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A thumbwheel mechanism for APOA1 activation of LCAT activity in HDL[S]
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The alignment of the two ApoA1 proteins in discoidal particles alters the ability of ApoA1 to activate LCAT and alters the rate of cholesterol esterification.
“The alignment of the two ApoA1 proteins in discoidal particles alter the ability of ApoA1 to activate LCAT and alters the rate of cholesterol esterification [119].”
From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [119]
ApoA1 in HDL adopts an antiparallel dimer.
“This is similar to ApoA1 in HDL which adopts an antiparallel dimer [60, 119].”
From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [119]
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A consensus model of human apolipoprotein A-I in its monomeric and lipid-free state
Melchior, J. T., Walker, R. G., Cooke, A. L., Morris, J., Castleberry, M., Thompson, T. B., Jones, M. K., Song, H. D., Rye, K.-A., Oda, M. N., et al. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3501 · Cited by 71
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Research works printed but not linked: 62
- Gordon, 1977, High density lipoprotein as a protective factor against coronary heart disease. The Framingham Study, Am. J. Med., 62, 707, 10.1016/0002-9343(77)90874-9 · DOI · Paper page
- Shah, 2013, Proteomic diversity of high density lipoproteins: our emerging understanding of its importance in lipid transport and beyond, J. Lipid Res., 54, 2575, 10.1194/jlr.R035725 · DOI
- Gu, 1998, The efficient cellular uptake of high density lipoprotein lipids via scavenger receptor class B type I requires not only receptor-mediated surface binding but also receptor-specific lipid transfer mediated by its extracellular domain, J. Biol. Chem., 273, 26338, 10.1074/jbc.273.41.26338 · DOI
- Puranik, 2008, Low dose apolipoprotein A-I rescues carotid arteries from inflammation in vivo, Atherosclerosis., 196, 240, 10.1016/j.atherosclerosis.2007.05.008 · DOI
- Navab, 1991, Monocyte transmigration induced by modification of low density lipoprotein in cocultures of human aortic wall cells is due to induction of monocyte chemotactic protein 1 synthesis and is abolished by high density lipoprotein, J. Clin. Invest., 88, 2039, 10.1172/JCI115532 · DOI
- Soutar, 1975, Effect of the human plasma apolipoproteins and phosphatidylcholine acyl donor on the activity of lecithin: cholesterol acyltransferase, Biochemistry., 14, 3057, 10.1021/bi00685a003 · DOI
- Jonas, 1991, Lecithin-cholesterol acyltransferase in the metabolism of high-density lipoproteins, Biochim. Biophys. Acta., 1084, 205, 10.1016/0005-2760(91)90062-M · DOI
- Jonas, 1984, Discoidal complexes of A and C apolipoproteins with lipids and their reactions with lecithin: cholesterol acyltransferase, J. Biol. Chem., 259, 6369, 10.1016/S0021-9258(20)82151-6 · DOI
- Zannis, 2006, Role of apoA-I, ABCA1, LCAT, and SR-BI in the biogenesis of HDL, J. Mol. Med. (Berl.)., 84, 276, 10.1007/s00109-005-0030-4 · DOI
- Fotakis, 2015, The effect of natural LCAT mutations on the biogenesis of HDL, Biochemistry., 54, 3348, 10.1021/acs.biochem.5b00180 · DOI
- Chroni, 2005, Point mutations in apolipoprotein A-I mimic the phenotype observed in patients with classical lecithin:cholesterol acyltransferase deficiency, Biochemistry., 44, 14353, 10.1021/bi050962o · DOI
- Sviridov, 2000, Identification of a sequence of apolipoprotein A-I associated with the activation of lecithin:cholesterol acyltransferase, J. Biol. Chem., 275, 19707, 10.1074/jbc.M000962200 · DOI
- Cho, 2001, Role of individual amino acids of apolipoprotein A-I in the activation of lecithin:cholesterol acyltransferase and in HDL rearrangements, J. Lipid Res., 42, 379, 10.1016/S0022-2275(20)31662-X · DOI
- Alexander, 2005, Apolipoprotein A-I helix 6 negatively charged residues attenuate lecithin-cholesterol acyltransferase (LCAT) reactivity, Biochemistry., 44, 5409, 10.1021/bi047412v · DOI
- Wu, 2007, The refined structure of nascent HDL reveals a key functional domain for particle maturation and dysfunction, Nat. Struct. Mol. Biol., 14, 861, 10.1038/nsmb1284 · DOI
- Borhani, 1997, Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation, Proc. Natl. Acad. Sci. USA., 94, 12291, 10.1073/pnas.94.23.12291 · DOI
- Jonas, 1990, Apolipoprotein A-I structure and lipid properties in homogeneous, reconstituted spherical and discoidal high density lipoproteins, J. Biol. Chem., 265, 22123, 10.1016/S0021-9258(18)45679-7 · DOI
- Segrest, 1999, A detailed molecular belt model for apolipoprotein A-I in discoidal high density lipoprotein, J. Biol. Chem., 274, 31755, 10.1074/jbc.274.45.31755 · DOI
- Panagotopulos, 2001, Apolipoprotein A-I adopts a belt-like orientation in reconstituted high density lipoproteins, J. Biol. Chem., 276, 42965, 10.1074/jbc.M106462200 · DOI
- Koppaka, 1999, The structure of human lipoprotein A-I. Evidence for the “belt” model, J. Biol. Chem., 274, 14541, 10.1074/jbc.274.21.14541 · DOI
- Segrest, 2000, Detailed molecular model of apolipoprotein A-I on the surface of high-density lipoproteins and its functional implications, Trends Cardiovasc. Med., 10, 246, 10.1016/S1050-1738(00)00078-5 · DOI
- Bhat, 2007, Conformational adaptation of apolipoprotein A-I to discretely sized phospholipid complexes, Biochemistry., 46, 7811, 10.1021/bi700384t · DOI
- Bhat, 2005, Intermolecular contact between globular N-terminal fold and C-terminal domain of ApoA-I stabilizes its lipid-bound conformation: studies employing chemical cross-linking and mass spectrometry, J. Biol. Chem., 280, 33015, 10.1074/jbc.M505081200 · DOI
- Wu, 2009, Double superhelix model of high density lipoprotein, J. Biol. Chem., 284, 36605, 10.1074/jbc.M109.039537 · DOI
- Bibow, 2017, Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I, Nat. Struct. Mol. Biol., 24, 187, 10.1038/nsmb.3345 · DOI
- Silva, 2005, A mass spectrometric determination of the conformation of dimeric apolipoprotein A-I in discoidal high density lipoproteins, Biochemistry., 44, 8600, 10.1021/bi050421z · DOI
- Silva, 2008, Structure of apolipoprotein A-I in spherical high density lipoproteins of different sizes, Proc. Natl. Acad. Sci. USA., 105, 12176, 10.1073/pnas.0803626105 · DOI
- Huang, 2011, Apolipoprotein A-I structural organization in high-density lipoproteins isolated from human plasma, Nat. Struct. Mol. Biol., 18, 416, 10.1038/nsmb.2028 · DOI
- Li, 2000, Structural determination of lipid-bound ApoA-I using fluorescence resonance energy transfer, J. Biol. Chem., 275, 37048, 10.1074/jbc.M005336200 · DOI
- Tubb, 2009, Purification of recombinant apolipoproteins A-I and A-IV and efficient affinity tag cleavage by tobacco etch virus protease, J. Lipid Res., 50, 1497, 10.1194/jlr.D900003-JLR200 · DOI
- Walker, 2014, The structure of human apolipoprotein A-IV as revealed by stable isotope-assisted cross-linking, molecular dynamics, and small angle x-ray scattering, J. Biol. Chem., 289, 5596, 10.1074/jbc.M113.541037 · DOI
- Bonomo, 1988, A rapid method for the synthesis of protein-lipid complexes using adsorption chromatography, J. Lipid Res., 29, 380, 10.1016/S0022-2275(20)38530-8 · DOI
- Lowry, 1951, Protein measurement with the Folin phenol reagent, J. Biol. Chem., 193, 265, 10.1016/S0021-9258(19)52451-6 · DOI
- Sreerama, 2000, Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set, Anal. Biochem., 287, 252, 10.1006/abio.2000.4880 · DOI
- Whitmore, 2004, DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data, Nucleic Acids Res., 32, W668, 10.1093/nar/gkh371 · DOI
- Smith, 2010, The role of hydrophobic and negatively charged surface patches of lipid-free apolipoprotein A-I in lipid binding and ABCA1-mediated cholesterol efflux, Biochim. Biophys. Acta., 1801, 64, 10.1016/j.bbalip.2009.09.012 · DOI
- Rousset, 2010, Effect of recombinant human lecithin cholesterol acyltransferase infusion on lipoprotein metabolism in mice, J. Pharmacol. Exp. Ther., 335, 140, 10.1124/jpet.110.169540 · DOI
- Leblond, 1991, The amphipathic alpha-helical repeats of apolipoprotein A-I are responsible for binding of high density lipoproteins to HepG2 cells, J. Biol. Chem., 266, 6058, 10.1016/S0021-9258(18)38083-9 · DOI
- Davidson, 2003, The spatial organization of apolipoprotein A-I on the edge of discoidal high density lipoprotein particles: a mass specrometry study, J. Biol. Chem., 278, 27199, 10.1074/jbc.M302764200 · DOI
- Melchior, 2016, An evaluation of the crystal structure of C-terminal truncated apolipoprotein A-I in solution reveals structural dynamics related to lipid binding, J. Biol. Chem., 291, 5439, 10.1074/jbc.M115.706093 · DOI
- Sorci-Thomas, 1993, Apolipoprotein A-I domains involved in lecithin-cholesterol acyltransferase activation. Structure:function relationships, J. Biol. Chem., 268, 21403, 10.1016/S0021-9258(19)36938-8 · DOI
- Oram, 2000, ABCA1 is the cAMP-inducible apolipoprotein receptor that mediates cholesterol secretion from macrophages, J. Biol. Chem., 275, 34508, 10.1074/jbc.M006738200 · DOI
- Jauhiainen, 1986, Human plasma lecithin-cholesterol acyltransferase. An elucidation of the catalytic mechanism, J. Biol. Chem., 261, 7032, 10.1016/S0021-9258(19)62718-3 · DOI · Paper page
- Verdery, 1981, Assay for lecithin: cholesterol acyltransferase, Methods Enzymol., 72, 375, 10.1016/S0076-6879(81)72027-5 · DOI
- Gu, 2016, A systematic investigation of structure/function requirements for the apolipoprotein A-I/lecithin cholesterol acyltransferase interaction loop of high-density lipoprotein, J. Biol. Chem., 291, 6386, 10.1074/jbc.M115.696088 · DOI
- Cavigiolio, 2010, Exchange of apolipoprotein A-I between lipid-associated and lipid-free states: a potential target for oxidative generation of dysfunctional high density lipoproteins, J. Biol. Chem., 285, 18847, 10.1074/jbc.M109.098434 · DOI
- Piper, 2015, The high-resolution crystal structure of human LCAT, J. Lipid Res., 56, 1711, 10.1194/jlr.M059873 · DOI
- Li, 2012, Rotational and hinge dynamics of discoidal high density lipoproteins probed by interchain disulfide bond formation, Biochim. Biophys. Acta., 1821, 481, 10.1016/j.bbalip.2011.10.013 · DOI
- Davidson, 1996, The role of apolipoprotein AI domains in lipid binding, Proc. Natl. Acad. Sci. USA., 93, 13605, 10.1073/pnas.93.24.13605 · DOI
- Gogonea, 2016, Structural insights into high density lipoprotein: old models and new facts, Front. Pharmacol., 6, 318, 10.3389/fphar.2015.00318 · DOI
- Banka, 1991, Localization of an apolipoprotein A-I epitope critical for activation of lecithin-cholesterol acyltransferase, J. Biol. Chem., 266, 23886, 10.1016/S0021-9258(18)54366-0 · DOI
- Spagnuolo, 2005, Assignment of the binding site for haptoglobin on apolipoprotein A-I, J. Biol. Chem., 280, 1193, 10.1074/jbc.M411390200 · DOI
- Gauthamadasa, 2012, Apolipoprotein A-II-mediated conformational changes of apolipoprotein A-I in discoidal high density lipoproteins, J. Biol. Chem., 287, 7615, 10.1074/jbc.M111.291070 · DOI
- Shao, 2005, Tyrosine 192 in apolipoprotein A-I is the major site of nitration and chlorination by myeloperoxidase, but only chlorination markedly impairs ABCA1-dependent cholesterol transport, J. Biol. Chem., 280, 5983, 10.1074/jbc.M411484200 · DOI
- Maiorano, 2000, The orientation of helix 4 in apolipoprotein A-I-containing reconstituted high density lipoproteins, J. Biol. Chem., 275, 17374, 10.1074/jbc.M000044200 · DOI
- Daniil, 2013, Effect of apoA-I mutations in the capacity of reconstituted HDL to promote ABCG1-mediated cholesterol efflux, PLoS One., 8, e67993, 10.1371/journal.pone.0067993 · DOI
- Chroni, 2004, Substitutions of glutamate 110 and 111 in the middle helix 4 of human apolipoprotein A-I (apoA-I) by alanine affect the structure and in vitro functions of apoA-I and induce severe hypertriglyceridemia in apoA-I-deficient mice, Biochemistry., 43, 10442, 10.1021/bi049782p · DOI
- Gonzalez, 2008, The central type Y amphipathic alpha-helices of apolipoprotein AI are involved in the mobilization of intracellular cholesterol depots, Arch. Biochem. Biophys., 473, 34, 10.1016/j.abb.2008.02.021 · DOI
- Bashtovyy, 2011, Sequence conservation of apolipoprotein A-I affords novel insights into HDL structure-function, J. Lipid Res., 52, 435, 10.1194/jlr.R012658 · DOI
- Kosek, 1999, Binding affinity and reactivity of lecithin cholesterol acyltransferase with native lipoproteins, Biochem. Biophys. Res. Commun., 258, 548, 10.1006/bbrc.1999.0690 · DOI
- Mei, 2011, Crystal structure of C-terminal truncated apolipoprotein A-I reveals the assembly of high density lipoprotein (HDL) by dimerization, J. Biol. Chem., 286, 38570, 10.1074/jbc.M111.260422 · DOI
- Emmanuel, 1994, Identification of specific amphipathic alpha-helical sequence of human apolipoprotein A-IV involved in lecithin:cholesterol acyltransferase activation, J. Biol. Chem., 269, 29883, 10.1016/S0021-9258(18)43963-4 · DOI
Cited by
Sorted by citations
Merrill, N. J., Davidson, W. S., He, Y., Díaz Ludovico, I., Sarkar, S., Berger, M. R., McDermott, J. E., Van Eldik, L. J., Wilcock, D. M., Monroe, M. E., et al. (2023) · Science Advances · doi:10.1126/sciadv.adi5571 · Cited by 27
Self-citationStrickland, M. R., & Holtzman, D. M. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-026-00970-0
Metadata
- Authors
- Cooke, A. L., Morris, J., Melchior, J. T., Street, S. E., Jerome, W. G., Huang, R., Herr, A. B., Smith, L. E., Segrest, J. P., Remaley, A. T., Shah, A. S., Thompson, T. B., & Davidson, W. S.
- Venue
- Journal of Lipid Research
- Publisher
- Elsevier BV
- Published
- 2018
- Volume
- 59
- Issue
- 7
- Pages
- 1244-1255
- ISSN
- 0022-2275
- Cited by
- 92
- References
- 1
- Language
- en
- Funders
- American Heart Association (15PRE25220021)
- National Institutes of Health (R01 HL127649, P01 HL12803, RR027015, CA68485, DK20593, DK58404, DK59637, EY08126)
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