Cited by 138

The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.

Molecular Pathways Underlying Cholesterol Homeostasis

Afonso, Milessa Silva, Machado, Roberta Marcondes, Lavrador, Maria, Quintao, Eder Carlos Rocha, Moore, Kathryn, Lottenberg, Ana·2018·Nutrients

Abstract

Cholesterol is an essential molecule that exerts pleiotropic actions. Although its presence is vital to the cell, its excess can be harmful and, therefore, sustaining cholesterol homeostasis is crucial to maintaining proper cellular functioning. It is well documented that high plasma cholesterol concentration increases the risk of atherosclerotic heart disease. In the last decades, several studies have investigated the association of plasma cholesterol concentrations and the risk of cardiovascular diseases as well as the signaling pathways involved in cholesterol homeostasis. Here, we present an overview of several mechanisms involved in intestinal cholesterol absorption, the regulation of cholesterol synthesis and uptake. We also discuss the importance of reverse cholesterol transport and transintestinal cholesterol transport to maintain cholesterol homeostasis and prevent atherosclerosis development. Additionally, we discuss the influence of dietary cholesterol on plasma cholesterol concentration and the new recommendations for cholesterol intake in a context of a healthy dietary pattern.

Verifying this paper

8 of 9 steps done · this page updates itself — you can leave and come back

  1. Registry recordVerified
  2. Full textFetching the open-access text — a few minutes for a paper we haven’t read before
  3. Reference listNot fetched yet
  4. Reference checkNot run yet for this paper
  5. StatisticsNeeds the full text
  6. ClaimsNeeds the full text
  7. Cited sourcesNeeds claims to check
  8. Self-checkNeeds the full text
  9. VerificationFindings verified

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3390/nu10060760

Cites

8 of 8 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Cholesterol accumulation can trigger compensatory regulatory mechanisms, including reducing cholesterol synthesis and enhancing bile acid synthesis, to eliminate high cholesterol levels and attempt to return the liver to a steady state.

    “In general, cholesterol accumulation can trigger compensatory regulatory mechanisms, including reducing cholesterol synthesis and enhancing bile acid synthesis, to eliminate high cholesterol levels and attempt to return the liver to a steady state.85–88”

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 125

  1. Ikonen, 2008, Cellular cholesterol trafficking and compartmentalization, Nat. Rev. Mol. Cell Biol., 9, 125, 10.1038/nrm2336 · DOI
  2. Lingwood, 2010, Lipid rafts as a membrane-organizing principle, Science, 327, 46, 10.1126/science.1174621 · DOI · Paper page
  3. Maxfield, 2010, Cholesterol, the central lipid of mammalian cells, Curr. Opin. Cell Biol., 22, 422, 10.1016/j.ceb.2010.05.004 · DOI · Paper page
  4. Bandyopadhyay, 2018, Cardiovascular Outcomes of PCSK9 Inhibitors: With Special Emphasis on Its Effect beyond LDL-Cholesterol Lowering, J. Lipids, 2018, 3179201, 10.1155/2018/3179201 · DOI
  5. Benjamin, 2018, Heart Disease and Stroke Statistics-2018 Update: A Report from the American Heart Association, Circulation, 137, e67, 10.1161/CIR.0000000000000558 · DOI · Paper page
  6. Mok, 1979, Effects of continuous and intermittent feeding on biliary lipid outputs in man: Application for measurements of intestinal absorption of cholesterol and bile acids, J. Lipid Res., 20, 389, 10.1016/S0022-2275(20)40622-4 · DOI
  7. Ikeda, 2015, Factors affecting intestinal absorption of cholesterol and plant sterols and stanols, J. Oleo Sci., 64, 9, 10.5650/jos.ess14221 · DOI
  8. Altmann, 2004, Niemann-Pick C1 Like 1 protein is critical for intestinal cholesterol absorption, Science, 303, 1201, 10.1126/science.1093131 · DOI
  9. Nguyen, 2012, Cholesterol esterification by ACAT2 is essential for efficient intestinal cholesterol absorption: Evidence from thoracic lymph duct cannulation, J. Lipid Res., 53, 95, 10.1194/jlr.M018820 · DOI · Paper page
  10. Iqbal, 2009, Intestinal lipid absorption, Am. J. Physiol. Endocrinol. Metab., 296, E1183, 10.1152/ajpendo.90899.2008 · DOI · Paper page
  11. Yu, 2002, Disruption of Abcg5 and Abcg8 in mice reveals their crucial role in biliary cholesterol secretion, Proc. Natl. Acad. Sci. USA, 99, 16237, 10.1073/pnas.252582399 · DOI
  12. Sugizaki, 2014, The Niemann-Pick C1 like 1 (NPC1L1) inhibitor ezetimibe improves metabolic disease via decreased liver X receptor (LXR) activity in liver of obese male mice, Endocrinology, 155, 2810, 10.1210/en.2013-2143 · DOI
  13. Yu, 2003, Stimulation of cholesterol excretion by the liver X receptor agonist requires ATP-binding cassette transporters G5 and G8, J. Biol. Chem., 278, 15565, 10.1074/jbc.M301311200 · DOI
  14. Hu, 2012, LXRβ activation increases intestinal cholesterol absorption, leading to an atherogenic lipoprotein profile, J. Intern. Med., 272, 452, 10.1111/j.1365-2796.2012.02529.x · DOI
  15. Hui, 2017, The good side of cholesterol: A requirement for maintenance of intestinal integrity, J. Lipid Res., 58, 1935, 10.1194/jlr.C079715 · DOI
  16. Adams, 2004, Cholesterol and 25-hydroxycholesterol inhibit activation of SREBPs by different mechanisms, both involving SCAP and Insigs, J. Biol. Chem., 279, 52772, 10.1074/jbc.M410302200 · DOI
  17. Brown, 2018, Retrospective on Cholesterol Homeostasis: The Central Role of Scap, Annu. Rev. Biochem., 87, 1.1, 10.1146/annurev-biochem-062917-011852 · DOI · Paper page
  18. Gong, 2006, Sterol-regulated ubiquitination and degradation of Insig-1 creates a convergent mechanism for feedback control of cholesterol synthesis and uptake, Cell Metab., 3, 15, 10.1016/j.cmet.2005.11.014 · DOI · Paper page
  19. Sun, 2005, Insig required for sterol-mediated inhibition of Scap/SREBP binding to COPII proteins in vitro, J. Biol. Chem., 280, 26483, 10.1074/jbc.M504041200 · DOI · Paper page
  20. Sato, 2004, COPII coat assembly and selective export from the endoplasmic reticulum, J. Biochem., 136, 755, 10.1093/jb/mvh184 · DOI
  21. Sun, 2007, Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: Insig renders sorting signal in Scap inaccessible to COPII proteins, Proc. Natl. Acad. Sci. USA, 104, 6519, 10.1073/pnas.0700907104 · DOI
  22. Brown, 2002, Cholesterol addition to ER membranes alters conformation of SCAP, the SREBP escort protein that regulates cholesterol metabolism, Mol. Cell, 10, 237, 10.1016/S1097-2765(02)00591-9 · DOI · Paper page
  23. Goldstein, 2006, Protein sensors for membrane sterols, Cell, 124, 35, 10.1016/j.cell.2005.12.022 · DOI · Paper page
  24. Zeng, 2004, Sterol-responsive element-binding protein (SREBP) 2 down-regulates ATP-binding cassette transporter A1 in vascular endothelial cells: A novel role of SREBP in regulating cholesterol metabolism, J. Biol Chem., 279, 48801, 10.1074/jbc.M407817200 · DOI
  25. Rayner, 2010, MiR-33 contributes to the regulation of cholesterol homeostasis, Science, 328, 1570, 10.1126/science.1189862 · DOI · Paper page
  26. Feramisco, 2005, Intramembrane aspartic acid in SCAP protein governs cholesterol-induced conformational change, Proc. Natl. Acad. Sci. USA, 102, 3242, 10.1073/pnas.0500206102 · DOI
  27. Cook, E.C., Nelson, J.K., Sorrentino, V., Koenis, D., Moeton, M., Scheij, S., Ottenhoff, R., Bleijlevens, B., Loregger, A., and Zelcer, N. (2017). Identification of the ER-resident E3 ubiquitin ligase RNF145 as a novel LXR-regulated gene. PLoS ONE, 12. · DOI
  28. Alphonse, 2016, Revisiting Human Cholesterol Synthesis and Absorption: The Reciprocity Paradigm and its Key Regulators, Lipids, 51, 519, 10.1007/s11745-015-4096-7 · DOI
  29. Vaklavas, 2009, Molecular basis of statin-associated myopathy, Atherosclerosis, 202, 18, 10.1016/j.atherosclerosis.2008.05.021 · DOI
  30. Berger, 2015, Dietary cholesterol and cardiovascular disease: A systematic review and meta-analysis, Am. J. Clin. Nutr., 102, 276, 10.3945/ajcn.114.100305 · DOI · Paper page
  31. Brown, 2009, Cholesterol feedback: From Schoenheimer’s bottle to Scap’s MELADL, J. Lipid Res., 50, S15, 10.1194/jlr.R800054-JLR200 · DOI · Paper page
  32. Sever, 2003, Insig-dependent ubiquitination and degradation of mammalian 3-hydroxy-3-methylglutaryl-CoA reductase stimulated by sterols andgeranylgeraniol, J. Biol. Chem., 278, 52479, 10.1074/jbc.M310053200 · DOI
  33. Jo, 2011, Sterol-induced degradation of HMG-CoA reductase depends on interplay of two Insigs and two ubiquitin ligases, gp78 and Trc8, Proc. Natl. Acad. Sci. USA, 108, 20503, 10.1073/pnas.1112831108 · DOI
  34. Song, 2005, Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase, Mol. Cell, 19, 829, 10.1016/j.molcel.2005.08.009 · DOI · Paper page
  35. Hartman, 2010, Sterol-induced dislocation of 3-hydroxy-3-methylglutaryl coenzyme A reductase from endoplasmic reticulum membranes into the cytosol through a subcellular compartment resembling lipid droplets, J. Biol. Chem., 285, 19288, 10.1074/jbc.M110.134213 · DOI
  36. Elsabrouty, 2013, Sterol-induced dislocation of 3-hydroxy-3-methylglutaryl coenzyme A reductase from membranes of permeabilized cells, Mol. Biol. Cell, 24, 3300, 10.1091/mbc.e13-03-0157 · DOI
  37. 2008, Feedback regulation of cholesterol synthesis: Sterol-accelerated ubiquitination and degradation of HMG CoA reductase, Cell Res., 18, 609, 10.1038/cr.2008.61 · DOI · Paper page
  38. Radhakrishnan, 2007, Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: Oxysterols block transport by binding to Insig, Proc. Natl. Acad. Sci. USA, 104, 6511, 10.1073/pnas.0700899104 · DOI · Paper page
  39. Song, 2005, Insig-mediated degradation of HMG CoA reductase stimulated by lanosterol, an intermediate in the synthesis of cholesterol, Cell Metab., 1, 179, 10.1016/j.cmet.2005.01.001 · DOI
  40. Lange, 2008, Effectors of rapid homeostatic responses of endoplasmic reticulum cholesterol and 3-hydroxy-3-methylglutaryl-CoA reductase, J. Biol. Chem., 283, 1445, 10.1074/jbc.M706967200 · DOI
  41. Sharpe, 2013, Controlling cholesterol synthesis beyond 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR), J. Biol. Chem., 288, 18707, 10.1074/jbc.R113.479808 · DOI · Paper page
  42. Sirtori, 2014, The pharmacology of statins, Pharmacol. Res., 88, 3, 10.1016/j.phrs.2014.03.002 · DOI
  43. 2013, Statins and lipid metabolism: An update, Curr. Opin. Lipidol., 24, 221, 10.1097/MOL.0b013e3283613b8b · DOI
  44. Scandinavian Simvastatin Study Group (1994). Randomised trial of cholesterol lowering in 4444 patients with coronary heart disease: The Scandinavian Simvastatin Survival Study (4S). Lancet, 344, 1383–1389. · DOI
  45. Taylor, 2013, Statins for the primary prevention of cardiovascular disease, Cochrane Database Syst. Rev., 1, CD004816
  46. Howe, 2015, The Regulatory Domain of Squalene Monooxygenase Contains a Re-entrant Loop and Senses Cholesterol via a Conformational Change, J. Biol. Chem., 290, 27533, 10.1074/jbc.M115.675181 · DOI
  47. Gill, 2011, Cholesterol-dependent degradation of squalene monooxygenase, a control point in cholesterol synthesis beyond HMG-CoA reductase, Cell Metab., 13, 260, 10.1016/j.cmet.2011.01.015 · DOI · Paper page
  48. Zelcer, 2014, The E3 ubiquitin ligase MARCH6 degrades squalene monooxygenase and affects 3-hydroxy-3-methyl-glutaryl coenzyme A reductase and the cholesterol synthesis pathway, Mol. Cell. Biol., 34, 1262, 10.1128/MCB.01140-13 · DOI · Paper page
  49. Tremblay, 2011, Atorvastatin increases intestinal expression of NPC1L1 in hyperlipidemic men, J. Lipid Res., 52, 558, 10.1194/jlr.M011080 · DOI
  50. Grundy, 1971, Effects of dietary cholesterol on the regulation of total body cholesterol in man, J. Lipid Res., 12, 233, 10.1016/S0022-2275(20)39534-1 · DOI · Paper page
  51. 1983, Long term steroid metabolism balance studies in subjects on cholesterol-free and cholesterol-rich diets: Comparison between normal and hypercholesterolemic individuals, J. Lipid Res., 24, 167, 10.1016/S0022-2275(20)38010-X · DOI
  52. Duane, 1993, Effects of lovastatin and dietary cholesterol on sterol homeostasis in healthy human subjects, J. Clin. Investig., 92, 911, 10.1172/JCI116666 · DOI
  53. Nestel, 1976, Changes in cholesterol synthesis and excretion when cholesterol intake is increased, Metabolism, 25, 1591, 10.1016/0026-0495(76)90112-8 · DOI
  54. McNamara, 1987, Heterogeneity of cholesterol homeostasis in man. Response to changes in dietary fat quality and cholesterol quantity, J. Clin. Investig., 79, 1729, 10.1172/JCI113013 · DOI
  55. Wang, 2007, Regulation of intestinal cholesterol absorption, Annu. Rev. Physiol., 69, 221, 10.1146/annurev.physiol.69.031905.160725 · DOI
  56. Chiang, 2013, Bile acid metabolism and signaling, Compr. Physiol., 3, 1191, 10.1002/cphy.c120023 · DOI
  57. Goldstein, 1976, The LDL pathway in human fibroblasts: A Receptor-mediated mechanism for the regulation of cholesterol metabolism, Curr. Top. Cell. Regul., 11, 147, 10.1016/B978-0-12-152811-9.50011-0 · DOI · Paper page
  58. Goldstein, 2009, The LDL receptor, Arterioscler. Thromb. Vasc. Biol., 29, 431, 10.1161/ATVBAHA.108.179564 · DOI · Paper page
  59. Poirier, 2009, Dissection of the endogenous cellular pathways of PCSK9-induced low density lipoprotein receptor degradation: Evidence for an intracellular route, J. Biol. Chem., 284, 28856, 10.1074/jbc.M109.037085 · DOI · Paper page
  60. Abifadel, 2003, Mutations in PCSK9 cause autosomal dominant hypercholesterolemia, Nat. Genet., 34, 154, 10.1038/ng1161 · DOI · Paper page
  61. Zelcer, 2009, LXR regulates cholesterol uptake through Idol-dependent ubiquitination of the LDL receptor, Science, 325, 100, 10.1126/science.1168974 · DOI · Paper page
  62. Bhakdi, 1995, On the pathogenesis of atherosclerosis: Enzymatic transformation of human low density lipoprotein to an atherogenic moiety, J. Exp. Med., 182, 1959, 10.1084/jem.182.6.1959 · DOI
  63. Parthasarathy, 2010, Oxidized low-density lipoprotein, Methods Mol. Biol., 610, 403, 10.1007/978-1-60327-029-8_24 · DOI
  64. Arjuman, 2017, LOX-1: A potential target for therapy in atherosclerosis; an in vitro study, Int. J. Biochem. Cell Biol., 91, 65, 10.1016/j.biocel.2017.08.013 · DOI
  65. Sacks, 2018, From High-Density Lipoprotein Cholesterol to Measurements of Function: Prospects for the Development of Tests for High-Density Lipoprotein Functionality in Cardiovascular Disease, Arterioscler. Thromb. Vasc. Biol., 38, 487, 10.1161/ATVBAHA.117.307025 · DOI
  66. Glomset, 1968, The plasma lecithins:cholesterol acyltransferase reaction, J. Lipid Res., 9, 155, 10.1016/S0022-2275(20)43114-1 · DOI
  67. Karathanasis, 2017, The Changing Face of HDL and the Best Way to Measure It, Clin. Chem., 63, 196, 10.1373/clinchem.2016.257725 · DOI
  68. Brufau, 2011, Reverse cholesterol transport revisited: Contribution of biliary versus intestinal cholesterol excretion, Arterioscler. Thromb. Vasc. Biol., 31, 1726, 10.1161/ATVBAHA.108.181206 · DOI
  69. Olkkonen, 2012, Macrophage oxysterols and their binding proteins: Roles in atherosclerosis, Curr. Opin. Lipidol., 23, 462, 10.1097/MOL.0b013e328356dba0 · DOI
  70. Huwait, 2015, Protein Kinase C is Involved in the Induction of ATP-Binding Cassette Transporter A1 Expression by Liver X Receptor/Retinoid X Receptor Agonist in Human Macrophages, J. Cell. Physiol., 116, 2032
  71. Monzel, 2017, Doxorubicin enhances oxysterol levels resulting in a LXR-mediated upregulation of cardiac cholesterol transporters, Biochem. Pharmacol., 144, 108, 10.1016/j.bcp.2017.08.008 · DOI
  72. Oram, 2000, ABCA1-mediated transport of cellular cholesterol and phospholipids to HDL apolipoproteins, Curr. Opin. Lipidol., 11, 253, 10.1097/00041433-200006000-00005 · DOI
  73. Costet, 2000, Sterol-dependent transactivation of the ABC1 promoter by the liver X receptor/retinoid X receptor, J. Biol. Chem., 275, 28240, 10.1074/jbc.M003337200 · DOI
  74. Qian, 2017, Structure of the Human Lipid Exporter ABCA1, Cell, 169, 1228, 10.1016/j.cell.2017.05.020 · DOI
  75. Fitzgerald, 2004, ABCA1 and amphipathic apolipoproteins form high-affinity molecular complexes required for cholesterol efflux, J. Lipid Res., 45, 287, 10.1194/jlr.M300355-JLR200 · DOI
  76. Casteleijn, 2018, Interaction of lecithin:cholesterol acyltransferase with lipid surfaces and apolipoprotein A-I-derived peptides, J. Lipid Res., 59, 670, 10.1194/jlr.M082685 · DOI
  77. Jonas, 2000, Lecithin cholesterol acyltransferase, Biochim. Biophys. Acta, 1529, 245, 10.1016/S1388-1981(00)00153-0 · DOI
  78. Gunawardane, 2016, Agonistic Human Antibodies Binding to Lecithin-Cholesterol Acyltransferase Modulate High Density Lipoprotein Metabolism, J. Biol. Chem., 291, 2799, 10.1074/jbc.M115.672790 · DOI
  79. Peelman, 1999, Effects of natural mutations in lecithin:cholesterol acyltransferase on the enzyme structure and activity, J. Lipid Res., 40, 59, 10.1016/S0022-2275(20)33339-3 · DOI
  80. Piper, 2015, The high-resolution crystal structure of human LCAT, J. Lipid Res., 56, 1711, 10.1194/jlr.M059873 · DOI
  81. Terasaka, 2007, High-density lipoprotein protects macrophages from oxidized low-density lipoprotein-induced apoptosis by promoting efflux of 7-ketocholesterol via ABCG1, Proc. Natl. Acad. Sci. USA, 104, 15093, 10.1073/pnas.0704602104 · DOI
  82. Li, 2010, Adenosine monophosphate activated protein kinase regulates ABCG1-mediated oxysterol efflux from endothelial cells and protects against hypercholesterolemia-induced endothelial dysfunction, Arterioscler. Thromb. Vasc. Biol., 30, 1354, 10.1161/ATVBAHA.110.204230 · DOI
  83. Li, 2017, The lipid moiety 7-ketocholesteryl-9-carboxynonanoate mediates binding interaction of oxLDL to LOX-1 and upregulates ABCA1 expression through PPARγ, Life Sci., 177, 27, 10.1016/j.lfs.2017.03.024 · DOI
  84. Li, 2017, The ω-carboxyl group of 7-ketocholesteryl-9-carboxynonanoate mediates the binding of oxLDL to CD36 receptor and enhances caveolin-1 expression in macrophages, Int. J. Biochem. Cell Biol., 90, 121, 10.1016/j.biocel.2017.07.022 · DOI
  85. Wu, 1979, Relative contributions by liver and intestine to individual plasma apolipoproteins in the rat, J. Biol. Chem., 254, 7316, 10.1016/S0021-9258(18)50321-5 · DOI
  86. Li, 2006, TNF-alpha induces ABCA1 through NF-kappaB in macrophages and in phagocytes ingesting apoptotic cells, Proc. Natl. Acad. Sci. USA, 103, 3112, 10.1073/pnas.0510345103 · DOI
  87. Shavva, V.S., Mogilenko, D.A., Nekrasova, E.V., Trulioff, A.S., Kudriavtsev, I.V., Larionova, E.E., Babina, A.V., Dizhe, E.B., Missyul, B.V., and Orlov, S.V. (2018). Tumor necrosis factor α stimulates endogenous apolipoprotein A-I expression and secretion by human monocytes and macrophages: Role of MAP-kinases, NF-κB, and nuclear receptors PPARα and LXRs. Mol. Cell. Biochem. · DOI
  88. Suzuki, 2017, Impact of TLR 2, TLR 4-activation on the Expression of ABCA1 and ABCG1 in Raw Cells, Ann. Clin. Lab. Sci., 47, 436
  89. Takiguchi, S., Ayaori, M., Yakushiji, E., Nishida, T., Nakaya, K., Sasaki, M., Iizuka, M., Uto-Kondo, H., Terao, Y., and Yogo, M. (2018). Hepatic Overexpression of Endothelial Lipase Lowers HDL (High-Density Lipoprotein) but Maintains Reverse Cholesterol Transport in Mice: Role of SR-BI (Scavenger Receptor Class B Type I)/ABCA1 (ATP-Binding Cassette Transporter A1)-Dependent Pathways. Arterioscler. Thromb. Vasc. Biol. · DOI · Paper page
  90. Shrestha, 2018, Cholesteryl ester transfer protein and its inhibitors, J. Lipid Res., 59, 772, 10.1194/jlr.R082735 · DOI
  91. Masson, 2009, The role of plasma lipid transfer proteins in lipoprotein metabolism and atherogenesis, J. Lipid Res., 50, S201, 10.1194/jlr.R800061-JLR200 · DOI
  92. Beamer, 1997, Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution, Science, 276, 1861, 10.1126/science.276.5320.1861 · DOI
  93. Jiang, 1992, Dietary cholesterol increases transcription of the human cholesteryl ester transfer protein gene in transgenic mice. Dependence on natural flanking sequences, J. Clin. Investig., 90, 1290, 10.1172/JCI115993 · DOI
  94. Martin, 1993, Cholesteryl ester transfer protein and high density lipoprotein responses to cholesterol feeding in men: Relationship to apolipoprotein E genotype, J. Lipid Res., 34, 437, 10.1016/S0022-2275(20)40735-7 · DOI
  95. Qiu, 2007, Crystal structure of cholesteryl ester transfer protein reveals a long tunnel and four bound lipid molecules, Nat. Struct. Mol. Biol., 14, 106, 10.1038/nsmb1197 · DOI
  96. Li, 2015, Bile acids as metabolic regulators, Curr. Opin. Gastroenterol., 31, 159, 10.1097/MOG.0000000000000156 · DOI
  97. Chiang, 2009, Bile acids: Regulation of synthesis, J. Lipid Res., 50, 1955, 10.1194/jlr.R900010-JLR200 · DOI · Paper page
  98. Gupta, 2002, LXR alpha is the dominant regulator of CYP7A1 transcription, Biochem. Biophys. Res. Commun., 293, 338, 10.1016/S0006-291X(02)00229-2 · DOI
  99. Davis, 2002, Regulation of cholesterol-7alpha-hydroxylase: BAREly missing a SHP, J. Lipid Res., 43, 533, 10.1016/S0022-2275(20)31482-6 · DOI
  100. Tarling, 2017, RNA-binding protein ZFP36L1 maintains posttranscriptional regulation of bile acid metabolism, J. Clin. Investig., 127, 3741, 10.1172/JCI94029 · DOI
  101. Goodwin, 2000, A regulatory cascade of the nuclear receptors FXR, SHP-1, and LRH-1 represses bile acid biosynthesis, Mol. Cell, 6, 517, 10.1016/S1097-2765(00)00051-4 · DOI · Paper page
  102. Reeskamp, 2018, Transintestinal cholesterol excretion in humans, Curr. Opin. Lipidol., 29, 10, 10.1097/MOL.0000000000000473 · DOI
  103. Berger, 2013, Transintestinal cholesterol excretion is an active metabolic process modulated by PCSK9 and statin involving ABCB1, Arterioscler. Thromb. Vasc. Biol., 33, 1484, 10.1161/ATVBAHA.112.300263 · DOI
  104. Vrins, 2012, Trans-intestinal cholesterol efflux is not mediated through high density lipoprotein, J. Lipid Res., 53, 2017, 10.1194/jlr.M022194 · DOI
  105. Vrins, 2008, Regulation of direct transintestinal cholesterol excretion in mice, Am. J. Physiol. Gastrointest. Liver Physiol., 295, G203, 10.1152/ajpgi.90231.2008 · DOI
  106. McGillicuddy, 2009, Inflammation impairs reverse cholesterol transport in vivo, Circulation, 119, 1135, 10.1161/CIRCULATIONAHA.108.810721 · DOI
  107. Dillon, 2016, High-Density Lipoprotein Proteomic Composition, and not Efflux Capacity, Reflects Differential Modulation of Reverse Cholesterol Transport by Saturated and Monounsaturated Fat Diets, Circulation, 133, 1838, 10.1161/CIRCULATIONAHA.115.020278 · DOI
  108. Castilho, 2012, ER stress is associated with reduced ABCA-1 protein levels in macrophages treated with advanced glycated albumin—Reversal by a chemical chaperone, Int. J. Biochem. Cell Biol., 44, 1078, 10.1016/j.biocel.2012.03.016 · DOI
  109. Castilho, 2012, Inhibition of macrophage oxidative stress prevents the reduction of ABCA-1 transporter induced by advanced glycated albumin, Lipids, 47, 443, 10.1007/s11745-011-3647-9 · DOI
  110. Zhou, 2016, Metformin Inhibits Advanced Glycation End Products-Induced Inflammatory Response in Murine Macrophages Partly through AMPK Activation and RAGE/NFκB Pathway Suppression, J. Diabetes Res., 2016, 4847812, 10.1155/2016/4847812 · DOI
  111. Iborra, 2018, AGE-albumin enhances ABCA1 degradation by ubiquitin-proteasome and lysosomal pathways in macrophages, J. Diabetes Complicat., 32, 1, 10.1016/j.jdiacomp.2017.09.012 · DOI
  112. Daffu, 2015, RAGE Suppresses ABCG1-Mediated Macrophage Cholesterol Efflux in Diabetes, Diabetes, 64, 4046, 10.2337/db15-0575 · DOI
  113. Aleidi, 2015, The E3 ubiquitin ligases, HUWE1 and NEDD4-1, are involved in the post-translational regulation of the ABCG1 and ABCG4 lipid transporters, J. Biol. Chem., 290, 24604, 10.1074/jbc.M115.675579 · DOI
  114. Aleidi, 2018, The E3 ubiquitin ligase, HECTD1, is involved in ABCA1-mediated cholesterol export from macrophages, Biochim. Biophys. Acta, 1863, 359, 10.1016/j.bbalip.2017.12.011 · DOI
  115. Clayton, 2017, Egg consumption and heart health: A review, Nutrition, 37, 79, 10.1016/j.nut.2016.12.014 · DOI
  116. Virtanen, 2016, Associations of egg and cholesterol intakes with carotid intima-media thickness and risk of incident coronary artery disease according to apolipoprotein E phenotype in men: The Kuopio Ischaemic Heart Disease Risk Factor Study, Am. J. Clin. Nutr., 103, 895, 10.3945/ajcn.115.122317 · DOI
  117. Goldberg, 2014, Egg consumption and carotid atherosclerosis in the Northern Manhattan study, Atherosclerosis, 235, 273, 10.1016/j.atherosclerosis.2014.04.019 · DOI
  118. Rhee, 2017, The association between dietary cholesterol intake and subclinical atherosclerosis in Korean adults: The Kangbuk Samsung Health Study, J. Clin. Lipidol., 11, 432, 10.1016/j.jacl.2017.01.021 · DOI
  119. Choi, 2015, Egg consumption and coronary artery calcification in asymptomatic men and women, Atherosclerosis, 241, 305, 10.1016/j.atherosclerosis.2015.05.036 · DOI
  120. Blesso, C.N., and Fernandez, M.L. (2018). Dietary Cholesterol, Serum Lipids, and Heart Disease: Are Eggs Working for or Against You?. Nutrients, 10. · DOI
  121. Barraj, 2009, A comparison of egg consumption with other modifiable coronary heart disease lifestyle risk factors: A relative risk apportionment study, Risk Anal., 29, 401, 10.1111/j.1539-6924.2008.01149.x · DOI
  122. Herron, 2003, Men classified as hypo- or hyperresponders to dietary cholesterol feeding exhibit differences in lipoprotein metabolism, J. Nutr., 133, 1036, 10.1093/jn/133.4.1036 · DOI
  123. Junyent, 2007, Increased intestinal cholesterol absorption in autosomal dominant hypercholesterolemia and no mutations in the low-density lipoprotein receptor or apolipoprotein B genes, J. Clin. Endocrinol. Metab., 92, 3667, 10.1210/jc.2006-2567 · DOI
  124. Grundy, 2016, Does Dietary Cholesterol Matter?, Curr. Atheroscler. Rep., 18, 68, 10.1007/s11883-016-0615-0 · DOI
  125. Ravera, A., Carubelli, V., Sciatti, E., Bonadei, I., Gorga, E., Cani, D., Vizzardi, E., Metra, M., and Lombardi, C. (2016). Nutrition and Cardiovascular Disease: Finding the Perfect Recipe for Cardiovascular Health. Nutrients, 8. · DOI

Cited by

Sorted by citations

Metadata

Authors
Afonso, M. S., Machado, R. M., Lavrador, M., Quintao, E. C. R., Moore, K., & Lottenberg, A.
Affiliations
  • Marc and Ruti Bell Vascular Biology and Disease Program, Leon H. Charney Division of Cardiology, Department of Medicine, New York University School of Medicine, New York, NY 10016, USA
  • Laboratorio de Lipides (LIM 10), Hospital das Clínicas HCFMUSP, Faculdade de Medicina, Universidade de Sao Paulo, Sao Paulo, SP 05403-000, Brazil
Venue
Nutrients
Publisher
MDPI AG
Published
2018-06-13
Volume
10
Issue
6
Pages
760
ISSN
2072-6643
Cited by
138
References
8
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review