Acellular hemoglobin-mediated oxidative stress toward endothelium: A role for ferryl iron

American Journal of Physiology - Heart and Circulatory Physiology

Volumn 275, Issue 3 44-3, 1998, Pages

  Goldman, Daniel W ^a   Breyer III, Richard J ^a   Yeh, David ^a   Brockner Ryan, Beth A ^a   Alayash, Abdu I ^a  

^a CENTER FOR BIOLOGICS EVALUATION AND RESEARCH   (United States)

Author keywords

Apoptosis; Blood substitutes

Indexed keywords

BLOOD SUBSTITUTE; FERRIC ION; HEMOGLOBIN; HYDROGEN PEROXIDE;

ANIMAL CELL; APOPTOSIS; ARTICLE; BLOOD COMPONENT THERAPY; CONTROLLED STUDY; CYTOTOXICITY; DNA DAMAGE; ENDOTHELIUM CELL; ENZYME ACTIVITY; NONHUMAN; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PRIORITY JOURNAL;

EID: 33750869692     PISSN: 03636135     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpheart.1998.275.3.h1046     Document Type: Article

References (34)

1. Alayash, A. I., and R. E. Cashon. Hemoglobin and free radicals: implications for the development of a safe blood substitute. Mol. Med. Today 1: 122-127, 1995.
2. Alayash, A. I., J. C. Fratantoni, C. Bonaventura, J. Bonaventura, and E. Bucci. Consequences of chemical modifications on the free radical reactions of human hemoglobin. Arch. Biochem. Biophys. 298: 114-120, 1992.
3. Alayash, A. I., J. C. Fratantoni, C. Bonaventura, J. Bonaventura, and R. E. Cashon. Nitric oxide binding to human ferrihemoglobins cross-linked between either α or β subunits. Arch. Biochem. Biophys. 303: 332-338, 1993.
4. Al-Rubeai, M. Apoptosis and cell culture technology. In: Advances in Biochemical Engineering/Biotechnology, edited by I. Scheper. Berlin: Springer, 1997, p. 225-249.
5. Amberson, W. R., J. J. Jennings, and C. M. Rhode. Clinical experience with hemoglobin-saline solutions. J. Appl. Physiol. 1: 469-489, 1949.
6. Balla, J., H. S. Jacob, G. Balla, K. Nath, J. W. Eaton, and G. M. Vercellotti. Endothelial-cell heme uptake from heme proteins: induction of sensitization and desensitization to oxidant damage. Proc. Natl. Acad. Sci. USA 90: 9258-9289, 1993.
7. Balla, G., H. S. Jacob, J. Balla, M. Rosenberg, K. Nath, F. Apple, J. W. Eaton, and G. M. Vercellotti. Ferritin: a cytoprotective antioxidant strategemof endothelium. J. Biol. Chem. 267: 18148-18153, 1992.
8. Balla, J., K. A. Nath, G. Balla, M. B. Juckett, H. S. Jacob, and G. M. Vercellotti. Endothelial cell heme oxygenase and ferritin induction in rat lung by hemoglobin in vivo. Am. J. Physiology 268 (Lung Cell. Mol. Physiol. 12): L321-L327, 1995.
9. Balla, G., G. M. Vercellotti, U. Muller-Eberhard, J. Eaton, and H. S. Jacob. Exposure of endothelial cells to free heme potentiates damage mediated by granulocytes and toxic oxygen species. Lab. Invest. 64: 648-655, 1991.
10. Brandt, J. L., N. R. Frank, and H. C. Lichtman. The effects of hemoglobin solutions on renal functions in man. Blood 6: 1152-1158, 1951.
11. Cabaud, P. G., and F. Wroblewski. Colorimetric measurement of lactic dehydrogenase activity of body fluids. Am. J. Clin. Pathol. 30: 234-236, 1958.
12. Cashon, R. E., and A. I. Alayash. Reactions of human hemoglobin Ao and two cross-linked derivatives with hydrogen peroxide: differential behavior of the ferryl intermediate. Arch. Biochem. Biophys. 316: 461-469, 1995.
13. Chow, S. C., D. J. McConkey, S. Orrenius, and M. Jondal. Quantitation of DNA fragmentation using fiberglass filters. Anal. Biochem. 183: 42-45, 1989.
14. Christensen, S. M., F. Medina, R. M. Winslow, S. M. Snell, A. Zegna, and M. A. Marini. Preparation of human hemoglobin Ao for possible use as a blood substitute. J. Biochem. Biophys. Methods 17: 143-154, 1988.
15. Colden-Stanfield, M., E. B. Cramer, and E. K. Gallin. Comparison of apical and basal surfaces of confluent endothelial cells: patch-clamp and viral studies. Am. J. Physiol. 263 (Cell Physiol. 32): C573-C583, 1992.
16. Comair, Y. G., H. M. Schipper, and S. Brem. The prevention of oxyhemoglobin-induced endothelial and smooth muscle cytoskeletal injury by deferoxamine. Neurosurgery 32: 58-65, 1993.
17. Darley-Usmar, V., and R. White. Disruption of vascular signalling by the reaction of nitric oxide with superoxide: implications for cardiovascular disease. Exp. Physiol. 82: 305-316, 1997.
18. Echaniz, P., M. D. Dejuan, and E. Cuadrado. DNA staining changes associated with apoptosis and necrosis in blood lymphocytes of individuals with HIV infection. Cytometry 19: 164-170, 1995.
19. 18a.Eich, R. F., T. Li, D. D. Lemon, D. H. Doherty, S. R. Curry, J. F. Aitken, A. J. Mathews, K. A. Johnson, R. D. Smith, G. N. Phillips, Jr., and J. S. Olson. Mechanism of NO-induced oxidation of myoglobin and hemoglobin. Biochemistry 35: 6976-6983, 1996.
20. Everse, J., and N. Hsia. The toxicities of native and modified hemoglobins. Free Radie. Biol. Med. 22: 1075-1099, 1997.
21. Everse, J., M. C. Johnson, and M. A. Marini. Peroxidative activities of hemoglobin and hemoglobin derivatives. In: Methods of Enzymology San Diego, edited by J. Everse, K. D. Vandegriff and R. M. Winslow. New York: Academic, 1994, vol. 231, p. 547-561.
22. Feola, M., J. Simoni, P. C. Canizaro, R. Tran, and G. Raschbaum. Toxicity of polymerized hemoglobin solutions. Surg. Gynecol. Obstet. 166: 211-222, 1988.
23. Galaris, D., A. Sevanian, E. Cadenas, and P. Hochstein. Ferrylmyoglobin-catalyzed linoleic acid peroxidation. Arch. Biochem. Biophys. 281: 163-169, 1990.
24. Giulivi, C., and K. J. A. Davies. A novel antioxidant role for hemoglobin. The comproportionation of ferrylhemoglobin with oxyhemoglobin. J. Biol. Chem. 265: 19453-19460, 1990.
25. Giulivi, G., F. J. Romero, and E. Cadenas. The interaction of Trolox C, a water-soluble vitamin E analog, with ferrylmyoglobin: reduction of the oxyferryl moiety. Arch. Biochem. Biophys. 299: 302-312, 1992.
26. Grisham, M. B., and J. Everse. Pro-oxidant activity of hemoglobin and myoglobin. In: Peroxidases in Chemistry and Biology, edited by J. Everse, K. E. Everse, and M. B. Grisham. Boca Raton, FL: CRC, 1991, p. 335-344.
27. Grisham, M. B., T. S. Gaginell, C. Von Ritter, H. Tamai, R. M. Be, and D. N. Granger. Effects of neutrophil-derived oxidants on intestinal permeability, electrolyte transport and epithelial cell viability. Inflammation 14: 531-542, 1990.
28. Gutteridge, J. M. C. The antioxidant activity of haptoglobin towards haemoglobin-stimulated lipid peroxidation. Biochim. Biophys. Acta 917: 219-223, 1987.
29. Hai, T. T., D. Nelson, D. Pereira, and A. Srnak. Diaspirin crosslinked hemoglobin (DCLHb) polymerization. Artif. Cells Blood Substit. Immobil. Biotechnol. 22: 923-931, 1994.
30. Harrison, G. J., L. R. Jordan, and R. J. Willis. Deleterious effects of hydrogen peroxide on the function and ultrastructure of cardiac muscle and the coronary vasculature of perfused rat hearts. Can. J. Cardiol. 10: 843-849, 1994.
31. Hess, R. J., and R. F. Reiss. Resuscitation and limited utility of the present generation of blood substitutes. Transfus. Med. Rev. 10: 276-285, 1996.
32. Kawamura, K., S. Kagiyama, A. Ogawa, and T. Yanase. Kinetics of peroxidase activity, absorption spectra and oxygen affinity of human-haptoglobin I-I complexes. Biochim. Biophys. Acta 285: 22-27, 1972.
33. Krishna, M. C., A. Samuni, J. Taira, S. Goldstein, J. B. Mitchell, and A. Russo. Stimulation by nitroxides of catalase-like activity of hemeproteins: kinetics and mechanism. J. Biol. Chem. 271: 26015-26025, 1996.
34. Kvietys, P. R., W. Inauen, B. R. Bacon, and M. B. Grisham. Xanthine oxidase-induced injury to endothelium: role of intracellular iron and hydroxyl radical. Am. J. Physiol. 257 (Heart Circ. Physiol. 26): H1640-H1646, 1989.