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Volumn 43, Issue 8, 2007, Pages 1208-1215

An electron paramagnetic resonance investigation of the oxygen dependence of the arterial-venous gradient of nitrosyl hemoglobin in blood circulation

Author keywords

EPR; Free radicals; Hemoglobin; Nitric oxide; Oxygen saturation

Indexed keywords

HEMOGLOBIN; NITRIC OXIDE; OXYGEN;

EID: 34548506531     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2007.06.024     Document Type: Article
Times cited : (8)

References (42)
  • 1
    • 0019195506 scopus 로고
    • The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine
    • Furchgott R.F., and Zawadzki J.V. The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine. Nature 288 (1980) 373-376
    • (1980) Nature , vol.288 , pp. 373-376
    • Furchgott, R.F.1    Zawadzki, J.V.2
  • 2
    • 0023198721 scopus 로고
    • Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
    • Palmer R.M.J., Ferrige A.G., and Moncada S. Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor. Nature 327 (1987) 524-526
    • (1987) Nature , vol.327 , pp. 524-526
    • Palmer, R.M.J.1    Ferrige, A.G.2    Moncada, S.3
  • 3
    • 0023505509 scopus 로고
    • Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide
    • Igarro L.J., Buga G.M., Wood K.S., Byrns R.E., and Chaudhuri G. Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide. Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 9265-9269
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 9265-9269
    • Igarro, L.J.1    Buga, G.M.2    Wood, K.S.3    Byrns, R.E.4    Chaudhuri, G.5
  • 4
    • 11244316895 scopus 로고    scopus 로고
    • Chemical physiology of blood flow regulation by red blood cells: the role of nitric oxide and S-nitrosohemoglobin
    • Singel D.J., and Stamler J.S. Chemical physiology of blood flow regulation by red blood cells: the role of nitric oxide and S-nitrosohemoglobin. Annu. Rev. Physiol. 67 (2005) 99-145
    • (2005) Annu. Rev. Physiol. , vol.67 , pp. 99-145
    • Singel, D.J.1    Stamler, J.S.2
  • 5
    • 0038578668 scopus 로고    scopus 로고
    • Nitric oxide's reactions with hemoglobin: a view through the SNO-storm
    • Gladwin M.T., Lancaster Jr. J.R., Freeman B.A., and Schechter A.N. Nitric oxide's reactions with hemoglobin: a view through the SNO-storm. Nat. Med. 9 (2003) 496-500
    • (2003) Nat. Med. , vol.9 , pp. 496-500
    • Gladwin, M.T.1    Lancaster Jr., J.R.2    Freeman, B.A.3    Schechter, A.N.4
  • 6
    • 18444369943 scopus 로고    scopus 로고
    • Nitric oxide in the human respiratory cycle
    • McMahon T.J., Moon R.E., Luschinger B.P., et al. Nitric oxide in the human respiratory cycle. Nat. Med. 8 (2002) 711-717
    • (2002) Nat. Med. , vol.8 , pp. 711-717
    • McMahon, T.J.1    Moon, R.E.2    Luschinger, B.P.3
  • 7
    • 16444362504 scopus 로고    scopus 로고
    • Hemoglobin-mediated, hypoxia-induced vasodilation via nitric oxide: mechanism(s) and physiologic versus pathophysiologic relevance
    • Robinson J.M., and Lancaster Jr. J.R. Hemoglobin-mediated, hypoxia-induced vasodilation via nitric oxide: mechanism(s) and physiologic versus pathophysiologic relevance. Am. J. Respir. Cell Mol. Biol. 32 (2005) 257-261
    • (2005) Am. J. Respir. Cell Mol. Biol. , vol.32 , pp. 257-261
    • Robinson, J.M.1    Lancaster Jr., J.R.2
  • 8
    • 0030791742 scopus 로고    scopus 로고
    • Blood flow regulation by S-nitrosohemoglobin in the physiological oxygen gradient
    • Stamler J.S., Jia L., Eu J.P., et al. Blood flow regulation by S-nitrosohemoglobin in the physiological oxygen gradient. Science 276 (1997) 2034-2037
    • (1997) Science , vol.276 , pp. 2034-2037
    • Stamler, J.S.1    Jia, L.2    Eu, J.P.3
  • 9
    • 0029875840 scopus 로고    scopus 로고
    • S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control
    • 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
    • (1996) Nature , vol.380 , pp. 221-226
    • Jia, L.1    Bonaventura, C.2    Bonaventura, J.3    Stamler, J.S.4
  • 10
    • 0034595830 scopus 로고    scopus 로고
    • Functional coupling of oxygen binding and vasoactivity in S-nitrosohemoglobin
    • McMahon T.J., Stone A.E., Bonaventura J., Singel D.J., and Stamler J.S. Functional coupling of oxygen binding and vasoactivity in S-nitrosohemoglobin. J. Biol. Chem. 275 (2000) 16738-16745
    • (2000) J. Biol. Chem. , vol.275 , pp. 16738-16745
    • McMahon, T.J.1    Stone, A.E.2    Bonaventura, J.3    Singel, D.J.4    Stamler, J.S.5
  • 11
    • 0032848295 scopus 로고    scopus 로고
    • Biochemical characterization of S-nitrosohemoglobin: mechanisms underlying synthesis, NO release, and biological activity
    • Wolzt M., MacAllister R.J., Davis D., et al. Biochemical characterization of S-nitrosohemoglobin: mechanisms underlying synthesis, NO release, and biological activity. J. Biol. Chem. 274 (1999) 28983-28990
    • (1999) J. Biol. Chem. , vol.274 , pp. 28983-28990
    • Wolzt, M.1    MacAllister, R.J.2    Davis, D.3
  • 12
    • 0033016469 scopus 로고    scopus 로고
    • Biochemical characterization of human S-nitrosohemoglobin: effects on oxygen binding and transnitrosation
    • Patel R.P., Hogg N., Spencer N.Y., Kalyanaraman B., Matalon S., and Darley-Usmar V.M. Biochemical characterization of human S-nitrosohemoglobin: effects on oxygen binding and transnitrosation. J. Biol. Chem. 274 (1999) 15487-15492
    • (1999) J. Biol. Chem. , vol.274 , pp. 15487-15492
    • Patel, R.P.1    Hogg, N.2    Spencer, N.Y.3    Kalyanaraman, B.4    Matalon, S.5    Darley-Usmar, V.M.6
  • 13
    • 0031590450 scopus 로고    scopus 로고
    • S-nitrosohemoglobin in the fetal circulation may represent a cycle for blood pressure regulation
    • Funai E.F., Davidson A., Seligman S.P., and Finlay T.H. S-nitrosohemoglobin in the fetal circulation may represent a cycle for blood pressure regulation. Biochem. Biophys. Res. Commun. 239 (1997) 875-877
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 875-877
    • Funai, E.F.1    Davidson, A.2    Seligman, S.P.3    Finlay, T.H.4
  • 14
    • 33645528748 scopus 로고    scopus 로고
    • Lack of allosterically controlled intramolecular transfer of nitric oxide from the heme to cysteine in the β subunit of hemoglobin
    • Huang K.T., Azarov I., Basu S., Huang J., and Kim-Shapiro D.B. Lack of allosterically controlled intramolecular transfer of nitric oxide from the heme to cysteine in the β subunit of hemoglobin. Blood 107 (2006) 2602-2604
    • (2006) Blood , vol.107 , pp. 2602-2604
    • Huang, K.T.1    Azarov, I.2    Basu, S.3    Huang, J.4    Kim-Shapiro, D.B.5
  • 15
    • 0034633659 scopus 로고    scopus 로고
    • Role of circulating nitrite and S-nitrosohemoglobin in the regulation of regional blood flow in humans
    • Gladwin M.T., Shelhamer J.H., Schechter A.N., et al. Role of circulating nitrite and S-nitrosohemoglobin in the regulation of regional blood flow in humans. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 11482-11487
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 11482-11487
    • Gladwin, M.T.1    Shelhamer, J.H.2    Schechter, A.N.3
  • 16
    • 9344269955 scopus 로고    scopus 로고
    • Pulmonary vascular effects of red blood cells containing S-nitrosated hemoglobin
    • Deem S., Kim S.S., Min J.-H., et al. Pulmonary vascular effects of red blood cells containing S-nitrosated hemoglobin. Am. J. Physiol.: Heart Circ. Physiol. 287 (2004) H2561-H2568
    • (2004) Am. J. Physiol.: Heart Circ. Physiol. , vol.287
    • Deem, S.1    Kim, S.S.2    Min, J.-H.3
  • 18
    • 0141448327 scopus 로고    scopus 로고
    • EPR spectroscopy studies on the structural transition of nitrosyl hemoglobin in the arterial-venous cycle of DEANO-treated rats as it relates to the proposed nitrosyl hemoglobin/nitrosothiol hemoglobin exchange
    • Jaszewski A.R., Fann Y.C., Chen Y.-R., Sato K., Corbett J., and Mason R.P. EPR spectroscopy studies on the structural transition of nitrosyl hemoglobin in the arterial-venous cycle of DEANO-treated rats as it relates to the proposed nitrosyl hemoglobin/nitrosothiol hemoglobin exchange. Free Radic. Biol. Med. 35 (2003) 444-451
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 444-451
    • Jaszewski, A.R.1    Fann, Y.C.2    Chen, Y.-R.3    Sato, K.4    Corbett, J.5    Mason, R.P.6
  • 19
    • 0028223401 scopus 로고
    • ESR spectral transition by arteriovenous cycle in nitric oxide hemoglobin of cytokine-treated rats
    • Kosaka H., Sawai Y., Sakaguchi H., et al. ESR spectral transition by arteriovenous cycle in nitric oxide hemoglobin of cytokine-treated rats. Am. J. Physiol. 266 (1994) C1400-C1405
    • (1994) Am. J. Physiol. , vol.266
    • Kosaka, H.1    Sawai, Y.2    Sakaguchi, H.3
  • 20
    • 0027447237 scopus 로고
    • Measurement of nitric oxide in biological models
    • Archer S. Measurement of nitric oxide in biological models. FASEB J. 7 (1993) 349-360
    • (1993) FASEB J. , vol.7 , pp. 349-360
    • Archer, S.1
  • 21
    • 22144457461 scopus 로고    scopus 로고
    • Methods of quantitative analysis of the nitric oxide metabolites nitrite and nitrate in human biological fluids
    • Tsikas D. Methods of quantitative analysis of the nitric oxide metabolites nitrite and nitrate in human biological fluids. Free Radic. Res. 39 (2005) 797-815
    • (2005) Free Radic. Res. , vol.39 , pp. 797-815
    • Tsikas, D.1
  • 22
    • 0025834312 scopus 로고
    • Nitric oxide hemoglobin in mice and rats in endotoxic shock
    • Wang Q., Jacobs J., DeLeo J., et al. Nitric oxide hemoglobin in mice and rats in endotoxic shock. Life Sci. 49 (1991) PL55-PL60
    • (1991) Life Sci. , vol.49
    • Wang, Q.1    Jacobs, J.2    DeLeo, J.3
  • 23
    • 27744606565 scopus 로고    scopus 로고
    • ESR techniques for the detection of nitric oxide in vivo and in tissues
    • Dikalov S., and Fink B. ESR techniques for the detection of nitric oxide in vivo and in tissues. Methods Enzymol. 396 (2005) 597-610
    • (2005) Methods Enzymol. , vol.396 , pp. 597-610
    • Dikalov, S.1    Fink, B.2
  • 24
    • 0027989397 scopus 로고
    • Nitric oxide production during endotoxic shock in carbon tetrachloride-treated rats
    • Chamulitrat W., Jordan S.J., and Mason R.P. Nitric oxide production during endotoxic shock in carbon tetrachloride-treated rats. Mol. Pharmacol. 46 (1994) 391-397
    • (1994) Mol. Pharmacol. , vol.46 , pp. 391-397
    • Chamulitrat, W.1    Jordan, S.J.2    Mason, R.P.3
  • 25
    • 0031468478 scopus 로고    scopus 로고
    • In vivo production of nitric oxide in rats after administration of hydroxyurea
    • Jiang J., Jordan S.J., Barr D.P., Gunther M.R., Maeda H., and Mason R.P. In vivo production of nitric oxide in rats after administration of hydroxyurea. Mol. Pharmacol. 52 (1997) 1081-1086
    • (1997) Mol. Pharmacol. , vol.52 , pp. 1081-1086
    • Jiang, J.1    Jordan, S.J.2    Barr, D.P.3    Gunther, M.R.4    Maeda, H.5    Mason, R.P.6
  • 26
    • 0032977037 scopus 로고    scopus 로고
    • Detection of nitrosyl hemoglobin in venous blood in the treatment of sickle cell anemia with hydroxyurea
    • Glover R.E., Ivey E.D., Orringer E.P., Maeda H., and Mason R.P. Detection of nitrosyl hemoglobin in venous blood in the treatment of sickle cell anemia with hydroxyurea. Mol. Pharmacol. 55 (1999) 1006-1010
    • (1999) Mol. Pharmacol. , vol.55 , pp. 1006-1010
    • Glover, R.E.1    Ivey, E.D.2    Orringer, E.P.3    Maeda, H.4    Mason, R.P.5
  • 28
    • 28844476036 scopus 로고    scopus 로고
    • Electron paramagnetic resonance analysis of nitrosylhemoglobin in humans during NO inhalation
    • Piknova B., Gladwin M.T., Schechter A.N., and Hogg N. Electron paramagnetic resonance analysis of nitrosylhemoglobin in humans during NO inhalation. J. Biol. Chem. 208 (2005) 40583-40588
    • (2005) J. Biol. Chem. , vol.208 , pp. 40583-40588
    • Piknova, B.1    Gladwin, M.T.2    Schechter, A.N.3    Hogg, N.4
  • 29
    • 0034730133 scopus 로고    scopus 로고
    • Relative role of heme nitrosylation and β-cysteine 93 nitrosation in the transport and metabolism of nitric oxide by hemoglobin in the human circulation
    • Gladwin M.T., Ognibene F.P., Pannell L.K., Nichols J.S., Pease-Feye M.E., Shelhamer J.H., and Schechter A.N. Relative role of heme nitrosylation and β-cysteine 93 nitrosation in the transport and metabolism of nitric oxide by hemoglobin in the human circulation. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 9943-9948
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 9943-9948
    • Gladwin, M.T.1    Ognibene, F.P.2    Pannell, L.K.3    Nichols, J.S.4    Pease-Feye, M.E.5    Shelhamer, J.H.6    Schechter, A.N.7
  • 30
    • 0035134037 scopus 로고    scopus 로고
    • A good practice guide to the administration of substances and removal of blood, including routes and volumes
    • Diehl K.-H., Hull R., Morton D., et al. A good practice guide to the administration of substances and removal of blood, including routes and volumes. J. Appl. Toxicol. 21 (2001) 15-23
    • (2001) J. Appl. Toxicol. , vol.21 , pp. 15-23
    • Diehl, K.-H.1    Hull, R.2    Morton, D.3
  • 31
  • 32
    • 0038299390 scopus 로고    scopus 로고
    • Evaluation of systemic blood NO dynamics by EPR spectroscopy: HbNO as an endogenous index of NO
    • Kirima K., Tsuchiya K., Sei H., et al. Evaluation of systemic blood NO dynamics by EPR spectroscopy: HbNO as an endogenous index of NO. Am. J. Physiol.: Heart Circ. Physiol. 285 (2003) H589-H596
    • (2003) Am. J. Physiol.: Heart Circ. Physiol. , vol.285
    • Kirima, K.1    Tsuchiya, K.2    Sei, H.3
  • 33
    • 0033578741 scopus 로고    scopus 로고
    • Nitrosothiol formation catalyzed by ceruloplasmin: implication for cytoprotective mechanism in vivo
    • Inoue K., Akaike T., Miyamoto Y., et al. Nitrosothiol formation catalyzed by ceruloplasmin: implication for cytoprotective mechanism in vivo. J. Biol. Chem. 274 (1999) 27069-27075
    • (1999) J. Biol. Chem. , vol.274 , pp. 27069-27075
    • Inoue, K.1    Akaike, T.2    Miyamoto, Y.3
  • 34
    • 0032493731 scopus 로고    scopus 로고
    • Electron paramagnetic resonance and oxygen binding studies of α-nitrosyl hemoglobin: a novel oxygen carrier having NO-assisted allosteric functions
    • Yonetani T., Tsuneshige A., Zhou Y., and Chen X. Electron paramagnetic resonance and oxygen binding studies of α-nitrosyl hemoglobin: a novel oxygen carrier having NO-assisted allosteric functions. J. Biol. Chem. 273 (1998) 20323-20333
    • (1998) J. Biol. Chem. , vol.273 , pp. 20323-20333
    • Yonetani, T.1    Tsuneshige, A.2    Zhou, Y.3    Chen, X.4
  • 36
    • 33748743427 scopus 로고    scopus 로고
    • Measurement of nitric oxide levels in the red cell validation of tri-iodide-based chemiluminescence with acid-sulfanilamide pretreatment
    • Wang X., Bryan N.S., MacArthur P.H., Rodriguez J., Gladwin M.T., and Feelisch M. Measurement of nitric oxide levels in the red cell validation of tri-iodide-based chemiluminescence with acid-sulfanilamide pretreatment. J. Biol. Chem. 281 (2006) 26994-27002
    • (2006) J. Biol. Chem. , vol.281 , pp. 26994-27002
    • Wang, X.1    Bryan, N.S.2    MacArthur, P.H.3    Rodriguez, J.4    Gladwin, M.T.5    Feelisch, M.6
  • 37
    • 0037470250 scopus 로고    scopus 로고
    • Reactions of deoxy-, oxy-, and methemoglobin with nitrogen monoxide: mechanistic studies of the S-nitrosothiol formation under different mixing conditions
    • Herold S., and Rock G. Reactions of deoxy-, oxy-, and methemoglobin with nitrogen monoxide: mechanistic studies of the S-nitrosothiol formation under different mixing conditions. J. Biol. Chem. 278 (2003) 6623-6634
    • (2003) J. Biol. Chem. , vol.278 , pp. 6623-6634
    • Herold, S.1    Rock, G.2
  • 38
    • 28244459618 scopus 로고    scopus 로고
    • Nitric oxide scavenging by red blood cells as a function of hematocrit and oxygenation
    • Azarov I., Huang K.T., Basu S., Gladwin M.T., Hogg N., and Kim-Shapiro D.B. Nitric oxide scavenging by red blood cells as a function of hematocrit and oxygenation. J. Biol. Chem. 280 (2005) 39024-39032
    • (2005) J. Biol. Chem. , vol.280 , pp. 39024-39032
    • Azarov, I.1    Huang, K.T.2    Basu, S.3    Gladwin, M.T.4    Hogg, N.5    Kim-Shapiro, D.B.6
  • 39
  • 40
    • 0003650610 scopus 로고
    • Quantitative EPR: some of the most difficult problems
    • Nagy V. Quantitative EPR: some of the most difficult problems. Appl. Magn Reson. 6 (1994) 259-285
    • (1994) Appl. Magn Reson. , vol.6 , pp. 259-285
    • Nagy, V.1
  • 41
    • 33644818493 scopus 로고    scopus 로고
    • A dozen useful tips on how to minimise the influence of sources of error in quantitative electron paramagnetic resonance (EPR) spectroscopy-a review
    • Mazur M. A dozen useful tips on how to minimise the influence of sources of error in quantitative electron paramagnetic resonance (EPR) spectroscopy-a review. Anal. Chem. Acta 561 (2006) 1-15
    • (2006) Anal. Chem. Acta , vol.561 , pp. 1-15
    • Mazur, M.1
  • 42
    • 0030549258 scopus 로고    scopus 로고
    • Quantitative EPR-sensitivity to experimental conditions and optimal setting of recording parameters
    • Czoch R. Quantitative EPR-sensitivity to experimental conditions and optimal setting of recording parameters. Appl. Magn. Reson. 10 (1996) 293-317
    • (1996) Appl. Magn. Reson. , vol.10 , pp. 293-317
    • Czoch, R.1


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