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Volumn 112, Issue 18, 2005, Pages 2812-2820

Myeloperoxidase-generated oxidants modulate left ventricular remodeling but not infarct size after myocardial infarction

Author keywords

Amino acids; Infarction; Inflammation; Remodeling

Indexed keywords

ACROLEIN; ALDEHYDE; ALPHA AMINO ACID; CYTOTOXIC AGENT; FORMALDEHYDE; GLYCINE; LYSINE; MYELOPEROXIDASE; OXIDIZING AGENT; THREONINE; TRYPTOPHAN;

EID: 27844442307     PISSN: 00097322     EISSN: None     Source Type: Journal    
DOI: 10.1161/CIRCULATIONAHA.105.542340     Document Type: Article
Times cited : (165)

References (40)
  • 1
    • 0035682993 scopus 로고    scopus 로고
    • Limitation of infarct size and attenuation of myeloperoxidase activity by an endothelin a receptor antagonist following ischaemia and reperfusion
    • Gonon AT, Gourine AV, Middelveld RJ, Alving K. Pernow J. Limitation of infarct size and attenuation of myeloperoxidase activity by an endothelin A receptor antagonist following ischaemia and reperfusion. Basic Res Cardiol. 2001;96:454-462.
    • (2001) Basic Res Cardiol , vol.96 , pp. 454-462
    • Gonon, A.T.1    Gourine, A.V.2    Middelveld, R.J.3    Alving, K.4    Pernow, J.5
  • 2
    • 0037116550 scopus 로고    scopus 로고
    • Prognostic significance of peripheral monocytosis after reperfused acute myocardial infarction: A possible role for left ventricular remodeling
    • Maekawa Y. Anzai T, Yoshikawa T, Asakura Y, Takahashi T, Ishikawa S, Mitamura H, Ogawa S. Prognostic significance of peripheral monocytosis after reperfused acute myocardial infarction: a possible role for left ventricular remodeling. J Am Coll Cardiol. 2002;39:241-246.
    • (2002) J Am Coll Cardiol , vol.39 , pp. 241-246
    • Maekawa, Y.1    Anzai, T.2    Yoshikawa, T.3    Asakura, Y.4    Takahashi, T.5    Ishikawa, S.6    Mitamura, H.7    Ogawa, S.8
  • 3
    • 0028234163 scopus 로고
    • Polymorphonuclear leukocytes in ischemic vascular disease
    • Fisher TC, Meiselmann HJ. Polymorphonuclear leukocytes in ischemic vascular disease. Thromb Res. 1994;74(suppl 1):S21-S34.
    • (1994) Thromb Res , vol.74 , Issue.SUPPL. 1
    • Fisher, T.C.1    Meiselmann, H.J.2
  • 4
    • 0034659164 scopus 로고    scopus 로고
    • Myeloperoxidase-generated oxidants and atherosclerosis
    • Podrez EA, Abu-Soud HM, Hazen SL. Myeloperoxidase-generated oxidants and atherosclerosis. Free Radic Biol Med. 2000;28:1717-1725.
    • (2000) Free Radic Biol Med , vol.28 , pp. 1717-1725
    • Podrez, E.A.1    Abu-Soud, H.M.2    Hazen, S.L.3
  • 5
    • 0026705310 scopus 로고
    • Proteolytic inactivation of alpha 1-proteinase inhibitor and alpha 1-antichymotrypsin by oxidatively activated human neutrophil metalloproteinases
    • Desrochers PE, Mookhtiar K. Van Wart HE, Hasty KA, Weiss SJ. Proteolytic inactivation of alpha 1-proteinase inhibitor and alpha 1-antichymotrypsin by oxidatively activated human neutrophil metalloproteinases. J Biol Chem. 1992;267:5005-5012.
    • (1992) J Biol Chem , vol.267 , pp. 5005-5012
    • Desrochers, P.E.1    Mookhtiar, K.2    Van Wart, H.E.3    Hasty, K.A.4    Weiss, S.J.5
  • 6
    • 0035798684 scopus 로고    scopus 로고
    • Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7): A mechanism for matrix, metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase
    • Fu X, Kassim SY, Parks WC, Heinecke JW. Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7): a mechanism for matrix, metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase. J Biol Chem. 2001;276:41279-41287.
    • (2001) J Biol Chem , vol.276 , pp. 41279-41287
    • Fu, X.1    Kassim, S.Y.2    Parks, W.C.3    Heinecke, J.W.4
  • 7
    • 0025687479 scopus 로고
    • Oxidation susceptibility of plasminogen activator inhibitors of human plasma
    • Stief TW, Martin E, Caso F, Rodriguez JM. Oxidation susceptibility of plasminogen activator inhibitors of human plasma. Thromb Res. 1990;60:177-180.
    • (1990) Thromb Res , vol.60 , pp. 177-180
    • Stief, T.W.1    Martin, E.2    Caso, F.3    Rodriguez, J.M.4
  • 8
    • 0037416219 scopus 로고    scopus 로고
    • Myeloperoxidase and plasminogen activator inhibitor-1 play a central role in ventricular remodeling after myocardial infarction
    • Askari A, Brennan ML, zhou X, Drinko J, morehead A, Thomas JT, Topol EJ, Hazen SL, Penn MS. Myeloperoxidase and plasminogen activator inhibitor-1 play a central role in ventricular remodeling after myocardial infarction. J Exp Med. 2003;197:615-624.
    • (2003) J Exp Med , vol.197 , pp. 615-624
    • Askari, A.1    Brennan, M.L.2    Zhou, X.3    Drinko, J.4    Morehead, A.5    Thomas, J.T.6    Topol, E.J.7    Hazen, S.L.8    Penn, M.S.9
  • 9
    • 0018178223 scopus 로고
    • Oxygen-dependent microbial killing by phagocytes (second of two parts)
    • Babior BM. Oxygen-dependent microbial killing by phagocytes (second of two parts). N Engl J Med. 1978;198:721-725.
    • (1978) N Engl J Med , vol.198 , pp. 721-725
    • Babior, B.M.1
  • 12
    • 0021337229 scopus 로고
    • Myeloperoxidase-dependent fluorescein chlorination by stimulated neutrophils
    • Hurst JK, Albrich JM, Green TR, Rosen H, Klebanoff S. Myeloperoxidase-dependent fluorescein chlorination by stimulated neutrophils. J Biol Chem. 1984;259:4812-4821.
    • (1984) J Biol Chem , vol.259 , pp. 4812-4821
    • Hurst, J.K.1    Albrich, J.M.2    Green, T.R.3    Rosen, H.4    Klebanoff, S.5
  • 13
    • 0014280629 scopus 로고
    • Myeloperoxidase of human leukaemic leucocytes: Oxidation of amino acids in the presence of hydrogen peroxide
    • Zgliczynski JM, Stelmaszynska T, Ostrowiski W, Naskalski J, Sznajd J. Myeloperoxidase of human leukaemic leucocytes: oxidation of amino acids in the presence of hydrogen peroxide. Eur J Biochem. 1968;4:540-547.
    • (1968) Eur J Biochem , vol.4 , pp. 540-547
    • Zgliczynski, J.M.1    Stelmaszynska, T.2    Ostrowiski, W.3    Naskalski, J.4    Sznajd, J.5
  • 15
    • 0032510811 scopus 로고    scopus 로고
    • Human neutrophils employ myeloperoxidase to convert alpha-amino acids to a battery of reactive aldehydes: A pathway for aldehyde generation at sites of inflammation
    • Hazen SL, Hsu FF, d'Avignon A, Heinecke JW. Human neutrophils employ myeloperoxidase to convert alpha-amino acids to a battery of reactive aldehydes: a pathway for aldehyde generation at sites of inflammation. Biochemistry. 1998;37:6864-6873.
    • (1998) Biochemistry , vol.37 , pp. 6864-6873
    • Hazen, S.L.1    Hsu, F.F.2    D'Avignon, A.3    Heinecke, J.W.4
  • 16
    • 0032570808 scopus 로고    scopus 로고
    • Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes: Mechanistic studies identifying labile intermediates along the reaction pathway
    • Hazen SL, d'Avignon A, Anderson MM, Hsu FF, Heinecke JW. Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes: mechanistic studies identifying labile intermediates along the reaction pathway. J Biol Chem. 1998;273:4997-5005.
    • (1998) J Biol Chem , vol.273 , pp. 4997-5005
    • Hazen, S.L.1    D'Avignon, A.2    Anderson, M.M.3    Hsu, F.F.4    Heinecke, J.W.5
  • 17
    • 0030854261 scopus 로고    scopus 로고
    • Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to convert hydroxy-amino acids into glycolaldehyde, 2-hydroxypropanal, and acrolein: A mechanism for the generation of highly reactive alpha-hydroxy and alpha, beta-unsaturated aldehydes by phagocytes at sites of inflammation
    • Anderson MM, Hazen SL, Hsu FF, Heinecke JW. Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to convert hydroxy-amino acids into glycolaldehyde, 2-hydroxypropanal, and acrolein: a mechanism for the generation of highly reactive alpha-hydroxy and alpha, beta-unsaturated aldehydes by phagocytes at sites of inflammation. J Clin Invest. 1997;99:424-432.
    • (1997) J Clin Invest , vol.99 , pp. 424-432
    • Anderson, M.M.1    Hazen, S.L.2    Hsu, F.F.3    Heinecke, J.W.4
  • 18
    • 0030053876 scopus 로고    scopus 로고
    • P-Hydroxyphenylacetaldehyde is the major product of L-tyrosine oxidation by activated human phagocytes: A chloride-dependent mechanism for the conversion of free amino acids into reactive aldehydes by myeloperoxidase
    • Hazen SL, Hsu FF, Heinecke JW. p-Hydroxyphenylacetaldehyde is the major product of L-tyrosine oxidation by activated human phagocytes: a chloride-dependent mechanism for the conversion of free amino acids into reactive aldehydes by myeloperoxidase. J Biol Chem. 1996;271:1861-1867.
    • (1996) J Biol Chem , vol.271 , pp. 1861-1867
    • Hazen, S.L.1    Hsu, F.F.2    Heinecke, J.W.3
  • 20
    • 3042735742 scopus 로고    scopus 로고
    • Myeloperoxidase and plaque vulnerability
    • Hazen SL. Myeloperoxidase and plaque vulnerability. Arterioscler Thromb Vasc Biol. 2004;24:1143-1146.
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , pp. 1143-1146
    • Hazen, S.L.1
  • 21
    • 0033520499 scopus 로고    scopus 로고
    • Eosinophil peroxidase nitrates protein tyrosyl residues: Implications for oxidative damage by nitrating intermediates in eosinophilic inflammatory disorders
    • Wu W, Chen Y, Hazen SL. Eosinophil peroxidase nitrates protein tyrosyl residues: implications for oxidative damage by nitrating intermediates in eosinophilic inflammatory disorders. J Biol Chem. 1999;274:25933-25944.
    • (1999) J Biol Chem , vol.274 , pp. 25933-25944
    • Wu, W.1    Chen, Y.2    Hazen, S.L.3
  • 22
    • 0015416039 scopus 로고
    • Enthalpy of decomposition of hydrogen peroxide by catalase at 25 degrees C (with molar extinction coefficients of H2O2 solutions in the UV)
    • Nelson DP, Kiesow LA. Enthalpy of decomposition of hydrogen peroxide by catalase at 25 degrees C (with molar extinction coefficients of H2O2 solutions in the UV). Anal Biochem. 1972;49:474-478.
    • (1972) Anal Biochem , vol.49 , pp. 474-478
    • Nelson, D.P.1    Kiesow, L.A.2
  • 23
    • 8544251150 scopus 로고
    • The acid ionization constant of HOCl from 5-35°C
    • Morris JC. The acid ionization constant of HOCl from 5-35°C. J Phys Chem. 1966;70:3798-3805.
    • (1966) J Phys Chem , vol.70 , pp. 3798-3805
    • Morris, J.C.1
  • 24
    • 0030872969 scopus 로고    scopus 로고
    • P-Hydroxyphenytacetatdehyde, the major product of L-tyrosine oxidation by the myeloperoxidase-H2O2-chloride system of phagocytes, covalently modifies epsilon-amino groups of protein lysine residues
    • Hazen SL, Gaul JP, Hsu FF, Crowley JR, d'Avignon A, Heinecke JW. p-Hydroxyphenytacetatdehyde, the major product of L-tyrosine oxidation by the myeloperoxidase-H2O2-chloride system of phagocytes, covalently modifies epsilon-amino groups of protein lysine residues. J Biol Chem. 1997;272:16990-16998.
    • (1997) J Biol Chem , vol.272 , pp. 16990-16998
    • Hazen, S.L.1    Gaul, J.P.2    Hsu, F.F.3    Crowley, J.R.4    D'Avignon, A.5    Heinecke, J.W.6
  • 25
    • 0025259422 scopus 로고
    • Cytotoxicity and metabolism of 4-hydroxy-2-nonenal and 2-nonenal in H2O2-resistant cell lines: Do aldehydic by-products of lipid peroxidation contribute to oxidative stress?
    • Spitz DR, Malcolm RR, Roberts RJ. Cytotoxicity and metabolism of 4-hydroxy-2-nonenal and 2-nonenal in H2O2-resistant cell lines: do aldehydic by-products of lipid peroxidation contribute to oxidative stress? Biochem J. 1990;267:453-459.
    • (1990) Biochem J , vol.267 , pp. 453-459
    • Spitz, D.R.1    Malcolm, R.R.2    Roberts, R.J.3
  • 29
    • 0034953219 scopus 로고    scopus 로고
    • Glutathione depletion in rat hepatocytes: A mixture toxicity study with alpha, beta-unsaturated esters
    • Freidig A, Hofhuis M, Van HI, Hermens J. Glutathione depletion in rat hepatocytes: a mixture toxicity study with alpha, beta-unsaturated esters. Xenobiotica. 2001;31:295-307.
    • (2001) Xenobiotica , vol.31 , pp. 295-307
    • Freidig, A.1    Hofhuis, M.2    Van, H.I.3    Hermens, J.4
  • 30
    • 0034988283 scopus 로고    scopus 로고
    • Glutathione elevation and its protective role in acrolein-induced protein damage in synaptosomal membranes: Relevance to brain lipid peroxidation in neurodegenerative disease
    • Pocernich CB, Cardin AL, Racine CL, Lauderback CM, Butterfield DA. Glutathione elevation and its protective role in acrolein-induced protein damage in synaptosomal membranes: relevance to brain lipid peroxidation in neurodegenerative disease. Neurochem Int. 2001;39:141-149.
    • (2001) Neurochem Int , vol.39 , pp. 141-149
    • Pocernich, C.B.1    Cardin, A.L.2    Racine, C.L.3    Lauderback, C.M.4    Butterfield, D.A.5
  • 32
    • 0034619517 scopus 로고    scopus 로고
    • Association between white blood cell count, epicardial blood flow, myocardial perfusion, and clinical outcomes in the setting of acute myocardial infarction: A Thrombolysis in Myocardial Infarction 10 substudy
    • Barron HV, Cannon CP, Murphy SA, Braunwald E, Gibson CM. Association between white blood cell count, epicardial blood flow, myocardial perfusion, and clinical outcomes in the setting of acute myocardial infarction: a Thrombolysis in Myocardial Infarction 10 substudy. Circulation. 2000;102:2329-2334.
    • (2000) Circulation , vol.102 , pp. 2329-2334
    • Barron, H.V.1    Cannon, C.P.2    Murphy, S.A.3    Braunwald, E.4    Gibson, C.M.5
  • 34
  • 35
    • 0022973331 scopus 로고
    • Role of cardiac glutathione transferase and of the glutathione S-conjugate export system in biotransformation of 4-hydroxynonenal in the heart
    • Ishikawa T, Esterbauer H, Sies H. Role of cardiac glutathione transferase and of the glutathione S-conjugate export system in biotransformation of 4-hydroxynonenal in the heart. J Biol Chem. 1986;261:1576-1581.
    • (1986) J Biol Chem , vol.261 , pp. 1576-1581
    • Ishikawa, T.1    Esterbauer, H.2    Sies, H.3
  • 36
    • 0022534948 scopus 로고
    • Rat glutathione transferase 8-8, an enzyme efficiently detoxifying 4-hydroxyalk-2-enals
    • Jensson H, Guthenberg C, Alin P, Mannervik B. Rat glutathione transferase 8-8, an enzyme efficiently detoxifying 4-hydroxyalk-2-enals. FEBS Lett. 1986;203:207-209.
    • (1986) FEBS Lett , vol.203 , pp. 207-209
    • Jensson, H.1    Guthenberg, C.2    Alin, P.3    Mannervik, B.4
  • 40
    • 0035808003 scopus 로고    scopus 로고
    • Double-blind, randomized trial of an anti-CD 18 antibody in conjunction with recombinant tissue plasminogen activator for acute myocardial infarction: Limitation of Myocardial Infarction Following Thrombolysis in Acute Myocardial Infarction (LIMIT AMI) study
    • Baran KW, Nguyen M, McKendall GR, Lambrew CT, Dykstra G, Palmeri ST, Gibbons RJ, Borzak S, Sobel BE, Gourlay SG, Rundle AC, Gibson CM, Barron HV. Double-blind, randomized trial of an anti-CD 18 antibody in conjunction with recombinant tissue plasminogen activator for acute myocardial infarction: Limitation of Myocardial Infarction Following Thrombolysis in Acute Myocardial Infarction (LIMIT AMI) study. Circulation. 2001;104:2778-2783.
    • (2001) Circulation , vol.104 , pp. 2778-2783
    • Baran, K.W.1    Nguyen, M.2    McKendall, G.R.3    Lambrew, C.T.4    Dykstra, G.5    Palmeri, S.T.6    Gibbons, R.J.7    Borzak, S.8    Sobel, B.E.9    Gourlay, S.G.10    Rundle, A.C.11    Gibson, C.M.12    Barron, H.V.13


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.