Dysfunctional HDL and atherosclerotic cardiovascular disease

Rosenson, Robert S.; Brewer, H. Bryan; Ansell, Benjamin J.; Barter, Philip; Chapman, M. John; Heinecke, Jay W.; Kontush, Anatol; Tall, Alan R.; Webb, Nancy R.

doi:10.1038/nrcardio.2015.124

Cited by 822Cholesterol and Lipid MetabolismAtherosclerosis and Cardiovascular DiseasesLipoproteins and Cardiovascular Health

Dysfunctional HDL and atherosclerotic cardiovascular disease

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Rosenson, Robert S., Brewer, H. Bryan, Ansell, Benjamin J., Barter, Philip, Chapman, M. John, Heinecke, Jay W., Kontush, Anatol, Tall, Alan R. +1 more·2016·Nature Reviews Cardiology

DOI 10.1038/nrcardio.2015.124PMC PMC6245940

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Abstract

High-density lipoproteins (HDLs) protect against atherosclerosis by removing excess cholesterol from macrophages through the ATP-binding cassette transporter A1 (ABCA1) and ATP-binding cassette transporter G1 (ABCG1) pathways involved in reverse cholesterol transport. Factors that impair the availability of functional apolipoproteins or the activities of ABCA1 and ABCG1 could, therefore, strongly influence atherogenesis. HDL also inhibits lipid oxidation, restores endothelial function, exerts anti-inflammatory and antiapoptotic actions, and exerts anti-inflammatory actions in animal models. Such properties could contribute considerably to the capacity of HDL to inhibit atherosclerosis. Systemic and vascular inflammation has been proposed to convert HDL to a dysfunctional form that has impaired antiatherogenic effects. A loss of anti-inflammatory and antioxidative proteins, perhaps in combination with a gain of proinflammatory proteins, might be another important component in rendering HDL dysfunctional. The proinflammatory enzyme myeloperoxidase induces both oxidative modification and nitrosylation of specific residues on plasma and arterial apolipoprotein A-I to render HDL dysfunctional, which results in impaired ABCA1 macrophage transport, the activation of inflammatory pathways, and an increased risk of coronary artery disease. Understanding the features of dysfunctional HDL or apolipoprotein A-I in clinical practice might lead to new diagnostic and therapeutic approaches to atherosclerosis.

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Some studies have indicated a complete loss of function and dysfunction gain concerning anti-inflammatory, vasodilatory, and antiapoptotic activities of HDL.
“Some studies have indicated a complete loss of function and dysfunction gain concerning anti-inflammatory, vasodilatory, and antiapoptotic activities.”
From Residual Cardiovascular Risk: Role of Remnants Cholesterol, Monocyte/HDL Ratio and Lipoprotein Ratios on Personalized Cardiovascular Prevention (2024) · cites this paper as [9]
There are instances where HDL's ability to deliver cholesterol esters via SCARB1 may be reduced, indicating only a partial loss of function.
“However, there are instances where HDL’s ability to deliver cholesterol esters via SCARB1 may be reduced, indicating only a partial loss of function.”
From Residual Cardiovascular Risk: Role of Remnants Cholesterol, Monocyte/HDL Ratio and Lipoprotein Ratios on Personalized Cardiovascular Prevention (2024) · cites this paper as [9]
HDL can lose its anti-inflammatory properties and even develop proinflammatory characteristics.
“It was noted that HDL could lose its anti-inflammatory properties and even develop proinflammatory characteristics.”
From Residual Cardiovascular Risk: Role of Remnants Cholesterol, Monocyte/HDL Ratio and Lipoprotein Ratios on Personalized Cardiovascular Prevention (2024) · cites this paper as [9]
For antioxidative activity and cholesterol efflux capacity, the deficiency observed in HDL's normal function falls short of complete dysfunction.
“However, when it comes to antioxidative activity and cholesterol efflux capacity, the deficiency observed in HDL’s normal function falls short of complete dysfunction [9].”
From Residual Cardiovascular Risk: Role of Remnants Cholesterol, Monocyte/HDL Ratio and Lipoprotein Ratios on Personalized Cardiovascular Prevention (2024) · cites this paper as [9]
The extent of HDL's normal function loss and dysfunction gain can vary depending on its different biological activities.
“Subsequent research has shown that the extent of HDL’s normal function loss and dysfunction gain can vary depending on its different biological activities.”
From Residual Cardiovascular Risk: Role of Remnants Cholesterol, Monocyte/HDL Ratio and Lipoprotein Ratios on Personalized Cardiovascular Prevention (2024) · cites this paper as [9]

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Nahrendorf, M., Sosnovik, D. E., Chen, J. W., Panizzi, P. R., Figueiredo, J., Aikawa, E. R., Libby, P., Świrski, F. K., & Weissleder, R. (2008) · Circulation · doi:10.1161/circulationaha.107.756510 · Cited by 197 · see citing works
Serum amyloid A (SAA): influence on HDL-mediated cellular cholesterol efflux.
Banka, C. L., Yuan, T., de Beer, M. C., Kindy, M. S., Curtiss, L. K., & de Beer, F. C. (1995) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)39863-1 · Cited by 197 · see citing works
Overexpression of Secretory Phospholipase A2 Causes Rapid Catabolism and Altered Tissue Uptake of High Density Lipoprotein Cholesteryl Ester and Apolipoprotein A-I*
Tietge, U., Maugeais, C., Cain, W. J., Grass, D., Glick, J., de Beer, F. D., & Rader, D. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.14.10077 · Cited by 190 · see citing works
Methionine oxidation impairs reverse cholesterol transport by apolipoprotein A-I
Shao, B., Cavigiolio, G., Brot, N., Oda, M. N., & Heinecke, J. W. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802025105 · Cited by 189 · see citing works
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Myeloperoxidase: An Oxidative Pathway for Generating Dysfunctional High-Density Lipoprotein
Shao, B., Oda, M. N., Oram, J. F., & Heinecke, J. W. (2009) · Chemical Research in Toxicology · doi:10.1021/tx9003775 · Cited by 185 · see citing works
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Pharmacogenomic Determinants of the Cardiovascular Effects of Dalcetrapib
Tardif, J., Rhéaume, É., Perreault, L. L., Grégoire, J. C., Zada, Y. F., Asselin, G., Provost, S., Barhdadi, A., Rhainds, D., L’Allier, P. L., et al. (2015) · Circulation Cardiovascular Genetics · doi:10.1161/circgenetics.114.000663 · Cited by 183 · see citing works
Effect of a short-term diet and exercise intervention on inflammatory/anti-inflammatory properties of HDL in overweight/obese men with cardiovascular risk factors
Roberts, C. K., Ng, C. J., Hama, S. Y., Eliseo, A. J. Y., & Barnard, R. J. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00345.2006 · Cited by 178 · see citing works
Platelet-activating Factor Acetylhydrolase, and Not Paraoxonase-1, Is the Oxidized Phospholipid Hydrolase of High Density Lipoprotein Particles
Marathe, G. K., Zimmerman, G. A., & McIntyre, T. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211126200 · Cited by 175 · see citing works
Expression of Human Myeloperoxidase by Macrophages Promotes Atherosclerosis in Mice
McMillen, T. S., Heinecke, J. W., & LeBoeuf, R. C. (2005) · Circulation · doi:10.1161/circulationaha.104.516278 · Cited by 168 · see citing works
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Enzyme-Sensitive Magnetic Resonance Imaging Targeting Myeloperoxidase Identifies Active Inflammation in Experimental Rabbit Atherosclerotic Plaques
Ronald, J. A., Chen, J. W., Chen, Y., Hamilton, A. M., Rodrı́guez, E., Reynolds, F., Hegele, R. A., Rogers, K. A., Querol, M., Bogdanov, A. A., Jr., et al. (2009) · Circulation · doi:10.1161/circulationaha.108.813998 · Cited by 161 · see citing works
HDL3-Mediated Inactivation of LDL-Associated Phospholipid Hydroperoxides Is Determined by the Redox Status of Apolipoprotein A-I and HDL Particle Surface Lipid Rigidity
Zerrad-Saadi, A., Thérond, P., Chantepie, S., Couturier, M., Rye, K., Chapman, M. J., & Kontush, A. (2009) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.109.194555 · Cited by 159 · see citing works
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Plasma HDL cholesterol and risk of myocardial infarction: a mendelian randomisation study
Voight, B. F., Peloso, G. M., Orho-Melander, M., Frikke-Schmidt, R., Barbalic, M., Jensen, M. K., Hindy, G., Hólm, H., Ding, E. L., Johnson, T., et al. (2012) · The Lancet · doi:10.1016/s0140-6736(12)60312-2 · Cited by 148 · see citing works
Effects of native and myeloperoxidase-modified apolipoprotein A-I on reverse cholesterol transport and atherosclerosis in mice
Hewing, B., Parathath, S., Barrett, T. J., Chung, W. K. K., Astudillo, Y., Hamada, T., Ramkhelawon, B., Tallant, T. C., Yusufishaq, M., DiDonato, J., et al. (2014) · Arteriosclerosis, Thrombosis and Vascular Biology · doi:10.1161/atvbaha.113.303044 · Cited by 147 · see citing works
Apolipoprotein C‐III as a Potential Modulator of the Association Between HDL‐Cholesterol and Incident Coronary Heart Disease
Jensen, M. K., Rimm, E. B., Furtado, J. D., & Sacks, F. M. (2012) · Journal of the American Heart Association · doi:10.1161/jaha.111.000232 · Cited by 142 · see citing works
A normotriglyceridemic, low HDL-cholesterol phenotype is characterised by elevated oxidative stress and HDL particles with attenuated antioxidative activity
Kontush, A., de Faria, E. C., Chantepie, S., & Chapman, M. J. (2005) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2005.03.001 · Cited by 141 · see citing works
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Reciprocal and Coordinate Regulation of Serum Amyloid A Versus Apolipoprotein A-I and Paraoxonase-1 by Inflammation in Murine Hepatocytes
Han, C. Y., Chiba, T., Campbell, J. S., Fausto, N., Chaisson, M. L., Orasanu, G., Plutzky, J., & Chait, A. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000227472.70734.ad · Cited by 140 · see citing works
HDL content and composition in acute phase response in three species: triglyceride enrichment of HDL a factor in its decrease
Cabana, V. G., Lukens, J. R., Rice, K. S., Hawkins, T., & Getz, G. S. (1996) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)37469-1 · Cited by 129 · see citing works
Metabolic syndrome features small, apolipoprotein A-I-poor, triglyceride-rich HDL3 particles with defective anti-apoptotic activity
Souza, J. A., Vindis, C., Hansel, B., Nègre‐Salvayre, A., Thérond, P., Junior, C. V. S., Chantepie, S., Salvayre, R., Bruckert, É., Chapman, M. J., et al. (2007) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2007.08.009 · Cited by 125 · see citing works
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Overexpression of Human Lecithin Cholesterol Acyltransferase Leads to Hyperalphalipoproteinemia in Transgenic Mice
Vaisman, B. L., Klein, H., Rouis, M., Bérard, A. M., Kindt, M. R., Talley, G. D., Meyn, S. M., Hoyt, R. F., Marcovina, S. M., Albers, J. J., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.20.12269 · Cited by 125 · see citing works
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Effects of cigarette smoking on HDL quantity and function: Implications for atherosclerosis
He, B., Zhao, S., & Peng, Z. (2013) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24581 · Cited by 123 · see citing works
Lysine Residues Direct the Chlorination of Tyrosines in YXXK Motifs of Apolipoprotein A-I When Hypochlorous Acid Oxidizes High Density Lipoprotein
Bergt, C., Fu, X., Saifee, N. H., Kao, J. L.-F., & Heinecke, J. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309046200 · Cited by 123 · see citing works
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Why is HDL functionally deficient in type 2 diabetes?
Kontush, A., & Chapman, M. J. (2008) · Current Diabetes Reports · doi:10.1007/s11892-008-0010-5 · Cited by 116 · see citing works
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Inability of HDL from type 2 diabetic patients to counteract the inhibitory effect of oxidised LDL on endothelium-dependent vasorelaxation
Perségol, L., Vergès, B. L., Foissac, M., Gambert, P., & Duvillard, L. (2006) · Diabetologia · doi:10.1007/s00125-006-0244-1 · Cited by 104 · see citing works
Dose-dependent action of atorvastatin in type IIB hyperlipidemia: preferential and progressive reduction of atherogenic apoB-containing lipoprotein subclasses (VLDL-2, IDL, small dense LDL) and stimulation of cellular cholesterol efflux
Guérin, M., Egger, P., Soudant, C., Goff, W. L., van Tol, A., Dupuis, R., & Chapman, M. J. (2002) · Atherosclerosis · doi:10.1016/s0021-9150(02)00037-0 · Cited by 99 · see citing works
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Apolipoprotein A-I Tryptophan Substitution Leads to Resistance to Myeloperoxidase-Mediated Loss of Function
Peng, D.-Q., Brubaker, G., Wu, Z., Zheng, L., Willard, B. B., Kinter, M. T., Hazen, S. L., & Smith, J. D. (2008) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.108.173815 · Cited by 99 · see citing works
Site-specific Nitration of Apolipoprotein A-I at Tyrosine 166 Is Both Abundant within Human Atherosclerotic Plaque and Dysfunctional
DiDonato, J. A., Aulak, K. S., Huang, Y. R., Wagner, M. A., Gerstenecker, G. S., Topbas, C., Gogonea, V., DiDonato, A. J., Tang, W. H. W., Mehl, R. A., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.556506 · Cited by 96 · see citing works
Myeloperoxidase Generates 5-Chlorouracil in Human Atherosclerotic Tissue
Takeshita, J., Byun, J., Nhan, T. Q., Pritchard, D. K., Pennathur, S., Schwartz, S. M., Chait, A., & Heinecke, J. W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509236200 · Cited by 95 · see citing works
Self-citation
Persistent abnormalities in lipoprotein composition in noninsulin-dependent diabetes after intensive insulin therapy.
Bagdade, J. D., Buchanan, W., Kuusi, T., & Taskinen, M. (1990) · Arteriosclerosis An Official Journal of the American Heart Association Inc · doi:10.1161/01.atv.10.2.232 · Cited by 95 · see citing works
Oxidation of apolipoprotein A-I by myeloperoxidase impairs the initial interactions with ABCA1 required for signaling and cholesterol export
Shao, B., Tang, C., Heinecke, J. W., & Oram, J. F. (2010) · Journal of Lipid Research · doi:10.1194/jlr.m004085 · Cited by 94 · see citing works
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Acute hypertriglyceridaemia in humans increases the triglyceride content and decreases the anti-inflammatory capacity of high density lipoproteins
Patel, S., Puranik, R., Nakhla, S., Lundman, P., Stocker, R., Wang, X., Lambert, G. C., Rye, K.-A., Barter, P. J., Nicholls, S. J., et al. (2008) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2008.07.047 · Cited by 92 · see citing works
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Low Clusterin Levels in High-Density Lipoprotein Associate With Insulin Resistance, Obesity, and Dyslipoproteinemia
Hoofnagle, A. N., Wu, M., Gosmanova, A. K., Becker, J. O., Wijsman, E. M., Brunzell, J. D., Kahn, S. E., Knopp, R. H., Lyons, T. J., & Heinecke, J. W. (2010) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.110.212894 · Cited by 87 · see citing works
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The effect of cholesteryl ester transfer protein inhibition on lipids, lipoproteins, and markers of HDL function after an acute coronary syndrome: the dal-ACUTE randomized trial
Ray, K. K., Ditmarsch, M., Kallend, D. G., Niesor, E. J., Suchánková, G., Upmanyu, R., Anzures‐Cabrera, J., Lehnert, V., Pauly-Evers, M., Holme, I., et al. (2014) · European Heart Journal · doi:10.1093/eurheartj/ehu105 · Cited by 87 · see citing works
Effect of Bariatric Surgery-Induced Weight Loss on SR-BI-, ABCG1-, and ABCA1-Mediated Cellular Cholesterol Efflux in Obese Women
Aron‐Wisnewsky, J., Julia, Z., Poitou, C., Bouillot, J., Basdevant, A., Chapman, M. J., Clément, K., & Guérin, M. (2011) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2010-2378 · Cited by 83 · see citing works
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Alterations in the main steps of reverse cholesterol transport in male patients with primary hypertriglyceridemia and low HDL-cholesterol levels
Brites, F. D., Bonavita, C. D., Geitere, C. D., Cloës, M., Delfly, B., Yael, M. J., Fruchart, J., Wikinski, R. L. W., & Castro, G. R. (2000) · Atherosclerosis · doi:10.1016/s0021-9150(99)00452-9 · Cited by 83 · see citing works
Antioxidative Activity of HDL Particle Subspecies Is Impaired in Hyperalphalipoproteinemia: Relevance of Enzymatic and Physicochemical Properties
Kontush, A., de Faria, E. C., Chantepie, S., & Chapman, M. J. (2004) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000118276.87061.00 · Cited by 79 · see citing works
Self-citation
Anacetrapib promotes reverse cholesterol transport and bulk cholesterol excretion in Syrian golden hamsters
Castro‐Perez, J. M., Briand, F., Gagen, K., Wang, S., Chen, Y., McLaren, D. G., Shah, V., Vreeken, R. J., Hankemeier, T., Sulpice, T., et al. (2011) · Journal of Lipid Research · doi:10.1194/jlr.m016410 · Cited by 78 · see citing works
Pathways for oxidation of low density lipoprotein by myeloperoxidase: tyrosyl radical, reactive aldehydes, hypochlorous acid and molecular chlorine
Heinecke, J. W. (1997) · BioFactors · doi:10.1002/biof.5520060208 · Cited by 78 · see citing works
Self-citation
The Addition of Niacin to Statin Therapy Improves High-Density Lipoprotein Cholesterol Levels But Not Metrics of Functionality
Khera, A. V., Patel, P. J., Reilly, M. P., & Rader, D. J. (2013) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2013.07.025 · Cited by 74 · see citing works
HDL modification by secretory phospholipase A2 promotes scavenger receptor class B type I interaction and accelerates HDL catabolism
de Beer, F. C., Connell, P. M., Yu, J., de Beer, M. C., Webb, N. R., & van der Westhuyzen, D. R. (2000) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)31979-9 · Cited by 72 · see citing works
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Abnormal Reverse Cholesterol Transport in Controlled Type II Diabetic Patients
Cavallero, E., Brites, F. D., Delfly, B., Nicolaı̈ew, N., Decossin, C., Geitere, C. D., Fruchart, J., Wikinski, R. L. W., JACOTOT, B., & Castro, G. R. (1995) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.15.12.2130 · Cited by 71 · see citing works
Phospholipase Action of Platelet-activating Factor Acetylhydrolase, but Not Paraoxonase-1, on Long Fatty Acyl Chain Phospholipid Hydroperoxides
Kriska, T., Marathe, G. K., Schmidt, J. C., McIntyre, T. M., & Girotti, A. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608135200 · Cited by 70 · see citing works
Secretory phospholipase A2: A multifaceted family of proatherogenic enzymes
Rosenson, R. S., & Gelb, M. H. (2009) · Current Cardiology Reports · doi:10.1007/s11886-009-0064-2 · Cited by 70 · see citing works
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Statin-Induced Decrease in ATP-Binding Cassette Transporter A1 Expression via microRNA33 Induction may Counteract Cholesterol Efflux to High-Density Lipoprotein
Niesor, E. J., Schwartz, G. G., Perez, A., Stauffer, A., Durrwell, A., Suchánková, G., Benghozi, R., Abt, M., & Kallend, D. G. (2015) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-015-6570-0 · Cited by 69 · see citing works
Torcetrapib Differentially Modulates the Biological Activities of HDL2 and HDL3 Particles in the Reverse Cholesterol Transport Pathway
Catalano, G., Julia, Z., Frisdal, É., Vedie, B., Fournier, N., Goff, W. L., Chapman, M. J., & Guérin, M. (2008) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.108.179416 · Cited by 68 · see citing works
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Pitavastatin Increases HDL Particles Functionally Preserved with Cholesterol Efflux Capacity and Antioxidative Actions in Dyslipidemic Patients
Miyamoto–Sasaki, M., Yasuda, T., Monguchi, T., Nakajima, H., Mori, K., Toh, R., Ishida, T., & Hirata, K. (2013) · Journal of Atherosclerosis and Thrombosis · doi:10.5551/jat.17210 · Cited by 67 · see citing works
HDL particles from type 1 diabetic patients are unable to reverse the inhibitory effect of oxidised LDL on endothelium-dependent vasorelaxation
Perségol, L., Foissac, M., Lagrost, L., Athias, A., Gambert, P., Vergès, B. L., & Duvillard, L. (2007) · Diabetologia · doi:10.1007/s00125-007-0808-8 · Cited by 67 · see citing works
Both Paraoxonase-1 Genotype and Activity Do Not Predict the Risk of Future Coronary Artery Disease; the EPIC-Norfolk Prospective Population Study
Birjmohun, R. S., Vergeer, M., Stroes, E. S. G., Sandhu, M. S., Ricketts, S. L., Tanck, M. W. T., Wareham, N. J., Jukema, J. W., Kastelein, J. J. P., Khaw, K., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006809 · Cited by 64 · see citing works
Atheroprotective lipoprotein effects of a niacin-simvastatin combination compared to low- and high-dose simvastatin monotherapy
Airan‐Javia, S., Wolf, R. L., Wolfe, M. L., Tadesse, M. G., Mohler, E. R., & Reilly, M. P. (2009) · American Heart Journal · doi:10.1016/j.ahj.2009.01.001 · Cited by 62 · see citing works
Paraoxonase-3 Is Depleted from the High-Density Lipoproteins of Autoimmune Disease Patients with Subclinical Atherosclerosis
Marsillach, J., Becker, J. O., Vaisar, T., Hahn, B. H., Brunzell, J. D., Furlong, C. E., de Boer, I. H., McMahon, M. A., Hoofnagle, A. N., & DCCT/EDIC Research Group (2015) · Journal of Proteome Research · doi:10.1021/pr5011586 · Cited by 61 · see citing works
Anti-Oxidative and Cholesterol Efflux Capacities of High-Density Lipoprotein are Reduced in Ischaemic Cardiomyopathy
Patel, P. J., Khera, A. V., Wilensky, R. L., & Rader, D. J. (2013) · European Journal of Heart Failure · doi:10.1093/eurjhf/hft084 · Cited by 61 · see citing works
Defective functionality of small, dense HDL3 subpopulations in ST segment elevation myocardial infarction: Relevance of enrichment in lysophosphatidylcholine, phosphatidic acid and serum amyloid A
Rached, F. H., Lhomme, M., Camont, L., Gomes, F. L. T., Dauteuille, C., Robillard, P., Santos, R. D., Lesnik, P., Junior, C. V. S., Chapman, M. J., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2015.05.007 · Cited by 59 · see citing works
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Effect of dalcetrapib plus pravastatin on lipoprotein metabolism and high-density lipoprotein composition and function in dyslipidemic patients: Results of a phase IIb dose-ranging study
Ballantyne, C. M., Miller, M. J., Niesor, E. J., Burgess, T., Kallend, D. G., & Stein, E. A. (2012) · American Heart Journal · doi:10.1016/j.ahj.2011.11.017 · Cited by 58 · see citing works
Secretory non-pancreatic phospholipase A2: influence on lipoprotein metabolism
de Beer, F. C., de Beer, M. C., van der Westhuyzen, D. R., Castellani, L. W., Lusis, A. J., Swanson, M. E., & Grass, D. (1997) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)34937-3 · Cited by 56 · see citing works
Studies on protective effects of human paraoxonases 1 and 3 on atherosclerosis in apolipoprotein E knockout mice
Zhang, C., Peng, W., WANG, M., Zhu, J., Zang, Y., Shi, W., Zhang, J., & Qin, J. (2010) · Gene Therapy · doi:10.1038/gt.2010.11 · Cited by 49 · see citing works
Lipoproteins as Biomarkers and Therapeutic Targets in the Setting of Acute Coronary Syndrome
Rosenson, R. S., Brewer, H. B., & Rader, D. J. (2014) · Circulation Research · doi:10.1161/circresaha.114.302805 · Cited by 45 · see citing works
Self-citation
Dysfunctional Lipoproteins from Young Smokers Exacerbate Cellular Senescence and Atherogenesis with Smaller Particle Size and Severe Oxidation and Glycation
Park, K.-H., Shin, D., & Cho, K. (2014) · Toxicological Sciences · doi:10.1093/toxsci/kfu076 · Cited by 44 · see citing works
A High Throughput Biochemical Fluorometric Method for Measuring Lipid Peroxidation in HDL
Kelesidis, T., Roberts, C. K., Huynh, D., Martı́nez-Maza, O., Currier, J. S., Reddy, S. T., & Yang, O. O. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111716 · Cited by 41 · see citing works
Specific Phospholipid Association with Apolipoprotein A-I Stimulates Cholesterol Efflux from Human Fibroblasts
Zhao, Y., Sparks, D. L., & Marcel, Y. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.41.25145 · Cited by 38 · see citing works
Evidence for the presence of lipid-free monomolecular apolipoprotein A-1 in plasma
Miyazaki, O., Ogihara, J., Fukamachi, I., & Kasumi, T. (2013) · Journal of Lipid Research · doi:10.1194/jlr.m041038 · Cited by 37 · see citing works
The implication of cigarette smoking and cessation on macrophage cholesterol efflux in coronary artery disease patients
Song, W., Wang, W., Dou, L.-Y., Wang, Y., Xu, Y., Chen, L., & Yan, X. (2015) · Journal of Lipid Research · doi:10.1194/jlr.p055491 · Cited by 36 · see citing works
Adenovirus-mediated expression of hepatic lipase in LCAT transgenic mice
Dugi, K. A., Vaisman, B. L., Sakai, N., Knapper, C. L., Meyn, S. M., Brewer, H. B., & Santamarina-Fojo, S. (1997) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)37156-x · Cited by 33 · see citing works
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The 15-Lipoxygenase-Modified High Density Lipoproteins 3 Fail to Inhibit the TNF-α-Induced Inflammatory Response in Human Endothelial Cells
Pirillo, A., Uboldi, P., Bolego, C., Kühn, H., & Catapano, A. L. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.4.2821 · Cited by 30 · see citing works
Mendelian randomisation, lipids, and cardiovascular disease
Harrison, S. C., Holmes, M. V., & Humphries, S. E. (2012) · The Lancet · doi:10.1016/s0140-6736(12)60481-4 · Cited by 30 · see citing works
HDL levels and oxidizability during myocardial infarction are associated with reduced endothelial-mediated vasodilation and nitric oxide bioavailability
de Carvalho, L. S. F., Panzoldo, N. B., dos Santos, S. N., Modolo, R., Almeida, B. O., Silva, J. C. Q. E., Nadruz, W., de Faria, E. C., & Sposito, A. C. (2014) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2014.10.103 · Cited by 30 · see citing works
Disorders in High-Density Metabolism With Insulin Resistance and Chronic Kidney Disease
Kaysen, G. A. (2007) · Journal of Renal Nutrition · doi:10.1053/j.jrn.2006.10.002 · Cited by 27 · see citing works
Nascent HDL formation by hepatocytes is reduced by the concerted action of serum amyloid A and endothelial lipase
Wroblewski, J. M., Jahangiri, A., Ji, A., de Beer, F. C., van der Westhuyzen, D. R., & Webb, N. R. (2011) · Journal of Lipid Research · doi:10.1194/jlr.m017681 · Cited by 27 · see citing works
Self-citation
C-Reactive Protein, Serum Amyloid A Protein, and Coronary Events
Choudhury, R. P., & Leyva, F. (1999) · Circulation · doi:10.1161/01.cir.100.15.e65 · Cited by 26 · see citing works
Reduction of cold ischemia–reperfusion injury by graft-expressing clusterin in heart transplantation
Li, S., Guan, Q., Chen, Z., Gleave, M. E., Nguan, C. Y. C., & Du, C. (2011) · The Journal of Heart and Lung Transplantation · doi:10.1016/j.healun.2011.03.007 · Cited by 25 · see citing works
Effects of lipid-probe interactions in biochemical fluorometric methods that assess HDL redox activity
Kelesidis, T., Reddy, S. T., Huynh, D., Meriwether, D., Fogelman, A. M., Navab, M., & Yang, O. O. (2012) · Lipids in Health and Disease · doi:10.1186/1476-511x-11-87 · Cited by 24 · see citing works
Oxidized phospholipid content destabilizes the structure of reconstituted high density lipoprotein particles and changes their function
Kar, S., Patel, M. A., Tripathy, R. K., Bajaj, P., Suvarnakar, U. V., & Pande, A. H. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2012.05.002 · Cited by 18 · see citing works
Associations among smoking status, lifestyle and lipoprotein subclasses
Beauchamp, A., Tonkin, A. M., Peeters, A., Wolfe, R. S., Turrell, G., Harriss, L. R., Giles, G. G., English, D. R., & Jenkins, A. J. (2010) · Journal of clinical lipidology · doi:10.1016/j.jacl.2010.09.003 · Cited by 16 · see citing works
Extended-Release Niacin/Laropiprant Effects on Lipoprotein Subfractions in Patients with Type 2 Diabetes Mellitus
Bays, H. E., Giezek, H., McKenney, J. M., O’Neill, E. A., & Tershakovec, A. M. (2012) · Metabolic Syndrome and Related Disorders · doi:10.1089/met.2012.0005 · Cited by 12 · see citing works

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Triglyceride-rich lipoproteins and their remnants: metabolic insights, role in atherosclerotic cardiovascular disease, and emerging therapeutic strategies—a consensus statement from the European Atherosclerosis Society
Ginsberg, H. N., Packard, C. J., Chapman, M. J., Borén, J., Aguilar-Salinas, C. A., Averna, M., Ference, B. A., Gaudet, D., Hegele, R. A., Kersten, S., et al. (2021) · European Heart Journal · doi:10.1093/eurheartj/ehab551 · Cited by 979 · see citing works
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Evacetrapib and cardiovascular outcomes in high-risk vascular disease
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Modified Lipoproteins Induce Arterial Wall Inflammation During Atherogenesis
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Association Between Oxidation-Modified Lipoproteins and Coronary Plaque in Psoriasis
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Oxidative Stress in Human Atherothrombosis: Sources, Markers and Therapeutic Targets
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High Concentration of Medium-Sized HDL Particles and Enrichment in HDL Paraoxonase 1 Associate With Protection From Vascular Complications in People With Long-standing Type 1 Diabetes
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Genotype-Dependent Effects of Dalcetrapib on Cholesterol Efflux and Inflammation
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CSL112 (Apolipoprotein A-I [Human]) Enhances Cholesterol Efflux Similarly in Healthy Individuals and Stable Atherosclerotic Disease Patients
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Interleukin-32 in chronic inflammatory conditions is associated with a higher risk of cardiovascular diseases
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Triglyceride-lowering therapies reduce cardiovascular disease event risk in subjects with hypertriglyceridemia
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MicroRNA-23a-5p promotes atherosclerotic plaque progression and vulnerability by repressing ATP-binding cassette transporter A1/G1 in macrophages
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Deficiency of Histone Methyltransferase SET Domain‐Containing 2 in Liver Leads to Abnormal Lipid Metabolism and HCC
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HDL Dysfunctionality: Clinical Relevance of Quality Rather Than Quantity
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HDL: Fact, fiction, or function? HDL cholesterol and cardiovascular risk
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Lipid metabolism in women: A review
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New Era of Lipid-Lowering Drugs
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Relations of GlycA and lipoprotein particle subspecies with cardiovascular events and mortality: A post hoc analysis of the AIM-HIGH trial
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Cyclocarya paliurus Leaves Tea Improves Dyslipidemia in Diabetic Mice: A Lipidomics-Based Network Pharmacology Study
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Assessing the performance of monocyte to high-density lipoprotein ratio for predicting ischemic stroke: insights from a population-based Chinese cohort
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HDL Proteome and Alzheimer’s Disease: Evidence of a Link
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Authors: Rosenson, R. S., Brewer, H. B., Ansell, B. J., Barter, P., Chapman, M. J., Heinecke, J. W., Kontush, A., Tall, A. R., & Webb, N. R.
Affiliations: Icahn School of Medicine at Mount Sinai (US)
MedStar Washington Hospital Center (US)
University of California, Los Angeles (US)
UNSW Sydney (AU)
Inserm (FR)
University of Washington (US)
Columbia University (US)
University of Kentucky (US)
Corresponding author: Rosenson, Robert S.
ORCID: Rosenson, Robert S.
Chapman, M. John
Heinecke, Jay W.
Kontush, Anatol
Tall, Alan R.
Webb, Nancy R.
Venue: Nature Reviews Cardiology
Publisher: Springer Science and Business Media LLC
Published: 2015-09-01
Volume: 13
Issue: 1
Pages: 48-60
ISSN: 1759-5002 (ISSN-L)
1759-5010
DOI: 10.1038/nrcardio.2015.124
PMC: PMC6245940
OpenAlex: W2175680864
Cited by: 822
References: 131
Citations by year: 2026: 89 · 2025: 89 · 2024: 66 · 2023: 79 · 2022: 86 · 2021: 79 · 2020: 79 · 2019: 62 · 2018: 69 · 2017: 61 · 2016: 56 · 2015: 5 · 2014: 1
FWCI: 12.01
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Nature Reviews Cardiology (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute of Diabetes and Digestive and Kidney Diseases (DP3DK108209, P30DK017047)
Topics: Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
Life Sciences › Immunology and Microbiology › Immunology › Atherosclerosis and Cardiovascular Diseases
Health Sciences › Medicine › Surgery › Lipoproteins and Cardiovascular Health
Keywords: HDL dysfunction, atherosclerosis, apolipoprotein A-I, reverse cholesterol transport, ABCA1, ABCG1, myeloperoxidase, nitrosylation, oxidative modification, inflammation, endothelial function, coronary artery disease, atherogenesis, anti-inflammatory activity
MeSH terms: Humans, Lipoproteins, HDL, Macrophages, Smoking, Apolipoprotein A-I, ATP-Binding Cassette Transporters, Diabetes Complications, Atherosclerosis, ATP Binding Cassette Transporter 1

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