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Volumn 104, Issue 7, 1999, Pages 937-945

Inhaled nitric oxide augments nitric oxide transport on sickle cell hemoglobin without affecting oxygen affinity

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; HEMOGLOBIN BETA CHAIN; HEMOGLOBIN S; NITRIC OXIDE; OXYGEN;

EID: 0032696892     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI7637     Document Type: Article
Times cited : (100)

References (26)
  • 1
    • 0030853711 scopus 로고    scopus 로고
    • Pathogenesis and treatment of sickle cell disease
    • Bunn, H.F. 1997. Pathogenesis and treatment of sickle cell disease. N. Engl. J. Med. 337:762-769.
    • (1997) N. Engl. J. Med. , vol.337 , pp. 762-769
    • Bunn, H.F.1
  • 2
    • 0033118835 scopus 로고    scopus 로고
    • Management of sickle cell disease
    • Steinberg, M.H. 1999. Management of sickle cell disease. N. Engl. J. Med. 340:1021-1030.
    • (1999) N. Engl. J. Med. , vol.340 , pp. 1021-1030
    • Steinberg, M.H.1
  • 3
    • 0027515050 scopus 로고
    • Endogenous nitrogen oxides and bronchodilator S-nitrosothiols in human airways
    • Gaston, B., et al. 1993. Endogenous nitrogen oxides and bronchodilator S-nitrosothiols in human airways. Proc. Natl. Acad. Sci. USA. 90:10957-10961.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10957-10961
    • Gaston, B.1
  • 4
    • 0026693724 scopus 로고
    • Nitric oxide circulates in mammalian plasma primarily as an S-nitroso adduct of serum albumin
    • Stamler, J.S., et al. 1992. Nitric oxide circulates in mammalian plasma primarily as an S-nitroso adduct of serum albumin. Proc. Natl. Acad. Sci. USA. 89:7674-7677.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7674-7677
    • Stamler, J.S.1
  • 5
    • 0028987969 scopus 로고
    • +, NO, and NO- donation by S-nitrosothiols: Implications for regulation of physiological functions by S-nitrosylation and acceleration of disulfide formation
    • +, NO, and NO- donation by S-nitrosothiols: implications for regulation of physiological functions by S-nitrosylation and acceleration of disulfide formation. Arch. Biochem. Biophys. 318:279-285.
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 279-285
    • Arnelle, D.R.1    Stamler, J.S.2
  • 6
    • 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. 1996. S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control. Nature. 380:221-226.
    • (1996) Nature , vol.380 , pp. 221-226
    • Jia, L.1    Bonaventura, C.2    Bonaventura, J.3    Stamler, J.S.4
  • 7
    • 0032495529 scopus 로고    scopus 로고
    • Reactions between nitric oxide and haemoglobin under physiological conditions
    • Gow, A.J., and Stamler, J.S. 1998. Reactions between nitric oxide and haemoglobin under physiological conditions. Nature. 391:169-173.
    • (1998) Nature , vol.391 , pp. 169-173
    • Gow, A.J.1    Stamler, J.S.2
  • 8
    • 0030791742 scopus 로고    scopus 로고
    • Blood flow regulation by S-nitrosohemoglobin in the physiological oxygen gradient
    • Stamler, J.S., et al. 1997. Blood flow regulation by S-nitrosohemoglobin in the physiological oxygen gradient. Science. 276:2034-2037.
    • (1997) Science , vol.276 , pp. 2034-2037
    • Stamler, J.S.1
  • 9
    • 0030982523 scopus 로고    scopus 로고
    • Low concentrations of nitric oxide increase oxygen affinity of sickle erythrocytes in vitro and in vivo
    • Head, C.A., et al. 1997. Low concentrations of nitric oxide increase oxygen affinity of sickle erythrocytes in vitro and in vivo. J. Clin. Invest. 100:1193-1198.
    • (1997) J. Clin. Invest. , vol.100 , pp. 1193-1198
    • Head, C.A.1
  • 10
    • 0028817948 scopus 로고
    • Performance characteristics of Hemox-Analyzer for assessment of the hemoglobin dissociation curve
    • Guarnone, R., Centenara, E., and Barosi, G. 1995, Performance characteristics of Hemox-Analyzer for assessment of the hemoglobin dissociation curve. Haematologica. 80:426-430.
    • (1995) Haematologica , vol.80 , pp. 426-430
    • Guarnone, R.1    Centenara, E.2    Barosi, G.3
  • 11
    • 0020448709 scopus 로고
    • Analysis of nitrate, nitrite, and [15N]nitrate in biological fluids
    • Green, L.C., et al. 1982. Analysis of nitrate, nitrite, and [15N]nitrate in biological fluids. Anal. Biochem. 126:131-138.
    • (1982) Anal. Biochem. , vol.126 , pp. 131-138
    • Green, L.C.1
  • 12
    • 0032080124 scopus 로고    scopus 로고
    • Development of chemiluminescence-based methods for specific quantitation of nitrosylated thiols
    • Samouilov, A., and Zweier, J.L. 1998. Development of chemiluminescence-based methods for specific quantitation of nitrosylated thiols. Anal. Biochem. 258:322-330.
    • (1998) Anal. Biochem. , vol.258 , pp. 322-330
    • Samouilov, A.1    Zweier, J.L.2
  • 13
    • 0031740405 scopus 로고    scopus 로고
    • Concerted nitric oxide/oxygen delivery by hemoglobin
    • McMahon, T.J., and Stamler, J.S. 1999. Concerted nitric oxide/oxygen delivery by hemoglobin. Methods Enzymol. 301:99-114.
    • (1999) Methods Enzymol. , vol.301 , pp. 99-114
    • McMahon, T.J.1    Stamler, J.S.2
  • 14
    • 0017684975 scopus 로고
    • Oxidation of human haemoglobin by copper. Mechanism and suggested role of the thiol group of residue beta-93
    • Winterbourn, C.C., and Carrell, R.W. 1977. Oxidation of human haemoglobin by copper. Mechanism and suggested role of the thiol group of residue beta-93. Biochem. J. 165:141-148.
    • (1977) Biochem. J. , vol.165 , pp. 141-148
    • Winterbourn, C.C.1    Carrell, R.W.2
  • 15
    • 0033016469 scopus 로고    scopus 로고
    • Biochemical characterization of human S-nitrosohemoglobin. Effects on oxygen binding and transnitrosation
    • Patel, R.P., et al. 1999, Biochemical characterization of human S-nitrosohemoglobin. Effects on oxygen binding and transnitrosation, J. Biol. Chem. 274:15487-15492.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15487-15492
    • Patel, R.P.1
  • 17
    • 0022828370 scopus 로고
    • Covalent binding of glutathione to hemoglobin. I. Inhibition of hemoglobin S polymerization
    • Garel, M.C., et al. 1986. Covalent binding of glutathione to hemoglobin. I. Inhibition of hemoglobin S polymerization. J. Biol. Chem. 261:14704-14709.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14704-14709
    • Garel, M.C.1
  • 18
    • 0032570313 scopus 로고    scopus 로고
    • Cell-free and erythrocytic S-nitrosohemoglobin inhibits human platelet aggregation
    • Pawloski, J.R., Swaminathan, R.V., and Stamler, J.S. 1998. Cell-free and erythrocytic S-nitrosohemoglobin inhibits human platelet aggregation. Circulation. 97:263-267
    • (1998) Circulation , vol.97 , pp. 263-267
    • Pawloski, J.R.1    Swaminathan, R.V.2    Stamler, J.S.3
  • 19
    • 0032102218 scopus 로고    scopus 로고
    • Inhaled NO as a viable antiadhesive therapy for ischemia/reperfusion injury of distal microvascular beds
    • Fox-Robichaud, A., et al. 1998. Inhaled NO as a viable antiadhesive therapy for ischemia/reperfusion injury of distal microvascular beds. J. Clin. Invest. 101:2497-2505.
    • (1998) J. Clin. Invest. , vol.101 , pp. 2497-2505
    • Fox-Robichaud, A.1
  • 20
    • 0032936879 scopus 로고    scopus 로고
    • The acute chest syndrome in sickle cell disease. Possible role of nitric oxide in its pathophysiology and treatment
    • Gladwin, M.T., Schechter, A.N., Shelhamer, J.H., and Ognibene, F.P. 1999. The acute chest syndrome in sickle cell disease. Possible role of nitric oxide in its pathophysiology and treatment. Am. J. Respir. Crit. Care Med. 159:1368-1376.
    • (1999) Am. J. Respir. Crit. Care Med. , vol.159 , pp. 1368-1376
    • Gladwin, M.T.1    Schechter, A.N.2    Shelhamer, J.H.3    Ognibene, F.P.4
  • 21
    • 0030669447 scopus 로고    scopus 로고
    • Inhaled nitric oxide in sickle cell disease with acute chest syndrome
    • Atz, A.M., and Wessel, D.L. 1997. Inhaled nitric oxide in sickle cell disease with acute chest syndrome. Anesthesiology. 87:988-990.
    • (1997) Anesthesiology , vol.87 , pp. 988-990
    • Atz, A.M.1    Wessel, D.L.2
  • 22
    • 0030912619 scopus 로고    scopus 로고
    • Mechanisms of stroke in sickle cell disease: Sickle erythrocytes decrease cerebral blood flow in rats after nitric oxide synthase inhibition
    • French, J.A., II, et al. 1997. Mechanisms of stroke in sickle cell disease: sickle erythrocytes decrease cerebral blood flow in rats after nitric oxide synthase inhibition. Blood. 89:4591-4599.
    • (1997) Blood , vol.89 , pp. 4591-4599
    • French J.A. II1
  • 23
    • 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. 1997. S-nitrosohemoglobin in the fetal circulation may represent a cycle for blood pressure regulation. Biochem. Biophys. Res. Commun. 239:875-877.
    • (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
  • 24
    • 33750858375 scopus 로고    scopus 로고
    • Nitrosyl hemoglobin in blood of normoxic and hypoxic sheep during nitric oxide inhalation
    • Takahashi, Y., et al. 1998. Nitrosyl hemoglobin in blood of normoxic and hypoxic sheep during nitric oxide inhalation. Am. J. Physiol. 274:H349-H357.
    • (1998) Am. J. Physiol. , vol.274
    • Takahashi, Y.1
  • 25
    • 0025124595 scopus 로고
    • Microcirculatory adaptations in sickle cell anemia: Reactive hyperemia response
    • Rodgers, G.P., et al. 1990. Microcirculatory adaptations in sickle cell anemia: reactive hyperemia response. Am. J. Physiol. 258:H113-H120.
    • (1990) Am. J. Physiol. , vol.258
    • Rodgers, G.P.1
  • 26
    • 0020962156 scopus 로고
    • Cardiorespiratory adjustments in chronic sickle cell anemia
    • Lonsdorfer, J., et al. 1983. Cardiorespiratory adjustments in chronic sickle cell anemia. Bull. Eur. Physiopathol. Respir. 19:339-344.
    • (1983) Bull. Eur. Physiopathol. Respir. , vol.19 , pp. 339-344
    • Lonsdorfer, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.