular Biology (R. H. Burdon, Ed.) Elsevier, Amsterdam.
23. Schwartz, R. S., Rybicki, A. C., Healt, R. H., and Lubin, B. H. 1987. Protein 4.1 in sickle erythrocytes. Evidence for oxidative damage. J. Biol. Chem. 262:15666-15672.
24. Shan, X. O., Aw, T. Y., and Jones, D. P. 1990. Glutathione dependent protection against oxidative injury. Pharmacol. Therap. 47:61-71.
25. Sies, H. 1997. Oxidative stress: Oxidants and antioxidants. Exp. Physiol. 82:291-295.
26. Skrzydlewska, E., and Farbiszewski, R. 1997. Decreased antioxidant defense mechanisms in rat liver after methanol intoxication. Free Radic. Res. 27:369-374.
27. Skrzydlewska, E, Elas, M., Farbiszewski, R., and Roszkowska, A. 2000. Effect of methanol intoxication on free-radical induced protein oxidation. J. Appl. Toxicol. 20:239-243.
28. Skrzydlewska, E. 2003. Toxicological and metabolic consequences of methanol poisoning. Toxicol. Mechanisms Meth. 11:277-293.
29. Tawatari, T., Kawabata, Y., and Katunuma, N. 1979. Crystallization and properties of cathepsin B from rat liver. Eur. J. Biochem. 102:279-289.
30. 13-n.m.r. characterization of formaldehyde bonds in model mixtures and proteins containing lysine. Int. J. Peptide Protein Res. 25:258-266.
31. 2 and chelated iron. Free Radic. Biol. Med. 7:499-505.
32. Zweier, M. L., Flaherty, J. L., and Weisfeldt, J. T. 1987. Direct measurement of free radical generation following reperfusion of ischemic myocardium. Proc. Natl. Acad. Sci USA 84:1404-1407.