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Volumn 40, Issue 4, 1999, Pages 686-698

Selective modification of apoB-100 in the oxidation of low density lipoproteins by myeloperoxidase in vitro

Author keywords

2,4 dinitrophenylhydrazine; ApoB 100; HOCl, hypochlorous acid; LDL, low density lipoproteins; Myeloperoxidase; Oxidized LDL peptides

Indexed keywords

2,4 DINITROPHENYLHYDRAZINE; APOLIPOPROTEIN B100; HYPOCHLOROUS ACID; LOW DENSITY LIPOPROTEIN; MYELOPEROXIDASE; SULFINIC ACID DERIVATIVE;

EID: 0345148809     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (69)

References (37)
  • 1
    • 0024603895 scopus 로고
    • Beyond cholesterol. Modifications of low density lipoprotein that increase its atherogenicity
    • Steinberg, D., S. Parthasarathy, T. E. Carew, J. C. Khoo, and J. L. Witzum. 1989. Beyond cholesterol. Modifications of low density lipoprotein that increase its atherogenicity. N. Engl. J. Med. 320: 915-924.
    • (1989) N. Engl. J. Med. , vol.320 , pp. 915-924
    • Steinberg, D.1    Parthasarathy, S.2    Carew, T.E.3    Khoo, J.C.4    Witzum, J.L.5
  • 3
    • 0028556264 scopus 로고
    • Lipoprotein oxidation: Mechanistic aspects, methodological approaches and clinical relevance
    • Stocker, R. 1994. Lipoprotein oxidation: mechanistic aspects, methodological approaches and clinical relevance. Curr. Opin. Lipidol. 5: 422-433.
    • (1994) Curr. Opin. Lipidol. , vol.5 , pp. 422-433
    • Stocker, R.1
  • 5
    • 0031010333 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman, E. R., and B. S. Berlett. 1997. Reactive oxygen-mediated protein oxidation in aging and disease. Chem. Res. Toxicol. 10: 485-494.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 485-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 6
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean, R. T., S. Fu, R. Stocker, and M. J. Davies. 1997. Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 324: 1-18.
    • (1997) Biochem. J. , vol.324 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 7
    • 0028292033 scopus 로고
    • Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions
    • Daugherty, A., J. L. Dunn, D. L. Rateri, and J. W. Heinecke. 1994. Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions. J. Clin. Invest. 94: 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
  • 8
    • 0029932445 scopus 로고    scopus 로고
    • Presence of hypochlorite-modified proteins in human atherosclerotic lesions
    • Hazell, L. J., L. Arnold, D. Flowers, G. Waeg, E. Malle, and R. Stocker. 1996. Presence of hypochlorite-modified proteins in human atherosclerotic lesions. J. Clin. Invest. 97: 1535-1544.
    • (1996) J. Clin. Invest. , vol.97 , pp. 1535-1544
    • Hazell, L.J.1    Arnold, L.2    Flowers, D.3    Waeg, G.4    Malle, E.5    Stocker, R.6
  • 9
    • 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 R. Stocker. 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
  • 10
    • 0028030788 scopus 로고
    • Oxidation of low-density lipoprotein by hypochlorite causes aggregation that is mediated by modification of lysine residues rather than lipid oxidation
    • Hazell, L. J., J. J. M. van den Berg, and R. Stocker. 1994. Oxidation of low-density lipoprotein by hypochlorite causes aggregation that is mediated by modification of lysine residues rather than lipid oxidation. Biochem. J. 302: 297-304.
    • (1994) Biochem. J. , vol.302 , pp. 297-304
    • Hazell, L.J.1    Van Den Berg, J.J.M.2    Stocker, R.3
  • 11
    • 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., and J. W. Heinecke. 1997. 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: 2075-2081.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2075-2081
    • Hazen, S.L.1    Heinecke, J.W.2
  • 12
    • 0030950291 scopus 로고    scopus 로고
    • Oxidative modifications of apoB-100 by exposure of low density lipoproteins to HOCl in vitro
    • Yang, C-Y., Z-W. Gu, H-X. Yang, A. M. Gotto, Jr., and C. V. Smith. 1997. Oxidative modifications of apoB-100 by exposure of low density lipoproteins to HOCl in vitro. Free Radical Biol. Med. 23: 82-89.
    • (1997) Free Radical Biol. Med. , vol.23 , pp. 82-89
    • Yang, C.-Y.1    Gu, Z.-W.2    Yang, H.-X.3    Gotto A.M., Jr.4    Smith, C.V.5
  • 13
    • 0001926444 scopus 로고
    • Solid phase peptide synthesis
    • E. Gross and J. Meienhofer, editors. Academic Press, New York
    • Barany, G., and R. B. Merrifield. 1980. Solid phase peptide synthesis. In The Peptides: Analysis, Synthesis, Biology. E. Gross and J. Meienhofer, editors. Academic Press, New York. 3-284.
    • (1980) The Peptides: Analysis, Synthesis, Biology , pp. 3-284
    • Barany, G.1    Merrifield, R.B.2
  • 14
    • 0027367640 scopus 로고
    • A high-performance liquid chromatographic assay for reduced and oxidized glutathione in biological samples
    • Jayatilleke, E., and S. Shaw. 1993. A high-performance liquid chromatographic assay for reduced and oxidized glutathione in biological samples. Anal. Biochem. 214: 452-157.
    • (1993) Anal. Biochem. , vol.214 , pp. 452-1157
    • Jayatilleke, E.1    Shaw, S.2
  • 15
    • 0000998052 scopus 로고
    • Some derivatives of glutathione
    • Calam, D. H., and S. G. Waley. 1962. Some derivatives of glutathione. Biochem. J. 85: 417-419.
    • (1962) Biochem. J. , vol.85 , pp. 417-419
    • Calam, D.H.1    Waley, S.G.2
  • 17
    • 0028365058 scopus 로고
    • Aromatic substrate molecules hind at the distal heme pocket of myeloperoxidase
    • Hori, H., R. E. Fenna, S. Kimura, and M. Ikeda-Saito. 1994. Aromatic substrate molecules hind 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    Ikeda-Saito, M.4
  • 18
    • 0025074449 scopus 로고
    • Isolation and characterization of sulfhydryl and disulfide peptides of human apoB-100
    • Yang, C. Y. T. W. Kim, S. A. Weng, B. Lee, M. Yang, and A. M. Gotto, Jr. 1990. Isolation and characterization of sulfhydryl and disulfide peptides of human apoB-100. Proc. Natl. Acad. Sci. USA. 87: 5523-5527.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5523-5527
    • Yang, C.Y.1    Kim, T.W.2    Weng, S.A.3    Lee, B.4    Yang, M.5    Gotto A.M., Jr.6
  • 19
    • 0028245251 scopus 로고
    • Chlorination of taurine by myeloperoxidase
    • Marquez, L. A., and H. B. Dunford. 1994. Chlorination of taurine by myeloperoxidase. J. Biol. Chem. 269: 7950-7956.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7950-7956
    • Marquez, L.A.1    Dunford, H.B.2
  • 20
    • 0029786641 scopus 로고    scopus 로고
    • Quantitating direct chlorine transfer from the enzyme to substrate in chloroperoxidase-catalyzed reactions
    • Libby, R. D., T. M. Beachy, and A. K. Phipps. 1996. Quantitating direct chlorine transfer from the enzyme to substrate in chloroperoxidase-catalyzed reactions. J. Biol. Chem. 271: 21820-21827.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21820-21827
    • Libby, R.D.1    Beachy, T.M.2    Phipps, A.K.3
  • 22
    • 0019470352 scopus 로고
    • Tumor cell anti-oxidant defenses. Inhibition of the glutathione redox cycle enhances macrophage-mediated cytolysis
    • Nathan, C. F., B. A. Arrick, H. W. Murray, N. M. DeSantis, and Z. A. Cohn. 1980. Tumor cell anti-oxidant defenses. Inhibition of the glutathione redox cycle enhances macrophage-mediated cytolysis. J. Exp. Med. 153: 766-782.
    • (1980) J. Exp. Med. , vol.153 , pp. 766-782
    • Nathan, C.F.1    Arrick, B.A.2    Murray, H.W.3    DeSantis, N.M.4    Cohn, Z.A.5
  • 23
    • 10144255096 scopus 로고    scopus 로고
    • Human neutrophils employ chlorine gas as an oxidant during phagocytosis
    • Hazen, S. L., F. F. Su, D. M. Mueller, J. R. Crowley, and J. W. Heinecke. 1996. Human neutrophils employ chlorine gas as an oxidant during phagocytosis. J. Clin. Invest. 98: 1283-1289.
    • (1996) J. Clin. Invest. , vol.98 , pp. 1283-1289
    • Hazen, S.L.1    Su, F.F.2    Mueller, D.M.3    Crowley, J.R.4    Heinecke, J.W.5
  • 24
    • 0025730414 scopus 로고
    • Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide
    • Radi, R., J. S. Beckman, K. M. Bush, and B. A. Freeman. 1991. Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide. J. Biol. Chem. 266: 4244-4250.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4244-4250
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 25
    • 0029160661 scopus 로고
    • Reaction of nitric oxide with the free sulfhydryl group of human serum albumin yields a sulfenic acid and nitrous oxide
    • DeMaster, E. G., B. J. Quast, B. Redfern, and H. T. Nagasawa. 1995. Reaction of nitric oxide with the free sulfhydryl group of human serum albumin yields a sulfenic acid and nitrous oxide. Biochemistry. 34: 11494-11499.
    • (1995) Biochemistry , vol.34 , pp. 11494-11499
    • DeMaster, E.G.1    Quast, B.J.2    Redfern, B.3    Nagasawa, H.T.4
  • 26
    • 0026073198 scopus 로고
    • Oxidation of propylthiouracil to reactive metabolites by activated neutrophils. Implications for agranulocytosis
    • Waldhauser, L., and J. Utrecht. 1991. Oxidation of propylthiouracil to reactive metabolites by activated neutrophils. Implications for agranulocytosis. Drug Metab. Dispos. 19: 354-359.
    • (1991) Drug Metab. Dispos. , vol.19 , pp. 354-359
    • Waldhauser, L.1    Utrecht, J.2
  • 27
    • 84965819872 scopus 로고
    • The presence and significance of bound aminoazo dyes in the livers of rats fed p-dimethylaminoazobenzene
    • Miller, E. C., and J. A. Miller. 1947. The presence and significance of bound aminoazo dyes in the livers of rats fed p-dimethylaminoazobenzene. Cancer Res. 7: 468-480.
    • (1947) Cancer Res. , vol.7 , pp. 468-480
    • Miller, E.C.1    Miller, J.A.2
  • 28
    • 0007739903 scopus 로고
    • Covalent binding and acute lethal injury in vivo: How has the hypothesis survived a decade of critical examination?
    • G. Wilkinson and M. D. Rawlins, editors. MTP Press, London
    • Smith C. V., B. H. Lauterburg, and J. R. Mitchell. 1985: Covalent binding and acute lethal injury in vivo: how has the hypothesis survived a decade of critical examination? In Drug Metabolism and Disposition: Considerations in Clinical Pharmacology. G. Wilkinson and M. D. Rawlins, editors. MTP Press, London, 161-181.
    • (1985) Drug Metabolism and Disposition: Considerations in Clinical Pharmacology , pp. 161-181
    • Smith, C.V.1    Lauterburg, B.H.2    Mitchell, J.R.3
  • 29
    • 0025274623 scopus 로고
    • Covalent and noncovalent interactions in acute lethal cell injury caused by chemicals
    • Nelson, S. D., and P. G. Pearson. 1990. Covalent and noncovalent interactions in acute lethal cell injury caused by chemicals. Annu. Rev. Pharmacol. Toxicol. 30: 169-195.
    • (1990) Annu. Rev. Pharmacol. Toxicol. , vol.30 , pp. 169-195
    • Nelson, S.D.1    Pearson, P.G.2
  • 30
    • 0031555344 scopus 로고    scopus 로고
    • Iron and oxidized β-casein in the lavages of hyperoxic Fischer-344 rats
    • Knight, S. A., C. V. Smith, and S. E. Welty. 1997. Iron and oxidized β-casein in the lavages of hyperoxic Fischer-344 rats. Life Sci. 62: 165-176.
    • (1997) Life Sci. , vol.62 , pp. 165-176
    • Knight, S.A.1    Smith, C.V.2    Welty, S.E.3
  • 31
    • 0032584017 scopus 로고    scopus 로고
    • Protein oxidation biomarkers in hyperoxic lung injury in rats: Effects of U-74389
    • In press
    • Awasthi, S., A. Gyurasics, S. A. Knight, S. E. Welty, and C. V. Smith. 1998. Protein oxidation biomarkers in hyperoxic lung injury in rats: effects of U-74389. Toxicol. Lett. In press.
    • (1998) Toxicol. Lett.
    • Awasthi, S.1    Gyurasics, A.2    Knight, S.A.3    Welty, S.E.4    Smith, C.V.5
  • 32
    • 0027937548 scopus 로고
    • Oxidative stress: Free radical production in neural degeneration
    • Gotz, M. E., G. A. Kunig, P. Riederer, and M. B. H. Youdim. 1994. Oxidative stress: free radical production in neural degeneration. Pharmacol. Ther. 63: 37-122.
    • (1994) Pharmacol. Ther. , vol.63 , pp. 37-122
    • Gotz, M.E.1    Kunig, G.A.2    Riederer, P.3    Youdim, M.B.H.4
  • 33
    • 0030220396 scopus 로고    scopus 로고
    • Hypochlorous acid interactions with thiols, nucleotides, DNA, and other biological substrates
    • Prutz, W. A. 1996. Hypochlorous acid interactions with thiols, nucleotides, DNA, and other biological substrates. Arch. Biochem. Biophys. 332: 110-120.
    • (1996) Arch. Biochem. Biophys , vol.332 , pp. 110-120
    • Prutz, W.A.1
  • 34
    • 0029926905 scopus 로고    scopus 로고
    • Bacterial glutathione: A sacrificial defense against chlorine compounds
    • Chesney, J. A., J. W. Eaton, and J. R. Mahoney, Jr. 1996. Bacterial glutathione: a sacrificial defense against chlorine compounds. J. Bacteriol. 178: 2131-2135.
    • (1996) J. Bacteriol. , vol.178 , pp. 2131-2135
    • Chesney, J.A.1    Eaton, J.W.2    Mahoney J.R., Jr.3
  • 35
    • 0030928562 scopus 로고    scopus 로고
    • Characterization of the oxidation products of the reaction between reduced glutathione and hypochlorous acid
    • Winterbourn, C. C., and S. O. Brennan. 1997. Characterization of the oxidation products of the reaction between reduced glutathione and hypochlorous acid. Biochem. J. 326: 87-92.
    • (1997) Biochem. J. , vol.326 , pp. 87-92
    • Winterbourn, C.C.1    Brennan, S.O.2
  • 36
    • 0026517032 scopus 로고
    • Accelerated endocytosis and incomplete catabolism of radical-damaged protein
    • Grant, A. J., W. Jessup, and R. T. Dean. 1992. Accelerated endocytosis and incomplete catabolism of radical-damaged protein. Biochim. Biophys. Acta. 1134: 203-209.
    • (1992) Biochim. Biophys. Acta , vol.1134 , pp. 203-209
    • Grant, A.J.1    Jessup, W.2    Dean, R.T.3
  • 37
    • 0028265812 scopus 로고
    • Biliary excretion of lysosomal enzymes, iron, and oxidized protein in Fischer-344 and Sprague-Dawley rats and the effects of diquat and acetaminophen
    • Gupta, S., L. K. Rogers, and C. V. Smith. 1994. Biliary excretion of lysosomal enzymes, iron, and oxidized protein in Fischer-344 and Sprague-Dawley rats and the effects of diquat and acetaminophen. Toxicol. Appl. Pharmacol. 125: 42-50.
    • (1994) Toxicol. Appl. Pharmacol. , vol.125 , pp. 42-50
    • Gupta, S.1    Rogers, L.K.2    Smith, C.V.3


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