Cholesterol
Volume 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
- WHO, “The top ten causes of death. Fact sheet 310,” 2011, http://www.who.int/mediacentre/factsheets/fs310_2008.pdf.
- 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
- 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
- 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/.
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- A. Jonas, “Lipoprotein structure,” in Biochemistry of Lipids, Lipoproteins and Membranes, Elsevier, Amsterdam, The Netherlands, 4th edition, 2002. View at Google Scholar
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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