메뉴 건너뛰기




Volumn 289, Issue 15, 2014, Pages 10276-10292

Site-specific nitration of apolipoprotein a-i at tyrosine 166 is both abundant within human atherosclerotic plaque and dysfunctional

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; MONOCLONAL ANTIBODIES; NITROGEN OXIDES; RECOVERY; TRANSPORT PROPERTIES;

EID: 84898627368     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.556506     Document Type: Article
Times cited : (85)

References (59)
  • 1
    • 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 Heinecke, J. W. (1997) 3-Chlorotyrosine, a specific marker of myeloperoxidase-catalyzed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima. J. Clin. Investig. 99, 2075-2081
    • (1997) J. Clin. Investig. , vol.99 , pp. 2075-2081
    • Hazen, S.L.1    Heinecke, J.W.2
  • 3
    • 13144259687 scopus 로고    scopus 로고
    • Immunohistochemical methods to detect nitrotyrosine
    • Viera, L., Ye, Y. Z., Estévez, A. G., and Beckman, J. S. (1999) Immunohistochemical methods to detect nitrotyrosine. Methods Enzymol. 301, 373-381
    • (1999) Methods Enzymol. , vol.301 , pp. 373-381
    • Viera, L.1    Ye, Y.Z.2    Estévez, A.G.3    Beckman, J.S.4
  • 5
    • 0037124020 scopus 로고    scopus 로고
    • A tale of two controversies: Defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species
    • Brennan, M. L., Wu, W., Fu, X., Shen, Z., Song, W., Frost, H., Vadseth, C., Narine, L., Lenkiewicz, E., Borchers, M. T., Lusis, A. J., Lee, J. J., Lee, N. A., Abu-Soud, H. M., Ischiropoulos, H., and Hazen, S. L. (2002) A tale of two controversies: defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species. J. Biol. Chem. 277, 17415-17427
    • (2002) J. Biol. Chem. , vol.277 , pp. 17415-17427
    • Brennan, M.L.1    Wu, W.2    Fu, X.3    Shen, Z.4    Song, W.5    Frost, H.6    Vadseth, C.7    Narine, L.8    Lenkiewicz, E.9    Borchers, M.T.10    Lusis, A.J.11    Lee, J.J.12    Lee, N.A.13    Abu-Soud, H.M.14    Ischiropoulos, H.15    Hazen, S.L.16
  • 8
    • 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
  • 9
    • 26644451392 scopus 로고    scopus 로고
    • Tyrosine modification is not required for myeloperoxidase-induced loss of apolipoprotein A-I functional activities
    • Peng, D.-Q., Wu, Z., Brubaker, G., Zheng, L., Settle, M., Gross, E., Kinter, M., Hazen, S. L., and Smith, J. D. (2005) Tyrosine modification is not required for myeloperoxidase-induced loss of apolipoprotein A-I functional activities. J. Biol. Chem. 280, 33775-33784
    • (2005) J. Biol. Chem. , vol.280 , pp. 33775-33784
    • Peng, D.-Q.1    Wu, Z.2    Brubaker, G.3    Zheng, L.4    Settle, M.5    Gross, E.6    Kinter, M.7    Hazen, S.L.8    Smith, J.D.9
  • 11
    • 36148937168 scopus 로고    scopus 로고
    • Myeloperoxidase and inflammatory proteins: Pathways for generating dysfunctional high-density lipoprotein in humans
    • Vaisar, T., Shao, B., Green, P. S., Oda, M. N., Oram, J. F., and Heinecke, J. W. (2007) Myeloperoxidase and inflammatory proteins: pathways for generating dysfunctional high-density lipoprotein in humans. Curr. Atheroscler. Rep. 9, 417-424
    • (2007) Curr. Atheroscler. Rep. , vol.9 , pp. 417-424
    • Vaisar, T.1    Shao, B.2    Green, P.S.3    Oda, M.N.4    Oram, J.F.5    Heinecke, J.W.6
  • 14
    • 77951236321 scopus 로고    scopus 로고
    • Beyond the canonical 20 amino acids: Expanding the genetic lexicon
    • Young, T. S., and Schultz, P. G. (2010) Beyond the canonical 20 amino acids: expanding the genetic lexicon. J. Biol. Chem. 285, 11039-11044
    • (2010) J. Biol. Chem. , vol.285 , pp. 11039-11044
    • Young, T.S.1    Schultz, P.G.2
  • 18
    • 71449125360 scopus 로고    scopus 로고
    • Modification of high density lipoprotein by myeloperoxidase generates a pro-inflammatory particle
    • Undurti, A., Huang, Y., Lupica, J. A., Smith, J. D., DiDonato, J. A., and Hazen, S. L. (2009) Modification of high density lipoprotein by myeloperoxidase generates a pro-inflammatory particle. J. Biol. Chem. 284, 30825-30835
    • (2009) J. Biol. Chem. , vol.284 , pp. 30825-30835
    • Undurti, A.1    Huang, Y.2    Lupica, J.A.3    Smith, J.D.4    Didonato, J.A.5    Hazen, S.L.6
  • 20
    • 84871440206 scopus 로고    scopus 로고
    • Myeloperoxidase-derived oxidants modify apolipoprotein A-I and generate dysfunctional high-density lipoproteins: Comparison of hypothiocyanous acid (HOSCN) with hypochlorous acid (HOCl)
    • Hadfield, K. A., Pattison, D. I., Brown, B. E., Hou, L., Rye, K. A., Davies, M. J., and Hawkins, C. L. (2013) Myeloperoxidase-derived oxidants modify apolipoprotein A-I and generate dysfunctional high-density lipoproteins: comparison of hypothiocyanous acid (HOSCN) with hypochlorous acid (HOCl). Biochem. J. 449, 531-542
    • (2013) Biochem. J. , vol.449 , pp. 531-542
    • Hadfield, K.A.1    Pattison, D.I.2    Brown, B.E.3    Hou, L.4    Rye, K.A.5    Davies, M.J.6    Hawkins, C.L.7
  • 21
    • 14044250955 scopus 로고    scopus 로고
    • Tyrosine 192 in apolipoprotein A-I is the major site of nitration and chlorination by myeloperoxidase, but only chlorination markedly impairs ABCA1-dependent cholesterol transport
    • Shao, B., Bergt, C., Fu, X., Green, P., Voss, J. C., Oda, M. N., Oram, J. F., and Heinecke, J. W. (2005) Tyrosine 192 in apolipoprotein A-I is the major site of nitration and chlorination by myeloperoxidase, but only chlorination markedly impairs ABCA1-dependent cholesterol transport. J. Biol. Chem. 280, 5983-5993
    • (2005) J. Biol. Chem. , vol.280 , pp. 5983-5993
    • Shao, B.1    Bergt, C.2    Fu, X.3    Green, P.4    Voss, J.C.5    Oda, M.N.6    Oram, J.F.7    Heinecke, J.W.8
  • 22
    • 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
  • 24
    • 38949111042 scopus 로고    scopus 로고
    • Proteomics and lipids of lipoproteins isolated at low salt concentrations in D2O/sucrose or in KBr
    • Stahlman, M., Davidsson, P., Kanmert, I., Rosengren, B., Borén, J., Fagerberg, B., and Camejo, G. (2008) Proteomics and lipids of lipoproteins isolated at low salt concentrations in D2O/sucrose or in KBr. J. Lipid Res. 49, 481-490
    • (2008) J. Lipid Res. , vol.49 , pp. 481-490
    • Stahlman, M.1    Davidsson, P.2    Kanmert, I.3    Rosengren, B.4    Borén, J.5    Fagerberg, B.6    Camejo, G.7
  • 25
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell, M. A., Haas, S. M., Bieber, L. L., and Tolbert, N. E. (1978) A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal. Biochem. 87, 206-210
    • (1978) Anal. Biochem. , vol.87 , pp. 206-210
    • Markwell, M.A.1    Haas, S.M.2    Bieber, L.L.3    Tolbert, N.E.4
  • 26
    • 0032615962 scopus 로고    scopus 로고
    • Lecithin-cholesterol acyltransferase. Assay of cholesterol esterification and phospholipase A2 activities
    • Parks, J. S., Gebre, A. K., and Furbee, J. W. (1999) Lecithin-cholesterol acyltransferase. Assay of cholesterol esterification and phospholipase A2 activities. Methods Mol. Biol. 109, 123-131
    • (1999) Methods Mol. Biol. , vol.109 , pp. 123-131
    • Parks, J.S.1    Gebre, A.K.2    Furbee, J.W.3
  • 28
    • 0020490523 scopus 로고
    • Micellar complexes of human apolipoprotein A-I with phosphatidylcholines and cholesterol prepared from cholate-lipid dispersions
    • Matz, C. E., and Jonas, A. (1982) Micellar complexes of human apolipoprotein A-I with phosphatidylcholines and cholesterol prepared from cholate-lipid dispersions. J. Biol. Chem. 257, 4535-4540
    • (1982) J. Biol. Chem. , vol.257 , pp. 4535-4540
    • Matz, C.E.1    Jonas, A.2
  • 29
    • 0025017863 scopus 로고
    • Differential inactivation of Escherichia coli membrane dehydrogenases by a myeloperoxidase-mediated antimicrobial system
    • Rakita, R. M., Michel, B. R., and Rosen, H. (1990) Differential inactivation of Escherichia coli membrane dehydrogenases by a myeloperoxidase-mediated antimicrobial system. Biochemistry 29, 1075-1080
    • (1990) Biochemistry , vol.29 , pp. 1075-1080
    • Rakita, R.M.1    Michel, B.R.2    Rosen, H.3
  • 30
    • 0022580733 scopus 로고
    • Crystallization and properties of myeloperoxidase from normal human leukocytes
    • Morita, Y., Iwamoto, H., Aibara, S., Kobayashi, T., and Hasegawa, E. (1986) Crystallization and properties of myeloperoxidase from normal human leukocytes. J. Biochem. 99, 761-770
    • (1986) J. Biochem. , vol.99 , pp. 761-770
    • Morita, Y.1    Iwamoto, H.2    Aibara, S.3    Kobayashi, T.4    Hasegawa, E.5
  • 31
    • 0015416039 scopus 로고
    • Enthalpy of decomposition of hydrogen peroxide by catalase at 25 degrees C (with molar extinction coefficients of H2O2 solutions in the UV)
    • Nelson, D. P., and Kiesow, L. A. (1972) Enthalpy of decomposition of hydrogen peroxide by catalase at 25 degrees C (with molar extinction coefficients of H2O2 solutions in the UV). Anal. Biochem. 49, 474-478
    • (1972) Anal. Biochem. , vol.49 , pp. 474-478
    • Nelson, D.P.1    Kiesow, L.A.2
  • 32
    • 8544251150 scopus 로고
    • The acid ionization constant of HOCl from 5 to 35°
    • Morris, J. C. (1966) The acid ionization constant of HOCl from 5 to 35°. J. Phys. Chem. 70, 3798-3805
    • (1966) J. Phys. Chem. , vol.70 , pp. 3798-3805
    • Morris, J.C.1
  • 33
    • 0034693038 scopus 로고    scopus 로고
    • Superoxide reacts with nitric oxide to nitrate tyrosine at physiological pH via peroxynitrite
    • Reiter, C. D., Teng, R. J., and Beckman, J. S. (2000) Superoxide reacts with nitric oxide to nitrate tyrosine at physiological pH via peroxynitrite. J. Biol. Chem. 275, 32460-32466
    • (2000) J. Biol. Chem. , vol.275 , pp. 32460-32466
    • Reiter, C.D.1    Teng, R.J.2    Beckman, J.S.3
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0035917812 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli
    • Wang, L., Brock, A., Herberich, B., and Schultz, P. G. (2001) Expanding the genetic code of Escherichia coli. Science 292, 498-500
    • (2001) Science , vol.292 , pp. 498-500
    • Wang, L.1    Brock, A.2    Herberich, B.3    Schultz, P.G.4
  • 36
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and ugly
    • Beckman, J. S., and Koppenol, W. H. (1996) Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly. Am. J. Physiol. Cell Physiol. 271, C1424-C1437
    • (1996) Am. J. Physiol. Cell Physiol. , vol.271
    • Beckman, J.S.1    Koppenol, W.H.2
  • 38
    • 0034648768 scopus 로고    scopus 로고
    • Atherosclerosis
    • Lusis, A. J. (2000) Atherosclerosis. Nature 407, 233-241
    • (2000) Nature , vol.407 , pp. 233-241
    • Lusis, A.J.1
  • 42
    • 84865485915 scopus 로고    scopus 로고
    • Inflammation in atherosclerosis
    • Libby, P. (2012) Inflammation in atherosclerosis. Arterioscler. Thromb. Vasc. Biol. 32, 2045-2051
    • (2012) Arterioscler. Thromb. Vasc. Biol. , vol.32 , pp. 2045-2051
    • Libby, P.1
  • 43
    • 0017384270 scopus 로고
    • High density lipoprotein as a protective factor against coronary heart disease. The Framingham Study
    • Gordon, T., Castelli, W. P., Hjortland, M. C., Kannel, W. B., and Dawber, T. R. (1977) High density lipoprotein as a protective factor against coronary heart disease. The Framingham Study. Am. J. Med. 62, 707-714
    • (1977) Am. J. Med. , vol.62 , pp. 707-714
    • Gordon, T.1    Castelli, W.P.2    Hjortland, M.C.3    Kannel, W.B.4    Dawber, T.R.5
  • 44
    • 0024550898 scopus 로고
    • High density lipoprotein plasma fractions inhibit aortic fatty streaks in cholesterol-fed rabbits
    • Badimon, J. J., Badimon, L., Galvez, A., Dische, R., and Fuster, V. (1989) High density lipoprotein plasma fractions inhibit aortic fatty streaks in cholesterol-fed rabbits. Lab. Invest. 60, 455-461
    • (1989) Lab. Invest. , vol.60 , pp. 455-461
    • Badimon, J.J.1    Badimon, L.2    Galvez, A.3    Dische, R.4    Fuster, V.5
  • 45
    • 0025322265 scopus 로고
    • Regression of atherosclerotic lesions by high density lipoprotein plasma fraction in the cholesterolfed rabbit
    • Badimon, J. J., Badimon, L., and Fuster, V. (1990) Regression of atherosclerotic lesions by high density lipoprotein plasma fraction in the cholesterolfed rabbit. J. Clin. Investig. 85, 1234-1241
    • (1990) J. Clin. Investig. , vol.85 , pp. 1234-1241
    • Badimon, J.J.1    Badimon, L.2    Fuster, V.3
  • 49
    • 0025902231 scopus 로고
    • Inhibition of early atherogenesis in transgenic mice by human apolipoprotein AI
    • Rubin, E. M., Krauss, R. M., Spangler, E. A., Verstuyft, J. G., and Clift, S. M. (1991) Inhibition of early atherogenesis in transgenic mice by human apolipoprotein AI. Nature 353, 265-267
    • (1991) Nature , vol.353 , pp. 265-267
    • Rubin, E.M.1    Krauss, R.M.2    Spangler, E.A.3    Verstuyft, J.G.4    Clift, S.M.5
  • 50
    • 0028025262 scopus 로고
    • Human apolipoprotein A-I gene expression increases high density lipoprotein and suppresses atherosclerosis in the apolipoprotein E-deficient mouse
    • Plump, A. S., Scott, C. J., and Breslow, J. L. (1994) Human apolipoprotein A-I gene expression increases high density lipoprotein and suppresses atherosclerosis in the apolipoprotein E-deficient mouse. Proc. Natl. Acad. Sci. U.S.A. 91, 9607-9611
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 9607-9611
    • Plump, A.S.1    Scott, C.J.2    Breslow, J.L.3
  • 51
    • 0030865194 scopus 로고    scopus 로고
    • HDL deficiency in genetically engineered mice requires elevated LDL to accelerate atherogenesis
    • Hughes, S. D., Verstuyft, J., and Rubin, E. M. (1997) HDL deficiency in genetically engineered mice requires elevated LDL to accelerate atherogenesis. Arterioscler. Thromb. Vasc. Biol. 17, 1725-1729
    • (1997) Arterioscler. Thromb. Vasc. Biol. , vol.17 , pp. 1725-1729
    • Hughes, S.D.1    Verstuyft, J.2    Rubin, E.M.3
  • 53
    • 0034926855 scopus 로고    scopus 로고
    • Endothelial function and coronary artery disease
    • Kinlay, S., Libby, P., and Ganz, P. (2001) Endothelial function and coronary artery disease. Curr. Opin. Lipidol 12, 383-389
    • (2001) Curr. Opin. Lipidol , vol.12 , pp. 383-389
    • Kinlay, S.1    Libby, P.2    Ganz, P.3
  • 57
    • 84892938632 scopus 로고    scopus 로고
    • High-density lipoprotein and atherosclerosis regression: Evidence from preclinical and clinical studies
    • Feig, J. E., Hewing, B., Smith, J. D., Hazen, S. L., and Fisher, E. A. (2014) High-density lipoprotein and atherosclerosis regression: evidence from preclinical and clinical studies. Circ. Res. 114, 205-213
    • (2014) Circ. Res. , vol.114 , pp. 205-213
    • Feig, J.E.1    Hewing, B.2    Smith, J.D.3    Hazen, S.L.4    Fisher, E.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.