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Comparison of angiopoietin-like protein 3 and 4 reveals structural and mechanistic similarities

Gunn, Kathryn H., Gutgsell, Aspen R., Xu, Yongmei, Johnson, Caitlin V., Liu, Jian, Neher, Saskia B.·2021·Journal of Biological Chemistry

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Research works printed but not linked: 55

  1. Dijk, 2016, Regulation of lipid metabolism by angiopoietin-like proteins, Curr. Opin. Lipidol., 27, 249, 10.1097/MOL.0000000000000290 · DOI
  2. Fried, 1983, Prolonged effects of fasting-refeeding on rat adipose tissue lipoprotein lipase activity: Influence of caloric restriction during refeeding, J. Nutr., 113, 1861, 10.1093/jn/113.9.1861 · DOI
  3. Quig, 1983, The influence of starvation and refeeding on the lipoprotein lipase activity of skeletal muscle and adipose tissue of lean and obese Zucker rats, J. Nutr., 113, 1150, 10.1093/jn/113.6.1150 · DOI
  4. Zhang, 2016, The ANGPTL3-4-8 model, a molecular mechanism for triglyceride trafficking, Open Biol., 6, 150272, 10.1098/rsob.150272 · DOI
  5. Kersten, 2000, Characterization of the fasting-induced adipose factor FIAF, a novel peroxisome proliferator-activated receptor target gene, J. Biol. Chem., 275, 28488, 10.1074/jbc.M004029200 · DOI · Paper page
  6. 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
  7. 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
  8. 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
  9. 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
  10. Chen, 2020, Angiopoietin-like protein 8 differentially regulates ANGPTL3 and ANGPTL4 during postprandial partitioning of fatty acids, J. Lipid Res., 61, 1203, 10.1194/jlr.RA120000781 · DOI · Paper page
  11. Willer, 2008, Newly identified loci that influence lipid concentrations and risk of coronary artery disease, Nat. Genet., 40, 161, 10.1038/ng.76 · DOI · Paper page
  12. 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
  13. Leiherer, 2020, High betatrophin in coronary patients protects from cardiovascular events, Atherosclerosis, 293, 62, 10.1016/j.atherosclerosis.2019.11.011 · DOI
  14. Essalmani, 2013, Furin is the primary in vivo convertase of angiopoietin-like 3 and endothelial lipase in hepatocytes, J. Biol. Chem., 288, 26410, 10.1074/jbc.M113.501304 · DOI · Paper page
  15. Yin, 2009, Genetic variation in ANGPTL4 provides insights into protein processing and function, J. Biol. Chem., 284, 13213, 10.1074/jbc.M900553200 · DOI · Paper page
  16. Lei, 2011, Proteolytic processing of angiopoietin-like protein 4 by proprotein convertases modulates its inhibitory effects on lipoprotein lipase activity, J. Biol. Chem., 286, 15747, 10.1074/jbc.M110.217638 · DOI · Paper page
  17. Ono, 2003, Protein region important for regulation of lipid metabolism in angiopoietin-like 3 (ANGPTL3): ANGPTL3 is cleaved and activated in vivo, J. Biol. Chem., 278, 41804, 10.1074/jbc.M302861200 · DOI · Paper page
  18. 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
  19. Shan, 2009, The angiopoietin-like proteins ANGPTL3 and ANGPTL4 inhibit lipoprotein lipase activity through distinct mechanisms, J. Biol. Chem., 284, 1419, 10.1074/jbc.M808477200 · DOI · Paper page
  20. 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
  21. Reimund, 2017, Lipoprotein lipase activity and interactions studied in human plasma by isothermal titration calorimetry, J. Lipid Res., 58, 279, 10.1194/jlr.D071787 · DOI · Paper page
  22. Nimonkar, 2020, A lipoprotein lipase-GPI-anchored high-density lipoprotein-binding protein 1 fusion lowers triglycerides in mice: Implications for managing familial chylomicronemia syndrome, J. Biol. Chem., 295, 2900, 10.1074/jbc.RA119.011079 · DOI
  23. 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
  24. Lafferty, 2013, Angiopoietin-like protein 4 inhibition of lipoprotein lipase: Evidence for reversible complex formation, J. Biol. Chem., 288, 28524, 10.1074/jbc.M113.497602 · DOI · Paper page
  25. Kristensen, 2020, Unfolding of monomeric lipoprotein lipase by ANGPTL4: Insight into the regulation of plasma triglyceride metabolism, Proc. Natl. Acad. Sci. U. S. A., 117, 4337, 10.1073/pnas.1920202117 · DOI · Paper page
  26. Biterova, 2018, Structures of Angptl3 and Angptl4, modulators of triglyceride levels and coronary artery disease, Sci. Rep., 8, 6752, 10.1038/s41598-018-25237-7 · DOI · Paper page
  27. Ge, 2005, Differential regulation and properties of angiopoietin-like proteins 3 and 4, J. Lipid Res., 46, 1484, 10.1194/jlr.M500005-JLR200 · DOI · Paper page
  28. Yau, 2009, A highly conserved motif within the NH2-terminal coiled-coil domain of angiopoietin-like protein 4 confers its inhibitory effects on lipoprotein lipase by disrupting the enzyme dimerization, J. Biol. Chem., 284, 11942, 10.1074/jbc.M809802200 · DOI · Paper page
  29. Yoshino, 1987, A graphical method for determining inhibition parameters for partial and complete inhibitors, Biochem. J., 248, 815, 10.1042/bj2480815 · DOI
  30. Shimamura, 2007, Angiopoietin-like protein3 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
  31. Cazes, 2006, Extracellular matrix-bound angiopoietin-like 4 inhibits endothelial cell adhesion, migration, and sprouting and alters actin cytoskeleton, Circ. Res., 99, 1207, 10.1161/01.RES.0000250758.63358.91 · DOI
  32. 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
  33. Bengtsson-Olivecrona, 1991, Phospholipase activity of milk lipoprotein lipase, Methods Enzymol., 197, 345, 10.1016/0076-6879(91)97160-Z · DOI
  34. Wu, 2018, Coexpression of novel furin-resistant LPL variants with lipase maturation factor 1 enhances LPL secretion and activity, J. Lipid Res., 59, 2456, 10.1194/jlr.D086793 · DOI · Paper page
  35. Classen, 2013, Implementation and performance of SIBYLS: A dual endstation small-angle X-ray scattering and macromolecular crystallography beamline at the advanced light source, J. Appl. Crystallogr., 46, 1, 10.1107/S0021889812048698 · DOI
  36. Dyer, 2014, High-throughput SAXS for the characterization of biomolecules in solution: A practical approach, Methods Mol. Biol., 1091, 245, 10.1007/978-1-62703-691-7_18 · DOI
  37. Hura, 2013, Comprehensive macromolecular conformations mapped by quantitative SAXS analyses, Nat. Methods, 10, 453, 10.1038/nmeth.2453 · DOI
  38. Putnam, 2007, X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution, Q. Rev. Biophys., 40, 191, 10.1017/S0033583507004635 · DOI · Paper page
  39. Forster, 2010, Scatter: Software for the analysis of nano- and mesoscale small-angle scattering, J. Appl. Crystallogr., 43, 639, 10.1107/S0021889810008289 · DOI
  40. Dominguez-Martin, 2020, Structural analysis of a new carotenoid-binding protein: The C-terminal domain homolog of the OCP, Sci. Rep., 10, 15564, 10.1038/s41598-020-72383-y · DOI
  41. Knott, 2019, Structural basis for AcrVA4 inhibition of specific CRISPR-Cas12a, Elife, 8, 10.7554/eLife.49110 · DOI
  42. Fischetti, 2004, The BioCAT undulator beamline 18ID: A facility for biological non-crystalline diffraction and X-ray absorption spectroscopy at the advanced photon source, J. Synchrotron Radiat., 11, 399, 10.1107/S0909049504016760 · DOI
  43. Hopkins, 2017, BioXTAS RAW: Improvements to a free open-source program for small-angle X-ray scattering data reduction and analysis, J. Appl. Crystallogr., 50, 1545, 10.1107/S1600576717011438 · DOI
  44. Franke, 2017, ATSAS 2.8: A comprehensive data analysis suite for small-angle scattering from macromolecular solutions, J. Appl. Crystallogr., 50, 1212, 10.1107/S1600576717007786 · DOI
  45. Konarev, 2003, PRIMUS: A windows PC-based system for small-angle scattering data analysis, J. Appl. Crystallogr., 36, 1277, 10.1107/S0021889803012779 · DOI
  46. Petoukhov, 2007, ATSAS 2.1 - towards automated and web-supported small-angle scattering data analysis, J. Appl. Crystallogr., 40, S223, 10.1107/S0021889807002853 · DOI
  47. Svergun, 1992, Determination of the regularization parameter in indirect-transform methods using perceptual criteria, J. Appl. Crystallogr., 25, 495, 10.1107/S0021889892001663 · DOI
  48. Franke, 2009, DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering, J. Appl. Crystallogr., 42, 342, 10.1107/S0021889809000338 · DOI · Paper page
  49. Volkov, 2003, Uniqueness of ab initio shape determination in small-angle scattering, J. Appl. Crystallogr., 36, 860, 10.1107/S0021889803000268 · DOI
  50. Svergun, 1999, Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing, Biophys. J., 76, 2879, 10.1016/S0006-3495(99)77443-6 · DOI
  51. Franke, 2015, Correlation Map, a goodness-of-fit test for one-dimensional X-ray scattering spectra, Nat. Methods, 12, 419, 10.1038/nmeth.3358 · DOI
  52. Gunn, 2020, The structure of helical lipoprotein lipase reveals an unexpected twist in lipase storage, Proc. Natl. Acad. Sci. U. S. A., 117, 10254, 10.1073/pnas.1916555117 · DOI
  53. Xu, 2017, Synthetic oligosaccharides can replace animal-sourced low-molecular weight heparins, Sci. Transl. Med., 9, 10.1126/scitranslmed.aan5954 · DOI
  54. Miller, 2018, 3-O sulfation of heparin leads to hepatotropism and longer circulatory half-life, Thromb. Res., 167, 80, 10.1016/j.thromres.2018.05.018 · DOI
  55. Kikhney, 2020, SASBDB: Towards an automatically curated and validated repository for biological scattering data, Protein Sci., 29, 66, 10.1002/pro.3731 · DOI

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Metadata

Authors
Gunn, K. H., Gutgsell, A. R., Xu, Y., Johnson, C. V., Liu, J., & Neher, S. B.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2021-01
Volume
296
Pages
100312
ISSN
0021-9258
Cited by
12
References
5
Language
en
Funders
  • American Heart Association (19PRE34370070, 20POST35210031)
  • Office of Science
  • National Institutes of Health (R01-HL094463)
  • Argonne National Laboratory (DE-AC02-06CH11357)
  • U.S. Department of Energy
  • University of North Carolina
  • National Cancer Institute
  • Office of Extramural Research, National Institutes of Health (1R42GM128484, 9 P41 GM103622, P30 GM124169, P30CA016086, R01-HL12565, R01-HL144970)
  • National Institute of General Medical Sciences (S10OD018483)

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