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

ANGPTL8 promotes the ability of ANGPTL3 to bind and inhibit lipoprotein lipase

Chi, Xun, Britt, Emily C., Shows, Hannah W., Hjelmaas, Alexander J., Shetty, Shwetha K., Cushing, Emily M., Li, Wendy, Dou, Alex, Zhang, Ren, Davies, Brandon S.J.·2017·Molecular Metabolism
DOI 10.1016/j.molmet.2017.06.014PMC PMC5641604
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Crossref · 10.1016/j.molmet.2017.06.014

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  • 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 [115]

    The Results section (‘ANGPTL8 promotes the inhibitory efficiency of ANGPTL3’; page unavailable) reports that co-expressed ANGPTL3 and ANGPTL8 significantly inhibited LPL where either protein alone had little effect. The Abstract Results likewise describes a dramatically increased inhibitory ability, but our copy does not establish the claimed ‘orders of magnitude’ difference. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

  • Overexpression of ANGPTL8 in the absence of ANGPTL3, or vice versa, has limited ability to increase plasma triglycerides.

    “overexpression of ANGPTL8 in the absence of ANGPTL3, or vice versa, has limited ability to increase plasma triglycerides (19, 115, 137)”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [115]

  • 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 [115]

  • GPIHBP1 protects LPL from ANGPTL3 inhibition as does heparin.

    “LPL’s endothelial cell receptor GPIHBP1 protects LPL from ANGPTL3 inhibition as does heparin (60, 115).”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [115]

  • Complex formation is necessary for efficient secretion of ANGPTL8.

    “Complex formation is necessary for efficient secretion of ANGPTL8 (115)”

    From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [115]

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Research works printed but not linked: 40

  1. De Man, 1996, Triglyceride-rich lipoproteins in non-insulin-dependent diabetes mellitus: post-prandial metabolism and relation to premature atherosclerosis, European Journal of Clinical Investigation, 26, 89, 10.1046/j.1365-2362.1996.114256.x · DOI
  2. Subramanian, 2012, Hypertriglyceridemia secondary to obesity and diabetes, Biochimica Et Biophysica Acta, 1821, 819, 10.1016/j.bbalip.2011.10.003 · DOI
  3. Do, 2013, Common variants associated with plasma triglycerides and risk for coronary artery disease, Nature Genetics, 45, 1345, 10.1038/ng.2795 · DOI · Paper page
  4. Kannel, 2009, Triglycerides as vascular risk factors: new epidemiologic insights, Current Opinion in Cardiology, 24, 345, 10.1097/HCO.0b013e32832c1284 · DOI · Paper page
  5. Korn, 1955, Clearing factor, a heparin-activated lipoprotein lipase i.e. isolation and characterization of the enzyme from normal rat heart, Journal of Biological Chemistry, 215, 1, 10.1016/S0021-9258(18)66011-9 · DOI
  6. Davies, 2010, GPIHBP1 is responsible for the entry of lipoprotein lipase into capillaries, Cell Metabolism, 12, 42, 10.1016/j.cmet.2010.04.016 · DOI · Paper page
  7. Beigneux, 2007, Glycosylphosphatidylinositol-anchored high density lipoprotein–binding protein 1 plays a critical role in the lipolytic processing of chylomicrons, Cell Metabolism, 5, 279, 10.1016/j.cmet.2007.02.002 · DOI · Paper page
  8. Goulbourne, 2014, The GPIHBP1-LPL complex is responsible for the margination of triglyceride-rich lipoproteins in capillaries, Cell Metabolism, 19, 849, 10.1016/j.cmet.2014.01.017 · DOI · Paper page
  9. Wang, 2015, Hepatic ANGPTL3 regulates adipose tissue energy homeostasis, Proceedings of the National Academy of Sciences, 112, 11630, 10.1073/pnas.1515374112 · DOI · Paper page
  10. Shimizugawa, 2002, ANGPTL3 decreases very low density lipoprotein triglyceride clearance by inhibition of lipoprotein lipase, The Journal of Biological Chemistry, 277, 33742, 10.1074/jbc.M203215200 · DOI · Paper page
  11. Koishi, 2002, ANGPTL3 regulates lipid metabolism in mice, Nature Genetics, 30, 151, 10.1038/ng814 · DOI · Paper page
  12. Romeo, 2009, Rare loss-of-function mutations in ANGPTL family members contribute to plasma triglyceride levels in humans, The Journal of Clinical Investigation, 119, 70
  13. Robciuc, 2013, ANGPTL3 deficiency is associated with increased insulin sensitivity, lipoprotein lipase activity, and decreased serum free fatty acids, Arteriosclerosis, Thrombosis, and Vascular Biology, 33, 1706, 10.1161/ATVBAHA.113.301397 · DOI · Paper page
  14. Zhang, 2012, Lipasin, a novel nutritionally-regulated liver-enriched factor that regulates serum triglyceride levels, Biochemical and Biophysical Research Communications, 424, 786, 10.1016/j.bbrc.2012.07.038 · DOI · Paper page
  15. Quagliarini, 2012, Atypical angiopoietin-like protein that regulates ANGPTL3, Proceedings of the National Academy of Sciences, 109, 19751, 10.1073/pnas.1217552109 · DOI · Paper page
  16. Ren, 2012, Identification of RIFL, a novel adipocyte-enriched insulin target gene with a role in lipid metabolism, American Journal of Physiology – Endocrinology and Metabolism, 303, E334, 10.1152/ajpendo.00084.2012 · DOI · Paper page
  17. Wang, 2013, Mice lacking ANGPTL8 (Betatrophin) manifest disrupted triglyceride metabolism without impaired glucose homeostasis, Proceedings of the National Academy of Sciences, 110, 16109, 10.1073/pnas.1315292110 · DOI · Paper page
  18. Yi, 2013, Betatrophin: a hormone that controls pancreatic β cell proliferation, Cell, 153, 747, 10.1016/j.cell.2013.04.008 · DOI · Paper page
  19. Fu, 2015, A lipasin/ANGPTL8 monoclonal antibody lowers mouse serum triglycerides involving increased postprandial activity of the cardiac lipoprotein lipase, Scientific Reports, 5, 10.1038/srep18502 · DOI
  20. Ge, 2005, Differential regulation and properties of angiopoietin-like proteins 3 and 4, Journal of Lipid Research, 46, 1484, 10.1194/jlr.M500005-JLR200 · DOI · Paper page
  21. Beigneux, 2009, Highly conserved cysteines within the ly6 domain of gpihbp1 are crucial for the binding of lipoprotein lipase, Journal of Biological Chemistry, 284, 30240, 10.1074/jbc.M109.046391 · DOI
  22. Chi, 2015, Angiopoietin-like 4 modifies the interactions between lipoprotein lipase and its endothelial cell transporter gpihbp1, Journal of Biological Chemistry, 290, 11865, 10.1074/jbc.M114.623769 · DOI · Paper page
  23. Basu, 2011, Determination of lipoprotein lipase activity using a novel fluorescent lipase assay, Journal of Lipid Research, 52, 826, 10.1194/jlr.D010744 · DOI
  24. Tang, 2010, A mouse knockout library for secreted and transmembrane proteins, Nature Biotechnology, 28, 749, 10.1038/nbt.1644 · DOI
  25. Young, 2011, GPIHBP1, an endothelial cell transporter for lipoprotein lipase, Journal of Lipid Research, 52, 1869, 10.1194/jlr.R018689 · DOI
  26. Hall, 2012, Engineered luciferase reporter from a deep sea shrimp utilizing a novel imidazopyrazinone substrate, ACS Chemical Biology, 7, 1848, 10.1021/cb3002478 · DOI
  27. Sonnenburg, 2009, GPIHBP1 stabilizes lipoprotein lipase and prevents its inhibition by angiopoietin-like 3 and angiopoietin-like 4, Journal of Lipid Research, 50, 2421, 10.1194/jlr.M900145-JLR200 · DOI · Paper page
  28. Ono, 2003, Protein region important for regulation of lipid metabolism in angiopoietin-like 3 (ANGPTL3) ANGPTL3 is cleaved and activated in vivo, Journal of Biological Chemistry, 278, 41804, 10.1074/jbc.M302861200 · DOI · Paper page
  29. Essalmani, 2013, Furin is the primary in vivo convertase of angiopoietin-like 3 and endothelial lipase in hepatocytes, Journal of Biological Chemistry, 288, 26410, 10.1074/jbc.M113.501304 · DOI · Paper page
  30. Lei, 2011, Proteolytic processing of angiopoietin-like protein 4 by proprotein convertases modulates its inhibitory effects on lipoprotein lipase activity, Journal of Biological Chemistry, 286, 15747, 10.1074/jbc.M110.217638 · DOI · Paper page
  31. Lu, 1994, Agouti protein is an antagonist of the melanocyte-stimulating-hormone receptor, Nature, 371, 799, 10.1038/371799a0 · DOI
  32. Haller, 2017, ANGPTL8 requires ANGPTL3 to inhibit lipoprotein lipase and plasma triglyceride clearance, Journal of Lipid Research, 10.1194/jlr.M075689 · DOI · Paper page
  33. Nidhina Haridas, 2015, Regulation of angiopoietin-like proteins (ANGPTLs) 3 and 8 by insulin, The Journal of Clinical Endocrinology & Metabolism, 100, E1299, 10.1210/jc.2015-1254 · DOI · Paper page
  34. Abu-Farha, 2016, Increased ANGPTL3, 4 and ANGPTL8/betatrophin expression levels in obesity and T2D, Lipids in Health and Disease, 15, 10.1186/s12944-016-0337-x · DOI
  35. Chung, 2016, Circulating angiopoietin-like protein 8 (ANGPTL8) and ANGPTL3 concentrations in relation to anthropometric and metabolic profiles in Korean children: a prospective cohort study, Cardiovascular Diabetology, 15, 10.1186/s12933-015-0324-y · DOI
  36. Haridas, 2015, Regulation of angiopoietin-like proteins (ANGPTLs) 3 and 8 by insulin, The Journal of Clinical Endocrinology & Metabolism, 100, E1299, 10.1210/jc.2015-1254 · DOI · Paper page
  37. Shimamura, 2007, Angiopoietin-like protein3 regulates plasma HDL cholesterol through suppression of endothelial lipase, Arteriosclerosis, Thrombosis, and Vascular Biology, 27, 366, 10.1161/01.ATV.0000252827.51626.89 · DOI · Paper page
  38. Zhang, 2016, The ANGPTL3-4-8 model, a molecular mechanism for triglyceride trafficking, Open Biology, 6, 10.1098/rsob.150272 · DOI
  39. Gusarova, 2015, ANGPTL3 blockade with a human monoclonal antibody reduces plasma lipids in dyslipidemic mice and monkeys, Journal of Lipid Research, 56, 1308, 10.1194/jlr.M054890 · DOI · Paper page
  40. Gusarova, 2017, ANGPTL8 blockade with a monoclonal antibody promotes triglyceride clearance, energy expenditure and weight loss in mice, Endocrinology, 10.1210/en.2016-1894 · DOI

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Metadata

Authors
Chi, X., Britt, E. C., Shows, H. W., Hjelmaas, A. J., Shetty, S. K., Cushing, E. M., Li, W., Dou, A., Zhang, R., & Davies, B. S. J.
ORCID
Venue
Molecular Metabolism
Publisher
Elsevier BV
Published
2017-10
Volume
6
Issue
10
Pages
1137-1149
ISSN
2212-8778
DOI
10.1016/j.molmet.2017.06.014
PMC
PMC5641604
Cited by
174
References
8
Language
en
Licence

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