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Volumn 290, Issue 17, 2015, Pages 10958-10971

Myeloperoxidase-mediated methionine oxidation promotes an amyloidogenic outcome for apolipoprotein A-I

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DEPOSITION; DISEASES; GLYCOPROTEINS; LIPOPROTEINS; OXIDATION; PROTEINS;

EID: 84928596578     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.630442     Document Type: Article
Times cited : (36)

References (51)
  • 1
    • 77957875471 scopus 로고    scopus 로고
    • Myeloperoxidase, inflammation, and dysfunctional high-density lipoprotein
    • Smith, J. D. (2010) Myeloperoxidase, inflammation, and dysfunctional high-density lipoprotein. J. Clin. Lipidol. 4, 382-388
    • (2010) J. Clin. Lipidol. , vol.4 , pp. 382-388
    • Smith, J.D.1
  • 2
    • 0028292033 scopus 로고
    • Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions
    • Daugherty, A., Dunn, J. L., Rateri, D. L., and Heinecke, J. W. (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
  • 3
    • 25144473410 scopus 로고    scopus 로고
    • Formation of dysfunctional high-density lipoprotein by myeloperoxidase
    • Nicholls, S. J., Zheng, L., and Hazen, S. L. (2005) Formation of dysfunctional high-density lipoprotein by myeloperoxidase. Trends Cardiovasc. Med. 15, 212-219
    • (2005) Trends Cardiovasc. Med. , vol.15 , pp. 212-219
    • Nicholls, S.J.1    Zheng, L.2    Hazen, S.L.3
  • 4
    • 33646941974 scopus 로고    scopus 로고
    • Myeloperoxidase impairs ABCA1-dependent cholesterol efflux through methionine oxidation and site-specific tyrosine chlorination of apolipoprotein A-I
    • Shao, B., Oda, M. N., Bergt, C., Fu, X., Green, P. S., Brot, N., Oram, J. F., and Heinecke, J. W. (2006) Myeloperoxidase impairs ABCA1-dependent cholesterol efflux through methionine oxidation and site-specific tyrosine chlorination of apolipoprotein A-I. J. Biol. Chem. 281, 9001-9004
    • (2006) J. Biol. Chem. , vol.281 , pp. 9001-9004
    • Shao, B.1    Oda, M.N.2    Bergt, C.3    Fu, X.4    Green, P.S.5    Brot, N.6    Oram, J.F.7    Heinecke, J.W.8
  • 5
    • 77953497990 scopus 로고    scopus 로고
    • Oxidation of apolipoprotein A-I by myeloperoxidase impairs the initial interactions with ABCA1 required for signaling and cholesterol export
    • Shao, B., Tang, C., Heinecke, J. W., and Oram, J. F. (2010) Oxidation of apolipoprotein A-I by myeloperoxidase impairs the initial interactions with ABCA1 required for signaling and cholesterol export. J. Lipid Res. 51, 1849-1858
    • (2010) J. Lipid Res. , vol.51 , pp. 1849-1858
    • Shao, B.1    Tang, C.2    Heinecke, J.W.3    Oram, J.F.4
  • 6
    • 12844268120 scopus 로고    scopus 로고
    • Localization of nitration and chlorination sites on apolipoprotein A-I catalyzed by myeloperoxidase in human atheroma and associated oxidative impairment in ABCA1-dependent cholesterol efflux from macrophages
    • Zheng, L., Settle, M., Brubaker, G., Schmitt, D., Hazen, S. L., Smith, J. D., and Kinter, M. (2005) Localization of nitration and chlorination sites on apolipoprotein A-I catalyzed by myeloperoxidase in human atheroma and associated oxidative impairment in ABCA1-dependent cholesterol efflux from macrophages. J. Biol. Chem. 280, 38-47
    • (2005) J. Biol. Chem. , vol.280 , pp. 38-47
    • Zheng, L.1    Settle, M.2    Brubaker, G.3    Schmitt, D.4    Hazen, S.L.5    Smith, J.D.6    Kinter, M.7
  • 7
    • 50449086363 scopus 로고    scopus 로고
    • Methionine oxidation impairs reverse cholesterol transport by apolipoprotein A-I
    • Shao, B., Cavigiolio, G., Brot, N., Oda, M. N., and Heinecke, J. W. (2008) Methionine oxidation impairs reverse cholesterol transport by apolipoprotein A-I. 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.1    Cavigiolio, G.2    Brot, N.3    Oda, M.N.4    Heinecke, J.W.5
  • 8
    • 84857491459 scopus 로고    scopus 로고
    • Myeloperoxidase targets apolipoprotein A-I, the major high density lipoprotein protein, for site-specific oxidation in human atherosclerotic lesions
    • Shao, B., Pennathur, S., and Heinecke, J. W. (2012) Myeloperoxidase targets apolipoprotein A-I, the major high density lipoprotein protein, for site-specific oxidation in human atherosclerotic lesions. J. Biol. Chem. 287, 6375-6386
    • (2012) J. Biol. Chem. , vol.287 , pp. 6375-6386
    • Shao, B.1    Pennathur, S.2    Heinecke, J.W.3
  • 12
    • 84901637810 scopus 로고    scopus 로고
    • Humans with atherosclerosis have impaired ABCA1 cholesterol efflux and enhanced high-density lipoprotein oxidation by myeloperoxidase
    • Shao, B., Tang, C., Sinha, A., Mayer, P. S., Davenport, G. D., Brot, N., Oda, M. N., Zhao, X. Q., and Heinecke, J. W. (2014) Humans with atherosclerosis have impaired ABCA1 cholesterol efflux and enhanced high-density lipoprotein oxidation by myeloperoxidase. Circ. Res. 114, 1733-1742
    • (2014) Circ. Res. , vol.114 , pp. 1733-1742
    • Shao, B.1    Tang, C.2    Sinha, A.3    Mayer, P.S.4    Davenport, G.D.5    Brot, N.6    Oda, M.N.7    Zhao, X.Q.8    Heinecke, J.W.9
  • 17
    • 22144469842 scopus 로고    scopus 로고
    • Ostertag revisited: The inherited systemic amyloidoses without neuropathy
    • Benson, M. D. (2005) Ostertag revisited: the inherited systemic amyloidoses without neuropathy. Amyloid 12, 75-87
    • (2005) Amyloid , vol.12 , pp. 75-87
    • Benson, M.D.1
  • 18
    • 0032887169 scopus 로고    scopus 로고
    • The new apolipoprotein A-I variant Leu-174 → Ser causes hereditary cardiac amyloidosis, and the amyloid fibrils are constituted by the 93-residue N-terminal polypeptide
    • Obici, L., Bellotti, V., Mangione, P., Stoppini, M., Arbustini, E., Verga, L., Zorzoli, I., Anesi, E., Zanotti, G., Campana, C., Viganò, M., and Merlini, G. (1999) The new apolipoprotein A-I variant Leu-174 → Ser causes hereditary cardiac amyloidosis, and the amyloid fibrils are constituted by the 93-residue N-terminal polypeptide. Am. J. Pathol. 155, 695-702
    • (1999) Am. J. Pathol. , vol.155 , pp. 695-702
    • Obici, L.1    Bellotti, V.2    Mangione, P.3    Stoppini, M.4    Arbustini, E.5    Verga, L.6    Zorzoli, I.7    Anesi, E.8    Zanotti, G.9    Campana, C.10    Viganò, M.11    Merlini, G.12
  • 21
    • 82255177161 scopus 로고    scopus 로고
    • Non-hereditary apolipoprotein AI-associated pulmonary amyloid
    • Murphy, C., Kestler, D., Weiss, D., and Solomon, A. (2011) Non-hereditary apolipoprotein AI-associated pulmonary amyloid. Amyloid 18, 219-220
    • (2011) Amyloid , vol.18 , pp. 219-220
    • Murphy, C.1    Kestler, D.2    Weiss, D.3    Solomon, A.4
  • 23
    • 84867362040 scopus 로고    scopus 로고
    • Mass spectrometry analysis reveals non-mutated apolipoprotein A1 lumbosacral radiculoplexus amyloidoma
    • Loavenbruck, A. J., Chaudhry, V., Zeldenrust, S. R., Spinner, R. J., Theis, J. D., and Klein, C. J. (2012) Mass spectrometry analysis reveals non-mutated apolipoprotein A1 lumbosacral radiculoplexus amyloidoma. Muscle Nerve 46, 817-822
    • (2012) Muscle Nerve , vol.46 , pp. 817-822
    • Loavenbruck, A.J.1    Chaudhry, V.2    Zeldenrust, S.R.3    Spinner, R.J.4    Theis, J.D.5    Klein, C.J.6
  • 25
    • 0028866543 scopus 로고
    • Apolipoprotein A1-derived amyloid in human aortic atherosclerotic plaques
    • Westermark, P., Mucchiano, G., Marthin, T., Johnson, K. H., and Sletten, K. (1995) Apolipoprotein A1-derived amyloid in human aortic atherosclerotic plaques. Am. J. Pathol. 147, 1186-1192
    • (1995) Am. J. Pathol. , vol.147 , pp. 1186-1192
    • Westermark, P.1    Mucchiano, G.2    Marthin, T.3    Johnson, K.H.4    Sletten, K.5
  • 26
    • 0034746557 scopus 로고    scopus 로고
    • Apolipoprotein A-1-derived amyloid in atherosclerotic plaques of the human aorta
    • Mucchiano, G. I., Häggqvist, B., Sletten, K., and Westermark, P. (2001) Apolipoprotein A-1-derived amyloid in atherosclerotic plaques of the human aorta. J. Pathol. 193, 270-275
    • (2001) J. Pathol. , vol.193 , pp. 270-275
    • Mucchiano, G.I.1    Häggqvist, B.2    Sletten, K.3    Westermark, P.4
  • 27
    • 0035125904 scopus 로고    scopus 로고
    • Apolipoprotein A-I-derived amyloid in atherosclerosis. Its association with plasma levels of apolipoprotein A-I and cholesterol
    • Mucchiano, G. I., Jonasson, L., Häggqvist, B., Einarsson, E., and Westermark, P. (2001) Apolipoprotein A-I-derived amyloid in atherosclerosis. Its association with plasma levels of apolipoprotein A-I and cholesterol. Am. J. Clin. Pathol. 115, 298-303
    • (2001) Am. J. Clin. Pathol. , vol.115 , pp. 298-303
    • Mucchiano, G.I.1    Jonasson, L.2    Häggqvist, B.3    Einarsson, E.4    Westermark, P.5
  • 28
    • 0020519870 scopus 로고
    • Frequency and distribution of senile cardiovascular amyloid: A clinicopathologic correlation
    • Cornwell, G. G., 3rd, Murdoch, W. L., Kyle, R. A., Westermark, P., and Pitkänen, P. (1983) Frequency and distribution of senile cardiovascular amyloid: a clinicopathologic correlation. Am. J. Med. 75, 618-623
    • (1983) Am. J. Med. , vol.75 , pp. 618-623
    • Cornwell, G.G.1    Murdoch, W.L.2    Kyle, R.A.3    Westermark, P.4    Pitkänen, P.5
  • 29
    • 0026551594 scopus 로고
    • Senile aortic amyloid: Evidence for two distinct forms of localized deposits
    • Mucchiano, G., Cornwell, G. G., 3rd, and Westermark, P. (1992) Senile aortic amyloid: evidence for two distinct forms of localized deposits. Am. J. Pathol. 140, 871-877
    • (1992) Am. J. Pathol. , vol.140 , pp. 871-877
    • Mucchiano, G.1    Cornwell, G.G.2    Westermark, P.3
  • 30
    • 76649124599 scopus 로고    scopus 로고
    • Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I
    • Wong, Y. Q., Binger, K. J., Howlett, G. J., and Griffin, M. D. (2010) Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. Proc. Natl. Acad. Sci. U.S.A. 107, 1977-1982
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 1977-1982
    • Wong, Y.Q.1    Binger, K.J.2    Howlett, G.J.3    Griffin, M.D.4
  • 31
    • 67650544156 scopus 로고    scopus 로고
    • Purification of recombinant apolipoproteins A-I and A-IV and efficient affinity tag cleavage by tobacco etch virus protease
    • Tubb, M. R., Smith, L. E., and Davidson, W. S. (2009) Purification of recombinant apolipoproteins A-I and A-IV and efficient affinity tag cleavage by tobacco etch virus protease. J. Lipid Res. 50, 1497-1504
    • (2009) J. Lipid Res. , vol.50 , pp. 1497-1504
    • Tubb, M.R.1    Smith, L.E.2    Davidson, W.S.3
  • 32
    • 0022556074 scopus 로고
    • Sequential flotation ultracentrifugation
    • Schumaker, V. N., and Puppione, D. L. (1986) Sequential flotation ultracentrifugation. Methods Enzymol. 128, 155-170
    • (1986) Methods Enzymol. , vol.128 , pp. 155-170
    • Schumaker, V.N.1    Puppione, D.L.2
  • 33
    • 0020405895 scopus 로고
    • Effect of dipalmitoylphosphatidylcholine vesicle curvature on the reaction with human apolipoprotein A-I
    • Wetterau, J. R., and Jonas, A. (1982) Effect of dipalmitoylphosphatidylcholine vesicle curvature on the reaction with human apolipoprotein A-I. J. Biol. Chem. 257, 10961-10966
    • (1982) J. Biol. Chem. , vol.257 , pp. 10961-10966
    • Wetterau, J.R.1    Jonas, A.2
  • 35
    • 80053920332 scopus 로고    scopus 로고
    • Impact of self-association on function of apolipoprotein A-I
    • Jayaraman, S., Abe-Dohmae, S., Yokoyama, S., and Cavigiolio, G. (2011) Impact of self-association on function of apolipoprotein A-I. J. Biol. Chem. 286, 35610-35623
    • (2011) J. Biol. Chem. , vol.286 , pp. 35610-35623
    • Jayaraman, S.1    Abe-Dohmae, S.2    Yokoyama, S.3    Cavigiolio, G.4
  • 36
    • 44849131744 scopus 로고    scopus 로고
    • Using tandem mass spectrometry to quantify site-specific chlorination and nitration of proteins: Model system studies with high-density lipoprotein oxidized by myeloperoxidase
    • Shao, B., and Heinecke, J. W. (2008) Using tandem mass spectrometry to quantify site-specific chlorination and nitration of proteins: model system studies with high-density lipoprotein oxidized by myeloperoxidase. Methods Enzymol. 440, 33-63
    • (2008) Methods Enzymol. , vol.440 , pp. 33-63
    • Shao, B.1    Heinecke, J.W.2
  • 37
    • 84902537346 scopus 로고    scopus 로고
    • Pitfalls associated with the use of thioflavin-T to monitor anti-fibrillogenic activity
    • Coelho-Cerqueira, E., Pinheiro, A. S., and Follmer, C. (2014) Pitfalls associated with the use of thioflavin-T to monitor anti-fibrillogenic activity. Bioorg. Med. Chem. Lett. 24, 3194-3198
    • (2014) Bioorg. Med. Chem. Lett. , vol.24 , pp. 3194-3198
    • Coelho-Cerqueira, E.1    Pinheiro, A.S.2    Follmer, C.3
  • 38
    • 0037453266 scopus 로고    scopus 로고
    • Human plasma high-density lipoproteins are stabilized by kinetic factors
    • Mehta, R., Gantz, D. L., and Gursky, O. (2003) Human plasma high-density lipoproteins are stabilized by kinetic factors. J. Mol. Biol. 328, 183-192
    • (2003) J. Mol. Biol. , vol.328 , pp. 183-192
    • Mehta, R.1    Gantz, D.L.2    Gursky, O.3
  • 39
    • 0032899322 scopus 로고    scopus 로고
    • Quantifying amyloid β-peptide (Aαβ) aggregation using the Congo red-Aβ (CR-aβ) spectrophotometric assay
    • Klunk, W. E., Jacob, R. F., and Mason, R. P. (1999) Quantifying amyloid β-peptide (Aαβ) aggregation using the Congo red-Aβ (CR-aβ) spectrophotometric assay. Anal. Biochem. 266, 66-76
    • (1999) Anal. Biochem. , vol.266 , pp. 66-76
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 43
    • 0012811428 scopus 로고
    • Identification of β,β-turns and unordered conformations in polypeptide chains by vacuum ultraviolet circular dichroism
    • Brahms, S., Brahms, J., Spach, G., and Brack, A. (1977) Identification of β,β-turns and unordered conformations in polypeptide chains by vacuum ultraviolet circular dichroism. Proc. Natl. Acad. Sci. U.S.A. 74, 3208-3212
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 3208-3212
    • Brahms, S.1    Brahms, J.2    Spach, G.3    Brack, A.4
  • 44
    • 9344243513 scopus 로고    scopus 로고
    • FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils
    • Zandomeneghi, G., Krebs, M. R., McCammon, M. G., and Fändrich, M. (2004) FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils. Protein Sci. 13, 3314-3321
    • (2004) Protein Sci. , vol.13 , pp. 3314-3321
    • Zandomeneghi, G.1    Krebs, M.R.2    McCammon, M.G.3    Fändrich, M.4
  • 47
    • 70449584579 scopus 로고    scopus 로고
    • 2D IR provides evidence for mobile water molecules in β-amyloid fibrils
    • Kim, Y. S., Liu, L., Axelsen, P. H., and Hochstrasser, R. M. (2009) 2D IR provides evidence for mobile water molecules in β-amyloid fibrils. Proc. Natl. Acad. Sci. U.S.A. 106, 17751-17756
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 17751-17756
    • Kim, Y.S.1    Liu, L.2    Axelsen, P.H.3    Hochstrasser, R.M.4
  • 48
    • 84857746675 scopus 로고    scopus 로고
    • Two-dimensional IR spectroscopy and segmental 13C labeling reveals the domain structure of human γD-crystallin amyloid fibrils
    • Moran, S. D., Woys, A. M., Buchanan, L. E., Bixby, E., Decatur, S. M., and Zanni, M. T. (2012) Two-dimensional IR spectroscopy and segmental 13C labeling reveals the domain structure of human γD-crystallin amyloid fibrils. Proc. Natl. Acad. Sci. U.S.A. 109, 3329-3334
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 3329-3334
    • Moran, S.D.1    Woys, A.M.2    Buchanan, L.E.3    Bixby, E.4    Decatur, S.M.5    Zanni, M.T.6
  • 51
    • 84921046821 scopus 로고    scopus 로고
    • Stable, metastable, and kinetically trapped amyloid aggregate phases
    • Miti, T., Mulaj, M., Schmit, J. D., and Muschol, M. (2015) Stable, metastable, and kinetically trapped amyloid aggregate phases. Biomacromolecules 16, 326-335
    • (2015) Biomacromolecules , vol.16 , pp. 326-335
    • Miti, T.1    Mulaj, M.2    Schmit, J.D.3    Muschol, M.4


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