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Mechanisms of Aβ Clearance and Degradation by Glial Cells
Open accessAbstract
Glial cells have a variety of functions in the brain, ranging from immune defense against external and endogenous hazardous stimuli, regulation of synaptic formation, calcium homeostasis, and metabolic support for neurons. Their dysregulation can contribute to the development of neurodegenerative disorders, including Alzheimer's disease (AD). One of the most important functions of glial cells in AD is the regulation of Amyloid-β (Aβ) levels in the brain. Microglia and astrocytes have been reported to play a central role as moderators of Aβ clearance and degradation. The mechanisms of Aβ degradation by glial cells include the production of proteases, including neprilysin, the insulin degrading enzyme, and the endothelin-converting enzymes, able to hydrolyse Aβ at different cleavage sites. Besides these enzymes, other proteases have been described to have some role in Aβ elimination, such as plasminogen activators, angiotensin-converting enzyme, and matrix metalloproteinases. Other relevant mediators that are released by glial cells are extracellular chaperones, involved in the clearance of Aβ alone or in association with receptors/transporters that facilitate their exit to the blood circulation. These include apolipoproteins, α2macroglobulin, and α1-antichymotrypsin. Finally, astrocytes and microglia have an essential role in phagocytosing Aβ, in many cases via a number of receptors that are expressed on their surface. In this review, we examine all of these mechanisms, providing an update on the latest research in this field.
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“Microglia activation reduces the accumulation of Aβ in the brain by increasing its phagocytosis, clearance, and degradation75.”
From Chlamydia pneumoniae can infect the central nervous system via the olfactory and trigeminal nerves and contributes to Alzheimer’s disease risk (2022) · cites this paper as [75]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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“The secretion of Aβ may thus be a normal immune response to any microbe that may invade the nervous system, and if infection clears, the deposited Aβ can be cleared by phagocytic glia71.”
From Chlamydia pneumoniae can infect the central nervous system via the olfactory and trigeminal nerves and contributes to Alzheimer’s disease risk (2022) · cites this paper as [71]
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“Astrocytes can produce Aβ peptidases, such as neprilysin and IDE as well as the Apolipoprotein E (ApoE) [15]”
From Pharmacological ablation of astrocytes reduces Aβ degradation and synaptic connectivity in an ex vivo model of Alzheimer’s disease (2021) · cites this paper as [15]
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“Neprilysin is mainly expressed in neurons [32] but can also be found in activated astrocytes and microglia [15]”
From Pharmacological ablation of astrocytes reduces Aβ degradation and synaptic connectivity in an ex vivo model of Alzheimer’s disease (2021) · cites this paper as [15]
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“ApoE is mainly produced in astrocytes but can be synthesized by microglia [15].”
From Pharmacological ablation of astrocytes reduces Aβ degradation and synaptic connectivity in an ex vivo model of Alzheimer’s disease (2021) · cites this paper as [15]
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“Indeed, microglia and astrocytes have been shown to play a key role in Aβ clearance and degradation [92].”
From Senescence-related impairment of autophagy induces toxic intraneuronal amyloid-β accumulation in a mouse model of amyloid pathology (2023) · cites this paper as [92]
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Cites
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Wang, Y., Cella, M., Mallinson, K., Ulrich, J. D., Young, K. L., Robinette, M. L., Gilfillan, S., Krishnan, G. M., Sudhakar, S., Zinselmeyer, B. H., et al. (2015) · Cell · doi:10.1016/j.cell.2015.01.049 · Cited by 1,736
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Tang, Y., Zhang, D., Gong, X., & Zheng, J. (2021) · Biophysical Chemistry · doi:10.1016/j.bpc.2021.106735 · Cited by 66
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“…of APP expression and the APP-cleaving secretases, or 2) by modulating clearance of Aβ, for instance by changes in transportation to the periphery or by altering the rate of phagocytosis by immune cells (Chesser et al., 2013; Deane et al., 2009; Martin et al., 2013; Ries and Sastre, 2016).”
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The Amyloid-Beta Clearance: From Molecular Targets to Glial and Neural Cells
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“Although opinions about the role of MG and AC are controversial, most researchers consider them immunostimulators after exposure to Aβ plaques by their toll-like surface receptors (TLRs) (TLR 2, TLR4, TLR6, and TLR9) and CD markers (CD36, CD14, and CD47) [83, 84].”
BackgroundRelationship between the cGAS−STING and NF-κB pathways-role in neurotoxicity
Zhong, S., Zhou, Q., Yang, J., Zhang, Z., Zhang, X., Liu, J., Chang, X., & Wang, H. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116698 · Cited by 66
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“Since astroglia play a role in Ab clearance (Ries and Sastre 2016), the elevated astrogliotic inflammatory response, particularly in AbPP/PS1 HFD mice, may have prevented additional plaque accumulation.”
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“degradation of gangliosides at the plaque periphery, but not in the center of the Aβ plaques [46, 67].”
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Lyu, J., Jiang, X., Leak, R. K., Shi, Y., Hu, X., & Chen, J. (2020) · Translational Stroke Research · doi:10.1007/s12975-020-00857-2 · Cited by 63
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“…development of neurodegenerative diseases (Bellucci et al., 2004; Hickman et al., 2008; Meyer-Luehmann et al., 2008; Sasaki et al., 2008; Zilka et al., 2009; Nalivaeva et al., 2012; Ries and Sastre, 2016; Perea et al., 2018a, 2020; Španíc et al., 2019; Jin et al., 2021; d’Errico et al., 2022).”
BackgroundInterleukin-4 affects microglial autophagic flux
Tang, R.-H., Qi, R.-Q., & Liu, H.-Y. (2019) · Neural Regeneration Research · doi:10.4103/1673-5374.255975 · Cited by 59
“…by IL-4, and partly reduced by blocking autophagy, indicating that IL-4 may mediate Aβ uptake and degradation through other mechanisms such as neprilysin (Doens and Fernandez, 2014), insulin-degrading enzyme (Lee and Landreth, 2010), or the ubiquitin-proteasome system (Ries and Sastre, 2016).”
BackgroundIridoids and other monoterpenes in the Alzheimer’s brain: Recent development and future prospects
Habtemariam, S. (2018) · Molecules · doi:10.3390/molecules23010117 · Cited by 55
Potential neurotoxic activity of diverse molecules released by microglia
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The role of glial autophagy in Alzheimer’s disease
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“In Alzheimer’s disease (AD), microglial phagocytosis of oligomeric and aggregated forms of amyloid beta (Aβ) is one of the key means by which amyloid burden is limited [26, 27].”
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“NEP is also over-expressed in Astrocytes surrounding Amyloid plaques [125].”
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The role of glia in protein aggregation
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“They are expressed by reactive astrocytes surrounding amyloid plaques in AD mouse models (Ries and Sastre, 2016).”
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Tipping points in neurodegeneration
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“24 Recently, it is reported that multi-sensory gamma stimulation can ameliorate Alzheimer's-associated pathology and improves cognition, enhancing microglial recruitment around the plaques and promoting of the A b phagocytosis and clearance played important roles in this process.”
Enhanced delivery of a low dose of aducanumab via FUS in 5×FAD mice, an AD model
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“Combined treatment with FUS and Adu induced activation of phagocytic microglia and increased astrocytes associated with amyloid plaques in the hippocampi of 5×FAD mice Microglia and astrocytes clear pathological deposits of molecules such as Aβ through phagocytosis and degradation in the central nervous system (CNS) […”
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“Astrocytes have been shown to contribute to both Aβ production and clearance (Kraft et al., 2013; Ries & Sastre, 2016) and also be significant targets themselves for Aβ toxicity.”
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Alzheimer’s Disease: What Can We Learn From the Peripheral Olfactory System?
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“…with either Aβ40 or Aβ42, the sustentacular cells clearly contain these protein fragments, perhaps indicating their potential role in the uptake and phagocytosis of Aβ (Cao et al., 2012b), similar to the role played in the brain by microglia, astrocytes, and macrophages (Ries and Sastre, 2016).”
BackgroundOptical Nanosensor for Intracellular and Intracranial Detection of Amyloid-Beta
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Alzheimer’s Disease: From Immune Homeostasis to Neuroinflammatory Condition
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Stereo-seq of the prefrontal cortex in aging and Alzheimer’s disease
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“Furthermore, Ast and microglia (Mic) surrounding highly stressed neurons become reactivated and play a crucial role in the processes of A β clearance and neuroprotection 65 .”
Phytosterols: Targeting Neuroinflammation in Neurodegeneration
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“While astrocyte reactivity is associated with amyloid beta (Aβ) plaques [3], the precise role of this astrocyte reactivity in neurodegeneration is still unclear.”
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Astrocytes and Adenosine A2A Receptors: Active Players in Alzheimer’s Disease
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“, lipoprotein receptorrelated ligand 1, receptor for advanced glycation end products (RAGE), scavenger receptors); (ii) reduced capacity to degrade the internalized Aβ, which involves the production of proteases, such as neprilysin, insulin-degrading enzyme, and enzymes of the ubiquitin-proteasome system (reviewed in…”
BackgroundJia, W., Su, Q., Cheng, Q., Peng, Q., Qiao, A., Luo, X., Zhang, J., & Wang, Y. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/9966223 · Cited by 45
“Once there is an imbalance between the production and clearance of amyloid-β peptide (Aβ), the accumulation of Aβ initiates self-assembly and the self-assembled Aβ then turns into toxic oligomers, large Aβ fibrils, and plaques associated with the onset and progression of Alzheimer’s disease (AD) [1, 2].”
BackgroundSuelves, N., Saleki, S., Ibrahim, T., Palomares, D., Moonen, S., Koper, M. J., Vrancx, C., Vadukul, D. M., Papadopoulos, N., Viceconte, N., et al. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01578-x · Cited by 43
“Indeed, microglia and astrocytes have been shown to play a key role in Aβ clearance and degradation [92].”
BackgroundThe multifaceted role of WNT signaling in Alzheimer’s disease onset and age-related progression.
Kostes, W. W., & Brafman, D. A. (2023) · Cells · doi:10.3390/cells12081204 · Cited by 43
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Bhargavan, B., Woollard, S. M., Mcmillan, J. E. M., & Kanmogne, G. D. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00500-0 · Cited by 45
Brain Glymphatic/Lymphatic Imaging by MRI and PET
Lee, D. S., Suh, M., Sarker, A. K., & Choi, Y. (2020) · Nuclear Medicine and Molecular Imaging · doi:10.1007/s13139-020-00665-4 · Cited by 45
“The clearance of toxic amyloid solutes and pathologic extracellular tau is supposed to take place by four different plausible mechanisms [89, 90], which are (1) protease and enzymatic activity in situ within or outside of the neurons, (2) by the support of the other neurons or more likely the”
BackgroundComplex roles for reactive astrocytes in the triple transgenic mouse model of Alzheimer disease
Guillemaud, O., Ceyzériat, K., Saint-Georges, T., Cambon, K., Petit, F., Haim, L. B., Sauvage, M.-A. C.-D., Guillermier, M., Bernier, S., Hérard, A., et al. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2020.02.010 · Cited by 40
Patient-Derived Midbrain Organoids to Explore the Molecular Basis of Parkinson's Disease
Galet, B., Cheval, H., & Ravassard, P. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.01005 · Cited by 47
“Furthermore, while glial cells play an essential role of clearance in disorders such as PD and AD [see reviews (95, 96)], gliogenesis mainly happens in later stages of organoid culture (after 6 months in forebrain organoids) (97), and typically does not include microglial cells, unless differentiation protocols favor…”
BackgroundDomínguez-Prieto, M., Velasco, A. L., Tabernero, A., & Medina, J. M. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180332 · Cited by 43
Tajbakhsh, A., Read, M. I., Barreto, G. E., Ávila-Rodriguez, M., Hayat, S. M. G., & Sahebkar, A. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.173873 · Cited by 41
Du, S., Jin, F., Maneix, L., Gedam, M., Xu, Y., Catic, A., Wang, M. C., & Zheng, H. (2021) · Aging Cell · doi:10.1111/acel.13432 · Cited by 43
“It has been shown that astrocytes could take up extracellular Aβ species to facilitate their clearance (Ries & Sastre, 2016).”
BackgroundDurand, D., Carniglia, L., Turati, J., Ramírez, D., Saba, J., Caruso, C. M., & Lasaga, M. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.05.008 · Cited by 41
“Oligomeric and fibrillar Ab are primarily internalized through receptor-mediated endocytosis (reviewed in (Ries and Sastre, 2016)).”
InfluentialAfsar, A., Castro, M. D. C. C., Soladogun, A. S., & Li, Z. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087258 · Cited by 45
BACE1 regulates expression of Clusterin in astrocytes for enhancing clearance of β-amyloid peptides
Zhou, J., Singh, N., Galske, J., Hudobenko, J., Hu, X., & Yan, R. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00611-w · Cited by 39
“Reactive astrocytes contribute to amyloid clearance, directly by endocytosis [39] or producing amyloid degrading enzymes [40, 41], and indirectly by preventing amyloid aggregation [42, 43] or enhancing clearance by other cell types [44, 45].”
BackgroundCorraliza-Gómez, M., Bermejo, T., Lilue, J., Rodríguez-Iglesias, N., Valero, J., Cózar‐Castellano, I., Arranz, E. M., Sánchez, D., & Ganfornina, M. D. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02914-7 · Cited by 39
“There are other intracellular mechanisms worth further study, such as intracellular proteases, the ubiquitin– proteasome system or the autophagy pathway [78], that might be altered when IDE is absent in microglia.”
BackgroundTakata, K., Ginhoux, F., & Shimohama, S. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114754 · Cited by 40
Phenylpropanoids and Alzheimer's disease: A potential therapeutic platform
Kolaj, I., Liyanage, S. I., & Weaver, D. F. (2018) · Neurochemistry International · doi:10.1016/j.neuint.2018.08.001 · Cited by 39
“These cells serve important developmental and maintenance roles, and are thus initially activated as a neuroprotective response to early AD pathologies (Barger and Harmon, 1997; Farina et al., 2007; Frautschy et al., 1998; Guillot-Sestier et al., 2015; Ries and Sastre, 2016).”
Ceyzériat, K., Zilli, T., Fall, A. B., Millet, P., Koutsouvelis, N., Dipasquale, G., Frisoni, G. B., Tournier, B. B., & Garibotto, V. (2021) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2021.03.008 · Cited by 36
Tropea, M. R., Puma, D. D. L., Melone, M., Gulisano, W., Arancio, O., Grassi, C., Conti, F., & Puzzo, D. (2021) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2021.102154 · Cited by 42
“, 2005) but also participate in Aβ clearance in physiological conditions (Mulder et al., 2012; Ries and Sastre, 2016).”
BackgroundDiminished stress resistance and defective adaptive homeostasis in age-related diseases
Lomeli, N., Bota, D. A., & Davies, K. J. A. (2017) · Clinical Science · doi:10.1042/cs20160982 · Cited by 39
Kaminari, A., Tsilibary, E. C., & Tzinia, A. K. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180035 · Cited by 39
Targeting Beta-Amyloid at the CSF: A New Therapeutic Strategy in Alzheimer’s Disease
Menéndez‐González, M., Padilla-Zambrano, H., Alvarez, G., Capetillo‐Zarate, E., Tomás‐Zapico, C., & Costa, A. D. D. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00100 · Cited by 38
“…al., 2017; Zuroff et al., 2017), including drainage to the vascular and glymphatic systems (DeMattos et al., 2001; Iliff et al., 2012, 2013; Tarasoff-Conway et al., 2015; Bakker et al., 2016; Zuroff et al., 2017), and in situ degradation by glial cells (Ries and Sastre, 2016; Zuroff et al., 2017).”
BackgroundInfluentialCheng, Z.-Y., Xia, Q.-P., Hu, Y., Wang, C., & He, L. (2020) · International Immunopharmacology · doi:10.1016/j.intimp.2020.106963 · Cited by 38
Alzheimer’s Disease: From Pathogenesis to Mesenchymal Stem Cell Therapy – Bridging the Missing Link
Hu, J., & Wang, X. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.811852 · Cited by 42
“Furthermore, astrocytes express aquaporin 4 (AQP4) water channels in their vascular end-feet and play an essential role in the glymphatic system implicated in the clearance of beta-amyloid (Ries and Sastre, 2016).”
BackgroundThe chaperone Clusterin in neurodegeneration−friend or foe?
Yuste‐Checa, P., Bracher, A., & Hartl, F. U. (2022) · BioEssays · doi:10.1002/bies.202100287 · Cited by 37
Xiao, S., Liu, Y.-J., Wang, L., Sha, Z., Che, X., Yu, Z., & Lee, S. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.875138 · Cited by 41
“At the early stage of AD, astrocytes serve as a protector of the neuro system to digest accumulated Aβ and transport it out of the BBB with the facilitation of chaperones, one type of heat shock proteins (Ries and Sastre, 2016).”
BackgroundEvidence for aggregation-independent, PrP C -mediated Aβ cellular internalization
Foley, A. R., Roseman, G. P., Chan, K., Smart, A., Finn, T. S., Yang, K., Lokey, R. S., Millhauser, G. L., & Raskatov, J. A. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2009238117 · Cited by 38
“S. Jin et al., Amyloid-β(1-42) aggregation initiates its cellular uptake and cytotoxicity.”
BackgroundInfluentialYang, E.-J., Kim, H.-J., Choi, Y., Kim, H. J., Kim, J. H., Yoon, J., Seo, Y.-S., & Kim, H.-S. (2021) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2021.06.012 · Cited by 36
Molecular crowding facilitates bundling of IMPDH polymers and cytoophidium formation
Chang, C., Peng, M., Zhong, J., Zhang, Z., Keppeke, G. D., Sung, L., & Liu, J. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04448-2 · Cited by 36
Ferreira, M., Francisco, S., Soares, A. R., Nobre, A., Pinheiro, M. M., Reis, A., Neto, S. C., Rodrigues, A. J., Sousa, N., Moura, G. R., et al. (2021) · Aging · doi:10.18632/aging.203379 · Cited by 34
Zhang, S.-S., Gao, Z., Feng, L., & Li, M. (2024) · Journal of Inflammation Research · doi:10.2147/jir.s483412 · Cited by 39
“135,136 Research indicates that astrocytes exhibit dual responses to AD, depending on the specific stimulatory factors involved.”
BackgroundChen, C., Huang, L., Nong, Z., Li, Y., Chen, W., Huang, J., Pan, X., Wu, G., & Lin, Y. (2017) · Neurochemical Research · doi:10.1007/s11064-016-2166-8 · Cited by 35
The Interplay Between Apolipoprotein E4 and the Autophagic–Endocytic–Lysosomal Axis
Schmukler, E., Michaelson, D. M., & Pinkas-Kramarski, R. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0892-4 · Cited by 35
Pro- and Anti-inflammatory Effects of High Cholesterol Diet on Aged Brain
Chen, Y., Yin, M., Cao, X., Hu, G., & Xiao, M. (2018) · Aging and Disease · doi:10.14336/ad.2017.0706 · Cited by 38
“Glia play an important role in maintaining the homeostasis of brain, such as phagocytosis and elimination of the harmful metabolites [52].”
BackgroundAstrocyte subtype-specific approach to Alzheimer's disease treatment
Sarkar, S., & Biswas, S. C. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.104956 · Cited by 35
López-Gambero, A. J., Rosell‐Valle, C., Vera, D. M., Navarro, J. A., Vargas, A., Rivera, P., Sanjuan, C., de Fonseca, F. R., & Suárez, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22105365 · Cited by 37
Lecordier, S., Pons, V., Rivest, S., & ElAli, A. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2021.813536 · Cited by 34
Molecular basis of selective amyloid‐β degrading enzymes in Alzheimer's disease
Żukowska, J., Moss, S. J., Subramanian, V., & Acharya, K. R. (2023) · FEBS Journal · doi:10.1111/febs.16939 · Cited by 36
“It is now known that A b level in the brain is maintained due to a dynamic equilibrium between its production from the APP and removal by amyloid clearance proteins (for recent reviews see references [56 – 59]).”
Guo, S., Cázarez‐Márquez, F., Jiao, H., Foppen, E., Korpel, N. L., Grootemaat, A. E., Liv, N., Gao, Y., van der Wel, N. N., Zhou, B., et al. (2022) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c22434 · Cited by 35
Hickey, J. P., Collins, A. E., Nelson, M. L., Chen, H., & Kalisch, B. E. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46050266 · Cited by 39
“…on myeloid cells 2 (TREM2), and lipoprotein receptor-related proteins (LRPs) when complexed with lipoproteins, and microglia can further process these fibrils through phagocytosis or upregulated proteinase activity with insulin-degrading enzyme (IDE) or metalloproteinase-9 (MMP-9) [58–61].”
BackgroundThe roles of cortical astrocytes in chronic pain and other brain pathologies
Eto, K., Kim, S. K., Takeda, I., & Nabekura, J. (2017) · Neuroscience Research · doi:10.1016/j.neures.2017.08.009 · Cited by 32
APOE2 mitigates disease-related phenotypes in an isogenic hiPSC-based model of Alzheimer’s disease
Brookhouser, N., Raman, S., Frisch, C., Srinivasan, G., & Brafman, D. A. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01076-3 · Cited by 33
“It has been well documented that astrocytes play a critical role in regulating the extracellular levels of Aβ through multiple clearance mechanisms [55].”
BackgroundThe Potential Role of Protein Kinase R as a Regulator of Age-Related Neurodegeneration
Martínez, N. W., Gómez, F. E., & Matus, S. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.638208 · Cited by 31
Serebrovska, Z. O., Xi, L., Tumanovska, L. V., Shysh, A. M., Goncharov, S. V., Khetsuriani, M., Kozak, T. O., Pashevin, D. O., Dosenko, V., Virko, S. V., et al. (2022) · Life · doi:10.3390/life12030432 · Cited by 34
Ahn, E. H., & Park, J. (2025) · Cells · doi:10.3390/cells14020089 · Cited by 37
“In the early phases of AD, microglia activated by A β attempt to eliminate A β deposits by inducing CD36 expression and stimulating phagocytosis in astrocytes and microglia [103,107,108].”
Genetic Variability in Molecular Pathways Implicated in Alzheimer's Disease: A Comprehensive Review
Vogrinc, D., Goričar, K., & Dolžan, V. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.646901 · Cited by 32
“Normally, Aβ plaques are being degraded and cleared in processes driven by glial cells (Ries and Sastre, 2016).”
BackgroundMetabolite Clearance During Wakefulness and Sleep
Hladky, S. B., & Barrand, M. A. (2017) · Handbook of experimental pharmacology · doi:10.1007/164_2017_37 · Cited by 36
“…insulin degrading enzyme (IDE) and matrix metalloproteases (MMPs) (Iwata et al. 2000, 2001; Van Uden et al. 2002; Tanzi et al. 2004; Saido and Iwata 2006; Farris et al. 2007; Bu 2009; Miners et al. 2011; Saido and Leissring 2012; Kanekiyo et al. 2013; McIntee et al. 2016; Ries and Sastre 2016).”
InfluentialGossypetin ameliorates 5xFAD spatial learning and memory through enhanced phagocytosis against Aβ
Jo, K. W., Lee, D., Cha, D. G., Oh, E.-J., Choi, Y. H., Kim, S., Park, E. S., Kim, J. K., & Kim, K. (2022) · Alzheimer s Research & Therapy · doi:10.1186/s13195-022-01096-3 · Cited by 33
Metadata
- Authors
- Ries, M., & Sastre, M.
- Affiliations
- Hammersmith Hospital (GB)
- Corresponding author
- Sastre, Magdalena
- Venue
- Frontiers in Aging Neuroscience
- Publisher
- Frontiers Media SA
- Published
- 2016-07-05
- Volume
- 8
- Pages
- 160-160
- ISSN
- 1663-4365 (ISSN-L)
- PMC
- PMC4932097
- OpenAlex
- W2460612985
- Cited by
- 527
- References
- 122
- Citations by year
- 2026: 32 · 2025: 53 · 2024: 62 · 2023: 60 · 2022: 77 · 2021: 76 · 2020: 57 · 2019: 47 · 2018: 32 · 2017: 31
- FWCI
- 4.31
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Frontiers in Aging Neuroscience (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Spiral (Imperial College London) (submittedVersion, other-oa)
- Funders
- Medical Research Council
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Clinical Neurology › Cerebrospinal fluid and hydrocephalus
- Keywords
- amyloid-beta clearance, amyloid beta degradation, glial cells, microglia, astrocytes, Alzheimer's disease, neprilysin, insulin-degrading enzyme, endothelin-converting enzyme, matrix metalloproteinases, plasminogen activator, angiotensin-converting enzyme, extracellular chaperones, apolipoproteins, alpha2-macroglobulin, alpha-1-antichymotrypsin, phagocytosis
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