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Role of Microglia in Regulating Cholesterol and Tau Pathology in Alzheimer’s Disease

Nanjundaiah, Shwetha, Chidambaram, Hariharakrishnan, Chandrashekar, Madhura, Chinnathambi, Subashchandrabose·2021·Cellular and Molecular Neurobiology
DOI 10.1007/s10571-020-00883-6
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  1. Abraha A, Ghoshal N, Gamblin TC et al (2000) C-terminal inhibition of tau assembly in vitro and in Alzheimer’s disease. J Cell Sci 113(Pt 21):3737–3745 · DOI
  2. del Alonso AC, Mederlyova A, Novak M et al (2004) Promotion of hyperphosphorylation by frontotemporal dementia tau mutations. J Biol Chem 279:34873–34881. https://doi.org/10.1074/jbc.M405131200 · DOI
  3. Alonso AC, Zaidi T, Grundke-Iqbal I, Iqbal K (1994) Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease. Proc Natl Acad Sci USA 91:5562–5566 · DOI · Paper page
  4. Andersen OM, Reiche J, Schmidt V et al (2005) Neuronal sorting protein-related receptor sorLA/LR11 regulates processing of the amyloid precursor protein. Proc Natl Acad Sci USA 102:13461–13466. https://doi.org/10.1073/pnas.0503689102 · DOI · Paper page
  5. Andersson M, Elmberger PG, Edlund C et al (1990) Rates of cholesterol, ubiquinone, dolichol and dolichyl-P biosynthesis in rat brain slices. FEBS Lett 269:15–18 · DOI
  6. Arendt T, Stieler JT, Holzer M (2016) Tau and tauopathies. Brain Res Bull 126:238–292. https://doi.org/10.1016/j.brainresbull.2016.08.018 · DOI · Paper page
  7. Ashford JW (2004) APOE genotype effects on Alzheimer’s disease onset and epidemiology. J Mol Neurosci 23:157–165. https://doi.org/10.1385/JMN:23:3:157 · DOI
  8. Bae SH, Lee JN, Fitzky BU et al (1999) Cholesterol biosynthesis from lanosterol. Molecular cloning, tissue distribution, expression, chromosomal localization, and regulation of rat 7-dehydrocholesterol reductase, a Smith-Lemli-Opitz syndrome-related protein. J Biol Chem 274:14624–14631 · DOI
  9. Baranowski M (2008) Biological role of liver X receptors. J Physiol Pharmacol 59(Suppl 7):31–55
  10. Björkhem I, Heverin M, Leoni V et al (2006) Oxysterols and Alzheimer’s disease. Acta Neurol Scand Suppl 185:43–49. https://doi.org/10.1111/j.1600-0404.2006.00684.x · DOI
  11. Björkhem I, Meaney S (2004) Brain cholesterol: long secret life behind a barrier. Arterioscler Thromb Vasc Biol 24:806–815. https://doi.org/10.1161/01.ATV.0000120374.59826.1b · DOI · Paper page
  12. Bolós M, Llorens-Martín M, Jurado-Arjona J et al (2016) Direct evidence of internalization of Tau by microglia in vitro and in vivo. J Alzheimers Dis 50:77–87. https://doi.org/10.3233/JAD-150704 · DOI · Paper page
  13. Bolós M, Pallas-Bazarra N, Terreros-Roncal J et al (2017b) Soluble Tau has devastating effects on the structural plasticity of hippocampal granule neurons. Transl Psychiatry 7:1267. https://doi.org/10.1038/s41398-017-0013-6 · DOI
  14. Bryleva EY, Rogers MA, Chang CCY et al (2010) ACAT1 gene ablation increases 24(S)-hydroxycholesterol content in the brain and ameliorates amyloid pathology in mice with AD. Proc Natl Acad Sci USA 107:3081–3086. https://doi.org/10.1073/pnas.0913828107 · DOI · Paper page
  15. Busche MA, Wegmann S, Dujardin S et al (2019) Tau impairs neural circuits, dominating amyloid-β effects, in Alzheimer models in vivo. Nat Neurosci. https://doi.org/10.1038/s41593-018-0289-8 · DOI · Paper page
  16. Calafate S, Flavin W, Verstreken P, Moechars D (2016) Loss of Bin1 promotes the propagation of Tau pathology. Cell Rep 17:931–940. https://doi.org/10.1016/j.celrep.2016.09.063 · DOI · Paper page
  17. Capsoni S, Carlo A-S, Vignone D et al (2013) SorLA deficiency dissects amyloid pathology from tau and cholinergic neurodegeneration in a mouse model of Alzheimer’s disease. J Alzheimers Dis 33:357–371. https://doi.org/10.3233/JAD-2012-121399 · DOI
  18. Carbajosa G, Malki K, Lawless N et al (2018) Loss of Trem2 in microglia leads to widespread disruption of cell coexpression networks in mouse brain. Neurobiol Aging 69:151–166. https://doi.org/10.1016/j.neurobiolaging.2018.04.019 · DOI
  19. Carstea ED, Morris JA, Coleman KG et al (1997) Niemann-Pick C1 disease gene: homology to mediators of cholesterol homeostasis. Science 277:228–231 · DOI · Paper page
  20. Chapuis J, Hansmannel F, Gistelinck M et al (2013) Increased expression of BIN1 mediates Alzheimer genetic risk by modulating tau pathology. Mol Psychiatry 18:1225–1234. https://doi.org/10.1038/mp.2013.1 · DOI · Paper page
  21. Colonna M, Butovsky O (2017) Microglia function in the central nervous system during health and neurodegeneration. Annu Rev Immunol 35:441–468. https://doi.org/10.1146/annurev-immunol-051116-052358 · DOI · Paper page
  22. Corder EH, Saunders AM, Strittmatter WJ et al (1993) Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer’s disease in late onset families. Science 261:921–923 · DOI · Paper page
  23. Couerbe JP (1984) Du cerveau, considéré sous le point du vue chimique et physiologique. Ann Chim Phys 56:160–193
  24. Cummings JL (2004) Alzheimer’s disease. N Engl J Med 351:56–67. https://doi.org/10.1056/NEJMra040223 · DOI · Paper page
  25. Das R, Balmik AA, Chinnathambi S (2020) Phagocytosis of full-length Tau oligomers by Actin-remodeling of activated microglia. J Neuroinflamm 17:10. https://doi.org/10.1186/s12974-019-1694-y · DOI
  26. de Chaves EI, Rusiñol AE, Vance DE et al (1997) Role of lipoproteins in the delivery of lipids to axons during axonal regeneration. J Biol Chem 272:30766–30773 · DOI
  27. Deane R, Wu Z, Sagare A et al (2004) LRP/amyloid beta-peptide interaction mediates differential brain efflux of Abeta isoforms. Neuron 43:333–344. https://doi.org/10.1016/j.neuron.2004.07.017 · DOI · Paper page
  28. Dedieu S, Langlois B (2008) LRP-1: a new modulator of cytoskeleton dynamics and adhesive complex turnover in cancer cells. Cell Adh Migr 2:77–80 · DOI
  29. DeGrella RF, Simoni RD (1982) Intracellular transport of cholesterol to the plasma membrane. J Biol Chem 257:14256–14262 · DOI
  30. Dietschy JM, Turley SD (2001) Cholesterol metabolism in the brain. Curr Opin Lipidol 12:105–112 · DOI · Paper page
  31. Dietschy JM, Turley SD (2004) Thematic review series: brain Lipids. Cholesterol metabolism in the central nervous system during early development and in the mature animal. J Lipid Res 45:1375–1397. https://doi.org/10.1194/jlr.R400004-JLR200 · DOI · Paper page
  32. Eberlé D, Hegarty B, Bossard P et al (2004) SREBP transcription factors: master regulators of lipid homeostasis. Biochimie 86:839–848. https://doi.org/10.1016/j.biochi.2004.09.018 · DOI
  33. Elali A, Rivest S (2013) The role of ABCB1 and ABCA1 in beta-amyloid clearance at the neurovascular unit in Alzheimer’s disease. Front Physiol 4:45. https://doi.org/10.3389/fphys.2013.00045 · DOI
  34. Ellis JD, Barrios-Rodiles M, Colak R et al (2012) Tissue-specific alternative splicing remodels protein-protein interaction networks. Mol Cell 46:884–892. https://doi.org/10.1016/j.molcel.2012.05.037 · DOI · Paper page
  35. Fan Q-W, Yu W, Senda T et al (2001) Cholesterol-dependent modulation of tau phosphorylation in cultured neurons. J Neurochem 76:391–400. https://doi.org/10.1046/j.1471-4159.2001.00063.x · DOI
  36. Fester L, Zhou L, Bütow A et al (2009) Cholesterol-promoted synaptogenesis requires the conversion of cholesterol to estradiol in the hippocampus. Hippocampus 19:692–705. https://doi.org/10.1002/hipo.20548 · DOI
  37. Fjorback AW, Seaman M, Gustafsen C et al (2012) Retromer binds the FANSHY sorting motif in SorLA to regulate amyloid precursor protein sorting and processing. J Neurosci 32:1467–1480. https://doi.org/10.1523/JNEUROSCI.2272-11.2012 · DOI · Paper page
  38. Gabbi C, Warner M, Gustafsson J-Å (2014) Action mechanisms of Liver X Receptors. Biochem Biophys Res Commun 446:647–650. https://doi.org/10.1016/j.bbrc.2013.11.077 · DOI
  39. Gamba P, Testa G, Gargiulo S et al (2015) Oxidized cholesterol as the driving force behind the development of Alzheimer’s disease. Front Aging Neurosci. https://doi.org/10.3389/fnagi.2015.00119 · DOI · Paper page
  40. Gaylor JL (2002) Membrane-bound enzymes of cholesterol synthesis from lanosterol. Biochem Biophys Res Commun 292:1139–1146. https://doi.org/10.1006/bbrc.2001.2008 · DOI
  41. Glöckner F, Ohm TG (2014) Tau pathology induces intraneuronal cholesterol accumulation. J Neuropathol Exp Neurol 73:846–854. https://doi.org/10.1097/NEN.0000000000000103 · DOI
  42. Goedert M, Spillantini MG (2011) Pathogenesis of the tauopathies. J Mol Neurosci 45:425–431. https://doi.org/10.1007/s12031-011-9593-4 · DOI
  43. Gong C-X, Iqbal K (2008) Hyperphosphorylation of microtubule-associated protein tau: a promising therapeutic target for Alzheimer disease. Curr Med Chem 15:2321–2328 · DOI
  44. Gong C-X, Liu F, Grundke-Iqbal I, Iqbal K (2006) Impaired brain glucose metabolism leads to Alzheimer neurofibrillary degeneration through a decrease in tau O-GlcNAcylation. J Alzheimers Dis 9:1–12 · DOI
  45. Gosselet F, Candela P, Sevin E et al (2009) Transcriptional profiles of receptors and transporters involved in brain cholesterol homeostasis at the blood-brain barrier: use of an in vitro model. Brain Res 1249:34–42. https://doi.org/10.1016/j.brainres.2008.10.036 · DOI
  46. Guerreiro R, Wojtas A, Bras J et al (2013a) TREM2 variants in Alzheimer’s disease. N Engl J Med 368:117–127. https://doi.org/10.1056/NEJMoa1211851 · DOI · Paper page
  47. Guerreiro R, Wojtas A, Bras J et al (2013b) TREM2 variants in Alzheimer’s disease. N Engl J Med 368:117–127. https://doi.org/10.1056/NEJMoa1211851 · DOI · Paper page
  48. Haase C, Stieler JT, Arendt T, Holzer M (2004) Pseudophosphorylation of tau protein alters its ability for self-aggregation. J Neurochem 88:1509–1520 · DOI
  49. Heino S, Lusa S, Somerharju P et al (2000) Dissecting the role of the golgi complex and lipid rafts in biosynthetic transport of cholesterol to the cell surface. Proc Natl Acad Sci USA 97:8375–8380. https://doi.org/10.1073/pnas.140218797 · DOI
  50. Heneka MT, Golenbock DT, Latz E (2015) Innate immunity in Alzheimer’s disease. Nat Immunol 16:229–236. https://doi.org/10.1038/ni.3102 · DOI · Paper page
  51. Heneka MT, Kummer MP, Stutz A et al (2013) NLRP3 is activated in Alzheimer’s disease and contributes to pathology in APP/PS1 mice. Nature 493:674–678. https://doi.org/10.1038/nature11729 · DOI · Paper page
  52. Ho L, Qin W, Pompl PN et al (2004) Diet-induced insulin resistance promotes amyloidosis in a transgenic mouse model of Alzheimer’s disease. FASEB J 18:902–904. https://doi.org/10.1096/fj.03-0978fje · DOI
  53. Holler CJ, Davis PR, Beckett TL et al (2014) Bridging integrator 1 (BIN1) protein expression increases in the Alzheimer’s disease brain and correlates with neurofibrillary tangle pathology. J Alzheimers Dis 42:1221–1227. https://doi.org/10.3233/JAD-132450 · DOI · Paper page
  54. Hollingworth P, Harold D, Sims R et al (2011) Common variants at ABCA7, MS4A6A/MS4A4E, EPHA1, CD33 and CD2AP are associated with Alzheimer’s disease. Nat Genet 43:429–435. https://doi.org/10.1038/ng.803 · DOI · Paper page
  55. Hooper C, Killick R, Lovestone S (2008) The GSK3 hypothesis of Alzheimer’s disease. J Neurochem 104:1433–1439. https://doi.org/10.1111/j.1471-4159.2007.05194.x · DOI · Paper page
  56. Hoyer S (2004) Causes and consequences of disturbances of cerebral glucose metabolism in sporadic Alzheimer disease: therapeutic implications. Adv Exp Med Biol 541:135–152 · DOI
  57. Hu W, Zhang X, Tung YC et al (2016) Hyperphosphorylation determines both the spread and the morphology of tau pathology. Alzheimers Dement 12:1066–1077. https://doi.org/10.1016/j.jalz.2016.01.014 · DOI
  58. Hutter-Paier B, Huttunen HJ, Puglielli L et al (2004) The ACAT inhibitor CP-113,818 markedly reduces amyloid pathology in a mouse model of Alzheimer’s disease. Neuron 44:227–238. https://doi.org/10.1016/j.neuron.2004.08.043 · DOI · Paper page
  59. Iliff JJ, Nedergaard M (2013) Is there a cerebral lymphatic system? Stroke 44:S93–S95. https://doi.org/10.1161/STROKEAHA.112.678698 · DOI
  60. Iliff JJ, Wang M, Liao Y et al (2012) A paravascular pathway facilitates CSF flow through the brain parenchyma and the clearance of interstitial solutes, including amyloid β. Sci Transl Med 4:147ra111. https://doi.org/10.1126/scitranslmed.3003748 · DOI · Paper page
  61. Iqbal K, Del C, Alonso A, Chen S et al (2005b) Tau pathology in Alzheimer disease and other tauopathies. Biochim Biophys Acta 1739:198–210. https://doi.org/10.1016/j.bbadis.2004.09.008 · DOI · Paper page
  62. Iqbal K, Liu F, Gong C-X et al (2009) Mechanisms of tau-induced neurodegeneration. Acta Neuropathol 118:53–69. https://doi.org/10.1007/s00401-009-0486-3 · DOI · Paper page
  63. Jay TR, von Saucken VE, Landreth GE (2017) TREM2 in neurodegenerative diseases. Mol Neurodegener 12:56. https://doi.org/10.1186/s13024-017-0197-5 · DOI · Paper page
  64. Johnson GV, Hartigan JA (1999) Tau protein in normal and Alzheimer’s disease brain: an update. J Alzheimers Dis 1:329–351 · DOI
  65. Jolivalt CG, Lee CA, Beiswenger KK et al (2008) Defective insulin signaling pathway and increased glycogen synthase kinase-3 activity in the brain of diabetic mice: parallels with Alzheimer’s disease and correction by insulin. J Neurosci Res 86:3265–3274. https://doi.org/10.1002/jnr.21787 · DOI
  66. Jonsson T, Stefansson H, Steinberg S et al (2013) Variant of TREM2 associated with the risk of Alzheimer’s disease. N Engl J Med 368:107–116. https://doi.org/10.1056/NEJMoa1211103 · DOI · Paper page
  67. Kajiho H, Sakurai K, Minoda T et al (2011) Characterization of RIN3 as a guanine nucleotide exchange factor for the Rab5 subfamily GTPase Rab31. J Biol Chem 286:24364–24373. https://doi.org/10.1074/jbc.M110.172445 · DOI
  68. Kallen CB, Billheimer JT, Summers SA et al (1998) Steroidogenic Acute Regulatory Protein (StAR) is a sterol transfer protein. J Biol Chem 273:26285–26288. https://doi.org/10.1074/jbc.273.41.26285 · DOI
  69. Kang J, Rivest S (2012) Lipid metabolism and neuroinflammation in Alzheimer’s disease: a role for liver X receptors. Endocr Rev 33:715–746. https://doi.org/10.1210/er.2011-1049 · DOI · Paper page
  70. Kaplan MR, Simoni RD (1985) Transport of cholesterol from the endoplasmic reticulum to the plasma membrane. J Cell Biol 101:446–453 · DOI
  71. Karch CM, Cruchaga C, Goate AM (2014) Alzheimer’s disease genetics: from the bench to the clinic. Neuron 83:11–26. https://doi.org/10.1016/j.neuron.2014.05.041 · DOI · Paper page
  72. Karch CM, Goate AM (2015) Alzheimer’s disease risk genes and mechanisms of disease pathogenesis. Biol Psychiatry 77:43–51. https://doi.org/10.1016/j.biopsych.2014.05.006 · DOI · Paper page
  73. Karten B, Campenot RB, Vance DE, Vance JE (2006) Expression of ABCG1, but not ABCA1, correlates with cholesterol release by cerebellar astroglia. J Biol Chem 281:4049–4057. https://doi.org/10.1074/jbc.M508915200 · DOI · Paper page
  74. Ke YD, Delerue F, Gladbach A et al (2009) Experimental diabetes mellitus exacerbates tau pathology in a transgenic mouse model of Alzheimer’s disease. PLoS ONE 4:e7917. https://doi.org/10.1371/journal.pone.0007917 · DOI
  75. Khatoon S, Grundke-Iqbal I, Iqbal K (1992) Brain levels of microtubule-associated protein tau are elevated in Alzheimer’s disease: a radioimmuno-slot-blot assay for nanograms of the protein. J Neurochem 59:750–753 · DOI
  76. Kim K-W, Vallon-Eberhard A, Zigmond E et al (2011) In vivo structure/function and expression analysis of the CX3C chemokine fractalkine. Blood 118:e156–e167. https://doi.org/10.1182/blood-2011-04-348946 · DOI
  77. Kim WS, Weickert CS, Garner B (2008) Role of ATP-binding cassette transporters in brain lipid transport and neurological disease. J Neurochem 104:1145–1166. https://doi.org/10.1111/j.1471-4159.2007.05099.x · DOI
  78. Köpke E, Tung YC, Shaikh S et al (1993) Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease. J Biol Chem 268:24374–24384 · DOI · Paper page
  79. Korach-André M, Gustafsson J-Å (2015) Liver X receptors as regulators of metabolism. Biomol Concepts 6:177–190. https://doi.org/10.1515/bmc-2015-0007 · DOI
  80. Korade Z, Kenworthy AK (2008) Lipid rafts, cholesterol, and the brain. Neuropharmacology 55:1265–1273. https://doi.org/10.1016/j.neuropharm.2008.02.019 · DOI · Paper page
  81. Koronyo-Hamaoui M, Ko MK, Koronyo Y et al (2009) Attenuation of AD-like neuropathology by harnessing peripheral immune cells: local elevation of IL-10 and MMP-9. J Neurochem 111:1409–1424. https://doi.org/10.1111/j.1471-4159.2009.06402.x · DOI
  82. Lahiri DK (2004) Apolipoprotein E as a target for developing new therapeutics for Alzheimer’s disease based on studies from protein, RNA, and regulatory region of the gene. J Mol Neurosci 23:225–233. https://doi.org/10.1385/JMN:23:3:225 · DOI
  83. Lambert JC, Ibrahim-Verbaas CA, Harold D et al (2013) Meta-analysis of 74,046 individuals identifies 11 new susceptibility loci for Alzheimer’s disease. Nat Genet 45:1452–1458. https://doi.org/10.1038/ng.2802 · DOI · Paper page
  84. Leoni V, Caccia C (2015) The impairment of cholesterol metabolism in Huntington disease. Biochim Biophys Acta 1851:1095–1105. https://doi.org/10.1016/j.bbalip.2014.12.018 · DOI
  85. Li J-T, Zhang Y (2018) TREM2 regulates innate immunity in Alzheimer’s disease. J Neuroinflamm 15:107. https://doi.org/10.1186/s12974-018-1148-y · DOI · Paper page
  86. Li J, Kanekiyo T, Shinohara M et al (2012) Differential regulation of amyloid-β endocytic trafficking and lysosomal degradation by apolipoprotein E isoforms. J Biol Chem 287:44593–44601. https://doi.org/10.1074/jbc.M112.420224 · DOI
  87. Li Y, Lu W, Marzolo MP, Bu G (2001) Differential functions of members of the low density lipoprotein receptor family suggested by their distinct endocytosis rates. J Biol Chem 276:18000–18006. https://doi.org/10.1074/jbc.M101589200 · DOI · Paper page
  88. Litvinov DY, Savushkin EV, Dergunov AD (2018) Intracellular and plasma membrane events in cholesterol transport and homeostasis. J Lipids 2018:1–22. https://doi.org/10.1155/2018/3965054 · DOI
  89. Liu F, Gong C-X (2008) Tau exon 10 alternative splicing and tauopathies. Mol Neurodegener 3:8. https://doi.org/10.1186/1750-1326-3-8 · DOI · Paper page
  90. Liu F, Li B, Tung E-J et al (2007a) Site-specific effects of tau phosphorylation on its microtubule assembly activity and self-aggregation. Eur J Neurosci 26:3429–3436. https://doi.org/10.1111/j.1460-9568.2007.05955.x · DOI · Paper page
  91. Liu Q, Zerbinatti CV, Zhang J et al (2007b) Amyloid precursor protein regulates brain apolipoprotein E and cholesterol metabolism through lipoprotein receptor LRP1. Neuron 56:66–78. https://doi.org/10.1016/j.neuron.2007.08.008 · DOI · Paper page
  92. Lizcano JM, Alessi DR (2002) The insulin signalling pathway. Curr Biol 12:R236–R238 · DOI
  93. Ma Y, Yang H, Qi J et al (2010) CD2AP is indispensable to multistep cytotoxic process by NK cells. Mol Immunol 47:1074–1082. https://doi.org/10.1016/j.molimm.2009.11.004 · DOI
  94. Maccioni RB, Farías G, Morales I, Navarrete L (2010) The revitalized tau hypothesis on Alzheimer’s disease. Arch Med Res 41:226–231. https://doi.org/10.1016/j.arcmed.2010.03.007 · DOI
  95. Maher PA, Schubert DR (2009) Metabolic links between diabetes and Alzheimer’s disease. Expert Rev Neurother 9:617–630. https://doi.org/10.1586/ern.09.18 · DOI
  96. Mahley RW (2016) Apolipoprotein E: from cardiovascular disease to neurodegenerative disorders. J Mol Med 94:739–746 · DOI · Paper page
  97. Mahley RW, Weisgraber KH, Huang Y (2006) Apolipoprotein E4: a causative factor and therapeutic target in neuropathology, including Alzheimer’s disease. Proc Natl Acad Sci USA 103:5644–5651. https://doi.org/10.1073/pnas.0600549103 · DOI · Paper page
  98. Malik M, Simpson JF, Parikh I et al (2013) CD33 Alzheimer’s risk-altering polymorphism, CD33 expression, and exon 2 splicing. J Neurosci 33:13320–13325. https://doi.org/10.1523/JNEUROSCI.1224-13.2013 · DOI · Paper page
  99. Manna P, Jain SK (2015) Phosphatidylinositol-3,4,5-triphosphate and cellular signaling: implications for obesity and diabetes. Cell Physiol Biochem 35:1253–1275. https://doi.org/10.1159/000373949 · DOI
  100. Manolopoulos KN, Klotz L-O, Korsten P et al (2010) Linking Alzheimer’s disease to insulin resistance: the FoxO response to oxidative stress. Mol Psychiatry 15:1046–1052. https://doi.org/10.1038/mp.2010.17 · DOI · Paper page
  101. Mantuano E, Jo M, Gonias SL, Campana WM (2010) Low density lipoprotein receptor-related protein (LRP1) regulates Rac1 and RhoA reciprocally to control Schwann cell adhesion and migration. J Biol Chem 285:14259–14266. https://doi.org/10.1074/jbc.M109.085126 · DOI
  102. Matsuzaki T, Sasaki K, Tanizaki Y et al (2010) Insulin resistance is associated with the pathology of Alzheimer disease: the Hisayama study. Neurology 75:764–770. https://doi.org/10.1212/WNL.0b013e3181eee25f · DOI · Paper page
  103. Mayor S, Pagano RE (2007) Pathways of clathrin-independent endocytosis. Nat Rev Mol Cell Biol 8:603–612. https://doi.org/10.1038/nrm2216 · DOI · Paper page
  104. Medeiros R, Baglietto-Vargas D, LaFerla FM (2011) The role of tau in Alzheimer’s disease and related disorders. CNS Neurosci Ther 17:514–524. https://doi.org/10.1111/j.1755-5949.2010.00177.x · DOI
  105. Medina M, Avila J (2014) The role of extracellular Tau in the spreading of neurofibrillary pathology. Front Cell Neurosci 8:113. https://doi.org/10.3389/fncel.2014.00113 · DOI · Paper page
  106. Michikawa M (2006) Role of cholesterol in amyloid cascade: cholesterol-dependent modulation of tau phosphorylation and mitochondrial function. Acta Neurol Scand Suppl 185:21–26. https://doi.org/10.1111/j.1600-0404.2006.00681.x · DOI
  107. Morell P, Jurevics H (1996) Origin of cholesterol in myelin. Neurochem Res 21:463–470 · DOI
  108. Morris M, Knudsen GM, Maeda S et al (2015) Tau post-translational modifications in wild-type and human amyloid precursor protein transgenic mice. Nat Neurosci 18:1183–1189. https://doi.org/10.1038/nn.4067 · DOI · Paper page
  109. Nayak D, Roth TL, McGavern DB (2014) Microglia development and function. Annu Rev Immunol 32:367–402. https://doi.org/10.1146/annurev-immunol-032713-120240 · DOI · Paper page
  110. Offe K, Dodson SE, Shoemaker JT et al (2006) The lipoprotein receptor LR11 regulates amyloid beta production and amyloid precursor protein traffic in endosomal compartments. J Neurosci 26:1596–1603. https://doi.org/10.1523/JNEUROSCI.4946-05.2006 · DOI · Paper page
  111. Orth M, Bellosta S (2012) Cholesterol: its regulation and role in central nervous system disorders. Cholesterol 2012:1–19. https://doi.org/10.1155/2012/292598 · DOI · Paper page
  112. Orth M, Weng W, Funke H et al (1999) Effects of a frequent apolipoprotein E isoform, ApoE4Freiburg (Leu28–%3ePro), on lipoproteins and the prevalence of coronary artery disease in whites. Arterioscler Thromb Vasc Biol 19:1306–1315 · DOI · Paper page
  113. Paolicelli RC, Bolasco G, Pagani F et al (2011) Synaptic pruning by microglia is necessary for normal brain development. Science 333:1456–1458. https://doi.org/10.1126/science.1202529 · DOI · Paper page
  114. Pei J-J, Gong C-X, An W-L et al (2003) Okadaic-acid-induced inhibition of protein phosphatase 2A produces activation of mitogen-activated protein kinases ERK1/2, MEK1/2, and p70 S6, similar to that in Alzheimer’s disease. Am J Pathol 163:845–858. https://doi.org/10.1016/S0002-9440(10)63445-1 · DOI
  115. Peng Q, Malhotra S, Torchia JA et al (2010) TREM2- and DAP12-dependent activation of PI3K requires DAP10 and is inhibited by SHIP1. Sci Signal 3:ra38. https://doi.org/10.1126/scisignal.2000500 · DOI · Paper page
  116. Perea JR, Llorens-Martín M, Ávila J, Bolós M (2018) The Role of Microglia in the Spread of Tau: Relevance for Tauopathies. Front Cell Neurosci 12:1–8. https://doi.org/10.3389/fncel.2018.00172 · DOI
  117. Pereira JB, Ossenkoppele R, Palmqvist S et al (2019) Amyloid and tau accumulate across distinct spatial networks and are differentially associated with brain connectivity. Elife 8:e50830. https://doi.org/10.7554/eLife.50830 · DOI
  118. Pérez-Cerdá F, Sánchez-Gómez MV, Matute C (2015) Pío del Río Hortega and the discovery of the oligodendrocytes. Front Neuroanat. https://doi.org/10.3389/fnana.2015.00092 · DOI
  119. Phiel CJ, Wilson CA, Lee VM, Klein PS (2003) GSK-3alpha regulates production of Alzheimer’s disease amyloid-beta peptides. Nature 423:435–439 · DOI
  120. Poppek D, Keck S, Ermak G et al (2006) Phosphorylation inhibits turnover of the tau protein by the proteasome: influence of RCAN1 and oxidative stress. Biochem J 400:511–520. https://doi.org/10.1042/BJ20060463 · DOI
  121. Pottier C, Hannequin D, Coutant S et al (2012) High frequency of potentially pathogenic SORL1 mutations in autosomal dominant early-onset Alzheimer disease. Mol Psychiatry 17:875–879. https://doi.org/10.1038/mp.2012.15 · DOI · Paper page
  122. Prokic I, Cowling BS, Laporte J (2014) Amphiphysin 2 (BIN1) in physiology and diseases. J Mol Med (Berl) 92:453–463. https://doi.org/10.1007/s00109-014-1138-1 · DOI · Paper page
  123. Puglielli L, Tanzi RE, Kovacs DM (2003) Alzheimer’s disease: the cholesterol connection. Nat Neurosci 6:345–351. https://doi.org/10.1038/nn0403-345 · DOI · Paper page
  124. Qing-Qing T, Yu-Chao C, Zhi-Ying W (2018) The role of CD2AP in the pathogenesis of Alzheimer’s Disease. Aging Dis. https://doi.org/10.14336/AD.2018.1025 · DOI · Paper page
  125. Qu Z, Jiao Z, Sun X et al (2011) Effects of streptozotocin-induced diabetes on tau phosphorylation in the rat brain. Brain Res 1383:300–306. https://doi.org/10.1016/j.brainres.2011.01.084 · DOI
  126. Radhakrishnan A, Ikeda Y, Kwon HJ et al (2007) Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: oxysterols block transport by binding to Insig. Proc Natl Acad Sci U S A 104:6511–6518. https://doi.org/10.1073/pnas.0700899104 · DOI · Paper page
  127. Rahman A, Akterin S, Flores-Morales A et al (2005) High cholesterol diet induces tau hyperphosphorylation in apolipoprotein E deficient mice. FEBS Lett 579:6411–6416. https://doi.org/10.1016/j.febslet.2005.10.024 · DOI
  128. Ramanathan A, Nelson AR, Sagare AP, Zlokovic BV (2015) Impaired vascular-mediated clearance of brain amyloid beta in Alzheimer’s disease: the role, regulation and restoration of LRP1. Front Aging Neurosci 7:136. https://doi.org/10.3389/fnagi.2015.00136 · DOI · Paper page
  129. Ramirez DMO, Andersson S, Russell DW (2008) Neuronal expression and subcellular localization of cholesterol 24-hydroxylase in the mouse brain. J Comp Neurol 507:1676–1693. https://doi.org/10.1002/cne.21605 · DOI
  130. Ramjaun AR, McPherson PS (1998) Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites. J Neurochem 70:2369–2376 · DOI
  131. Rankin CA, Sun Q, Gamblin TC (2007) Tau phosphorylation by GSK-3β promotes tangle-like filament morphology. Mol Neurodegener 2:12. https://doi.org/10.1186/1750-1326-2-12 · DOI
  132. Rebeck GW, Reiter JS, Strickland DK, Hyman BT (1993) Apolipoprotein E in sporadic Alzheimer’s disease: allelic variation and receptor interactions. Neuron 11:575–580 · DOI · Paper page
  133. Reid PC, Sakashita N, Sugii S et al (2004) A novel cholesterol stain reveals early neuronal cholesterol accumulation in the Niemann-Pick type C1 mouse brain. J Lipid Res 45:582–591. https://doi.org/10.1194/jlr.D300032-JLR200 · DOI
  134. Rodrıguez-Rodrıguez E, Vázquez-Higuera JL, Sánchez-Juan P et al (2010) Epistasis between intracellular cholesterol trafficking-related genes (NPC1 and ABCA1) and Alzheimer’s disease risk. J Alzheimer’s Dis 21:619–625. https://doi.org/10.3233/JAD-2010-100432 · DOI
  135. Rogers MA, Liu J, Song B-L et al (2015) Acyl-CoA:cholesterol acyltransferases (ACATs/SOATs): Enzymes with multiple sterols as substrates and as activators. J Steroid Biochem Mol Biol 151:102–107. https://doi.org/10.1016/j.jsbmb.2014.09.008 · DOI
  136. Rouka E, Simister PC, Janning M et al (2015) Differential recognition preferences of the three Src homology 3 (SH3) domains from the adaptor CD2-associated protein (CD2AP) and direct association with Ras and Rab interactor 3 (RIN3). J Biol Chem 290:25275–25292. https://doi.org/10.1074/jbc.M115.637207 · DOI
  137. Saltiel AR, Kahn CR (2001) Insulin signalling and the regulation of glucose and lipid metabolism. Nature 414:799–806. https://doi.org/10.1038/414799a · DOI · Paper page
  138. Sato N, Morishita R (2014) Brain alterations and clinical symptoms of dementia in diabetes: aβ/tau-dependent and independent mechanisms. Front Endocrinol (Lausanne) 5:143. https://doi.org/10.3389/fendo.2014.00143 · DOI
  139. Selkoe DJ, Hardy J (2016) The amyloid hypothesis of Alzheimer’s disease at 25 years. EMBO Mol Med 8:595–608. https://doi.org/10.15252/emmm.201606210 · DOI · Paper page
  140. Sengupta A, Kabat J, Novak M et al (1998) Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules. Arch Biochem Biophys 357:299–309. https://doi.org/10.1006/abbi.1998.0813 · DOI · Paper page
  141. Simard AR, Soulet D, Gowing G et al (2006) Bone marrow-derived microglia play a critical role in restricting senile plaque formation in Alzheimer’s disease. Neuron 49:489–502. https://doi.org/10.1016/j.neuron.2006.01.022 · DOI · Paper page
  142. Simón D, Hernández F, Avila J (2013) The involvement of cholinergic neurons in the spreading of tau pathology. Front Neurol 4:74. https://doi.org/10.3389/fneur.2013.00074 · DOI
  143. Singh TJ, Grundke-Iqbal I, McDonald B, Iqbal K (1994) Comparison of the phosphorylation of microtubule-associated protein tau by non-proline dependent protein kinases. Mol Cell Biochem 131:181–189 · DOI
  144. Slepnev VI, Ochoa GC, Butler MH, De Camilli P (2000) Tandem arrangement of the clathrin and AP-2 binding domains in amphiphysin 1 and disruption of clathrin coat function by amphiphysin fragments comprising these sites. J Biol Chem 275:17583–17589. https://doi.org/10.1074/jbc.M910430199 · DOI
  145. Sonawane SK, Chinnathambi S (2018) Prion-Like propagation of post-translationally modified tau in Alzheimer’s disease: a hypothesis. J Mol Neurosci 65:480–490. https://doi.org/10.1007/s12031-018-1111-5 · DOI
  146. Song H-L, Shim S, Kim D-H et al (2014) β-Amyloid is transmitted via neuronal connections along axonal membranes. Ann Neurol 75:88–97. https://doi.org/10.1002/ana.24029 · DOI
  147. Spuch C, Ortolano S, Navarro C (2012) LRP-1 and LRP-2 receptors function in the membrane neuron. Trafficking mechanisms and proteolytic processing in Alzheimer’s disease. Front Physiol 3:269. https://doi.org/10.3389/fphys.2012.00269 · DOI · Paper page
  148. Starks EJ, Patrick O’Grady J, Hoscheidt SM et al (2015) Insulin resistance is associated with higher cerebrospinal fluid Tau levels in asymptomatic APOEɛ4 carriers. J Alzheimers Dis 46:525–533. https://doi.org/10.3233/JAD-150072 · DOI
  149. Takei Y, Teng J, Harada A, Hirokawa N (2000) Defects in axonal elongation and neuronal migration in mice with disrupted tau and map1b genes. J Cell Biol 150:989–1000 · DOI
  150. Tan M-S, Yu J-T, Tan L (2013) Bridging integrator 1 (BIN1): form, function, and Alzheimer’s disease. Trends Mol Med 19:594–603. https://doi.org/10.1016/j.molmed.2013.06.004 · DOI
  151. Tarasoff-Conway JM, Carare RO, Osorio RS et al (2015) Clearance systems in the brain-implications for Alzheimer disease. Nat Rev Neurol 11:457–470. https://doi.org/10.1038/nrneurol.2015.119 · DOI · Paper page
  152. Tarr PT, Edwards PA (2008) ABCG1 and ABCG4 are coexpressed in neurons and astrocytes of the CNS and regulate cholesterol homeostasis through SREBP-2. J Lipid Res 49:169–182. https://doi.org/10.1194/jlr.M700364-JLR200 · DOI
  153. Teng J, Takei Y, Harada A et al (2001) Synergistic effects of MAP2 and MAP1B knockout in neuronal migration, dendritic outgrowth, and microtubule organization. J Cell Biol 155:65–76. https://doi.org/10.1083/jcb.200106025 · DOI
  154. Vanier MT (2015) Complex lipid trafficking in Niemann-Pick disease type C. J Inherit Metab Dis 38:187–199. https://doi.org/10.1007/s10545-014-9794-4 · DOI
  155. Wang JZ, Grundke-Iqbal I, Iqbal K (1996) Restoration of biological activity of Alzheimer abnormally phosphorylated tau by dephosphorylation with protein phosphatase-2A, -2B and -1. Brain Res Mol Brain Res 38:200–208 · DOI
  156. Wang Q, Yan J, Chen X et al (2011) Statins: multiple neuroprotective mechanisms in neurodegenerative diseases. Exp Neurol 230:27–34. https://doi.org/10.1016/j.expneurol.2010.04.006 · DOI · Paper page
  157. Wang Y, Mandelkow E (2016) Tau in physiology and pathology. Nat Rev Neurosci 17:22–35. https://doi.org/10.1038/nrn.2015.1 · DOI · Paper page
  158. Wang Y, Rogers PM, Su C et al (2008) Regulation of cholesterologenesis by the oxysterol receptor, LXRalpha. J Biol Chem 283:26332–26339. https://doi.org/10.1074/jbc.M804808200 · DOI
  159. Wegmann S, Jung YJ, Chinnathambi S et al (2010) Human Tau isoforms assemble into ribbon-like fibrils that display polymorphic structure and stability. J Biol Chem 285:27302–27313. https://doi.org/10.1074/jbc.M110.145318 · DOI
  160. Weller RO, Subash M, Preston SD et al (2008) Perivascular drainage of amyloid-beta peptides from the brain and its failure in cerebral amyloid angiopathy and Alzheimer’s disease. Brain Pathol 18:253–266. https://doi.org/10.1111/j.1750-3639.2008.00133.x · DOI
  161. Wildsmith KR, Holley M, Savage JC et al (2013) Evidence for impaired amyloid β clearance in Alzheimer’s disease. Alzheimers Res Ther 5:33. https://doi.org/10.1186/alzrt187 · DOI
  162. Wilsie LC, Orlando RA (2003) The low density lipoprotein receptor-related protein complexes with cell surface heparan sulfate proteoglycans to regulate proteoglycan-mediated lipoprotein catabolism. J Biol Chem 278:15758–15764. https://doi.org/10.1074/jbc.M208786200 · DOI · Paper page
  163. Witzlack T, Wenzeck T, Thiery J, Orth M (2007) cAMP-induced expression of ABCA1 is associated with MAP-kinase-pathway activation. Biochem Biophys Res Commun 363:89–94. https://doi.org/10.1016/j.bbrc.2007.08.109 · DOI
  164. Wolf G, Stahl RA (2003) CD2-associated protein and glomerular disease. Lancet 362:1746–1748. https://doi.org/10.1016/S0140-6736(03)14856-8 · DOI
  165. Wolfe C, Fitz N, Nam K et al (2019) The Role of APOE and TREM2 in Alzheimer’s disease—current understanding and perspectives. Int J Mol Sci 20:81. https://doi.org/10.3390/ijms20010081 · DOI
  166. Wollmer MA, Streffer JR, Tsolaki M et al (2003) Genetic association of acyl-coenzyme A: cholesterol acyltransferase with cerebrospinal fluid cholesterol levels, brain amyloid load, and risk for Alzheimer’s disease. Mol Psychiatry 8:635–638. https://doi.org/10.1038/sj.mp.4001296 · DOI
  167. Wong BX, Hung YH, Bush AI, Duce JA (2014) Metals and cholesterol: two sides of the same coin in Alzheimer’s disease pathology. Front Aging Neurosci 6:91. https://doi.org/10.3389/fnagi.2014.00091 · DOI
  168. Wüstner D, Mondal M, Tabas I, Maxfield FR (2005) Direct observation of rapid internalization and intracellular transport of sterol by macrophage foam cells. Traffic 6:396–412. https://doi.org/10.1111/j.1600-0854.2005.00285.x · DOI
  169. Xu S, Zhang X, Liu P (2018) Lipid droplet proteins and metabolic diseases. Biochim Biophys Acta 1864:1968–1983 · DOI
  170. Yu C, Nwabuisi-Heath E, Laxton K, LaDu MJ (2010) Endocytic pathways mediating oligomeric Abeta42 neurotoxicity. Mol Neurodegener 5:19. https://doi.org/10.1186/1750-1326-5-19 · DOI
  171. Zefirov AL, Petrov AM (2010) Lipids in the process of synaptic vesicle exo- and endocytosis. Ross Fiziol zhurnal Im IM Sechenova 96:753–765
  172. Zhan Y, Paolicelli RC, Sforazzini F et al (2014) Deficient neuron-microglia signaling results in impaired functional brain connectivity and social behavior. Nat Neurosci 17:400–406. https://doi.org/10.1038/nn.3641 · DOI · Paper page
  173. Zhang J, Liu Q (2015) Cholesterol metabolism and homeostasis in the brain. Protein Cell 6:254–264. https://doi.org/10.1007/s13238-014-0131-3 · DOI · Paper page
  174. Zheng H, Jia L, Liu C-C et al (2017) TREM2 promotes microglial survival by activating Wnt/β-catenin pathway. J Neurosci 37:1772–1784. https://doi.org/10.1523/JNEUROSCI.2459-16.2017 · DOI · Paper page
  175. Zhou Y, Hayashi I, Wong J et al (2014) Intracellular clusterin interacts with brain isoforms of the bridging integrator 1 and with the microtubule-associated protein Tau in Alzheimer’s disease. PLoS ONE 9:e103187. https://doi.org/10.1371/journal.pone.0103187 · DOI · Paper page

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Metadata

Authors
Nanjundaiah, S., Chidambaram, H., Chandrashekar, M., & Chinnathambi, S.
ORCID
Chinnathambi, Subashchandrabose
Venue
Cellular and Molecular Neurobiology
Publisher
Springer Science and Business Media LLC
Published
2020-05-28
Volume
41
Issue
4
Pages
651-668
ISSN
  • 0272-4340
  • 1573-6830
DOI
10.1007/s10571-020-00883-6
Cited by
36
References
52
Language
en
Licence
Funders
Council of Scientific and Industrial Research, India (CSIR NCL MLP 029526)

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