Lipidler ve Lipid Metabolizması
Özet
Lipidler, vücudun enerji kaynağı, hücre yapılarının temel bileşenleri ve hormonların sentezi için gerekli bileşiklerdir. Yağlar, fosfolipitler ve steroller gibi farklı türleri bulunmaktadır. Lipitlerin ana işlevi, hücre zarlarını oluşturmak, enerji depolamak ve hormon üretiminde yer almaktır. Lipid metabolizması vücutta, yağların sindirilmesi, emilmesi ve taşınması süreçlerini içermektedir. Diyetle alınan yağlar, bağırsakta şilomikronlar olarak işlenerek kan yolu ile taşınmaktadır. Karaciğer, lipidleri çok düşük yoğunluklu lipoprotein (VLDL) olarak salgılamaktadır. Yağ asitleri, beta-oksidasyon yolu ile enerji üretimi için kullanılmakta fazla yağ ise depolanmaktadır. Yüksek yoğunluklu lipoproteinler (HDL), kolesterolü dokulardan karaciğere taşırken, düşük yoğunluklu lipoproteinler (LDL) kolesterolü karaciğere taşımaktadır.
Yağ asitlerinin oksidasyonu, vücuttaki enerji üretiminin temel yollarından biridir. Yağ asitleri, mitokondriyal beta-oksidasyon yoluyla parçalanarak ATP üretilmektedir. Bu süreçte yağ asitleri, asetil-CoA'ya dönüştürülmekte ve enerji üretimi için Krebs döngüsüne katılmaktadır.
Lipid metabolizması vücutta enerji üretiminin yanı sıra kardiyovasküler sağlığı da doğrudan etkilemektedir. Yüksek yoğunluklu lipoproteinin kolesterol taşıma işlevi koruyucu bir etki sağlarken, LDL'nin oksidasyonu ve plak oluşumu kalp-damar hastalıkları riskini artırabilmektedir.
Lipids are the body's source of energy, the basic building blocks of cell structures, and compounds necessary for the synthesis of hormones. There are different types, such as fats, phospholipids and sterols. The main function of lipids is to form cell membranes, store energy and participate in hormone production. Lipid metabolism involves the processes of digestion, absorption and transport of fats in the body. Dietary fats are processed in the intestines as chylomicrons and transported through the blood. The liver secretes lipids as very low density lipoproteins (VLDL). Fatty acids are used for energy via beta-oxidation and excess fat is stored. High-density lipoproteins (HDL) carry cholesterol from tissues to the liver, while low-density lipoproteins (LDL) carry cholesterol to the liver.
Fatty acid oxidation is one of the body's main ways of producing energy. Fatty acids are broken down by mitochondrial beta-oxidation to produce ATP. In the process, fatty acids are converted to acetyl-CoA and participate in the Krebs cycle for energy production. Lipid metabolism has a direct impact on cardiovascular health and energy production in the body. While the cholesterol-transporting function of high-density lipoprotein is protective, LDL oxidation and plaque formation can increase the risk of cardiovascular disease.
Referanslar
Smith AD. Oxford Dictionary of Biochemistry and Molecular Biology. Oxford University Press; 1998.
Valenzuela A. Docosahexaenoic acid (DHA), an essential fatty acid for the proper functioning of neuronal cells: Their role in mood disorders. Grasas y Aceites. 2009;60(2): 203–212. https://doi.org/10.3989/gya.2009.02.
Simopoulos AP. Evolutionary aspects of diet: The omega-6/omega-3 ratio and the brain. Molecular Neurobiology. 2011;44(2): 203–215. https://doi.org/10.1007/s12035-011-8230-6.
Weylandt KH, Chiu CY, Gomolka B, et al. Omega-3 fatty acids and their lipid mediators: Towards an understanding of resolvin and protectin formation. Prostaglandins & Other Lipid Mediators. 2012;97(3–4): 73–82. https://doi.org/10.1016/j.prostaglandins.2012.01.001.
Zúñiga J, Cancino M, Medina F, et al. N-3 PUFA supplementation triggers PPAR-α activation and PPAR-α/NF-κB interaction: Anti-inflammatory implications in liver ischemia-reperfusion injury. PLOS ONE. 2011;6(12): e28502. https://doi.org/10.1371/journal.pone.0028502.
Lipid Library. Lipoproteins and Membranes (4th ed.). (n.d.). http://lipidlibrary.aocs.org.
Cyberlipid Center. Cyberlipid Center website. Retrieved from: http://www.cyberlipid.org
Watanabe K, Yasugi E, Oshima M. How to search the glycolipid data in “LIPIDBANK for Web,” the newly developed lipid database in Japan. Trends in Glycoscience and Glycotechnology. 2000;12(1):175–84.
Fahy E, Cotter D, Sud M, Subramaniam S. Lipid classification, structures and tools. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 2011;1811(11):637–647. doi:10.1016/j.bbalip.2011.06.009.
Lipid MAPS. https://www.lipidmaps.org/
Vance DE, Vance JE. Biochemistry of Lipids. Elsevier Science; 2002.
Fahy E, Subramaniam S, Brown HA, Glass CK, Merrill AH, Murphy RC, et al. A comprehensive classification system for lipids. Journal of Lipid Research. 2005;46(5):839–861. doi:10.1194/jlr.E400004-JLR200.
Coleman RA, Lee DP. Enzymes of triacylglycerol synthesis and their regulation. Progress in Lipid Research. 2004;43(2):134–176. doi:10.1016/j.plipres.2004.01.001
Pahlsson P, Spitalnik SL, Spitalnik PF, et al. Characterization of galactosyl glycerolipids in the HT29 human colon carcinoma cell line. Archives of Biochemistry and Biophysics. 1998;396(2): 187–198. https://doi.org/10.1006/abbi.2001.2627.
Pereto J, Lopez-Garcia P, Moreira D. Ancestral lipid biosynthesis and early membrane evolution. Trends in Biochemical Sciences. 2004;29(9): 469–477. https://doi.org/10.1016/j.tibs.2004.07.005.
Merrill AH, Jr., Sandhoff K. Sphingolipids: Metabolism and cell signaling. In: Vance DE, Vance JE, editors. New Comprehensive Biochemistry: Biochemistry of Lipids, Lipoproteins, and Membranes. 2002;373–407.
IUPAC-IUB Commission on Biochemical Nomenclature (CBN). The nomenclature of lipids (recommendations 1976). European Journal of Biochemistry. 1977;79(1):11–21. Retrieved from IUPAC website.
Bach, D., & Wachtel, E. Phospholipid/cholesterol model membranes: Formation of cholesterol crystallites. Biochimica et Biophysica Acta (BBA) - Biomembranes. 2003;1610(2):187–197. https://doi.org/10.1016/S0005-2736(03)00113-2.
Tsai MJ, O'Malley BW. Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annual Review of Biochemistry. 1994;63: 451–486. https://doi.org/10.1146/annurev.biochem.63.1.451.
Jones G, Strugnell SA, DeLuca HF. Current understanding of the molecular actions of vitamin D. Physiological Reviews. American Physiological Society; 1998;78(4):1193–231.
Russell DW. The enzymes, regulation, and genetics of bile acid synthesis. Annual Review of Biochemistry. 2003;72: 137–174. https://doi.org/10.1146/annurev.biochem.72.121801.161838.
Kuzuyama T, Seto H. Diversity of the biosynthesis of the isoprene units. Natural Product Reports. 2003;20(2): 171–183. https://doi.org/10.1039/B202038F.
Rodriguez-Concepcion M. The MEP pathway: A new target for the development of herbicides, antibiotics and antimalarial drugs. Current Pharmaceutical Research. 2004;10(12): 2391–2400. https://doi.org/10.2174/1381344043375101.
Demming-Adams B, Adams WW. Antioxidants in photosynthesis and human nutrition. Science. 2002;298(5601):2149–2153. doi:10.1126/science.1078682
Ricciarelli R, Zingg JM, Azzi A. Vitamin E: Protective role of a Janus molecule. FASEB Journal. 2001;15(15): 2314–2325. https://doi.org/10.1096/fj.00-0549fje.
Meganathan R. Biosynthesis of menaquinone (vitamin K2) and ubiquinone (coenzyme Q): A perspective on enzymatic mechanisms. Vitamins and Hormones. 2001;61: 173–218. https://doi.org/10.1016/S0083-6729(01)61008-5.
Raetz CRH, Whitfield C. Lipopolysaccharide endotoxins. Annual Review of Biochemistry. 2002;71: 635–700. https://doi.org/10.1146/annurev.biochem.71.110601.135414.
Zähringer U, Lindner B, Rietschel ET. Chemical structure of Lipid A: Recent advances in structural analysis of biologically active molecules. In: Brade H, Opal SM, Vogel SN, Morrison DC, editors. Endotoxin in Health and Disease. Marcel Dekker; 1999. p. 93–114.
Brennan, P. J., & Nikaido, H. The envelope of mycobacteria. Annual Review of Biochemistry. 1995;64:29–63. https://doi.org/10.1146/annurev.bi.64.070195.000333
Walsh CT. Polyketide and nonribosomal peptide antibiotics: Modularity and versatility. Science. 2004;303(5665): 1805–1810. https://doi.org/10.1126/science.1093724.
Reeves CD. The enzymology of combinatorial biosynthesis. Critical Reviews in Biotechnology. 2003;23(2): 95–147. https://doi.org/10.1080/07388550390220471.
Binder, H. J., & Reuben, A. Nutrient digestion and absorption. In Medical Physiology: A Cellular and Molecular Approach. Philadelphia, PA: Saunders; 2009:949–979.
Lowe ME. The triglyceride lipases of the pancreas. Journal of Lipid Research. 2002;43(12): 2007–2016. https://doi.org/10.1194/jlr.R200014-JLR200.
Iqbal J, Hussain MM. Intestinal lipid absorption. American Journal of Physiology-Endocrinology and Metabolism. American Physiological Society; 2009;296(6)–94. doi:10.1152/ajpendo.90669.2008
Goodman BE. Insights into digestion and absorption of major nutrients in humans. Advances in Physiology Education. 2010.
Mansbach CM, Gorelick F. Development and physiological regulation of intestinal lipid absorption. II. Dietary lipid absorption, complex lipid synthesis, and the intracellular packaging and secretion of chylomicrons. American Journal of Physiology. Gastrointestinal and Liver Physiology. 2007;293(3): G645–G650.
Ophardt CE. Overview of lipid function. In: Virtual ChemBook. Elmhurst College. 2003.
Huang J, Borensztajn J, Reddy JK. Hepatic lipid metabolism. In: Monga S, editor. Molecular Pathology of Liver Diseases. Springer; 2011. pp. 133–46.
Arumugam, R., & Natesan, V. Urea cycle pathway targeted therapeutic action of naringin against ammonium chloride-induced hyperammonemic rats. Biomedicine & Pharmacotherapy. 2017;94:1028–1037. https://doi.org/10.1016/j.biopha.2017.07.128.
Nguyen PHUONGT, Leray V, Diez M, Serisier S, Bloc’h JL, Siliart B, Dumon H. Liver lipid metabolism. Journal of Animal Physiology and Animal Nutrition. 2008;92(3): 272-283.
Rosca MG, Vazquez EJ, Chen Q, et al. Oxidation of fatty acids is the source of increased mitochondrial reactive oxygen species production in kidney cortical tubules in early diabetes. Diabetes. 2012;61(8): 2074–2083. https://doi.org/10.2337/db11-1786.
Houten SM, Violante S, Ventura FV, Wanders RJ. The biochemistry and physiology of mitochondrial fatty acid β-oxidation and its genetic disorders. Annual Review of Physiology. Annual Reviews; 2016;78(1):23–44.
Kunau WH, Dommes V, Schulz H. Beta-oxidation of fatty acids in mitochondria, peroxisomes, and bacteria: A century of continued progress. Progress in Lipid Research. 1995;34(3): 267–342. https://doi.org/10.1016/0163-7827(95)00009-9.
Price N, van der Leij FR, Jackson V, et al. A novel brain-expressed protein related to carnitine palmitoyltransferase I. Genomics. 2002;80(4): 433–442. https://doi.org/10.1006/geno.2002.6985.
Ramsay RR, Gandour RD, van der Leij FR. Molecular enzymology of carnitine transfer and transport. Biochimica et Biophysica Acta. 2001;1546(1): 21–43. https://doi.org/10.1016/S0005-2760(01)00234-9.
Bonnefont, J. P., Djouadi, F., Prip-Buus, C., Gobin, S., Munnich, A., & Bastin, J. Carnitine palmitoyltransferases 1 and 2: Biochemical, molecular, and medical aspects. Molecular Aspects of Medicine. 2004;25(6):495–520. https://doi.org/10.1016/j.mam.2004.06.004.
Adams, S. H., Hoppel, C. L., Lok, K. H., et al. Plasma acylcarnitine profiles suggest incomplete long-chain fatty acid β-oxidation and altered tricarboxylic acid cycle activity in type 2 diabetic African-American women. The Journal of Nutrition. 2009;139(6):1073–1081. https://doi.org/10.3945/jn.108.101253.
Mynatt RL. Carnitine and type 2 diabetes. Diabetes/Metabolism Research and Reviews. 2009;25(1): S45–S49. https://doi.org/10.1002/dmrr.1017.
Noland RC, Koves TR, Seiler SE, et al. Carnitine insufficiency caused by aging and overnutrition compromises mitochondrial performance and metabolic control. Journal of Biological Chemistry. 2009;284(34): 22840–22852. https://doi.org/10.1074/jbc.M109.022655.
Houten SM, Wanders RJ. A general introduction to the biochemistry of mitochondrial fatty acid β-oxidation. Journal of Inherited Metabolic Disease. Springer; 2010;33:469–77.
Le W, Abbas SA, Sprecher H, Vockley J, Schulz H. Long-chain acyl-CoA dehydrogenase is a key enzyme in the mitochondrial beta-oxidation of unsaturated fatty acids. Biochimica et Biophysica Acta. 2000;1485(2): 121–128. https://doi.org/10.1016/S0005-2760(00)00161-9.
Chegary M, te Brinke H, Ruiter JP, et al. Mitochondrial long-chain fatty acid β-oxidation in man and mouse. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 2009;1791(10):806–815. doi:10.1016/j.bbamcr.2009.05.010
Kunau WH, Bartnik F. Studies on the partial degradation of polyunsaturated fatty acids in rat-liver mitochondria. European Journal of Biochemistry. 1974;48(1): 311-318.
Kunau WH, Dommes P. Degradation of unsaturated fatty acids. Identification of intermediates in the degradation of cis-4-decenoly-CoA by extracts of beef-liver mitochondria. European Journal of Biochemistry. 1978;91(2): 533-544.
Hiltunen JK, Kärki T, Hassinen IE, Osmundsen H. Beta-oxidation of polyunsaturated fatty acids by rat liver peroxisomes. A role for 2,4-dienoyl-coenzyme A reductase in peroxisomal beta-oxidation. Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology; 1986;261(35):16484–93.
Aoyama, T., Peters, J. M., Iritani, N., Nakajima, T., Furihata, K., et al. Altered constitutive expression of fatty acid-metabolizing enzymes in mice lacking the peroxisome proliferator-activated receptor α (PPARα). The Journal of Biological Chemistry. 1998;273(10):5678–5684. https://doi.org/10.1074/jbc.273.10.5678.
Houten SM, Denis S, Argmann CA, Jia Y, Ferdinandusse S, et al. Peroxisomal L-bifunctional enzyme (Ehhadh) is essential for the production of medium-chain dicarboxylic acids. Journal of Lipid Research. American Society for Biochemistry and Molecular Biology; 2012;53(6):1296–303. doi:10.1194/jlr.M024037.
Neels JG, Grimaldi PA. Physiological functions of peroxisome proliferator–activated receptor beta. Physiological Reviews. 2014;94(4): 795–858. https://doi.org/10.1152/physrev.00010.2013.
Huss JM, Kopp RP, Kelly DP. Peroxisome proliferator–activated receptor coactivator-1α (PGC-1α) coactivates the cardiac-enriched nuclear receptors estrogen-related receptor-α and -γ. Identification of novel leucine-rich interaction motif within PGC-1α. Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology; 2002;277(45):40265–74. doi:10.1074/jbc.M206408200.
Drynan L, Quant PA, Zammit VA. Flux control exerted by mitochondrial outer membrane carnitine palmitoyltransferase over beta-oxidation, ketogenesis and tricarboxylic acid cycle activity in hepatocytes isolated from rats in different metabolic states. Biochemical Journal. 1996;317(3):791–795. doi:10.1042/bj3170791.
Smith BK, Perry CG, Koves TR, et al. Identification of a novel malonyl-CoA IC50 for CPT-I: Implications for predicting in vivo fatty acid oxidation rates. Biochemical Journal. 2012;448(1): 13–20. https://doi.org/10.1042/BJ20120261.
Canto C, Gerhart-Hines Z, Feige JN, Lagouge M, Noriega L, et al. AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity. Nature. 2009;458(7241):1056–1060. doi:10.1038/nature07813.
Pougovkina O, te Brinke H, Ofman R, et al. Mitochondrial protein acetylation is driven by acetyl-CoA from fatty acid oxidation. Human Molecular Genetics. 2014;23(13): 3513–3522. https://doi.org/10.1093/hmg/ddu057.
Tenopoulou M, Chen J, Bastin J, et al. Strategies for correcting very long chain acyl-CoA dehydrogenase deficiency. Journal of Biological Chemistry. 2015;290(17): 10486–10494. https://doi.org/10.1074/jbc.M115.644469.
Verhoeven NM, Wanders RJA, Poll-The BT, et al. The metabolism of phytanic acid and pristanic acid in man: A review. Journal of Inherited Metabolic Disease. 1998;21(6): 697–728. https://doi.org/10.1023/A:1005393912122.
Casteels M, Foulon V, Mannaerts GP, Van Veldhoven PP. α-Oxidation of 3-methyl-substituted fatty acids and its thiamine dependence. European Journal of Biochemistry. 2003;270(7):1619–1627. doi:10.1046/j.1432-1033.2003.03533.x.
Jansen GA, Mihalik SJ, Watkins PA, Moser HW, Jakobs C, et al. Phytanoyl-CoA hydroxylase is present in human liver, located in peroxisomes, and deficient in Zellweger syndrome. Biochemical and Biophysical Research Communications. Academic Press; 1996;229(1):205–10. doi:10.1006/bbrc.1996.1355.
Jansen GA, Ferdinandusse S, Ijlst L, Muijsers AO, Skjeldal OH, et al. Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene. Nature Genetics. Springer; 1997;17(2):190–3. doi:10.1038/ng1197-190.
Croes K, Van Veldhoven PP, Mannaerts GP, Casteels M. Production of formyl-CoA during peroxisomal α-oxidation of 3-methyl-branched fatty acids. FEBS Letters. 1997;407(2):197–200. doi:10.1016/S0014-5793(97)00426-7.
Casteels M, Sniekers M, Fraccascia P, Mannaerts GP, Van Veldhoven PP. The role of 2-hydroxyacyl-CoA lyase, a thiamin pyrophosphate-dependent enzyme, in the peroxisomal metabolism of 3-methyl-branched fatty acids and 2-hydroxy straight-chain fatty acids. Biochemical Society Transactions. 2007;35(4):876–880. doi:10.1042/BST0350876.
Cintolesi A, Rodríguez-Moyá M, Gonzalez R. Fatty acid oxidation: Systems analysis and applications. Wiley Interdisciplinary Reviews: Systems Biology and Medicine. 2013;5(5):575–585. doi:10.1002/wsbm.1229.
Feingold KR. Introduction to lipids and lipoproteins. In: Stokes AP, Stevens JST, Johnson ET, editors. Endotext. MDText.com, Inc.; 2024.
Julve J, Martin-Campos JM, Escola-Gil JC, Blanco-Vaca F. Chylomicrons: Advances in biology, pathology, laboratory testing, and therapeutics. Clinical Chemistry and Laboratory Medicine. Elsevier; 2016;455:134–48. doi:10.1016/j.cca.2016.02.020.
Chait A, Ginsberg HN, Vaisar T, Heinecke JW, Goldberg IJ, Bornfeldt KE. Remnants of the triglyceride-rich lipoproteins, diabetes, and cardiovascular disease. Diabetes. 2020;69(3):508–516. doi:10.2337/dbi19-0011.
Krauss RM, King SM. Remnant lipoprotein particles and cardiovascular disease risk. Best Practice & Research Clinical Endocrinology & Metabolism. 2023;37: 101682. https://doi.org/10.1016/j.beem.2023.101682.
Berneis, K. K., & Krauss, R. M. Metabolic origins and clinical significance of LDL heterogeneity. The Journal of Lipid Research. 2002;43(9):1363–1379. https://doi.org/10.1194/jlr.R200009-JLR200.
Vaisar T, Pennathur S, Green PS, et al. Shotgun proteomics implicates protease inhibition and complement activation in the antiinflammatory properties of HDL. Journal of Clinical Investigation. 2007;117(3): 746–756. https://doi.org/10.1172/JCI30862.
Kostner KM, Kostner GM. Lipoprotein (a): A historical appraisal. Journal of Lipid Research. 2017;58(1): 1-14. https://doi.org/10.1194/jlr.R078756.
Nordestgaard BG, Langsted A. Lipoprotein (a) as a cause of cardiovascular disease: Insights from epidemiology, genetics, and biology. Journal of Lipid Research. 2016;57(11): 1953–1975. https://doi.org/10.1194/jlr.R067240.
Mahley RW, Innerarity TL, Rall SC, Jr., Weisgraber KH. Plasma lipoproteins: Apolipoprotein structure and function. Journal of Lipid Research. 1984;25(11): 1277-1294. https://doi.org/10.1016/S0022-2275(20)34342-6.
Breslow, J. L. (1985). Human apolipoprotein molecular biology and genetic variation. Annual Review of Biochemistry, 54, 699–727.
Olivecrona G. Role of lipoprotein lipase in lipid metabolism. Current Opinion in Lipidology. 2016;27(3): 233–241. https://doi.org/10.1097/MOL.0000000000000315.
Kobayashi J, Miyashita K, Nakajima K, Mabuchi H. Hepatic lipase: A comprehensive view of its role on plasma lipid and lipoprotein metabolism. Journal of Atherosclerosis and Thrombosis. Japan Atherosclerosis Society; 2015;22(9):1001–11. doi:10.5551/jat.28192.
Yasuda T, Ishida T, Rader DJ. Update on the role of endothelial lipase in high-density lipoprotein metabolism, reverse cholesterol transport, and atherosclerosis. Circulation Journal. 2010;74(11): 2263–2270. https://doi.org/10.1253/circj.CJ-10-0284.
Ossoli A, Simonelli S, Vitali C, Franceschini G, Calabresi L. Role of LCAT in atherosclerosis. Journal of Atherosclerosis and Thrombosis. 2016;23(2): 119–127. https://doi.org/10.5551/jat.30573.
Mabuchi H, Nohara A, Inazu A. Cholesteryl ester transfer protein (CETP) deficiency and CETP inhibitors. Molecular Cells. 2014;37(10): 777-784. https://doi.org/10.14348/molcells.2014.0132.
Shrestha S, Wu BJ, Guiney L, Barter PJ, Rye KA. Cholesteryl ester transfer protein and its inhibitors. Journal of Lipid Research. 2018;59(5): 772–783. https://doi.org/10.1194/jlr.R080736.
Hooper AJ, Burnett JR, Watts GF. Contemporary aspects of the biology and therapeutic regulation of the microsomal triglyceride transfer protein. Circulation Research. Lippincott Williams & Wilkins; 2015;116(2):193–205. doi:10.1161/CIRCRESAHA.116.305869.
Abumrad, N. A., & Davidson, N. O. Role of the gut in lipid homeostasis. Physiological Reviews. 2012;92(3):1061–1085. https://doi.org/10.1152/physrev.00019.2011.
D'Aquila T, Hung YH, Carreiro A, Buhman KK. Recent discoveries on absorption of dietary fat: Presence, synthesis, and metabolism of cytoplasmic lipid droplets within enterocytes. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 2016;1861(6):730–747. doi:10.1016/j.bbalip.2016.02.015.
Hussain MM. Intestinal lipid absorption and lipoprotein formation. Current Opinion in Lipidology. Lippincott Williams & Wilkins; 2014;25(3):200–6. doi:10.1097/MOL.0000000000000070.
Kindel T, Lee DM, Tso P. The mechanism of the formation and secretion of chylomicrons. Atherosclerosis Supplements. Elsevier; 2010;11(1):11–6. doi:10.1016/j.atherosclerosissup.2010.06.001.
Ramasamy, I. "Recent advances in physiological lipoprotein metabolism." Clinical Chemistry and Laboratory Medicine (CCLM) 52.12 (2014): 1695-1727.
Shapiro MD, Feingold KR. Monogenic disorders causing hypobetalipoproteinemia. 2015.
Fong LG, Young SG, Beigneux AP, Bensadoun A, Oberer M, Jiang H, et al. GPIHBP1 and plasma triglyceride metabolism. Trends in Endocrinology & Metabolism. Elsevier; 2016;27(7):455–69. doi:10.1016/j.tem.2016.04.003
Taskinen MR, Boren J. Why is apolipoprotein CIII emerging as a novel therapeutic target to reduce the burden of cardiovascular disease? Current Atherosclerosis Reports. 2016;18(10): 59. https://doi.org/10.1007/s11883-016-0617-9.
Feingold KR. Cholesterol lowering drugs. In: Stokes AP, Stevens JST, Johnson ET, editors. Endotext. MDText.com, Inc.; 2016.
Wolska A, Dunbar RL, Freeman LA, et al. Apolipoprotein C-II: New findings related to genetics, biochemistry, and role in triglyceride metabolism. Atherosclerosis. 2017;267: 49–60. https://doi.org/10.1016/j.atherosclerosis.2017.01.020.
Patni NA, Wilson DP, Feingold KR, Blackman MR, Boyce A, Chrousos G, et al. Genetics and dyslipidemia. 2023.
Choi SH, Ginsberg HN. Increased very low density lipoprotein (VLDL) secretion, hepatic steatosis, and insulin resistance. Trends in Endocrinology & Metabolism. 2011;22(10):353–363. doi:10.1016/j.tem.2011.05.007.
Feingold KR, Anawalt B, Blackman MR, Boyce A, Chrousos G, Corpas E, et al. 2000.
Feingold KR. Obesity and dyslipidemia. In: Stokes AP, Stevens JST, Johnson ET, editors. Endotext. MDText.com, Inc.; 2015.
Dallinga-Thie GM, Franssen R, Mooij HL, Visser ME, Hassing HC, Peelman F, Kastelein JJ, Peterfy M, Nieuwdorp M. The metabolism of triglyceride-rich lipoproteins revisited: New players, new insight. Atherosclerosis. 2010;211(1):1–8. doi:10.1016/j.atherosclerosis.2010.01.035
Goldstein JL, Brown MS. A century of cholesterol and coronaries: From plaques to genes to statins. Cell. Elsevier; 2015;161(1):161–72. doi:10.1016/j.cell.2015.03.031
Zhang L, Reue K, Fong LG, et al. Feedback regulation of cholesterol uptake by the LXR-IDOL-LDLR axis. Arteriosclerosis, Thrombosis, and Vascular Biology. 2012;32(10): 2541–2546. https://doi.org/10.1161/ATVBAHA.112.252075.
Baldan, A., Tarr, P., Lee, R., & Edwards, P. A. ATP-binding cassette transporter G1 and lipid homeostasis. Current Opinion in Lipidology. 2006;17(3):227–232. https://doi.org/10.1097/01.mol.0000217955.75228.3b
Shapiro MD, Feingold KR. Monogenic disorders altering HDL levels. 2021.
Wang S, Smith JD. ABCA1 and nascent HDL biogenesis. BioFactors. 2014;40(5): 547–554. https://doi.org/10.1002/biof.1187.
Trigatti BL. SR-B1 and PDZK1: Partners in HDL regulation. Current Opinion in Lipidology. 2017;28(3): 201–208. https://doi.org/10.1097/MOL.0000000000000395.
Rye KA, Barter PJ. Cardioprotective functions of HDLs. Journal of Lipid Research. 2014;55(2): 168–179. https://doi.org/10.1194/jlr.R035767.
Tall AR. Cholesterol efflux pathways and other potential mechanisms involved in the athero-protective effect of high density lipoproteins. Journal of Internal Medicine. 2008;263(3): 256–273. https://doi.org/10.1111/j.1365-2796.2007.01959.x.
Zhao Y, Van Berkel TJ, Van Eck M. Relative roles of various efflux pathways in net cholesterol efflux from macrophage foam cells in atherosclerotic lesions. Current Opinion in Lipidology. 2010;21(5): 441–453. https://doi.org/10.1097/MOL.0b013e32833a6ac5.
Siddiqi HK, Kiss D, Rader D. HDL-cholesterol and cardiovascular disease: Rethinking our approach. Current Opinion in Cardiology. 2015;30(5): 536–542. https://doi.org/10.1097/HCO.0000000000000205.
Ouimet M, Barrett TJ, Fisher EA. HDL and reverse cholesterol transport. Circulation Research. 2019;124(10): 1505–1518. https://doi.org/10.1161/CIRCRESAHA.118.311334.
Schmidt K, Noureen A, Kronenberg F, Utermann G. Structure, function, and genetics of lipoprotein (a). Journal of Lipid Research. 2016;57(8): 1339–1359. https://doi.org/10.1194/jlr.R064717.
Khovidhunkit W. Lipoprotein (a). In: Encyclopedia of Lipidomics. Springer; 2023. pp. 133–6. doi:10.1007/978-3-030-30153-3_23.
Hoover-Plow J, Huang M. Lipoprotein(a) metabolism: Potential sites for therapeutic targets. Metabolism. Elsevier; 2013;62(4):479–91. doi:10.1016/j.metabol.2012.11.007.