Cited by 184Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsUbiquitin and proteasome pathways

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Reactive glia show increased immunoproteasome activity in Alzheimer’s disease

Orre, Marie, Kamphuis, Willem, Dooves, Stephanie, Kooijman, Lieneke, Chan, Elena T., Kirk, Christopher J., Dimayuga Smith, Vanessa, Koot, Sanne, Mamber, Carlyn, Jansen, Anne H., Ovaa, Huib, Hol, Elly M.·2013·Brain

DOI 10.1093/brain/awt083

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Abstract

The proteasome is the major protein degradation system within the cell, comprised of different proteolytic subunits; amyloid-β is thought to impair its activity in Alzheimer's disease. Neuroinflammation is a prominent hallmark of Alzheimer's disease, which may implicate an activation of the immunoproteasome, a specific proteasome variant induced by immune signalling that holds slightly different proteolytic properties than the constitutive proteasome. Using a novel cell-permeable proteasome activity probe, we found that amyloid-β enhances proteasome activity in glial and neuronal cultures. Additionally, using a subunit-specific proteasome activity assay we showed that in the cortex of the APPswePS1dE9 plaque pathology mouse model, immunoproteasome activities were strongly increased together with increased messenger RNA and protein expression in reactive glia surrounding plaques. Importantly, this elevated activity was confirmed in human post-mortem tissue from donors with Alzheimer's disease. These findings are in contrast with earlier studies, which reported impairment of proteasome activity in human Alzheimer's disease tissue and mouse models. Targeting the increased immunoproteasome activity with a specific inhibitor resulted in a decreased expression of inflammatory markers in ex vivo microglia. This may serve as a potential novel approach to modulate sustained neuroinflammation and glial dysfunction associated with Alzheimer's disease.

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Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
Vandesompele, J., De Preter, K., Pattyn, F., Poppe, B., Van Roy, N., De Paepe, A., & Speleman, F. (2002) · Genome Biology · doi:10.1186/gb-2002-3-7-research0034 · Cited by 20,038
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123
Innate immune recognition
Janeway, C. A., & Medzhitov, R. (2002) · Annual Review of Immunology · doi:10.1146/annurev.immunol.20.083001.084359 · Cited by 8,394
Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
The ubiquitinproteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
Palombella, V. J., Rando, O. J., Goldberg, A. L., & Maniatis, T. (1994) · Cell · doi:10.1016/s0092-8674(94)90482-0 · Cited by 2,089
Protein degradation and protection against misfolded or damaged proteins.
Goldberg, A. L. (2003) · Nature · doi:10.1038/nature02263 · Cited by 2,088
Microglia in neurodegenerative disease
Perry, V. H., Nicoll, J. A. R., & Holmes, C. (2010) · Nature Reviews Neurology · doi:10.1038/nrneurol.2010.17 · Cited by 1,543
Microglial Dysfunction and Defective β-Amyloid Clearance Pathways in Aging Alzheimer's Disease Mice
Hickman, S. E., Allison, E. K., & El Khoury, J. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.0616-08.2008 · Cited by 1,329 · cited 3×
“Sustained immune signalling has previously been shown to lead to reduced levels of amyloid-b recognition receptors and of amyloidb degrading enzymes in microglia from aged Alzheimer’s disease mice (Hickman et al., 2008), as well as a reduction of general cognitive functions (Corona et al., 2011).”
Background
Impaired Proteasome Function in Alzheimer's Disease
Keller, J. N., Hanni, K. B., & Markesbery, W. R. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750436.x · Cited by 848
CD14 is required for MyD88-independent LPS signaling
Jiang, Z., Georgel, P., Du, X., Shamel, L., Sovath, S., Mudd, S., Huber, M., Kalis, C., Keck, S., Galanos, C., et al. (2005) · Nature Immunology · doi:10.1038/ni1207 · Cited by 683

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Arisi, I., D’Onofrio, M., Brandi, R., Cattaneo, A., Bertolazzi, P., Cumbo, F., Felici, G., & Guerra, C. (2015) · BMC Neuroscience · doi:10.1186/s12868-015-0155-5 · Cited by 3
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(2020) · Case Medical Research · doi:10.31525/ct1-nct04274998 · Cited by 2
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Chantong, B., & Nusuetrong, P. (2015) · Cited by 2
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Pickering, A. M., & Miller, R. A. (2019) · Springer eBooks · doi:10.1007/978-3-319-99375-1_111 · Cited by 1
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Anatolou, D., & Krokidis, M. G. (2024) · AIMS neuroscience · doi:10.3934/neuroscience.2024007 · Cited by 1
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Che, J., Wang, A., & Liu, L. (2016) · International Journal of Neurology Research · doi:10.17554/j.issn.2313-5611.2016.02.48 · Cited by 1
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The Development of Novel Proteasome Inhibitors for the Treatment of Multiple Myeloma and Alzheimer's Disease
Lee, M. J. (2019) · UKnowledge (University of Kentucky) · doi:10.13023/etd.2019.169 · Cited by 1
Preservation Analysis on Spatiotemporal Specific Co-expression Networks Suggests the Immunopathogenesis of Alzheimer’s Disease
Guo, L., Liu, Y., & Wang, J. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.727928 · Cited by 1
CCR7+ CD4 T Cell Immunosurveillance Disrupted in Chronic SIV-Induced Neuroinflammation in Rhesus BrainPreprint
Elizaldi, S. R., Hawes, C. E., Verma, A., Dinasarapu, A. R., Lakshmanappa, Y. S., Schlegel, B. T., Rajasundaram, D., Li, J., Durbin-Johnson, B. P., Ma, Z.-M., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.28.555037 · Cited by 1
Modulation of the JAK2/STAT3 pathway in vivo : understanding reactive astrocyte functional features and contribution to neurodegenerative diseases
Haim, L. B. (2014) · theses.fr (ABES) · doi:10.70675/75a69111z994cz43dfzb795zfeae9ffc88ab · Cited by 1
Effects of Aβ42 on the human proteome and compound library screening using cellular models of Alzheimer's disease
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Smith, B. C., Sinyuk, M., Jenkins, J. E., Psenicka, M. W., & Williams, J. L. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2019.12.23.887455
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Faculty Opinions recommendation of Neuroinflammation in Alzheimer's disease.
Perani, D. (2017) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.725413893.793537457
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Maltsev, A. V., Funikov, S. Y., Rezvykh, A. P., Teterina, E. V., Nebogatikov, V. O., Burov, A. V., Bal, N. V., Ustyugov, A. A., Карпов, В. Л., & Morozov, A. V. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24098172
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Additional file 1 of P2X7 receptor inhibition ameliorates ubiquitin–proteasome system dysfunction associated with Alzheimer’s disease
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Nakamura, Y., Labarchède, M., Mendes, T., Nakamura, Y., Longueville, S., Albertini, G., Marion‐Poll, L., Mariani, L., Hervé, D., Roumier, A., et al. (2025) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2025.111574
Additional file 2 of P2X7 receptor inhibition ameliorates ubiquitin–proteasome system dysfunction associated with Alzheimer’s disease
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Khan, S. S., & Khatri, D. K. (2026) · Springer eBooks · doi:10.1007/978-981-95-6099-8_8
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Abjean, L. (2019) · theses.fr (ABES) · doi:10.70675/f664e003zf93fz467eza6a3z3d953eaffe4e
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Riquelme‐Perez, M. (2023) · theses.fr (ABES) · doi:10.70675/72aad0d8z36a8z4a7azb1eaze65fa79463da
Hétérogénéité et régulation des astrocytes dans la maladie d'Alzheimer : vers des interventions ciblées sur les voies JAK2-STAT3 et NF-kB
Poulot-Becq-Giraudon, Y. (2024) · theses.fr (ABES) · doi:10.70675/0d7a8b92z8393z4d76z82a8z87efe0790346
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Hu, W.-F., Lee, C.-H., Huang, H.-Y., Pang, C., Wu, Y., Lin, T., Lin, P. B., Tsai, S., Lin, C.-H., & Liew, H. (2026) · Cells · doi:10.3390/cells15080664
Pharmacokinetics, Target Engagement of an Immunoproteasome Subunit Low-Molecular-Mass Polypeptide-2 (LMP2) Inhibitor AR-01, and Its Anti-Alzheimer’s Effects in Rodents
Magar, T. B. T., Kim, M., Kim, Y., Choi, E. Y., Choi, Y. K., Kim, D. K., Kim, K. B., & Park, J. E. (2026) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.6c00116
Association between Alzheimer’s disease and MHC-I antigen processing and presentation pathway: a narrative review
Wang, C., Yun, Q. I., Zhang, Z., Zhao, H., Lin, F., & Cao, H. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1877167
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Mao, Y., Ma, R., Lin, Z., Zhao, H., Liu, Y., Su, Y., Zhang, X., & Chen, X. (2026) · Advanced Science · doi:10.1002/advs.202523902
BindingDB Entry 50007932: The Immunoproteasome: An Emerging Target in Cancer and Autoimmune and Neurological Disorders.
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BindingDB Entry 50021052: Brain-Permeable Immunoproteasome-Targeting Macrocyclic Peptide Epoxyketones for Alzheimer's Disease.
BindingDB (2025) · UC San Diego · doi:10.7270/q2w09bjd
BindingDB Entry 50014225: Macrocyclic Immunoproteasome Inhibitors as a Potential Therapy for Alzheimer's Disease.
BindingDB (2022) · UC San Diego · doi:10.7270/q2rx9gwm
BindingDB Entry 50010377: LMP2 Inhibitors as a Potential Treatment for Alzheimer's Disease.
BindingDB (2021) · UC San Diego · doi:10.7270/q2hh6pm2

Authors: Orre, M., Kamphuis, W., Dooves, S., Kooijman, L., Chan, E. T., Kirk, C. J., Dimayuga Smith, V., Koot, S., Mamber, C., Jansen, A. H., Ovaa, H., & Hol, E. M.
Affiliations: Netherlands Institute for Neuroscience (NL)
The Netherlands Cancer Institute (NL)
ORCID: Dooves, Stephanie
Ovaa, Huib
Hol, Elly M.
Venue: Brain
Publisher: Oxford University Press (OUP)
Published: 2013-04-19
Volume: 136
Issue: 5
Pages: 1415-1431
ISSN: 0006-8950 (ISSN-L)
1460-2156
DOI: 10.1093/brain/awt083
OpenAlex: W2034724560
Cited by: 180
References: 66
Citations by year: 2026: 13 · 2025: 13 · 2024: 14 · 2023: 16 · 2022: 10 · 2021: 17 · 2020: 11 · 2019: 19 · 2018: 13 · 2017: 11 · 2016: 14 · 2015: 10 · 2014: 14 · 2013: 5
FWCI: 9.98
Type: journal article
Language: en
Open access: closed
Locations: Brain (publishedVersion)
PubMed (publishedVersion)
KNAW research portal (Royal Academy of Art and Sciences (KNAW)) (publishedVersion)
Data Archiving and Networked Services (DANS) (submittedVersion)
VU Research Portal (submittedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: immunoproteasome, Alzheimer's disease, reactive glia, neuroinflammation, amyloid-beta, proteasome activity, microglia, amyloid plaques, proteasome inhibitors, glial dysfunction
MeSH terms: Adult, Aged, Aged, 80 and over, Alzheimer Disease, Animals, Cells, Cultured, Enzyme Activation, Female, Humans, Male, Mice, Transgenic, Middle Aged, Neuroglia, Tumor Cells, Cultured, Proteasome Endopeptidase Complex, Mice

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Reactive glia show increased immunoproteasome activity in Alzheimer’s disease

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