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Volumn 33, Issue 8, 2002, Pages 1153-1164

A role for the myoglobin redox cycle in the induction of endothelial cell apoptosis

Author keywords

Apoptosis; Cell cycle; Free radicals; Hydrogen peroxide; Myoglobin; Oxidative stress; Rhabdomyolysis; Vascular injury

Indexed keywords

ASCORBIC ACID; BUTHIONINE SULFOXIMINE; CASPASE 3; CATALASE; GLUCOSE OXIDASE; GLUTATHIONE; HOE 33342; HYDROGEN PEROXIDE; IRON DERIVATIVE; MYOGLOBIN; PHOSPHATIDYLSERINE;

EID: 0037108018     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(02)01007-9     Document Type: Article
Times cited : (40)

References (48)
  • 1
    • 0034022619 scopus 로고    scopus 로고
    • Pathogenesis of renal failure in rhabdomyolysis: The role of myoglobin
    • Holt S., Moore K. Pathogenesis of renal failure in rhabdomyolysis the role of myoglobin . Exp. Nephrol. 8:2000;72-76.
    • (2000) Exp. Nephrol , vol.8 , pp. 72-76
    • Holt, S.1    Moore, K.2
  • 2
    • 0024324796 scopus 로고
    • Mechanisms of reoxygenation injury in myocardial infarction: Implications of a myoglobin redox cycle
    • Galaris D., Eddy L., Arduini A., Cadenas E., Hochstein P. Mechanisms of reoxygenation injury in myocardial infarction implications of a myoglobin redox cycle . Biochem. Biophys. Res. Commun. 160:1989;1162-1168.
    • (1989) Biochem. Biophys. Res. Commun , vol.160 , pp. 1162-1168
    • Galaris, D.1    Eddy, L.2    Arduini, A.3    Cadenas, E.4    Hochstein, P.5
  • 4
    • 0035001778 scopus 로고    scopus 로고
    • Redox reactions of hemoglobin and myoglobin: Biological and toxicological implications
    • Alayash A.I., Patel R.P., Cashon R.E. Redox reactions of hemoglobin and myoglobin biological and toxicological implications . Antioxid. Redox Signal. 3:2001;313-327.
    • (2001) Antioxid. Redox Signal , vol.3 , pp. 313-327
    • Alayash, A.I.1    Patel, R.P.2    Cashon, R.E.3
  • 5
    • 0032004514 scopus 로고    scopus 로고
    • Effect of nitric oxide on hemoprotein-catalyzed oxidative reactions
    • Jourd'heuil D., Mills L., Miles A.M., Grisham M.B. Effect of nitric oxide on hemoprotein-catalyzed oxidative reactions. Nitric Oxide. 2:1998;37-44.
    • (1998) Nitric Oxide , vol.2 , pp. 37-44
    • Jourd'heuil, D.1    Mills, L.2    Miles, A.M.3    Grisham, M.B.4
  • 6
    • 0001202803 scopus 로고
    • The reaction between metmyoglobin and hydrogen peroxide
    • George P., Irvine D.H. The reaction between metmyoglobin and hydrogen peroxide. Biochem. J. 52:1952;511-517.
    • (1952) Biochem. J , vol.52 , pp. 511-517
    • George, P.1    Irvine, D.H.2
  • 7
    • 0023624230 scopus 로고
    • The interaction of oxymyoglobin with hydrogen peroxide: The formation of ferrylmyoglobin at moderate excesses of hydrogen peroxide
    • Whitburn K.D. The interaction of oxymyoglobin with hydrogen peroxide the formation of ferrylmyoglobin at moderate excesses of hydrogen peroxide . Arch. Biochem. Biophys. 253:1987;419-430.
    • (1987) Arch. Biochem. Biophys , vol.253 , pp. 419-430
    • Whitburn, K.D.1
  • 8
    • 0028360918 scopus 로고
    • Ferrylmyoglobin: Formation and chemical reactivity toward electron-donating compounds
    • Giulivi C., Cadenas E. Ferrylmyoglobin formation and chemical reactivity toward electron-donating compounds . Methods Enzymol. 233:1994;189-202.
    • (1994) Methods Enzymol , vol.233 , pp. 189-202
    • Giulivi, C.1    Cadenas, E.2
  • 9
    • 0035371323 scopus 로고    scopus 로고
    • The effects of pH on the mechanism of hydrogen peroxide and lipid hydroperoxide consumption by myoglobin: A role for the protonated ferryl species
    • Reeder B.J., Wilson M.T. The effects of pH on the mechanism of hydrogen peroxide and lipid hydroperoxide consumption by myoglobin a role for the protonated ferryl species . Free Radic. Biol. Med. 30:2001;1311-1318.
    • (2001) Free Radic. Biol. Med , vol.30 , pp. 1311-1318
    • Reeder, B.J.1    Wilson, M.T.2
  • 10
    • 0035820321 scopus 로고    scopus 로고
    • An EPR study of the peroxyl radicals induced by hydrogen peroxide in the haem proteins
    • Svistunenko D.A. An EPR study of the peroxyl radicals induced by hydrogen peroxide in the haem proteins. Biochim. Biophys. Acta. 1546:2001;365-378.
    • (2001) Biochim. Biophys. Acta , vol.1546 , pp. 365-378
    • Svistunenko, D.A.1
  • 11
    • 0026063955 scopus 로고
    • Identification of a globin free radical in equine myoglobin treated with peroxides
    • Davies M.J. Identification of a globin free radical in equine myoglobin treated with peroxides. Biochim. Biophys. Acta. 1077:1991;86-90.
    • (1991) Biochim. Biophys. Acta , vol.1077 , pp. 86-90
    • Davies, M.J.1
  • 12
    • 0031984429 scopus 로고    scopus 로고
    • Heme protein radicals: Formation, fate, and biological consequences
    • Giulivi C., Cadenas E. Heme protein radicals formation, fate, and biological consequences . Free Radic. Biol. Med. 24:1998;269-279.
    • (1998) Free Radic. Biol. Med , vol.24 , pp. 269-279
    • Giulivi, C.1    Cadenas, E.2
  • 13
    • 0028284759 scopus 로고
    • Reaction of myoglobin with hydrogen peroxide forms a peroxyl radical which oxidizes substrates
    • Kelman D.J., DeGray J.A., Mason R.P. Reaction of myoglobin with hydrogen peroxide forms a peroxyl radical which oxidizes substrates. J. Biol. Chem. 269:1994;7458-7463.
    • (1994) J. Biol. Chem , vol.269 , pp. 7458-7463
    • Kelman, D.J.1    DeGray, J.A.2    Mason, R.P.3
  • 14
    • 0022273861 scopus 로고
    • Epoxidation of styrene by hemoglobin and myoglobin. Transfer of oxidizing equivalents to the protein surface
    • Ortiz de Montellano P.R., Catalano C.E. Epoxidation of styrene by hemoglobin and myoglobin. Transfer of oxidizing equivalents to the protein surface. J. Biol. Chem. 260:1985;9265-9271.
    • (1985) J. Biol. Chem , vol.260 , pp. 9265-9271
    • Ortiz de Montellano, P.R.1    Catalano, C.E.2
  • 16
    • 0031028512 scopus 로고    scopus 로고
    • On the molecular mechanism of metmyoglobin-catalyzed reduction of hydrogen peroxide by ascorbate
    • Galaris D., Korantzopoulos P. On the molecular mechanism of metmyoglobin-catalyzed reduction of hydrogen peroxide by ascorbate. Free Radic. Biol. Med. 22:1997;657-667.
    • (1997) Free Radic. Biol. Med , vol.22 , pp. 657-667
    • Galaris, D.1    Korantzopoulos, P.2
  • 17
    • 0024431857 scopus 로고
    • The suppression of iron release from activated myoglobin by physiological electron donors and by desferrioxamine
    • Rice-Evans C., Okunade G., Khan R. The suppression of iron release from activated myoglobin by physiological electron donors and by desferrioxamine. Free Radic. Res. Commun. 7:1989;45-54.
    • (1989) Free Radic. Res. Commun , vol.7 , pp. 45-54
    • Rice-Evans, C.1    Okunade, G.2    Khan, R.3
  • 18
    • 0022396339 scopus 로고
    • Myoglobin-catalyzed hydrogen peroxide dependent arachidonic acid peroxidation
    • Grisham M.B. Myoglobin-catalyzed hydrogen peroxide dependent arachidonic acid peroxidation. J. Free Radic. Biol. Med. 1:1985;227-232.
    • (1985) J. Free Radic. Biol. Med , vol.1 , pp. 227-232
    • Grisham, M.B.1
  • 19
    • 0033696273 scopus 로고    scopus 로고
    • Interactions of hemoglobin with hydrogen peroxide alters thiol levels and course of endothelial cell death
    • D'Agnillo F., Alayash A.I. Interactions of hemoglobin with hydrogen peroxide alters thiol levels and course of endothelial cell death. Am. J. Physiol. 279:2000;H1880-H1889.
    • (2000) Am. J. Physiol , vol.279
    • D'Agnillo, F.1    Alayash, A.I.2
  • 20
    • 0027398636 scopus 로고
    • Myoglobin protects against endothelial cell membrane damage associated with hydrogen peroxide or xanthine/xanthine oxidase
    • Yang W., de Bono D. Myoglobin protects against endothelial cell membrane damage associated with hydrogen peroxide or xanthine/xanthine oxidase. FEBS Lett. 319:1993;145-150.
    • (1993) FEBS Lett , vol.319 , pp. 145-150
    • Yang, W.1    De Bono, D.2
  • 21
    • 0035760898 scopus 로고    scopus 로고
    • Redox cycling of diaspirin cross-linked hemoglobin induces G2/M arrest and apoptosis in cultured endothelial cells
    • D'Agnillo F., Alayash A.I. Redox cycling of diaspirin cross-linked hemoglobin induces G2/M arrest and apoptosis in cultured endothelial cells. Blood. 98:2001;3315-3323.
    • (2001) Blood , vol.98 , pp. 3315-3323
    • D'Agnillo, F.1    Alayash, A.I.2
  • 22
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B., Sies H., Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59:1979;527-605.
    • (1979) Physiol. Rev , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 23
    • 0035341719 scopus 로고    scopus 로고
    • 2 induce apoptosis through Fenton chemistry independent of the cellular thiol state
    • 2 induce apoptosis through Fenton chemistry independent of the cellular thiol state . Free Radic. Biol. Med. 30:2001;1008-1018.
    • (2001) Free Radic. Biol. Med , vol.30 , pp. 1008-1018
    • Antunes, F.1    Cadenas, E.2
  • 24
    • 0031441858 scopus 로고    scopus 로고
    • Preferential mitochondrial DNA injury caused by glucose oxidase as a steady generator of hydrogen peroxide in human fibroblasts
    • Salazar J.J., Van Houten B. Preferential mitochondrial DNA injury caused by glucose oxidase as a steady generator of hydrogen peroxide in human fibroblasts. Mutat. Res. 385:1997;139-149.
    • (1997) Mutat. Res , vol.385 , pp. 139-149
    • Salazar, J.J.1    Van Houten, B.2
  • 25
    • 0035933846 scopus 로고    scopus 로고
    • IRP1 activation by extracellular oxidative stress in the perfused rat liver
    • Mueller S., Pantopoulos K., Hubner C.A., Stremmel W., Hentze M.W. IRP1 activation by extracellular oxidative stress in the perfused rat liver. J. Biol. Chem. 276:2001;23192-23196.
    • (2001) J. Biol. Chem , vol.276 , pp. 23192-23196
    • Mueller, S.1    Pantopoulos, K.2    Hubner, C.A.3    Stremmel, W.4    Hentze, M.W.5
  • 26
    • 0022521858 scopus 로고
    • Neutrophil-endothelial cell interaction. Evidence for and mechanisms of the self-protection of bovine microvascular endothelial cells from hydrogen peroxide-induced oxidative stress
    • Dobrina A., Patriarca P. Neutrophil-endothelial cell interaction. Evidence for and mechanisms of the self-protection of bovine microvascular endothelial cells from hydrogen peroxide-induced oxidative stress. J. Clin. Invest. 78:1986;462-471.
    • (1986) J. Clin. Invest , vol.78 , pp. 462-471
    • Dobrina, A.1    Patriarca, P.2
  • 27
    • 0026605725 scopus 로고
    • Cystine uptake and glutathione level in endothelial cells exposed to oxidative stress
    • Miura K., Ishii T., Sugita Y., Bannai S. Cystine uptake and glutathione level in endothelial cells exposed to oxidative stress. Am. J. Physiol. 262:1992;C50-C58.
    • (1992) Am. J. Physiol , vol.262
    • Miura, K.1    Ishii, T.2    Sugita, Y.3    Bannai, S.4
  • 28
    • 0019739893 scopus 로고
    • Preparation of derivatives of ferrous and ferric hemoglobin
    • Di Lorio E.E. Preparation of derivatives of ferrous and ferric hemoglobin. Methods Enzymol. 76:1981;57-87.
    • (1981) Methods Enzymol , vol.76 , pp. 57-87
    • Di Lorio, E.E.1
  • 29
    • 0033969034 scopus 로고    scopus 로고
    • Effects of hypoxia and glutathione depletion on hemoglobin- and myoglobin-mediated oxidative stress toward endothelium
    • D'Agnillo F., Wood F., Porras C., Macdonald V.W., Alayash A.I. Effects of hypoxia and glutathione depletion on hemoglobin- and myoglobin-mediated oxidative stress toward endothelium. Biochim. Biophys. Acta. 1495:2000;150-159.
    • (2000) Biochim. Biophys. Acta , vol.1495 , pp. 150-159
    • D'Agnillo, F.1    Wood, F.2    Porras, C.3    Macdonald, V.W.4    Alayash, A.I.5
  • 30
    • 0027482489 scopus 로고
    • The reaction of ascorbic acid with different heme iron redox states of myoglobin. Antioxidant and prooxidant aspects
    • Giulivi C., Cadenas E. The reaction of ascorbic acid with different heme iron redox states of myoglobin. Antioxidant and prooxidant aspects. FEBS Lett. 332:1993;287-290.
    • (1993) FEBS Lett , vol.332 , pp. 287-290
    • Giulivi, C.1    Cadenas, E.2
  • 31
    • 0029744914 scopus 로고    scopus 로고
    • Myoglobin inhibits proliferation of cultured human proximal tubular (HK-2) cells
    • Iwata M., Zager R.A. Myoglobin inhibits proliferation of cultured human proximal tubular (HK-2) cells. Kidney Int. 50:1996;796-804.
    • (1996) Kidney Int , vol.50 , pp. 796-804
    • Iwata, M.1    Zager, R.A.2
  • 32
    • 0034982120 scopus 로고    scopus 로고
    • Continuous veno-venous hemofiltration for the immediate management of massive rhabdomyolysis after fulminant malignant hyperthermia in a bodybuilder
    • Schenk M.R., Beck D.H., Nolte M., Kox W.J. Continuous veno-venous hemofiltration for the immediate management of massive rhabdomyolysis after fulminant malignant hyperthermia in a bodybuilder. Anesthesiology. 94:2001;1139-1141.
    • (2001) Anesthesiology , vol.94 , pp. 1139-1141
    • Schenk, M.R.1    Beck, D.H.2    Nolte, M.3    Kox, W.J.4
  • 33
    • 0026732620 scopus 로고
    • A prospective study of urine and serum myoglobin levels in patients with acute rhabdomyolysis
    • Feinfeld D.A., Cheng J.T., Beysolow T.D., Briscoe A.M. A prospective study of urine and serum myoglobin levels in patients with acute rhabdomyolysis. Clin. Nephrol. 38:1992;193-195.
    • (1992) Clin. Nephrol , vol.38 , pp. 193-195
    • Feinfeld, D.A.1    Cheng, J.T.2    Beysolow, T.D.3    Briscoe, A.M.4
  • 34
    • 0021647751 scopus 로고
    • Myoglobin determination by high-performance liquid chromatography
    • Powell S.C., Friedlander E.R., Shihabi Z.K. Myoglobin determination by high-performance liquid chromatography. J. Chromatogr. 317:1984;87-92.
    • (1984) J. Chromatogr , vol.317 , pp. 87-92
    • Powell, S.C.1    Friedlander, E.R.2    Shihabi, Z.K.3
  • 38
    • 0034683031 scopus 로고    scopus 로고
    • Status of myocardial antioxidants in ischemia-reperfusion injury
    • Dhalla N.S., Elmoselhi A.B., Hata T., Makino N. Status of myocardial antioxidants in ischemia-reperfusion injury. Cardiovasc. Res. 47:2000;446-456.
    • (2000) Cardiovasc. Res , vol.47 , pp. 446-456
    • Dhalla, N.S.1    Elmoselhi, A.B.2    Hata, T.3    Makino, N.4
  • 39
    • 17744409780 scopus 로고    scopus 로고
    • Networking antioxidants in the isolated rat heart are selectively depleted by ischemia-reperfusion
    • Haramaki N., Stewart D.B., Aggarwal S., Ikeda H., Reznick A.Z., Packer L. Networking antioxidants in the isolated rat heart are selectively depleted by ischemia-reperfusion. Free Radic. Biol. Med. 25:1998;329-339.
    • (1998) Free Radic. Biol. Med , vol.25 , pp. 329-339
    • Haramaki, N.1    Stewart, D.B.2    Aggarwal, S.3    Ikeda, H.4    Reznick, A.Z.5    Packer, L.6
  • 40
    • 0025942041 scopus 로고
    • Role of glutathione in an animal model of myoglobinuric acute renal failure
    • Abul-Ezz S.R., Walker P.D., Shah S.V. Role of glutathione in an animal model of myoglobinuric acute renal failure. Proc. Natl. Acad. Sci. USA. 88:1991;9833-9837.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9833-9837
    • Abul-Ezz, S.R.1    Walker, P.D.2    Shah, S.V.3
  • 41
    • 0034818864 scopus 로고    scopus 로고
    • Glutathione deficiency intensifies ischaemia-reperfusion induced cardiac dysfunction and oxidative stress
    • Leichtweis S., Ji L.L. Glutathione deficiency intensifies ischaemia-reperfusion induced cardiac dysfunction and oxidative stress. Acta Physiol. Scand. 172:2001;1-10.
    • (2001) Acta Physiol. Scand , vol.172 , pp. 1-10
    • Leichtweis, S.1    Ji, L.L.2
  • 42
    • 0028057525 scopus 로고
    • Ferrylmyoglobin formation induced by acute magnesium deficiency in perfused rat heart causes cardiac failure
    • Wu F., Altura B.T., Gao J., Barbour R.L., Altura B.M. Ferrylmyoglobin formation induced by acute magnesium deficiency in perfused rat heart causes cardiac failure. Biochim. Biophys. Acta. 1225:1994;158-164.
    • (1994) Biochim. Biophys. Acta , vol.1225 , pp. 158-164
    • Wu, F.1    Altura, B.T.2    Gao, J.3    Barbour, R.L.4    Altura, B.M.5
  • 43
    • 0032694302 scopus 로고    scopus 로고
    • The broad spectrum of responses to oxidants in proliferating cells: A new paradigm for oxidative stress
    • Davies K.J. The broad spectrum of responses to oxidants in proliferating cells a new paradigm for oxidative stress . IUBMB Life. 48:1999;41-47.
    • (1999) IUBMB Life , vol.48 , pp. 41-47
    • Davies, K.J.1
  • 44
  • 45
    • 0033833788 scopus 로고    scopus 로고
    • Oxidative stress and cardiac disease
    • Lefer D.J., Granger D.N. Oxidative stress and cardiac disease. Am. J. Med. 109:2000;315-323.
    • (2000) Am. J. Med , vol.109 , pp. 315-323
    • Lefer, D.J.1    Granger, D.N.2
  • 47
    • 0034617045 scopus 로고    scopus 로고
    • 2. Involvement of a thiyl radical produced at cysteine 110
    • 2. Involvement of a thiyl radical produced at cysteine 110. J. Biol. Chem. 275:2000;20391-20398.
    • (2000) J. Biol. Chem , vol.275 , pp. 20391-20398
    • Witting, P.K.1    Douglas, D.J.2    Mauk, A.G.3
  • 48
    • 0035830832 scopus 로고    scopus 로고
    • Reaction of human myoglobin and nitric oxide. Heme iron or protein sulfhydryl (s) nitrosation dependence on the absence or presence of oxygen
    • Witting P.K., Douglas D.J., Mauk A.G. Reaction of human myoglobin and nitric oxide. Heme iron or protein sulfhydryl (s) nitrosation dependence on the absence or presence of oxygen. J. Biol. Chem. 276:2001;3991-3998.
    • (2001) J. Biol. Chem , vol.276 , pp. 3991-3998
    • Witting, P.K.1    Douglas, D.J.2    Mauk, A.G.3


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