Acellular invertebrate hemoglobins as model therapeutic oxygen carriers: Unique redox potentials

Artificial Cells, Blood Substitutes, and Biotechnology

Volumn 35, Issue 1, 2007, Pages 53-67

  Harrington, John P ^a,b   Kobayashi, Shiho ^a   Dorman, Scott C ^c   Zito, Samantha L ^c   Hirsch, Rhoda Elison ^d  

^a STATE UNIVERSITY OF NEW YORK   (United States)

^b MARINE BIOLOGICAL LABORATORY   (United States)

^c BIRMINGHAM SOUTHERN COLLEGE   (United States)

^d ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

Arenicola hemoglobin; Hemoglobin Based Oxygen Carrier (HBOC); Lumbricus hemoglobin; Red cell substitute; Redox potential

Indexed keywords

BIOPOLYMERS; CELLS; OXIDATION;

ARENICOLA HEMOGLOBIN; HEMOGLOBIN BASED OXYGEN CARRIER (HBOC); LUMBRICUS HEMOGLOBIN; RED CELL SUBSTITUTE; REDOX POTENTIALS;

HEMOGLOBIN;

BLOOD SUBSTITUTE; HEMOGLOBIN; IRON COMPLEX; OXYGEN; POLYMERIZED HEMOGLOBIN; POTASSIUM FERRICYANIDE;

ARTICLE; AUTOOXIDATION; ELECTRON TRANSPORT; ERYTHROCYTE; INVERTEBRATE; MARINE SPECIES; NONHUMAN; OXIDATION; OXIDATION REDUCTION REACTION; OXYGEN AFFINITY; OXYGEN TRANSPORT;

ANIMALS; BLOOD SUBSTITUTES; DRUG STABILITY; ELECTROCHEMISTRY; HEMOGLOBINS; INVERTEBRATES; MODELS, BIOLOGICAL; OLIGOCHAETA; OXIDATION-REDUCTION; OXYGEN;

ARENICOLA; INVERTEBRATA; LUMBRICUS; LUMBRICUS TERRESTRIS;

EID: 33847296165     PISSN: 10731199     EISSN: 15324184     Source Type: Journal    
DOI: 10.1080/10731190600974491     Document Type: Article

References (42)

1. Lee, R., Neya, K., Svizzero, T.A., Vlahahas, G.T. (1995). Limitations of the efficacy of hemoglobin-based oxygen carrying solutions. J. Appl. Physiol. 78: 236-246.
2. Alayash, A.I., Cashon, R.E. (1995). Hemoglobin and free radicals: Implications for the development of a saf blood substitute. Mol. Med. Today. 1: 122-127.
3. Alayash, A.I. (1999). Hemoglobin-based blood substitutes: Oxygen carriers, pressor agents, or oxidants. Nature Biotechnol. 17: 545-549.
4. Alayash, A.I. (2000). Hemoglobin-based blood substitutes and the hazards of blood radicals. Free Radic. Res. 33: 341-348.
5. D'Agnello, F., Alayash, A.I. (2000). Interactions of hemoglobin with hydrogen peroxide alters thiol levels and course of endothelial cell death. Adv. Drug Deliv. Res. 40: 199-212.
6. Hirsch, R.E., Harrington, J.P. (2000). Blood substitutes: An overview and perspective. Einstein Quart. J. Biol. Med. 17: 113-123.
7. Harrington, J.P., Hirsch, R.E. (2003). XIIIth Intern. Conference on Invertebrate Dioxygen Binding Proteins, Mainz, Germany, September.
8. Dorman, S.C., Kenny, C.F., Miller, L., Hirsch, R.E., Harrington, J.P. (2002). Role of redo potential of hemoglobin-based oxygen cariers on methemoglobin reducton by plasma components. Art. Cells, Blood Subst. and Immob. Biotech. 30: 43-56.
9. Harrington, J.P., Shear, H.L., Hirsch, R.E. (1993). Blood, 589a.
10. Hirsch, R.E., Jelicks, L.A., Wittenberg, B.A., Kaul, D.K., Shear, H.L., Harrington, J.P. (1997). A first evaluation of the high molecular weight polymeric Lumbricus terrestris hemoglobin as an oxygen carrier. Art. Cells, Blood Subst. and Immob. Biotech. 25: 429-444.
11. Kuchumov, A.R., Taveau, J.C., Lamy, J.N., Wall, J.S., Weber, R.E., Vinogradov, S.N. (1999). The role of linkers in the reassembly of the 3.6 Mda hexagonal bilayer hemoglobin from Lumbricus terrestris. J. Mol. Biol. 289: 1361-1374.
12. Green, B.N., Gotoh, T., Suzuki, T., Zal, F., Lallier, F.H., Toulmond, A., Vinogradov, S.N. (2001). Observation of large, non-covalent globin subassemblies in the approximately 3600 kDa hexagonal bilayer hemoglobin by electrospray ionization time-of-flight mass spectrometry. J. Mol. Biol. 309: 553-560.
13. Fushitani, K., Imai, K., Riggs, A.F. (1986). Oxygenation properties of hemoglobin from the earthworm, Lumbricus terrestris. Effects of pH, salt, and temperature. J. Biol. Chem. 261: 8414-8423.
14. Zhu, H., Ownby, D.W., Riggs, C.K., Nolasco, N.J., Stoops, J.K., Riggs, A.F. (1996). Assembly of the gigantic hemoglobin of the earthworm Lumbricus terrestris. Roles of subunit equilibria, non-globin linker chains, and valence of the heme iron. J. Biol. Chem. 271: 30007-30021.
15. Harrington, J.P. (1994). Multimeric Lumbricus hemoglobin stabilization by alkali and alkaline earth cations. Comp. Biochem. Physiol. 109A: 799-803.
16. Chabasse, C., Rousselot, M., Bailly, X., Harnois, T., Zal, F. (2005). Novel dissociation mechanism of a polychaetous annid extracellular hemoglobin. Xth Intern. Symp. on Blood Subst., Providence, RI, p. 55a.
17. Harrington, J.P., Pandolfelli, E., Herskovits, T.T. (1973). Solution studies on heme proteins: Circular dichroism and opical rotation of Lumbricus terrestris and Glycera diranchiata hemoglobin. Biochim. Biophys. Acta. 328: 71-83.
18. Harrington, J.P., Hicks, R. (1994). Spectral analysis of Fe(III)-complex reduction by hemoglobin: Possible mechanisms of interaction. Intern. J. Biochem. 26: 1111-1117.
19. DiIorio, E. (1981). Methods in Enzymology 96: 47-72.
20. Harrington, J.P., Gonzalez, Y., Hirsch, R.E. (2000). Redox concerns in the use of acellular hemoglobin-based oxygen carriers: The role of plasma components. Art. Cells, Blood Subst. and Immob. Biotech. 28: 477-492.
21. Dorman, S.C., Harrington, J.P., Martin, M.S., Johnson, T.V. (2004). Determination of the formal reduction potential of Lumbricus terrestris hemoglobin using thin-layer spectroelectrochemistry. J. Inorg. Biochem. 98: 195-198.
22. Faulkner, K.M., Bonaventura, C., Crumbliss, A.L. (1994). A spectroelectrochemical method for evaluating factors which regulate the redox potential of hemoglobins. Inorg. Chim. Acta. 226: 187-194.
23. Faulkner, K.M., Bonaventura, C., Crumbliss, A.L. (1995). A spectroelectrochemical method for differentiation of steric and electronic effects in hemoglobins and myoglobins. J. Biol. Chem. 270: 13604-13612.
24. Vinogradov, S.N., Lugo, S., Mainwaring, M.G., Kapp, O.H., Crewe, A.V. (1986). Bracelet protein: A quaternary structure proposed for the giant extracellular hemoglobin of Lumbricus terrestris. Proc. Nat. Acad. Sci. USA 83: 8034-8038.
25. Zal, F., Green, B.N., Lallier, F.H., Vinogradov, S.N., Toulmond, A. (1997). Quaternary structure of the extracellular hemoglobin of the lugworm Arenicola marina: A multi-angle-laser-light-scattering and electrosprayionization-mass-spectrometry analysis. Eur. J. Biochem. 243: 85-92.
26. Fushitani, K., Matsuura, M.S.A., Riggs, A.F. (1988). The amino acid sequences of chains a, b, and c that form the trimer of the extracellular hemoglobin from. J. Biol. Chem. 263: 6502-6517.
27. Yager, T.D., Terwilliger, N.B., Terwilliger, R.C., Schabtach, E., Van Holde, K.E. (1892). Organization and physical properties of the giant extracellular hemoglobin of the clam Astarte castanea. Biochim. Biophys. Acta. 709: 194-203.
28. Terwilliger, N.B. (1992). Adv. Comp. Environ.Physiol. 13: 193-229.
29. Terwilliger, R.C., Terwilliger, N.B., Schabtach, E. (1978). Extracellular hemoglobin of the clam, Cardita borealis: An unusual polymeric hemoglobin. Comp. Biochem. Physiol. 59B: 9-14.
30. Herskovits, T.T., Behrens, C.F., Siuta, P.B, Pandofelli, E.R. (1977). Solvent denaturation of globular proteins: Unfolding by the monalkyl- and dialkyl-substituted formamides and ureas. Biochim. Biophys. Acta. 490: 192-199.
31. Regis, W.C.B., Fattori, J., Santoro, M.M., Jamin, M., Ramos, C.H.I. (2005). Of the differences in stability between horse and sperm whale myoglobins. Arch. Biochem Biophys. 436: 168-177.
32. Kobayashi, S., Harrington, J.P. (2005). Unpublished data.
33. Sampeth, V., Caughey, W.S. (1985). Prooxidant effects of glutathione in aerobic hemoglobin solutions. Superoxide generation from uncoordinated dioxygen. J. Am. Chem. Soc. 107: 4076-4078.
34. Royer, W.E., Strand, K., Van Heel, M., Hendrickson, W.A. (2000). Structural hierarchy in erythrocruorin, the giant respiratory assemblage of annelids. Proc. Nat. Acad. Sci. USA 97: 7107-7111.
35. Strand, K., Knapp, J.E., Bhyravbhatla, B, Royer, W.E. (2004). Crystal structure of the hemoglobin docecamer from Lumbricus terrestris erythrocruorin: Allosteric core of giant annelid respiratory complexes. J. Mol. Biol. 344: 119-134.
36. Hirsch, R.E., Harrington, J.P., Scarlata, S. (1993). The differential effects of carbon monoxide and oxygen on the pressure dissociation of Lumbricus terrestris hemoglobin. Biochim. Biophys. Acta. 1161: 285-290.
37. Harrington, J.P., Friedman, J.M., Hirsch, R.E. (1997). The effect of alkaline earth cations and of ionic strength on the dissociation of earthworm hemoglobin at alkaline pH. Biophys. J. 72(2): A86.
38. Ochiai, T., Weber, R.E. (2002). Effects of Magnesium and calcium on the oxygenation reaction of erythrocruorin from the marine polychaete Arenicola marina and the terrestrial oligochaete Lumbricus terrestris. Zoolog. Sci. 19: 995-1000.
39. Stellwagen, E. (1978). Heme exposure as the determinate of oxidation-reduction potential of heme proteins. Nature 275: 73-74.
40. Chen, Z., Ost, T.W.B., Schelvis, J.P.M. (2004). Phe393 mutants of cytochrome P450 BM3 with modified heme redox potentials have altered heme vinyl and proprionate conformations. Biochemistry 43: 1798-1808.
41. Mao, J., Hauser, K., Gunner, M.R. (2003). How cytochromes with different folds control heme redox potentials. Biochemistry 42: 9829-9840.
42. Bispo, J.A.C., Landini, G.F., Santos, J.L.R., Norberto, D.R., Bonafe, C.F.S. (2005). Tendency for oxidation of annelid hemoglobin at alkaline pH and dissociated states probed by redox titration. Comp. Biochem. Physiol. 141B: 498-504.