CoChat
Sign Up
Cited by 94

The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.

Cholesterol as a key player in amyloid β-mediated toxicity in Alzheimer’s disease

Rudajev, Vladimir, Novotny, Jiri·2022·Frontiers in Molecular Neuroscience
DOI 10.3389/fnmol.2022.937056PMC PMC9453481
Open this paper in CoChat — free account

Abstract

Alzheimer’s disease (AD) is a neurodegenerative disorder that is one of the most devastating and widespread diseases worldwide, mainly affecting the aging population. One of the key factors contributing to AD-related neurotoxicity is the production and aggregation of amyloid β (Aβ). Many studies have shown the ability of Aβ to bind to the cell membrane and disrupt its structure, leading to cell death. Because amyloid damage affects different parts of the brain differently, it seems likely that not only Aβ but also the nature of the membrane interface with which the amyloid interacts, helps determine the final neurotoxic effect. Because cholesterol is the dominant component of the plasma membrane, it plays an important role in Aβ-induced toxicity. Elevated cholesterol levels and their regulation by statins have been shown to be important factors influencing the progression of neurodegeneration. However, data from many studies have shown that cholesterol has both neuroprotective and aggravating effects in relation to the development of AD. In this review, we attempt to summarize recent findings on the role of cholesterol in Aβ toxicity mediated by membrane binding in the pathogenesis of AD and to consider it in the broader context of the lipid composition of cell membranes.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3389/fnmol.2022.937056

Cites

30 of 30 references verified0 citation errors · 0 not checkable

Statistics

Figures

Figure 1 Amyloid β-membrane interactions. Amyloid β interacts with the plasma membrane in different ways, leading to disruption of cell homeostasis. Aβ exists in a disordered state (in the center) or can change its conformation to an α-helical or β-sheet containing form after contact with membrane lipids (especially cholesterol-rich lipid rafts), Aβ binds to the surface of the bilayer and destabilizes the membrane by a carpeting effect (1), or it may act as a detergent (2). In addition, the membrane may serve as a platform for aggregation of Aβ in its most harmful β-sheet-rich conformation (3). Under certain conditions, with or without the help of cholesterol, Aβ self-organizes into an α-helical (4) or β-barrel (5) transmembrane pore that is often selective for calcium ions. Changing cholesterol content and leaflet distribution may cause Aβ to transition from the surface-bound to the transmembrane form and vice-versa (not shown). Red—amyloid β, yellow—membrane lipids, purple—cholesterol. The scheme was prepared according to Eckert et al. (2001); Yip et al. (2002); D’Errico et al. (2008); Abramov et al. (2011); Zhao et al. (2011); Drolle et al. (2012); Yu and Zheng (2012); Fantini et al. (2014); Seghezza et al. (2014); Brown and Bevan (2016); Press-Sandler and Miller (2018); Staneva et al. (2018); Fabiani and Antollini (2019); Qu et al. (2019); and Banerjee et al. (2021).
Figure 1 Amyloid β-membrane interactions. Amyloid β interacts with the plasma membrane in different ways, leading to disruption of cell homeostasis. Aβ exists in a disordered state (in the center) or can change its conformation to an α-helical or β-sheet containing form after contact with membrane lipids (especially cholesterol-rich lipid rafts), Aβ binds to the surface of the bilayer and destabilizes the membrane by a carpeting effect (1), or it may act as a detergent (2). In addition, the membrane may serve as a platform for aggregation of Aβ in its most harmful β-sheet-rich conformation (3). Under certain conditions, with or without the help of cholesterol, Aβ self-organizes into an α-helical (4) or β-barrel (5) transmembrane pore that is often selective for calcium ions. Changing cholesterol content and leaflet distribution may cause Aβ to transition from the surface-bound to the transmembrane form and vice-versa (not shown). Red—amyloid β, yellow—membrane lipids, purple—cholesterol. The scheme was prepared according to Eckert et al. (2001); Yip et al. (2002); D’Errico et al. (2008); Abramov et al. (2011); Zhao et al. (2011); Drolle et al. (2012); Yu and Zheng (2012); Fantini et al. (2014); Seghezza et al. (2014); Brown and Bevan (2016); Press-Sandler and Miller (2018); Staneva et al. (2018); Fabiani and Antollini (2019); Qu et al. (2019); and Banerjee et al. (2021).CC BY · PubMed Central
Figure 2 Mechanisms of cholesterol-mediated protection against amyloid β toxicity. (A) Left: under cholesterol-deficient conditions, amyloid β (Aβ) penetrates the membrane and aggregates in calcium-selective pores, leading to calcium dyshomeostasis and cytotoxicity. Right: cholesterol-induced rigidization of the membrane prevents amyloid peptide from entering the bilayer. (B) Another mechanism designates cholesterol as a lipid that reduces the ability of Aβ to bind the membrane. (C) A cholesterol-rich membrane (which may also contain oxysterols) retains Aβ peptides in a transmembrane (TM), non-toxic form. At low cholesterol levels, Aβ can self-organize into toxic aggregates at the membrane surface. (D) Aβ forms calcium-selective TM channels when the bilayer has low cholesterol content, whereas high cholesterol concentration induces the formation of non-toxic, anion-selective pores. Red—amyloid β, yellow—membrane lipids, purple—cholesterol, pink—oxysterol, blue—calcium influx into the cytosol. The scheme was prepared according to Arispe and Doh (2002); Curtain et al. (2003); Micelli et al. (2004); Qiu et al. (2009); Qiu et al. (2011); Meleleo et al. (2013); Evangelisti et al. (2014); Phan et al. (2014); Phan et al. (2018); Bode et al. (2017); Fernandez-Perez et al. (2018); and Meleleo et al. (2019).
Figure 2 Mechanisms of cholesterol-mediated protection against amyloid β toxicity. (A) Left: under cholesterol-deficient conditions, amyloid β (Aβ) penetrates the membrane and aggregates in calcium-selective pores, leading to calcium dyshomeostasis and cytotoxicity. Right: cholesterol-induced rigidization of the membrane prevents amyloid peptide from entering the bilayer. (B) Another mechanism designates cholesterol as a lipid that reduces the ability of Aβ to bind the membrane. (C) A cholesterol-rich membrane (which may also contain oxysterols) retains Aβ peptides in a transmembrane (TM), non-toxic form. At low cholesterol levels, Aβ can self-organize into toxic aggregates at the membrane surface. (D) Aβ forms calcium-selective TM channels when the bilayer has low cholesterol content, whereas high cholesterol concentration induces the formation of non-toxic, anion-selective pores. Red—amyloid β, yellow—membrane lipids, purple—cholesterol, pink—oxysterol, blue—calcium influx into the cytosol. The scheme was prepared according to Arispe and Doh (2002); Curtain et al. (2003); Micelli et al. (2004); Qiu et al. (2009); Qiu et al. (2011); Meleleo et al. (2013); Evangelisti et al. (2014); Phan et al. (2014); Phan et al. (2018); Bode et al. (2017); Fernandez-Perez et al. (2018); and Meleleo et al. (2019).CC BY · PubMed Central
Figure 3 Cholesterol-dependent GM1 clustering and Aβ-membrane binding. Ganglioside GM1 was found to form membrane clusters in a cholesterol-dependent manner. Aggregated GM1 exists in a different spatial configuration that favors Aβ binding. With its -OH group, cholesterol forms a hydrogen bond with a sugar moiety of the polar group of the ganglioside, which positions it parallel to the membrane. When not bound to cholesterol, the polar head of the lipid is less able to interact with the amyloid peptide (dashed arrow). Red—amyloid β, yellow—membrane lipids, purple—cholesterol, blue—sugars in GM1 polar head, green—sialic acid. The scheme was prepared according to Yahi et al. (2010) and Matsuzaki (2014).
Figure 3 Cholesterol-dependent GM1 clustering and Aβ-membrane binding. Ganglioside GM1 was found to form membrane clusters in a cholesterol-dependent manner. Aggregated GM1 exists in a different spatial configuration that favors Aβ binding. With its -OH group, cholesterol forms a hydrogen bond with a sugar moiety of the polar group of the ganglioside, which positions it parallel to the membrane. When not bound to cholesterol, the polar head of the lipid is less able to interact with the amyloid peptide (dashed arrow). Red—amyloid β, yellow—membrane lipids, purple—cholesterol, blue—sugars in GM1 polar head, green—sialic acid. The scheme was prepared according to Yahi et al. (2010) and Matsuzaki (2014).CC BY · PubMed Central

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 30 references

Research works printed but not linked: 293

  1. Abe-Dohmae, 2021, ABCA7 links sterol metabolism to the host defense system: molecular background for potential management measure of Alzheimer’s disease, Gene, 768, 145316, 10.1016/j.gene.2020.145316 · DOI
  2. Abramov, 2011, Membrane cholesterol content plays a key role in the neurotoxicity of β-amyloid: implications for Alzheimer’s disease, Aging Cell, 10, 595, 10.1111/j.1474-9726.2011.00685.x · DOI
  3. Agarwal, 2020, Plasma lipids as biomarxers for Alzheimer’s disease: a systematic review, Cureus, 12, e12008, 10.7759/cureus.12008 · DOI
  4. Agrawal, 2020, The silence of the fats: a MAM’s story about Alzheimer, Neurobiol. Dis., 145, 105062, 10.1016/j.nbd.2020.105062 · DOI
  5. Ahyayauch, 2020, The binding of Aβ42 peptide monomers to sphingomyelin/cholesterol/ganglioside bilayers assayed by density gradient ultracentrifugation, Int. J. Mol. Sci., 21, 1674, 10.3390/ijms21051674 · DOI
  6. Ahyayauch, 2021, The interaction of Aβ42 peptide in monomer, oligomer or fibril forms with sphingomyelin/cholesterol/ganglioside bilayers, Int. J. Biol. Macromol., 168, 611, 10.1016/j.ijbiomac.2020.11.112 · DOI
  7. Amaro, 2016, GM1 ganglioside inhibits β-amyloid oligomerization induced by sphingomyelin, Angew. Chem. Int. Ed. Engl., 55, 9411, 10.1002/anie.201603178 · DOI
  8. Anderson, 2002, Cell biology - a role for lipid shells in targeting proteins to caveolae, rafts and other lipid domains, Science, 296, 1821, 10.1126/science.1068886 · DOI
  9. Angelova, 2017, α-synuclein and β-amyloid - different targets, same players: calcium, free radicals and mitochondria in the mechanism of neurodegeneration, Biochem. Biophys. Res. Commun., 483, 1110, 10.1016/j.bbrc.2016.07.103 · DOI
  10. Arbor, 2016, Amyloid-β Alzheimer targets - protein processing, lipid rafts and amyloid-β pores, Yale J. Biol. Med., 89, 5
  11. Area-Gomez, 2009, Presenilins are enriched in endoplasmic reticulum membranes associated with mitochondria, Am. J. Pathol., 175, 1810, 10.2353/ajpath.2009.090219 · DOI · Paper page
  12. Arispe, 2002, Plasma membrane cholesterol controls the cytotoxicity of Alzheimer’s disease AbetaP (1–40) and (1–42) peptides, FASEB J., 16, 1526, 10.1096/fj.02-0829com · DOI
  13. Ashley, 2006, Autoinsertion of soluble oligomers of Alzheimer’s Aβ(1–42) peptide into cholesterol-containing membranes is accompanied by relocation of the sterol towards the bilayer surface, BMC Struct. Biol., 6, 21, 10.1186/1472-6807-6-21 · DOI
  14. Audagnotto, 2018, Recruitment of the amyloid precursor protein by γ-secretase at the synaptic plasma membrane, Biochem. Biophys. Res. Commun., 498, 334, 10.1016/j.bbrc.2017.10.164 · DOI
  15. Avdulov, 1997, Lipid binding to amyloid β-peptide aggregates: preferential binding of cholesterol as compared with phosphatidylcholine and fatty acids, J. Neurochem., 69, 1746, 10.1046/j.1471-4159.1997.69041746.x · DOI
  16. Azouz, 2019, Membrane domain modulation of Aβ1-42 oligomer interactions with supported lipid bilayers: an atomic force microscopy investigation, Nanoscale, 11, 20857, 10.1039/c9nr06361g · DOI
  17. Baldwin, 2011, Metastability of native proteins and the phenomenon of amyloid formation, J. Am. Chem. Soc., 133, 14160, 10.1021/ja2017703 · DOI
  18. Banerjee, 2021, Cholesterol in membranes facilitates aggregation of amyloid β protein at physiologically relevant concentrations, ACS Chem. Neurosci., 12, 506, 10.1021/acschemneuro.0c00688 · DOI
  19. Barbero-Camps, 2013, APP/PS1 mice overexpressing SREBP-2 exhibit combined Aβ accumulation and tau pathology underlying Alzheimer’s disease, Hum. Mol. Gen., 22, 3460, 10.1093/hmg/ddt201 · DOI · Paper page
  20. Barrett, 2015, The position of Aβ22-40 and Aβ1-42 in anionic lipid membranes containing cholesterol, Membranes (Basel), 5, 824, 10.3390/membranes5040824 · DOI
  21. Barrett, 2012, The amyloid precursor protein has a flexible transmembrane domain and binds cholesterol, Science, 336, 1168, 10.1126/science.1219988 · DOI · Paper page
  22. Beel, 2010, Direct binding of cholesterol to the amyloid precursor protein: an important interaction in lipid-Alzheimer’s disease relationships?, Biochim. Biophys. Acta, 1801, 975, 10.1016/j.bbalip.2010.03.008 · DOI
  23. Belkouch, 2016, The pleiotropic effects of omega-3 docosahexaenoic acid on the hallmarks of Alzheimer’s disease, J. Nutr. Biochem, 38, 1, 10.1016/j.jnutbio.2016.03.002 · DOI
  24. Bennett, 2020, The association between midlife lipid levels and late-life brain amyloid deposition, Neurobiol. Aging, 92, 73, 10.1016/j.neurobiolaging.2020.03.015 · DOI
  25. Bera, 2019, Unravelling the role of amino acid sequence order in the assembly and function of the amyloid-β core, Chem. Commun. (Camb), 55, 8595, 10.1039/c9cc03654g · DOI
  26. Bode, 2017, Ion channel formation by amyloid-β42 oligomers but not amyloid-β40 in cellular membranes, J. Biol. Chem., 292, 1404, 10.1074/jbc.M116.762526 · DOI
  27. Bodovitz, 1996, Cholesterol modulates α-secretase cleavage of amyloid precursor protein, J. Biol. Chem., 271, 4436, 10.1074/jbc.271.8.4436 · DOI · Paper page
  28. Boisvert, 2018, The aging astrocyte transcriptome from multiple regions of the mouse brain, Cell Rep., 22, 269, 10.1016/j.celrep.2017.12.039 · DOI · Paper page
  29. Braak, 1997, Frequency of stages of Alzheimer-related lesions in different age categories, Neurobiol. Aging, 18, 351, 10.1016/s0197-4580(97)00056-0 · DOI · Paper page
  30. Brown, 1998, Sphingolipid organization in biomembranes: what physical studies of model membranes reveal, J. Cell Sci., 111, 1, 10.1242/jcs.111.1.1 · DOI
  31. Brown, 2016, Molecular dynamics simulations of amyloid β-peptide (1–42): tetramer formation and membrane interactions, Biophys. J., 111, 937, 10.1016/j.bpj.2016.08.001 · DOI
  32. Brown, 2017, Influence of sequence and lipid type on membrane perturbation by human and rat amyloid β-peptide (1–42), Arch. Biochem. Biophys., 614, 1, 10.1016/j.abb.2016.11.006 · DOI
  33. Bucciantini, 2014, Amyloid aggregation: role of biological membranes and the aggregate-membrane system, J. Phys. Chem. Lett., 5, 517, 10.1021/jz4024354 · DOI
  34. Burns, 2006, Cholesterol distribution, not total levels, correlate with altered amyloid precursor, protein processing in statin-treated mice, Neuromol. Med., 8, 319, 10.1385/nmm:8:3:319 · DOI
  35. Burns, 2003, Co-localization of cholesterol, apolipoprotein E and fibrillar Aβ in amyloid plaques, Brain Res. Mol. Brain Res., 110, 119, 10.1016/s0169-328x(02)00647-2 · DOI
  36. Carlsson, 2008, Effects of simvastatin on cerebrospinal fluid biomarkers and cognition in middle-aged adults at risk for Alzheimer’s disease, J. Alzheimers Dis., 13, 187, 10.3233/jad-2008-13209 · DOI
  37. Carrotta, 2021, Small angle X-ray scattering sensing membrane composition: the role of sphingolipids in membrane-amyloid β-peptide interaction, Biology (Basel), 11, 26, 10.3390/biology11010026 · DOI
  38. Cecchi, 2009, A protective role for lipid raft cholesterol against amyloid-induced membrane damage in human neuroblastoma cells, Biochim. Biophys. Acta, 1788, 2204, 10.1016/j.bbamem.2009.07.019 · DOI
  39. Cecchi, 2013, The amyloid-cell membrane system. The interplay between the biophysical features of oligomers/fibrils and cell membrane defines amyloid toxicity, Biophys. Chem., 182, 30, 10.1016/j.bpc.2013.06.003 · DOI
  40. Chang, 2017, Cellular cholesterol homeostasis and Alzheimer’s disease, J. Lipid Res., 58, 2239, 10.1194/jlr.R075630 · DOI · Paper page
  41. Chen, 2017, Amyloid β: structure, biology and structure-based therapeutic development, Acta Pharmacol. Sin., 38, 1205, 10.1038/aps.2017.28 · DOI · Paper page
  42. Cheng, 2013, Farnesyltransferase haplodeficiency reduces neuropathology and rescues cognitive function in a mouse model of Alzheimer disease, J. Biol. Chem., 288, 35952, 10.1074/jbc.M113.503904 · DOI
  43. Cheng, 2013, Specific changes of sulfatide levels in individuals with preclinical Alzheimer’s disease: an early event in disease pathogenesis, J. Neurochem., 127, 733, 10.1111/jnc.12368 · DOI
  44. Chew, 2020, Involvement of lipids in Alzheimer’s disease pathology and potential therapies, Front. Physiol., 11, 598, 10.3389/fphys.2020.00598 · DOI · Paper page
  45. Chochina, 2001, Amyloid β-peptide1-40 increases neuronal membrane fluidity: role of cholesterol and brain region, J. Lipid Res., 42, 1292, 10.1016/S0022-2275(20)31580-7 · DOI
  46. Choucair, 2007, Preferential accumulation of Aβ(1–42) on gel phase domains of lipid bilayers: an AFM and fluorescence study, Biochim. Biophys. Acta, 1768, 146, 10.1016/j.bbamem.2006.09.005 · DOI
  47. Chow, 2010, An overview of app processing enzymes and products, Neuromol. Med., 12, 1, 10.1007/s12017-009-8104-z · DOI · Paper page
  48. Chung, 2019, Variability in total cholesterol concentration is associated with the risk of dementia: a nationwide population-based cohort study, Front. Neurol., 10, 441, 10.3389/fneur.2019.00441 · DOI
  49. Chung, 2018, Endosomal-lysosomal cholesterol sequestration by U18666A differentially regulates amyloid precursor protein (APP) metabolism in normal and APP-overexpressing cells, Mol. Cell. Biol., 38, e00529, 10.1128/MCB.00529-17 · DOI
  50. Ciudad, 2020, Aβ1–42 tetramer and octamer structures reveal edge conductivity pores as a mechanism for membrane damage, Nat. Commun., 11, 3014, 10.1038/s41467-020-16566-1 · DOI
  51. Cossec, 2010, Clathrin-dependent APP endocytosis and Aβ secretion are highly sensitive to the level of plasma membrane cholesterol, Biochim. Biophys. Acta, 1801, 846, 10.1016/j.bbalip.2010.05.010 · DOI
  52. Cuco, 2016, Interaction of the Alzheimer Aβ(25–35) peptide segment with model membranes, Colloids Surf. B Biointerfaces, 141, 10, 10.1016/j.colsurfb.2016.01.015 · DOI
  53. Curtain, 2003, Metal ions, pH and cholesterol regulate the interactions of Alzheimer’s disease amyloid-β peptide with membrane lipid, J. Biol. Chem., 278, 2977, 10.1074/jbc.M205455200 · DOI
  54. Czuba, 2017, Cholesterol as a modifying agent of the neurovascular unit structure and function under physiological and pathological conditions, Metabol. Brain Dis., 32, 935, 10.1007/s11011-017-0015-3 · DOI
  55. Dai, 2020, Kinetic study of Aβ(1–42) amyloidosis in the presence of ganglioside-containing vesicles, Colloids Surf. B Biointerfaces, 185, 110615, 10.1016/j.colsurfb.2019.110615 · DOI
  56. Dai, 2021, Cholesterol metabolism in neurodegenerative diseases: molecular mechanisms and therapeutic targets, Mol. Neurobiol., 58, 2183, 10.1007/s12035-020-02232-6 · DOI
  57. Dante, 2006, Cholesterol inhibits the insertion of the Alzheimer’s peptide Aβ(25–35) in lipid bilayers, Eur. Biophys. J., 35, 523, 10.1007/s00249-006-0062-x · DOI
  58. Das, 2014, Three pools of plasma membrane cholesterol and their relation to cholesterol homeostasis, eLife, 3, e02882, 10.7554/eLife.02882 · DOI · Paper page
  59. de Oliveira, 2017, Longitudinal lipid profile variations and clinical change in Alzheimer’s disease dementia, Neurosci. Lett., 646, 36, 10.1016/j.neulet.2017.03.003 · DOI
  60. Decock, 2015, Analysis by a highly sensitive split luciferase assay of the regions involved in APP dimerization and its impact on processing, FEBS Open. Bio., 5, 763, 10.1016/j.fob.2015.09.002 · DOI
  61. DelBove, 2019, Reciprocal modulation between amyloid precursor protein and synaptic membrane cholesterol revealed by live cell imaging, Neurobiol. Dis., 127, 449, 10.1016/j.nbd.2019.03.009 · DOI
  62. D’Errico, 2008, Interaction between Alzheimer’s Aβ(25–35) peptide and phospholipid bilayers: the role of cholesterol, Biochim. Biophys. Acta, 1778, 2710, 10.1016/j.bbamem.2008.07.014 · DOI
  63. Devanathan, 2006, Effects of sphingomyelin, cholesterol and zinc ions on the binding, insertion and aggregation of the amyloid Aβ1-40 peptide in solid-supported lipid bilayers, FEBS J., 273, 1389, 10.1111/j.1742-4658.2006.05162.x · DOI
  64. Di Scala, 2014, Mechanism of cholesterol-assisted oligomeric channel formation by a short Alzheimer β-amyloid peptide, J. Neurochem., 128, 186, 10.1111/jnc.12390 · DOI
  65. Di Scala, 2016, Common molecular mechanism of amyloid pore formation by Alzheimer’s β-amyloid peptide and α-synuclein, Sci. Rep., 6, 28781, 10.1038/srep28781 · DOI
  66. Di Scala, 2013, Biochemical identification of a linear cholesterol-binding domain within Alzheimer’s β amyloid peptide, ACS Chem. Neurosci., 4, 509, 10.1021/cn300203a · DOI
  67. Diaz, 2018, “Lipid raft aging” in the human frontal cortex during nonpathological aging: gender influences and potential implications in Alzheimer’s disease, Neurobiol. Aging, 67, 42, 10.1016/j.neurobiolaging.2018.02.022 · DOI
  68. Diaz, 2015, Biophysical alterations in lipid rafts from human cerebral cortex associate with increased BACE1/AβPP interaction in early stages of Alzheimer’s disease, J. Alzheimers Dis., 43, 1185, 10.3233/JAD-141146 · DOI
  69. Dies, 2014, The interaction between amyloid-β peptides and anionic lipid membranes containing cholesterol and melatonin, PLoS One, 9, e99124, 10.1371/journal.pone.0099124 · DOI
  70. Dietschy, 2004, Thematic review series: brain lipids. Cholesterol metabolism in the central nervous system during early development and in the mature animal, J. Lipid Res., 45, 1375, 10.1194/jlr.R400004-JLR200 · DOI · Paper page
  71. Ding, 2012, β-amyloid (1–40) peptide interactions with supported phospholipid membranes: a single-molecule study, Biophys. J., 103, 1500, 10.1016/j.bpj.2012.08.051 · DOI
  72. Distl, 2001, Tangle-bearing neurons contain more free cholesterol than adjacent tangle-free neurons, Acta Neuropathol., 101, 547, 10.1007/s004010000314 · DOI
  73. Dong, 2017, Binding of protofibrillar Aβ trimers to lipid bilayer surface enhances Aβ structural stability and causes membrane thinning, Phys. Chem. Chem. Phys., 19, 27556, 10.1039/c7cp05959k · DOI
  74. Drolle, 2012, Nanoscale electrostatic domains in cholesterol-laden lipid membranes create a target for amyloid binding, Biophys. J., 103, L27, 10.1016/j.bpj.2012.06.053 · DOI
  75. Eckert, 2000, Cholesterol modulates the membrane-disordering effects of β-amyloid peptides in the hippocampus: specific changes in Alzheimer’s disease, Dement. Geriatr. Cogn. Disord., 11, 181, 10.1159/000017234 · DOI
  76. Eckert, 2001, Effects of aging and β-amyloid on the properties of brain synaptic and mitochondrial membranes, J. Neural Transm. (Vienna), 108, 1051, 10.1007/s007020170024 · DOI
  77. Egawa, 2016, Membrane lipid rafts and neurobiology: age-related changes in membrane lipids and loss of neuronal function, J. Physiol., 594, 4565, 10.1113/JP270590 · DOI
  78. Ehehalt, 2003, Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts, J. Cell Biol., 160, 113, 10.1083/jcb.200207113 · DOI · Paper page
  79. Elias, 2005, Serum cholesterol and cognitive performance in the Framingham heart study, Psychosom. Med., 67, 24, 10.1097/01.psy.0000151745.67285.c2 · DOI
  80. Emre, 2021, Age-related changes in brain phospholipids and bioactive lipids in the APP knock-in mouse model of Alzheimer’s disease, Acta Neuropathol. Commun., 9, 116, 10.1186/s40478-021-01216-4 · DOI
  81. Evangelisti, 2016, Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases, Sci. Rep., 6, 32721, 10.1038/srep32721 · DOI
  82. Evangelisti, 2014, Plasma membrane injury depends on bilayer lipid composition in Alzheimer’s disease, J. Alzheimers Dis., 41, 289, 10.3233/JAD-131406 · DOI
  83. Ewald, 2019, High speed atomic force microscopy to investigate the interactions between toxic Aβ1–42 peptides and model membranes in real time: impact of the membrane composition, Nanoscale, 11, 7229, 10.1039/c8nr08714h · DOI
  84. Fabelo, 2014, Altered lipid composition in cortical lipid rafts occurs at early stages of sporadic Alzheimer’s disease and facilitates APP/BACE1 interactions, Neurobiol. Aging, 35, 1801, 10.1016/j.neurobiolaging.2014.02.005 · DOI
  85. Fabelo, 2012, Evidence for premature lipid raft aging in APP/PS1 double-transgenic mice, a model of familial Alzheimer disease, J. Neuropathol. Exp. Neurol., 71, 868, 10.1097/NEN.0b013e31826be03c · DOI
  86. Fabiani, 2019, Alzheimer’s disease as a membrane disorder: spatial cross-talk among β-amyloid peptides, nicotinic acetylcholine receptors and lipid rafts, Front. Cell. Neurosci., 13, 309, 10.3389/fncel.2019.00309 · DOI
  87. Fantini, 2020, Progress toward Alzheimer’s disease treatment: leveraging the Achilles’ heel of Aβ oligomers?, Protein Sci., 29, 1748, 10.1002/pro.3906 · DOI
  88. Fantini, 2016, Molecular mechanisms of protein-cholesterol interactions in plasma membranes: functional distinction between topological (tilted) and consensus (CARC/CRAC) domains, Chem. Phys. Lipids, 199, 52, 10.1016/j.chemphyslip.2016.02.009 · DOI
  89. Fantini, 2014, Bexarotene blocks calcium-permeable ion channels formed by neurotoxic Alzheimer’s β-amyloid peptides, ACS Chem. Neurosci., 5, 216, 10.1021/cn400183w · DOI
  90. Fantini, 2010, Molecular insights into amyloid regulation by membrane cholesterol and sphingolipids: common mechanisms in neurodegenerative diseases, Exp. Rev. Mol. Med., 12, e27, 10.1017/S1462399410001602 · DOI
  91. Farooqui, 1997, Membrane phospholipid alterations in Alzheimer’s disease: deficiency of ethanolamine plasmalogens, Neurochem. Res., 22, 523, 10.1023/a:1027380331807 · DOI
  92. Fassbender, 2001, Simvastatin strongly reduces levels of Alzheimer’s disease β-amyloid peptides Aβ 42 and Aβ 40 in vitro and in vivo, Proc. Natl. Acad. Sci. U S A, 98, 5856, 10.1073/pnas.081620098 · DOI · Paper page
  93. Fernandez, 2009, Mitochondrial cholesterol loading exacerbates amyloid β peptide-induced inflammation and neurotoxicity, J. Neurosci., 29, 6394, 10.1523/JNEUROSCI.4909-08.2009 · DOI
  94. Fernandez-Perez, 2018, Effect of cholesterol on membrane fluidity and association of Aβ oligomers and subsequent neuronal damage: a double-edged sword, Front. Aging Neurosci., 10, 226, 10.3389/fnagi.2018.00226 · DOI
  95. Fitz, 2010, Liver X receptor agonist treatment ameliorates amyloid pathology and memory deficits caused by high-fat diet in APP23 mice, J. Neurosci., 30, 6862, 10.1523/JNEUROSCI.1051-10.2010 · DOI · Paper page
  96. Fraering, 2004, Purification and characterization of the human γ-secretase complex, Biochemistry, 43, 9774, 10.1021/bi0494976 · DOI
  97. Frank, 2008, Cholesterol depletion inhibits synaptic transmission and synaptic plasticity in rat hippocampus, Exp. Neurol., 212, 407, 10.1016/j.expneurol.2008.04.019 · DOI
  98. Frankel, 2020, Cholesterol-rich naked mole-rat brain lipid membranes are susceptible to amyloid β-induced damage in vitro, Aging (Albany NY), 12, 22266, 10.18632/aging.202138 · DOI
  99. Fukui, 2015, Effect of cholesterol reduction on receptor signaling in neurons, J. Biol. Chem., 290, 26383, 10.1074/jbc.M115.664367 · DOI
  100. Gao, 2020, Cholesterol modulates the formation of the Aβ ion channel in lipid bilayers, Biochemistry, 59, 992, 10.1021/acs.biochem.9b00968 · DOI
  101. Ghribi, 2006, High cholesterol content in neurons increases BACE, β-amyloid and phosphorylated tau levels in rabbit hippocampus, Exp. Neurol., 200, 460, 10.1016/j.expneurol.2006.03.019 · DOI · Paper page
  102. Grassi, 2020, Lipid rafts and neurodegeneration: structural and functional roles in physiologic aging and neurodegenerative diseases, J. Lipid Res., 61, 636, 10.1194/jlr.TR119000427 · DOI
  103. Green, 2006, Statin use and the risk of Alzheimer’s disease: the MIRAGE study, Alzheimers Dement., 2, 96, 10.1016/j.jalz.2006.02.003 · DOI
  104. Grouleff, 2015, The influence of cholesterol on membrane protein structure, function and dynamics studied by molecular dynamics simulations, Biochim. Biophys. Acta, 1848, 1783, 10.1016/j.bbamem.2015.03.029 · DOI
  105. Gylys, 2007, Increased cholesterol in Aβ-positive nerve terminals from Alzheimer’s disease cortex, Neurobiol. Aging, 28, 8, 10.1016/j.neurobiolaging.2005.10.018 · DOI
  106. Haag, 2009, Statins are associated with a reduced risk of Alzheimer disease regardless of lipophilicity. The Rotterdam study, J. Neurol. Neurosurg. Psych., 80, 13, 10.1136/jnnp.2008.150433 · DOI · Paper page
  107. Habchi, 2018, Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes, Nat. Chem., 10, 673, 10.1038/s41557-018-0031-x · DOI
  108. Harris, 2008, Cholesterol binding to amyloid-β fibrils: a TEM study, Micron, 39, 1192, 10.1016/j.micron.2008.05.001 · DOI
  109. Hashimoto, 2011, Docosahexaenoic acid withstands the Aβ25–35-induced neurotoxicity in SH-SY5Y cells, J. Nutr. Biochem., 22, 22, 10.1016/j.jnutbio.2009.11.005 · DOI
  110. Hayashi, 2002, Cholesterol is increased in the exofacial leaflet of synaptic plasma membranes of human apolipoprotein E4 knock-in mice, Neuroreport, 13, 383, 10.1097/00001756-200203250-00004 · DOI
  111. Henry, 2018, Interaction of Aβ1–42 peptide or their variant with model membrane of different composition probed by infrared nanospectroscopy, Nanoscale, 10, 936, 10.1039/c7nr07489a · DOI
  112. Hernandez, 2009, Tau phosphorylation by cdk5 and Fyn in response to amyloid peptide Aβ25–35: involvement of lipid rafts, J. Alzheimers Dis., 16, 149, 10.3233/JAD-2009-0933 · DOI · Paper page
  113. Heverin, 2004, Changes in the levels of cerebral and extracerebral sterols in the brain of patients with Alzheimer’s disease, J. Lipid Res., 45, 186, 10.1194/jlr.M300320-JLR200 · DOI
  114. Hicks, 2012, Lipid rafts and Alzheimer’s disease: protein-lipid interactions and perturbation of signaling, Front. Physiol., 3, 189, 10.3389/fphys.2012.00189 · DOI
  115. Hirai, 2018, Preferential intercalation of human amyloid-β peptide into interbilayer region of lipid-raft membrane in macromolecular crowding environment, J. Phys. Chem. B, 122, 9482, 10.1021/acs.jpcb.8b08006 · DOI
  116. Hirai, 2013, Change of dynamics of raft-model membrane induced by amyloid-β protein binding, Eur. Phys. J. E Soft Matter, 36, 74, 10.1140/epje/i2013-13074-3 · DOI
  117. Honeycutt, 1990, Metastability of the folded states of globular-proteins, Proc. Natl. Acad. Sci. U S A, 87, 3526, 10.1073/pnas.87.9.3526 · DOI
  118. Hooijmans, 2007, Changes in cerebral blood volume and amyloid pathology in aged Alzheimer APP/PS1 mice on a docosahexaenoic acid (DHA) diet or cholesterol enriched Typical Western Diet (TWD), Neurobiol. Dis., 28, 16, 10.1016/j.nbd.2007.06.007 · DOI
  119. Hu, 2015, Raman spectroscopy for detecting supported planar lipid bilayers composed of ganglioside-GM1/sphingomyelin/cholesterol in the presence of amyloid-β, Phys. Chem. Chem. Phys., 17, 22711, 10.1039/c5cp02366a · DOI
  120. Huang, 2019, DHA and vitamin E antagonized the Aβ25–35-mediated neuron oxidative damage through activation of Nrf2 signaling pathways and regulation of CD36, SRB1 and FABP5 expression in PC12 cells, Food Funct., 10, 1049, 10.1039/C8FO01713A · DOI
  121. Hussain, 2019, Role of cholesterol and sphingolipids in brain development and neurological diseases, Lipids Health Dis., 18, 26, 10.1186/s12944-019-0965-z · DOI
  122. Igbavboa, 1996, Increasing age alters transbilayer fluidity and cholesterol asymmetry in synaptic plasma membranes of mice, J. Neurochem., 66, 1717, 10.1046/j.1471-4159.1996.66041717.x · DOI
  123. Jamasbi, 2017, Phosphorylation of a full length amyloid-β peptide modulates its amyloid aggregation, cell binding and neurotoxic properties, Mol. Biosyst., 13, 1545, 10.1039/c7mb00249a · DOI
  124. Janickova, 2015, Lipid-based diets improve muscarinic neurotransmission in the hippocampus of transgenic APPswe/PS1dE9 Mice, Curr. Alzheimer Res., 12, 923, 10.2174/1567205012666151027130350 · DOI
  125. Jaya Prasanthi, 2008, Regulation of β-amyloid levels in the brain of cholesterol-fed rabbit, a model system for sporadic Alzheimer’s disease, Mech. Ageing Dev., 129, 649, 10.1016/j.mad.2008.09.002 · DOI
  126. Jeong, 2021, Protein farnesylation is upregulated in Alzheimer’s human brains and neuron-specific suppression of farnesyltransferase mitigates pathogenic processes in Alzheimer’s model mice, Acta Neuropathol. Commun., 9, 129, 10.1186/s40478-021-01231-5 · DOI
  127. Ji, 2002, Cholesterol is an important factor affecting the membrane insertion of β-amyloid peptide (Aβ1-40), which may potentially inhibit the fibril formation, J. Biol. Chem., 277, 6273, 10.1074/jbc.M104146200 · DOI
  128. Jick, 2000, Statins and the risk of dementia, Lancet, 356, 1627, 10.1016/s0140-6736(00)03155-x · DOI
  129. Jin, 2018, Alzheimer-like brain metabolic and structural features in cholesterol-fed rabbit detected by magnetic resonance imaging, Lipids Health Dis., 17, 61, 10.1186/s12944-018-0705-9 · DOI
  130. Julien, 2018, In vivo induction of membrane damage by β-amyloid peptide oligomers, Acta Neuropathol. Commun., 6, 131, 10.1186/s40478-018-0634-x · DOI
  131. Jurevics, 1995, Cholesterol for synthesis of myelin is made locally, not imported into brain, J. Neurochem., 64, 895, 10.1046/j.1471-4159.1995.64020895.x · DOI · Paper page
  132. Kakio, 2001, Cholesterol-dependent formation of GM1 ganglioside-bound amyloid β-protein, an endogenous seed for Alzheimer amyloid, J. Biol. Chem., 276, 24985, 10.1074/jbc.M100252200 · DOI
  133. Kakio, 2002, Interactions of amyloid β-protein with various gangliosides in raft-like membranes: importance of GM1 ganglioside-bound form as an endogenous seed for Alzheimer amyloid, Biochemistry, 41, 7385, 10.1021/bi0255874 · DOI
  134. Kalvodova, 2005, Lipids as modulators of proteolytic activity of BACE - involvement of cholesterol, glycosphingolipids and anionic phospholipids in vitro, J. Biol. Chem., 280, 36815, 10.1074/jbc.M504484200 · DOI
  135. Kandel, 2019, Structure of amyloid β25-35 in lipid environment and cholesterol-dependent membrane pore formation, Sci. Rep., 9, 2689, 10.1038/s41598-019-38749-7 · DOI
  136. Karimi, 2019, The interactions of an Aβ protofibril with a cholesterol-enriched membrane and involvement of neuroprotective carbazolium-based substances, Phys. Chem. Chem. Phys., 21, 11066, 10.1039/c9cp00859d · DOI
  137. Kawarabayashi, 2004, Dimeric amyloid β protein rapidly accumulates in lipid rafts followed by apolipoprotein E and phosphorylated tau accumulation in the Tg2576 mouse model of Alzheimer’s disease, J. Neurosci., 24, 3801, 10.1523/JNEUROSCI.5543-03.2004 · DOI · Paper page
  138. Kerr, 2017, Mitophagy and Alzheimer’s disease: cellular and molecular mechanisms, Trends Neurosci., 40, 151, 10.1016/j.tins.2017.01.002 · DOI · Paper page
  139. Kim, 2017, Integrated late onset alzheimer’s disease (LOAD) susceptibility genes: cholesterol metabolism and trafficking perspectives, Gene, 597, 10, 10.1016/j.gene.2016.10.022 · DOI
  140. Kim, 2016, Inhibition of cholesterol biosynthesis reduces γ-secretase activity and amyloid-β generation, J. Alzheimers Dis., 51, 1057, 10.3233/JAD-150982 · DOI
  141. Kim, 2006, Amyloid β oligomerization is induced by brain lipid rafts, J. Cell. Biochem., 99, 878, 10.1002/jcb.20978 · DOI
  142. Kirsch, 2002, Cholesterol attenuates the membrane perturbing properties of β-amyloid peptides, Amyloid, 9, 149, 10.3109/13506120209114816 · DOI
  143. Kirsch, 2003, Statin effects on cholesterol micro-domains in brain plasma membranes, Biochem. Pharmacol., 65, 843, 10.1016/s0006-2952(02)01654-4 · DOI
  144. Kivipelto, 2001, Midlife vascular risk factors and late-life mild cognitive impairment: a longitudinal, population-based study, Neurology, 56, 1683, 10.1212/wnl.56.12.1683 · DOI · Paper page
  145. Kojro, 2001, Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM 10, Proc. Natl. Acad. Sci. U S A, 98, 5815, 10.1073/pnas.081612998 · DOI · Paper page
  146. Kunkle, 2019, Genetic meta-analysis of diagnosed Alzheimer’s disease identifies new risk loci and implicates Aβ, tau, immunity and lipid processing, Nat. Genet., 51, 414, 10.1038/s41588-019-0358-2 · DOI · Paper page
  147. Kurinami, 2008, Prevention of amyloid ss-induced memory impairment by fluvastatin, associated with the decrease in amyloid ss accumulation and oxidative stress in amyloid ss injection mouse model, Int. J. Mol. Med., 21, 531
  148. Lazar, 2013, Time-of-flight secondary ion mass spectrometry (TOF-SIMS) imaging reveals cholesterol overload in the cerebral cortex of Alzheimer disease patients, Acta Neuropathol., 125, 133, 10.1007/s00401-012-1041-1 · DOI
  149. Ledesma, 2003, Raft disorganization leads to reduced plasmin activity in Alzheimer’s disease brains, EMBO Rep., 4, 1190, 10.1038/sj.embor.7400021 · DOI
  150. Ledesma, 2012, Lipid changes in the aged brain: effect on synaptic function and neuronal survival, Prog. Lipid Res., 51, 23, 10.1016/j.plipres.2011.11.004 · DOI
  151. Ledreux, 2016, Detrimental effects of a high fat/high cholesterol diet on memory and hippocampal markers in aged rats, Behav. Brain Res., 312, 294, 10.1016/j.bbr.2016.06.012 · DOI
  152. Lee, 2021, APOE4-carrying human astrocytes oversupply cholesterol to promote neuronal lipid raft expansion and Aβ generation, Stem Cell Rep., 16, 2128, 10.1016/j.stemcr.2021.07.017 · DOI · Paper page
  153. Lee, 2017, Amyloid β ion channels in a membrane comprising brain total lipid extracts, ACS Chem. Neurosci., 8, 1348, 10.1021/acschemneuro.7b00006 · DOI
  154. Lee, 1998, A detergent-insoluble membrane compartment contains Aβ in vivo, Nat. Med., 4, 730, 10.1038/nm0698-730 · DOI
  155. Leoni, 2006, Are the CSF levels of 24S-hydroxychole sterol a sensitive biomarker for mild cognitive impairment?, Neurosci. Lett., 397, 83, 10.1016/j.neulet.2005.11.046 · DOI
  156. Leoni, 2010, Links between ApoE, brain cholesterol metabolism, tau and amyloid β-peptide in patients with cognitive impairment, Biochem. Soc. Trans., 38, 1021, 10.1042/BST0381021 · DOI
  157. Liguori, 2013, Embedding Aβ42 in heterogeneous membranes depends on cholesterol asymmetries, Biophys. J., 105, 899, 10.1016/j.bpj.2013.06.046 · DOI
  158. Lin, 2008, Examining the levels of ganglioside and cholesterol in cell membrane on attenuation the cytotoxicity of β-amyloid peptide, Colloids Surf. B Biointerfaces, 65, 172, 10.1016/j.colsurfb.2008.03.012 · DOI
  159. Lin, 2015, Early statin use and the progression of Alzheimer disease a total population-based case-control study, Medicine (Baltimore), 94, e2143, 10.1097/MD.0000000000002143 · DOI
  160. Lin, 2002, Electrophysiologic properties of channels induced by Aβ25–35 in planar lipid bilayers, Peptides, 23, 1215, 10.1016/s0196-9781(02)00057-8 · DOI
  161. Lingwood, 2010, Lipid rafts as a membrane-organizing principle, Science, 327, 46, 10.1126/science.1174621 · DOI · Paper page
  162. Litvinov, 2018, Intracellular and plasma membrane events in cholesterol transport and homeostasis, J. Lipids, 2018, 3965054, 10.1155/2018/3965054 · DOI
  163. Liu, 2015, Quaternary structure defines a large class of amyloid-β oligomers neutralized by sequestration, Cell Rep., 11, 1760, 10.1016/j.celrep.2015.05.021 · DOI
  164. Liu, 2015, Characterization of the interactions between β-amyloid peptide and the membranes of human SK-N-SH cells, FEBS Lett., 589, 1929, 10.1016/j.febslet.2015.05.035 · DOI
  165. Loera-Valencia, 2019, Alterations in cholesterol metabolism as a risk factor for developing Alzheimer’s disease: potential novel targets for treatment, J. Steroid Biochem. Mol. Biol., 190, 104, 10.1016/j.jsbmb.2019.03.003 · DOI · Paper page
  166. Malchiodi-Albedi, 2010, Lipid raft disruption protects mature neurons against amyloid oligomer toxicity, Biochim. Biophys. Acta, 1802, 406, 10.1016/j.bbadis.2010.01.007 · DOI
  167. Mao, 2010, Surface-induced phase separation of a sphingomyelin/cholesterol/ganglioside GM1-planar bilayer on mica surfaces and microdomain molecular conformation that accelerates Aβ oligomerization, Biochim. Biophy. Acta, 1798, 1090, 10.1016/j.bbamem.2010.03.003 · DOI
  168. Marin, 2017, Anomalies occurring in lipid profiles and protein distribution in frontal cortex lipid rafts in dementia with Lewy bodies disclose neurochemical traits partially shared by Alzheimer’s and Parkinson’s diseases, Neurobiol. Aging, 49, 52, 10.1016/j.neurobiolaging.2016.08.027 · DOI
  169. Marquer, 2011, Local cholesterol increase triggers amyloid precursor protein-Bace1 clustering in lipid rafts and rapid endocytosis, FASEB J., 25, 1295, 10.1096/fj.10-168633 · DOI
  170. Marquer, 2014, Increasing membrane cholesterol of neurons in culture recapitulates Alzheimer’s disease early phenotypes, Mol. Neurodegener., 9, 60, 10.1186/1750-1326-9-60 · DOI
  171. Martin, 2010, Brain cholesterol in normal and pathological aging, Biochim. Biophys. Acta, 1801, 934, 10.1016/j.bbalip.2010.03.011 · DOI · Paper page
  172. Martín, 2010, Lipid alterations in lipid rafts from Alzheimer’s disease human brain cortex, J. Alzheimers Dis., 19, 489, 10.3233/JAD-2010-1242 · DOI
  173. Martin, 2011, Cyp46-mediated cholesterol loss promotes survival in stressed hippocampal neurons, Neurobiol. Aging, 32, 933, 10.1016/j.neurobiolaging.2009.04.022 · DOI
  174. Matsubara, 2017, Size and shape of amyloid fibrils induced by ganglioside nanoclusters: role of sialyl oligosaccharide in fibril formation, Langmuir, 33, 13874, 10.1021/acs.langmuir.7b02091 · DOI
  175. Matsubara, 2018, Amyloid- fibrils assembled on ganglioside-enriched membranes contain both parallel -sheets and turns, J. Biol. Chem., 293, 14146, 10.1074/jbc.RA118.002787 · DOI
  176. Matsuzaki, 2011, Formation of toxic amyloid fibrils by amyloid beta-protein on ganglioside clusters, Int. J. Alzheimers Dis., 2011, 956104, 10.4061/2011/956104 · DOI
  177. Matsuzaki, 2014, How do membranes initiate Alzheimer’s disease? Formation of toxic arnyloid fibrils by the amyloid β-protein on ganglioside clusters, Acc. Chem. Res., 47, 2397, 10.1021/ar500127z · DOI
  178. Matsuzaki, 1999, Interactions of amyloid β-peptide (1–40) with ganglioside-containing membranes, Biochemistry, 38, 4137, 10.1021/bi982345o · DOI
  179. Maxfield, 2002, Intracellular cholesterol transport, J. Clin. Invest., 110, 891, 10.1172/JCI16500 · DOI
  180. McFarlane, 2020, Cholesterol and dementia: a long and complicated relationship, Curr. Aging Sci., 13, 42, 10.2174/1874609812666190917155400 · DOI
  181. Meleleo, 2013, AβP1–42 incorporation and channel formation in planar lipid membranes: the role of cholesterol and its oxidation products, J. Bioenerg. Biomembr., 45, 369, 10.1007/s10863-013-9513-0 · DOI
  182. Meleleo, 2019, Concentration-dependent effects of mercury and lead on A42: possible implications for Alzheimer’s disease, Eur. Biophys. J., 48, 173, 10.1007/s00249-018-1344-9 · DOI
  183. Micelli, 2004, Effect of sterols on β-amyloid peptide (AβP 1-40) channel formation and their properties in planar lipid membranes, Biophys. J., 86, 2231, 10.1016/S0006-3495(04)74281-2 · DOI
  184. Mizuno, 1999, Cholesterol-dependent generation of a seeding amyloid β-protein in cell culture, J. Biol. Chem., 274, 15110, 10.1074/jbc.274.21.15110 · DOI
  185. Mohamed, 2018, Aβ inhibits SREBP-2 activation through Akt inhibition, J. Lipid Res., 59, 1, 10.1194/jlr.M076703 · DOI
  186. Molander-Melin, 2005, Structural membrane alterations in Alzheimer brains found to be associated with regional disease development; increased density of gangliosides GM1 and GM2 and loss of cholesterol in detergent-resistant membrane domains, J. Neurochem., 92, 171, 10.1111/j.1471-4159.2004.02849.x · DOI
  187. Montesinos, 2020, The Alzheimer’s disease-associated C99 fragment of APP regulates cellular cholesterol trafficking, EMBO J., 39, e103791, 10.15252/embj.2019103791 · DOI
  188. Mori, 2012, Formation of GM1 ganglioside clusters on the lipid membrane containing sphingomyeline and cholesterol, J. Phys. Chem. B, 116, 5111, 10.1021/jp207881k · DOI
  189. Narayan, 2014, Rare individual amyloid-β oligomers act on astrocytes to initiate neuronal damage, Biochemistry, 53, 2442, 10.1021/bi401606f · DOI
  190. Naudi, 2015, Lipidomics of human brain aging and Alzheimer’s disease pathology, Int. Rev. Neurobiol., 122, 133, 10.1016/bs.irn.2015.05.008 · DOI
  191. Nicastro, 2016, Amyloid β-peptide insertion in liposomes containing GM1-cholesterol domains, Biophys. Chem., 208, 9, 10.1016/j.bpc.2015.07.010 · DOI
  192. Nicholson, 2009, Increased membrane cholesterol might render mature hippocampal neurons more susceptible to β-amyloid-induced calpain activation and tau toxicity, J. Neurosci., 29, 4640, 10.1523/JNEUROSCI.0862-09.2009 · DOI
  193. Nierzwicki, 2021, Role of cholesterol in substrate recognition by γ-secretase, Sci. Rep., 11, 15213, 10.1038/s41598-021-94618-2 · DOI
  194. Nilsson, 2021, Association of a total cholesterol polygenic score with cholesterol levels and pathological biomarkers across the Alzheimer’s disease spectrum, Genes (Basel), 12, 1805, 10.3390/genes12111805 · DOI
  195. Oikawa, 2014, Influence of APOE genotype and the presence of Alzheimer’s pathology on synaptic membrane lipids of human brains, J. Neurosci. Res., 92, 641, 10.1002/jnr.23341 · DOI
  196. Okada, 2008, Formation of toxic Aβ(1-40) fibrils on GM1 ganglioside-containing membranes mimicking lipid rafts: polymorphisms in Aβ(1–40) fibrils, J. Mol. Biol., 382, 1066, 10.1016/j.jmb.2008.07.072 · DOI
  197. Oksman, 2006, Impact of different saturated fatty acid, polyunsaturated fatty acid and cholesterol containing diets on β-amyloid accumulation in APP/PS1 transgenic mice, Neurobiol. Dis., 23, 563, 10.1016/j.nbd.2006.04.013 · DOI
  198. Oku, 2017, Synthesized Aβ42 caused intracellular oxidative damage, leading to cell death, via lysosome rupture, Cell Struct. Funct., 42, 71, 10.1247/csf.17006 · DOI
  199. Ong, 2010, Changes in brain cholesterol metabolome after excitotoxicity, Mol. Neurobiol., 41, 299, 10.1007/s12035-010-8099-3 · DOI
  200. Osenkowski, 2008, Direct and potent regulation of γ-secretase by its lipid microenvironment, J. Biol. Chem., 283, 22529, 10.1074/jbc.M801925200 · DOI

200 of 293 shown

Cited by

Sorted by citations

Metadata

Authors
Rudajev, V., & Novotny, J.
Venue
Frontiers in Molecular Neuroscience
Publisher
Frontiers Media SA
Published
2022-08-25
Volume
15
ISSN
1662-5099
DOI
10.3389/fnmol.2022.937056
PMC
PMC9453481
Cited by
94
References
30
Licence
creativecommons.org/licenses/by/4.0/ (vor)
Funders
Přírodovědecká Fakulta, Univerzita Karlova

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review