메뉴 건너뛰기




Volumn 369, Issue 1-2, 2011, Pages 141-145

Detection of 3-chlorinated tyrosine residues in human cells by flow cytometry

Author keywords

3 chlorotyrosine; Antibody; Flow cytometry; Hypochlorite

Indexed keywords

3 CHLOROTYROSINE; 3 CHLOROTYROSINE ANTIBODY; ANTIBODY; CHLORINE; CHLOROHYDRIN DERIVATIVE; FLUORESCEIN ISOTHIOCYANATE; HYPOCHLORITE; IMMUNOGLOBULIN G; UNCLASSIFIED DRUG;

EID: 79958808950     PISSN: 00221759     EISSN: 18727905     Source Type: Journal    
DOI: 10.1016/j.jim.2011.05.006     Document Type: Article
Times cited : (9)

References (22)
  • 1
    • 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 1999, 301:151.
    • (1999) Methods Enzymol , vol.301 , pp. 151
    • Crow, J.P.1
  • 2
    • 0024232736 scopus 로고
    • Oxidation of proteins in rat heart and lungs by polymorphonuclear leukocyte oxidants
    • Fliss H. Oxidation of proteins in rat heart and lungs by polymorphonuclear leukocyte oxidants. Mol. Cell. Biochem. 1988, 84:177.
    • (1988) Mol. Cell. Biochem. , vol.84 , pp. 177
    • Fliss, H.1
  • 3
    • 79551607386 scopus 로고    scopus 로고
    • Hypertonic saline increases lung epithelial lining fluid glutathione and thiocyanate: two protective CFTR-dependent thiols against oxidative injury
    • Gould N.S., Gauthier S., Kariya C.T., Min E., Huang J., Brian D.J. Hypertonic saline increases lung epithelial lining fluid glutathione and thiocyanate: two protective CFTR-dependent thiols against oxidative injury. Respir. Res. 2010, 11:119.
    • (2010) Respir. Res. , vol.11 , pp. 119
    • Gould, N.S.1    Gauthier, S.2    Kariya, C.T.3    Min, E.4    Huang, J.5    Brian, D.J.6
  • 4
    • 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., Heinecke J. 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.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2075
    • Hazen, S.1    Heinecke, J.2
  • 5
    • 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. 1997, 23:909.
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 909
    • Hazen, S.L.1    Crowley, J.R.2    Mueller, D.M.3    Heinecke, J.W.4
  • 6
    • 0036203395 scopus 로고    scopus 로고
    • Rapid assessment of the physiological status of the polychlorinated biphenyl degrader Comamonas testosteroni TK102 by flow cytometry
    • Hiraoka Y., Kimbara K. Rapid assessment of the physiological status of the polychlorinated biphenyl degrader Comamonas testosteroni TK102 by flow cytometry. Appl. Environ. Microbiol. 2002, 68:2031.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 2031
    • Hiraoka, Y.1    Kimbara, K.2
  • 7
    • 0028233559 scopus 로고
    • Assays for the chlorination activity of myeloperoxidase
    • Kettle A.J., Winterbourn C.C. Assays for the chlorination activity of myeloperoxidase. Methods Enzymol 1994, 233:502.
    • (1994) Methods Enzymol , vol.233 , pp. 502
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 9
    • 8544251150 scopus 로고    scopus 로고
    • The acid ionization constant of HOCl from 5° to 35°
    • Morris J. The acid ionization constant of HOCl from 5° to 35°. J. Phys. Chem. 1996, 70:3798.
    • (1996) J. Phys. Chem. , vol.70 , pp. 3798
    • Morris, J.1
  • 10
    • 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.
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 1453
    • Pattison, D.I.1    Davies, M.J.2
  • 11
    • 18544368511 scopus 로고    scopus 로고
    • Kinetic analysis of the role of histidine chloramines in hypochlorous acid mediated protein oxidation
    • Pattison D.I., Davies M.J. Kinetic analysis of the role of histidine chloramines in hypochlorous acid mediated protein oxidation. Biochemistry 2005, 44:7378.
    • (2005) Biochemistry , vol.44 , pp. 7378
    • Pattison, D.I.1    Davies, M.J.2
  • 12
    • 33745629631 scopus 로고    scopus 로고
    • Evidence for rapid inter- and intramolecular chlorine transfer reactions of histamine and carnosine chloramines: implications for the prevention of hypochlorous-acid-mediated damage
    • Pattison D.I., Davies M.J. Evidence for rapid inter- and intramolecular chlorine transfer reactions of histamine and carnosine chloramines: implications for the prevention of hypochlorous-acid-mediated damage. Biochemistry 2006, 45:8152.
    • (2006) Biochemistry , vol.45 , pp. 8152
    • Pattison, D.I.1    Davies, M.J.2
  • 13
    • 5344271785 scopus 로고    scopus 로고
    • Chlorine transfer between glycine, taurine, and histamine: reaction rates and impact on cellular reactivity
    • Peskin A.V., Midwinter R.G., Harwood D.T., Winterbourn C.C. Chlorine transfer between glycine, taurine, and histamine: reaction rates and impact on cellular reactivity. Free Radic. Biol. Med. 2004, 37:1622.
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 1622
    • Peskin, A.V.1    Midwinter, R.G.2    Harwood, D.T.3    Winterbourn, C.C.4
  • 14
    • 0034457129 scopus 로고    scopus 로고
    • Living with a killer: the effects of hypochlorous acid on mammalian cells
    • Pullar J.M., Vissers M.C., Winterbourn C.C. Living with a killer: the effects of hypochlorous acid on mammalian cells. IUBMB Life 2000, 50:259.
    • (2000) IUBMB Life , vol.50 , pp. 259
    • Pullar, J.M.1    Vissers, M.C.2    Winterbourn, C.C.3
  • 15
    • 54249090219 scopus 로고    scopus 로고
    • N-chloroamino acids cause oxidative protein modifications in the erythrocyte membrane
    • Robaszkiewicz A., Bartosz G., Soszynski M. N-chloroamino acids cause oxidative protein modifications in the erythrocyte membrane. Mech. Ageing. Dev. 2008, 129:572.
    • (2008) Mech. Ageing. Dev. , vol.129 , pp. 572
    • Robaszkiewicz, A.1    Bartosz, G.2    Soszynski, M.3
  • 17
    • 77955403185 scopus 로고    scopus 로고
    • Ability of hypochlorous acid and N-chloramines to chlorinate DNA and its constituents
    • Stanley N.R., Pattison D.I., Hawkins C.L. Ability of hypochlorous acid and N-chloramines to chlorinate DNA and its constituents. Chem. Res. Toxicol. 2010, 23:1293.
    • (2010) Chem. Res. Toxicol. , vol.23 , pp. 1293
    • Stanley, N.R.1    Pattison, D.I.2    Hawkins, C.L.3
  • 18
    • 0019304939 scopus 로고
    • Colorimetric determination of phospholipids with ammonium ferrothiocyanate
    • Stewart J.C. Colorimetric determination of phospholipids with ammonium ferrothiocyanate. Anal. Biochem. 1980, 104:10.
    • (1980) Anal. Biochem. , vol.104 , pp. 10
    • Stewart, J.C.1
  • 19
    • 0022928045 scopus 로고
    • Preparation and characterization of chloramines
    • Thomas E., Grisham M., Jefferson M. Preparation and characterization of chloramines. Methods Enzymol. 1986, 132:569.
    • (1986) Methods Enzymol. , vol.132 , pp. 569
    • Thomas, E.1    Grisham, M.2    Jefferson, M.3
  • 20
    • 73449143528 scopus 로고    scopus 로고
    • Myeloperoxidase: molecular mechanisms of action and their relevance to human health and disease
    • van der Veen B.S., de Winther M.P., Heeringa P. Myeloperoxidase: molecular mechanisms of action and their relevance to human health and disease. Antioxid. Redox. Signal 2009, 11:2899.
    • (2009) Antioxid. Redox. Signal , vol.11 , pp. 2899
    • van der Veen, B.S.1    de Winther, M.P.2    Heeringa, P.3
  • 21
    • 42949147076 scopus 로고    scopus 로고
    • Loss of 3-chlorotyrosine by inflammatory oxidants: implications for the use of 3-chlorotyrosine as a bio-marker in vivo
    • Whiteman M., Spencer J.P. Loss of 3-chlorotyrosine by inflammatory oxidants: implications for the use of 3-chlorotyrosine as a bio-marker in vivo. Biochem. Biophys. Res. Commun. 2008, 371:50.
    • (2008) Biochem. Biophys. Res. Commun. , vol.371 , pp. 50
    • Whiteman, M.1    Spencer, J.P.2
  • 22
    • 0034282230 scopus 로고    scopus 로고
    • Biomarkers of myeloperoxidase-derived hypochlorous acid
    • Winterbourn C.C., Kettle A.J. Biomarkers of myeloperoxidase-derived hypochlorous acid. Free Radic. Biol. Med. 2000, 29:403.
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 403
    • Winterbourn, C.C.1    Kettle, A.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.