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Angiopoietin-like protein 8 differentially regulates ANGPTL3 and ANGPTL4 during postprandial partitioning of fatty acids

Chen, Yan Q., Pottanat, Thomas G., Siegel, Robert W., Ehsani, Mariam, Qian, Yue-Wei, Zhen, Eugene Y., Regmi, Ajit, Roell, William C., Guo, Haihong, Luo, M. Jane, Gimeno, Ruth E., van't Hooft, Ferdinand, Konrad, Robert J.·2020·Journal of Lipid Research
DOI 10.1194/jlr.ra120000781PMC PMC7397750
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  • Multiple laboratories have confirmed the ability of ANGPTL4 to inhibit LPL.

    “In the years since, multiple laboratories have confirmed the ability of ANGPTL4 to inhibit LPL (49–55).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [54]

  • More recent studies have shown that ANGPTL3 forms a complex with ANGPTL8 and that this complex is most likely the physiologically relevant LPL inhibitor.

    “As discussed below, more recent studies have shown that ANGPTL3 forms of complex with ANGPTL8 and that this complex is most likely the physiologically relevant LPL inhibitor (19, 54, 115, 137, 138).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [54]

  • In vitro, ANGPTL3-ANGPTL8 complexes inhibit LPL orders of magnitude better than either ANGPTL3 or ANGPTL8 alone.

    “in vitro several studies have found that the ability of ANGPTL3-ANGPTL8 complexes to inhibit LPL is orders of magnitude better than that of either ANGPTL3 or ANGPTL8 alone (54, 115, 137, 138)”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [54]

  • ANGPTL4-ANGPTL8 complexes are secreted.

    “Chen et al. (54), however, did observe secretion of ANGPTL4-ANGPTL8 complexes”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [54]

  • Binding of ANGPTL4-ANGPTL8 complexes appears to prevent ANGPTL3-ANGPTL8 complexes and uncomplexed ANGPTL4 from inhibiting LPL.

    “Moreover, the binding of ANGPTL4-ANGPTL8 complexes appeared to prevent ANGPTL3-ANGPTL8 complexes and uncomplexed ANGPTL4 from inhibiting LPL (54).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [54]

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Research works printed but not linked: 92

  1. Speakman, 2013, Evolutionary perspectives on the obesity epidemic: adaptive, maladaptive, and neutral viewpoints, Annu. Rev. Nutr., 33, 289, 10.1146/annurev-nutr-071811-150711 · DOI · Paper page
  2. Neel, 1962, Diabetes mellitus: A “thrifty” genotype rendered detrimental by “progress”?, Am. J. Hum. Genet., 14, 353
  3. Ungar, 2006, Diet in early homo: a review of the evidence and a new model of adaptive versatility, Annu. Rev. Anthropol., 35, 209, 10.1146/annurev.anthro.35.081705.123153 · DOI
  4. Hardy, 2015, The importance of dietary carbohydrate in human evolution, Q. Rev. Biol., 90, 251, 10.1086/682587 · DOI
  5. Harris, 2019, Evolution of hominin polyunsaturated fatty acid metabolism: from africa to the new world, Genome Biol. Evol., 11, 1417, 10.1093/gbe/evz071 · DOI
  6. Messer, 1984, Anthropological perspectives on diet, Annu. Rev. Anthropol., 13, 205, 10.1146/annurev.an.13.100184.001225 · DOI
  7. Wells, 2012, The evolution of human adiposity and obesity: where did it all go wrong?, Dis. Model. Mech., 5, 595, 10.1242/dmm.009613 · DOI
  8. Wells, 2006, The evolution of human fatness and susceptibility to obesity: an ethological approach, Biol. Rev. Camb. Philos. Soc., 81, 183, 10.1017/S1464793105006974 · DOI
  9. Saklayen, 2018, The global epidemic of the metabolic syndrome, Curr. Hypertens. Rep., 20, 12, 10.1007/s11906-018-0812-z · DOI · Paper page
  10. Mendrick, 2018, Metabolic syndrome and associated diseases: from the bench to the clinic, Toxicol. Sci., 162, 36, 10.1093/toxsci/kfx233 · DOI
  11. Esposito, 2012, Metabolic syndrome and risk of cancer: a systematic review and meta-analysis, Diabetes Care., 35, 2402, 10.2337/dc12-0336 · DOI
  12. Bhandari, 2014, Metabolic syndrome is associated with increased breast cancer risk: a systematic review with meta-analysis, Int. J. Breast Cancer., 2014, 189384, 10.1155/2014/189384 · DOI
  13. O'Neill, 2015, Metabolic syndrome: a closer look at the growing epidemic and its associated pathologies, Obes. Rev., 16, 1, 10.1111/obr.12229 · DOI
  14. Allott, 2015, Obesity and cancer: mechanistic insights from transdisciplinary studies, Endocr. Relat. Cancer., 22, R365, 10.1530/ERC-15-0400 · DOI
  15. González-Muniesa, 2017, Obesity, Nat. Rev. Dis. Primers., 3, 17034, 10.1038/nrdp.2017.34 · DOI
  16. Câmara, 2017, Kidney disease and obesity: epidemiology, mechanisms and treatment, Nat. Rev. Nephrol., 13, 181, 10.1038/nrneph.2016.191 · DOI
  17. Colditz, 2018, Obesity and cancer: evidence, impact, and future directions, Clin. Chem., 64, 154, 10.1373/clinchem.2017.277376 · DOI
  18. Seidell, 2016, Obesity: the obesity epidemic in the USA - no end in sight?, Nat. Rev. Endocrinol., 12, 499, 10.1038/nrendo.2016.121 · DOI
  19. Nolan, 2017, Prevalence of metabolic syndrome and metabolic syndrome components in young adults: a pooled analysis, Prev. Med. Rep., 7, 211, 10.1016/j.pmedr.2017.07.004 · DOI
  20. Gurka, 2018, Geographical variation in the prevalence of obesity, metabolic syndrome, and diabetes among US adults, Nutr. Diabetes., 8, 14, 10.1038/s41387-018-0024-2 · DOI
  21. Jensen, 2014, 2013 AHA/ACC/TOS guideline for the management of overweight and obesity in adults: a report of the American College of Cardiology/American Heart Association Task Force on Practice Guidelines and The Obesity Society, J. Am. Coll. Cardiol., 63, 2985, 10.1016/j.jacc.2013.11.004 · DOI · Paper page
  22. von Bibra, 2017, Impact of the triglyceride/high-density lipoprotein cholesterol ratio and the hypertriglyceremic-waist phenotype to predict the metabolic syndrome and insulin resistance, Horm. Metab. Res., 49, 542, 10.1055/s-0043-107782 · DOI
  23. Marotta, 2010, Triglyceride-to-HDL cholesterol ratio and metabolic syndrome as contributors to cardiovascular risk in overweight patients, Obesity (Silver Spring)., 18, 1608, 10.1038/oby.2009.446 · DOI
  24. Bitzur, 2009, Triglycerides and HDLcholesterol: stars or second leads in diabetes?, Diabetes Care., 32, S373, 10.2337/dc09-S343 · DOI · Paper page
  25. Frayn, 2001, Adipose tissue and the insulin resistance syndrome, Proc. Nutr. Soc., 60, 375, 10.1079/PNS200195 · DOI
  26. Smith, 2016, Adipose tissue regulates insulin sensitivity: role of adipogenesis, de novo lipogenesis and novel lipids, J. Intern. Med., 280, 465, 10.1111/joim.12540 · DOI
  27. Zhou, 2012, Adipocyte dysfunction and hypertension, Am. J. Cardiovasc. Dis., 2, 143
  28. Yiannikouris, 2012, Adipocyte deficiency of angiotensinogen prevents obesity-induced hypertension in male mice, Hypertension., 60, 1524, 10.1161/HYPERTENSIONAHA.112.192690 · DOI
  29. Patel, 2007, Adiponectin and hypertension: a putative link between adipocyte function and atherosclerotic risk?, J. Hum. Hypertens., 21, 1, 10.1038/sj.jhh.1002078 · DOI
  30. Oriowo, 2015, Perivascular adipose tissue, vascular reactivity and hypertension, Med. Princ. Pract., 24, 29, 10.1159/000356380 · DOI
  31. Ferrannini, 1992, The haemodynamics of obesity: a theoretical analysis, J. Hypertens., 10, 1417, 10.1097/00004872-199211000-00015 · DOI
  32. Stapleton, 2008, Obesity and vascular dysfunction, Pathophysiology., 15, 79, 10.1016/j.pathophys.2008.04.007 · DOI
  33. Ren, 2012, Identification of rifl, a novel adipocyte-enriched insulin target gene with a role in lipid metabolism, Am. J. Physiol. Endocrinol. Metab., 303, E334, 10.1152/ajpendo.00084.2012 · DOI · Paper page
  34. Chi, 2017, ANGPTL8 promotes the ability of ANGPTL3 to bind and inhibit lipoprotein lipase, Mol. Metab., 6, 1137, 10.1016/j.molmet.2017.06.014 · DOI · Paper page
  35. Haller, 2017, ANGPTL8 requires ANGPTL3 to inhibit lipoprotein lipase and plasma triglyceride clearance, J. Lipid Res., 58, 1166, 10.1194/jlr.M075689 · DOI · Paper page
  36. Wang, 2013, Mice lacking ANGPTL8 (betatrophin) manifest disrupted triglyceride metabolism without impaired glucose homeostasis, Proc. Natl. Acad. Sci. USA., 110, 16109, 10.1073/pnas.1315292110 · DOI · Paper page
  37. Zhang, 2016, The ANGPTL3-4-8 model, a molecular mechanism for triglyceride trafficking, Open Biol., 6, 150272, 10.1098/rsob.150272 · DOI
  38. Izumi, 2018, CRISPR/Cas9-mediated Angptl8 knockout suppresses plasma triglyceride concentrations and adiposity in rats, J. Lipid Res., 59, 1575, 10.1194/jlr.M082099 · DOI
  39. Abu-Farha, 2016, Circulating angiopoietin-like protein 8 (betatrophin) association with hsCRP and metabolic syndrome, Cardiovasc. Diabetol., 15, 25, 10.1186/s12933-016-0346-0 · DOI
  40. Fu, 2015, A lipasin/Angptl8 monoclonal antibody lowers mouse serum triglycerides involving increased postprandial activity of the cardiac lipoprotein lipase, Sci. Rep., 5, 18502, 10.1038/srep18502 · DOI
  41. Zhang, 2013, Emerging roles of lipasin as a critical lipid regulator, Biochem. Biophys. Res. Commun., 432, 401, 10.1016/j.bbrc.2013.01.129 · DOI
  42. Zhang, 2012, Lipasin, a novel nutritionally-regulated liver-enriched factor that regulates serum triglyceride levels, Biochem. Biophys. Res. Commun., 424, 786, 10.1016/j.bbrc.2012.07.038 · DOI · Paper page
  43. Gusarova, 2017, ANGPTL8 blockade with a monoclonal antibody promotes triglyceride clearance, energy expenditure, and weight loss in mice, Endocrinology., 158, 1252, 10.1210/en.2016-1894 · DOI
  44. Quagliarini, 2012, Atypical angiopoietin-like protein that regulates ANGPTL3, Proc. Natl. Acad. Sci. USA., 109, 19751, 10.1073/pnas.1217552109 · DOI · Paper page
  45. Siddiqa, 2016, Structural characterization of ANGPTL8 (betatrophin) with its interacting partner lipoprotein lipase, Comput. Biol. Chem., 61, 210, 10.1016/j.compbiolchem.2016.01.009 · DOI
  46. He, 2018, Lipoprotein lipase: biosynthesis, regulatory factors, and its role in atherosclerosis and other diseases, Clin. Chim. Acta., 480, 126, 10.1016/j.cca.2018.02.006 · DOI
  47. Mead, 2002, Lipoprotein lipase: structure, function, regulation, and role in disease, J. Mol. Med. (Berl.)., 80, 753, 10.1007/s00109-002-0384-9 · DOI
  48. Beigneux, 2019, Lipoprotein lipase is active as a monomer, Proc. Natl. Acad. Sci. USA., 116, 6319, 10.1073/pnas.1900983116 · DOI · Paper page
  49. Chappell, 1993, Lipoprotein lipase induces catabolism of normal triglyceride-rich lipoproteins via the low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor in vitro. A process facilitated by cell-surface proteoglycans, J. Biol. Chem., 268, 14168, 10.1016/S0021-9258(19)85223-7 · DOI
  50. Young, 2019, GPIHBP1 and lipoprotein lipase, partners in plasma triglyceride metabolism, Cell Metab., 30, 51, 10.1016/j.cmet.2019.05.023 · DOI
  51. Gusarova, 2015, ANGPTL3 blockade with a human monoclonal antibody reduces plasma lipids in dyslipidemic mice and monkeys, J. Lipid Res., 56, 1308, 10.1194/jlr.M054890 · DOI · Paper page
  52. Aryal, 2019, ANGPTL4 in metabolic and cardiovascular disease, Trends Mol. Med., 25, 723, 10.1016/j.molmed.2019.05.010 · DOI
  53. Dijk, 2014, Regulation of lipoprotein lipase by ANGPTL4, Trends Endocrinol. Metab., 25, 146, 10.1016/j.tem.2013.12.005 · DOI
  54. Gutgsell, 2019, Mapping the sites of the lipoprotein lipase (LPL)-angiopoietin-like protein 4 (ANGPTL4) interaction provides mechanistic insight into LPL inhibition, J. Biol. Chem., 294, 2678, 10.1074/jbc.RA118.005932 · DOI
  55. Dijk, 2018, Regulation of angiopoietin-like 4 and lipoprotein lipase in human adipose tissue, J. Clin. Lipidol., 12, 773, 10.1016/j.jacl.2018.02.006 · DOI
  56. Mysling, 2016, The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding, eLife., 5, 1
  57. Liu, 2010, Angiopoietin-like protein 3 inhibits lipoprotein lipase activity through enhancing its cleavage by proprotein convertases, J. Biol. Chem., 285, 27561, 10.1074/jbc.M110.144279 · DOI · Paper page
  58. Lee, 2009, Identification of a new functional domain in angiopoietin-like 3 (ANGPTL3) and angiopoietin-like 4 (ANGPTL4) involved in binding and inhibition of lipoprotein lipase (LPL), J. Biol. Chem., 284, 13735, 10.1074/jbc.M807899200 · DOI · Paper page
  59. Sonnenburg, 2009, GPIHBP1 stabilizes lipoprotein lipase and prevents its inhibition by angiopoietin-like 3 and angiopoietin-like 4, J. Lipid Res., 50, 2421, 10.1194/jlr.M900145-JLR200 · DOI · Paper page
  60. Ahmad, 2019, Inhibition of angiopoietin-like protein 3 with a monoclonal antibody reduces triglycerides in hypertriglyceridemia, Circulation., 140, 470, 10.1161/CIRCULATIONAHA.118.039107 · DOI
  61. Shimamura, 2007, Angiopoietin-like protein 3 regulates plasma HDL cholesterol through suppression of endothelial lipase, Arterioscler. Thromb. Vasc. Biol., 27, 366, 10.1161/01.ATV.0000252827.51626.89 · DOI · Paper page
  62. Wang, 2015, Hepatic ANGPTL3 regulates adipose tissue energy homeostasis, Proc. Natl. Acad. Sci. USA., 112, 11630, 10.1073/pnas.1515374112 · DOI · Paper page
  63. Musunuru, 2010, Exome sequencing, ANGPTL3 mutations, and familial combined hypolipidemia, N. Engl. J. Med., 363, 2220, 10.1056/NEJMoa1002926 · DOI · Paper page
  64. Noto, 2012, Prevalence of ANGPTL3 and APOB gene mutations in subjects with combined hypolipidemia, Arterioscler. Thromb. Vasc. Biol., 32, 805, 10.1161/ATVBAHA.111.238766 · DOI · Paper page
  65. Desai, 2007, Lipid-lowering effects of anti-angiopoietin-like 4 antibody recapitulate the lipid phenotype found in angiopoietin-like 4 knockout mice, Proc. Natl. Acad. Sci. USA., 104, 11766, 10.1073/pnas.0705041104 · DOI · Paper page
  66. Oteng, 2017, Feeding Angptl4(-/-) mice trans fat promotes foam cell formation in mesenteric lymph nodes without leading to ascites, J. Lipid Res., 58, 1100, 10.1194/jlr.M074278 · DOI
  67. Lichtenstein, 2010, Angptl4 protects against severe proinflammatory effects of saturated fat by inhibiting fatty acid uptake into mesenteric lymph node macrophages, Cell Metab., 12, 580, 10.1016/j.cmet.2010.11.002 · DOI · Paper page
  68. Bailetti, 2018, ANGPTL4 gene E40K variation protects against obesity-associated dyslipidemia in participants with obesity, Obes. Sci. Pract., 5, 83, 10.1002/osp4.311 · DOI
  69. Smart-Halajko, 2011, ANGPTL4 variants E40K and T266M are associated with lower fasting triglyceride levels in non-hispanic white americans from the Look AHEAD clinical trial, BMC Med. Genet., 12, 89, 10.1186/1471-2350-12-89 · DOI
  70. Lim, 2016, Genetics: polymorphisms in ANGPTL4 link triglycerides with CAD, Nat. Rev. Cardiol., 13, 245, 10.1038/nrcardio.2016.46 · DOI
  71. Gusarova, 2018, Genetic inactivation of ANGPTL4 improves glucose homeostasis and is associated with reduced risk of diabetes, Nat. Commun., 9, 2252, 10.1038/s41467-018-04611-z · DOI · Paper page
  72. Peloso, 2014, Association of low-frequency and rare coding-sequence variants with blood lipids and coronary heart disease in 56,000 whites and blacks, Am. J. Hum. Genet., 94, 223, 10.1016/j.ajhg.2014.01.009 · DOI
  73. Kovrov, 2019, On the mechanism of angiopoietin-like protein 8 for control of lipoprotein lipase activity, J. Lipid Res., 60, 783, 10.1194/jlr.M088807 · DOI · Paper page
  74. Samnegård, 2005, Serum matrix metalloproteinase-3 concentration is influenced by MMP-3–1612 5A/6A promoter genotype and associated with myocardial infarction, J. Intern. Med., 258, 411, 10.1111/j.1365-2796.2005.01561.x · DOI
  75. Mannila, 2005, Contribution of haplotypes across the fibrinogen gene cluster to variation in risk of myocardial infarction, Thromb. Haemost., 93, 570, 10.1160/TH04-10-0698 · DOI
  76. Silveira, 2012, Relationships of plasma factor VIIa-antithrombin complexes to manifest and future cardiovascular disease, Thromb. Res., 130, 221, 10.1016/j.thromres.2011.08.029 · DOI
  77. Hayne, 2017, Biochemical analysis of the lipoprotein lipase truncation variant, LPL(s447x), reveals increased lipoprotein uptake, Biochemistry., 56, 525, 10.1021/acs.biochem.6b00945 · DOI · Paper page
  78. Basu, 2011, Determination of lipoprotein lipase activity using a novel fluorescent lipase assay, J. Lipid Res., 52, 826, 10.1194/jlr.D010744 · DOI
  79. Henry, 2014, Basal insulin peglispro demonstrates preferential hepatic versus peripheral action relative to insulin glargine in healthy subjects, Diabetes Care., 37, 2609, 10.2337/dc14-0210 · DOI
  80. Ginsberg, 2016, Lipid changes during basal insulin peglispro, insulin glargine, or NPH treatment in six IMAGINE trials, Diabetes Obes. Metab., 18, 1089, 10.1111/dom.12754 · DOI
  81. Rip, 2006, Lipoprotein lipase s447x: a naturally occurring gain-of-function mutation, Arterioscler. Thromb. Vasc. Biol., 26, 1236, 10.1161/01.ATV.0000219283.10832.43 · DOI · Paper page
  82. Medh, 2000, Lipoprotein lipase- and hepatic triglyceride lipase- promoted very low density lipoprotein degradation proceeds via an apolipoprotein E-dependent mechanism, J. Lipid Res., 41, 1858, 10.1016/S0022-2275(20)31980-5 · DOI
  83. Luo, 2018, ANGPTL8: an important regulator in metabolic disorders, Front. Endocrinol. (Lausanne)., 9, 169, 10.3389/fendo.2018.00169 · DOI
  84. Nidhina Haridas, 2015, Regulation of angiopoietin-like proteins (ANGPTLs) 3 and 8 by insulin, J. Clin. Endocrinol. Metab., 100, E1299, 10.1210/jc.2015-1254 · DOI · Paper page
  85. Troutt, 2011, Dual-monoclonal, sandwich immunoassay specific for glucose-dependent insulinotropic peptide1–42, the active form of the incretin hormone, Clin. Chem., 57, 849, 10.1373/clinchem.2010.159954 · DOI
  86. Su, 2018, New insights into ANGPTL3 in controlling lipoprotein metabolism and risk of cardiovascular diseases, Lipids Health Dis., 17, 12, 10.1186/s12944-018-0659-y · DOI
  87. Williams, 1994, The carboxyl-terminal domain of lipoprotein lipase binds to the low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor (LRP) and mediates binding of normal very low density lipoproteins to LRP, J. Biol. Chem., 269, 8653, 10.1016/S0021-9258(17)37017-5 · DOI · Paper page
  88. Beisiegel, 1991, Lipoprotein lipase enhances the binding of chylomicrons to low density lipoprotein receptor-related protein, Proc. Natl. Acad. Sci. USA., 88, 8342, 10.1073/pnas.88.19.8342 · DOI · Paper page
  89. Takahashi, 1995, Enhancement of the binding of triglyceride-rich lipoproteins to the very low density lipoprotein receptor by apolipoprotein E and lipoprotein lipase, J. Biol. Chem., 270, 15747, 10.1074/jbc.270.26.15747 · DOI
  90. Loeffler, 2007, Lipoprotein lipase-facilitated uptake of LDL is mediated by the LDL receptor, J. Lipid Res., 48, 288, 10.1194/jlr.M600292-JLR200 · DOI
  91. Wung, 2006, The lipoprotein lipase gene in combined hyperlipidemia: evidence of a protective allele depletion, Lipids Health Dis., 5, 19, 10.1186/1476-511X-5-19 · DOI
  92. Adachi, 2011, Angptl4 deficiency decreases serum triglyceride levels in low-density lipoprotein receptor knockout mice and streptozotocin-induced diabetic mice, Biochem. Biophys. Res. Commun., 409, 177, 10.1016/j.bbrc.2011.04.110 · DOI

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Metadata

Authors
Chen, Y. Q., Pottanat, T. G., Siegel, R. W., Ehsani, M., Qian, Y.-W., Zhen, E. Y., Regmi, A., Roell, W. C., Guo, H., Luo, M. J., Gimeno, R. E., van't Hooft, F., & Konrad, R. J.
Venue
Journal of Lipid Research
Publisher
Elsevier BV
Published
2020-08
Volume
61
Issue
8
Pages
1203-1220
ISSN
0022-2275
DOI
10.1194/jlr.ra120000781
PMC
PMC7397750
Cited by
147
References
11
Language
en
Licence
Funders
Eli Lilly and Company

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