메뉴 건너뛰기




Volumn 421, Issue 1, 2009, Pages 79-86

Inhibition of myeloperoxidase-mediated hypochlorous acid production by nitroxides

Author keywords

Hypochlorous acid; Myeloperoxidase; Neutrophil; Nitroxide; Protein oxidation; Superoxide

Indexed keywords

HYPOCHLOROUS ACID; MYELOPEROXIDASE; NEUTROPHIL; NITROXIDE; PROTEIN OXIDATION; SUPEROXIDE;

EID: 67650281758     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20090309     Document Type: Article
Times cited : (71)

References (43)
  • 1
    • 0032213375 scopus 로고    scopus 로고
    • Inside the neutrophil phagosome: Oxidants, myeloperoxidase, and bacterial killing
    • Hampton, M. B., Kettle, A. J. and Winterbourn, C. C. (1998) Inside the neutrophil phagosome: Oxidants, myeloperoxidase, and bacterial killing. Blood 92, 3007-3017
    • (1998) Blood , vol.92 , pp. 3007-3017
    • Hampton, M.B.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 2
    • 30544453005 scopus 로고    scopus 로고
    • Bromination and chlorination reactions of myeloperoxidase at physiological concentrations of bromide and chloride
    • Senthilmohan, R. and Kettle, A. J. (2006) Bromination and chlorination reactions of myeloperoxidase at physiological concentrations of bromide and chloride. Arch. Biochem. Biophys. 445, 235-244
    • (2006) Arch. Biochem. Biophys , vol.445 , pp. 235-244
    • Senthilmohan, R.1    Kettle, A.J.2
  • 3
    • 0030660227 scopus 로고    scopus 로고
    • Thiocyanate and chloride as competing substrates for myeloperoxidase
    • van Dalen, C. J., Whitehouse, M. W., Winterbourn, C. C. and Kettle, A. J. (1997) Thiocyanate and chloride as competing substrates for myeloperoxidase. Biochem. J. 327, 487-492
    • (1997) Biochem. J , vol.327 , pp. 487-492
    • van Dalen, C.J.1    Whitehouse, M.W.2    Winterbourn, C.C.3    Kettle, A.J.4
  • 4
    • 18244390487 scopus 로고    scopus 로고
    • Myeloperoxidase: Friend and foe
    • Klebanoff, S. J. (2005) Myeloperoxidase: Friend and foe. J. Leukoc. Biol. 77, 598-625
    • (2005) J. Leukoc. Biol , vol.77 , pp. 598-625
    • Klebanoff, S.J.1
  • 6
    • 43049173503 scopus 로고    scopus 로고
    • Mammalian heme peroxidases: From molecular mechanisms to health implications
    • Davies, M. J., Hawkins, C. L., Pattison, D. I. and Rees, M. D. (2008) Mammalian heme peroxidases: From molecular mechanisms to health implications. Antioxid. Redox Signal. 10, 1199-1234
    • (2008) Antioxid. Redox Signal , vol.10 , pp. 1199-1234
    • Davies, M.J.1    Hawkins, C.L.2    Pattison, D.I.3    Rees, M.D.4
  • 7
    • 0027516393 scopus 로고
    • Oxidation of low-density lipoprotein with hypochlorite causes transformation of the lipoprotein into a high-uptake form for macrophages
    • Hazell, L. J. and Stocker, R. (1993) Oxidation of low-density lipoprotein with hypochlorite causes transformation of the lipoprotein into a high-uptake form for macrophages. Biochem. J. 290, 165-172
    • (1993) Biochem. J , vol.290 , pp. 165-172
    • Hazell, L.J.1    Stocker, R.2
  • 8
    • 50449086363 scopus 로고    scopus 로고
    • Methionine oxidation impairs reverse cholesterol transport by apolipoprotein A-1
    • Shao, B. H., Cavigiolio, G., Brot, N., Oda, M. N. and Heinecke, J. W. (2008) Methionine oxidation impairs reverse cholesterol transport by apolipoprotein A-1. Proc. Natl. Acad. Sci. U.S.A. 105, 12224-12229
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 12224-12229
    • Shao, B.H.1    Cavigiolio, G.2    Brot, N.3    Oda, M.N.4    Heinecke, J.W.5
  • 9
    • 44149089267 scopus 로고    scopus 로고
    • Oxidative damage to extracellular matrix and its role in human pathologies
    • Rees, M. D., Kennett, E. C., Whitelock, J. M. and Davies, M. J. (2008) Oxidative damage to extracellular matrix and its role in human pathologies. Free Radical Biol. Med. 44, 1973-2001
    • (2008) Free Radical Biol. Med , vol.44 , pp. 1973-2001
    • Rees, M.D.1    Kennett, E.C.2    Whitelock, J.M.3    Davies, M.J.4
  • 11
    • 39749145196 scopus 로고    scopus 로고
    • Translating molecular discoveries into new therapies for atherosclerosis
    • Rader, D. J. and Daugherty, A. (2008) Translating molecular discoveries into new therapies for atherosclerosis. Nature 451, 904-913
    • (2008) Nature , vol.451 , pp. 904-913
    • Rader, D.J.1    Daugherty, A.2
  • 12
    • 0026079216 scopus 로고
    • Mechanism of inhibition of myeloperoxidase by anti-inflammatory drugs
    • Kettle, A. J. and Winterbourn, C. C. (1991) Mechanism of inhibition of myeloperoxidase by anti-inflammatory drugs. Biochem. Pharmacol. 41 1485-1492
    • (1991) Biochem. Pharmacol , vol.41 , pp. 1485-1492
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 13
    • 0031029267 scopus 로고    scopus 로고
    • Mechanism of inactivation of myeloperoxidase by 4-aminobenzoic acid hydrazide
    • Kettle, A. J., Gedye, C. A. and Winterbourn, C. C. (1997) Mechanism of inactivation of myeloperoxidase by 4-aminobenzoic acid hydrazide. Biochem. J. 321, 503-508
    • (1997) Biochem. J , vol.321 , pp. 503-508
    • Kettle, A.J.1    Gedye, C.A.2    Winterbourn, C.C.3
  • 16
    • 46149125703 scopus 로고    scopus 로고
    • Inhibition of myeloperoxidase-mediated protein nitration by tempol: Kinetics, mechanism, and implications
    • Vaz, S. M. and Augusto, O. (2008) Inhibition of myeloperoxidase-mediated protein nitration by tempol: Kinetics, mechanism, and implications. Proc. Natl. Acad. Sci. U.S.A. 105, 8191-8196
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 8191-8196
    • Vaz, S.M.1    Augusto, O.2
  • 17
    • 3342875505 scopus 로고    scopus 로고
    • Nitroxides scavenge myeloperoxidase-catalyzed thiyl radicals in model systems and in cells
    • Borisenko, G. G., Martin, I., Zhao, Q., Amoscato, A. and Kagan, V. E. (2004) Nitroxides scavenge myeloperoxidase-catalyzed thiyl radicals in model systems and in cells. J. Am. Chem. Soc. 126, 9221-9232
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 9221-9232
    • Borisenko, G.G.1    Martin, I.2    Zhao, Q.3    Amoscato, A.4    Kagan, V.E.5
  • 18
    • 0001480130 scopus 로고    scopus 로고
    • The synthesis of water soluble isoindoline nitroxides and a pronitroxide hydroxylamine hydrochloride UV-VIS probe for free radicals
    • Reid, D. A., Bottle, S. E. and Micallef, A. S. (1998) The synthesis of water soluble isoindoline nitroxides and a pronitroxide hydroxylamine hydrochloride UV-VIS probe for free radicals. Chem. Commun. 17, 1907-1908
    • (1998) Chem. Commun , vol.17 , pp. 1907-1908
    • Reid, D.A.1    Bottle, S.E.2    Micallef, A.S.3
  • 21
    • 0032893101 scopus 로고    scopus 로고
    • Human perlecan immunopurified from different endothelial cell sources has different adhesive properties for vascular cells
    • Whitelock, J. M., Graham, L. D., Melrose, J., Murdoch, A. D., Iozzo, R. V. and Underwood, P. A. (1999) Human perlecan immunopurified from different endothelial cell sources has different adhesive properties for vascular cells. Matrix Biol. 18, 163-178
    • (1999) Matrix Biol , vol.18 , pp. 163-178
    • Whitelock, J.M.1    Graham, L.D.2    Melrose, J.3    Murdoch, A.D.4    Iozzo, R.V.5    Underwood, P.A.6
  • 22
    • 36248932605 scopus 로고    scopus 로고
    • Myricitrin as a substrate and inhibitor of myeloperoxidase: Implications for the pharmacological effects of flavonoids
    • Meotti, F. C., Senthilmohan, R., Harwood, D. T., Missau, F. C., Pizzolatti, M. G. and Kettle, A. J. (2008) Myricitrin as a substrate and inhibitor of myeloperoxidase: Implications for the pharmacological effects of flavonoids. Free Radical Biol. Med. 44, 109-120
    • (2008) Free Radical Biol. Med , vol.44 , pp. 109-120
    • Meotti, F.C.1    Senthilmohan, R.2    Harwood, D.T.3    Missau, F.C.4    Pizzolatti, M.G.5    Kettle, A.J.6
  • 23
    • 34548206228 scopus 로고    scopus 로고
    • Hypochlorous acid-mediated protein oxidation: How important are chloramine transfer reactions and protein tertiary structure?
    • Pattison, D. I., Hawkins, C. L. and Davies, M. J. (2007) Hypochlorous acid-mediated protein oxidation: How important are chloramine transfer reactions and protein tertiary structure? Biochemistry 46, 9853-9864
    • (2007) Biochemistry , vol.46 , pp. 9853-9864
    • Pattison, D.I.1    Hawkins, C.L.2    Davies, M.J.3
  • 24
    • 0029036325 scopus 로고
    • Immunological detection and measurement of hypochlorite-modified LDL with specific monoclonal antibodies
    • Malle, F., Hazell, L., Stocker, R., Sattler, W., Esterbauer, H. and Waeg, G. (1995) Immunological detection and measurement of hypochlorite-modified LDL with specific monoclonal antibodies. Arterioseler. Thromb. Vasc, Biol. 15, 982-989
    • (1995) Arterioseler. Thromb. Vasc, Biol , vol.15 , pp. 982-989
    • Malle, F.1    Hazell, L.2    Stocker, R.3    Sattler, W.4    Esterbauer, H.5    Waeg, G.6
  • 25
    • 0032558979 scopus 로고    scopus 로고
    • Reaction of myeloperoxidase compound with chloride, bromide, iodide, and thiocyanate
    • Furtmuller, P. G., Burner, U. and Obinger, C. (1998) Reaction of myeloperoxidase compound with chloride, bromide, iodide, and thiocyanate. Biochemistry 37, 17923-17930
    • (1998) Biochemistry , vol.37 , pp. 17923-17930
    • Furtmuller, P.G.1    Burner, U.2    Obinger, C.3
  • 27
    • 0025240884 scopus 로고
    • Kinetic studies on the reaction of compound II of myeloperoxidase with ascorbic acid. Role of ascorbic acid in myeloperoxidase function
    • Marquez, L. A., Dunford, H. B. and Vanwart, H. (1990) Kinetic studies on the reaction of compound II of myeloperoxidase with ascorbic acid. Role of ascorbic acid in myeloperoxidase function. J. Biol. Chem. 265, 5666-5670
    • (1990) J. Biol. Chem , vol.265 , pp. 5666-5670
    • Marquez, L.A.1    Dunford, H.B.2    Vanwart, H.3
  • 28
    • 0027180068 scopus 로고
    • Interaction of acetaminophen with myeloperoxidase intermediates - optimum stimulation of enzyme-activity
    • Marquez, L. A. and Dunford, H. B. (1993) Interaction of acetaminophen with myeloperoxidase intermediates - optimum stimulation of enzyme-activity. Arch. Biochem. Biophys. 305, 414-420
    • (1993) Arch. Biochem. Biophys , vol.305 , pp. 414-420
    • Marquez, L.A.1    Dunford, H.B.2
  • 29
    • 0029957646 scopus 로고    scopus 로고
    • Stimulation by nitroxides of catalase-like activity of hemeproteins - Kinetics and mechanism
    • Krishna, M. C., Samuni, A., Taira, J., Goldstein, S., Mitchell, J. B. and Russo, A. (1996) Stimulation by nitroxides of catalase-like activity of hemeproteins - Kinetics and mechanism. J. Biol. Chem. 271, 26018-26025
    • (1996) J. Biol. Chem , vol.271 , pp. 26018-26025
    • Krishna, M.C.1    Samuni, A.2    Taira, J.3    Goldstein, S.4    Mitchell, J.B.5    Russo, A.6
  • 30
  • 31
    • 0027336842 scopus 로고
    • Superoxide is an antagonist of antiinflammatory drugs that inhibit hypochlorous acid production by myeloperoxidase
    • Kettle, A. J., Gedye, C. A. and Winterbourn, C. C. (1993) Superoxide is an antagonist of antiinflammatory drugs that inhibit hypochlorous acid production by myeloperoxidase. Biochem. Pharmacol. 45, 2003-2010
    • (1993) Biochem. Pharmacol , vol.45 , pp. 2003-2010
    • Kettle, A.J.1    Gedye, C.A.2    Winterbourn, C.C.3
  • 32
    • 0037577421 scopus 로고
    • Metabolism of nitroxides and their products in cells
    • Kocherginsky, N. and Swartz, H. M, eds, pp, CRC Press, FL
    • Swartz, H. M., Sentjurc, M. and Kocherginsky, N. (1995) Metabolism of nitroxides and their products in cells. In Nitroxide Spin Labels (Kocherginsky, N. and Swartz, H. M., eds.), pp. 113-147, CRC Press, FL
    • (1995) Nitroxide Spin Labels , pp. 113-147
    • Swartz, H.M.1    Sentjurc, M.2    Kocherginsky, N.3
  • 33
    • 33645503629 scopus 로고    scopus 로고
    • Structure-activity relationship of cyclic nitroxides as SOD mimics and scavengers of nitrogen dioxide and carbonate radicals
    • Goldstein, S., Samuni, A., Hideg, K. and Merenyi, G. (2006) Structure-activity relationship of cyclic nitroxides as SOD mimics and scavengers of nitrogen dioxide and carbonate radicals. J. Phys. Chem. A 110, 3679-3685
    • (2006) J. Phys. Chem. A , vol.110 , pp. 3679-3685
    • Goldstein, S.1    Samuni, A.2    Hideg, K.3    Merenyi, G.4
  • 34
    • 38349159640 scopus 로고    scopus 로고
    • One-electron oxidation and reduction potentials of nitroxide antioxidants: A theoretical study
    • Hodgson, J. L., Namazian, M., Bottle, S. E. and Coote, M. L. (2007) One-electron oxidation and reduction potentials of nitroxide antioxidants: A theoretical study. J. Phys. Chem. A 111, 13595-12605
    • (2007) J. Phys. Chem. A , vol.111 , pp. 13595-12605
    • Hodgson, J.L.1    Namazian, M.2    Bottle, S.E.3    Coote, M.L.4
  • 35
    • 0037423684 scopus 로고    scopus 로고
    • Redox properties of the couples compound I/compound II and compound II/native enzyme of human myeloperoxidase
    • Furtmuller, P. G., Arnhold, J., Jantschko, W., Pichler, H. and Obinger, C. (2003) Redox properties of the couples compound I/compound II and compound II/native enzyme of human myeloperoxidase. Biochem. Biophys. Res. Commun. 301, 551-557
    • (2003) Biochem. Biophys. Res. Commun , vol.301 , pp. 551-557
    • Furtmuller, P.G.1    Arnhold, J.2    Jantschko, W.3    Pichler, H.4    Obinger, C.5
  • 36
    • 0033030493 scopus 로고    scopus 로고
    • Kinetics of oxidation of aliphatic and aromatic thiols by myeloperoxidase compounds I and II
    • Burner, U., Jantschko, W. and Obinger, C. (1999) Kinetics of oxidation of aliphatic and aromatic thiols by myeloperoxidase compounds I and II. FEBS Lett. 443, 290-296
    • (1999) FEBS Lett , vol.443 , pp. 290-296
    • Burner, U.1    Jantschko, W.2    Obinger, C.3
  • 37
    • 0028365058 scopus 로고
    • Aromatic substrate molecules bind at the distal heme pocket of myeloperoxidase
    • Hori, H., Fenna, R. E., Kimura, S. and Ikedasaito, M. (1994) Aromatic substrate molecules bind at the distal heme pocket of myeloperoxidase. J. Biol. Chem. 269, 8388-8392
    • (1994) J. Biol. Chem , vol.269 , pp. 8388-8392
    • Hori, H.1    Fenna, R.E.2    Kimura, S.3    Ikedasaito, M.4
  • 39
    • 0037460164 scopus 로고    scopus 로고
    • The role of oxoammonium cation in the SOD-mimic activity of cyclic nitroxides
    • Goldstein, S., Merenyi, G., Russo, A. and Samuni, A. (2003) The role of oxoammonium cation in the SOD-mimic activity of cyclic nitroxides. J. Am. Chem. Soc. 125, 789-795
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 789-795
    • Goldstein, S.1    Merenyi, G.2    Russo, A.3    Samuni, A.4
  • 41
    • 0037248324 scopus 로고    scopus 로고
    • Membrane-permeable radical scavengers (tempol) for shock, ischemia-reperfusion injury, and inflammation
    • Thiemermann, C. (2003) Membrane-permeable radical scavengers (tempol) for shock, ischemia-reperfusion injury, and inflammation. Crit. Care Med. 31, S76-S84
    • (2003) Crit. Care Med , vol.31
    • Thiemermann, C.1
  • 42
    • 41149117388 scopus 로고    scopus 로고
    • Inhibition of in vivo leishmanicidal mechanisms by tempol: Nitric oxide down-regulation and oxidant scavenging
    • Linares, E., Giorgio, S. and Augusto, O. (2008) Inhibition of in vivo leishmanicidal mechanisms by tempol: Nitric oxide down-regulation and oxidant scavenging. Free Radical Biol. Med. 44, 1668-1676
    • (2008) Free Radical Biol. Med , vol.44 , pp. 1668-1676
    • Linares, E.1    Giorgio, S.2    Augusto, O.3
  • 43
    • 34250893755 scopus 로고    scopus 로고
    • Kagan, V. E., Jiang, J. F., Bayir, H. and Stoyanovsky, D. A. (2007) Targeting nitroxides to mitochondria: Location, location, location, and... concentration - Highlight Commentary on Mitochondrial superoxide dismutase mimetic inhibits peroxide-induced oxidative damage and apoptosis: Role of mitochondrial superoxide. Free Radical Biol. Med. 43, 348-350
    • Kagan, V. E., Jiang, J. F., Bayir, H. and Stoyanovsky, D. A. (2007) Targeting nitroxides to mitochondria: Location, location, location, and... concentration - Highlight Commentary on "Mitochondrial superoxide dismutase mimetic inhibits peroxide-induced oxidative damage and apoptosis: Role of mitochondrial superoxide". Free Radical Biol. Med. 43, 348-350


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.