메뉴 건너뛰기




Volumn 298, Issue 2, 2010, Pages

Antisickling property of fetal hemoglobin enhances nitric oxide bioavailability and ameliorates organ oxidative stress in transgenic-knockout sickle mice

Author keywords

Hemolysis; Inflammation; Multiple organ damage; Reperfusion; Sickle cell disease

Indexed keywords

ALPHA GLOBIN; ANTISICKLING AGENT; BETA GLOBIN; CATALASE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; HEMOGLOBIN F; LIPID; NITRIC OXIDE; SUPEROXIDE DISMUTASE;

EID: 75449108995     PISSN: 03636119     EISSN: 15221490     Source Type: Journal    
DOI: 10.1152/ajpregu.00611.2009     Document Type: Article
Times cited : (41)

References (57)
  • 1
    • 0021318441 scopus 로고
    • Catalase in vitro
    • Aebi H. Catalase in vitro. Methods Enzymol 105: 121-126, 1984.
    • (1984) Methods Enzymol , vol.105 , pp. 121-126
    • Aebi, H.1
  • 2
    • 1542283780 scopus 로고    scopus 로고
    • Regulation of endothelial nitric oxide synthase by tetrahydrobiopterin in vascular disease
    • Alp NJ, Channon KM. Regulation of endothelial nitric oxide synthase by tetrahydrobiopterin in vascular disease. Arterioscler Thromb Vasc Biol 24: 413-420, 2004.
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , pp. 413-420
    • Alp, N.J.1    Channon, K.M.2
  • 3
    • 2042501244 scopus 로고    scopus 로고
    • Glutathione and glutathione delivery compounds
    • Anderson ME. Glutathione and glutathione delivery compounds. Adv Pharmacol 38: 65-78, 1997.
    • (1997) Adv Pharmacol , vol.38 , pp. 65-78
    • Anderson, M.E.1
  • 5
    • 0345687458 scopus 로고    scopus 로고
    • Mechanisms of action of DNA intercalating acridine-based drugs: How important are contributions from electron transfer and oxidative stress?
    • Baguley BC, Wakelin LP, Jacintho JD, Kovacic P. Mechanisms of action of DNA intercalating acridine-based drugs: how important are contributions from electron transfer and oxidative stress? Curr Med Chem 10: 2643-2649, 2003.
    • (2003) Curr Med Chem , vol.10 , pp. 2643-2649
    • Baguley, B.C.1    Wakelin, L.P.2    Jacintho, J.D.3    Kovacic, P.4
  • 6
    • 0022853319 scopus 로고
    • The involvement of iron in lipid peroxidation. Importance of ferric to ferrous ratios in initiation
    • Braughler JM, Duncan LA, Chase RL. The involvement of iron in lipid peroxidation. Importance of ferric to ferrous ratios in initiation. J Biol Chem 261: 10282-10289, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 10282-10289
    • Braughler, J.M.1    Duncan, L.A.2    Chase, R.L.3
  • 8
    • 0018696285 scopus 로고
    • Abnormal vitamin E and glutathione peroxidase levels in sickle cell anemia: Evidence for increased susceptibility to lipid peroxidation in vivo
    • Chiu D, Lubin B. Abnormal vitamin E and glutathione peroxidase levels in sickle cell anemia: evidence for increased susceptibility to lipid peroxidation in vivo. J Lab Clin Med 94: 542-548, 1979.
    • (1979) J Lab Clin Med , vol.94 , pp. 542-548
    • Chiu, D.1    Lubin, B.2
  • 9
    • 38949192565 scopus 로고    scopus 로고
    • Hydroxyurea nitrosylates and activates soluble guanylyl cyclase in human erythroid cells
    • Cokic VP, Andric SA, Stojilkovic SS, Noguchi CT, Schechter AN. Hydroxyurea nitrosylates and activates soluble guanylyl cyclase in human erythroid cells. Blood 111: 1117-1123, 2008.
    • (2008) Blood , vol.111 , pp. 1117-1123
    • Cokic, V.P.1    Andric, S.A.2    Stojilkovic, S.S.3    Noguchi, C.T.4    Schechter, A.N.5
  • 11
    • 41849144894 scopus 로고    scopus 로고
    • Crabtree MJ, Smith CL, Lam G, Goligorsky MS, Gross SS. Ratio of 5,6,7,8-tetrahydrobiopterin to 7,8-dihydrobiopterin in endothelial cells determines glucose-elicited changes in NO vs. superoxide production by eNOS. Am J Physiol Heart Circ Physiol 294: H1530-H1540, 2008.
    • Crabtree MJ, Smith CL, Lam G, Goligorsky MS, Gross SS. Ratio of 5,6,7,8-tetrahydrobiopterin to 7,8-dihydrobiopterin in endothelial cells determines glucose-elicited changes in NO vs. superoxide production by eNOS. Am J Physiol Heart Circ Physiol 294: H1530-H1540, 2008.
  • 12
    • 0018854950 scopus 로고
    • Superoxide dismutase, glutathione peroxidase, catalase and lipid peroxidation of normal and sickled erythrocytes
    • Das SK, Nair RC. Superoxide dismutase, glutathione peroxidase, catalase and lipid peroxidation of normal and sickled erythrocytes. Br J Haematol 44: 87-92, 1980.
    • (1980) Br J Haematol , vol.44 , pp. 87-92
    • Das, S.K.1    Nair, R.C.2
  • 13
    • 33751530487 scopus 로고    scopus 로고
    • Protective effect of arginine on oxidative stress in transgenic sickle mouse models
    • Dasgupta T, Hebbel RP, Kaul DK. Protective effect of arginine on oxidative stress in transgenic sickle mouse models. Free Radic Biol Med 41: 1771-1780, 2006.
    • (2006) Free Radic Biol Med , vol.41 , pp. 1771-1780
    • Dasgupta, T.1    Hebbel, R.P.2    Kaul, D.K.3
  • 15
    • 0020422995 scopus 로고
    • The effect of deoxygenation on red cell density: Significance for the pathophysiology of sickle cell anemia
    • Fabry ME, Nagel RL. The effect of deoxygenation on red cell density: significance for the pathophysiology of sickle cell anemia. Blood 60: 1370-1377, 1982.
    • (1982) Blood , vol.60 , pp. 1370-1377
    • Fabry, M.E.1    Nagel, R.L.2
  • 19
    • 17444368668 scopus 로고    scopus 로고
    • Lipid peroxidation measurement by thiobarbituric acid assay in rat cerebellar slices
    • Garcia YJ, Rodriguez-Malaver AJ, Penaloza N. Lipid peroxidation measurement by thiobarbituric acid assay in rat cerebellar slices. J Neurosci Methods 144: 127-135, 2005.
    • (2005) J Neurosci Methods , vol.144 , pp. 127-135
    • Garcia, Y.J.1    Rodriguez-Malaver, A.J.2    Penaloza, N.3
  • 21
    • 0034677947 scopus 로고    scopus 로고
    • NAD(P)H oxidase: Role in cardiovascular biology and disease
    • Griendling KK, Sorescu D, Ushio-Fukai M. NAD(P)H oxidase: role in cardiovascular biology and disease. Circ Res 86: 494-501, 2000.
    • (2000) Circ Res , vol.86 , pp. 494-501
    • Griendling, K.K.1    Sorescu, D.2    Ushio-Fukai, M.3
  • 22
    • 3242792093 scopus 로고    scopus 로고
    • The endothelial biology of sickle cell disease: Inflammation and a chronic vasculopathy
    • Hebbel RP, Osarogiagbon R, Kaul D. The endothelial biology of sickle cell disease: inflammation and a chronic vasculopathy. Microcirculation 11: 129-151, 2004.
    • (2004) Microcirculation , vol.11 , pp. 129-151
    • Hebbel, R.P.1    Osarogiagbon, R.2    Kaul, D.3
  • 25
    • 0035800823 scopus 로고    scopus 로고
    • Reaction of superoxide and nitric oxide with peroxynitrite. Implications for peroxynitrite-mediated oxidation reactions in vivo
    • Jourd'heuil D, Jourd'heuil FL, Kutchukian PS, Musah RA, Wink DA, Grisham MB. Reaction of superoxide and nitric oxide with peroxynitrite. Implications for peroxynitrite-mediated oxidation reactions in vivo. J Biol Chem 276: 28799-28805, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 28799-28805
    • Jourd'heuil, D.1    Jourd'heuil, F.L.2    Kutchukian, P.S.3    Musah, R.A.4    Wink, D.A.5    Grisham, M.B.6
  • 26
    • 0033624253 scopus 로고    scopus 로고
    • Hypoxia/reoxygenation causes inflammatory response in transgenic sickle mice but not in normal mice [see comments]
    • Kaul DK, Hebbel RP. Hypoxia/reoxygenation causes inflammatory response in transgenic sickle mice but not in normal mice [see comments]. J Clin Invest 106: 411-420, 2000.
    • (2000) J Clin Invest , vol.106 , pp. 411-420
    • Kaul, D.K.1    Hebbel, R.P.2
  • 27
    • 9644260566 scopus 로고    scopus 로고
    • Effect of fetal hemoglobin on microvascular regulation in sickle transgenic-knockout mice
    • Kaul DK, Liu XD, Chang HY, Nagel RL, Fabry ME. Effect of fetal hemoglobin on microvascular regulation in sickle transgenic-knockout mice. J Clin Invest 114: 1136-1145, 2004.
    • (2004) J Clin Invest , vol.114 , pp. 1136-1145
    • Kaul, D.K.1    Liu, X.D.2    Chang, H.Y.3    Nagel, R.L.4    Fabry, M.E.5
  • 28
    • 0025865231 scopus 로고
    • Rate of deoxygenation and rheologic behavior of blood in sickle cell anemia
    • Kaul DK, Xue H. Rate of deoxygenation and rheologic behavior of blood in sickle cell anemia. Blood 77: 1353-1361, 1991.
    • (1991) Blood , vol.77 , pp. 1353-1361
    • Kaul, D.K.1    Xue, H.2
  • 29
    • 49849101277 scopus 로고    scopus 로고
    • Arginine therapy of transgenic-knockout sickle mice improves microvascular function by reducing non-nitric oxide vasodilators, hemolysis, and oxidative stress
    • Kaul DK, Zhang X, Dasgupta T, Fabry ME. Arginine therapy of transgenic-knockout sickle mice improves microvascular function by reducing non-nitric oxide vasodilators, hemolysis, and oxidative stress. Am J Physiol Heart Circ Physiol 295: H39-H47, 2008.
    • (2008) Am J Physiol Heart Circ Physiol , vol.295
    • Kaul, D.K.1    Zhang, X.2    Dasgupta, T.3    Fabry, M.E.4
  • 30
    • 0030605982 scopus 로고    scopus 로고
    • Nitrotyrosine attenuates the hemodynamic effects of adrenoceptor agonists in vivo: Relevance to the pathophysiology of peroxynitrite
    • Kooy NW, Lewis SJ. Nitrotyrosine attenuates the hemodynamic effects of adrenoceptor agonists in vivo: relevance to the pathophysiology of peroxynitrite. Eur J Pharmacol 310: 155-161, 1996.
    • (1996) Eur J Pharmacol , vol.310 , pp. 155-161
    • Kooy, N.W.1    Lewis, S.J.2
  • 31
    • 0030583695 scopus 로고    scopus 로고
    • Kooy NW, Lewis SJ. The peroxynitrite product 3-nitro-L-tyrosine attenuates the hemodynamic responses to angiotensin II in vivo. Eur J Pharmacol 315: 165-170, 1996. 32. Krajewski ML, Hsu LL, Gladwin MT. The proverbial chicken or the egg? Dissection of the role of cell-free hemoglobin versus reactive oxygen species in sickle cell pathophysiology. Am J Physiol Heart Circ Physiol 295: H4-H7, 2008.
    • Kooy NW, Lewis SJ. The peroxynitrite product 3-nitro-L-tyrosine attenuates the hemodynamic responses to angiotensin II in vivo. Eur J Pharmacol 315: 165-170, 1996. 32. Krajewski ML, Hsu LL, Gladwin MT. The proverbial chicken or the egg? Dissection of the role of cell-free hemoglobin versus reactive oxygen species in sickle cell pathophysiology. Am J Physiol Heart Circ Physiol 295: H4-H7, 2008.
  • 32
    • 5444273795 scopus 로고    scopus 로고
    • The role of phosphatidylserine in recognition and removal of erythrocytes
    • Kuypers FA, de Jong K. The role of phosphatidylserine in recognition and removal of erythrocytes. Cell Mol Biol (Noisy -le-grand) 50: 147-158, 2004.
    • (2004) Cell Mol Biol (Noisy -le-grand) , vol.50 , pp. 147-158
    • Kuypers, F.A.1    de Jong, K.2
  • 33
    • 0036123235 scopus 로고    scopus 로고
    • In vivo antioxidant role of glutathione peroxidase: Evidence from knockout mice
    • Lei XG. In vivo antioxidant role of glutathione peroxidase: evidence from knockout mice. Methods Enzymol 347: 213-225, 2002.
    • (2002) Methods Enzymol , vol.347 , pp. 213-225
    • Lei, X.G.1
  • 34
    • 0016272750 scopus 로고
    • Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase
    • Marklund S, Marklund G. Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur J Biochem 47: 469-474, 1974.
    • (1974) Eur J Biochem , vol.47 , pp. 469-474
    • Marklund, S.1    Marklund, G.2
  • 35
    • 0028263767 scopus 로고
    • Glutathione-ascorbic acid antioxidant system in animals
    • Meister A. Glutathione-ascorbic acid antioxidant system in animals. J Biol Chem 269: 9397-9400, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 9397-9400
    • Meister, A.1
  • 36
    • 0018327389 scopus 로고
    • Levels of glutathione, glutathione reductase and glutathione S-transferase activities in rat lung and liver
    • Moron MS, DePierre JW, Mannervik B. Levels of glutathione, glutathione reductase and glutathione S-transferase activities in rat lung and liver. Biochim Biophys Acta 582: 67-78, 1979.
    • (1979) Biochim Biophys Acta , vol.582 , pp. 67-78
    • Moron, M.S.1    DePierre, J.W.2    Mannervik, B.3
  • 38
    • 0035824170 scopus 로고    scopus 로고
    • The challenge of painful crisis in sickle cell disease
    • Nagel RL. The challenge of painful crisis in sickle cell disease. JAMA 286: 2152-2153, 2001.
    • (2001) JAMA , vol.286 , pp. 2152-2153
    • Nagel, R.L.1
  • 40
    • 0030700237 scopus 로고    scopus 로고
    • Nitric oxide inhibition of lipid peroxidation: Kinetics of reaction with lipid peroxyl radicals and comparison with alpha-tocopherol
    • O'Donnell VB, Chumley PH, Hogg N, Bloodsworth A, Darley-Usmar VM, Freeman BA. Nitric oxide inhibition of lipid peroxidation: kinetics of reaction with lipid peroxyl radicals and comparison with alpha-tocopherol. Biochemistry 36: 15216-15223, 1997.
    • (1997) Biochemistry , vol.36 , pp. 15216-15223
    • O'Donnell, V.B.1    Chumley, P.H.2    Hogg, N.3    Bloodsworth, A.4    Darley-Usmar, V.M.5    Freeman, B.A.6
  • 41
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction
    • Ohkawa H, Ohishi N, Yagi K. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal Biochem 95: 351-358, 1979.
    • (1979) Anal Biochem , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 42
    • 0014108436 scopus 로고
    • Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase
    • Paglia DE, Valentine WN. Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J Lab Clin Med 70: 158-169, 1967.
    • (1967) J Lab Clin Med , vol.70 , pp. 158-169
    • Paglia, D.E.1    Valentine, W.N.2
  • 43
    • 1842408336 scopus 로고    scopus 로고
    • Transgenic knockout mice with exclusively human sickle hemoglobin and sickle cell disease [see comments]
    • Paszty C, Brion CM, Manci E, Witkowska HE, Stevens ME, Mohandas N, Rubin EM. Transgenic knockout mice with exclusively human sickle hemoglobin and sickle cell disease [see comments]. Science 278: 876-878, 1997.
    • (1997) Science , vol.278 , pp. 876-878
    • Paszty, C.1    Brion, C.M.2    Manci, E.3    Witkowska, H.E.4    Stevens, M.E.5    Mohandas, N.6    Rubin, E.M.7
  • 45
    • 0037443467 scopus 로고    scopus 로고
    • The degree of phenotypic correction of murine beta-thalassemia intermedia following lentiviral-mediated transfer of a human gamma-globin gene is influenced by chromosomal position effects and vector copy number
    • Persons DA, Hargrove PW, Allay ER, Hanawa H, Nienhuis AW. The degree of phenotypic correction of murine beta-thalassemia intermedia following lentiviral-mediated transfer of a human gamma-globin gene is influenced by chromosomal position effects and vector copy number. Blood 101: 2175-2183, 2003.
    • (2003) Blood , vol.101 , pp. 2175-2183
    • Persons, D.A.1    Hargrove, P.W.2    Allay, E.R.3    Hanawa, H.4    Nienhuis, A.W.5
  • 46
    • 0025874048 scopus 로고
    • Peroxynitrite-induced membrane lipid peroxidation: The cytotoxic potential of superoxide and nitric oxide
    • Radi R, Beckman JS, Bush KM, Freeman BA. Peroxynitrite-induced membrane lipid peroxidation: the cytotoxic potential of superoxide and nitric oxide. Arch Biochem Biophys 288: 481-487, 1991.
    • (1991) Arch Biochem Biophys , vol.288 , pp. 481-487
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 47
    • 0031959197 scopus 로고    scopus 로고
    • New considerations in the treatment of sickle cell disease
    • Reed W, Vichinsky EP. New considerations in the treatment of sickle cell disease. Annu Rev Med 49: 461-474, 1998.
    • (1998) Annu Rev Med , vol.49 , pp. 461-474
    • Reed, W.1    Vichinsky, E.P.2
  • 49
    • 0028151406 scopus 로고
    • Nitric oxide regulation of superoxide and peroxynitrite-dependent lipid peroxidation. Formation of novel nitrogencontaining oxidized lipid derivatives
    • Rubbo H, Radi R, Trujillo M, Telleri R, Kalyanaraman B, Barnes S, Kirk M, Freeman BA. Nitric oxide regulation of superoxide and peroxynitrite-dependent lipid peroxidation. Formation of novel nitrogencontaining oxidized lipid derivatives. J Biol Chem 269: 26066-26075, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 26066-26075
    • Rubbo, H.1    Radi, R.2    Trujillo, M.3    Telleri, R.4    Kalyanaraman, B.5    Barnes, S.6    Kirk, M.7    Freeman, B.A.8
  • 50
    • 0023226343 scopus 로고
    • Protein 4.1 in sickle erythrocytes. Evidence for oxidative damage
    • Schwartz RS, Rybicki AC, Heath RH, Lubin BH. Protein 4.1 in sickle erythrocytes. Evidence for oxidative damage. J Biol Chem 262: 15666-15672, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 15666-15672
    • Schwartz, R.S.1    Rybicki, A.C.2    Heath, R.H.3    Lubin, B.H.4
  • 51
    • 0027417591 scopus 로고
    • Lethal thalassemia after insertional disruption of the mouse major adult beta-globin gene
    • Shehee WR, Oliver P, Smithies O. Lethal thalassemia after insertional disruption of the mouse major adult beta-globin gene. Proc Natl Acad Sci USA 90: 3177-3181, 1993.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3177-3181
    • Shehee, W.R.1    Oliver, P.2    Smithies, O.3
  • 52
    • 0030893396 scopus 로고    scopus 로고
    • Fetal hemoglobin in sickle cell anemia: Determinants of response to hydroxyurea. Multicenter Study of Hydroxyurea
    • Steinberg MH, Lu ZH, Barton FB, Terrin ML, Charache S, Dover GJ. Fetal hemoglobin in sickle cell anemia: determinants of response to hydroxyurea. Multicenter Study of Hydroxyurea. Blood 89: 1078-1088, 1997.
    • (1997) Blood , vol.89 , pp. 1078-1088
    • Steinberg, M.H.1    Lu, Z.H.2    Barton, F.B.3    Terrin, M.L.4    Charache, S.5    Dover, G.J.6
  • 53
    • 0036790992 scopus 로고    scopus 로고
    • Protein nitration is mediated by heme and free metals through Fenton-type chemistry: An alternative to the NO/O2- reaction
    • Thomas DD, Espey MG, Vitek MP, Miranda KM, Wink DA. Protein nitration is mediated by heme and free metals through Fenton-type chemistry: an alternative to the NO/O2- reaction. Proc Natl Acad Sci USA 99: 12691-12696, 2002.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12691-12696
    • Thomas, D.D.1    Espey, M.G.2    Vitek, M.P.3    Miranda, K.M.4    Wink, D.A.5
  • 55
    • 0032171420 scopus 로고    scopus 로고
    • Chemical biology of nitric oxide: Insights into regulatory, cytotoxic, and cytoprotective mechanisms of nitric oxide
    • Wink DA, Mitchell JB. Chemical biology of nitric oxide: Insights into regulatory, cytotoxic, and cytoprotective mechanisms of nitric oxide. Free Radic Biol Med 25: 434-456, 1998.
    • (1998) Free Radic Biol Med , vol.25 , pp. 434-456
    • Wink, D.A.1    Mitchell, J.B.2
  • 56
    • 20444468127 scopus 로고    scopus 로고
    • Endothelial cell NADPH oxidase mediates the cerebral microvascular dysfunction in sickle cell transgenic mice
    • Wood KC, Hebbel RP, Granger DN. Endothelial cell NADPH oxidase mediates the cerebral microvascular dysfunction in sickle cell transgenic mice. FASEB J 19: 989-991, 2005.
    • (2005) FASEB J , vol.19 , pp. 989-991
    • Wood, K.C.1    Hebbel, R.P.2    Granger, D.N.3
  • 57
    • 1542376929 scopus 로고    scopus 로고
    • Glutathione metabolism and its implications for health
    • Wu G, Fang YZ, Yang S, Lupton JR, Turner ND. Glutathione metabolism and its implications for health. J Nutr 134: 489-492, 2004.
    • (2004) J Nutr , vol.134 , pp. 489-492
    • Wu, G.1    Fang, Y.Z.2    Yang, S.3    Lupton, J.R.4    Turner, N.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.