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Disease Markers
Volume 2015, Article ID 708282, 8 pages
http://dx.doi.org/10.1155/2015/708282
Review Article

3-Nitrotyrosine Modified Proteins in Atherosclerosis

Instituto de Química Biológica, Facultad de Ciencias, Universidad de la República, Iguá 4225, 11400 Montevideo, Uruguay

Received 28 December 2014; Accepted 17 February 2015

Academic Editor: Dinesh Kumbhare

Copyright © 2015 Leonor Thomson. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. X.-L. Niu, N. R. Madamanchi, A. E. Vendrov et al., “Nox activator 1: a potential target for modulation of vascular reactive oxygen species in atherosclerotic arteries,” Circulation, vol. 121, no. 4, pp. 549–559, 2010. View at Publisher · View at Google Scholar · View at Scopus
  2. P. Minuz, P. Patrignani, S. Gaino et al., “Increased oxidative stress and platelet activation in patients with hypertension and renovascular disease,” Circulation, vol. 106, no. 22, pp. 2800–2805, 2002. View at Publisher · View at Google Scholar · View at Scopus
  3. T. Hidaka, K. Nakagawa, C. Goto et al., “Pioglitazone improves endothelium-dependent vasodilation in hypertensive patients with impaired glucose tolerance in part through a decrease in oxidative stress,” Atherosclerosis, vol. 210, no. 2, pp. 521–524, 2010. View at Publisher · View at Google Scholar · View at Scopus
  4. C. Heymes, J. K. Bendall, P. Ratajczak et al., “Increased myocardial NADPH oxidase activity in human heart failure,” Journal of the American College of Cardiology, vol. 41, no. 12, pp. 2164–2171, 2003. View at Publisher · View at Google Scholar · View at Scopus
  5. P. A. Barry-Lane, C. Patterson, M. van der Merwe et al., “p47phox is required for atherosclerotic lesion progression in ApoE−/− mice,” The Journal of Clinical Investigation, vol. 108, no. 10, pp. 1513–1522, 2001. View at Publisher · View at Google Scholar · View at Scopus
  6. S. W. Ballinger, C. Patterson, C. A. Knight-Lozano et al., “Mitochondrial integrity and function in atherogenesis,” Circulation, vol. 106, no. 5, pp. 544–549, 2002. View at Publisher · View at Google Scholar · View at Scopus
  7. E. Schwedhelm, A. Bartling, H. Lenzen et al., “Urinary 8-iso-prostaglandin F2alpha as a risk marker in patients with coronary heart disease: a matched case-control study,” Circulation, vol. 109, no. 7, pp. 843–848, 2004. View at Publisher · View at Google Scholar · View at Scopus
  8. J. F. Keaney Jr., M. G. Larson, R. S. Vasan et al., “Obesity and systemic oxidative stress: clinical correlates of oxidative stress in the Framingham study,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 23, no. 3, pp. 434–439, 2003. View at Publisher · View at Google Scholar · View at Scopus
  9. M. Karakas, W. Koenig, A. Zierer et al., “Myeloperoxidase is associated with incident coronary heart disease independently of traditional risk factors: results from the MONICA/KORA Augsburg study,” Journal of Internal Medicine, vol. 271, no. 1, pp. 43–50, 2012. View at Publisher · View at Google Scholar · View at Scopus
  10. N. R. Madamanchi, A. Vendrov, and M. S. Runge, “Oxidative stress and vascular disease,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 25, no. 1, pp. 29–38, 2005. View at Publisher · View at Google Scholar · View at Scopus
  11. A. C. Li and C. K. Glass, “The macrophage foam cell as a target for therapeutic intervention,” Nature Medicine, vol. 8, no. 11, pp. 1235–1242, 2002. View at Publisher · View at Google Scholar · View at Scopus
  12. M. P. Young, M. Febbraio, and R. L. Silverstein, “CD36 modulates migration of mouse and human macrophages in response to oxidized LDL and may contribute to macrophage trapping in the arterial intima,” The Journal of Clinical Investigation, vol. 119, no. 1, pp. 136–145, 2009. View at Publisher · View at Google Scholar · View at Scopus
  13. D. R. Greaves and S. Gordon, “Recent insights into the biology of macrophage scavenger receptors,” Journal of Lipid Research, vol. 46, no. 1, pp. 11–20, 2005. View at Publisher · View at Google Scholar · View at Scopus
  14. M. van Eck, M. Pennings, M. Hoekstra, R. Out, and T. J. C. van Berkel, “Scavenger receptor BI and ATP-binding cassette transporter A1 in reverse cholesterol transport atherosclerosis,” Current Opinion in Lipidology, vol. 16, no. 3, pp. 307–315, 2005. View at Publisher · View at Google Scholar · View at Scopus
  15. A. M. Cassina, R. Hodara, J. M. Souza et al., “Cytochrome c nitration by peroxynitrite,” Journal of Biological Chemistry, vol. 275, no. 28, pp. 21409–21415, 2000. View at Publisher · View at Google Scholar · View at Scopus
  16. M. Trujillo, B. Alvarez, J. M. Souza et al., “Mechanisms and biological consequences of peroxynitrite-dependent protein oxidation and nitration,” in Nitric Oxide. Biology and Pathobiology, L. Ignarro, Ed., pp. 1010–1050, Academic Press, San Diego, Calif, USA, 2010. View at Google Scholar
  17. I. Parastatidis, L. Thomson, D. M. Fries et al., “Increased protein nitration burden in the atherosclerotic lesions and plasma of apolipoprotein A-I-deficient mice,” Circulation Research, vol. 101, no. 4, pp. 368–376, 2007. View at Publisher · View at Google Scholar · View at Scopus
  18. L. Thomson, M. Tenopoulou, R. Lightfoot et al., “Immunoglobulins against tyrosine-nitrated epitopes in coronary artery disease,” Circulation, vol. 126, no. 20, pp. 2392–2401, 2012. View at Publisher · View at Google Scholar · View at Scopus
  19. S. M. Vaz and O. Augusto, “Inhibition of myeloperoxidase-mediated protein nitration by tempol: kinetics, mechanism, and implications,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 24, pp. 8191–8196, 2008. View at Publisher · View at Google Scholar · View at Scopus
  20. S. Solar, W. Solar, and N. Getoff, “Reactivity of hydroxyl with tyrosine in aqueous solution studied by pulse radiolysis,” The Journal of Physical Chemistry, vol. 88, no. 10, pp. 2091–2095, 1984. View at Publisher · View at Google Scholar · View at Scopus
  21. W. A. Prütz, H. Mönig, J. Butler, and E. J. Land, “Reactions of nitrogen dioxide in aqueous model systems: oxidation of tyrosine units in peptides and proteins,” Archives of Biochemistry and Biophysics, vol. 243, no. 1, pp. 125–134, 1985. View at Publisher · View at Google Scholar · View at Scopus
  22. O. Augusto, M. G. Bonini, A. M. Amanso, E. Linares, C. C. X. Santos, and S. L. de Menezes, “Nitrogen dioxide and carbonate radical anion: two emerging radicals in biology,” Free Radical Biology and Medicine, vol. 32, no. 9, pp. 841–859, 2002. View at Publisher · View at Google Scholar · View at Scopus
  23. L. K. Folkes, S. Bartesaghi, M. Trujillo, R. Radi, and P. Wardman, “Kinetics of oxidation of tyrosine by a model alkoxyl radical,” Free Radical Research, vol. 46, no. 9, pp. 1150–1156, 2012. View at Publisher · View at Google Scholar · View at Scopus
  24. S. Bartesaghi, J. Wenzel, M. Trujillo et al., “Lipid peroxyl radicals mediate tyrosine dimerization and nitration in membranes,” Chemical Research in Toxicology, vol. 23, no. 4, pp. 821–835, 2010. View at Publisher · View at Google Scholar · View at Scopus
  25. M. Tien, “Myeloperoxidase-catalyzed oxidation of tyrosine,” Archives of Biochemistry and Biophysics, vol. 367, no. 1, pp. 61–66, 1999. View at Publisher · View at Google Scholar · View at Scopus
  26. L. A. Marquez and H. B. Dunford, “Kinetics of oxidation of tyrosine and dityrosine by myeloperoxidase compounds I and II: implications for lipoprotein peroxidation studies,” Journal of Biological Chemistry, vol. 270, no. 51, pp. 30434–30440, 1995. View at Publisher · View at Google Scholar · View at Scopus
  27. A. van der Vliet, J. P. Eiserich, B. Halliwell, and C. E. Cross, “Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite: a potential additional mechanism of nitric oxide- dependent toxicity,” The Journal of Biological Chemistry, vol. 272, no. 12, pp. 7617–7625, 1997. View at Publisher · View at Google Scholar · View at Scopus
  28. H. F. G. Heijnen, E. van Donselaar, J. W. Slot et al., “Subcellular localization of tyrosine-nitrated proteins is dictated by reactive oxygen species generating enzymes and by proximity to nitric oxide synthase,” Free Radical Biology and Medicine, vol. 40, no. 11, pp. 1903–1913, 2006. View at Publisher · View at Google Scholar · View at Scopus
  29. B. Lassègue and K. K. Griendling, “NADPH oxidases: functions and pathologies in the vasculature,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 30, no. 4, pp. 653–661, 2010. View at Publisher · View at Google Scholar · View at Scopus
  30. G. Csányi, W. R. Taylor, and P. J. Pagano, “NOX and inflammation in the vascular adventitia,” Free Radical Biology and Medicine, vol. 47, no. 9, pp. 1254–1266, 2009. View at Publisher · View at Google Scholar · View at Scopus
  31. B. Lassègue and R. E. Clempus, “Vascular NAD(P)H oxidases: specific features, expression, and regulation,” The American Journal of Physiology—Regulatory Integrative and Comparative Physiology, vol. 285, no. 2, pp. R277–R297, 2003. View at Google Scholar · View at Scopus
  32. A. H. Chamseddine and F. J. Miller Jr., “gp91phox contributes to NADPH oxidase activity in aortic fibroblasts but not smooth muscle cells,” The American Journal of Physiology—Heart and Circulatory Physiology, vol. 285, no. 6, pp. H2284–H2289, 2003. View at Google Scholar · View at Scopus
  33. B. Lassègue, A. S. Martín, and K. K. Griendling, “Biochemistry, physiology, and pathophysiology of NADPH oxidases in the cardiovascular system,” Circulation Research, vol. 110, no. 10, pp. 1364–1390, 2012. View at Publisher · View at Google Scholar · View at Scopus
  34. A. N. Lyle, N. N. Deshpande, Y. Taniyama et al., “Poldip2, a novel regulator of Nox4 and cytoskeletal integrity in vascular smooth muscle cells,” Circulation Research, vol. 105, no. 3, pp. 249–259, 2009. View at Publisher · View at Google Scholar · View at Scopus
  35. A. El Jamali, A. J. Valente, J. D. Lechleiter et al., “Novel redox-dependent regulation of NOX5 by the tyrosine kinase c-Abl,” Free Radical Biology and Medicine, vol. 44, no. 5, pp. 868–881, 2008. View at Publisher · View at Google Scholar · View at Scopus
  36. R. Radi, H. Rubbo, L. Thomson, and E. Prodanov, “Luminol chemiluminescence using xanthine and hypoxanthine as xanthine oxidase substrates,” Free Radical Biology and Medicine, vol. 8, no. 2, pp. 121–126, 1990. View at Publisher · View at Google Scholar · View at Scopus
  37. M. Aslan and B. A. Freeman, “Oxidases and oxygenases in regulation of vascular nitric oxide signaling and inflammatory responses,” Immunologic Research, vol. 26, no. 1–3, pp. 107–118, 2002. View at Publisher · View at Google Scholar · View at Scopus
  38. M. Houston, A. Estevez, P. Chumley et al., “Binding of xanthine oxidase to vascular endothelium. Kinetic characterization and oxidative impairment of nitric oxide-dependent signaling,” Journal of Biological Chemistry, vol. 274, no. 8, pp. 4985–4994, 1999. View at Publisher · View at Google Scholar · View at Scopus
  39. A. J. Kowaltowski, N. C. de Souza-Pinto, R. F. Castilho, and A. E. Vercesi, “Mitochondria and reactive oxygen species,” Free Radical Biology and Medicine, vol. 47, no. 4, pp. 333–343, 2009. View at Publisher · View at Google Scholar · View at Scopus
  40. S. Dröse and U. Brandt, “Molecular mechanisms of superoxide production by the mitochondrial respiratory chain,” Advances in Experimental Medicine and Biology, vol. 748, pp. 145–169, 2012. View at Publisher · View at Google Scholar · View at Scopus
  41. K. Bedard, B. Lardy, and K.-H. Krause, “NOX family NADPH oxidases: not just in mammals,” Biochimie, vol. 89, no. 9, pp. 1107–1112, 2007. View at Publisher · View at Google Scholar · View at Scopus
  42. U. Förstermann and W. C. Sessa, “Nitric oxide synthases: regulation and function,” European Heart Journal, vol. 33, no. 7, pp. 829–837, 2012. View at Publisher · View at Google Scholar · View at Scopus
  43. C. J. Lowenstein and E. Padalko, “iNOS (NOS2) at a glance,” Journal of Cell Science, vol. 117, pp. 2865–2867, 2004. View at Publisher · View at Google Scholar
  44. S. J. Klebanoff, “Oxygen metabolism and the toxic properties of phagocytes,” Annals of Internal Medicine, vol. 93, no. 3, pp. 480–489, 1980. View at Publisher · View at Google Scholar · View at Scopus
  45. S. L. Hazen, R. Zhang, Z. Shen et al., “Formation of nitric oxide-derived oxidants by myeloperoxidase in monocytes: pathways for monocyte-mediated protein nitration and lipid peroxidation In vivo,” Circulation Research, vol. 85, no. 10, pp. 950–958, 1999. View at Publisher · View at Google Scholar · View at Scopus
  46. A. Daugherty, J. L. Dunn, D. L. Rateri, and J. W. Heinecke, “Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions,” Journal of Clinical Investigation, vol. 94, no. 1, pp. 437–444, 1994. View at Publisher · View at Google Scholar · View at Scopus
  47. M.-L. Brennan, M. S. Penn, F. Van Lente et al., “Prognostic value of myeloperoxidase in patients with chest pain,” The New England Journal of Medicine, vol. 349, no. 17, pp. 1595–1604, 2003. View at Publisher · View at Google Scholar · View at Scopus
  48. S. J. Nicholls, W. H. Wilson Tang, D. Brennan et al., “Risk prediction with serial myeloperoxidase monitoring in patients with acute chest pain,” Clinical Chemistry, vol. 57, no. 12, pp. 1762–1770, 2011. View at Publisher · View at Google Scholar · View at Scopus
  49. M. C. Meuwese, E. S. G. Stroes, S. L. Hazen et al., “Serum myeloperoxidase levels are associated with the future risk of coronary artery disease in apparently healthy individuals: the EPIC-Norfolk Prospective Population Study,” Journal of the American College of Cardiology, vol. 50, no. 2, pp. 159–165, 2007. View at Publisher · View at Google Scholar · View at Scopus
  50. J. S. Rana, B. J. Arsenault, J.-P. Després et al., “Inflammatory biomarkers, physical activity, waist circumference, and risk of future coronary heart disease in healthy men and women,” European Heart Journal, vol. 32, no. 3, pp. 336–344, 2011. View at Publisher · View at Google Scholar · View at Scopus
  51. W. H. W. Tang, Y. Wu, S. J. Nicholls, and S. L. Hazen, “Plasma myeloperoxidase predicts incident cardiovascular risks in stable patients undergoing medical management for coronary artery disease,” Clinical Chemistry, vol. 57, no. 1, pp. 33–39, 2011. View at Publisher · View at Google Scholar · View at Scopus
  52. S. Sugiyama, K. Kugiyama, M. Aikawa, S. Nakamura, H. Ogawa, and P. Libby, “Hypochlorous acid, a macrophage product, induces endothelial apoptosis and tissue factor expression: involvement of myeloperoxidase-mediated oxidant in plaque erosion and thrombogenesis,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 24, no. 7, pp. 1309–1314, 2004. View at Publisher · View at Google Scholar · View at Scopus
  53. S. Sugiyama, Y. Okada, G. K. Sukhova, R. Virmani, J. W. Heinecke, and P. Libby, “Macrophage myeloperoxidase regulation by granulocyte macrophage colony-stimulating factor in human atherosclerosis and implications in acute coronary syndromes,” The American Journal of Pathology, vol. 158, no. 3, pp. 879–891, 2001. View at Publisher · View at Google Scholar · View at Scopus
  54. M. H. Shishehbor, R. J. Aviles, M.-L. Brennan et al., “Association of nitrotyrosine levels with cardiovascular disease and modulation by statin therapy,” Journal of the American Medical Association, vol. 289, no. 13, pp. 1675–1680, 2003. View at Publisher · View at Google Scholar · View at Scopus
  55. I. Parastatidis, L. Thomson, A. Burke et al., “Fibrinogen β-chain tyrosine nitration is a prothrombotic risk factor,” The Journal of Biological Chemistry, vol. 283, no. 49, pp. 33846–33853, 2008. View at Publisher · View at Google Scholar · View at Scopus
  56. M. Martinez, A. Cuker, A. Mills et al., “Nitrated fibrinogen is a biomarker of oxidative stress in venous thromboembolism,” Free Radical Biology and Medicine, vol. 53, no. 2, pp. 230–236, 2012. View at Publisher · View at Google Scholar · View at Scopus
  57. L. Zheng, B. Nukuna, M. L. Brennan et al., “Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and function impairment in subjects with cardiovascular disease,” Journal of Clinical Investigation, vol. 114, no. 4, pp. 529–541, 2004. View at Publisher · View at Google Scholar · View at Scopus
  58. S. J. Nicholls and S. L. Hazen, “Myeloperoxidase, modified lipoproteins, and atherogenesis,” The Journal of Lipid Research, vol. 50, supplement, pp. S346–S351, 2009. View at Publisher · View at Google Scholar · View at Scopus
  59. L. Zheng, M. Settle, G. Brubaker et al., “Localization of nitration and chlorination sites on apolipoprotein A-I catalysed by myeloperoxidase in human atheroma and associated oxidative impairment in ABCA1-dependent cholesterol efflux from macrophages,” Journal of Biological Chemistry, vol. 280, no. 1, pp. 38–47, 2005. View at Publisher · View at Google Scholar · View at Scopus
  60. Y. Kataoka, M. Shao, K. Wolski et al., “Myeloperoxidase levels predict accelerated progression of coronary atherosclerosis in diabetic patients: insights from intravascular ultrasound,” Atherosclerosis, vol. 232, no. 2, pp. 377–383, 2014. View at Publisher · View at Google Scholar · View at Scopus
  61. B. Shao, C. Tang, A. Sinha et al., “Humans with atherosclerosis have impaired ABCA1 cholesterol efflux and enhanced high-density lipoprotein oxidation by myeloperoxidase,” Circulation Research, vol. 114, no. 11, pp. 1733–1742, 2014. View at Publisher · View at Google Scholar · View at Scopus
  62. M. Navab, S. T. Reddy, B. J. van Lenten, and A. M. Fogelman, “HDL and cardiovascular disease: atherogenic and atheroprotective mechanisms,” Nature Reviews Cardiology, vol. 8, no. 4, pp. 222–232, 2011. View at Publisher · View at Google Scholar · View at Scopus
  63. B. Shao, G. Cavigiolio, N. Brot, M. N. Oda, and J. W. Heinecke, “Methionine oxidation impairs reverse cholesterol transport by apolipoprotein A-I,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 34, pp. 12224–12229, 2008. View at Publisher · View at Google Scholar · View at Scopus
  64. Z. Wu, M. A. Wagner, L. Zheng et al., “The refined structure of nascent HDL reveals a key functional domain for particle maturation and dysfunction,” Nature Structural and Molecular Biology, vol. 14, pp. 861–868, 2007. View at Google Scholar
  65. B. Pan, B. Yu, H. Ren et al., “High-density lipoprotein nitration and chlorination catalyzed by myeloperoxidase impair its effect of promoting endothelial repair,” Free Radical Biology and Medicine, vol. 60, pp. 272–281, 2013. View at Publisher · View at Google Scholar · View at Scopus
  66. A. Urundhati, Y. Huang, J. A. Lupica, J. D. Smith, J. A. DiDonato, and S. L. Hazen, “Modification of high density lipoprotein by myeloperoxidase generates a pro-inflammatory particle,” Journal of Biological Chemistry, vol. 284, no. 45, pp. 30825–30835, 2009. View at Publisher · View at Google Scholar · View at Scopus
  67. T. K. Hsiai, J. Hwang, M. L. Barr et al., “Hemodynamics influences vascular peroxynitrite formation: implication for low-density lipoprotein apo-B-100 nitration,” Free Radical Biology and Medicine, vol. 42, no. 4, pp. 519–529, 2007. View at Publisher · View at Google Scholar · View at Scopus
  68. S. Chakraborty, Y. Cai, and M. A. Tarr, “In vitro oxidative footprinting provides insight into apolipoprotein B-100 structure in low-density lipoprotein,” Proteomics, vol. 14, pp. 2614–2622, 2014. View at Google Scholar
  69. R. T. Hamilton, L. Asatryan, J. T. Nilsen et al., “LDL protein nitration: implication for LDL protein unfolding,” Archives of Biochemistry and Biophysics, vol. 479, no. 1, pp. 1–14, 2008. View at Publisher · View at Google Scholar · View at Scopus
  70. E. A. Podrez, D. Schmitt, H. F. Hoff, and S. L. Hazen, “Myeloperoxidase-generated reactive nitrogen species convert LDL into an atherogenic form in vitro,” The Journal of Clinical Investigation, vol. 103, no. 11, pp. 1547–1560, 1999. View at Publisher · View at Google Scholar · View at Scopus
  71. S. P. Heffron, I. Parastatidis, M. Cuchel et al., “Inflammation induces fibrinogen nitration in experimental human endotoxemia,” Free Radical Biology and Medicine, vol. 47, no. 8, pp. 1140–1146, 2009. View at Publisher · View at Google Scholar · View at Scopus
  72. C. Vadseth, J. M. Souza, L. Thomson et al., “Pro-thrombotic state induced by post-translational modification of fibrinogen by reactive nitrogen species,” Journal of Biological Chemistry, vol. 279, no. 10, pp. 8820–8826, 2004. View at Publisher · View at Google Scholar · View at Scopus
  73. L. Thomson, J. Christie, C. Vadseth et al., “Identification of immunoglobulins that recognize 3-nitrotyrosine in patients with acute lung injury after major trauma,” The American Journal of Respiratory Cell and Molecular Biology, vol. 36, no. 2, pp. 152–157, 2007. View at Publisher · View at Google Scholar · View at Scopus
  74. G. Peluffo and R. Radi, “Biochemistry of protein tyrosine nitration in cardiovascular pathology,” Cardiovascular Research, vol. 75, no. 2, pp. 291–302, 2007. View at Publisher · View at Google Scholar · View at Scopus
  75. R. S. Vasan, “Biomarkers of cardiovascular disease: molecular basis and practical considerations,” Circulation, vol. 113, no. 19, pp. 2335–2362, 2006. View at Publisher · View at Google Scholar · View at Scopus
  76. P. Artimo, M. Jonnalagedda, K. Arnold et al., “ExPASy: SIB bioinformatics resource portal,” Nucleic Acids Research, vol. 40, no. 1, pp. W597–W603, 2012. View at Publisher · View at Google Scholar · View at Scopus
  77. J. A. DiDonato, K. Aulak, Y. Huang et al., “Site-specific nitration of apolipoprotein A-I at tyrosine 166 is both abundant within human atherosclerotic plaque and dysfunctional,” The Journal of Biological Chemistry, vol. 289, no. 15, pp. 10276–10292, 2014. View at Publisher · View at Google Scholar · View at Scopus
  78. B. Shao, M. N. Oda, J. F. Oram, and J. W. Heinecke, “Myeloperoxidase: an oxidative pathway for generating dysfunctional high-density lipoprotein,” Chemical Research in Toxicology, vol. 23, no. 3, pp. 447–454, 2010. View at Publisher · View at Google Scholar · View at Scopus
  79. B. Shao, C. Bergt, X. Fu et al., “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,” The Journal of Biological Chemistry, vol. 280, no. 7, pp. 5983–5993, 2005. View at Publisher · View at Google Scholar · View at Scopus