Cholesterol impairs autophagy-mediated clearance of amyloid beta while promoting its secretion

Barbero-Camps, Elisabet; Roca-Agujetas, Vicente; Bartolessis, Isabel; de Dios, Cristina; Fernández-Checa, Jose C.; Marí, Montserrat; Morales, Albert; Hartmann, Tobias; Colell, Anna

doi:10.1080/15548627.2018.1438807

Cited by 127Alzheimer's disease research and treatmentsAutophagy in Disease and TherapyNeuroinflammation and Neurodegeneration Mechanisms

Cholesterol impairs autophagy-mediated clearance of amyloid beta while promoting its secretion

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Barbero-Camps, Elisabet, Roca-Agujetas, Vicente, Bartolessis, Isabel, de Dios, Cristina, Fernández-Checa, Jose C., Marí, Montserrat, Morales, Albert, Hartmann, Tobias +1 more·2018·Autophagy

DOI 10.1080/15548627.2018.1438807PMC PMC6103708

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Abstract

Macroautophagy/autophagy failure with the accumulation of autophagosomes is an early neuropathological feature of Alzheimer disease (AD) that directly affects amyloid beta (Aβ) metabolism. Although loss of presenilin 1 function has been reported to impair lysosomal function and prevent autophagy flux, the detailed mechanism leading to autophagy dysfunction in AD remains to be elucidated. The resemblance between pathological hallmarks of AD and Niemann-Pick Type C disease, including endosome-lysosome abnormalities and impaired autophagy, suggests cholesterol accumulation as a common link. Using a mouse model of AD (APP-PSEN1-SREBF2 mice), expressing chimeric mouse-human amyloid precursor protein with the familial Alzheimer Swedish mutation (APP695swe) and mutant presenilin 1 (PSEN1-dE9), together with a dominant-positive, truncated and active form of SREBF2/SREBP2 (sterol regulatory element binding factor 2), we demonstrated that high brain cholesterol enhanced autophagosome formation, but disrupted its fusion with endosomal-lysosomal vesicles. The combination of these alterations resulted in impaired degradation of Aβ and endogenous MAPT (microtubule associated protein tau), and stimulated autophagy-dependent Aβ secretion. Exacerbated Aβ-induced oxidative stress in APP-PSEN1-SREBF2 mice, due to cholesterol-mediated depletion of mitochondrial glutathione/mGSH, is critical for autophagy induction. In agreement, in vivo mitochondrial GSH recovery with GSH ethyl ester, inhibited autophagosome synthesis by preventing the oxidative inhibition of ATG4B deconjugation activity exerted by Aβ. Moreover, cholesterol-enrichment within the endosomes-lysosomes modified the levels and membrane distribution of RAB7A and SNAP receptors (SNAREs), which affected its fusogenic ability. Accordingly, in vivo treatment with 2-hydroxypropyl-β-cyclodextrin completely rescued these alterations, making it a potential therapeutic tool for AD.

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Aβ catabolism genes RAB5A, RAB11A, CLU, and LRP2 are down-regulated in AD monocytes, suggesting impaired Aβ catabolism in AD monocytes.
“Similarly, several genes reported to be involved in Aβ catabolism, such as RAB5A, RAB11A, CLU, and LRP2 (49–53), were also down-regulated in AD monocytes, suggesting the impaired Aβ catabolism in AD monocytes.”
From Understanding monocyte-driven neuroinflammation in Alzheimer’s disease using human cortical organoid microphysiological systems (2025) · cites this paper as [50]
The citation is attached to the description of RAB5A, RAB11A, CLU, and LRP2 as genes involved in Aβ catabolism; the down-regulation in AD monocytes is the citing authors’ own finding. The Discussion mentions RAB5A only as an indicator of early endosomal enlargement, while the Introduction describes Aβ clearance without linking it to those four genes. Searches for the gene names and their roles in Aβ degradation found no passage establishing the cited claim. (LLM, conf=0.72)
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Wang, Y., Li, L., Hou, C., Lai, Y., Long, J., Liu, J., Zhong, Q., & Diao, J. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.07.009 · Cited by 135 · see citing works
APP/PS1 mice overexpressing SREBP-2 exhibit combined Aβ accumulation and tau pathology underlying Alzheimer's disease
Barbero‐Camps, E., Fernández, A., Martínez-Gili, L., Fernández-Checa, J. C., & Colell, A. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt201 · Cited by 127 · see citing works
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Attenuation of the Lysosomal Death Pathway by Lysosomal Cholesterol Accumulation
Appelqvist, H., Nilsson, C., Garner, B., Brown, A. J., Kågedal, K., & Öllinger, K. M. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2010.10.030 · Cited by 124 · see citing works
Role of Cholesterol in APP Metabolism and Its Significance in Alzheimer’s Disease Pathogenesis
Maulik, M., Westaway, D. A., Jhamandas, J. H., & Kar, S. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8337-y · Cited by 117 · see citing works
DJ-1 Protects Dopaminergic Neurons against Rotenone-Induced Apoptosis by Enhancing ERK-Dependent Mitophagy
Gao, H., Yang, W., Qi, Z., Lu, L., Duan, C., Zhao, C., & Yang, H. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.06.034 · Cited by 116 · see citing works
Glutathione participates in the modulation of starvation-induced autophagy in carcinoma cells
Desideri, E., Filomeni, G., & Ciriolo, M. R. (2012) · Autophagy · doi:10.4161/auto.22037 · Cited by 116 · see citing works
Cytosolic Proteolysis of τ by Cathepsin D in Hippocampus Following Suppression of Cathepsins B and L
Bednarski, E., & LYNCH, G. S. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67051846.x · Cited by 110 · see citing works
Cholesterol synthesis rate in human hippocampus declines with aging
Thelen, K. M., Falkai, P., Bayer, T. A., & Lütjohann, D. (2006) · Neuroscience Letters · doi:10.1016/j.neulet.2006.04.034 · Cited by 107 · see citing works
Endoplasmic Reticulum Stress Mediates Amyloid β Neurotoxicity via Mitochondrial Cholesterol Trafficking
Barbero‐Camps, E., Fernández, A., Baulies, A., Martínez-Gili, L., Fernández-Checa, J. C., & Colell, A. (2014) · American Journal Of Pathology · doi:10.1016/j.ajpath.2014.03.014 · Cited by 105 · see citing works
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Increasing membrane cholesterol of neurons in culture recapitulates Alzheimer’s disease early phenotypes
Marquer, C., Lainé, J., Dauphinot, L., Hanbouch, L., Lemercier-Neuillet, C., Pierrot, N., Bossers, K., Le, M., Corlier, F. W., Benstaali, C., et al. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-60 · Cited by 101 · see citing works
Oxidative Stress and Altered Mitochondrial Function in Neurodegenerative Diseases: Lessons From Mouse Models
Fernández-Checa, J. C., Fernandez, A., Morales, A., Marı́, M., García‐Ruiz, C., & Colell, A. (2010) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152710791556113 · Cited by 98 · see citing works
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Mechanism of Mitochondrial Glutathione-Dependent Hepatocellular Susceptibility to TNF Despite NF-κB Activation
Marı́, M., Colell, A., Morales, A., Caballero, F., Moles, A., Fernández, A., Terrones, O., Basáñez, G., Antonsson, B. E., García‐Ruiz, C., et al. (2008) · Gastroenterology · doi:10.1053/j.gastro.2008.01.073 · Cited by 96 · see citing works
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Longitudinal follow-up of autophagy and inflammation in brain of APPswePS1dE9 transgenic mice
François, A., Bilan, A. R., Quellard, N., Fernandez, B., Janet, T., Chassaing, D., Paccalin, M., Terro, F., & Page, G. (2014) · Journal of Neuroinflammation · doi:10.1186/s12974-014-0139-x · Cited by 95 · see citing works
Permeabilization of the Mitochondrial Outer Membrane by Bax/Truncated Bid (tBid) Proteins as Sensitized by Cardiolipin Hydroperoxide Translocation
Korytowski, W., Basova, L. V., Pilat, A. K., Kernstock, R. M., & Girotti, A. W. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.188516 · Cited by 92 · see citing works
Peroxiredoxin 6 Is a Crucial Factor in the Initial Step of Mitochondrial Clearance and Is Upstream of the PINK1-Parkin Pathway
Ma, S., Zhang, X., Zheng, L., Li, Z., Zhao, X., Lai, W., Shen, H., Lv, J., Yang, G., Wang, Q., et al. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6336 · Cited by 92 · see citing works
Tangle-bearing neurons contain more free cholesterol than adjacent tangle-free neurons
Distl, R., Meske, V., & Ohm, T. (2001) · Acta Neuropathologica · doi:10.1007/s004010000314 · Cited by 91 · see citing works
Bidirectional links between Alzheimer's disease and Niemann–Pick type C disease
Malnar, M., Hecimovic, S. K., Mattsson, N., & Zetterberg, H. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.05.033 · Cited by 89 · see citing works
Starvation and inhibition of lysosomal function increased tau secretion by primary cortical neurons
Mohamed, N., Plouffe, V., Rémillard‐Labrosse, G., Planel, E., & Leclerc, N. M. (2014) · Scientific Reports · doi:10.1038/srep05715 · Cited by 86 · see citing works
Neural Cell Adhesion Molecule Modulates Dopaminergic Signaling and Behavior by Regulating Dopamine D2Receptor Internalization
Xiao, M.-F., Xu, J.-C., Tereshchenko, Y., Novak, D., Schachner, M., & KLEENE, R. B. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4860-09.2009 · Cited by 78 · see citing works
Ultrastructural Localization of Intraneuronal Aβ-Peptide in Alzheimer Disease Brains
Gómez-Ramos, P., & Asunción Morán, M. (2007) · Journal of Alzheimer's Disease · doi:10.3233/jad-2007-11109 · Cited by 76 · see citing works
Cholesterol transport from late endosomes to the Golgi regulates t-SNARE trafficking, assembly, and function
Reverter, M., Rentero, C., de Muga, S. V., Álvarez-Guaita, A., Mulay, V., Cairns, R. F., Wood, P., Monastyrskaya, K., Pol, A., Tebar, F., et al. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-04-0332 · Cited by 72 · see citing works
Role of cholesterol in SNARE-mediated trafficking on intracellular membranes
Enrich, C., Rentero, C., Hierro, A., & Grewal, T. (2015) · Journal of Cell Science · doi:10.1242/jcs.164459 · Cited by 71 · see citing works
Cardiolipin Signaling Mechanisms: Collapse of Asymmetry and Oxidation
Kagan, V. E., Tyurina, Y. Y., Tyurin, V. A., Mohammadyani, D., Angeli, J. P. F., Баранов, В. С., Klein‐Seetharaman, J., Friedlander, R. M., Mallampalli, R. K., Conrad, M., et al. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6219 · Cited by 65 · see citing works
ROS inhibit autophagy by downregulating ULK1 mediated by the phosphorylation of p53 in selenite-treated NB4 cells
Ci, Y., Shi, K., An, J., Yang, Y., Hui, K., Wu, P., Shi, L., & Xu, C. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.506 · Cited by 64 · see citing works
Endolysosome involvement in LDL cholesterol-induced Alzheimer's disease-like pathology in primary cultured neurons
Hui, L., Chen, X., & Geiger, J. D. (2012) · Life Sciences · doi:10.1016/j.lfs.2012.04.039 · Cited by 62 · see citing works
Accumulation of Tau in Autophagic Vacuoles in Chloroquine Myopathy
Murakami, N., Oyama, F., Gu, Y., McLennan, I. S., Nonaka, I., & Ihara, Y. (1998) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199807000-00003 · Cited by 47 · see citing works
Mutant human APP exacerbates pathology in a mouse model of NPC and its reversal by a β-cyclodextrin
Maulik, M., Ghoshal, B., Kim, J., Wang, Y., Yang, J., Westaway, D. A., & Kar, S. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds322 · Cited by 38 · see citing works
APP overexpression in the absence of NPC1 exacerbates metabolism of amyloidogenic proteins of Alzheimer's disease
Maulik, M., Peake, K., Chung, J.-Y., Wang, Y., Vance, J. E., & Kar, S. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv413 · Cited by 28 · see citing works

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Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) <sup>1</sup>
Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,622 · see citing works
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Common and rare variant association analyses in amyotrophic lateral sclerosis identify 15 risk loci with distinct genetic architectures and neuron-specific biology
van Rheenen, W., van der Spek, R. A. A., Bakker, M. K., van Vugt, J. J. F. A., Hop, P. J., Zwamborn, R. A. J., de Klein, N., Westra, H.-J., Bakker, O. B., Deelen, P., et al. (2021) · Nature Genetics · doi:10.1038/s41588-021-00973-1 · Cited by 542 · see citing works
Modifiable Risk Factors for Alzheimer’s Disease
Edwards III, G. A., Gamez, N., Escobedo Jr., G., Calderon, O., & Moreno-Gonzalez, I. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00146 · Cited by 253 · see citing works
Mitochondrial Glutathione: Recent Insights and Role in Disease
Marı́, M., de Gregorio, E., de Dios, C., Agujetas, V. R., Cucarull, B., Tutusaus, A., Morales, A., & Colell, A. (2020) · Antioxidants · doi:10.3390/antiox9100909 · Cited by 177 · see citing works
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Recent Insights into the Mitochondrial Role in Autophagy and Its Regulation by Oxidative Stress
Agujetas, V. R., de Dios, C., Pinilla, L. L., Marı́, M., Morales, A., & Colell, A. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/3809308 · Cited by 149 · see citing works
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Cholesterol alters mitophagy by impairing optineurin recruitment and lysosomal clearance in Alzheimer’s disease
Agujetas, V. R., Barbero‐Camps, E., de Dios, C., Podlesniy, P., Abadin, X., Morales, A., Marı́, M., Trullás, R., & Colell, A. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00435-6 · Cited by 110 · see citing works
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Autophagy: Supporting cellular and organismal homeostasis by self-eating
Eskelinen, E. (2019) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2019.03.010 · Cited by 106 · see citing works
Mitochondrial reactive oxygen species in physiology and disease
Antonucci, S., Lisa, F. D., & Kaludercic, N. (2021) · Cell Calcium · doi:10.1016/j.ceca.2020.102344 · Cited by 99 · see citing works
Genome-wide study of DNA methylation shows alterations in metabolic, inflammatory, and cholesterol pathways in ALS
Hop, P. J., Zwamborn, R. A. J., Hannon, E. J., Shireby, G. L., Nabais, M. F., Walker, E., van Rheenen, W., van Vugt, J. J. F. A., Dekker, A. M., Westeneng, H., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abj0264 · Cited by 102 · see citing works
ATAD3A oligomerization promotes neuropathology and cognitive deficits in Alzheimer’s disease models
Zhao, Y., Hu, D., Wang, R., Sun, X., Ropelewski, P., Hubler, Z. M. L., Lundberg, K. C., Wang, Q., Adams, D., Xu, R., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28769-9 · Cited by 97 · see citing works
The role of APOE4 in Alzheimer’s disease: strategies for future therapeutic interventions
Hunsberger, H. C., Pinky, P. D., Smith, W., Suppiramaniam, V., & Reed, M. N. (2019) · Neuronal Signaling · doi:10.1042/ns20180203 · Cited by 94 · see citing works
Cholesterol as a key player in amyloid β-mediated toxicity in Alzheimer’s disease
Rudajev, V., & Novotný, J. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.937056 · Cited by 94 · see citing works
Sphingolipids in Alzheimer's disease, how can we target them?
Crivelli, S. M., Giovagnoni, C., Visseren, L., Scheithauer, A.-L., de Wit, N. M., den Hoedt, S., Losen, M. H., Mulder, M. T., Walter, J., de Vries, H. E., et al. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2019.12.003 · Cited by 85 · see citing works
Inflammasome activation under high cholesterol load triggers a protective microglial phenotype while promoting neuronal pyroptosis
de Dios, C., Abadin, X., Roca-Agujetas, V., Jimenez-Martinez, M., Morales, A., Trullas, R., Mari, M., & Colell, A. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00343-3 · Cited by 85 · see citing works
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Unraveling the impact of Omega-3 polyunsaturated fatty acids on blood-brain barrier (BBB) integrity and glymphatic function
Wen, J., Satyanarayanan, S. K., Li, A., Yan, L., Zhao, Z., Yuan, Q., Su, K., & Su, H. (2023) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2023.10.018 · Cited by 84 · see citing works
Circular RNA NF1-419 enhances autophagy to ameliorate senile dementia by binding Dynamin-1 and Adaptor protein 2 B1 in AD-like mice
Diling, C., Guo, Y., Qi, L., Xiaocui, T., Liu, Y., Xin, Y., Guoyan, H., Shuai, O., Yong, T., Wang, D., et al. (2019) · Aging · doi:10.18632/aging.102529 · Cited by 78 · see citing works
Retracted
Cholesterol Metabolism in Aging and Age-Related Disorders
Saher, G. (2023) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-091922-034237 · Cited by 81 · see citing works
Omega-3 polyunsaturated fatty acids promote brain-to-blood clearance of β-Amyloid in a mouse model with Alzheimer’s disease
Yan, L., Xie, Y., Satyanarayanan, S. K., Zeng, H., Liu, Q., Huang, M., Ma, Y., Wan, J., Yao, X., Su, K., et al. (2019) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2019.05.033 · Cited by 72 · see citing works
A multitude of signaling pathways associated with Alzheimer's disease and their roles in AD pathogenesis and therapy
Gadhave, K., Kumar, D., Uversky, V. N., & Giri, R. (2020) · Medicinal Research Reviews · doi:10.1002/med.21719 · Cited by 70 · see citing works
27-Hydroxycholesterol Contributes to Lysosomal Membrane Permeabilization-Mediated Pyroptosis in Co-cultured SH-SY5Y Cells and C6 Cells
Chen, S., Zhou, C. L., Yu, H., Tao, L., An, Y., Zhang, X., Wang, Y., Wang, Y., & Xiao, R. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00014 · Cited by 67 · see citing works
Focus on the morphogenesis, fate and the role in tumor progression of multivesicular bodies
Peng, X., Yang, L., Ma, Y., Li, Y., & Li, H. (2020) · Cell Communication and Signaling · doi:10.1186/s12964-020-00619-5 · Cited by 60 · see citing works
Exosomes, autophagy and ER stress pathways in human diseases: Cross-regulation and therapeutic approaches
Jahangiri, B., Saei, A. K., Obi, P. O., Asghari, N., Lorzadeh, S., Hekmatirad, S., Rahmati, M., Velayatipour, F., Asghari, M. H., Saleem, A., et al. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2022.166484 · Cited by 60 · see citing works
Cyclodextrins: Only Pharmaceutical Excipients or Full-Fledged Drug Candidates?
Kovács, T., Nagy, P., Panyi, G., Szente, L., Varga, Z., & Zákány, F. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14122559 · Cited by 57 · see citing works
Honokiol improves cognitive impairment in APP/PS1 mice through activating mitophagy and mitochondrial unfolded protein response
Hou, M., Bao, W., Gao, Y., Chen, J., & Song, G. (2021) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2021.109741 · Cited by 56 · see citing works
MeCP2 Is an Epigenetic Factor That Links DNA Methylation with Brain Metabolism
Vuu, Y. M., Roberts, C.-T., & Rastegar, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24044218 · Cited by 53 · see citing works
Oxidative inactivation of amyloid beta-degrading proteases by cholesterol-enhanced mitochondrial stress
de Dios, C., Bartolessis, I., Agujetas, V. R., Barbero‐Camps, E., Marı́, M., Morales, A., & Colell, A. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101283 · Cited by 47 · see citing works
Self-citation
Cholesterol-dependent amyloid β production: space for multifarious interactions between amyloid precursor protein, secretases, and cholesterol
Rudajev, V., & Novotný, J. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-01127-y · Cited by 47 · see citing works
Autophagy induction in the treatment of Alzheimer's disease
Schmukler, E., & Pinkas‐Kramarski, R. (2019) · Drug Development Research · doi:10.1002/ddr.21605 · Cited by 43 · see citing works
The Emerging Role of Circular RNAs in Alzheimer’s Disease and Parkinson’s Disease
Zhang, M., & Bian, Z. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.691512 · Cited by 40 · see citing works
The pleiotropic roles of autophagy in Alzheimer’s disease: From pathophysiology to therapy
Festa, B. P., Barbosa, A. D., Rob, M., & Rubinsztein, D. C. (2021) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2021.07.011 · Cited by 41 · see citing works
Mitochondrial Cholesterol in Alzheimer's Disease and Niemann–Pick Type C Disease
Torres, S., García‐Ruiz, C., & Fernández-Checa, J. C. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.01168 · Cited by 40 · see citing works
Self-citation
Key Disease Mechanisms Linked to Alzheimer’s Disease in the Entorhinal Cortex
Bottero, V., Powers, D., Yalamanchi, A., Quinn, J. P., & Potashkin, J. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22083915 · Cited by 35 · see citing works
Defective Autophagy and Mitophagy in Alzheimer’s Disease: Mechanisms and Translational Implications
Chen, J., He, H., Ye, Q., Feng, F., Wang, W., Gu, Y., Han, R., & Xie, C. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02487-7 · Cited by 36 · see citing works
The role of exosome lipids in central nervous system diseases
Wang, G., Wang, Y., Liu, N., & Liu, M. (2020) · Reviews in the Neurosciences · doi:10.1515/revneuro-2020-0013 · Cited by 34 · see citing works
Molecular mechanisms underlying actions of certain long noncoding RNAs in Alzheimer’s disease
Ahmadi, S., Zobeiri, M., & Bradburn, S. (2020) · Metabolic Brain Disease · doi:10.1007/s11011-020-00564-9 · Cited by 35 · see citing works
Cholesterol-associated lysosomal disorder triggers cell death of hematological malignancy: Dynamic analysis on cytotoxic effects of LW-218
Hu, P., Li, H., Sun, W., Wang, H.-Z., Yu, X.-X., Qing, Y.-J., Wang, Z., Zhu, M.-Y., Xu, J.-Y., Guo, Q.-L., et al. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.02.004 · Cited by 31 · see citing works
Distinct functional roles of Vps41-mediated neuroprotection in Alzheimer’s and Parkinson’s disease models of neurodegeneration
Griffin, E. F., Yan, X., Caldwell, K. A., & Caldwell, G. A. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy308 · Cited by 32 · see citing works
IKKβ activation promotes amphisome formation and extracellular vesicle secretion in tumor cells
Peng, X., Yang, L., Ma, Y., Li, X., Yang, S., Li, Y., Wu, B., Tang, S., Zhang, F., Zhang, B., et al. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118857 · Cited by 32 · see citing works
The interplay between lipid and Aβ amyloid homeostasis in Alzheimer’s Disease: risk factors and therapeutic opportunities
García‐Viñuales, S., Sciacca, M. F. M., Lanza, V., Santoro, A. M., Grasso, G., Tundo, G. R., Sbardella, D., Coletta, M., Grasso, G., Rosa, C. L., et al. (2021) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2021.105072 · Cited by 33 · see citing works
Cholesterol-induced leucine aminopeptidase 3 (LAP3) upregulation inhibits cell autophagy in pathogenesis of NAFLD
Feng, L., Chen, Y., Xu, K., Li, Y., Riaz, F., Lu, K., Chen, Q., Du, X., Wu, L., Cao, D., et al. (2022) · Aging · doi:10.18632/aging.204011 · Cited by 31 · see citing works
Pseudoginsenoside‐F11 alleviates oligomeric β‐amyloid‐induced endosome‐lysosome defects in microglia
Yao, X., Xue, X., Zhang, H. T., Zhu, M., Yang, X. W., Wu, C. F., & Yang, J. (2018) · Traffic · doi:10.1111/tra.12620 · Cited by 30 · see citing works
Ethanol, neurosteroids and cellular stress responses: Impact on central nervous system toxicity, inflammation and autophagy
Fujii, C., Zorumski, C. F., & Izumi, Y. (2021) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2021.01.026 · Cited by 30 · see citing works
The interplay between aging‐associated loss of protein homeostasis and extracellular vesicles in neurodegeneration
Guix, F. X. (2019) · Journal of Neuroscience Research · doi:10.1002/jnr.24526 · Cited by 29 · see citing works
Cubeben induces autophagy via PI3K-AKT-mTOR pathway to protect primary neurons against amyloid beta in Alzheimer’s disease
Li, X., Song, J., & Dong, R. (2019) · Cytotechnology · doi:10.1007/s10616-019-00313-6 · Cited by 29 · see citing works
2-Hydroxypropyl-gamma-cyclodextrin overcomes NPC1 deficiency by enhancing lysosome-ER association and autophagy
Singhal, A., Krystofiak, E., Jerome, W. G., & Song, B. (2020) · Scientific Reports · doi:10.1038/s41598-020-65627-4 · Cited by 30 · see citing works
Finding pathogenic commonalities between Niemann-Pick type C and other lysosomal storage disorders: Opportunities for shared therapeutic interventions
Yañez, M. J., Marín, T., Balboa, E., Klein, A. D., Alvarez, A. R., & Zanlungo, S. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165875 · Cited by 29 · see citing works
STARD1 and NPC1 expression as pathological markers associated with astrogliosis in post-mortem brains from patients with Alzheimer's disease and Down syndrome
Arenas, F., Castro, F., Núñez, S., Gay, G., García‐Ruiz, C., & Fernández-Checa, J. C. (2020) · Aging · doi:10.18632/aging.102641 · Cited by 28 · see citing works
Self-citation
Molecular Mind Games: The Medicinal Action of Cyclodextrins in Neurodegenerative Diseases
Braga, S. S. (2023) · Biomolecules · doi:10.3390/biom13040666 · Cited by 27 · see citing works
Transmissible Endosomal Intoxication: A Balance between Exosomes and Lysosomes at the Basis of Intercellular Amyloid Propagation
Bécot, A., Volgers, C., & van Niel, G. (2020) · Biomedicines · doi:10.3390/biomedicines8080272 · Cited by 23 · see citing works
Autophagy Genes for Wet Age-Related Macular Degeneration in a Finnish Case-Control Study
Paterno, J. J., Koskela, A. K. J., Hyttinen, J. M. T., Vattulainen, E., Synowiec, E., Tuuminen, R., Watała, C. W., Błasiak, J., & Kaarniranta, K. (2020) · Genes · doi:10.3390/genes11111318 · Cited by 20 · see citing works
Cholesterol Metabolism in CNS Diseases: The Potential of SREBP2 and LXR as Therapeutic Targets
Wang, N.-Q., Sun, P.-X., Shen, Q.-Q., & Deng, M.-Y. (2025) · Molecular Neurobiology · doi:10.1007/s12035-024-04672-w · Cited by 19 · see citing works
CHIP modulates APP‐induced autophagy‐dependent pathological symptoms in Drosophila
Zhuang, L., Peng, F., Huang, Y., Li, W., Huang, J., Chu, Y., Ren, P., Sun, Y., Zhang, Y., Xue, E., et al. (2019) · Aging Cell · doi:10.1111/acel.13070 · Cited by 19 · see citing works
Cholesterol-enriched membrane micro-domain deficiency induces doxorubicin resistance via promoting autophagy in breast cancer
Shi, Y. P., Ye, Z., Lu, G. X., Yang, N., Zhang, J., Wang, L., Cui, J., del Pozo, M. Á., Wu, Y., Xia, D., et al. (2021) · Molecular Therapy — Oncolytics · doi:10.1016/j.omto.2021.10.005 · Cited by 19 · see citing works
Proteomics for Studying the Effects of Ketogenic Diet Against Lithium Chloride/Pilocarpine Induced Epilepsy in Rats
Zheng, Y., Jin, M., Suo, G., Wu, Y., Sun, Y., & Ni, H. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.562853 · Cited by 19 · see citing works
The complexity of extracellular vesicles: Bridging the gap between cellular communication and neuropathology
Tam, S., Wear, D., Morrone, C. D., & Yu, W. H. (2024) · Journal of Neurochemistry · doi:10.1111/jnc.16108 · Cited by 18 · see citing works
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P1–121: SREBP‐2‐mediated cholesterol accumulation regulates beta‐amyloid–induced autophagy in APP/PS1/SREBP‐2 mice
Barbero‐Camps, E., Fernández-Checa, J. C., & Colell, A. (2013) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.05.343
Self-citation
Cholesterol alters mitophagy by impairing optineurin recruitment and lysosomal clearance in Alzheimer’s disease
Agujetas, V. R., Barbero‐Camps, E., de Dios, C., Podlesniy, P., Abadin, X., Morales, A., Marı́, M., Trullás, R., & Colell, A. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00435-6 · Cited by 110 · see citing works
Self-citation
Cholesterol contribution to autophagy and mitophagy impairment in Alzheimer's disease
Agujetas, V. R. (2020) · doi:10.13140/rg.2.2.36355.84002
Additional file 1 of Cholesterol alters mitophagy by impairing optineurin recruitment and lysosomal clearance in Alzheimer’s disease
Agujetas, V. R., Barbero-Camps, E., de Dios, C., Podlesniy, P., Abadin, X., Morales, A., Marı́, M., Trullás, R., & Colell, A. (2021) · Figshare · doi:10.6084/m9.figshare.14183579
Self-citation
Upregulation of brain cholesterol levels inhibits mitophagy in Alzheimer disease
Agujetas, V. R., de Dios, C., Abadin, X., & Colell, A. (2021) · Autophagy · doi:10.1080/15548627.2021.1920814 · Cited by 36 · see citing works
Self-citation

Authors: Barbero-Camps, E., Roca-Agujetas, V., Bartolessis, I., de Dios, C., Fernández-Checa, J. C., Marí, M., Morales, A., Hartmann, T., & Colell, A.
Affiliations: Department of Cell Death and Proliferation, Institut d'Investigacions Biomèdiques de Barcelona, Consejo Superior de Investigaciones Científicas (CSIC), Institut d'Investigacions Biomèdiques August Pi i Sunyer (IDIBAPS), Barcelona, Spain
Consejo Superior de Investigaciones Científicas (ES)
Saarland University (DE)
Corresponding author: Colell, Anna
ORCID: Bartolessis, Isabel
Marí, Montserrat
Morales, Albert
Hartmann, Tobias
Colell, Anna
Venue: Autophagy
Publisher: Informa UK Limited
Published: 2018-06-04
Volume: 14
Issue: 7
Pages: 1129-1154
ISSN: 1554-8627 (ISSN-L)
1554-8635
DOI: 10.1080/15548627.2018.1438807
PMC: PMC6103708
OpenAlex: W2805481194
Cited by: 125
References: 99
Citations by year: 2026: 8 · 2025: 19 · 2024: 10 · 2023: 12 · 2022: 13 · 2021: 19 · 2020: 20 · 2019: 18 · 2018: 5
FWCI: 10.66
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-nd
Locations: Autophagy (publishedVersion, cc-by-nc-nd)
Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
PubMed Central (publishedVersion, cc-by-nc-nd)
PubMed (publishedVersion)
DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion, cc-by-nc-nd)
Funders: Ministerio de Economía y Competitividad (SAF2013-47246-R, SAF2015-66515-R, SAF2015-69944-R)
FEDER
Fundació La Marató de TV3 (2014-0930)
Instituto de Salud Carlos III (PI13/00374, PI16/00930)
US NIAAA (P50-AA-11999)
AGAUR (2014-SGR785)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: cholesterol, amyloid-beta, Alzheimer's disease, presenilin 1, autophagosome-lysosome fusion, amyloid-beta secretion, oxidative stress, mitochondrial glutathione, ATG4B, Rab7, snares, hydroxypropyl-β-cyclodextrin, Niemann-Pick disease type C
MeSH terms: Autophagosomes, Autophagy-Related Proteins, Beclin-1, Sequestosome-1 Protein, 2-Hydroxypropyl-beta-cyclodextrin, Animals, Autophagy, Cholesterol, Cysteine Endopeptidases, Lysosomes, Membrane Fusion, Membrane Proteins, Mitochondria, Endosomes, Signal Transduction, Amyloid beta-Peptides, tau Proteins, Sirolimus, Mice, Sterol Regulatory Element Binding Protein 2, Presenilin-1, TOR Serine-Threonine Kinases

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Cholesterol impairs autophagy-mediated clearance of amyloid beta while promoting its secretion

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