Dclhb and rhb1.1

Blood Substitutes

Volumn , Issue , 2006, Pages 399-414

  Nelson, Deanna J ^a  

^a BioLink Life Sciences Inc   (United States)

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EID: 70449122770     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012759760-7/50044-5     Document Type: Chapter

References (72)

1. Apostol I. Assessing the relative stabilities of engineered hemoglobins using electrospray mass spectrometry. Anal Biochem. 1999, 272:8-18.
2. TM): Characterization of the process and the product manufactured under GMP requirements for clinical studies. Artif. Cells Blood Subst. Immob. Biotech. 1994, 22(3):701-708.
3. Baldwin A.L. Modified hemoglobins produce venular interendothelial gaps and albumin leakage to the rat mesentery. Am. J. Physiol. Heart Circ. Physiol. 1999, 277:H650-H659.
4. Baldwin A.L., Thurston G., Naemi H.A. Inhibition of nitric oxide synthesis increases venular permeability and alters endothelial actin cytoskeleton. Am. J. Physiol. Heart Circ. Physiol. 1998, 274:H1776-H1784.
5. Beckman J.S., Koppenol W.H. Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and the ugly. Am. J. Physiol. 1996, 271:C1424-C1437.
6. Brucker E.A. Genetically crosslinked hemoglobin: a structural study. Acta Crystallogr. 2000, D56:812-816.
7. Bunn H.F., Forget B.G. Hemoglobin: Molecular, Genetic, and Clinical Aspects 1986, WB Saunders Co., Philadelphia.
8. TM): Bioanalytical studies in swine. Artif. Cells Blood Subst. Immob. Biotech. 1994, 22(3):917-922.
9. Chang T.M.S. Blood Substitutes: Princi s, Methods, Products and Clinical Trials 1997, Karger, Basel.
10. Chatterjee R., Welty E.V., Walder R.Y., et al. Isolation and characterization of a new hemoglobin derivative crosslinked between the α chains (Lysine 99α 1 Lysine 99α2). J. Biol. Chem. 1986, 261(21):9929-9937.
11. Conklin J.L., Murray J., Ledlow A., et al. Effects of recombinant human hemoglobin on motor functions of the opossum esophagus. J. Pharmacol. Exper. Ther. 1995, 273:762-767.
12. Cullen J.J., Conklin J.L., Murray J., et al. Effects of recombinat human hemoglobin on opossum sphincter of Oddi motor function in vivo and in vitro. Dig. Dis. Sci. 1996, 41:289-294.
13. Doherty D.H., Doyle M.P., Curry S.R., et al. Rate of reaction with nitric oxide determines the hypertensive effect of cell-free hemoglobin. Nat. Biotechnol. 1998, 16:672-676.
14. Eich R.F., Li T., Lemon D.D., et al. Mechanism of NO-induced oxidation of myoglobin and hemoglobin. Biochemistry 1996, 35:6976-6983.
15. Fermi G., Perutz M., Shaanan B., Fourme R. The crystal structure of human deoxyhaemoglobin at 1.74- resolution. J. Molec. Biol. 1984, 175(2):159-174.
16. Fernandez E.J. Crystallographic Studies on Chemically Modified Hemoglobin. PhD thesis 1995, Loyola University, Chicago.
17. TM) on isolated porcine blood vessels. J. Lab. Clin. Med. 1995, 125:762-767.
18. TM (recombinant human hemoglobin): a therapeutic for the delivery of oxygen and the restoration of blood volume in the treatment of acute blood loss in trauma and surgery. Red Blood Cell Substitutes: Basic Principles and Clinical Applications 1998, 325-333. Marcel Dekker, Inc., New York. A.S. Rudolph, R. Rabinovici, G.Z. Feuerstein (Eds.).
19. Gibson Q.H. The reduction of methaemoglobin by ascorbic acid. Biochem. J. 1943, 37:615-618.
20. Gould S.A., Moss G.S. Clinical development of human polymerized hemoglobin as a blood substitute. World J. Surg. 1996, 20:1200-1207.
21. Gulati A., Rebello S. Role of adrenergic mechanisms in the pressor effect of diaspirin crosslinked hemoglobin. J. Lab. Clin. Med. 1994, 124:125-133.
22. Gulati A., Singh G., Rebello A., Sharma A.C. Effect of diaspirin crosslinked and stroma-free hemoglobin on mean arterial pressure and endothelin-1 concentration in rats. Life Sci. 1995, 56:1433-1442.
23. Guslandi M. Nitric oxide: an ubiquitous actor in the gastrointestinal tract. Dig. Dis. 1994, 12:28-36.
24. Hai T.T., Nelson D.J., Srnak A. Process for the production of crosslinked hemoglobin in the presence of sodium tripolyphosphate. US Patent No. 5,128,452, issued 7 July 1992 1992.
25. TM) polymerization. Artif. Cells Blood Subst. Immob. Biotech. 1994, 22(3):923-931.
26. Hai T.T., Nelson D.J., Pereira D.E., Estep T.N. Therapeutic hemoglobin composition having isotropically increased size. US Patent No. 5,981,710, issued 9 November 1999 1999.
27. Hartman J.C., Argoudelis G., Doherty D., et al. Reduced nitric oxide reactivity of a new recombinant human hemoglobin attenuates gastric dysmotility. Eur. J. Pharmacol. 1998, 363:175-178.
28. Heller A., Ragaller M., Schmeck J., et al. Role of NO and endothelin in hemoglobin-induced pulmonary vasconstriction. Shock 1998, 10:401-406.
29. Hoffman S.J., Looker D.L., Roehrich J.M., et al. Expression of fully functional tetrameric human hemoglobin in Escherichia coli. Proc. Natl. Acad. Sci. USA 1990, 87:8521-8525.
30. Jones R.T. Structural characterization of modified hemoglobins. Methods Enzymol. 1989, 231:322-343.
31. Katsuyama S.S., Cole D.J., Drummond J.C., Bradley K. Nitric oxide mediates the hyper-tensive response to a modified hemoglobin solution (DCLHb) in rats. Artif. Cells Blood Subst. Immob. Biotech. 1994, 22:1-7.
32. Kavanaugh J.S., Rogers P.H., Arnone A. High-resolution X-ray study of deoxy recombinant human hemoglobins synthesized from beta-globins having mutated amino termini. Biochemistry 1992, 31(36):8640-8647.
33. Kerwin B.A., Akers M.J., Apostol I., et al. Acute and long-term stability studies of deoxyhemoglobin and characterization of ascorbate-induced modifications. J. Pharm. Sci. 1999, 88(1):79-88.
34. Konomi H., Woods C.M., Meedeniya A.C.B., et al. Effects of diaspirin crosslinked hemoglobin on motor function of the duodenum and biliary system in the Australian brush-tailed possum in vivo. Pharmacol. Exper. Ther. 2001, 296(3):1067-1073.
35. Kroeger K.S., Kundrot C.E. Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins. Structure 1997, 5:227-237.
36. Leppäniemi A., Soltero R., Burris D., et al. Early resuscitation with low-volume polyDCLHb is effective in the treatment of shock induced by penetrating vascular injury. J. Trauma Inj. Inf. Crit. Care 1996, 40(2):242-248.
37. Levin J., Roth R.I. Interactions between hemoglobin and bacterial endotoxin in vitro and in vivo. Red Blood Cell Substitutes: Basic Principles and Clinical Applications 1998, 235-262. Marcel Dekker, Inc., New York. A.S. Rudolph, R. Rabinovici, G.Z. Feuerstein (Eds.).
38. Levine J., Weickert M., Pagratis M., et al. Identification of a nickel(II) binding site on hemoglobin which confers susceptibility to oxidative deamination and intramolecular crosslinking. J. Biol. Chem. 1998, 273(21):13037-13046.
39. Levine J., Etter J., Apostol I. Nickel-catalyzed N-terminal oxidative deamination in peptides containing histidine at position 2 coupled with sulfite oxidation. J. Biol. Chem. 1999, 274(8):4848-4857.
40. Lippincott J., Apostol I. Carbamylation of cysteine: a potential artifact in peptide mapping of hemoglobins in the presence of urea. Anal. Biochem. 1999, 267:57-64.
41. Looker D., Mathews A.J., Neway J.O., Stetler G.L. Expression of recombinant human hemoglobin in Escherichia coli. Methods Enzymol. 1994, 231:364-374.
42. Looker D.L., Apostol I.Z., Brucker E.A., et al. Reduced side-effect hemoglobin compositions. US Patent No. 6,670,323, issued 30 December 2003 2003.
43. Moo-Penn W.F., Wolff J.A., Simon G., et al. Hemoglobin Presbyterian: beta108 (G10) asparagine leads to lysine, a hemoglobin variant with low oxygen affinity. FEBS Lett. 1978, 92(1):53-56.
44. Mundy A.L., Dorrington K.L. Inhibition of nitric oxide synthesis augments pulmonary oedema in isolated perfused rabbit lung. Br. J. Anaesth. 2000, 85:570-576.
45. Nagai K., Perutz M.F., Poyart C. Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli. Proc. Natl. Acad. Sci. USA 1985, 82:7252-7255.
46. Nelson D.J. Blood substitutes: hemoglobin-based oxygen carriers. Encyclopedia of Pharmaceutical Technology 2000, 1-33. Marcel Dekker, Inc., New York. J. Swarbrick, J.C. Boylan (Eds.).
47. Nelson D.J. Blood substitutes: hemoglobin-based oxygen carriers. Encyclopedia of Pharmaceutical Technology 2002, 236-262. Marcel Dekker, Inc., New York. 2nd edn. J. Swarbrick, J.C. Boylan (Eds.).
48. Nelson D., Azari M., Brown R., et al. Preparation and characterization of diaspirin cross-linked hemoglobin solutions for preclinical studies. Biomat. Artif. Cells Immob. Biotech. 1992, 20(2-4):423-427.
49. Nelson D., Hai T., Srnak A., et al. Synthesis and properties of polymerized, diaspirin crosslinked hemoglobins. Biomat. Artif. Cells Immob. Biotech. 1992, 20(2-4):253-258.
50. Nelson D.J., Hai T.T., Srnak A. Oxirane-modified hemoglobin based composition. US Patent No. 5,248,766, issued 28 September 1993 1993.
51. O'Hara J.F., Tetzlaff J.E., Sintean M.E., et al. Diaspirin crosslinked hemoglobin increases serum amylase in humans post-operatively. Anesth. Analg. 1998, 86:143S.
52. Polmer J.J., Ryland J.R., Matthews M.A.H., et al. Purification of hemoglobin. US Patent No. 5,840,851, issued 24 November 1998 1998.
53. Rattan S., Rosenthal G.J., Chakder S. Human recombinant hemoglobin (rHb1.1) inhibits nonadrenergic noncholinergic (NANAC) nervemediated relaxation of internal anal sphincter. Pharmacol. Exper. Ther. 1995, 272(3):1211-1216.
54. Resta T.C., Walker B.R., Eichinger M.R., Doyle M.P. Rate of NO scavenging alters effects of recombinant hemoglobin solutions on pulmonary vasoreactivity. J. Appl. Physiol. 2002, 93:1327-1336.
55. Saxena R., Wijnhoud A.D., Man in't Veld A.J., et al. Effect of diaspirin crosslinked hemoglobin on endothelin-1 and blood pressure in acute ischemic stroke in man. J. Hypertens. 1998, 16:1459-1465.
56. Schultz S.C., Grady B., Cole F., et al. A role for endothelin and nitric oxide in the pressor response to diaspirin crosslinked hemoglobin. J. Lab. Clin. Med. 1993, 122:301-308.
57. Shaanan B. Structure of human oxyhaemoglobin at 2.1- resolution. J. Molec. Biol. 1983, 171(1):31-59.
58. Sharma A.C., Gulati A. Yohimbine modulates diaspirin crosslinked hemoglobin-induced systemic hemodynamics and regional circulatory effects. Crit. Care Med. 1995, 23:874-884.
59. Sharma A.C., Singh G., Gulati A. Role of NO mechanism in cardiovascular effects of diasprin crosslinked hemoglobin in anesthetized rats. Am. J. Physiol. Heart Circ. Physiol. 1995, 269:H1379-H1388.
60. Snyder S.R., Welty E.V., Walder R.Y., et al. HBXL99α. A hemoglobin derivative that is crosslinked between the α subunits is useful as a blood substitute. Proc. Natl. Acad. Sci. USA 1987, 84:7280-7284.
61. Thompson A., McGarry A.E., Valeri C.R., Lieberthal W. Stroma-free hemoglobin increases blood pressure and GFR in the hypotensive rat: role of nitric oxide. J. Appl. Physiol. 1994, 77:2348-2354.
62. Uc A., Oh S.T., Murray J.A., et al. Biphasic relaxation of the opossum lower esophageal sphincter: roles of NO, VIP, and CGRP. Am. J. Physiol. 1999, 277:G548-G554.
63. Vandegriff K.D., Winslow R.M. A theoretical analysis of oxygen transport: a new strategy for the design of hemoglobin-based red cell substitutes. Blood Substitutes: Physiological Basis of Efficacy 1996, 143-154. Birkhäuser, Boston. R.M. Winslow, K.D. Vandegriff, M. Intaglietta (Eds.).
64. Verderber E., Lucast L.J., Van Dehy J.A., et al. Role of the hemA gene product and δ-aminolevulinic acid in regulation of Escherichia coli heme synthesis. J. Bacteriol. 1997, 179(14):4583-4590.
65. Vestling C.S. The reduction of methemoglobin by ascorbic acid. J. Biol. Chem. 1942, 143:439-446.
66. Viele M.K., Weiskopf R.B., Fisher D. Recombinant human hemoglobin does not affect renal function in humans: analysis of safety and pharmacokinetics. Anesthesiology 1997, 86(4):848-858.
67. Walford G., Loscalzo J. Nitric oxide in vascular biology. J. Thromb. Haemost. 2003, 1(10):2112-2118.
68. Weickert M.J., Apostol A. High-fidelity translation of recombinant human hemoglobin in Escherichia coli. Appl. Environ. Microbiol. 1998, 64(5):1589-1593.
69. Weickert M.J., Curry S.R. Turnover of recombinant human hemoglobin in Escherichia coli occurs rapidly for insoluble and slowly for soluble globin. Arch. Biochem. Biophys. 1997, 348(2):337-346.
70. Weickert M.J., Doherty D.H., Best E.A., Olins P.O. Optimization of heterologous protein production in Escherichia coli. Curr. Opin. Biotechnol. 1996, 7:494-499.
71. Weickert M.J., Pagratis M., Curry S.R., Blackmore R. Stabilization of apoglobin by low temperature increases yield of soluble recombinant hemoglobin in Escherichia coli. Appl. Environ. Microbiol. 1997, 63(11):4313-4320.
72. Yu Z., Friso G., Miranda J.J., et al. Structural characterization of human hemoglobin crosslinked by bis(3,5-dibromosalicyl) fumarate using mass spectrometric techniques. Prot. Sci. 1997, 6:2568-2577.