NO reactions with sol-gel and solution phase samples of the ferric nitrite derivative of HbA

Nitric Oxide - Biology and Chemistry

Volumn 22, Issue 2, 2010, Pages 180-190

  Roche, Camille J ^a   Friedman, Joel M ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

Dinitrogentrioxide; Hemoglobin; Nitric oxide; Nitrite; S nitrosolation; Sol gel

Indexed keywords

CHEMICAL COMPOUND; CYANIDE; DINITROGEN TRIOXIDE; FERRIC ION; FLUORESCENT DYE; FLUORIDE SODIUM; GLUTATHIONE; HEMOGLOBIN; HEMOGLOBIN DERIVATIVE; METHEMOGLOBIN; NITRIC OXIDE; NITRITE; REACTIVE NITROGEN SPECIES; S NITROSOTHIOL; UNCLASSIFIED DRUG;

ABSORPTION SPECTROSCOPY; ARTICLE; CHEMICAL INTERACTION; CHEMICAL REACTION; ENCAPSULATION; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE; SOLUTION AND SOLUBILITY;

ADULT; GELS; HEMOGLOBINS; HUMANS; IRON; NITRIC OXIDE; NITRITES; NITROGEN OXIDES; OXIDATION-REDUCTION; SOLUTIONS;

EID: 75149123823     PISSN: 10898603     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.niox.2009.11.003     Document Type: Article

References (68)

1. Frei A.C., Guo Y., Jones D.W., Pritchard Jr. K.A., Fagan K.A., Hogg N., and Wandersee N.J. Vascular dysfunction in a murine model of severe hemolysis. Blood 112 (2008) 398-405
2. Hsu L.L., Champion H.C., Campbell-Lee S.A., Bivalacqua T.J., Manci E.A., Diwan B.A., Schimel D.M., Cochard A.E., Wang X., Schechter A.N., Noguchi C.T., and Gladwin M.T. Hemolysis in sickle cell mice causes pulmonary hypertension due to global impairment in nitric oxide bioavailability. Blood 109 (2007) 3088-3098
3. Minneci P.C., Deans K.J., Shiva S., Zhi H., Banks S.M., Kern S., Natanson C., Solomon S.B., and Gladwin M.T. Nitrite reductase activity of hemoglobin as a systemic nitric oxide generator mechanism to detoxify plasma hemoglobin produced during hemolysis. Am. J. Physiol. Heart Circ. Physiol. 295 (2008) H743-H754
4. Cabrales P., Tsai A.G., Winslow R.M., and Intaglietta M. Extreme hemodilution with PEG-hemoglobin vs. PEG-albumin. Am. J. Physiol. 289 (2005) H2392-H2400
5. 2 during extreme hemodilution with hemoglobin site specifically PEGylated at Cys-93(beta) in hamster window chamber. Am. J. Physiol. 287 (2004) H1609-H1617
6. Wettstein R., Tsai A.G., Erni D., Winslow R.M., and Intaglietta M. Resuscitation with MalPEG-hemoglobin improves microcirculatory blood flow and tissue oxygenation after hemorrhagic shock in awake hamsters. Crit. Care Med. 31 (2003) 1824-1830
7. Cabrales P., and Friedman J. PEGylated hemoglobins mechanisms to avoid vasoconstriction and maintain perfusion. Transfus. Altern. Transfus. Med. 9 (2007) 281-293
8. 2 affinity and tissue oxygenation. Biochem. J. 405 (2007) 503-511
9. Cooper C.E. Radical producing and consuming reactions of hemoglobin: how can we limit toxicity?. Artif. Organs 33 (2009) 110-114
10. Fitzpatrick C.M., Savage S.A., Kerby J.D., Clouse W.D., and Kashyap V.S. Resuscitation with a blood substitute causes vasoconstriction without nitric oxide scavenging in a model of arterial hemorrhage. J. Am. Coll. Surg. 199 (2004) 693-701
11. Fronticelli C., and Koehler R.C. Design of recombinant hemoglobins for use in transfusion fluids. Crit. Care Clin. 25 (2009) 357-371 (Table of contents)
12. D. Irwin, P.W. Buehler, A.I. Alayash, Y. Jia, J. Bonventura, B. Foreman, M. White, R. Jacobs, B. Piteo, M.C. Tissotvanpatot, K.L. Hamilton, R.W. Gotshall, Mixed S -nitrosylated polymerized bovine hemoglobin species moderate hemodynamic effects in acute hypoxic rats, Am. J. Respir. Cell Mol. Biol. (2009), in press.
13. Jahr J.S., Walker V., and Manoochehri K. Blood substitutes as pharmacotherapies in clinical practice. Curr. Opin. Anaesthesiol. 20 (2007) 325-330
14. Kim H.W., and Greenburg A.G. Hemoglobin mediated vasoactivity in isolated vascular rings. Artif. Cells Blood Substit. Immobil. Biotechnol. 23 (1995) 303-309
15. Kim H.W., and Greenburg A.G. Mechanisms for vasoconstriction and decreased blood flow following intravenous administration of cell-free native hemoglobin solutions. Adv. Exp. Med. Biol. 566 (2005) 397-401
16. Mongan P.D., Moon-Massat P.F., Rentko V., Mihok S., Dragovich A., and Sharma P. Regional blood flow after serial normovolemic exchange transfusion with HBOC-201 (Hemopure) in anesthetized swine. J. Trauma 67 (2009) 51-60
17. Raat N.J., Liu J.F., Doyle M.P., Burhop K.E., Klein J., and Ince C. Effects of recombinant-hemoglobin solutions rHb2.0 and rHb1.1 on blood pressure, intestinal blood flow, and gut oxygenation in a rat model of hemorrhagic shock. J. Lab. Clin. Med. 145 (2005) 21-32
18. Serruys P.W., Vranckx P., Slagboom T., Regar E., Meliga E., de Winter R.J., Heyndrickx G., Schuler G., van Remortel E.A., Dube G.P., and Symons J. Haemodynamic effects, safety, and tolerability of haemoglobin-based oxygen carrier-201 in patients undergoing PCI for CAD. EuroIntervention 3 (2008) 600-609
19. Lui F.E., Dong P., and Kluger R. Polyethylene glycol conjugation enhances the nitrite reductase activity of native and cross-linked hemoglobin. Biochemistry 47 (2008) 10773-10780
20. Tsai A.G., Cabrales P., Manjula B.N., Acharya S.A., Winslow R.M., and Intaglietta M. Dissociation of local nitric oxide concentration and vasoconstriction in the presence of cell-free hemoglobin oxygen carriers. Blood 108 (2006) 3603-3610
21. Ignarro L.J., Edwards J.C., Gruetter D.Y., Barry B.K., and Gruetter C.A. Possible involvement of S-nitrosothiols in the activation of guanylate cyclase by nitroso compounds. FEBS Lett. 110 (1980) 275-278
22. Ramachandran N., Root P., Jiang X.M., Hogg P.J., and Mutus B. Mechanism of transfer of NO from extracellular S-nitrosothiols into the cytosol by cell-surface protein disulfide isomerase. Proc. Natl. Acad. Sci. USA 98 (2001) 9539-9544
23. Zhang Y., and Hogg N. S-nitrosothiols: cellular formation and transport. Free Radic. Biol. Med. 38 (2005) 831-838
24. Hogg N. The biochemistry and physiology of S-nitrosothiols. Annu. Rev. Pharmacol. Toxicol. 42 (2002) 585-600
25. Hogg N. Biological chemistry and clinical potential of S-nitrosothiols. Free Radic. Biol. Med. 28 (2000) 1478-1486
26. Foster M.W., Pawloski J.R., Singel D.J., and Stamler J.S. Role of circulating S-nitrosothiols in control of blood pressure. Hypertension 45 (2005) 15-17
27. Liu L., Yan Y., Zeng M., Zhang J., Hanes M.A., Ahearn G., McMahon T.J., Dickfeld T., Marshall H.E., Que L.G., and Stamler J.S. Essential roles of S-nitrosothiols in vascular homeostasis and endotoxic shock. Cell 116 (2004) 617-628
28. - donation by S-nitrosothiols: implications for regulation of physiological functions by S-nitrosylation and acceleration of disulfide formation. Arch. Biochem. Biophys. 318 (1995) 279-285
29. Stamler J.S. S-nitrosothiols and the bioregulatory actions of nitrogen oxides through reactions with thiol groups. Curr. Top. Microbiol. Immunol. 196 (1995) 19-36
30. Angelo M., Singel D.J., and Stamler J.S. An S-nitrosothiol (SNO) synthase function of hemoglobin that utilizes nitrite as a substrate. Proc. Natl. Acad. Sci. USA 103 (2006) 8366-8371
31. Stamler J.S., Jia L., Eu J.P., McMahon T.J., Demchenko I.T., Bonaventura J., Gernert K., and Piantadosi C.A. Blood flow regulation by S-nitrosohemoglobin in the physiological oxygen gradient. Science 276 (1997) 2034-2037
32. Fernandez B.O., and Ford P.C. Nitrite catalyzes ferriheme protein reductive nitrosylation. J. Am. Chem. Soc. 125 (2003) 10510-10511
33. Fernandez B.O., Lorkovic I.M., and Ford P.C. Mechanisms of ferriheme reduction by nitric oxide: nitrite and general base catalysis. Inorg. Chem. 43 (2004) 5393-5402
34. Gow A.J., and Stamler J.S. Reactions between nitric oxide and haemoglobin under physiological conditions. Nature 391 (1998) 169-173
35. Jia L., Bonaventura C., Bonaventura J., and Stamler J.S. S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control. Nature 380 (1996) 221-226
36. Gow A.J., Luchsinger B.P., Pawloski J.R., Singel D.J., and Stamler J.S. The oxyhemoglobin reaction of nitric oxide. Proc. Natl. Acad. Sci. USA 96 (1999) 9027-9032
37. Luchsinger B.P., Rich E.N., Gow A.J., Williams E.M., Stamler J.S., and Singel D.J. Routes to S-nitroso-hemoglobin formation with heme redox and preferential reactivity in the beta subunits. Proc. Natl. Acad. Sci. USA 100 (2003) 461-466
38. McMahon T.J., and Stamler J.S. Concerted nitric oxide/oxygen delivery by hemoglobin. Methods Enzymol. 301 (1999) 99-114
39. Salgado M.T., Nagababu E., and Rifkind J.M. Quantification of intermediates formed during the reduction of nitrite by deoxyhemoglobin. J. Biol. Chem. 284 (2009) 12710-12718
40. Nagababu E., Ramasamy S., and Rifkind J.M. Intermediates detected by visible spectroscopy during the reaction of nitrite with deoxyhemoglobin: the effect of nitrite concentration and diphosphoglycerate. Biochemistry 46 (2007) 11650-11659
41. Gladwin M.T., and Kim-Shapiro D.B. The functional nitrite reductase activity of the heme-globins. Blood 112 (2008) 2636-2647
42. Gladwin M.T., Grubina R., and Doyle M.P. The new chemical biology of nitrite reactions with hemoglobin: R-state catalysis, oxidative denitrosylation, and nitrite reductase/anhydrase. Acc. Chem. Res. 42 (2008) 157-167
43. Roche C.J., Dantsker D., Samuni U., and Friedman J.M. Nitrite reductase activity of sol-gel-encapsulated deoxyhemoglobin. Influence of quaternary and tertiary structure. J. Biol. Chem. 281 (2006) 36874-36882
44. Gladwin M.T., Raat N.J., Shiva S., Dezfulian C., Hogg N., Kim-Shapiro D.B., and Patel R.P. Nitrite as a vascular endocrine nitric oxide reservoir that contributes to hypoxic signaling, cytoprotection, and vasodilation. Am. J. Physiol. Heart Circ. Physiol. 291 (2006) H2026-H2035
45. Huang Z., Shiva S., Kim-Shapiro D.B., Patel R.P., Ringwood L.A., Irby C.E., Huang K.T., Ho C., Hogg N., Schechter A.N., and Gladwin M.T. Enzymatic function of hemoglobin as a nitrite reductase that produces NO under allosteric control. J. Clin. Invest. 115 (2005) 2099-2107
46. Isbell T.S., Gladwin M.T., and Patel R.P. Hemoglobin oxygen fractional saturation regulates nitrite-dependent vasodilation of aortic ring bioassays. Am. J. Physiol. Heart Circ. Physiol. 293 (2007) H2565-H2572
47. Grubina R., Basu S., Tiso M., Kim-Shapiro D.B., and Gladwin M.T. Nitrite reductase activity of hemoglobin S (sickle) provides insight into contributions of heme redox potential versus ligand affinity. J. Biol. Chem. 283 (2008) 3628-3638
48. 3 by the concerted nitrite reductase and anhydrase activity of hemoglobin. Nat. Chem. Biol. 3 (2007) 785-794
49. Navati M.S., and Friedman J.M. Reactivity of glass-embedded met hemoglobin derivatives toward external NO: implications for nitrite-mediated production of bioactive NO. J. Am. Chem. Soc. 131 (2009) 12273-12279
50. Samuni U., Roche C., Dantsker D., and Friedman J. T- and R-state tertiary relaxations in sol-gel encapsulated haemoglobin. In: Bolognesi M., di Prisco G., and Verde C. (Eds). Dioxygen Binding and Sensing Proteins. A Tribute to Beatrice and Jonathan Wittenberg (2008), Springer, Springer Berlin Heidelberg New York 133-159
51. Samuni U., Roche C.J., Dantsker D., Juszczak L.J., and Friedman J.M. Modulation of reactivity and conformation within the T-quaternary state of human hemoglobin: the combined use of mutagenesis and sol-gel encapsulation. Biochemistry 45 (2006) 2820-2835
52. Viappiani C., Bettati S., Bruno S., Ronda L., Abbruzzetti S., Mozzarelli A., and Eaton W.A. New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels. Proc. Natl. Acad. Sci. USA 101 (2004) 14414-14419
53. Samuni U., Dantsker D., Khan I., Friedman A.J., Peterson E., and Friedman J.M. Spectroscopically and kinetically distinct conformational populations of sol-gel-encapsulated carbonmonoxy myoglobin. A comparison with hemoglobin. J. Biol. Chem. 277 (2002) 25783-25790
54. Shibayama N., and Saigo S. Direct observation of two distinct affinity conformations in the T state human deoxyhemoglobin. FEBS Lett. 492 (2001) 50-53
55. Mozzarelli A., and Bettati S. Functional properties of immobilized proteins. In: Nalwa H. (Ed). Advanced Functional Molecules and Polymers (2001), Gordon and Breach Science Publishers, Amsterdam 55-97
56. Khan I., Dantsker D., Samuni U., Friedman A.J., Bonaventura C., Manjula B., Acharya S.A., and Friedman J.M. Beta 93 modified hemoglobin: kinetic and conformational consequences. Biochemistry 40 (2001) 7581-7592
57. Bruno S., Bonaccio M., Bettati S., Rivetti C., Viappiani C., Abbruzzetti S., and Mozzarelli A. High and low oxygen affinity conformations of T state hemoglobin. Protein Sci. 10 (2001) 2401-2407
58. Abbruzzetti S., Viappiani C., Bruno S., Bettati S., Bonaccio M., and Mozzarelli A. Functional characterization of heme proteins encapsulated in wet nanoporous silica gels. J. Nanosci. Nanotechnol. 1 (2001) 407-415
59. Khan I., Shannon C.F., Dantsker D., Friedman A.J., Perez-Gonzalez-de-Apodaca J., and Friedman J.M. Sol-gel trapping of functional intermediates of hemoglobin: geminate and bimolecular recombination studies. Biochemistry 39 (2000) 16099-16109
60. Das T.K., Khan I., Rousseau D.L., and Friedman J.M. Temperature dependent quaternary state relaxation in sol-gel encapsulated hemoglobin. Biospectroscopy 5S (1999) 64-70
61. Samuni U., Roche C., Danstker D., and Friedman F. T and R State Tertiary Relaxations in Sol-Gel Encapsulated Hemoglobin (2008), Springer
62. Chen Q., Lalezari I., Nagel R.L., and Hirsch R.E. Liganded hemoglobin structural perturbations by the allosteric effector L35. Biophys. J. 88 (2005) 2057-2067
63. Lalezari I., Lalezari P., Poyart C., Marden M., Kister J., Bohn B., Fermi G., and Perutz M.F. New effectors of human hemoglobin: structure and function. Biochemistry 29 (1990) 1515-1523
64. 2-affinity-inducing central cavity cross-bridges. J. Protein Chem. 19 (2000) 255-267
65. Marden M.C., Bohn B., Kister J., and Poyart C. Effectors of hemoglobin. Separation of allosteric and affinity factors. Biophys. J. 57 (1990) 397-403
66. Peterson E.S., Shinder R., Khan I., Juczszak L., Wang J., Manjula B., Acharya S.A., Bonaventura C., and Friedman J.M. Domain-specific effector interactions within the central cavity of human adult hemoglobin in solution and in porous sol-gel matrices: evidence for long-range communication pathways. Biochemistry 43 (2004) 4832-4843
67. Yokoyama T., Neya S., Tsuneshige A., Yonetani T., Park S.Y., and Tame J.R. R-state haemoglobin with low oxygen affinity: crystal structures of deoxy human and carbonmonoxy horse haemoglobin bound to the effector molecule L35. J. Mol. Biol. 356 (2006) 790-801
68. Kojima H., Nakatsubo N., Kikuchi K., Kawahara S., Kirino Y., Nagoshi H., Hirata Y., and Nagano T. Detection and imaging of nitric oxide with novel fluorescent indicators: diaminofluoresceins. Anal. Chem. 70 (1998) 2446-2453