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Cholesterol
Volume 2015 (2015), Article ID 296417, 22 pages
http://dx.doi.org/10.1155/2015/296417
Review Article

Dysfunctional High-Density Lipoprotein: An Innovative Target for Proteomics and Lipidomics

Endocrine-Metabolic Research Center, “Dr. Félix Gómez,” Faculty of Medicine, University of Zulia, Zulia State, Maracaibo 4004, Venezuela

Received 23 August 2015; Revised 12 October 2015; Accepted 12 October 2015

Academic Editor: Matti Jauhiainen

Copyright © 2015 Juan Salazar et al. 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. WHO, “The top ten causes of death. Fact sheet 310,” 2011, http://www.who.int/mediacentre/factsheets/fs310_2008.pdf.
  2. C. J. O'Donell and R. Elosua, “CVR factors. Insights from Framingham Heart Study,” Revista Española de Cardiología, vol. 61, no. 3, pp. 299–310, 2008. View at Google Scholar
  3. J. Millán, X. Pintó, A. Muñoz et al., “Lipoprotein ratios: physiological significance and clinical usefulness in cardiovascular prevention,” Vascular Health and Risk Management, vol. 5, pp. 757–765, 2009. View at Google Scholar · View at Scopus
  4. World Health Organization, Report on the Global Tobacco Epidemic 2011: Warning about the Dangers of Tobacco, World Health Organization, Geneva, Switzerland, 2011, http://www.who.int/tobacco/global_report/2011/en/.
  5. K. K. Ray, J. J. P. Kastelein, S. M. Boekholdt et al., “The ACC/AHA 2013 guideline on the treatment of blood cholesterol to reduce atherosclerotic cardiovascular disease risk in adults: the good the bad and the uncertain: a comparison with ESC/EAS guidelines for the management of dyslipidaemias 2011,” European Heart Journal, vol. 35, no. 15, pp. 960–968, 2014. View at Publisher · View at Google Scholar · View at Scopus
  6. P. Barter, A. M. Gotto, J. C. LaRosa et al., “HDL cholesterol, very low levels of LDL cholesterol, and cardiovascular events,” The New England Journal of Medicine, vol. 357, no. 13, pp. 1301–1310, 2007. View at Publisher · View at Google Scholar · View at Scopus
  7. A. Kontush and M. J. Chapman, “Antiatherogenic small, dense HDL—guardian angel of the arterial wall?” Nature Clinical Practice Cardiovascular Medicine, vol. 3, no. 3, pp. 144–153, 2006. View at Publisher · View at Google Scholar · View at Scopus
  8. S. Lund-Katz and M. C. Phillips, “High density lipoprotein structure-function and role in reverse cholesterol transport,” Sub-Cellular Biochemistry, vol. 51, pp. 183–227, 2010. View at Publisher · View at Google Scholar · View at Scopus
  9. L. Camont, M. J. Chapman, and A. Kontush, “Biological activities of HDL subpopulations and their relevance to cardiovascular disease,” Trends in Molecular Medicine, vol. 17, no. 10, pp. 594–603, 2011. View at Publisher · View at Google Scholar · View at Scopus
  10. W. P. Castelli, J. T. Doyle, T. Gordon et al., “HDL cholesterol and other lipids in coronary heart disease. The cooperative lipoprotein phenotyping study,” Circulation, vol. 55, no. 5, pp. 767–772, 1977. View at Publisher · View at Google Scholar · View at Scopus
  11. T. Gordon, W. P. Castelli, M. C. Hjortland, W. B. Kannel, and T. R. Dawber, “High density lipoprotein as a protective factor against coronary heart disease: the Framingham study,” The American Journal of Medicine, vol. 62, no. 5, pp. 707–714, 1977. View at Publisher · View at Google Scholar · View at Scopus
  12. P. W. F. Wilson, R. D. Abbott, and W. P. Castelli, “High density lipoprotein cholesterol and mortality. The Framingham Heart Study,” Arteriosclerosis, vol. 8, no. 6, pp. 737–741, 1988. View at Publisher · View at Google Scholar · View at Scopus
  13. J. A. Kuivenhoven, H. Pritchard, J. Hill, J. Frohlich, G. Assmann, and J. Kastelein, “The molecular pathology of lecithin: cholesterol acyltransferase (LCAT) deficiency syndromes,” Journal of Lipid Research, vol. 38, no. 2, pp. 191–205, 1997. View at Google Scholar · View at Scopus
  14. G. Franceschini, C. R. Sirtori, A. Capurso, K. H. Weisgraber, and R. W. Mahley, “A-I Milano apoprotein: decreased high density lipoprotein cholesterol levels with significant lipoprotein modifications and without clinical atherosclerosis in an Italian family,” The Journal of Clinical Investigation, vol. 66, no. 5, pp. 892–900, 1980. View at Google Scholar
  15. E. Bruckert, A. von Eckardstein, H. Funke et al., “The replacement of arginine by cysteine at residue 151 in apolipoprotein A-I produces a phenotype similar to that of apolipoprotein A-I Milano,” Atherosclerosis, vol. 128, no. 1, pp. 121–128, 1997. View at Publisher · View at Google Scholar · View at Scopus
  16. P. J. Barter, M. Caulfield, M. Eriksson et al., “Effects of torcetrapib in patients at high risk for coronary events,” The New England Journal of Medicine, vol. 357, no. 21, pp. 2109–2122, 2007. View at Publisher · View at Google Scholar · View at Scopus
  17. E. Eren, N. Yilmaz, and O. Aydin, “High density lipoprotein and it's dysfunction,” Open Biochemistry Journal, vol. 6, pp. 78–93, 2012. View at Publisher · View at Google Scholar · View at Scopus
  18. G. Schonfeld and B. Pfleger, “The structure of human high density lipoprotein and the levels of apolipoprotein A-I in plasma as determined by radioimmunoassay,” The Journal of Clinical Investigation, vol. 54, no. 2, pp. 236–246, 1974. View at Publisher · View at Google Scholar · View at Scopus
  19. L. S. Kumpula, J. M. Kumpula, M.-R. Taskinen, M. Jauhiainen, K. Kaski, and M. R. Ala-Korpela, “Reconsideration of hydrophobic lipid distributions in lipoprotein particles,” Chemistry and Physics of Lipids, vol. 155, no. 1, pp. 57–62, 2008. View at Publisher · View at Google Scholar · View at Scopus
  20. M. G. Sorci-Thomas, S. Bhat, and M. J. Thomas, “Activation of lecithin: cholesterol acyltransferase by HDL ApoA-I central helices,” Clinical Lipidology, vol. 4, no. 1, pp. 113–124, 2009. View at Publisher · View at Google Scholar · View at Scopus
  21. L. Zhang, F. Yan, S. Zhang et al., “Structural basis of transfer between lipoproteins by cholesteryl ester transfer protein,” Nature Chemical Biology, vol. 8, no. 4, pp. 342–349, 2012. View at Publisher · View at Google Scholar · View at Scopus
  22. H.-O. Mowri, J. R. Patsch, A. Ritsch, B. Foger, S. Brown, and W. Patsch, “High density lipoproteins with differing apolipoproteins: relationships to postprandial lipemia, cholesteryl ester transfer protein, and activities of lipoprotein lipase, hepatic lipase, and lecithin: cholesterol acyltransferase,” Journal of Lipid Research, vol. 35, no. 2, pp. 291–299, 1994. View at Google Scholar · View at Scopus
  23. A. Jonas, “Lipoprotein structure,” in Biochemistry of Lipids, Lipoproteins and Membranes, Elsevier, Amsterdam, The Netherlands, 4th edition, 2002. View at Google Scholar
  24. H. B. Brewer Jr. and S. Santamarina-Fojo, “Clinical significance of high-density lipoproteins and the development of atherosclerosis: focus on the role of the adenosine triphosphate-binding cassette protein A1 transporter,” The American Journal of Cardiology, vol. 92, no. 4, pp. 0K–16K, 2003. View at Google Scholar · View at Scopus
  25. S. Kunnen and M. Van Eck, “Lecithin: cholesterol acyltransferase: old friend or foe in atherosclerosis?” Journal of Lipid Research, vol. 53, no. 9, pp. 1783–1799, 2012. View at Publisher · View at Google Scholar · View at Scopus
  26. K.-A. Rye, C. A. Bursill, G. Lambert, F. Tabet, and P. J. Barter, “The metabolism and anti-atherogenic properties of HDL,” Journal of Lipid Research, vol. 50, supplement, pp. S195–S200, 2009. View at Publisher · View at Google Scholar · View at Scopus
  27. D. Bailey, I. Ruel, A. Hafiane et al., “Analysis of lipid transfer activity between model nascent HDL particles and plasma lipoproteins: implications for current concepts of nascent HDL maturation and genesis,” Journal of Lipid Research, vol. 51, no. 4, pp. 785–797, 2010. View at Publisher · View at Google Scholar · View at Scopus
  28. M. Jauhiainen, J. Metso, R. Pahlman, S. Blomqvist, A. Van Tol, and C. Ehnholm, “Human plasma phospholipid transfer protein causes high density lipoprotein conversion,” Journal of Biological Chemistry, vol. 268, no. 6, pp. 4032–4036, 1993. View at Google Scholar · View at Scopus
  29. S. Lusa, M. Jauhiainen, J. Metso, P. Somerharju, and C. Ehnholm, “The mechanism of human plasma phospholipid transfer protein-induced enlargement of high-density lipoprotein particles: evidence for particle fusion,” Biochemical Journal, vol. 313, no. 1, pp. 275–282, 1996. View at Publisher · View at Google Scholar · View at Scopus
  30. G. Wolfbauer, J. J. Albers, and J. F. Oram, “Phospholipid transfer protein enhances removal of cellular cholesterol and phospholipids by high-density lipoprotein apolipoproteins,” Biochimica et Biophysica Acta, vol. 1439, no. 1, pp. 65–76, 1999. View at Publisher · View at Google Scholar · View at Scopus
  31. J. Huuskonen, V. M. Olkkonen, C. Ehnholm, J. Metso, I. Julkunen, and M. Jauhiainen, “Phospholipid transfer is a prerequisite for PLTP-mediated HDL conversion,” Biochemistry, vol. 39, no. 51, pp. 16092–16098, 2000. View at Publisher · View at Google Scholar · View at Scopus
  32. J. F. Oram, G. Wolfbauer, C. Tang, W. S. Davidson, and J. J. Albers, “An amphipathic helical region of the N-terminal barrel of phospholipid transfer protein is critical for ABCA1-dependent cholesterol efflux,” The Journal of Biological Chemistry, vol. 283, no. 17, pp. 11541–11549, 2008. View at Publisher · View at Google Scholar · View at Scopus
  33. C. J. Fielding and P. E. Fielding, “Molecular physiology of reverse cholesterol transport,” Journal of Lipid Research, vol. 36, no. 2, pp. 211–228, 1995. View at Google Scholar · View at Scopus
  34. M. J. Chapman, W. Le Goff, M. Guerin, and A. Kontush, “Cholesteryl ester transfer protein: at the heart of the action of lipid-modulating therapy with statins, fibrates, niacin, and cholesteryl ester transfer protein inhibitors,” European Heart Journal, vol. 31, no. 2, pp. 149–164, 2010. View at Publisher · View at Google Scholar · View at Scopus
  35. H. Mabuchi, A. Nohara, and A. Inazu, “Cholesteryl ester transfer protein (CETP) deficiency and CETP inhibitors,” Molecules and Cells, vol. 37, no. 11, pp. 777–784, 2014. View at Publisher · View at Google Scholar
  36. T. Yasuda, T. Ishida, and D. J. Rader, “Update on the role of endothelial lipase in high-density lipoprotein metabolism, reverse cholesterol transport, and atherosclerosis,” Circulation Journal, vol. 74, no. 11, pp. 2263–2270, 2010. View at Publisher · View at Google Scholar · View at Scopus
  37. B. Trigatti, S. Covey, and A. Rizvi, “Scavenger receptor class B type I in high-density lipoprotein metabolism, atherosclerosis and heart disease: Lessons from gene-targeted mice,” Biochemical Society Transactions, vol. 32, part 1, pp. 116–120, 2004. View at Publisher · View at Google Scholar · View at Scopus
  38. G. F. Lewis and D. J. Rader, “New insights into the regulation of HDL metabolism and reverse cholesterol transport,” Circulation Research, vol. 96, no. 12, pp. 1221–1232, 2005. View at Publisher · View at Google Scholar · View at Scopus
  39. D. L. Silver, N. Wang, X. Xiao, and A. R. Tall, “High density lipoprotein (HDL) particle uptake mediated by scavenger receptor class B type 1 results in selective sorting of HDL cholesterol from protein and polarized cholesterol secretion,” Journal of Biological Chemistry, vol. 276, no. 27, pp. 25287–25293, 2001. View at Publisher · View at Google Scholar · View at Scopus
  40. T. A. Pagler, S. Rhode, A. Neuhofer et al., “SR-BI-mediated high density lipoprotein (HDL) endocytosis leads to HDL resecretion facilitating cholesterol efflux,” The Journal of Biological Chemistry, vol. 281, no. 16, pp. 11193–11204, 2006. View at Publisher · View at Google Scholar · View at Scopus
  41. R. Alam, F. M. Yatsu, L. Tsui, and S. Alam, “Receptor-mediated uptake and ‘retroendocytosis’ of high-density lipoproteins by cholesterol-loaded human monocyte-derived macrophages: possible role in enhancing reverse cholesterol transport,” Biochimica et Biophysica Acta, vol. 1004, no. 3, pp. 292–299, 1989. View at Publisher · View at Google Scholar · View at Scopus
  42. S. Rhode, A. Breuer, J. Hesse et al., “Visualization of the uptake of individual HDL particles in living cells via the scavenger receptor class B type I,” Cell Biochemistry and Biophysics, vol. 41, no. 3, pp. 343–356, 2004. View at Publisher · View at Google Scholar · View at Scopus
  43. B. Sun, E. R. M. Eckhardt, S. Shetty, D. R. van der Westhuyzen, and N. R. Webb, “Quantitative analysis of SR-BI-dependent HDL retroendocytosis in hepatocytes and fibroblasts,” Journal of Lipid Research, vol. 47, no. 8, pp. 1700–1713, 2006. View at Publisher · View at Google Scholar · View at Scopus
  44. E. Di Angelantonio, N. Sarwar, P. Perry et al., “Major lipids, apolipoproteins, and risk of vascular disease,” Journal of the American Medical Association, vol. 302, no. 18, pp. 1993–2000, 2009. View at Publisher · View at Google Scholar · View at Scopus
  45. G. Assmann, H. Schulte, A. Von Eckardstein, and Y. Huang, “High-density lipoprotein cholesterol as a predictor of coronary heart disease risk. The PROCAM experience and pathophysiological implications for reverse cholesterol transport,” Atherosclerosis, vol. 124, supplement, pp. S11–S20, 1996. View at Publisher · View at Google Scholar · View at Scopus
  46. G. Assmann, P. Cullen, and H. Schulte, “The Münster heart study (PROCAM). Results of follow-up at 8 years,” European Heart Journal, vol. 19, supplement A, pp. A2–A11, 1998. View at Google Scholar
  47. P. S. Yusuf, S. Hawken, S. Ôunpuu et al., “Effect of potentially modifiable risk factors associated with myocardial infarction in 52 countries (the INTERHEART study): case-control study,” The Lancet, vol. 364, no. 9438, pp. 937–952, 2004. View at Publisher · View at Google Scholar · View at Scopus
  48. M. E. Brousseau, E. J. Schaefer, M. L. Wolfe et al., “Effects of an inhibitor of cholesteryl ester transfer protein on HDL cholesterol,” The New England Journal of Medicine, vol. 350, no. 15, pp. 1505–1515, 2004. View at Publisher · View at Google Scholar · View at Scopus
  49. S. E. Nissen, J.-C. Tardif, S. J. Nicholls et al., “Effect of torcetrapib on the progression of coronary atherosclerosis,” The New England Journal of Medicine, vol. 356, no. 13, pp. 1304–1316, 2007. View at Publisher · View at Google Scholar · View at Scopus
  50. J. J. P. Kastelein, S. I. Van Leuven, L. Burgess et al., “Effect of torcetrapib on carotid atherosclerosis in familial hypercholesterolemia,” The New England Journal of Medicine, vol. 356, no. 16, pp. 1620–1630, 2007. View at Publisher · View at Google Scholar · View at Scopus
  51. M. Vergeer, M. L. Bots, S. I. Van Leuven et al., “Cholesteryl ester transfer protein inhibitor torcetrapib and off-target toxicity: a pooled analysis of the rating atherosclerotic disease change by imaging with a new CETP inhibitor (RADIANCE) trials,” Circulation, vol. 118, no. 24, pp. 2515–2522, 2008. View at Publisher · View at Google Scholar · View at Scopus
  52. C. P. Cannon, H. M. Dansky, M. Davidson et al., “Design of the DEFINE trial: determining the efficacy and tolerability of CETP inhibition with anacetrapib,” American Heart Journal, vol. 158, no. 4, pp. 513.e3–519.e3, 2009. View at Publisher · View at Google Scholar · View at Scopus
  53. J. M. Peacock, D. K. Arnett, L. D. Atwood et al., “Genome scan for quantitative trait loci linked to high-density lipoprotein cholesterol: the NHLBI Family Heart Study,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 21, no. 11, pp. 1823–1828, 2001. View at Publisher · View at Google Scholar · View at Scopus
  54. X. Wang and B. Paigen, “Genome-wide search for new genes controlling plasma lipid concentrations in mice and humans,” Current Opinion in Lipidology, vol. 16, no. 2, pp. 127–137, 2005. View at Publisher · View at Google Scholar · View at Scopus
  55. C. F. Sing, J. H. Stengard, and S. L. R. Kardia, “Genes, environment and cardiovascular disease,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 23, pp. 1190–1196, 2003. View at Google Scholar
  56. A. von Eckardstein, “Differential diagnosis of familial high density lipoprotein deficiency syndromes,” Atherosclerosis, vol. 186, no. 2, pp. 231–239, 2006. View at Publisher · View at Google Scholar · View at Scopus
  57. G. Franceschini, C. R. Sirtori, E. Bosisio et al., “Relationship of the phenotypic expression of the A-I Milano apoprotein with plasma lipid and lipoprotein patterns,” Atherosclerosis, vol. 58, no. 1–3, pp. 159–174, 1985. View at Publisher · View at Google Scholar · View at Scopus
  58. G. Chiesa and C. R. Sirtori, “Apolipoprotein A-IMilano: current perspectives,” Current Opinion in Lipidology, vol. 14, no. 2, pp. 159–163, 2003. View at Publisher · View at Google Scholar · View at Scopus
  59. J. F. Oram and J. W. Heinecke, “ATP-binding cassette transporter A1: a cell cholesterol exporter that protects against cardiovascular disease,” Physiological Reviews, vol. 85, no. 4, pp. 1343–1372, 2005. View at Publisher · View at Google Scholar · View at Scopus
  60. J. L. Benton, J. Ding, M. Y. Tsai et al., “Associations between two common polymorphisms in the ABCA1 gene and subclinical atherosclerosis. Multi-Ethnic Study of Atherosclerosis (MESA),” Atherosclerosis, vol. 193, no. 2, pp. 352–360, 2007. View at Publisher · View at Google Scholar · View at Scopus
  61. R. V. Andersen, H. H. Wittrup, A. Tybjærg-Hansen, R. Steffensen, P. Schnohr, and B. G. Nordestgaard, “Hepatic lipase mutations,elevated high-density lipoprotein cholesterol, and increased risk of ischemic heart disease: the Copenhagen City Heart Study,” Journal of the American College of Cardiology, vol. 41, no. 11, pp. 1972–1982, 2003. View at Publisher · View at Google Scholar · View at Scopus
  62. B. F. Voight, G. M. Peloso, M. Orho-Melander et al., “Plasma HDL cholesterol and risk of myocardial infarction: a mendelian randomisation study,” The Lancet, vol. 380, no. 9841, pp. 572–580, 2012. View at Publisher · View at Google Scholar · View at Scopus
  63. C. L. Haase, R. Frikke-Schmidt, B. G. Nordestgaard et al., “Mutation in APOA1 predicts increased risk of ischaemic heart disease and total mortality without low HDL cholesterol levels,” Journal of Internal Medicine, vol. 270, no. 2, pp. 136–146, 2011. View at Publisher · View at Google Scholar · View at Scopus
  64. V. I. Zannis, A. Chroni, and M. Krieger, “Role of apoA-I, ABCA1, LCAT, and SR-BI in the biogenesis of HDL,” Journal of Molecular Medicine, vol. 84, no. 4, pp. 276–294, 2006. View at Publisher · View at Google Scholar · View at Scopus
  65. A. Rohatgi, A. Khera, J. D. Berry et al., “HDL cholesterol efflux capacity and incident cardiovascular events,” The New England Journal of Medicine, vol. 371, no. 25, pp. 2383–2393, 2014. View at Publisher · View at Google Scholar · View at Scopus
  66. T. Vaisar, S. Pennathur, P. S. Green et al., “Shotgun proteomics implicates protease inhibition and complement activation in the antiinflammatory properties of HDL,” The Journal of Clinical Investigation, vol. 117, no. 3, pp. 746–756, 2007. View at Publisher · View at Google Scholar · View at Scopus
  67. A. M. Shiflett, J. R. Bishop, A. Pahwa, and S. L. Hajduk, “Human high density lipoproteins are platforms for the assembly of multi-component innate immune complexes,” Journal of Biological Chemistry, vol. 280, no. 38, pp. 32578–32585, 2005. View at Publisher · View at Google Scholar · View at Scopus
  68. E. J. Reschly, M. G. Sorci-Thomas, W. Sean Davidson, S. C. Meredith, C. A. Reardon, and G. S. Getz, “Apolipoprotein A-I alpha-helices 7 and 8 modulate high density lipoprotein subclass distribution,” The Journal of Biological Chemistry, vol. 277, no. 12, pp. 9645–9654, 2002. View at Publisher · View at Google Scholar · View at Scopus
  69. M. Rizzo, J. Otvos, D. Nikolic, G. Montalto, P. P. Toth, and M. Banach, “Subfractions and subpopulations of HDL: an update,” Current Medicinal Chemistry, vol. 21, no. 25, pp. 2881–2891, 2014. View at Publisher · View at Google Scholar · View at Scopus
  70. A. Kontush and M. J. Chapman, “Functionally defective high-density lipoprotein: a new therapeutic target at the crossroads of dyslipidemia, inflammation, and atherosclerosis,” Pharmacological Reviews, vol. 58, no. 3, pp. 342–374, 2006. View at Publisher · View at Google Scholar · View at Scopus
  71. C. Grunfeld, M. Pang, W. Doerrler, J. K. Shigenaga, P. Jensen, and K. R. Feingold, “Lipids, lipoproteins, triglyceride clearance, and cytokines in human immunodeficiency virus infection and the acquired immunodeficiency syndrome,” Journal of Clinical Endocrinology and Metabolism, vol. 74, no. 5, pp. 1045–1052, 1992. View at Publisher · View at Google Scholar · View at Scopus
  72. C. Popa, M. G. Netea, P. L. C. M. van Riel, J. W. M. van der Meer, and A. F. H. Stalenhoef, “The role of TNF-α in chronic inflammatory conditions, intermediary metabolism, and cardiovascular risk,” Journal of Lipid Research, vol. 48, no. 4, pp. 751–752, 2007. View at Publisher · View at Google Scholar · View at Scopus
  73. W. Khovidhunkit, R. A. Memon, K. R. Feingold, and C. Grunfeld, “Infection and inflammation-induced proatherogenic changes of lipoproteins,” Journal of Infectious Diseases, vol. 181, supplement 3, pp. S462–S472, 2000. View at Publisher · View at Google Scholar · View at Scopus
  74. A. Chait, Y. H. Chang, J. F. Oram, and J. W. Heinecke, “Thematic review series: The immune system and atherogenesis. Lipoprotein-associated inflammatory proteins: markers or mediators of cardiovascular disease?” Journal of Lipid Research, vol. 46, no. 3, pp. 389–403, 2005. View at Publisher · View at Google Scholar · View at Scopus
  75. A. Hoang, A. J. Murphy, M. T. Coughlan et al., “Advanced glycation of apolipoprotein A-I impairs its anti-atherogenic properties,” Diabetologia, vol. 50, no. 8, pp. 1770–1779, 2007. View at Publisher · View at Google Scholar · View at Scopus
  76. E. Nobecourt, M. J. Davies, B. E. Brown et al., “The impact of glycation on apolipoprotein A-I structure and its ability to activate lecithin:cholesterol acyltransferase,” Diabetologia, vol. 50, no. 3, pp. 643–653, 2007. View at Publisher · View at Google Scholar · View at Scopus
  77. E. Nobécourt, F. Tabet, G. Lambert et al., “Nonenzymatic glycation impairs the antiinflammatory properties of apolipoprotein A-I,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 30, no. 4, pp. 766–772, 2010. View at Publisher · View at Google Scholar · View at Scopus
  78. A. C. Carr, M. R. McCall, and B. Frei, “Oxidation of LDL by myeloperoxidase and reactive nitrogen species: reaction pathways and antioxidant protection,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 20, no. 7, pp. 1716–1723, 2000. View at Publisher · View at Google Scholar · View at Scopus
  79. 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
  80. A. Daugherty, J. L. Dunn, D. L. Rateri, and J. W. Heinecke, “Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions,” The Journal of Clinical Investigation, vol. 94, no. 1, pp. 437–444, 1994. View at Publisher · View at Google Scholar · View at Scopus
  81. L. Zheng, M. Settle, G. Brubaker et al., “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,” The Journal of Biological Chemistry, vol. 280, no. 1, pp. 38–47, 2005. View at Publisher · View at Google Scholar · View at Scopus
  82. 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
  83. K.-H. Cho, D. M. Durbin, and A. Jonas, “Role of individual amino acids of apolipoprotein A-I in the activation of lecithin: cholesterol acyltransferase and in HDL rearrangements,” Journal of Lipid Research, vol. 42, no. 3, pp. 379–389, 2001. View at Google Scholar · View at Scopus
  84. B. Garner, A. R. Waldeck, P. K. Witting, K.-A. Rye, and R. Stocker, “Oxidation of high density lipoproteins. II. Evidence for direct reduction of lipid hydroperoxides by methionine residues of apolipoproteins AI and AII,” Journal of Biological Chemistry, vol. 273, no. 11, pp. 6088–6095, 1998. View at Publisher · View at Google Scholar · View at Scopus
  85. B. Shao, M. N. Oda, C. Bergt et al., “Myeloperoxidase impairs ABCA1-dependent cholesterol efflux through methionine oxidation and site-specific tyrosine chlorination of apolipoprotein A-I,” The Journal of Biological Chemistry, vol. 281, no. 14, pp. 9001–9004, 2006. View at Publisher · View at Google Scholar · View at Scopus
  86. G. Daniil, A. A. P. Phedonos, A. G. Holleboom et al., “Characterization of antioxidant/anti-inflammatory properties and apoA-I-containing subpopulations of HDL from family subjects with monogenic low HDL disorders,” Clinica Chimica Acta, vol. 412, no. 13-14, pp. 1213–1220, 2011. View at Publisher · View at Google Scholar · View at Scopus
  87. C. Cavelier, I. Lorenzi, L. Rohrer, and A. von Eckardstein, “Lipid efflux by the ATP-binding cassette transporters ABCA1 and ABCG1,” Biochimica et Biophysica Acta, vol. 1761, no. 7, pp. 655–666, 2006. View at Publisher · View at Google Scholar · View at Scopus
  88. C. Bergt, S. Pennathur, X. Fu et al., “The myeloperoxidase product hypochlorous acid oxidizes HDL in the human artery wall and impairs ABCA1-dependent cholesterol transport,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 35, pp. 13032–13037, 2004. View at Publisher · View at Google Scholar · View at Scopus
  89. B. Shao, S. Pennathur, and J. W. Heinecke, “Myeloperoxidase targets apolipoprotein A-I, the major high density lipoprotein protein, for site-specific oxidation in human atherosclerotic lesions,” Journal of Biological Chemistry, vol. 287, no. 9, pp. 6375–6386, 2012. View at Publisher · View at Google Scholar · View at Scopus
  90. B. Shao, C. Tang, J. W. Heinecke, and J. F. Oram, “Oxidation of apolipoprotein A-I by myeloperoxidase impairs the initial interactions with ABCA1 required for signaling and cholesterol export,” Journal of Lipid Research, vol. 51, no. 7, pp. 1849–1858, 2010. View at Publisher · View at Google Scholar · View at Scopus
  91. M. M. Hussain, “Intestinal lipid absorption and lipoprotein formation,” Current Opinion in Lipidology, vol. 25, no. 3, pp. 200–206, 2014. View at Publisher · View at Google Scholar · View at Scopus
  92. E. J. Niesor, E. Chaput, J.-L. Mary et al., “Effect of compounds affecting ABCA1 expression and CETP activity on the HDL pathway involved in intestinal absorption of lutein and zeaxanthin,” Lipids, vol. 49, no. 12, pp. 1233–1243, 2014. View at Publisher · View at Google Scholar · View at Scopus
  93. N. Nicod and R. S. Parker, “Vitamin E secretion by Caco-2 monolayers to APOA1, but not to HDL, is vitamer selective,” Journal of Nutrition, vol. 143, no. 10, pp. 1565–1572, 2013. View at Publisher · View at Google Scholar · View at Scopus
  94. M. de la Llera-Moya, D. Drazul-Schrader, B. F. Asztalos, M. Cuchel, D. J. Rader, and G. H. Rothblat, “The ability to promote efflux via ABCA1 determines the capacity of serum specimens with similar high-density lipoprotein cholesterol to remove cholesterol from macrophages,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 30, no. 4, pp. 796–801, 2010. View at Publisher · View at Google Scholar · View at Scopus
  95. A. Mulya, J.-Y. Lee, A. K. Gebre et al., “Initial interaction of apoA-I with ABCA1 impacts in vivo metabolic fate of nascent HDL,” Journal of Lipid Research, vol. 49, no. 11, pp. 2390–2401, 2008. View at Publisher · View at Google Scholar · View at Scopus
  96. K.-A. Rye and P. J. Barter, “Formation and metabolism of prebeta-migrating, lipid-poor apolipoprotein A-I,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 24, no. 3, pp. 421–428, 2004. View at Publisher · View at Google Scholar · View at Scopus
  97. 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
  98. 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
  99. 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,” The Journal of Biological Chemistry, vol. 284, no. 45, pp. 30825–30835, 2009. View at Publisher · View at Google Scholar · View at Scopus
  100. L. Perségol, M.-C. Brindisi, D. Rageot et al., “Oxidation-induced loss of the ability of HDL to counteract the inhibitory effect of oxidized LDL on vasorelaxation,” Heart and Vessels, pp. 1–5, 2014. View at Publisher · View at Google Scholar · View at Scopus
  101. K. Wang and P. V. Subbaiah, “Importance of the free sulfhydryl groups of lecithin-cholesterol acyltransferase for its sensitivity to oxidative inactivation,” Biochimica et Biophysica Acta: Molecular and Cell Biology of Lipids, vol. 1488, no. 3, pp. 268–277, 2000. View at Publisher · View at Google Scholar · View at Scopus
  102. G. K. Hovingh, B. A. Hutten, A. G. Holleboom et al., “Compromised LCAT function is associated with increased atherosclerosis,” Circulation, vol. 112, no. 6, pp. 879–884, 2005. View at Publisher · View at Google Scholar · View at Scopus
  103. E. Gjone and B. Bergaust, “Corneal opacity in familial plasma cholesterol ester deficiency,” Acta Ophthalmologica, vol. 47, no. 1, pp. 222–227, 1969. View at Google Scholar · View at Scopus
  104. R. Scarpioni, C. Paties, and G. Bergonzi, “Dramatic atherosclerotic vascular burden in a patient with familial lecithin-cholesterol acyltransferase (LCAT) deficiency,” Nephrology Dialysis Transplantation, vol. 23, no. 3, pp. 1074–1075, 2008. View at Publisher · View at Google Scholar
  105. A. R. Tall, P. Costet, and N. Wang, “Regulation and mechanisms of macrophage cholesterol efflux,” Journal of Clinical Investigation, vol. 110, no. 7, pp. 899–904, 2002. View at Publisher · View at Google Scholar · View at Scopus
  106. J. F. Oram, “Tangier disease and ABCA1,” Biochimica et Biophysica Acta: Molecular and Cell Biology of Lipids, vol. 1529, no. 1–3, pp. 321–330, 2000. View at Publisher · View at Google Scholar · View at Scopus
  107. M. E. Brousseau, G. P. Eberhart, J. Dupuis et al., “Cellular cholesterol efflux in heterozygotes for Tangier disease is markedly reduced and correlates with high density lipoprotein cholesterol concentration and particle size,” Journal of Lipid Research, vol. 41, no. 7, pp. 1125–1135, 2000. View at Google Scholar · View at Scopus
  108. A. E. van der Velde and A. K. Groen, “Shifting gears: liver SR-BI drives reverse cholesterol transport in macrophages,” The Journal of Clinical Investigation, vol. 115, no. 10, pp. 2699–2701, 2005. View at Publisher · View at Google Scholar · View at Scopus
  109. A. Leiva, H. Verdejo, M. L. Benítez, A. Martínez, D. Busso, and A. Rigotti, “Mechanisms regulating hepatic SR-BI expression and their impact on HDL metabolism,” Atherosclerosis, vol. 217, no. 2, pp. 299–307, 2011. View at Publisher · View at Google Scholar · View at Scopus
  110. M. L. Varban, F. Rinninger, N. Wang et al., “Targeted mutation reveals a central role for SR-BI in hepatic selective uptake of high density lipoprotein cholesterol,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 8, pp. 4619–4624, 1998. View at Publisher · View at Google Scholar · View at Scopus
  111. W. Zhu, S. Saddar, D. Seetharam et al., “The scavenger receptor class B type I adaptor protein PDZK1 maintains endothelial monolayer integrity,” Circulation Research, vol. 102, no. 4, pp. 480–487, 2008. View at Publisher · View at Google Scholar · View at Scopus
  112. B. Pan, Y. Ma, H. Ren et al., “Diabetic HDL is dysfunctional in stimulating endothelial cell migration and proliferation due to down regulation of SR-BI expression,” PLoS ONE, vol. 7, no. 11, Article ID e48530, 2012. View at Publisher · View at Google Scholar · View at Scopus
  113. S. A. Sorrentino, C. Besler, L. Rohrer et al., “Endothelial-vasoprotective effects of high-density lipoprotein are impaired in patients with type 2 diabetes mellitus but are improved after extended-release niacin therapy,” Circulation, vol. 121, no. 1, pp. 110–122, 2010. View at Publisher · View at Google Scholar · View at Scopus
  114. M. C. de Beer, A. Ji, A. Jahangiri et al., “ATP binding cassette G1-dependent cholesterol efflux during inflammation,” Journal of Lipid Research, vol. 52, no. 2, pp. 345–353, 2011. View at Publisher · View at Google Scholar · View at Scopus
  115. I. Kudo and M. Murakami, “Phospholipase A2 enzymes,” Prostaglandins & Other Lipid Mediators, vol. 68-69, pp. 3–58, 2002. View at Publisher · View at Google Scholar · View at Scopus
  116. R. H. Schaloske and E. A. Dennis, “The phospholipase A2 superfamily and its group numbering system,” Biochimica et Biophysica Acta: Molecular and Cell Biology of Lipids, vol. 1761, no. 11, pp. 1246–1259, 2006. View at Publisher · View at Google Scholar · View at Scopus
  117. Z. Mallat, G. Lambeau, and A. Tedgui, “Lipoprotein-associated and secreted phospholipases A2 in cardiovascular disease: roles as biological effectors and biomarkers,” Circulation, vol. 122, no. 21, pp. 2183–2200, 2010. View at Publisher · View at Google Scholar · View at Scopus
  118. F. C. de Beer, M. C. de Beer, D. R. van der Westhuyzen et al., “Secretory non-pancreatic phospholipase A2: influence on lipoprotein metabolism,” Journal of Lipid Research, vol. 38, no. 11, pp. 2232–2239, 1997. View at Google Scholar · View at Scopus
  119. P. Shridas, W. M. Bailey, F. Gizard et al., “Group X secretory phospholipase A2 negatively regulates ABCA1 and ABCG1 expression and cholesterol efflux in macrophages,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 30, no. 10, pp. 2014–2021, 2010. View at Publisher · View at Google Scholar · View at Scopus
  120. P. Jousilahti, V. Salomaa, V. Rasi, E. Vahtera, and T. Palosuo, “The association of c-reactive protein, serum amyloid a and fibrinogen with prevalent coronary heart disease—baseline findings of the PAIS project,” Atherosclerosis, vol. 156, no. 2, pp. 451–456, 2001. View at Publisher · View at Google Scholar · View at Scopus
  121. A. S. Whitehead, M. C. de Beer, D. M. Steel et al., “Identification of novel members of the serum amyloid A protein superfamily as constitutive apolipoproteins of high density lipoprotein,” The Journal of Biological Chemistry, vol. 267, no. 6, pp. 3862–3867, 1992. View at Google Scholar · View at Scopus
  122. J. M. Wroblewski, A. Jahangiri, A. Ji, F. C. de Beer, D. R. van der Westhuyzen, and N. R. Webb, “Nascent HDL formation by hepatocytes is reduced by the concerted action of serum amyloid A and endothelial lipase,” Journal of Lipid Research, vol. 52, no. 12, pp. 2255–2261, 2011. View at Publisher · View at Google Scholar · View at Scopus
  123. K. Kotani, T. Yamada, and A. Gugliucci, “Paired measurements of paraoxonase 1 and serum amyloid A as useful disease markers,” BioMed Research International, vol. 2013, Article ID 481437, 4 pages, 2013. View at Publisher · View at Google Scholar · View at Scopus
  124. T. Vaisar, C. Tang, I. Babenko et al., “Inflammatory remodeling of the HDL proteome impairs cholesterol efflux capacity,” Journal of Lipid Research, vol. 56, no. 8, pp. 1519–1530, 2015. View at Publisher · View at Google Scholar
  125. M. Aviram, M. Rosenblat, C. L. Bisgaier, R. S. Newton, S. L. Primo-Parmo, and B. N. La Du, “Paraoxonase inhibits high-density lipoprotein oxidation and preserves its functions: a possible peroxidative role for paraoxonase,” Journal of Clinical Investigation, vol. 101, no. 8, pp. 1581–1590, 1998. View at Publisher · View at Google Scholar · View at Scopus
  126. C. Mineo and P. W. Shaul, “PON-dering differences in HDL function in coronary artery disease,” The Journal of Clinical Investigation, vol. 121, no. 7, pp. 2545–2548, 2011. View at Publisher · View at Google Scholar · View at Scopus
  127. L. Jaouad, C. Milochevitch, and A. Khalil, “PON1 paraoxonase activity is reduced during HDL oxidation and is an indicator of HDL antioxidant capacity,” Free Radical Research, vol. 37, no. 1, pp. 77–83, 2003. View at Publisher · View at Google Scholar · View at Scopus
  128. T. Bacchetti, S. Masciangelo, T. Armeni, V. Bicchiega, and G. Ferretti, “Glycation of human high density lipoprotein by methylglyoxal: effect on HDL-paraoxonase activity,” Metabolism, vol. 63, no. 3, pp. 307–311, 2014. View at Publisher · View at Google Scholar · View at Scopus
  129. B. Mackness, P. N. Durrington, B. Abuashia, A. J. M. Boulton, and M. I. Mackness, “Low paraoxonase activity in type II diabetes mellitus complicated by retinopathy,” Clinical Science, vol. 98, no. 3, pp. 355–363, 2000. View at Publisher · View at Google Scholar · View at Scopus
  130. S. K. Kota, L. K. Meher, S. K. Kota, S. Jammula, S. V. Krishna, and K. D. Modi, “Implications of serum paraoxonase activity in obesity, diabetes mellitus, and dyslipidemia,” Indian Journal of Endocrinology and Metabolism, vol. 17, no. 3, pp. 402–412, 2013. View at Google Scholar
  131. Y. Huang, Z. Wu, M. Riwanto et al., “Myeloperoxidase, paraoxonase-1, and HDL form a functional ternary complex,” Journal of Clinical Investigation, vol. 123, no. 9, pp. 3815–3828, 2013. View at Publisher · View at Google Scholar · View at Scopus
  132. P. S. MacLean, C. J. Tanner, J. A. Houmard, and H. A. Barakat, “Plasma cholesteryl ester transfer protein activity is not linked to insulin sensitivity,” Metabolism, vol. 50, no. 7, pp. 783–788, 2001. View at Publisher · View at Google Scholar · View at Scopus
  133. S. M. Boekholdt, F. M. Sacks, J. W. Jukema et al., “Cholesteryl ester transfer protein TaqIB variant, high-density lipoprotein cholesterol levels, cardiovascular risk, and efficacy of pravastatin treatment: individual patient meta-analysis of 13 677 subjects,” Circulation, vol. 111, no. 3, pp. 278–287, 2005. View at Publisher · View at Google Scholar · View at Scopus
  134. A. Inazu, X.-C. Jiang, T. Haraki et al., “Genetic cholesteryl ester transfer protein deficiency caused by two prevalent mutations as a major determinant of increased levels of high density lipoprotein cholesterol,” Journal of Clinical Investigation, vol. 94, no. 5, pp. 1872–1882, 1994. View at Publisher · View at Google Scholar · View at Scopus
  135. K.-I. Hirano, S. Yamashita, N. Nakajima et al., “Genetic cholesteryl ester transfer protein deficiency is extremely frequent in the Omagari area of Japan. Marked hyperalphalipoproteinemia caused by CETP gene mutation is not associated with longevity,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 17, no. 6, pp. 1053–1059, 1997. View at Publisher · View at Google Scholar · View at Scopus
  136. S. Yamashita, T. Maruyama, K.-I. Hirano, N. Sakai, N. Nakajima, and Y. Matsuzawa, “Molecular mechanisms, lipoprotein abnormalities and atherogenicity of hyperalphalipoproteinemia,” Atherosclerosis, vol. 152, no. 2, pp. 271–285, 2000. View at Publisher · View at Google Scholar · View at Scopus
  137. P. Wiesner, K. Leidl, A. Boettcher, G. Schmitz, and G. Liebisch, “Lipid profiling of FPLC-separated lipoprotein fractions by electrospray ionization tandem mass spectrometry,” Journal of Lipid Research, vol. 50, no. 3, pp. 574–585, 2009. View at Publisher · View at Google Scholar · View at Scopus
  138. A. Kontush, M. Lhomme, and M. J. Chapman, “Unraveling the complexities of the HDL lipidome,” Journal of Lipid Research, vol. 54, no. 11, pp. 2950–2963, 2013. View at Publisher · View at Google Scholar · View at Scopus
  139. K. Sattler and B. Levkau, “Sphingosine-1-phosphate as a mediator of high-density lipoprotein effects in cardiovascular protection,” Cardiovascular Research, vol. 82, no. 2, pp. 201–211, 2009. View at Publisher · View at Google Scholar · View at Scopus
  140. V. H. Sunesen, C. Weber, and G. Hølmer, “Lipophilic antioxidants and polyunsaturated fatty acids in lipoprotein classes: distribution and interaction,” European Journal of Clinical Nutrition, vol. 55, no. 2, pp. 115–123, 2001. View at Publisher · View at Google Scholar · View at Scopus
  141. W. Pruzanski, E. Stefanski, F. C. de Beer, M. C. de Beer, A. Ravandi, and A. Kuksis, “Comparative analysis of lipid composition of normal and acute-phase high density lipoproteins,” Journal of Lipid Research, vol. 41, no. 7, pp. 1035–1047, 2000. View at Google Scholar · View at Scopus
  142. A. Kontush, E. C. de Faria, S. Chantepie, and M. J. Chapman, “A normotriglyceridemic, low HDL-cholesterol phenotype is characterised by elevated oxidative stress and HDL particles with attenuated antioxidative activity,” Atherosclerosis, vol. 182, no. 2, pp. 277–285, 2005. View at Publisher · View at Google Scholar · View at Scopus
  143. D. J. Greene, J. W. Skeggs, and R. E. Morton, “Elevated triglyceride content diminishes the capacity of high density lipoprotein to deliver cholesteryl esters via the scavenger receptor class B type I (SR-BI),” The Journal of Biological Chemistry, vol. 276, no. 7, pp. 4804–4811, 2001. View at Publisher · View at Google Scholar · View at Scopus
  144. W. Pruzanski, E. Stefanski, F. C. de Beer et al., “Lipoproteins are substrates for human secretory group IIA phospholipase A2: preferential hydrolysis of acute phase HDL,” Journal of Lipid Research, vol. 39, no. 11, pp. 2150–2160, 1998. View at Google Scholar · View at Scopus
  145. S. Kar, M. A. Patel, R. K. Tripathy, P. Bajaj, U. V. Suvarnakar, and A. H. Pande, “Oxidized phospholipid content destabilizes the structure of reconstituted high density lipoprotein particles and changes their function,” Biochimica et Biophysica Acta—Molecular and Cell Biology of Lipids, vol. 1821, no. 9, pp. 1200–1210, 2012. View at Publisher · View at Google Scholar · View at Scopus
  146. A. Papathanasiou, C. Kostara, M.-T. Cung et al., “Analysis of the composition of plasma lipoproteins in patients with extensive coronary heart disease using 1H NMR spectroscopy,” Hellenic Journal of Cardiology, vol. 49, no. 2, pp. 72–78, 2008. View at Google Scholar · View at Scopus
  147. U. J. F. Tietge, C. Maugeais, S. Lund-Katz, D. Grass, F. C. DeBeer, and D. J. Rader, “Human secretory phospholipase A2 mediates decreased plasma levels of HDL cholesterol and ApoA-I in response to inflammation in human ApoA-I transgenic mice,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 22, no. 7, pp. 1213–1218, 2002. View at Publisher · View at Google Scholar · View at Scopus
  148. P. G. Yancey, M. de la Llera-Moya, S. Swarnakar et al., “High density lipoprotein phospholipid composition is a major determinant of the bi-directional flux and net movement of cellular free cholesterol mediated by scavenger receptor BI,” Journal of Biological Chemistry, vol. 275, no. 47, pp. 36596–36604, 2000. View at Publisher · View at Google Scholar · View at Scopus
  149. M. Bamberger, S. Lund-Katz, M. C. Phillips, and G. H. Rothblat, “Mechanism of the hepatic lipase induced accumulation of high-density lipoprotein cholesterol by cells in culture,” Biochemistry, vol. 24, no. 14, pp. 3693–3701, 1985. View at Publisher · View at Google Scholar · View at Scopus
  150. A. Zerrad-Saadi, P. Therond, S. Chantepie et al., “HDL3-mediated inactivation of LDL-associated phospholipid hydroperoxides is determined by the redox status of apolipoprotein A-I and HDL particle surface lipid rigidity: relevance to inflammation and atherogenesis,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 29, no. 12, pp. 2169–2175, 2009. View at Publisher · View at Google Scholar · View at Scopus
  151. M. I. Mackness, P. N. Durrington, and B. Mackness, “How high-density lipoprotein protects against the effects of lipid peroxidation,” Current Opinion in Lipidology, vol. 11, no. 4, pp. 383–388, 2000. View at Publisher · View at Google Scholar · View at Scopus
  152. S. Mitra, T. Goyal, and J. L. Mehta, “Oxidized LDL, LOX-1 and atherosclerosis,” Cardiovascular Drugs and Therapy, vol. 25, no. 5, pp. 419–429, 2011. View at Publisher · View at Google Scholar · View at Scopus
  153. A. D. Watson, N. Leitinger, M. Navab et al., “Structural identification by mass spectrometry of oxidized phospholipids in minimally oxidized low density lipoprotein that induce monocyte/endothelial interactions and evidence for their presence in vivo,” The Journal of Biological Chemistry, vol. 272, no. 21, pp. 13597–13607, 1997. View at Publisher · View at Google Scholar · View at Scopus
  154. S. D. Cushing, J. A. Berliner, A. J. Valente et al., “Minimally modified low density lipoprotein induces monocyte chemotactic protein 1 in human endothelial cells and smooth muscle cells,” Proceedings of the National Academy of Sciences of the United States of America, vol. 87, no. 13, pp. 5134–5138, 1990. View at Publisher · View at Google Scholar · View at Scopus
  155. W. Jaross, R. Eckey, and M. Menschikowski, “Biological effects of secretory phospholipase A2 group IIA on lipoproteins and in atherogenesis,” European Journal of Clinical Investigation, vol. 32, no. 6, pp. 383–393, 2002. View at Publisher · View at Google Scholar · View at Scopus
  156. Y. Ishimoto, K. Yamada, S. Yamamoto, T. Ono, M. Notoya, and K. Hanasaki, “Group V and X secretory phospholipase A2s-induced modification of high-density lipoprotein linked to the reduction of its antiatherogenic functions,” Biochimica et Biophysica Acta: Molecular Cell Research, vol. 1642, no. 3, pp. 129–138, 2003. View at Publisher · View at Google Scholar · View at Scopus
  157. D. Mannheim, J. Herrmann, D. Versari et al., “Enhanced expression of Lp-PLA2 and lysophosphatidylcholine in symptomatic carotid atherosclerotic plaques,” Stroke, vol. 39, no. 5, pp. 1448–1455, 2008. View at Publisher · View at Google Scholar · View at Scopus
  158. T. Kita, N. Kume, M. Minami et al., “Role of oxidized LDL in atherosclerosis,” Annals of the New York Academy of Sciences, vol. 947, pp. 199–205, 2001. View at Google Scholar · View at Scopus
  159. F. Rached, M. Lhomme, L. Camont et al., “Defective functionality of small, dense HDL3 subpopulations in ST segment elevation myocardial infarction: relevance of enrichment in lysophosphatidylcholine, phosphatidic acid and serum amyloid A,” Biochimica et Biophysica Acta—Molecular and Cell Biology of Lipids, vol. 1851, no. 9, pp. 1254–1261, 2015. View at Publisher · View at Google Scholar
  160. N. Leitinger, A. D. Watson, S. Y. Hama et al., “Role of group II secretory phospholipase A2 in atherosclerosis: 2 potential involvement of biologically active oxidized phospholipids,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 19, no. 5, pp. 1291–1298, 1999. View at Publisher · View at Google Scholar · View at Scopus
  161. C. Morgantini, A. Natali, B. Boldrini et al., “Anti-inflammatory and antioxidant properties of HDLs are impaired in type 2 diabetes,” Diabetes, vol. 60, no. 10, pp. 2617–2623, 2011. View at Publisher · View at Google Scholar · View at Scopus
  162. Y. Wang and J. F. Oram, “Unsaturated fatty acids inhibit cholesterol efflux from macrophages by increasing degradation of ATP-binding cassette transporter A1,” The Journal of Biological Chemistry, vol. 277, no. 7, pp. 5692–5697, 2002. View at Publisher · View at Google Scholar · View at Scopus
  163. Y. Uehara, S.-I. Miura, A. von Eckardstein et al., “Unsaturated fatty acids suppress the expression of the ATP-binding cassette transporter G1 (ABCG1) and ABCA1 genes via an LXR/RXR responsive element,” Atherosclerosis, vol. 191, no. 1, pp. 11–21, 2007. View at Publisher · View at Google Scholar · View at Scopus
  164. Y. Wang and J. F. Oram, “Unsaturated fatty acids phosphorylate and destabilize ABCA1 through a protein kinase C δ pathway,” Journal of Lipid Research, vol. 48, no. 5, pp. 1062–1068, 2007. View at Publisher · View at Google Scholar · View at Scopus
  165. A. Carro, M. Martín, I. Lozano, and S. Hevia, “Low HDL-C: more than atherosclerosis,” Cardiocore, vol. 46, no. 3, pp. e39–e41, 2011. View at Publisher · View at Google Scholar · View at Scopus
  166. M. McMahon, J. Grossman, J. FitzGerald et al., “Proinflammatory high-density lipoprotein as a biomarker for atherosclerosis in patients with systemic lupus erythematosus and rheumatoid arthritis,” Arthritis and Rheumatism, vol. 54, no. 8, pp. 2541–2549, 2006. View at Publisher · View at Google Scholar · View at Scopus
  167. M. McMahon, J. Grossman, B. Skaggs et al., “Dysfunctional proinflammatory high-density lipoproteins confer increased risk of atherosclerosis in women with systemic lupus erythematosus,” Arthritis and Rheumatism, vol. 60, no. 8, pp. 2428–2437, 2009. View at Publisher · View at Google Scholar · View at Scopus
  168. D. Farbstein and A. P. Levy, “HDL dysfunction in diabetes: causes and possible treatments,” Expert Review of Cardiovascular Therapy, vol. 10, no. 3, pp. 353–361, 2012. View at Publisher · View at Google Scholar · View at Scopus
  169. L. R. Brunham, J. K. Kruit, J. Iqbal et al., “Intestinal ABCA1 directly contributes to HDL biogenesis in vivo,” Journal of Clinical Investigation, vol. 116, no. 4, pp. 1052–1062, 2006. View at Publisher · View at Google Scholar · View at Scopus
  170. Y. Zhang, F. C. McGillicuddy, C. C. Hinkle et al., “Adipocyte modulation of high-density lipoprotein cholesterol,” Circulation, vol. 121, no. 11, pp. 1347–1355, 2010. View at Publisher · View at Google Scholar · View at Scopus
  171. S. Le Lay, C. Robichon, X. Le Liepvre, G. Dagher, P. Ferre, and I. Dugail, “Regulation of ABCA1 expression and cholesterol efflux during adipose differentiation of 3T3-L1 cells,” Journal of Lipid Research, vol. 44, no. 8, pp. 1499–1507, 2003. View at Publisher · View at Google Scholar · View at Scopus
  172. C. N. Lumeng, S. M. DeYoung, J. L. Bodzin, and A. R. Saltiel, “Increased inflammatory properties of adipose tissue macrophages recruited during diet-induced obesity,” Diabetes, vol. 56, no. 1, pp. 16–23, 2007. View at Publisher · View at Google Scholar · View at Scopus
  173. S. J. Nicholls, P. Lundman, J. A. Harmer et al., “Consumption of saturated fat impairs the anti-inflammatory properties of high-density lipoproteins and endothelial function,” Journal of the American College of Cardiology, vol. 48, no. 4, pp. 715–720, 2006. View at Publisher · View at Google Scholar · View at Scopus
  174. C. K. Roberts, M. Katiraie, D. M. Croymans, O. O. Yang, and T. Kelesidis, “Untrained young men have dysfunctional HDL compared with strength-trained men irrespective of body weight status,” Journal of Applied Physiology, vol. 115, no. 7, pp. 1043–1049, 2013. View at Publisher · View at Google Scholar · View at Scopus
  175. B.-M. He, S.-P. Zhao, and Z.-Y. Peng, “Effects of cigarette smoking on HDL quantity and function: implications for atherosclerosis,” Journal of Cellular Biochemistry, vol. 114, no. 11, pp. 2431–2436, 2013. View at Publisher · View at Google Scholar · View at Scopus
  176. R. Aebersold and B. F. Cravatt, “Proteomics—advances, applications and the challenges that remain,” Trends in Biotechnology, vol. 20, no. 12, supplement, pp. 1–2, 2002. View at Google Scholar · View at Scopus
  177. B. Brügger, “Lipidomics: analysis of the lipid composition of cells and Subcellular organelles by electrospray ionization mass spectrometry,” Annual Review of Biochemistry, vol. 83, pp. 79–98, 2014. View at Publisher · View at Google Scholar · View at Scopus
  178. P. J. Barter, S. Nicholls, K.-A. Rye, G. M. Anantharamaiah, M. Navab, and A. M. Fogelman, “Antiinflammatory properties of HDL,” Circulation Research, vol. 95, no. 8, pp. 764–772, 2004. View at Publisher · View at Google Scholar · View at Scopus
  179. C. Wadham, N. Albanese, J. Roberts et al., “High-density lipoproteins neutralize C-reactive protein proinflammatory activity,” Circulation, vol. 109, no. 17, pp. 2116–2122, 2004. View at Publisher · View at Google Scholar · View at Scopus
  180. M. G. Sorci-Thomas and M. J. Thomas, “Why targeting HDL should work as a therapeutic tool, but has not,” Journal of Cardiovascular Pharmacology, vol. 62, no. 3, pp. 239–246, 2013. View at Publisher · View at Google Scholar · View at Scopus
  181. J.-Y. Hsieh, C.-T. Chang, M. T. Huang et al., “Biochemical and functional characterization of charge-defined subfractions of high-density lipoprotein from normal adults,” Analytical Chemistry, vol. 85, no. 23, pp. 11440–11448, 2013. View at Publisher · View at Google Scholar · View at Scopus
  182. W. S. Davidson, R. A. G. D. Silva, S. Chantepie, W. R. Lagor, M. J. Chapman, and A. Kontush, “Proteomic analysis of defined hdl subpopulations reveals particle-specific protein clusters: relevance to antioxidative function,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 29, no. 6, pp. 870–876, 2009. View at Publisher · View at Google Scholar · View at Scopus
  183. J. W. Heinecke, “The HDL proteome: a marker-and perhaps mediator-of coronary artery disease,” The Journal of Lipid Research, vol. 50, supplement, pp. S167–S171, 2009. View at Publisher · View at Google Scholar
  184. D. Nedelkov, “Mass spectrometry-based immunoassays for the next phase of clinical applications,” Expert Review of Proteomics, vol. 3, no. 6, pp. 631–640, 2006. View at Publisher · View at Google Scholar · View at Scopus
  185. O. Trenchevska and D. Nedelkov, “Targeted quantitative mass spectrometric immunoassay for human protein variants,” Proteome Science, vol. 9, no. 1, article 19, 2011. View at Publisher · View at Google Scholar · View at Scopus
  186. H. Yassine, C. R. Borges, M. R. Schaab et al., “Mass spectrometric immunoassay and MRM as targeted MS-based quantitative approaches in biomarker development: potential applications to cardiovascular disease and diabetes,” Proteomics: Clinical Applications, vol. 7, no. 7-8, pp. 528–540, 2013. View at Publisher · View at Google Scholar · View at Scopus
  187. A. N. Hoofnagle and M. H. Wener, “The fundamental flaws of immunoassays and potential solutions using tandem mass spectrometry,” Journal of Immunological Methods, vol. 347, no. 1-2, pp. 3–11, 2009. View at Publisher · View at Google Scholar · View at Scopus
  188. T. Shi, D. Su, T. Liu et al., “Advancing the sensitivity of selected reaction monitoring-based targeted quantitative proteomics,” Proteomics, vol. 12, no. 8, pp. 1074–1092, 2012. View at Publisher · View at Google Scholar · View at Scopus
  189. G. E. Ronsein, N. Pamir, P. D. von Haller et al., “Parallel reaction monitoring (PRM) and selected reaction monitoring (SRM) exhibit comparable linearity, dynamic range and precision for targeted quantitative HDL proteomics,” Journal of Proteomics, vol. 113, pp. 388–399, 2015. View at Publisher · View at Google Scholar · View at Scopus
  190. T. A. Addona, S. E. Abbatiello, B. Schilling et al., “Multi-site assessment of the precision and reproducibility of multiple reaction monitoring-based measurements of proteins in plasma,” Nature Biotechnology, vol. 27, no. 7, pp. 633–641, 2009. View at Publisher · View at Google Scholar · View at Scopus
  191. H. N. Yassine, A. M. Jackson, C. R. Borges et al., “The application of multiple reaction monitoring and multi-analyte profiling to HDL proteins,” Lipids in Health and Disease, vol. 13, article 8, 2014. View at Publisher · View at Google Scholar · View at Scopus
  192. H. Karlsson, P. Leanderson, C. Tagesson, and M. Lindahl, “Lipoproteomics II: mapping of proteins in high-density lipoprotein using two-dimensional gel electrophoresis and mass spectrometry,” Proteomics, vol. 5, no. 5, pp. 1431–1445, 2005. View at Publisher · View at Google Scholar · View at Scopus
  193. F. Rezaee, B. Casetta, J. H. M. Levels, D. Speijer, and J. C. M. Meijers, “Proteomic analysis of high-density lipoprotein,” Proteomics, vol. 6, no. 2, pp. 721–730, 2006. View at Publisher · View at Google Scholar · View at Scopus
  194. J. Patzelt, A. Verschoor, and H. F. Langer, “Platelets and the complement cascade in atherosclerosis,” Frontiers in Physiology, vol. 6, article 49, 2015. View at Publisher · View at Google Scholar
  195. A. K. Chauhan and T. L. Moore, “Presence of plasma complement regulatory proteins clusterin (Apo J) and vitronectin (S40) on circulating immune complexes (CIC),” Clinical and Experimental Immunology, vol. 145, no. 3, pp. 398–406, 2006. View at Publisher · View at Google Scholar · View at Scopus
  196. S. I. Rosenfeld, C. H. Packman, and J. P. Leddy, “Inhibition of the lytic action of cell-bound terminal complement components by human high density lipoproteins and apoproteins,” The Journal of Clinical Investigation, vol. 71, no. 4, pp. 795–808, 1983. View at Publisher · View at Google Scholar · View at Scopus
  197. K. K. Hamilton, J. Zhao, and P. J. Sims, “Interaction between apolipoproteins A-I and A-II and the membrane attack complex of complement. Affinity of the apoproteins for polymeric C9,” Journal of Biological Chemistry, vol. 268, no. 5, pp. 3632–3638, 1993. View at Google Scholar · View at Scopus
  198. A. L. Pasqui, L. Puccetti, G. Bova et al., “Relationship between serum complement and different lipid disorders,” Clinical & Experimental Medicine, vol. 2, no. 1, pp. 33–38, 2002. View at Publisher · View at Google Scholar · View at Scopus
  199. J. Wagner, M. Riwanto, C. Besler et al., “Characterization of levels and cellular transfer of circulating lipoprotein-bound microRNAs,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 33, no. 6, pp. 1392–1400, 2013. View at Publisher · View at Google Scholar · View at Scopus
  200. F. Momen-Heravi, L. Balaj, S. Alian et al., “Current methods for the isolation of extracellular vesicles,” Biological Chemistry, vol. 394, no. 10, pp. 1253–1262, 2013. View at Publisher · View at Google Scholar · View at Scopus
  201. É. Biró, J. M. van den Goor, B. A. de Mol et al., “Complement activation on the surface of cell-derived microparticles during cardiac surgery with cardiopulmonary bypass—is retransfusion of pericardial blood harmful?” Perfusion, vol. 26, no. 1, pp. 21–29, 2011. View at Publisher · View at Google Scholar · View at Scopus
  202. A. M. Shiflett, J. R. Bishop, A. Pahwa, and S. L. Hajduk, “Human high density lipoproteins are platforms for the assembly of multi-component innate immune complexes,” The Journal of Biological Chemistry, vol. 280, no. 38, pp. 32578–32585, 2005. View at Publisher · View at Google Scholar · View at Scopus
  203. J. M. Harrington, T. Nishanova, S. R. Pena et al., “A retained secretory signal peptide mediates high density lipoprotein (HDL) assembly and function of haptoglobin-related protein,” Journal of Biological Chemistry, vol. 289, no. 36, pp. 24811–24820, 2014. View at Publisher · View at Google Scholar · View at Scopus
  204. J. Widener, M. J. Nielsen, A. Shiflett, S. K. Moestrup, and S. Hajduk, “Hemoglobin is a co-factor of human trypanosome lytic factor,” PLoS Pathog, vol. 3, no. 9, article e129, 2008. View at Publisher · View at Google Scholar
  205. M. Sanson, E. Distel, and E. A. Fisher, “HDL induces the expression of the M2 macrophage markers arginase 1 and Fizz-1 in a STAT6-dependent process,” PLoS ONE, vol. 8, no. 8, Article ID e74676, 2013. View at Publisher · View at Google Scholar · View at Scopus
  206. J. Marsillach, J. O. Becker, T. Vaisar et al., “Paraoxonase-3 is depleted from the high-density lipoproteins of autoimmune disease patients with subclinical atherosclerosis,” Journal of Proteome Research, vol. 14, no. 5, pp. 2046–2054, 2015. View at Publisher · View at Google Scholar
  207. P. Malmberg, K. Börner, Y. Chen et al., “Localization of lipids in the aortic wall with imaging TOF-SIMS,” Biochimica et Biophysica Acta: Molecular and Cell Biology of Lipids, vol. 1771, no. 2, pp. 185–195, 2007. View at Publisher · View at Google Scholar · View at Scopus
  208. M. R. M. Domingues, A. Reis, and P. Domingues, “Mass spectrometry analysis of oxidized phospholipids,” Chemistry and Physics of Lipids, vol. 156, no. 1-2, pp. 1–12, 2008. View at Publisher · View at Google Scholar · View at Scopus
  209. A. J. Lepedda, A. Cigliano, G. M. Cherchi et al., “A proteomic approach to differentiate histologically classified stable and unstable plaques from human carotid arteries,” Atherosclerosis, vol. 203, no. 1, pp. 112–118, 2009. View at Publisher · View at Google Scholar · View at Scopus
  210. A. J. Lepedda, A. Zinellu, G. Nieddu et al., “Protein sulfhydryl group oxidation and mixed-disulfide modifications in stable and unstable human carotid plaques,” Oxidative Medicine and Cellular Longevity, vol. 2013, Article ID 403973, 8 pages, 2013. View at Publisher · View at Google Scholar · View at Scopus
  211. F. M. Faraci and S. P. Didion, “Vascular protection: superoxide dismutase isoforms in the vessel wall,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 24, no. 8, pp. 1367–1373, 2004. View at Publisher · View at Google Scholar · View at Scopus
  212. S. L. Harley, J. Sturge, and J. T. Powell, “Regulation by fibrinogen and its products of intercellular adhesion molecule-1 expression in human saphenous vein endothelial cells,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 20, no. 3, pp. 652–658, 2000. View at Publisher · View at Google Scholar · View at Scopus
  213. N. G. He, S. Awasthi, S. S. Singhal, M. B. Trent, and P. J. Boor, “The role of glutathione S-transferases as a defense against reactive electrophiles in the blood vessel wall,” Toxicology and Applied Pharmacology, vol. 152, no. 1, pp. 83–89, 1998. View at Publisher · View at Google Scholar · View at Scopus
  214. J. L. Martin-Ventura, V. Nicolas, X. Houard et al., “Biological significance of decreased HSP27 in human atherosclerosis,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 26, no. 6, pp. 1337–1343, 2006. View at Publisher · View at Google Scholar · View at Scopus
  215. G. J. Won, S. K. Hye, K.-G. Park et al., “Analysis of proteome and transcriptome of tumor necrosis factor α stimulated vascular smooth muscle cells with or without alpha lipoic acid,” Proteomics, vol. 4, no. 11, pp. 3383–3393, 2004. View at Publisher · View at Google Scholar · View at Scopus
  216. H. Kaji, “High-density lipoproteins and the immune system,” Journal of Lipids, vol. 2013, Article ID 684903, 8 pages, 2013. View at Publisher · View at Google Scholar
  217. B. Arnesjö, B. Danielsson, R. Ekman, B. G. Johansson, and B. G. Petersson, “Characterization of high density lipoproteins in human cholestasis,” Scandinavian Journal of Clinical and Laboratory Investigation, vol. 37, no. 7, pp. 587–597, 1977. View at Publisher · View at Google Scholar · View at Scopus
  218. P. H. Joshi, P. P. Toth, S. T. Lirette et al., “Association of high-density lipoprotein subclasses and incident coronary heart disease: The Jackson Heart and Framingham Offspring Cohort Studies,” European Journal of Preventive Cardiology, 2014. View at Publisher · View at Google Scholar
  219. D. S. Kim, A. A. Burt, E. A. Rosenthal et al., “HDL-3 is a superior predictor of carotid artery disease in a case-control cohort of 1725 participants,” Journal of the American Heart Association, vol. 3, no. 3, Article ID e000902, 2014. View at Publisher · View at Google Scholar
  220. S. S. Martin, A. A. Khokhar, H. T. May et al., “HDL cholesterol subclasses, myocardial infarction, and mortality in secondary prevention: the Lipoprotein Investigators Collaborative,” European Heart Journal, vol. 36, no. 1, pp. 22–30, 2015. View at Publisher · View at Google Scholar
  221. A. V. G. Edwards, M. Y. White, and S. J. Cordwell, “The role of proteomics in clinical cardiovascular biomarker discovery,” Molecular & Cellular Proteomics, vol. 7, no. 10, pp. 1824–1837, 2008. View at Publisher · View at Google Scholar · View at Scopus
  222. Y. Tan, T. R. Liu, S. W. Hu et al., “Acute coronary syndrome remodels the protein cargo and functions of high-density lipoprotein subfractions,” PLoS ONE, vol. 9, no. 4, Article ID e94264, 2014. View at Publisher · View at Google Scholar · View at Scopus
  223. L.-R. Yan, D.-X. Wang, H. Liu et al., “A pro-atherogenic HDL profile in coronary heart disease patients: an iTRAQ labelling-based proteomic approach,” PLoS ONE, vol. 9, no. 5, Article ID e98368, 2014. View at Publisher · View at Google Scholar · View at Scopus
  224. A. J. Lepedda, G. Nieddu, E. Zinellu et al., “Proteomic analysis of plasma-purified VLDL, LDL, and HDL fractions from atherosclerotic patients undergoing carotid endarterectomy: Identification of serum amyloid a as a potential marker,” Oxidative Medicine and Cellular Longevity, vol. 2013, Article ID 385214, 11 pages, 2013. View at Publisher · View at Google Scholar · View at Scopus
  225. M. Ståhlman, B. Fagerberg, M. Adiels et al., “Dyslipidemia, but not hyperglycemia and insulin resistance, is associated with marked alterations in the HDL lipidome in type 2 diabetic subjects in the DIWA cohort: impact on small HDL particles,” Biochimica et Biophysica Acta—Molecular and Cell Biology of Lipids, vol. 1831, no. 11, pp. 1609–1617, 2013. View at Publisher · View at Google Scholar · View at Scopus
  226. M. Holzer, R. Birner-Gruenberger, T. Stojakovic et al., “Uremia alters HDL composition and function,” Journal of the American Society of Nephrology, vol. 22, no. 9, pp. 1631–1641, 2011. View at Publisher · View at Google Scholar · View at Scopus
  227. A. Mangé, A. Goux, S. Badiou et al., “HDL proteome in hemodialysis patients: a quantitative nanoflow liquid chromatography-tandem mass spectrometry approach,” PLoS ONE, vol. 7, no. 3, Article ID e34107, 2012. View at Publisher · View at Google Scholar · View at Scopus
  228. C. Kopecky, B. Genser, C. Drechsler et al., “Quantification of HDL proteins, cardiac events, and mortality in patients with type 2 diabetes on hemodialysis,” Clinical Journal of the American Society of Nephrology, vol. 10, no. 2, pp. 224–231, 2015. View at Google Scholar
  229. J. Watanabe, C. Charles-Schoeman, Y. Miao et al., “Proteomic profiling following immunoaffinity capture of high-density lipoprotein: association of acute-phase proteins and complement factors with proinflammatory high-density lipoprotein in rheumatoid arthritis,” Arthritis and Rheumatism, vol. 64, no. 6, pp. 1828–1837, 2012. View at Publisher · View at Google Scholar · View at Scopus
  230. T. Weichhart, C. Kopecky, M. Kubicek et al., “Serum amyloid A in uremic HDL promotes inflammation,” Journal of the American Society of Nephrology, vol. 23, no. 5, pp. 934–947, 2012. View at Publisher · View at Google Scholar · View at Scopus
  231. H. N. Yassine, A. M. Jackson, P. D. Reaven et al., “The application of multiple reaction monitoring to assess ApoA-I methionine oxidations in diabetes and cardiovascular disease,” Translational Proteomics, vol. 4-5, pp. 18–24, 2014. View at Publisher · View at Google Scholar · View at Scopus
  232. M. K. Jensen, E. B. Rimm, J. D. Furtado, and F. M. Sacks, “Apolipoprotein C-III as a potential modulator of the association between HDL-cholesterol and incident coronary heart disease,” Journal of the American Heart Association, vol. 1, no. 2, Article ID e000232, 2012. View at Publisher · View at Google Scholar
  233. M. Kosuge, T. Ebina, T. Ishikawa et al., “Serum amyloid A is a better predictor of clinical outcomes than C-reactive protein in non-ST-segment elevation acute coronary syndromes,” Circulation Journal, vol. 71, no. 2, pp. 186–190, 2007. View at Publisher · View at Google Scholar · View at Scopus
  234. K. Alwaili, D. Bailey, Z. Awan et al., “The HDL proteome in acute coronary syndromes shifts to an inflammatory profile,” Biochimica et Biophysica Acta—Molecular and Cell Biology of Lipids, vol. 1821, no. 3, pp. 405–415, 2012. View at Publisher · View at Google Scholar · View at Scopus
  235. D. P. Cormode, J. C. Frias, Y. Ma et al., “HDL as a contrast agent for medical imaging,” Future Lipidology, vol. 4, no. 4, pp. 493–500, 2009. View at Publisher · View at Google Scholar · View at Scopus
  236. P. S. Green, T. Vaisar, S. Pennathur et al., “Combined statin and niacin therapy remodels the high-density lipoprotein proteome,” Circulation, vol. 118, no. 12, pp. 1259–1267, 2008. View at Publisher · View at Google Scholar · View at Scopus
  237. R. Laaksonen, M. T. Jänis, and M. Oresic, “Lipidomics-based safety biomarkers for lipid-lowering treatments,” Angiology, vol. 59, no. 2, pp. 65S–68S, 2008. View at Google Scholar · View at Scopus
  238. A. Keech, R. J. Simes, P. Barter et al., “Effects of long-term fenofibrate therapy on cardiovascular events in 9795 people with type 2 diabetes mellitus (the FIELD study): randomised controlled trial,” The Lancet, vol. 366, no. 9500, pp. 1849–1861, 2005. View at Publisher · View at Google Scholar
  239. P. V. Subbaiah and M. Liu, “Role of sphingomyelin in the regulation of cholesterol esterification in the plasma lipoproteins. Inhibition of lecithin-cholesterol acyltransferase reaction,” The Journal of Biological Chemistry, vol. 268, no. 27, pp. 20156–20163, 1993. View at Google Scholar · View at Scopus
  240. L. Yetukuri, I. Huopaniemi, A. Koivuniemi et al., “High density lipoprotein structural changes and drug response in lipidomic profiles following the long-term fenofibrate therapy in the FIELD substudy,” PLoS ONE, vol. 6, no. 8, Article ID e23589, 2011. View at Publisher · View at Google Scholar · View at Scopus
  241. M. F. Lopez, B. Krastins, D. A. Sarracino et al., “Proteomic signatures of serum albumin-bound proteins from stroke patients with and without endovascular closure of PFO are significantly different and suggest a novel mechanism for cholesterol efflux,” Clinical Proteomics, vol. 12, no. 1, article 2, 2015. View at Publisher · View at Google Scholar · View at Scopus
  242. M. C. Ochoa, J. Fioravanti, I. Rodriguez et al., “Antitumor immunotherapeutic and toxic properties of an HDL-conjugated chimeric IL-15 fusion protein,” Cancer Research, vol. 73, no. 1, pp. 139–149, 2013. View at Publisher · View at Google Scholar · View at Scopus
  243. J. Fioravanti, I. González, J. Medina-Echeverz et al., “Anchoring interferon alpha to apolipoprotein A-I reduces hematological toxicity while enhancing immunostimulatory properties,” Hepatology, vol. 53, no. 6, pp. 1864–1873, 2011. View at Publisher · View at Google Scholar · View at Scopus
  244. C. E. Kostara, A. Papathanasiou, N. Psychogios et al., “NMR-based lipidomic analysis of blood lipoproteins differentiates the progression of coronary heart disease,” Journal of Proteome Research, vol. 13, no. 5, pp. 2585–2598, 2014. View at Publisher · View at Google Scholar · View at Scopus
  245. C. E. Kostara, A. Papathanasiou, M. T. Cung, M. S. Elisaf, J. Goudevenos, and E. T. Bairaktari, “Evaluation of established coronary heart disease on the basis of HDL and non-HDL NMR lipid profiling,” Journal of Proteome Research, vol. 9, no. 2, pp. 897–911, 2010. View at Publisher · View at Google Scholar · View at Scopus
  246. C. Morgantini, D. Meriwether, S. Baldi et al., “HDL lipid composition is profoundly altered in patients with type 2 diabetes and atherosclerotic vascular disease,” Nutrition, Metabolism and Cardiovascular Diseases, vol. 24, no. 6, pp. 594–599, 2014. View at Publisher · View at Google Scholar · View at Scopus
  247. C. R. Sirtori, L. Calabresi, G. Franceschini et al., “Cardiovascular status of carriers of the apolipoprotein A-I Milano mutant: the limone sul garda study,” Circulation, vol. 103, no. 15, pp. 1949–1954, 2001. View at Publisher · View at Google Scholar · View at Scopus
  248. G. G. Schwartz, A. G. Olsson, M. Abt et al., “Effects of dalcetrapib in patients with a recent acute coronary syndrome,” The New England Journal of Medicine, vol. 367, no. 22, pp. 2089–2099, 2012. View at Publisher · View at Google Scholar · View at Scopus