Release of glutathione from erythrocytes and other markers of oxidative stress in carbon monoxide poisoning

Journal of Applied Physiology

Volumn 82, Issue 5, 1997, Pages 1424-1432

  Thom, Stephen R ^a,b   Kang, Melissa ^a   Fisher, Donald ^a   Ischiropoulos, Harry ^a,b  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

hexose transport; nitric oxide; oxidized proteins; peroxynitrite; thiobarbituric acid reactive substances

Indexed keywords

CARBON MONOXIDE; CARBOXYHEMOGLOBIN; CYTOCHALASIN B; GLUCOSE; GLUTATHIONE; GLUTATHIONE DISULFIDE; HEXOSE; MALTOSE; NITRIC OXIDE; NITRIC OXIDE SYNTHASE INHIBITOR; PEROXYNITRITE; THIOBARBITURIC ACID REACTIVE SUBSTANCE;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CARBON MONOXIDE INTOXICATION; CONTROLLED STUDY; ERYTHROCYTE; EXCHANGE BLOOD TRANSFUSION; EXTRACELLULAR SPACE; HEXOSE TRANSPORT; HYPOXIA; MALE; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN SECRETION; RAT;

EID: 0030979730     PISSN: 87507587     EISSN: None     Source Type: Journal    
DOI: 10.1152/jappl.1997.82.5.1424     Document Type: Article

References (38)

1. Abbott, R. E., D. Schachter, E. R. Batt, and M. Flamm. Sulfhydryl substituents of the human erythrocyte hexose transport mechanism. Am. J. Physiol. 250 (Cell. Physiol. 19): C853-C860, 1986.
2. Adams, J. D., B. H. Lauterburg, and J. R. Mitchell. Plasma glutathione and glutathione disulfide in the rat: regulation and response to oxidative stress. J. Pharmacol. Exp. Ther. 227: 749-754, 1983.
3. Akaike, T., M. Yoshida, Y. Miyamoto, K. Sato, M. Kohno, K. Sasamoto, K. Miyazaki, S. Ueda, and H. Maeda. Antagonistic action of imidazolineoxyl N-oxides against endothelium-derived relaxing factor/·NO through a radical reaction. Biochemistry 32: 827-832, 1993.
4. Akerboom, T. P. M., M. Bilzer, and H. Sies. The relationship of biliary glutathione disulfide efflux and intracellular glutathione disulfide content in perfused rat liver. J. Biol. Chem. 257: 4248-4252, 1982.
5. Anderson, M. E., R. J. Bridges, and A. Meister. Direct evidence for inter-organ transport of glutathione and that the non-filtration renal mechanism for glutathione utilization involves gamma-glutamyl transpeptidase. Biochem. Biophy. Res. Commun. 96: 848-853, 1980.
6. Choi, I. S. Delayed neurologic sequelae in carbon monoxide intoxication. Arch. Neurol. 40: 433-435, 1983.
7. 1H-NMR spin-echo study of intact human erythrocytes. Eur. J. Biochem. 215: 711-718, 1993.
8. 1H-spin echo NMR of intact human erythrocytes. Biochem. Int. 20: 397-403, 1990.
9. Gohil, K., C. Viguie, W. C. Stanley, G. A. Brooks, and L. Packer. Blood glutathione oxidation during human exercise. J. Appl. Physiol. 64: 115-119, 1988.
10. Griffith, O. W., and A. Meister. Translocation of intracellular glutathione to membrane-bound γ-glutamyl transpeptidase as a discrete step in the γ-glutamyl cycle: glutathionuria after inhibition of transpeptidase. Proc. Natl. Acad. Sci. USA 76: 268-272, 1979.
11. Hardy, K. R., and S. R. Thom. Pathophysiology and treatment of carbon monoxide poisoning. Clin. Toxicol. 32: 613-629, 1994.
12. Huie, R. E., and S. Padjama. The reaction of ·NO with superoxide. Free Radical Res. Commun. 18: 195-199, 1993.
13. Ischiropoulos, H., M. F. Beers, S. T. Ohnishi, D. Fisher, S. E. Garner, and S. R. Thom. Nitric oxide production and perivascular tyrosine nitration in brain following carbon monoxide poisoning in the rat. J. Clin. Invest. 97: 2260-2267, 1996.
14. Ischiropoulos, H., D. Duran, and J. Horwitz. Peroxynitrite-mediated inhibition of DOPA synthesis in PC12 cells. J. Neurochem. 65: 2366-2372, 1995.
15. Ischiropoulos, H., I. Mendiguren, D. Fisher, A. B. Fisher, and S. R. Thom. Role of neutrophils and nitric oxide in lung alveolar injury from smoke inhalation. Am. J. Respir. Crit. Care Med. 150: 337-341, 1994.
16. Lunn, G., G. L. Dale, and E. Beutler. Transport accounts for glutathione turnover in human erythrocytes. Blood 54: 238-244, 1979.
17. Mayevsky, A., S. Meilin, G. G. Rogatsky, N. Zarchin, and S. R. Thom. Multiparametric monitoring of the awake brain exposed to carbon monoxide. J. Appl. Physiol. 78: 1188-1196, 1995.
18. McCord, J. M., and I. Fridovich. Superoxide dismutase - an enzymic function for erythrocuprein. J. Biol. Chem. 244: 6049-6055, 1969.
19. Meister, A. On the cycles of glutathione metabolism and transport. Curr. Top. Cell Regul. 18: 21-58, 1981.
20. Min, S. K. A brain syndrome associated with delayed neuropsychiatric sequelae following acute carbon monoxide poisoning. Psychiatr. Scand. 73: 80-86, 1986.
21. Nemeth, I., and D. Boda. Blood glutathione redox ratio as a parameter of oxidative stress in premature infants with IRDS. Free Radical Biol. Med. 16: 347-353, 1994.
22. Oldroyd, K. G., J. R. Paterson, A. G. Rumley, H. Eteiba, A. P. Rae, J. Shepherd, S. M. Cobbe, and I. Hutton. Coronary venous lipid peroxide concentrations after coronary angioplasty: correlation with biochemical and electrocardiographic evidence of myocardial ischaemia. Br. Heart J. 68: 43-47, 1992.
23. Prchal, J., S. K. Srivastava, and E. Beutler. Active transport of GSSG from reconstituted erythrocyte ghosts. Blood 46: 111-117, 1975.
24. Pucheu, S., C. Coudray, G. Vanzetto, A. Favier, J. Machecourt, and J. D. Leiri. Assessment of radical activity during the acute phase of myocardial infarction following fibrinolysis: utility of assaying plasma malondialdehyde. Free Radical Biol. Med. 19: 873-881, 1995.
25. Reglinski, J., S. Hoey, W. E. Smith, and R. D. Sturrock. Cellular response to oxidative stress at sulfhydryl group receptor sites on the erythrocyte membrane. J. Biol. Chem. 263: 12360-12366, 1988.
26. Snedecor, G. W., and W. G. Cochran. Statistical Methods. Ames, IA: Iowa State University, 1980.
27. Srivastava, S. K., and E. Beutler. Permeability of normal and cataractous rabbit lenses to glutathione. Proc. Soc. Exp. Biol. Med. 127: 512-514, 1968.
28. Stern, A. Red cell oxidative damage. In: Oxidative Stress, edited by H. Sies. London: Academic, 1985, p. 331-344.
29. Thom, S. R. Carbon monoxide-mediated brain lipid peroxidation in the rat. J. Appl. Physiol. 68: 997-1003, 1990.
30. Thom, S. R. Dehydrogenase conversion to oxidase and lipid peroxidation in brain after carbon monoxide poisoning. J. Appl. Physiol. 73: 1581-1589, 1992.
31. Thom, S. R. Leukocytes in carbon monoxide-mediated brain oxidative injury. Toxicol. Appl. Pharmacol. 123: 234-247, 1993.
32. Thom, S. R., and H. Ischiropoulos. Oxidant production by vascular endothelium in response to carbon monoxide. Undersea Hyperbar. Med. 23, Suppl.: 53, 1996.
33. 2-integrin function following acute carbon monoxide poisoning. Toxicol. Appl. Pharmacol. 128: 105-110, 1994.
34. Tietz, N. W. Fundamentals of Clinical Chemistry. Philadelphia, PA: Saunders, 1976, p. 437-441.
35. Tomaszewski, C., J. Rudy, J. Wathen, J. Brent, N. Rosenberg, and K. Kulig. Prevention of neurologic sequelae from carbon monoxide by hyperbaric oxygen in rats. Ann. Emerg. Med. 21: 631-632, 1994.
36. Winterbourn, C. C., and A. Stern. Human red cells scavage extracellular hydrogen peroxide and inhibit formation of hypochlorous acid and hydroxyl radical. J. Clin. Invest. 80: 1486-1491, 1987.
37. Young, I. S., J. A. Purvis, J. H. Lightbody, A. A. J. Adgey, and E. R. Trimble. Lipid peroxidation and antioxidant status following thrombolytic therapy for acute myocardial infarction. Eur. Heart J. 14: 1027-1033, 1993.
38. Zhang, J., and C. A. Piantadosi. Mitochondrial oxidative stress after carbon monoxide hypoxia in the rat brain. J. Clin. Invest. 90: 1193-1199, 1991.