Improved blood substitute: Evaluation of its effects on human endothelial cells

ASAIO Journal

Volumn 44, Issue 5, 1998, Pages

  Simoni, Jan ^a   Simoni, Grace ^a   Martinez Zaguilan, Raul ^a   Wesson, Donald E ^a   Lox, Charles D ^a   Prien, Samuel D ^a   Kumar, Ramana Vijay ^b  

^a TEXAS TECH UNIVERSITY HEALTH SCIENCES CENTER SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; CYTOLOGY; HEMOGLOBIN; MOLECULAR DYNAMICS; NITROGEN OXIDES;

INFLAMMATORY RESPONSES;

BLOOD SUBSTITUTES;

8 ISOPROSTAGLANDIN F2 ALPHA; ADENOSINE; GLUTATHIONE; HEMOGLOBIN; INTERCELLULAR ADHESION MOLECULE 1; PROSTAGLANDIN F2 ALPHA DERIVATIVE; UNCLASSIFIED DRUG; VASOCONSTRICTOR AGENT;

ARTICLE; BLOOD SUBSTITUTION; CALCIUM TRANSPORT; CONTROLLED STUDY; CORONARY ARTERY; ENDOTHELIUM CELL; HEMOGLOBIN DETERMINATION; HUMAN; HUMAN CELL; HUMAN TISSUE; QUALITY CONTROL; VASOCONSTRICTION;

EID: 0032169962     PISSN: 10582916     EISSN: None     Source Type: Journal    
DOI: 10.1097/00002480-199809000-00007     Document Type: Article

References (95)

1. Hess JR: Blood substitutes. Sem Hematol 33: 369-378, 1996.
2. Kasper SM, Walter M, Grune F, et al: Effect of hemoglobin-based oxygen carrier (HBOC-201) on hemodynamics and oxygen transport in patients undergoing preoperative hemodilation for elective abdominal aortal surgery. Anesth Anal 83: 921 -927, 1966.
3. Swam SK, Halstenson CE, Collins AJ, et al: Pharmacological profile of diaspirin cross-linked hemoglobin in hemodialysis patients. Am J Kidney Dis 26: 918-923, 1995.
4. Viele MK, Weiskopf RB, Fisher D: Recombinant human hemoglobin does not affect renal function in humans: analysis of safety and pharmacokinetics. Anesthesiology 86: 848-858, 1997.
5. O'Hara JF, Tetzlaff JE, Sintean ME, et al: Diaspirin cross-linked hemoglobin increases serum amylase in humans postoperatively. Anesth Analg 86(Suppl): S143, 1998.
6. Twenty four of fifty two die in tests of blood substitute. Chicago Tribune April 12, 1998.
7. Waschke KF, Frietsch TH, Wuintel M, et al. Hemoglobin solutions. Acta Anaesth Scand 41: 259-263, 1997.
8. Winslow RM: Hemoglobin-Based Red Blood Cell Substitutes. Baltimore, John Hopkins University Press, 1992.
9. Hess JR, Macdonald VW, Gomez CS, et al: Increased vascular resistance with hemoglobin based oxygen carriers. Artif Cells Blood Substit Immobil Biotechnol 22: 361-372, 1994.
10. Macdonald VW, Motterlini R: Vasoconstrictor effect in isolated rabbit heart perfused with bis (3,5-dibromosalicyl) fumarate cross-linked hemoglobin. Artif Cells Blood Substit Immobil Biotechnol 22: 565-575, 1994.
11. Alayash AI: Hemoglobin based blood substitutes: potential free radical toxicity. Free Rad Biol Med 16: 137-138, 1994.
12. Simoni J, Feola M, Canizaro PC: Generation of free oxygen radicals and toxicity of hemoglobin solutions. Biomater Artif Cells Artif Organs 18: 189-202, 1990.
13. Chang TMS: Past present and future prospective on the 40th anniversary of hemoglobin based blood substitutes. Artif Cells Blood Substit Immobil Biotechnol 24: ix-xxiv, 1996.
14. Simoni J, Feola M, Tran R, et al: Biocompatibility of hemoglobin solutions: II. The inflammatory reactions of human monocytes and mouse peritoneal macrophages. Artif Organs 14: 98-109, 1990.
15. Smith DJ, Winslow RM: Effects of extraerythrocytic hemoglobin and its components on mononuclear cell procoagulant activity. J Lab Clin Med 119: 176-182, 1992.
16. Simoni J, Simoni G, Lox CD, et al: Reaction of human endothelial cells to bovine hemoglobin solution and tumor necrosis factor. Artif Cells Blood Substit Immobil Biotechnol 22: 777-787, 1994.
17. Simoni J, Simoni G, Lox CD, et al: Cytokines and PAF release from human monocytes and macrophages: effect of hemoglobin and contaminants. Artif Cells Blood Substit Immobil Biotechnol 22: 525-534, 1994.
18. Motterlini R, Foresti R, Vandergriff K, et al: Oxidative-stress response in vascular endothelial cells exposed to acellular hemoglobin solutions. Am J Physiol 269: H648-644, 1995.
19. Bloom O, Wang H, Vishnubhakat J, et al: Hemoglobin participates in enhancing tumor necrosis factor (TNF) production by stimulated macrophages (Abstract). FASEB J 11: A201, 1997.
20. McFaul SJ, Bowman PD, Villa VM, et al: Hemoglobin stimulates mononuclear leukocytes to release interleukin-8 and tumor necrosis factor alpha. Blood 84: 3175-3181, 1994.
21. Feola M, Simoni J, Fishman D, et al: Biocompatibility of hemoglobin solutions: I. Reactions of vascular endothelial cells to pure and impure hemoglobins. Artif Organs 13: 209-215, 1989.
22. Feola M, Simoni J, Canizaro PC: Polyhemoglobin stabilized by purine derivatives and glutathione. European patent no. EP507870, 1996.
23. Feola M, Simoni J, Canizaro PC: Blood substitute. U.S. patent no. 5439882, 1995.
24. Simoni J, Simoni C, Newman G, et al. An improved blood substitute: in vivo evaluation of its hemodynamic effects. ASAIO J 42: M773-M782, 1996.
25. Simoni J, Simoni C, Hartsell A, et al. An improved blood substitute: in vivo evaluation of its renal effects. ASAIO J 43: M714-M725, 1997.
26. Simoni J, Simoni G, Lox CD, et al. Evidence for the direct inhibition of endothelin-1 secretion by hemoglobin in human endothelial cells. ASAIO J 41: M641-M651, 1995.
27. Simoni J, Simoni G, Lox CD, et al. Modified Hb solution with desired pharmacological properties, does not activate the transcription factor NF-kappa B in human vascular endothelial cells. Artif Cells Blood Substit Immobil Biotechnol 25: 193-210, 1997.
28. Simoni J, Simoni G, Lox CD, et al. Expression of adhesion molecules and von Willebrand factor in human coronary artery endothelial cells incubated with differently modified hemoglobin solutions. Artif Cells Blood Substit Immobil Biotechnol 25: 211-225, 1997.
29. Feola M, Simoni J, Canizaro PC: Quality control of hemoglobin solutions: I. The purity of hemoglobin before modification. Artif Organs 15: 243-248, 1991.
30. Feola M, Simoni J, Canizaro PC, et al. Toxicity of polymerized hemoglobin solutions. Surg Gynecol Obstet 166: 211-222, 1988.
31. Simoni J, Simoni G, Feola M: Chromatographic analysis of biopolymers distribution in 'poly-hemoglobin', and intermolecularly cross-linked hemoglobin solution. Anal Chim Acta 279: 73-88, 1993.
32. Simoni J, Simoni G, Feola M, et al. Evaluation of anion-exchange liquid chromatography for purification of hemoglobin from peptides and other proteins. Anal Chim Acta 249: 169-183, 1991.
33. Simoni J, Simoni G, Garcia EL, et al. Protective effect of selenium on hemoglobin mediated lipid peroxidation. Artif Cells Blood Substit Immobil Biotechnol 23: 469-486, 1995.
34. 2+ using the fluorescence of SNARF-1 and Fura-2. Am J Physiol 260: C297-C307, 1991.
35. Morrow JD, Hill KE, Burk RF, et al. A series of prostaglandin F2-like compounds are produced in vivo in humans by a noncyclooxygenase free radical-catalyzed mechanism. Proc Natl Acad Sci U S A 87: 9383-9387, 1990.
36. Morrow JD, Robberts LJ: The isoprostanes: current knowledge and directions for future research. Biochem Pharmacol 51: 1-9, 1996.
37. Archer S: Measurement of nitric oxide in biological models. FASEB 77: 349-360, 1993.
38. Alayash AI, Fratantoni JC, Bonaventura C, et al: Nitric oxide binding to human ferrihemoglobins cross-linked between either a of β subunits. Arch Biochem Biophys 303: 332-338, 1993.
39. Jia L, Bonaventura C, Bonaventura J, et al: S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control. Nature 380: 221-226, 1996.
40. Foresti R, Clark JE, Green CJ, et al. Thiol compounds interact with nitric oxide in regulating heme oxygenase-1 induction in endothelial cells. J Biol Chem 272: 18411-18417, 1997.
41. Vane JR, Anggard EE, Botting RM: Regulatory functions of the vascular endothelium. N Engl J Med 323: 27-36, 1990.
42. Mantovani A, Bussolino F, Dejana E: Cytokine regulation of endothelial cell function. FASEB J 6: 2591-2599, 1992.
43. Koch T, Duckner HP, Heller A, et al: Effect of stroma-free hemoglobin solutions on pulmonary vascular resistance and mediator release in the isolated perfused rabbit lung. Shock 1: 146-152, 1994.
44. Vollrath B, Chan P, Findlay M, et al: Lazaroids and deferoxamine attenuate the intracellular effects of oxyhaemoglobin in vascular smooth muscle. Cardiovas Res 30: 619-626, 1995.
45. Toda N: Mechanisms of contracting action of oxyhemoglobin in isolated monkey and dog cerebral arteries. Am J Physiol 258: H57-H63, 1990.
46. Kim HW, Greenburg AG: Ferrous hemoglobin scavenging of endothelium derived nitric oxide is a principal mechanism from hemoglobin mediated vasoactivities in isolated rat thoracic aorta. Artif Cells Blood Substit Immobil Biotechnol 25: 121-133, 1997.
47. Moncada S, Palmer RMJ, Higgs EA: Nitric oxide physiology, pathophysiology, and pharmacology. Pharmacol Rev 43: 109-142, 1991.
48. Mian KB, Martin E: Differential sensitivity of basal and acetylcholine-stimulated activity of nitric oxide to destruction by superoxide anion in rat aorta. Br J Pharmacol 115: 993-1000, 1995.
49. Schultz SC, Grady B, Cole F, et al: A role for endothelin and nitric oxide in the pressor response to diaspirin cross-linked hemoglobin. J Lab Clin Med 122: 301-308, 1993.
50. Tai J, Kim HW, Greenburg AG: Endothelin-1 is not involved in hemoglobin associated vasoactivities. Artif Cells Blood Substit Immobil Biotechnol 25: 135-140, 1997.
51. Liberthal W, Wolf EF, Merril EW, et al: Hemodynamic effects of stroma free hemolysates in the isolated perfused rat kidney. Life Sci 41: 2525-2533, 1987.
52. Zilletti L, Ciuffi M, Franchi-Micheli S, et al: Cyclo-oxygenase activity of hemoglobin. Methods Enzymology 231: 562-573, 1994.
53. Burhop KE, Farrel L, Nigro C, et al: Effects of intravenous infusion of diaspirin cross-linked hemoglobin (DCLHb™) on sheep. Biomater Artif Cells Immobil Biotechnol 20: 581-585, 1992.
54. Feola M, Simoni J, Tran R, et al: Toxic factors in the red blood cell membrane. J Trauma 29: 1065-1075, 1989.
55. John GW, Valentin JP: Analysis of the pulmonary hypertensive effects of the isoprostane derivative, 8-iso PGF 2 alpha in the rat. Br J Pharmacol 122: 899-905, 1997.
56. Mohler ER, Franklin MT, Adam LP: Intracellular signaling by 8-epi-prostaglandin F2 alpha is mediated by thromboxane A2/ prostaglandin endoperoxide receptors in porcine carotid arteries. Biochem Biophys Res Commun 225: 915-923, 1996.
57. Sametz W, Prasthofer S, Krobuschek T, et al: Vascular effects of isoprostanes (Abstract). Arch Pharmacol 356: A25, 1997.
58. Jourdan KB, Evans TW, Curzen NP, et al: Evidence for a dilator function of 8-iso prostaglandin F2α in rat pulmonary artery. Br J Pharmacol 120: 1280-1285, 1997.
59. Alayash AI, Fratantoni JC, Bonaventura C, et al: Consequences of chemical modification on the free radical reactions of human hemoglobin. Arch Biochem Biophys 298: 114-120, 1992.
60. Harrel S, Kanner J: The generation of ferryl or hydroxyl radicals during interaction of haemoproteins with hydrogen peroxide. Free Radic Res Commun 5: 21-33, 1988.
61. Yoshida Y, Kashiba K, Niki E: Free radical mediated oxidation of lipid induced by hemoglobin in aqueous dispersions. Biochem Biophys Acta 120: 165-172, 1994.
62. i elevation induced by erythrocyte components in endothelial cells. J Pharmacol Exp Ther 277: 1501-1509, 1966.
63. Shasby DM, Yorek M, Shasby SS: Exogenous oxidants initiate hydrolysis of endothelial cell inositol phospholipids. Blood 72: 481-499, 1988.
64. Berridge MJ, Irvine RF: Inositol trisphosphate, a novel second messenger in cellular signal transduction. Nature 312: 315-319, 1984.
65. Somers M, Gawryl M, Siegel NJ, et al: Interaction of ultrapure hemoglobin (Hb) with renal epithelial cells (Abstract). Artif Cells Blood Substit Immobil Biotechnol 22: A163, 1994.
66. Suttorp N, Weber U, Welsch T, et al: Role of phosphodiesterases in the regulation of endothelial permeability in vivo. J Clin Invest 91: 1421-1428, 1993.
67. Grimm S, Baeuerle PA: The inducible transcription factor NF-kappa B: structure-function relationship of its protein subunits. Biochem J 290: 297-308, 1993.
68. Parry GC, Mackman N: A set of inducible genes expressed by activated human monocytic and endothelial cells contain kappa B-like sites that specifically bind c-rel-p65 heterodimers. J Biol Chem 269: 20823-20825, 1994.
69. Thanos D, Maniatis T: NF-kappa B: lesson in family values. Cell 80: 529-532, 1995.
70. Siebenlist U, Franzoso G, Brown K: Structure, regulation and function of NF-kappa B. Annu Rev Cell Biol 10: 405-455, 1994.
71. Schreck R, Albermann K, Baeuerle PA: Nuclear factor kappa B: an oxidative stress responsive transcription factor of eukariotic cells. Free Rad Res Commun 17: 221-237, 1992.
72. Toledano MB, Leonard WJ: Modulation of transcription factor NF-kappa B binding activity by oxidation-reduction in vitro. Proc Natl Acad Sci U S A 88: 4328-4332, 1991.
73. 2+ in oxidant-induced NF-kappa B activation. FEBS Lett 385: 58-62, 1996.
74. Anadalibi A, Liao F, Imes S, et al: Oxidized lipoproteins influence gene expression by causing oxidative stress and activating the transcription factor NF-kappa B. Biochem Soc Trans 21: 651-655, 1993.
75. Henning B, Toborek M, Joshi-Barve S, et al: Linoleic acid activates nuclear transcription factor-kappa B (NF-kappa B) and induced NF-kappa B-dependent transcription in cultured endothelial cells. Am J Clin Nutr 63: 322-328, 1996.
76. Billings RE, Przybocki JM, Stoll AC, et al: Hepatic inflammatory responses to αα-crosslinked hemoglobin infusion in rats. VII International Symposium on Blood Substitutes, Program & Abstracts, Waseda University, Tokyo, September 7-10, 1997, p. 90.
77. Balla G, Vercellotti GM, Muller-Eberhard U, et al: Exposure of endothelial cells to free heme potentiates damage mediated by granulocytes and toxic oxygen species. Lab Invest 64: 648-655, 1991.
78. Johnson RA, Lavesa M, Askari B, et al: A heme oxygenase product, presumably carbon monoxide, mediates a vasodepressor function in rats. Hypertension 25: 166-169, 1995.
79. Lavrovsky Y, Schwartzman ML, Levere RD, et al: Identification of binding sites for transcription factors NF-kappa B and AP-2 in the promoter region of the human oxygenase-1 gene. Proc Natl Acad Sci U S A 91: 5987-5991, 1994.
80. Benton LD, Khan M, Greco RS, et al: Integrins, adhesion molecules and surgical research. Surg Gynecol Obstet 177: 311-327, 1993.
81. Daval JL, Nehling A, Nicolas F: Physiological and pharmacological properties of adenosine: therapeutic implications. Life Sci 49: 1435-1453, 1991.
82. Hayens J Jr, Obuako B, Thompson WJ, et al. Adenosine induced vasodilation: receptor characterization in pulmonary circulation. Am J Physiol 266: H1862-1868, 1995.
83. Yamagishi T, Yaginisawa T, Satoh K, et al: Relaxant mechanism of cyclic AMP-increasing agents in porcine coronary artery. Eur J Pharmacol 251: 253-262, 1994.
84. Silver PJ, Walus K, DiSalvo J: Adenosine-mediated relaxation and activation of cyclic AMP-dependent protein kinase in coronary arterial smooth muscle. J Pharmacol Exper Ther 228: 342-347, 1984.
85. Matsunaga T, Okumura K, Tsunoda R, et al: Role of adenosine in regulation of coronary flow in dogs with inhibited synthesis of endothelium-derived nitric oxide. Am J Physiol 270: H427-434, 1996.
86. Cronstein BN: Adenosine, an endogenous anti-inflammatory agent. J Appl Physiol 76: 5-13, 1994.
87. Maggirwar SB, Dhanraj DN, Somani SM, et al: Adenosine acts as an endogenous activator of the cellular antioxidant defense system. Biochem Biophys Res Commun 201: 508-515, 1994.
88. Bouma MG, Stad RK, van der Wildenberg FAJM, et al: Differential regulatory effects of adenosine on cytokine release by activated human monocytes. J Immunol 153: 4159-4168, 1994.
89. Bouma MG, van der Wildenberg FAJM, Buurman WA: Adenosine inhibits cytokine release and expression of adhesion molecules by activated human endothelial cells. Am J Physiol 270: C522-C559, 1996.
90. Adkins WK, Barnard JW, May S, et al. Compounds that increase cAMP prevent ischemia-reperfusion pulmonary capillary injury. J Appl Physiol 72: 492-497, 1992.
91. Morandini R, Ghanem G, Portier-Lemarie A, et al: Action of cAMP on expression and release of adhesion molecules in human endothelial cells. Am J Physiol 270: H807-H816, 1996.
92. Ghersa P, van Huijsduijnen RH, Whelan J, et al: Inhibition of E-selectin gene transcription through a cAMP-dependent protein kinase pathway. J Biol Chem 269: 29129-29137, 1994.
93. 2+ by cAMP in vascular smooth muscle cells. Am J Physiol 258: C300-C407, 1990.
94. Jans DA: The regulation of protein transport to the nucleus by phosphorylation. Biochem J 311: 705-716, 1995.
95. Ramkumar V, Nie Z, Rybak LP, et al: Adenosine, antioxidant enzymes and cytoprotection. Trends Pharmacol Sci 16: 283-285, 1995.