Methemoglobin formation in hemoglobin vesicles and reduction by encapsukated thiols

Bioconjugate Chemistry

Volumn 8, Issue 4, 1997, Pages 539-544

  Takeoka, Shinji ^a   Sakai, Hiromi ^a   Kose, Takehiro ^a   Mano, Yuichi ^a   Seino, Yuriko ^a   Nishide, Hiroyuki ^a   Tsuchida, Eishun ^a  

^a WASEDA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CARDIOVASCULAR SYSTEM; ENZYMES; HEMOGLOBIN; OXYGEN; PHOSPHOLIPIDS;

% REDUCTIONS; ACTIVE OXYGEN; GLUTHATHIONE; HEMOGLOBIN VESICLES; HOMOCYSTEINES; LONG-TERM MAINTENANCES; PHOSPHOLIPID VESICLES; REDUCTANTS; SUPER OXIDE DISMUTASE; SUPEROXIDE DISMUTASES;

AMINO ACIDS;

ANIMALIA; RATTUS NORVEGICUS;

EID: 0031193434     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc970091y     Document Type: Article

References (37)

1. Brantley, R. E., Smerdon, S. J., Wilkinson, A. J., Singleton, E. W., and Olson, J. S. (1993) The Mechanism of Autoxidation of Myoglobin. J. Biol. Chem. 268, 6995-7010.
2. Brunori, M., Falcioni, G., Giardina, B., and Rotilio, G. (1975) Formation of Superoxide in the Autoxidation of the Isolated a and β Chanis of Human Hemoglobin and Its Involvement in Hemichrome Precipitation. Eur. J. Biochem. 53, 99-104.
3. Chung, J. E., Hamada, K., Sakai, H., Takeoka, S., and Tsuchida, E. (1995) Ligand Exchange Reaction of Carbonylhemoglobin to Oxyhemoglobin in a Hemoglobin Liquid Membrane. Nihonkagakukaishi 2, 123-127.
4. Djordjevich, L., and Miller, I. F. (1980) Synthetic Erythrocytes from Lipid Encapsulated Hemoglobin. Exp. Hematol. (Charlottesville, Va.) 8, 584-592.
5. Eyer, P., Hertle, H., Kiese, M., and Klein, G. (1975) Kinetics of Ferrihemoglobin Formation by some Reducing Agents, and the Role of Hydrogen Peroxide. Mol. Pharmacol. 11, 326-334.
6. Faivre, B., Menu, P., Labrude, P., Grandgeorge, M., and Vigneron, C. (1994) Methemoglobin Formation after Administration of Hemoglobin Conjugated to Carboxylate Dextran in Guinea Pigs. Attemps to Prevent the Oxidation of Hemoglobin. Artif. Cells, Blood Substitutes, Immobilization Biotechnol. 22, 551-558.
7. Friedman, M., Cavins, J. F., and Wall, J. S. (1965) Relative Nucleophilic Reactivities of Amino Groups and Mercaptide Ions in Addition Reactions with α,β-Unsaturated compounds. J. Am. Chem.. Soc. 87, 3672-3682.
8. Gutteridge, J. M. C. (1986) Iron Promoters of the Fenton Reaction and Lipid Peroxidation can be Released from Haemoglobin by Peroxides. FEBS Lett. 201, 291-295.
9. Hamada, K., Kose, T., Ohgushi, T., Sakai, H., Takeoka, S., Nishide, H., and Tsuchida, E. (1995) Assay Systems for the Components of Red Cell Substitutes (NRC). Artif. Blood 3, 96-101.
10. Hunt, C. A., Burnette, R. R., MacGregor, R. D., Strubbe, A. E., Lau, D. T., Taylor, N., and Kawada, H. (1985) Synthesis and Evaluation of a Prototypal Artificial Red Cell. Science 230, 1165-1168.
11. Izumi, Y., Sakai, H., Hamada, K., Takeoka, S., Yamahata, K., Katoh, H., Nishide, H., Tsuchida, E., and Kobayashi, K. (1996) Physiological Responses to Exchange Transfusion with Hemoglobin Vesicles as an Artificial Oxygen Carrier in Anesthetized Rats: Changes in Mean Arterial Pressure and Renal Cortical Tissue Oxygen Tension. Crit. Care Med. 24, 1869-1873.
12. Izumi, Y., Sakai, H., Takeoka, S., Kose, T., Hamada, K., Yoshizu, A., Nishide, H., Tsuchida, E., and Kobayashi, K. (1997) Evaluation of the Capabilitites of Hemoglobin Vesicles as Artificial Oxygen Carriers in a Rat Exchange Transfusion Model. ASAIO J. 43 (in press).
13. Levy, A., Zhang, L., and Rifkind, J. M. (1988) Hemoglobin: A Source of Superoxide Radical under Hypoxic Conditions. Oxy-Radicals Mol. Biol. Pathol., Proc. Upjohn-UCLA Symp., 11-25.
14. Mansouri, A., and Winterhalter, H. (1973) Nonequivalence of Chains in Hemoglobin Oxidation. Biochemistry 12, 4946-4949.
15. Misra, H. P. (1974) Generation of Superoxide Free Radicals during the Autoxidation of Thiols. J. Biol. Chem. 249, 2151-2155.
16. Morell, S. A., Ayers, V. E., Grenwalt, T. J., and Hoffman, P. (1964) Thiols of the Erythrocyte. J. Biol. Chem. 239, 2696-2705.
17. Ogata, Y., Okamoto, T., Suzuki, K., and Kamitani, T. (1994) The Development of Neo Red Cells (NRC) with Enzymatic Reduction System of the Methemoglobin. Artif. Blood 2, 62-66.
18. Olsen, S. B., Tang, D. B., Jackson, M. R., Gomez, E. R., Ayala, B., and Alving, B. M. (1996) Enhancement of Platelet Deposition by Cross-linked Hemoglobin in a Rat Carotid Endarterectomy Model. Circulation 93, 327-332.
19. Quebec, E. A., and Chang, T. M. S. (1995) Superoxide Dismutase and Catalase Cross-linked to Polyhemoglobin Reduces Methemoglobin Formation in vitro. Artif. Cells, Blood Substitutes, Immobilization Biotechnol. 23, 693-705.
20. Rudolph, A. S. (1995) Encapsulation of Hemoglobin in Liposomes. In Blood Substitutes: Physiological Basis of Efficacy (R. M. Winslow, K. D. Vandegriff, and M. Intaglietta, Eds.) pp 90-104, Birkhauser, Boston.
21. Sakai, H., Takeoka, S., Yokohama, H., Seino, Y., Nishide, H., and Tsuchida, E. (1993) Purification of Concentrated Hemoglobin Using Organic Solvent and Heat Treatment. Protein Expression Purif. 4, 563-569.
22. Sakai, H., Takeoka, S., Seino, Y., and Tsuchida, E. (1994) Suppression of Methemoglobin Formation by Glutathione in a Concentrated Hemoglobin Solution and in a Hemoglobin Vesicle. Bull. Chem. Soc. Jpn. 67, 1120-1125.
23. Sakai, H., Hamada, K., Takeoka, S., Nishide, H., and Tsuchida, E. (1996) Physical Characteristics of Hemoglobin Vesicles as Red Cell Substitutes. Biotechnol. Prog. 12, 119-125.
24. Sakai, H., Takeoka, S., Park, S. I., Kose, T., Hamada, K., Izumi, Y., Yoshizu, A., Nishide, H., Kobayashi, K., and Tsuchida, E. (1997) Surface Modification of Hemoglobin Vesicles with Poly-(ethylene glycol) and Effects on Aggregation, Viscosity, and Blood Flow during 90% Exchange Transfusion in Anesthetized Rats. Bioconjugate Chem. 8, 23-30.
25. Sampath, V., and Caughey W. S. (1985) Prooxidant Effects of Glutathione in Aerobic Hemoglobin Solutions. Superoxide Generation from Uncoordinated Dioxygen. J. Am. Chem. Soc. 107, 4076-4078.
26. Shikama, K. (1984) A Controversy on the Mechanism of Autoxidation of Oxymyoglobin and Oxyhemoglobin: Oxidation, Dissociation, or Displacement? Biochem. J. 223, 279-280.
27. Stratton, L. P., Rudolph, A. S., Knoll, W. K., Jr., Bayne, S., and Farmer, M. C. (1988) The Reduction of Methemoglobin Levels by Antioxidants. Hemoglobin 12, 358-368.
28. Takeoka, S., Ohgushi, T., Ohmori, T., Terase, K., Nishide, H., and Tsuchida, E. (1996) Layer Controlled Hemoglobin Vesicles by Interaction of Hemoglobin with Phospholipid Assembly. Langmuir 12, 1775-1779.
29. Tomoda, A., Yoneyama, T., and Tsuji, A. (1981) Changes in Intermediate Haemoglobins during Autoxidation of Haemoglobin. Biochem. J. 195, 485-492.
30. Tsai, A. G., Kerger, H., and Intaglietta, M. (1996) Microvascular Oxygen Distribution: Effects due to Free Hemoglobin in Plasma. In Blood Substitutes: New Challenges (R. M. Winslow, K. D. Vandegriff, and M. Intaglietta, Eds.) pp 124-131, Birkhauser, Boston.
31. Tsuchida, E., and Takeoka, S. (1995) Stabilized Hemoglobin Vesicles. In Artificial Red Cells (E. Tsuchida, Ed.) pp 35-64, John Wiley and Sons, New York.
32. Van Assendelft, O. W. (1970) Spectrophotometry of Haemoglobin Derivatives, pp 128-129, Royal Vangorcun Ltd., Assen, The Netherlands.
33. Vandegriff, K. D., and Winslow, R. M. (1995) The Theoretical Analysis of Oxygen Transport: A New Strategy for the Design of Hemoglobin-based Red Cell Substitutes. In Blood Substitutes: Physiological Basis of Efficacy (R. M. Winslow, K. D. Vandegriff, and M. Intaglietta, Eds.) pp 143-154, Birkhauser, Boston.
34. Wallace, W. J., Houtchens, R. A., Maxwell, J. C., and Caughey, W. S. (1982) Mechanism of Autoxidation for Hemoglobins and Myoglobins. J. Biol. Chem. 257, 4966-4977.
35. Watkins, J. A., Kawanishi, S., and Caughey, W. S. (1985) Autoxidation Reactions of Hemoglobin A Free from Other Red Cell Components: A Minimal Mechanism. Biochem. Biophys. Res. Commun. 132, 742-748.
36. Winslow, R. M. (1995) Blood Substitutes: A Moving Target. Nature Med. 1, 1212-1215.
37. Yang, T., and Olsen, K. W. (1989) The Effect of Crosslinking by Bis(3,5-dibromosalicyl) Fumarate on the Autoxidation of Hemoglobin. Biochem. Biophys. Res. Commun. 163, 733-738.