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Volumn 29, Issue 5, 2000, Pages 403-409

Biomarkers of myeloperoxidase-derived hypochlorous acid

Author keywords

Chlorohydrin; Chlorotyrosine; Free radicals; Hypochlorous acid; Myeloperoxidase; Neutrophil oxidant; Oxidant biomarker

Indexed keywords

ANTIBODY; BIOCHEMICAL MARKER; CARBONYL DERIVATIVE; CHLORIDE; CHLOROHYDRIN DERIVATIVE; CYTOSINE DERIVATIVE; HYDROGEN PEROXIDE; HYPOCHLOROUS ACID; MYELOPEROXIDASE; SULFONAMIDE; TYROSINE DERIVATIVE;

EID: 0034282230     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(00)00204-5     Document Type: Article
Times cited : (359)

References (53)
  • 1
    • 0000498676 scopus 로고    scopus 로고
    • Oxygen metabolites from phagocytes
    • J.I. Gallin, & R. Snyderman. Philadelphia: Lippincott Williams & Wilkins
    • Klebanoff S.J. Oxygen metabolites from phagocytes. Gallin J.I., Snyderman R., Inflammation basic principles and clinical correlates . 1999;721-768 Lippincott Williams & Wilkins, Philadelphia.
    • (1999) Inflammation: Basic Principles and Clinical Correlates , pp. 721-768
    • Klebanoff, S.J.1
  • 2
    • 0032213375 scopus 로고    scopus 로고
    • Inside the neutrophil phagosome: Oxidants, myeloperoxidase and bacterial killing
    • Hampton M.B., Kettle A.J., Winterbourn C.C. Inside the neutrophil phagosome oxidants, myeloperoxidase and bacterial killing . Blood. 92:1998;3007-3017.
    • (1998) Blood , vol.92 , pp. 3007-3017
    • Hampton, M.B.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 3
    • 0017240322 scopus 로고
    • Studies on the chlorinating activity of myeloperoxidase
    • Harrison J.E., Shultz J. Studies on the chlorinating activity of myeloperoxidase. J. Biol. Chem. 251:1976;1371-1374.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1371-1374
    • Harrison, J.E.1    Shultz, J.2
  • 4
    • 0030915481 scopus 로고    scopus 로고
    • Myeloperoxidase: A key regulator of neutrophil oxidant production
    • Kettle A.J., Winterbourn C.C. Myeloperoxidase A key regulator of neutrophil oxidant production . Redox Rep. 3:1997;3-15.
    • (1997) Redox Rep. , vol.3 , pp. 3-15
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 5
    • 0028292033 scopus 로고
    • Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions
    • Daugherty A., Dunn J.L., Rateri D.L., Heinecke J.W. Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions. J. Clin. Invest. 94:1994;437-444.
    • (1994) J. Clin. Invest. , vol.94 , pp. 437-444
    • Daugherty, A.1    Dunn, J.L.2    Rateri, D.L.3    Heinecke, J.W.4
  • 7
    • 0003698541 scopus 로고
    • Biological reactivity of hypochlorous acid: Implications for microbicidal mechanisms of leukocyte myeloperoxidase
    • Albrich J.M., McCarthy C.A., Hurst J.K. Biological reactivity of hypochlorous acid implications for microbicidal mechanisms of leukocyte myeloperoxidase . Proc. Natl. Acad. Sci. USA. 78:1981;210-214.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 210-214
    • Albrich, J.M.1    McCarthy, C.A.2    Hurst, J.K.3
  • 8
    • 0021807129 scopus 로고
    • Comparative reactivities of various biological compounds with myeloperoxidase-hydrogen peroxide-chloride, and similarity of the oxidant to hypochlorite
    • Winterbourn C.C. Comparative reactivities of various biological compounds with myeloperoxidase-hydrogen peroxide-chloride, and similarity of the oxidant to hypochlorite. Biochim. Biophys. Acta. 840:1985;204-210.
    • (1985) Biochim. Biophys. Acta , vol.840 , pp. 204-210
    • Winterbourn, C.C.1
  • 10
    • 0030220396 scopus 로고    scopus 로고
    • Hypochlorous acid interactions with thiols, nucleotides, DNA, and other biological substrates
    • Prutz W.A. Hypochlorous acid interactions with thiols, nucleotides, DNA, and other biological substrates. Arch. Biochem. Biophys. 332:1996;110-120.
    • (1996) Arch. Biochem. Biophys. , vol.332 , pp. 110-120
    • Prutz, W.A.1
  • 11
    • 0031820996 scopus 로고    scopus 로고
    • Interactions of hypochlorous acid with pyrimidine nucleotides, and secondary reactions of chlorinated pyrimidines with GSH, NADH, and other substrates
    • Prutz W.A. Interactions of hypochlorous acid with pyrimidine nucleotides, and secondary reactions of chlorinated pyrimidines with GSH, NADH, and other substrates. Arch. Biochem. Biophys. 349:1998;183-191.
    • (1998) Arch. Biochem. Biophys. , vol.349 , pp. 183-191
    • Prutz, W.A.1
  • 12
    • 0030046117 scopus 로고    scopus 로고
    • Neutrophils convert tyrosyl residues in albumin to chlorotyrosine
    • Kettle A.J. Neutrophils convert tyrosyl residues in albumin to chlorotyrosine. FEBS Lett. 379:1996;103-106.
    • (1996) FEBS Lett. , vol.379 , pp. 103-106
    • Kettle, A.J.1
  • 14
    • 0028023373 scopus 로고
    • Cholesterol chlorohydrin synthesis by the myeloperoxidase-hydrogen peroxide-chloride system: Potential markers for lipoproteins oxidatively damaged by phagocytes
    • Heinecke J.W., Li W., Mueller D.M., Bohrer A., Turk J. Cholesterol chlorohydrin synthesis by the myeloperoxidase-hydrogen peroxide-chloride system potential markers for lipoproteins oxidatively damaged by phagocytes . Biochemistry. 33:1994;10127-10136.
    • (1994) Biochemistry , vol.33 , pp. 10127-10136
    • Heinecke, J.W.1    Li, W.2    Mueller, D.M.3    Bohrer, A.4    Turk, J.5
  • 15
    • 0033584939 scopus 로고    scopus 로고
    • Molecular chlorine generated by the myeloperoxidase-hydrogen peroxide-chloride system of phagocytes produces 5-chlorocytosine in bacterial RNA
    • Henderson J.P., Byun J., Heinecke J.W. Molecular chlorine generated by the myeloperoxidase-hydrogen peroxide-chloride system of phagocytes produces 5-chlorocytosine in bacterial RNA. J. Biol. Chem. 274:1999;33440-33448.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33440-33448
    • Henderson, J.P.1    Byun, J.2    Heinecke, J.W.3
  • 17
    • 0030928562 scopus 로고    scopus 로고
    • Characterisation of the oxidation products of the reaction between reduced glutathione and hypochlorous acid
    • Winterbourn C.C., Brennan S.O. Characterisation of the oxidation products of the reaction between reduced glutathione and hypochlorous acid. Biochem. J. 326:1997;87-92.
    • (1997) Biochem. J. , vol.326 , pp. 87-92
    • Winterbourn, C.C.1    Brennan, S.O.2
  • 18
    • 0014280629 scopus 로고
    • Myeloperoxidase of human leukaemic leucocytes: Oxidation of amino acids in the presence of hydrogen peroxide
    • Zgliczynski J.M., Stelmaszynska T., Ostrowski W., Naskalski J., Sznajd J. Myeloperoxidase of human leukaemic leucocytes oxidation of amino acids in the presence of hydrogen peroxide . Eur. J. Biochem. 4:1968;540-547.
    • (1968) Eur. J. Biochem. , vol.4 , pp. 540-547
    • Zgliczynski, J.M.1    Stelmaszynska, T.2    Ostrowski, W.3    Naskalski, J.4    Sznajd, J.5
  • 19
    • 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 S.L., d'Avignon A., Anderson M.M., Hsu F.F., Heinecke J.W. 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. 273:1998;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
  • 20
    • 0029055476 scopus 로고
    • Chlorination of tyrosyl residues in peptides by myeloperoxidase and human neutrophils
    • Domigan N.M., Charlton T.S., Duncan M.W., Winterbourn C.C., Kettle A.J. Chlorination of tyrosyl residues in peptides by myeloperoxidase and human neutrophils. J. Biol. Chem. 270:1995;16542-16548.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16542-16548
    • Domigan, N.M.1    Charlton, T.S.2    Duncan, M.W.3    Winterbourn, C.C.4    Kettle, A.J.5
  • 21
    • 0031835174 scopus 로고    scopus 로고
    • Differential reactivities of hypochlorous and hypobromous acids with purified E. coli phospholipid: Formation of haloamines and halohydrins
    • Carr A.C., van den Berg J.J.M., Winterbourn C.C. Differential reactivities of hypochlorous and hypobromous acids with purified E. coli phospholipid formation of haloamines and halohydrins . Biochim. Biophys. Acta. 1392:1998;254-264.
    • (1998) Biochim. Biophys. Acta , vol.1392 , pp. 254-264
    • Carr, A.C.1    Van den Berg, J.J.M.2    Winterbourn, C.C.3
  • 22
    • 0032525801 scopus 로고    scopus 로고
    • Hypochlorite-induced damage to proteins: Formation of nitrogen-centered radicals from lysine residues and their role in protein fragmentation
    • Hawkins C.L., Davies M.J. Hypochlorite-induced damage to proteins formation of nitrogen-centered radicals from lysine residues and their role in protein fragmentation . Biochem. J. 332:1998;617-625.
    • (1998) Biochem. J. , vol.332 , pp. 617-625
    • Hawkins, C.L.1    Davies, M.J.2
  • 24
    • 0025980710 scopus 로고
    • Oxidative damage to fibronectin. I. The effects of the neutrophil myeloperoxidase system and HOCl
    • Vissers M.C.M., Winterbourn C.C. Oxidative damage to fibronectin. I. The effects of the neutrophil myeloperoxidase system and HOCl. Arch. Biochem. Biophys. 285:1991;53-59.
    • (1991) Arch. Biochem. Biophys. , vol.285 , pp. 53-59
    • Vissers, M.C.M.1    Winterbourn, C.C.2
  • 27
    • 0034194459 scopus 로고    scopus 로고
    • Comparison of mono and dichlorinated tyrosines with carbonyls for detection of hypochlorous acid-modified proteins
    • Chapman, A. L. P., Senthilmohan , R.; Winterbourn, C. C.; Kettle, A. J. Comparison of mono and dichlorinated tyrosines with carbonyls for detection of hypochlorous acid-modified proteins. Arch. Biochem. Biophys. 376; 2000.
    • (2000) Arch. Biochem. Biophys. , vol.376
    • Chapman, A.L.P.1    Senthilmohan, R.2    Winterbourn, C.C.3    Kettle, A.J.4
  • 28
    • 0030803161 scopus 로고    scopus 로고
    • Mass spectrometric quantification of 3-chlorotyrosine in human tissues with attomole sensitivity: A sensitive and specific marker for myeloperoxidase-catalyzed chlorination at sites of inflammation
    • Hazen S.L., Crowley J.R., Mueller D.M., Heinecke J.W. Mass spectrometric quantification of 3-chlorotyrosine in human tissues with attomole sensitivity a sensitive and specific marker for myeloperoxidase-catalyzed chlorination at sites of inflammation . Free Radic. Biol. Med. 23:1997;909-916.
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 909-916
    • Hazen, S.L.1    Crowley, J.R.2    Mueller, D.M.3    Heinecke, J.W.4
  • 29
    • 0025959286 scopus 로고
    • Reactions of aqueous chlorine in vitro in stomach fluid from the rat: Chlorination of tyrosine
    • Nickelsen M.G., Nweke A., Scully F.E.J., Ringhand H.P. Reactions of aqueous chlorine in vitro in stomach fluid from the rat chlorination of tyrosine . Chem. Res. Toxicol. 4:1991;94-101.
    • (1991) Chem. Res. Toxicol. , vol.4 , pp. 94-101
    • Nickelsen, M.G.1    Nweke, A.2    Scully, F.E.J.3    Ringhand, H.P.4
  • 30
    • 0030979720 scopus 로고    scopus 로고
    • 3-Chlorotyrosine, a specific marker of myeloperoxidase-catalyzed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima
    • Hazen S.L., Heinecke J.W. 3-Chlorotyrosine, a specific marker of myeloperoxidase-catalyzed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima. J. Clin. Invest. 99:1997;2075-2081.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2075-2081
    • Hazen, S.L.1    Heinecke, J.W.2
  • 31
    • 0032880537 scopus 로고    scopus 로고
    • Oxidative damage to proteins of bronchoalveolar lavage fluid in patients with acute respiratory distress syndrome: Evidence for neutrophil-mediated hydroxylation, nitration, and chlorination
    • Lamb N.J., Gutteridge J.M., Baker C., Evans T.W., Quinlan G.J. Oxidative damage to proteins of bronchoalveolar lavage fluid in patients with acute respiratory distress syndrome evidence for neutrophil-mediated hydroxylation, nitration, and chlorination . Crit. Care Med. 27:1999;1738-1744.
    • (1999) Crit. Care Med. , vol.27 , pp. 1738-1744
    • Lamb, N.J.1    Gutteridge, J.M.2    Baker, C.3    Evans, T.W.4    Quinlan, G.J.5
  • 32
    • 0031772688 scopus 로고    scopus 로고
    • Measurement and significance of free and protein-bound 3-nitrotyrosine, 3-chlorotyrosine, and free 3-nitro-4-hydroxyphenylacetic acid in biologic samples: A high-performance liquid chromatography method using electrochemical detection
    • Crow J.P. Measurement and significance of free and protein-bound 3-nitrotyrosine, 3-chlorotyrosine, and free 3-nitro-4-hydroxyphenylacetic acid in biologic samples a high-performance liquid chromatography method using electrochemical detection . Methods Enzymol. 301:1999;151-160.
    • (1999) Methods Enzymol. , vol.301 , pp. 151-160
    • Crow, J.P.1
  • 33
    • 0031740893 scopus 로고    scopus 로고
    • Analysis of aromatic nitration, chlorination, and hydroxylation by gas chromatography-mass spectrometry
    • van der Vliet A., Jenner A., Eiserich J.P., Cross C.E., Halliwell B. Analysis of aromatic nitration, chlorination, and hydroxylation by gas chromatography-mass spectrometry. Methods Enzymol. 301:1999;471-483.
    • (1999) Methods Enzymol. , vol.301 , pp. 471-483
    • Van der Vliet, A.1    Jenner, A.2    Eiserich, J.P.3    Cross, C.E.4    Halliwell, B.5
  • 34
    • 0029040377 scopus 로고
    • Mass spectrometric identification of amino acid transformations during oxidation of peptides and proteins: Modifications of methionine and tyrosine
    • Chowdhury S.K., Eshraghi J., Wolfe H., Forde D., Hlavac A.G., Johnston D. Mass spectrometric identification of amino acid transformations during oxidation of peptides and proteins modifications of methionine and tyrosine . Anal. Chem. 67:1995;390-398.
    • (1995) Anal. Chem. , vol.67 , pp. 390-398
    • Chowdhury, S.K.1    Eshraghi, J.2    Wolfe, H.3    Forde, D.4    Hlavac, A.G.5    Johnston, D.6
  • 35
    • 0033596905 scopus 로고    scopus 로고
    • 3-Bromotyrosine and 3,5-dibromotyrosine are major products of protein oxidation by eosinophil peroxidase: Potential markers for eosinophil-dependent tissue injury in vivo
    • Wu W., Chen B.K., d'Avignon A., Hazen S.L. 3-Bromotyrosine and 3,5-dibromotyrosine are major products of protein oxidation by eosinophil peroxidase potential markers for eosinophil-dependent tissue injury in vivo . Biochemistry. 38:1999;3538-3548.
    • (1999) Biochemistry , vol.38 , pp. 3538-3548
    • Wu, W.1    Chen, B.K.2    D'Avignon, A.3    Hazen, S.L.4
  • 37
    • 0345683904 scopus 로고    scopus 로고
    • Detecting oxidative modification of biomolecules with isotope dilution mass spectrometry: Sensitive and quantitative assays for oxidized amino acids in proteins and tissues
    • Heinecke J.W., Hsu F.F., Crowley J.R., Hazen S.L., Leeuwenburgh C., Mueller D.M., Rasmussen J.E., Turk J. Detecting oxidative modification of biomolecules with isotope dilution mass spectrometry sensitive and quantitative assays for oxidized amino acids in proteins and tissues . Methods Enzymol. 300:1999;124-144.
    • (1999) Methods Enzymol. , vol.300 , pp. 124-144
    • Heinecke, J.W.1    Hsu, F.F.2    Crowley, J.R.3    Hazen, S.L.4    Leeuwenburgh, C.5    Mueller, D.M.6    Rasmussen, J.E.7    Turk, J.8
  • 38
    • 0027360402 scopus 로고
    • Hypochlorous acid-mediated oxidation of cholesterol and phospholipid: Analysis of reaction products by gas chromatography-mass spectrometry
    • van den Berg J.J.M., Winterbourn C.C., Kuypers F.A. Hypochlorous acid-mediated oxidation of cholesterol and phospholipid analysis of reaction products by gas chromatography-mass spectrometry . J. Lipid Res. 34:1993;2005-2012.
    • (1993) J. Lipid Res. , vol.34 , pp. 2005-2012
    • Van den Berg, J.J.M.1    Winterbourn, C.C.2    Kuypers, F.A.3
  • 40
    • 0002019504 scopus 로고    scopus 로고
    • Molecular chlorine generated by the myeloperoxidase-hydrogen peroxide-chloride system of phagocytes converts low density lipoprotein cholesterol into a family of chlorinated sterols
    • Hazen S.L., Hsu F.F., Duffin K., Heinecke J.W. Molecular chlorine generated by the myeloperoxidase-hydrogen peroxide-chloride system of phagocytes converts low density lipoprotein cholesterol into a family of chlorinated sterols. J. Biol. Chem. 271:1996;23080-23088.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23080-23088
    • Hazen, S.L.1    Hsu, F.F.2    Duffin, K.3    Heinecke, J.W.4
  • 42
    • 0030745738 scopus 로고    scopus 로고
    • A monoclonal antibody recognising the chlorohydrin derivatives of oleic acid for probing hypochlorous acid involvement in tissue injury
    • Domigan N.M., Carr A.C., Elder P.A., Lewis J.G., Winterbourn C.C. A monoclonal antibody recognising the chlorohydrin derivatives of oleic acid for probing hypochlorous acid involvement in tissue injury. Redox Rep. 3:1997;57-63.
    • (1997) Redox Rep. , vol.3 , pp. 57-63
    • Domigan, N.M.1    Carr, A.C.2    Elder, P.A.3    Lewis, J.G.4    Winterbourn, C.C.5
  • 43
    • 0031350219 scopus 로고    scopus 로고
    • Modification of red cell membrane lipids by hypochlorous acid and haemolysis by preformed lipid chlorohydrins
    • Carr A.C., Domigan N.M., Vissers M.C.M., Winterbourn C.C. Modification of red cell membrane lipids by hypochlorous acid and haemolysis by preformed lipid chlorohydrins. Redox Rep. 3:1997;263-271.
    • (1997) Redox Rep. , vol.3 , pp. 263-271
    • Carr, A.C.1    Domigan, N.M.2    Vissers, M.C.M.3    Winterbourn, C.C.4
  • 44
    • 0029914313 scopus 로고    scopus 로고
    • Peroxidase mediated bromination of unsaturated fatty acids to form bromohydrins
    • Carr A.C., Winterbourn C.C., van den Berg J.J.M. Peroxidase mediated bromination of unsaturated fatty acids to form bromohydrins. Arch. Biochem. Biophys. 327:1996;227-233.
    • (1996) Arch. Biochem. Biophys. , vol.327 , pp. 227-233
    • Carr, A.C.1    Winterbourn, C.C.2    Van den Berg, J.J.M.3
  • 45
    • 0034020050 scopus 로고    scopus 로고
    • Pathways of phospholipid oxidation by HOCl in human LDL detected by LC-MS
    • Jerlich A., Pitt A.R., Schaur R.J., Spickett C.M. Pathways of phospholipid oxidation by HOCl in human LDL detected by LC-MS. Free Radic. Biol. Med. 28:2000;673-682.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 673-682
    • Jerlich, A.1    Pitt, A.R.2    Schaur, R.J.3    Spickett, C.M.4
  • 47
  • 48
    • 0031795026 scopus 로고    scopus 로고
    • Protein carbonyl measurement by enzyme-linked immunosorbent assay
    • Winterbourn C.C., Buss H. Protein carbonyl measurement by enzyme-linked immunosorbent assay. Methods Enzymol. 300:1999;106-111.
    • (1999) Methods Enzymol. , vol.300 , pp. 106-111
    • Winterbourn, C.C.1    Buss, H.2
  • 49
    • 0033961598 scopus 로고    scopus 로고
    • Protein carbonyl measurements show evidence of early oxidative stress in critically ill patients
    • Winterbourn C.C., Buss I.H., Chan T.P., Plank L.D., Clark M.A., Windsor J.A. Protein carbonyl measurements show evidence of early oxidative stress in critically ill patients. Crit. Care Med. 28:2000;143-149.
    • (2000) Crit. Care Med. , vol.28 , pp. 143-149
    • Winterbourn, C.C.1    Buss, I.H.2    Chan, T.P.3    Plank, L.D.4    Clark, M.A.5    Windsor, J.A.6
  • 50
    • 0025911829 scopus 로고
    • Metal-catalyzed oxidation of proteins. Physiological consequences
    • Stadtman E.R., Oliver C.N. Metal-catalyzed oxidation of proteins. Physiological consequences. J. Biol. Chem. 266:1991;2005-2008.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2005-2008
    • Stadtman, E.R.1    Oliver, C.N.2
  • 53
    • 0030708939 scopus 로고    scopus 로고
    • Oxidation of neutrophil glutathione and protein thiols by myeloperoxidase-derived hypochlorous acid
    • Carr A.C., Winterbourn C.C. Oxidation of neutrophil glutathione and protein thiols by myeloperoxidase-derived hypochlorous acid. Biochem. J. 327:1997;275-281.
    • (1997) Biochem. J. , vol.327 , pp. 275-281
    • Carr, A.C.1    Winterbourn, C.C.2


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