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Volumn , Issue 1, 2010, Pages 27-39

Halogenizing stress and its biomarkers

Author keywords

Halogenizing stress; Hypobromite; Hypochlorite; Inflammation; Myeloperoxidase; Oesinophilic peroxidase; Reactive forms of halogens

Indexed keywords


EID: 77950144384     PISSN: 08696047     EISSN: 24143545     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (24)

References (89)
  • 2
    • 0000807647 scopus 로고
    • Myeloperoxidase of the leucocyte of normal human blood. I. Content and localization
    • Schultz J., Kaminker K. Myeloperoxidase of the leucocyte of normal human blood. I. Content and localization. Arch. Biochem. Biophys. 1962; 96: 465-467.
    • (1962) Arch. Biochem. Biophys. , Issue.96 , pp. 465-467
    • Schultz, J.1    Kaminker, K.2
  • 3
    • 0039106191 scopus 로고    scopus 로고
    • Neutrophil myeloperoxidase revisited: Its role in health and disease
    • Deby-Dupont G., Deby C., Lamy M. Neutrophil myeloperoxidase revisited: its role in health and disease. Intensivmed. 1999; 36: 500-513.
    • (1999) Intensivmed. , vol.36 , pp. 500-513
    • Deby-Dupont, G.1    Deby, C.2    Lamy, M.3
  • 4
  • 5
    • 0032558979 scopus 로고    scopus 로고
    • Reaction of myeloperoxidase compound i with chloride, bromide, iodide, and thiocyanate
    • Furtmüller P. G., Burner U., Obinger C. Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate. Biochemistry 1998; 37: 17923-17930.
    • (1998) Biochemistry , vol.37 , pp. 17923-17930
    • Furtmüller, P.G.1    Burner, U.2    Obinger, C.3
  • 6
    • 0034697020 scopus 로고    scopus 로고
    • X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution
    • Fiedler T. J., Davey C. A., Fenna R. E. X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution. J. Biol. Chem. 2000; 275: 11964-11971.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11964-11971
    • Fiedler, T.J.1    Davey, C.A.2    Fenna, R.E.3
  • 7
    • 0030915481 scopus 로고    scopus 로고
    • Myeloperoxidase: A key regulator of neutrophil oxidant production
    • Kettle A. J., Winterboum C. C. Myeloperoxidase: a key regulator of neutrophil oxidant production. Redox Report 1997; 3: 3-15.
    • (1997) Redox Report , vol.3 , pp. 3-15
    • Kettle, A.J.1    Winterboum, C.C.2
  • 8
    • 77950101814 scopus 로고    scopus 로고
    • Russian source
  • 9
    • 0034492989 scopus 로고    scopus 로고
    • Lactoperoxidase: Physico-chemical properties, occurrence, mechanism of action and applications
    • Kussendrager K D., van Hooijdonk A. C. Lactoperoxidase: physico-chemical properties, occurrence, mechanism of action and applications. Br. J. Nutr. 2000; 84 (suppl. 1): S19-S25.
    • (2000) Br. J. Nutr. , vol.84 , Issue.SUPPL. 1
    • Kussendrager, K.D.1    Van Hooijdonk, A.C.2
  • 10
    • 30544439048 scopus 로고    scopus 로고
    • Structural and functional aspects of peroxidase
    • Ruf J., Carayon P. Structural and functional aspects of peroxidase. Arch. Biochem. Biophys. 2006; 445: 269-277.
    • (2006) Arch. Biochem. Biophys. , vol.445 , pp. 269-277
    • Ruf, J.1    Carayon, P.2
  • 11
    • 77950182416 scopus 로고    scopus 로고
    • Russian source
  • 12
    • 77950100401 scopus 로고    scopus 로고
    • Russian source
  • 13
    • 33750564770 scopus 로고    scopus 로고
    • Reactions of myeloperoxidase-derived oxidants with biological substrates: Gaining chemical insight into human inflammatory diseases
    • Pattison D. I., Davies M. J. Reactions of myeloperoxidase-derived oxidants with biological substrates: gaining chemical insight into human inflammatory diseases. Cur. Med. Chem. 2006; 13: 3271-3290.
    • (2006) Cur. Med. Chem. , vol.13 , pp. 3271-3290
    • Pattison, D.I.1    Davies, M.J.2
  • 14
    • 33646826643 scopus 로고    scopus 로고
    • Modification of low-density lipoprotein by myeloperoxidase-derived oxidants and reagent hypochlorous acid
    • Malle E., Marsche G., Arnhold J., Davies M. J. Modification of low-density lipoprotein by myeloperoxidase-derived oxidants and reagent hypochlorous acid. Biochim. Biophys. Acta 2006; 1761: 392-415.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 392-415
    • Malle, E.1    Marsche, G.2    Arnhold, J.3    Davies, M.J.4
  • 15
    • 0003513861 scopus 로고
    • New York: McGraw-Hill Book Company Inc.
    • Selye H. The stress of life. New York: McGraw-Hill Book Company Inc.; 1957.
    • (1957) The Stress of Life
    • Selye, H.1
  • 16
    • 30544452572 scopus 로고    scopus 로고
    • Formation of reactive halide species by myeloperoxidase and eosinophil peroxidase
    • Spalteholz H., Panasenko O. M., Arnhold J. Formation of reactive halide species by myeloperoxidase and eosinophil peroxidase. Arch. Biochem. Biophys. 2006; 445: 225-234.
    • (2006) Arch. Biochem. Biophys. , vol.445 , pp. 225-234
    • Spalteholz, H.1    Panasenko, O.M.2    Arnhold, J.3
  • 17
    • 0002019504 scopus 로고    scopus 로고
    • Molecular chlorine generated by the myeloperoxidase-hydrogen peroxidechloride 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 peroxidechloride system of phagocytes converts low density lipoprotein cholesterol into a family of chlorinated sterols. J. Biol. Chem. 1996; 271: 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
  • 18
    • 0031571108 scopus 로고    scopus 로고
    • Oxidative modification and nitration of human low-density lipoproteins by the reaction of hypochlorous acid with nitrite
    • Panasenko O. M., Briviba K., Klotz L.-O., Sies H. Oxidative modification and nitration of human low-density lipoproteins by the reaction of hypochlorous acid with nitrite. Arch. Biochem. Biophys. 1997; 232: 254-259.
    • (1997) Arch. Biochem. Biophys. , vol.232 , pp. 254-259
    • Panasenko, O.M.1    Briviba, K.2    Klotz, L.-O.3    Sies, H.4
  • 19
    • 0028801505 scopus 로고
    • Oxidation of bromide by the human leukocyte enzymes myeloperoxidase and eosinophile peroxidase. Formation of bromamines
    • Thomas E. L., Bozeman P. M., Jefferson M. M., King C. C. Oxidation of bromide by the human leukocyte enzymes myeloperoxidase and eosinophile peroxidase. Formation of bromamines. J. Biol. Chem. 1995; 270: 2906-2913.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2906-2913
    • Thomas, E.L.1    Bozeman, P.M.2    Jefferson, M.M.3    King, C.C.4
  • 20
    • 30544453005 scopus 로고    scopus 로고
    • Bromination and chlorination reactions of myeloperoxidase at physiological concentrations of bromide and chloride
    • Senthilmohan R., Kettle A. J. Bromination and chlorination reactions of myeloperoxidase at physiological concentrations of bromide and chloride. Arch. Biochem. Biophys. 2006; 445: 235-244.
    • (2006) Arch. Biochem. Biophys. , vol.445 , pp. 235-244
    • Senthilmohan, R.1    Kettle, A.J.2
  • 21
    • 0001165950 scopus 로고
    • Atom-transfer redox kinetics: General-acid-assisted oxidation of iodide by chloramines and hypochlorite
    • Kumar K., Day R. A., Margerum D. W. Atom-transfer redox kinetics: general-acid-assisted oxidation of iodide by chloramines and hypochlorite. Inorg. Chem. 1986; 25: 4344-4350.
    • (1986) Inorg. Chem. , vol.25 , pp. 4344-4350
    • Kumar, K.1    Day, R.A.2    Margerum, D.W.3
  • 22
    • 0034687654 scopus 로고    scopus 로고
    • Spectral and kinetic studies on the formation of eosinophil peroxidase compound i and its reaction with halides and thiocyanate
    • Furtmüller P. G., Burner U., Regelsberger G., Obinger C. Spectral and kinetic studies on the formation of eosinophil peroxidase compound I and its reaction with halides and thiocyanate. Biochemistry 2000; 39: 15578-15584.
    • (2000) Biochemistry , vol.39 , pp. 15578-15584
    • Furtmüller, P.G.1    Burner, U.2    Regelsberger, G.3    Obinger, C.4
  • 23
    • 10144255096 scopus 로고    scopus 로고
    • Human neutrophils employ chlorine gas as an oxidant during phagocytosis
    • Hazen S. L., Hsu F. F., Mueller D. M. et al. Human neutrophils employ chlorine gas as an oxidant during phagocytosis. J. Clin. Invest. 1996; 98: 1283-1289.
    • (1996) J. Clin. Invest. , vol.98 , pp. 1283-1289
    • Hazen, S.L.1    Hsu, F.F.2    Mueller, D.M.3
  • 24
    • 0029760021 scopus 로고    scopus 로고
    • Formation of nitrating and chlorinating species by reaction of nutrite with hypochlorous acid. A novel mechanism for nitric oxide-mediated protein modification
    • Eiserich J. P., Cross C. E., Jones A. D. et al. Formation of nitrating and chlorinating species by reaction of nutrite with hypochlorous acid. A novel mechanism for nitric oxide-mediated protein modification. J. Biol. Chem. 1996; 271: 19199-19208.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19199-19208
    • Eiserich, J.P.1    Cross, C.E.2    Jones, A.D.3
  • 25
    • 27144432972 scopus 로고    scopus 로고
    • The role of reactive N-bromo species and radical intermediates in hypobromous acid-induced protein oxidation
    • Hawkins C. L., Davies M. J. The role of reactive N-bromo species and radical intermediates in hypobromous acid-induced protein oxidation. Free Radie. Biol. Med. 2005; 39: 900-912.
    • (2005) Free Radie. Biol. Med. , vol.39 , pp. 900-912
    • Hawkins, C.L.1    Davies, M.J.2
  • 26
    • 0034781061 scopus 로고    scopus 로고
    • Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds
    • Pattison D. I., Davies M. J. Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds. Chem. Res. Toxicol. 2001; 14: 1453-1464.
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 1453-1464
    • Pattison, D.I.1    Davies, M.J.2
  • 27
    • 0344410068 scopus 로고    scopus 로고
    • Hypochlorite-induced oxidation of amino acids, peptides and proteins
    • Hawkins C. L., Pattison D. I., Daves M. J. Hypochlorite-induced oxidation of amino acids, peptides and proteins. Amino Acids 2003; 25: 259-274.
    • (2003) Amino Acids , vol.25 , pp. 259-274
    • Hawkins, C.L.1    Pattison, D.I.2    Daves, M.J.3
  • 28
    • 1942502782 scopus 로고    scopus 로고
    • Kinetic analysis of the reactions of hypobromous acid with protein components: Implications for cellular damage and use of 3-bromotyrosine as a marker of oxidative stress
    • Pattison D. I., Davies M. J. Kinetic analysis of the reactions of hypobromous acid with protein components: implications for cellular damage and use of 3-bromotyrosine as a marker of oxidative stress. Biochemistry 2004; 43: 4799-4809.
    • (2004) Biochemistry , vol.43 , pp. 4799-4809
    • Pattison, D.I.1    Davies, M.J.2
  • 29
    • 0030874123 scopus 로고    scopus 로고
    • Hypochlorite-induced peroxidation of egg yolk phosphatidylcholine is mediated by hydroperoxides
    • Panasenko O. M., Arnhold J., Vladimirov Yu. A. et al. Hypochlorite-induced peroxidation of egg yolk phosphatidylcholine is mediated by hydroperoxides. Free Radie. Res. 1997; 27: 1-12.
    • (1997) Free Radie. Res. , vol.27 , pp. 1-12
    • Panasenko, O.M.1    Arnhold, J.2    Vladimirov Yu, A.3
  • 30
    • 77950110904 scopus 로고    scopus 로고
    • Russian source
  • 31
    • 0037371518 scopus 로고    scopus 로고
    • Myeloperoxidase-induced formation of chlorohydrins and lysophospholipids from unsaturated phosphatidylcholines
    • Panasenko O. M., Spalteholz H., Schiller J., Arnhold J. Myeloperoxidase-induced formation of chlorohydrins and lysophospholipids from unsaturated phosphatidylcholines. Free Radic. Biol. Med. 2003; 34: 553-562.
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 553-562
    • Panasenko, O.M.1    Spalteholz, H.2    Schiller, J.3    Arnhold, J.4
  • 32
    • 77950138725 scopus 로고    scopus 로고
    • Russian source
  • 33
    • 77950186161 scopus 로고    scopus 로고
    • Russian source
  • 34
    • 77950173152 scopus 로고    scopus 로고
    • Russian source
  • 35
    • 0032519779 scopus 로고    scopus 로고
    • Comparison of human red cell lysis by hypochlorous and hypobromous acids: Insights into the mechanism of lysis
    • Vissers M. C., CarrA. C., Chapman A. L. Comparison of human red cell lysis by hypochlorous and hypobromous acids: insights into the mechanism of lysis. Biochem. J. 1998; 330: 131-138.
    • (1998) Biochem. J. , vol.330 , pp. 131-138
    • Vissers, M.C.1    Carra, C.2    Chapman, A.L.3
  • 36
    • 34447630487 scopus 로고    scopus 로고
    • Influence of chloride on modification of unsaturated phosphatidylcholines by the myeloperoxidase/hydrogen peroxide/bromide system
    • Panasenko O. M., Vakhrusheva T., Tretyakov Vet al. Influence of chloride on modification of unsaturated phosphatidylcholines by the myeloperoxidase/ hydrogen peroxide/bromide system. Chem. Phys. Lipids 2007; 149: 40-51.
    • (2007) Chem. Phys. Lipids , vol.149 , pp. 40-51
    • Panasenko, O.M.1    Vakhrusheva, T.2    Tretyakov, V.3
  • 37
    • 77950125862 scopus 로고    scopus 로고
    • Russian source
  • 38
    • 0028792292 scopus 로고
    • The action of hypochlorous acid on phosphatidylcholine liposomes in dependence on the content of double bonds. Stoichiometry and NMR analysis
    • Arnhold J., Panasenko O. M., Schiller J. et al. The action of hypochlorous acid on phosphatidylcholine liposomes in dependence on the content of double bonds. Stoichiometry and NMR analysis. Chem. Phys. Lipids 1995; 78: 55-64.
    • (1995) Chem. Phys. Lipids , vol.78 , pp. 55-64
    • Arnhold, J.1    Panasenko, O.M.2    Schiller, J.3
  • 39
    • 0037104667 scopus 로고    scopus 로고
    • Formation of lysophospholipids from unsaturated phosphatidylcholines under the influence of hypochlorous acid
    • Arnhold J., Osipov A. N., Spalteholz H. et al. Formation of lysophospholipids from unsaturated phosphatidylcholines under the influence of hypochlorous acid. Biochim. Biophys. Acta 2002; 1572: 91-100.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 91-100
    • Arnhold, J.1    Osipov, A.N.2    Spalteholz, H.3
  • 40
    • 0035501107 scopus 로고    scopus 로고
    • Effects of hypochlorous acid on unsaturated phosphatidylcholines
    • Arnhold J., Osipov A. N., Spalteholz H. et al. Effects of hypochlorous acid on unsaturated phosphatidylcholines. Free Radie. Biol. Med. 2001; 31: 1111-1119.
    • (2001) Free Radie. Biol. Med. , vol.31 , pp. 1111-1119
    • Arnhold, J.1    Osipov, A.N.2    Spalteholz, H.3
  • 41
    • 33751584261 scopus 로고    scopus 로고
    • Hypochlorous acid-derived modification of phospholipids: Characterization of aminophospholipids as regulatory molecules for lipid peroxidation
    • Kawai Y., Kiyokawa H., Kimura Y. et al. Hypochlorous acid-derived modification of phospholipids: characterization of aminophospholipids as regulatory molecules for lipid peroxidation. Biochemistry 2006; 45: 14201-14211.
    • (2006) Biochemistry , vol.45 , pp. 14201-14211
    • Kawai, Y.1    Kiyokawa, H.2    Kimura, Y.3
  • 43
    • 77950178199 scopus 로고    scopus 로고
    • Russian source
  • 44
    • 77950170945 scopus 로고    scopus 로고
    • Russian source
  • 46
    • 0029077907 scopus 로고
    • Hypochlorite induces lipid peroxidation in blood lipoproteins and phospholipid liposomes
    • Panasenko O. M., Evgina S. A., Driomina E. S. et al. Hypochlorite induces lipid peroxidation in blood lipoproteins and phospholipid liposomes. Free Radic. Biol. Med. 1995; 19: 133-140.
    • (1995) Free Radic. Biol. Med. , vol.19 , pp. 133-140
    • Panasenko, O.M.1    Evgina, S.A.2    Driomina, E.S.3
  • 47
    • 77950119238 scopus 로고    scopus 로고
    • Russian source
  • 48
    • 0030693191 scopus 로고    scopus 로고
    • The mechanism of the hypochlorite-induced lipid peroxidation
    • Panasenko O. M. The mechanism of the hypochlorite-induced lipid peroxidation. BioFactors 1997; 6: 181-190.
    • (1997) BioFactors , vol.6 , pp. 181-190
    • Panasenko, O.M.1
  • 49
    • 0032773379 scopus 로고    scopus 로고
    • Linoleic acid hydroperoxide favours hypochlorite- and myeloperoxidase-induced lipid peroxidation
    • Panasenko O. M., Arnhold J. Linoleic acid hydroperoxide favours hypochlorite- and myeloperoxidase-induced lipid peroxidation. Free Radie. Res. 1999; 30: 479-487.
    • (1999) Free Radie. Res. , vol.30 , pp. 479-487
    • Panasenko, O.M.1    Arnhold, J.2
  • 50
    • 77950177276 scopus 로고    scopus 로고
    • Russian source
  • 51
    • 77950174960 scopus 로고    scopus 로고
    • Russian source
  • 52
    • 0035990525 scopus 로고    scopus 로고
    • Interaction of tert-butyl hydroperoxide with hypochlorous acid. A spin trappirg and chemiluminescence study
    • Osipov A. N., Panasenko O. M., Chekanov A. V., Arnhold J. Interaction of tert-butyl hydroperoxide with hypochlorous acid. A spin trappirg and chemiluminescence study. Free Radic. Res. 2002; 36: 749-754.
    • (2002) Free Radic. Res. , vol.36 , pp. 749-754
    • Osipov, A.N.1    Panasenko, O.M.2    Chekanov, A.V.3    Arnhold, J.4
  • 53
    • 77950115491 scopus 로고    scopus 로고
    • Russian source
  • 54
    • 77950134973 scopus 로고    scopus 로고
    • Russian source
  • 55
    • 77950103130 scopus 로고    scopus 로고
    • Russian source
  • 56
    • 77950118179 scopus 로고    scopus 로고
    • Russian source
  • 57
    • 77950154301 scopus 로고    scopus 로고
    • Russian source
  • 58
    • 77950156816 scopus 로고    scopus 로고
    • Russian source
  • 59
    • 0242407243 scopus 로고    scopus 로고
    • Hypochlorite-mediated fragmentation of hyaluronan, chondroitin sulfates, and related N-acetyl glycosamines: Evidence for chloramide intermediates, free radical transfer reactions, and site-specific fragmentation
    • Rees M. D., Hawkins C. L., Davies M. J. Hypochlorite-mediated fragmentation of hyaluronan, chondroitin sulfates, and related N-acetyl glycosamines: evidence for chloramide intermediates, free radical transfer reactions, and site-specific fragmentation. J. Am. Chem. Soc. 2003; 125: 13719-13733.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13719-13733
    • Rees, M.D.1    Hawkins, C.L.2    Davies, M.J.3
  • 60
    • 33846531190 scopus 로고    scopus 로고
    • Degradation of extracellular matrix and its components by hypobromous acid
    • Rees M. D., Mcniven T. N., Davies M. J. Degradation of extracellular matrix and its components by hypobromous acid. Biochem. J. 2007; 401: 587-596.
    • (2007) Biochem. J. , vol.401 , pp. 587-596
    • Rees, M.D.1    Mcniven, T.N.2    Davies, M.J.3
  • 61
    • 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. 1996; 332: 110-120.
    • (1996) Arch. Biochem. Biophys. , vol.332 , pp. 110-120
    • Prutz, W.A.1
  • 62
    • 0034861165 scopus 로고    scopus 로고
    • Hypochlorite-induced damage to nucleosides: Formation of chloramines and nitrogen-centered radicals
    • Hawkins C. L., Davies M. J. Hypochlorite-induced damage to nucleosides: formation of chloramines and nitrogen-centered radicals. Chem. Res. Toxicol. 2001; 14: 1071-1081.
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 1071-1081
    • Hawkins, C.L.1    Davies, M.J.2
  • 63
    • 0036151383 scopus 로고    scopus 로고
    • Hypochlorite-induced damage to DNA, RNA, and polynucleotides: Formation of chloramines and nitrogen-centered radicals
    • Hawkins C. L., Davies M. J. Hypochlorite-induced damage to DNA, RNA, and polynucleotides: formation of chloramines and nitrogen-centered radicals. Chem. Res. Toxicol. 2002; 15: 83-92.
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 83-92
    • Hawkins, C.L.1    Davies, M.J.2
  • 64
    • 0030894162 scopus 로고    scopus 로고
    • Oxidative stress: Oxidants and antioxidants
    • Sies H. Oxidative stress: oxidants and antioxidants. Exp. Physiol. 1997; 82 (2): 291-295.
    • (1997) Exp. Physiol. , vol.82 , Issue.2 , pp. 291-295
    • Sies, H.1
  • 65
    • 0036268224 scopus 로고    scopus 로고
    • Hypothesis: Proteasomal dysfunction: a primary event in neurogeneration that leads to nitrative and oxidative stress and subsequent cell death
    • Halliwell B. Hypothesis: proteasomal dysfunction: a primary event in neurogeneration that leads to nitrative and oxidative stress and subsequent cell death. Ann. N. Y. Acad. Sci. 2002; 962: 182-194.
    • (2002) Ann. N. Y. Acad. Sci. , vol.962 , pp. 182-194
    • Halliwell, B.1
  • 66
    • 77950155661 scopus 로고    scopus 로고
    • Russian source
  • 67
    • 0021352686 scopus 로고
    • Singlet oxygen production by chloroperoxidasehydrogen peroxide-halide systems
    • Kanofsky J. R. Singlet oxygen production by chloroperoxidasehydrogen peroxide-halide systems. J. Biol. Chem. 1984; 259: 5596-5600.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5596-5600
    • Kanofsky, J.R.1
  • 68
    • 0026524163 scopus 로고
    • Priming of human neutrophil functions by tumor necrosis factor: Enhancement of superoxide anion generation, degranulation, and Chemotaxis to chemoattractants C5a and F-Met-Leu-Phe
    • Bajaj M. S., Kew R. R., Webster R. O., Hyers T. M. Priming of human neutrophil functions by tumor necrosis factor: enhancement of superoxide anion generation, degranulation, and Chemotaxis to chemoattractants C5a and F-Met-Leu-Phe. Inflammation 1992; 16: 241-250.
    • (1992) Inflammation , vol.16 , pp. 241-250
    • Bajaj, M.S.1    Kew, R.R.2    Webster, R.O.3    Hyers, T.M.4
  • 69
    • 15244343080 scopus 로고    scopus 로고
    • Rapid non-genomic inhibitory effects of glucocorticoids on human neutrophil degranulation
    • Liu L., Wang Y. X., Zhou J. et al. Rapid non-genomic inhibitory effects of glucocorticoids on human neutrophil degranulation. Inflamm. Res. 2005; 54: 37-41.
    • (2005) Inflamm. Res. , vol.54 , pp. 37-41
    • Liu, L.1    Wang, Y.X.2    Zhou, J.3
  • 70
    • 0027402353 scopus 로고
    • Crystal-induced protein tyrosine phosphorylation in neutrophils and the effect of a tyrosine kinase inhibitor on neutrophil responses
    • Burt H. M., Jackson J. K, Dryden P., Salari H. Crystal-induced protein tyrosine phosphorylation in neutrophils and the effect of a tyrosine kinase inhibitor on neutrophil responses. Mol. Pharmacol. 1993; 43: 30-36.
    • (1993) Mol. Pharmacol. , vol.43 , pp. 30-36
    • Burt, H.M.1    Jackson, J.K.2    Dryden, P.3    Salari, H.4
  • 71
    • 0032213207 scopus 로고    scopus 로고
    • Effect of serum amyloid A on selected in vitro functions of isolated human neutrophils
    • Gatt M. E., Urieli-Shoval S., Preciado-Patt L. et al. Effect of serum amyloid A on selected in vitro functions of isolated human neutrophils. J. Lab. Clin. Med. 1998; 132: 414-420.
    • (1998) J. Lab. Clin. Med. , vol.132 , pp. 414-420
    • Gatt, M.E.1    Urieli-Shoval, S.2    Preciado-Patt, L.3
  • 72
    • 57649201397 scopus 로고    scopus 로고
    • Ceruloplasmin and myeloperoxidase in complex affect the enzymatic properties of each other
    • Sokolov A. V., Ageeva K V., Pulina M. O. et al. Ceruloplasmin and myeloperoxidase in complex affect the enzymatic properties of each other. Free Radic. Res. 2008; 42: 989-998.
    • (2008) Free Radic. Res. , vol.42 , pp. 989-998
    • Sokolov, A.V.1    Ageeva, K.V.2    Pulina, M.O.3
  • 73
    • 77950143310 scopus 로고    scopus 로고
    • Russian source
  • 74
    • 0036478818 scopus 로고    scopus 로고
    • Redox intermediates of plant and mammalian peroxidase: A comparative transient-kinetic of their reactivity toward indole derivatives
    • Jantschko W., Furtmüller P. G., Allegro M. et al. Redox intermediates of plant and mammalian peroxidase: a comparative transient-kinetic of their reactivity toward indole derivatives. Arch. Biochem. Biophys. 2002; 398: 12-22.
    • (2002) Arch. Biochem. Biophys. , vol.398 , pp. 12-22
    • Jantschko, W.1    Furtmüller, P.G.2    Allegro, M.3
  • 75
    • 41149090064 scopus 로고    scopus 로고
    • Potential role of tryptophan and chloride in the inhibition of human myeloperoxidase
    • Galijasevic S., Abdulhamid I., Abu-Soud H. M. Potential role of tryptophan and chloride in the inhibition of human myeloperoxidase. Free Radic. Biol. Med. 2008; 44: 1570-1577.
    • (2008) Free Radic. Biol. Med. , Issue.44 , pp. 1570-1577
    • Galijasevic, S.1    Abdulhamid, I.2    Abu-Soud, H.M.3
  • 76
    • 77950187077 scopus 로고    scopus 로고
    • Russian source
  • 78
    • 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. 1997; 99: 2075-2081.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2075-2081
    • Hazen, S.L.1    Heinecke, J.W.2
  • 79
    • 4744374195 scopus 로고    scopus 로고
    • NMR analysis of neutrophil activation in sputum samples from patients with cystic fibrosis
    • Saude E. J., Lacy P., Musat-Marcu S. et al. NMR analysis of neutrophil activation in sputum samples from patients with cystic fibrosis. Magn. Reson. Med. 2004; 52: 807-814.
    • (2004) Magn. Reson. Med. , vol.52 , pp. 807-814
    • Saude, E.J.1    Lacy, P.2    Musat-Marcu, S.3
  • 80
    • 9644290855 scopus 로고    scopus 로고
    • Urinary eicosanoid and tyrosine derivative concentrations in patients with vasculitides
    • Higashi N., Mita H., Taniguchl M. et al. Urinary eicosanoid and tyrosine derivative concentrations in patients with vasculitides. J. Allergy Clin. Immunol. 2004; 114: 1353-1358.
    • (2004) J. Allergy Clin. Immunol. , vol.114 , pp. 1353-1358
    • Higashi, N.1    Mita, H.2    Taniguchl, M.3
  • 82
    • 3042675247 scopus 로고    scopus 로고
    • Urinary 3-bromotyrosine and 3-chlorotysine concentrations in asthmatic patients: Lack of increase in 3-bromotyrosine concentration in urine and plasma proteins in aspirin-induced asthma after intravenous aspirin challenge
    • Mita H., Higashi N., Taniguchi M. et al. Urinary 3-bromotyrosine and 3-chlorotysine concentrations in asthmatic patients: lack of increase in 3-bromotyrosine concentration in urine and plasma proteins in aspirin-induced asthma after intravenous aspirin challenge. Clin. Exp. Allergy, 2004; 34: 931-938.
    • (2004) Clin. Exp. Allergy , vol.34 , pp. 931-938
    • Mita, H.1    Higashi, N.2    Taniguchi, M.3
  • 83
    • 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. et al. 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. 1999; 27: 1738-1744.
    • (1999) Crit. Care Med. , vol.27 , pp. 1738-1744
    • Lamb, N.J.1    Gutteridge, J.M.2    Baker, C.3
  • 84
    • 0037372157 scopus 로고    scopus 로고
    • 3-Chlorotyrosine as a marker of protein damage by myeloperoxidase in tracheal aspirates from preterm infants: Association with adverse respiratory outcome
    • Buss I. H., Senthilmohan R., Darlow B. A. et al. 3-Chlorotyrosine as a marker of protein damage by myeloperoxidase in tracheal aspirates from preterm infants: association with adverse respiratory outcome. Pediatr. Res. 2003; 53: 455-462.
    • (2003) Pediatr. Res. , vol.53 , pp. 455-462
    • Buss, I.H.1    Senthilmohan, R.2    Darlow, B.A.3
  • 85
    • 0029932445 scopus 로고    scopus 로고
    • Presence of hypochlorite-modified proteins in human atherosclerotic lesions
    • Hazell L. J., Arnold L., Flowers D. et al. Presence of hypochlorite-modified proteins in human atherosclerotic lesions. J. Clin. Invest. 1996; 97: 1535-1544.
    • (1996) J. Clin. Invest. , vol.97 , pp. 1535-1544
    • Hazell, L.J.1    Arnold, L.2    Flowers, D.3
  • 86
    • 0031024294 scopus 로고    scopus 로고
    • Immunological evidence for hypochloritemodified proteins in human kidney
    • Malle E., Woenckhaus C., Waeg G. et al. Immunological evidence for hypochloritemodified proteins in human kidney. Am. J. Pathol. 1997; 150: 603-615.
    • (1997) Am. J. Pathol. , vol.150 , pp. 603-615
    • Malle, E.1    Woenckhaus, C.2    Waeg, G.3
  • 87
    • 41149106758 scopus 로고    scopus 로고
    • Identification of lysophosphatidylcholine-chlorohydrin in human atherosclerotic lesions
    • Messner M. C., Albert C. J., McHowat J., Ford D. A. Identification of lysophosphatidylcholine-chlorohydrin in human atherosclerotic lesions. Lipids 2008; 43: 243-249.
    • (2008) Lipids , vol.43 , pp. 243-249
    • Messner, M.C.1    Albert, C.J.2    McHowat, J.3    Ford, D.A.4
  • 88
    • 0348049466 scopus 로고    scopus 로고
    • Identification of alpha-chloro fatty aldehydes and unsaturated lyphosphatidylcholine molecular species in human atherosclerotic lesions
    • Thukkanl A. K., McHowat J., Hsu F. F. et al. Identification of alpha-chloro fatty aldehydes and unsaturated lyphosphatidylcholine molecular species in human atherosclerotic lesions. Circulation 2003; 108: 3128-3133.
    • (2003) Circulation , vol.108 , pp. 3128-3133
    • Thukkanl, A.K.1    McHowat, J.2    Hsu, F.F.3
  • 89
    • 33645638306 scopus 로고    scopus 로고
    • Myeloperoxidase generates 5-chlorouracil in human atherosclerotic tissue
    • Takeshlta J., Byun J., Nhan T. Q. et al. Myeloperoxidase generates 5-chlorouracil in human atherosclerotic tissue. J. Biol. Chem. 2006; 281: 3096-3104.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3096-3104
    • Takeshlta, J.1    Byun, J.2    Nhan, T.Q.3


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