Cytokine-Mediated Inhibition of Fibrillar Amyloid-β Peptide Degradation by Human Mononuclear Phagocytes

Yamamoto, Masaru; Kiyota, Tomomi; Walsh, Shannon M; Liu, Jianuo; Kipnis, Jonathan; Ikezu, Tsuneya

doi:10.4049/jimmunol.181.6.3877

Cited by 100Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsDementia and Cognitive Impairment Research

Cytokine-Mediated Inhibition of Fibrillar Amyloid-β Peptide Degradation by Human Mononuclear Phagocytes

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Yamamoto, Masaru, Kiyota, Tomomi, Walsh, Shannon M, Liu, Jianuo, Kipnis, Jonathan, Ikezu, Tsuneya·2008·The Journal of Immunology

DOI 10.4049/jimmunol.181.6.3877PMC PMC2603577

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Abstract

Vaccination therapy of AD animal models and patients strongly suggests an active role of brain mononuclear phagocytes in immune-mediated clearance of amyloid-beta peptides (Abeta) in brain. Although Abeta uptake by macrophages can be regulated by pro- and anti-inflammatory cytokines, their effects on macrophage-mediated Abeta degradation are poorly understood. To better understand this mechanism of degradation, we examined whether pro- and anti-inflammatory cytokines affect the degradation of Abeta using primary cultured human monocyte-derived macrophages (MDM) and microglia using pulse-chase analysis of fibrillar and oligomer (125)I-Abeta40 and Abeta42. Initial uptake of fibrillar Abeta40 and Abeta42 was 40% and its degradation was saturated by 120 h in both MDM and microglia, compared with an initial uptake of oligomeric Abeta less than 0.5% and saturation of degradation within 24 h. IFN-gamma increased the intracellular retention of fibrillar Abeta40 and Abeta42 by inhibiting degradation, whereas IL-4, IL-10, and TGF-beta1, but not IL-13 and IL-27, enhanced degradation. Fibrillar Abeta degradation in MDM is sensitive to lysosomal and insulin degrading enzyme inhibitors but insensitive to proteasomal and neprilysin inhibitors. IFN-gamma and TNF-alpha directly reduced the expression of insulin degrading enzyme and chaperone molecules (heat shock protein 70 and heat shock cognate protein 70), which are involved in refolding of aggregated proteins. Coculture of MDM with activated, but not naive T cells, suppressed Abeta degradation in MDM, which was partially blocked by a combination of neutralizing Abs against proinflammatory cytokines. These data suggest that proinflammatory cytokines suppress Abeta degradation in MDM, whereas select anti-inflammatory and regulatory cytokines antagonize these effects.

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TNFα has been shown to directly reduce microglial expression of Aβ-degrading enzymes such as insulin-degrading enzyme and neprilysin.
“TNF␣ has been shown to directly reduce microglial expression of A␤-degrading enzymes such as insulin-degrading enzyme and neprilysin.51,52”
From CX3CR1 Deficiency Alters Microglial Activation and Reduces Beta-Amyloid Deposition in Two Alzheimer's Disease Mouse Models (2010) · cites this paper as [51]
The Results section on IDE expression reports that TNF-α combined with IFN-γ reduced IDE expression in monocyte-derived macrophages, but TNF-α alone had no effect. The microglia Results section measures Aβ degradation, not enzyme expression; the copy does not report reduced microglial expression of IDE or neprilysin. (LLM, conf=0.90)
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In the AD brain, chronic activation of microglia is associated with inflammatory cytokines including TNFα that can substantially block the ability of microglia to remove or degrade Aβ.
“Within the AD brain, there is a chronic activation of microglia associated with inflammatory cytokines including TNF␣ that can substantially block of ability of the microglia to remove 47,49,50 or degrade A␤. 51,52”
From CX3CR1 Deficiency Alters Microglial Activation and Reduces Beta-Amyloid Deposition in Two Alzheimer's Disease Mouse Models (2010) · cites this paper as [51]
The Results report that TNF-α reduced a measure of fibrillar Aβ42 degradation in cultured human microglia. The Discussion says pro-inflammatory cytokines suppressed Aβ degradation in microglia, mainly through IFN-γ, but that the microglial response was small. The study does not establish substantial inhibition in chronically activated microglia within the AD brain. (LLM, conf=0.88)
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Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160 · see citing works
Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease
Morgan, D., Diamond, D. M., Gottschall, P. E., Ugen, K. E., Dickey, C. A., Hardy, J., Duff, K., Jantzen, P. T., DiCarlo, G., Wilcock, D. M., et al. (2000) · Nature · doi:10.1038/35050116 · Cited by 1,488 · see citing works
Subacute meningoencephalitis in a subset of patients with AD after Aβ42 immunization
Orgogozo, J.-M., Gilman, S., Dartigues, J.-F., Laurent, B., Puel, M., Kirby, L. C., Jouanny, P., Dubois, B., Eisner, L., Flitman, S., et al. (2003) · Neurology · doi:10.1212/01.wnl.0000073623.84147.a8 · Cited by 1,356 · see citing works
Metabolic Regulation of Brain Aβ by Neprilysin
Iwata, N., Tsubuki, S., Takaki, Y., Shirotani, K., Lu, B., Gerard, N., Gerard, C., Hama, E., Lee, H., & Saido, T. (2001) · Science · doi:10.1126/science.1059946 · Cited by 894 · see citing works
Identification of the major Aβ1–42-degrading catabolic pathway in brain parenchyma: Suppression leads to biochemical and pathological deposition
Iwata, N., Tsubuki, S., Takaki, Y., Watanabe, K., Sekiguchi, M., Hosoki, E., Kawashima-Morishima, M., Lee, H.-J., Hama, E., Sekine-Aizawa, Y., et al. (2000) · Nature Medicine · doi:10.1038/72237 · Cited by 867 · see citing works
Insulin-degrading Enzyme Regulates Extracellular Levels of Amyloid β-Protein by Degradation
Qiu, W. Q., Walsh, D. M., Ye, Z., Vekrellis, K., Zhang, J., Podlisny, M. B., Rosner, M. R., Safavi, A., Hersh, L. B., & Selkoe, D. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.49.32730 · Cited by 812 · see citing works
A dominant function for interleukin 27 in generating interleukin 10–producing anti-inflammatory T cells
Awasthi, A., Carrier, Y., Peron, J. P. S., Bettelli, E., Kamanaka, M., Flavell, R. A., Kuchroo, V. K., Oukka, M., & Weiner, H. L. (2007) · Nature Immunology · doi:10.1038/ni1541 · Cited by 804 · see citing works
Efficient isolation and propagation of human immunodeficiency virus on recombinant colony-stimulating factor 1-treated monocytes.
Gendelman, H. E., Orenstein, J. M., Martin, M. A., Ferrua, C., Mitra, R., Phipps, T. J., Wahl, L. A., Lane, H. C., Fauci, A. S., & Burke, D. (1988) · The Journal of Experimental Medicine · doi:10.1084/jem.167.4.1428 · Cited by 781 · see citing works
Antibodies against β-Amyloid Slow Cognitive Decline in Alzheimer's Disease
Höck, C., Konietzko, U., Streffer, J. R., Tracy, J., Signorell, A., Müller-Tillmanns, B., Lemke, U., Henke, K., Moritz, E., Garcia, E., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00294-0 · Cited by 777 · see citing works
TGF-β1 promotes microglial amyloid-β clearance and reduces plaque burden in transgenic mice
Wyss-Coray, T., Lin, C., Yan, F., Yu, G.-Q., Rohde, M., McConlogue, L., Masliah, E., & Mucke, L. (2001) · Nature Medicine · doi:10.1038/87945 · Cited by 587 · see citing works
Self-Assembly of Aβ 1 - 42 into Globular Neurotoxins
Chromy, B. A., Nowak, R. J., Lambert, M. P., Viola, K. L., Chang, L., Velasco, P. T., Jones, B. W., Fernandez, S. J., Lacor, P. N., Horowitz, P., et al. (2003) · Biochemistry · doi:10.1021/bi030029q · Cited by 522 · see citing works
Epitope and isotype specificities of antibodies to β-amyloid peptide for protection against Alzheimer's disease-like neuropathology
Bard, F., Barbour, R., Cannon, C., Carretto, R., Fox, M., Games, D., Guido, T., Hoenow, K., Hu, K., Johnson-Wood, K., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0436286100 · Cited by 411 · see citing works
Glatiramer acetate fights against Alzheimer’s disease by inducing dendritic-like microglia expressing insulin-like growth factor 1
Butovsky, O., Koronyo-Hamaoui, M., Kunis, G., Ophir, E., Landa, G., Cohen, H., & Schwartz, M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604681103 · Cited by 388 · see citing works
Interferon-γ and Tumor Necrosis Factor-α Regulate Amyloid-β Plaque Deposition and β-Secretase Expression in Swedish Mutant APP Transgenic Mice
Yamamoto, M., Kiyota, T., Horiba, M., Buescher, J. L., Walsh, S. M., Gendelman, H. E., & Ikezu, T. (2007) · The American Journal of Pathology · doi:10.2353/ajpath.2007.060378 · Cited by 367 · see citing works
Self-citation
Immunology and immunotherapy of Alzheimer's disease
Weiner, H. L., & Frenkel, D. (2006) · Nature Reviews Immunology · doi:10.1038/nri1843 · Cited by 335 · see citing works
Evidence for glial-mediated inflammation in aged APPSW transgenic mice
Benzing, W. C., Wujek, J. R., Ward, E. K., Shaffer, D. J., Ashe, K. H., Younkin, S. G., & Brunden, K. R. (1999) · Neurobiology of Aging · doi:10.1016/s0197-4580(99)00065-2 · Cited by 298 · see citing works
β-Amyloid-induced glial expression of both pro- and anti-inflammatory cytokines in cerebral cortex of aged transgenic Tg2576 mice with Alzheimer plaque pathology
Apelt, J., & Schliebs, R. (2001) · Brain Research · doi:10.1016/s0006-8993(00)03176-0 · Cited by 287 · see citing works
Slow Degradation of Aggregates of the Alzheimer's Disease Amyloid β-Protein by Microglial Cells
Paresce, D. M., Chung, H., & Maxfield, F. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.46.29390 · Cited by 269 · see citing works
Role of CD40 ligand in amyloidosis in transgenic Alzheimer's mice
Tan, J., Town, T., Crawford, F., Mori, T., DelleDonne, A., Crescentini, R., Obregon, D., Flavell, R. A., & Mullan, M. J. (2002) · Nature Neuroscience · doi:10.1038/nn968 · Cited by 217 · see citing works
Uptake, Degradation, and Release of Fibrillar and Soluble Forms of Alzheimer's Amyloid β-Peptide by Microglial Cells
Chung, H., Brazil, M. I., Soe, T. T., & Maxfield, F. R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.45.32301 · Cited by 212 · see citing works
Nasal vaccination with a proteosome-based adjuvant and glatiramer acetate clears β-amyloid in a mouse model of Alzheimer disease
Frenkel, D., Maron, R., Burt, D. S., & Weiner, H. L. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23241 · Cited by 186 · see citing works
Degradation of Amyloid β-Protein by a Metalloprotease Secreted by Microglia and Other Neural and Non-neural Cells
Qiu, W. Q., Ye, Z., Kholodenko, D., Seubert, P. A., & Selkoe, D. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.10.6641 · Cited by 175 · see citing works
Disruption of T helper 2-immune responses in Epstein–Barr virus-induced gene 3-deficient mice
Nieuwenhuis, E. E. S., Neurath, M. F., Corazza, N., Iijima, H., Trgovcich, J., Wirtz, S. J., Glickman, J. N., Bailey, D. T., Yoshida, M., Galle, P. R., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252648899 · Cited by 172 · see citing works
Residues 17–20 and 30–35 of beta‐amyloid play critical roles in aggregation
Liu, R., McAllister, C., Lyubchenko, Y. L., & Sierks, M. R. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10859 · Cited by 165 · see citing works
Up-regulation of the inflammatory cytokines IFN-γ and IL-12 and down-regulation of IL-4 in cerebral cortex regions of APPSWE transgenic mice
Abbas, N., Bednar, I., Mix, E., Svedberg, M., Paterson, D., Ljungberg, A., Morris, C. M., Winblad, B. G., Nordberg, A. K., & Zhu, J. (2002) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(02)00050-4 · Cited by 161 · see citing works
Human microglial cell defense against Toxoplasma gondii. The role of cytokines.
Chao, C., Gekker, G., Hu, S., & Peterson, P. K. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.152.3.1246 · Cited by 160 · see citing works
The IL-4 Receptor α-Chain-Binding Cytokines, IL-4 and IL-13, Induce Forkhead Box P3-Expressing CD25+CD4+ Regulatory T Cells from CD25−CD4+ Precursors
Skapenko, A., Kalden, J. R., Lipsky, P. E., & Schulze‐Koops, H. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.9.6107 · Cited by 157 · see citing works
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Wilkinson, B. L., Koenigsknecht-Talboo, J., Grommes, C., Lee, C. Y. D., & Landreth, G. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600627200 · Cited by 131 · see citing works
CD40 signaling regulates innate and adaptive activation of microglia in response to amyloid β‐peptide
Townsend, K. P., Town, T., Mori, T., Lue, L., Shytle, D., Sanberg, P. R., Morgan, D., Fernandez, F., Flavell, R. A., & Tan, J. (2005) · European Journal of Immunology · doi:10.1002/eji.200425585 · Cited by 121 · see citing works
Single Chain Variable Fragments against β-Amyloid (Aβ) Can Inhibit Aβ Aggregation and Prevent Aβ-Induced Neurotoxicity
Liu, R., Yuan, B., Emadi, S., Zameer, A., Schulz, P., McAllister, C., Lyubchenko, Y. L., Goud, G. N., & Sierks, M. R. (2004) · Biochemistry · doi:10.1021/bi049933o · Cited by 113 · see citing works
Pubertal Changes in Biochemical Markers of Growth
Federico, G., Baroncelli, G. I., Vanacore, T., Fiore, L., & Saggese, G. (2003) · Hormone Research in Paediatrics · doi:10.1159/000071225 · Cited by 102 · see citing works
Amino acid copolymer-specific IL-10-secreting regulatory T cells that ameliorate autoimmune diseases in mice
Stern, J. N. H., Keskin, D. B., Zhang, H., Lv, H., Kato, Z., & Strominger, J. L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712131105 · Cited by 54 · see citing works
Increased T Cell Recruitment to the CNS after Amyloid β1–42Immunization in Alzheimer's Mice Overproducing Transforming Growth Factor-β1
Buckwalter, M. S., Coleman, B. S., Buttini, M., Barbour, R., Schenk, D., Games, D., Seubert, P. A., & Wyss‐Coray, T. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.2436-06.2006 · Cited by 47 · see citing works
C1q–calreticulin induced oxidative neurotoxicity: relevance for the neuropathogenesis of Alzheimer's disease
Luo, X., Weber, G. A., Zheng, J., Gendelman, H. E., & Ikezu, T. (2003) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(02)00444-7 · Cited by 45 · see citing works
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Chabot, S., Yong, F., Le, D., Metz, L., Myles, T., & Yong, V. W. (2002) · Multiple Sclerosis Journal · doi:10.1191/1352458502ms810oa · Cited by 40 · see citing works
Amyloid precursor protein‐processing products affect mononuclear phagocyte activation: pathways for sAPP‐ and Aβ‐mediated neurotoxicity
Ikezu, T., Luo, X., Weber, G. A., Zhao, J., McCabe, L., Buescher, J. L., Ghorpade, A., Zheng, J., & Xiong, H. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01739.x · Cited by 39 · see citing works
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Yamamoto, M., Kiyota, T., Walsh, S. M., & Ikezu, T. (2006) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-006-9049-8 · Cited by 17 · see citing works
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Borgmann, K., Gendelman, H. E., & Ghorpade, A. (2005) · Humana Press eBooks · doi:10.1385/1-59259-907-9:049 · Cited by 14 · see citing works

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Reynolds, A. D., Stone, D. K., Mosley, R. L., & Gendelman, H. E. (2009) · Journal of Proteome Research · doi:10.1021/pr9001614 · Cited by 83 · see citing works
Macrophage efferocytosis in health and disease
Razi, S., Khojini, J. Y., Kargarijam, F., Panahi, S., Tahershamsi, Z., Tajbakhsh, A., & Hayat, S. M. G. (2023) · Cell Biochemistry and Function · doi:10.1002/cbf.3780 · Cited by 80 · see citing works
Oxidative stress and expression of insulin signaling proteins in the brain of diabetic rats: Role of Nigella sativa oil and antidiabetic drugs
Balbaa, M., Abdulmalek, S. A., & Khalil, S. (2017) · PLoS ONE · doi:10.1371/journal.pone.0172429 · Cited by 76 · see citing works
The anti-inflammatory glycoprotein, CD200, restores neurogenesis and enhances amyloid phagocytosis in a mouse model of Alzheimer's disease
Varnum, M. M., Kiyota, T., Dixie, K. L. I., Ikezu, S., & Ikezu, T. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.07.027 · Cited by 75 · see citing works
Self-citation
Alzheimer’s disease and type 2 diabetes via chronic inflammatory mechanisms
Mushtaq, G., Khan, J. A., Kumosani, T. A., & Kamal, M. A. (2014) · Saudi Journal of Biological Sciences · doi:10.1016/j.sjbs.2014.05.003 · Cited by 73 · see citing works
Peripheral Delivery of a CNS Targeted, Metalo-Protease Reduces Aβ Toxicity in a Mouse Model of Alzheimer's Disease
Spencer, B. J., Marr, R. A., Gindi, R., Potkar, R., Michael, S. A., Adame, A., Rockenstein, E. M., Verma, I. M., & Masliah, E. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016575 · Cited by 69 · see citing works
AAV1/2-mediated CNS Gene Delivery of Dominant-negative CCL2 Mutant Suppresses Gliosis, β-amyloidosis, and Learning Impairment of APP/PS1 Mice
Kiyota, T., Yamamoto, M., Schroder, B., Jacobsen, M. T., Swan, R. J., Lambert, M. P., Klein, W. L., Gendelman, H. E., Ransohoff, R. M., & Ikezu, T. (2009) · Molecular Therapy · doi:10.1038/mt.2009.44 · Cited by 68 · see citing works
Self-citation
Glycogen Synthase Kinase‐3β: A Mediator of Inflammation in Alzheimer′s Disease?
Koıstınaho, J., Malm, T., & Goldsteins, G. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/129753 · Cited by 66 · see citing works
Microglial toll-like receptors and Alzheimer’s disease
Su, F., Bai, F., Zhou, H., & Zhang, Z. (2015) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2015.10.010 · Cited by 67 · see citing works
Lipid metabolism in microglia: Emerging mechanisms and therapeutic opportunities for neurodegenerative diseases (Review)
Sun, Y., Wei, K., Liao, X., Wang, J., Gao, L., & Pang, B. (2025) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2025.5580 · Cited by 57 · see citing works
CD 4+ T cells in the pathobiology of neurodegenerative disorders
Huang, X., Reynolds, A. D., Mosley, R. L., & Gendelman, H. E. (2009) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2009.04.006 · Cited by 51 · see citing works
Therapeutic potential of mangiferin in the treatment of various neuropsychiatric and neurodegenerative disorders
Walia, V., Chaudhary, S. K., & Kumar Sethiya, N. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2020.104939 · Cited by 51 · see citing works
Neuroprotective, Neurogenic, and Amyloid Beta Reducing Effect of a Novel Alpha 2-Adrenoblocker, Mesedin, on Astroglia and Neuronal Progenitors upon Hypoxia and Glutamate Exposure
Melkonyan, M. M., Hunanyan, L. S., Lourhmati, A., Layer, N., Beer‐Hammer, S., Yenkoyan, K. B., Schwab, M. G., & Danielyan, L. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms19010009 · Cited by 49 · see citing works
DOCK2 Is a Microglial Specific Regulator of Central Nervous System Innate Immunity Found in Normal and Alzheimer’s Disease Brain
Cimino, P. J., Sokal, I., Leverenz, J., Fukui, Y., & Montine, T. J. (2009) · The American Journal of Pathology · doi:10.2353/ajpath.2009.090443 · Cited by 49 · see citing works
Targeting of Tumor Necrosis Factor Alpha Receptors as a Therapeutic Strategy for Neurodegenerative Disorders
Dong, Y., Dekens, D. W., de Deyn, P., Naudé, P., & Eisel, U. (2015) · Antibodies · doi:10.3390/antib4040369 · Cited by 47 · see citing works
CD200-, CX3CL1-, and TREM2-mediated neuron-microglia interactions and their involvements in Alzheimer’s disease
Zhang, L., Xu, J., Gao, J., Wu, Y., Yin, M., & Zhao, W. (2018) · Reviews in the Neurosciences · doi:10.1515/revneuro-2017-0084 · Cited by 48 · see citing works
IKKβ Deficiency in Myeloid Cells Ameliorates Alzheimer's Disease-Related Symptoms and Pathology
Liu, Y., Liu, X., Hao, W., Decker, Y., Schomburg, R., Fülöp, L., Pasparakis, M., Menger, M. D., & Fassbender, K. C. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1348-14.2014 · Cited by 44 · see citing works
Inhibition of IKKβ by celastrol and its analogues – an in silico and in vitro approach
Veerappan, K., Natarajan, S., Ethiraj, P., Vetrivel, U., & Samuel, S. (2016) · Pharmaceutical Biology · doi:10.1080/13880209.2016.1241809 · Cited by 45 · see citing works
The biochemical aftermath of anti-amyloid immunotherapy
Maarouf, C. L., Daugs, I. D., Kokjohn, T. A., Kalback, W. M., Patton, R., Luehrs, D. C., Masliah, E., Nicoll, J. A. R., Sabbagh, M. N., Beach, T. G., et al. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-39 · Cited by 43 · see citing works
Europium-Doped Cerium Oxide Nanoparticles for Microglial Amyloid Beta Clearance and Homeostasis
Machhi, J., Yeapuri, P., Marković, M., Patel, M., Yan, W., Lu, Y., Cohen, J. D., Hasan, M., Abdelmoaty, M. M., Zhou, Y., et al. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00847 · Cited by 34 · see citing works
Metabolic, immune, epigenetic, endocrine and phenotypic abnormalities found in individuals with autism spectrum disorders, Down syndrome and Alzheimer disease may be caused by congenital and/or acquired chronic cerebral toxoplasmosis
Prandota, J. (2010) · Research in Autism · doi:10.1016/j.rasd.2010.03.009 · Cited by 33 · see citing works
The Effect of HIV Protease Inhibitors on Amyloid-β Peptide Degradation and Synthesis in Human Cells and Alzheimer’s Disease Animal Model
Lan, X., Kiyota, T., Hanamsagar, R. M., Huang, Y., Andrews, S., Peng, H., Zheng, J., Swindells, S., Carlson, G. A., & Ikezu, T. (2011) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-011-9304-5 · Cited by 34 · see citing works
Self-citation
Role of Suppressor of Cytokine Signaling 3 (SOCS3) in Altering Activated Microglia Phenotype in APPswe/PS1dE9 Mice
Iwahara, N., Hisahara, S., Kawamata, J., Matsumura, A., Yokokawa, K., Saito, T., Fujikura, M., Manabe, T., Suzuki, H., Matsushita, T., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160887 · Cited by 34 · see citing works
Rationale for Peptide and DNA Based Epitope Vaccines for Alzheimers Disease Immunotherapy
Ghochikyan, A. (2009) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152709787847298 · Cited by 31 · see citing works
Heat shock protein profiles on the protein and gene expression levels in olive flounder kidney infected with Streptococcus parauberis
Cha, I. S., Kwon, J. S., Park, S. B., Jang, H. B., Nho, S. W., Kim, Y. K., Hikima, J.-I., Aoki, T., & Jung, T. S. (2013) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2013.03.355 · Cited by 30 · see citing works
HIV-1 Reduces Aβ-Degrading Enzymatic Activities in Primary Human Mononuclear Phagocytes
Lan, X., Xu, J., Kiyota, T., Peng, H., Zheng, J., & Ikezu, T. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100211 · Cited by 29 · see citing works
Self-citation
The mixed-lineage kinase 3 inhibitor URMC-099 facilitates microglial amyloid-β degradation
Dong, W., Embury, C. M., Lu, Y., Whitmire, S. M., Dyavarshetty, B., Gelbard, H. A., Gendelman, H. E., & Kiyota, T. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0646-z · Cited by 28 · see citing works
Self-citation
ICAM-1 protects neurons against Amyloid-β and improves cognitive behaviors in 5xFAD mice by inhibiting NF-Κb
Guha, S., Paidi, R. K., Goswami, S., Saha, P., & Biswas, S. C. (2022) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2021.11.021 · Cited by 26 · see citing works
RAGE Does Not Affect Amyloid Pathology in Transgenic ArcAβ Mice
Vodopivec, I., Galichet, A., Knobloch, M., Bierhaus, A., Heizmann, C. W., & Nitsch, R. M. (2009) · Neurodegenerative Diseases · doi:10.1159/000261723 · Cited by 23 · see citing works
Soluble and insoluble protein aggregates, endoplasmic reticulum stress, and vascular dysfunction in Alzheimer’s disease and cardiovascular diseases
Waigi, E. W., Webb, R. C., Moss, M. A., Uline, M. J., McCarthy, C. G., & Wenceslau, C. F. (2023) · GeroScience · doi:10.1007/s11357-023-00748-y · Cited by 24 · see citing works
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Combination of plasma tumor necrosis factor receptors signaling proteins, beta-amyloid and apolipoprotein E for the detection of Alzheimer's disease
Zhang, J., Jia, J., Qin, W., & Wang, S. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.03.007 · Cited by 22 · see citing works
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Innate and adaptive immunity in neurodegenerative disease
Huang, Y., Zhang, G., Li, S., Feng, J., & Zhang, Z. (2025) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05533-4 · Cited by 21 · see citing works
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Su, F., Bai, F., Zhou, H., & Zhang, Z. (2016) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2016.05.016 · Cited by 19 · see citing works
Shared pathological pathways of Alzheimer's disease with specific comorbidities: current perspectives and interventions
Nday, C. M., Eleftheriadou, D., & Jackson, G. E. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14256 · Cited by 20 · see citing works
N-truncation and pyroglutaminylation enhances the opsonizing capacity of Aβ-peptides and facilitates phagocytosis by macrophages and microglia
Condic, M., Oberstein, T. J., i, M. H., Reimann, M. C., Kornhuber, J., Maler, J. M., & Spitzer, P. (2014) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2014.05.003 · Cited by 19 · see citing works
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Otgongerel, D., Lee, H.-J., & Jo, S. A. (2022) · NeuroMolecular Medicine · doi:10.1007/s12017-022-08726-x · Cited by 17 · see citing works
Microglial Modulation in Alzheimer’s Disease: Central Players in Neuroinflammation and Pathogenesis
Hussain, M. S., Khan, Y., Fatima, R., Maqbool, M., Ramalingam, P. S., Khan, M. G., & Bisht, A. S. (2025) · Current Alzheimer Research · doi:10.2174/0115672050364292250113063513 · Cited by 15 · see citing works
Effect and Mechanism of Exogenous Melatonin on Cognitive Deficits in Animal Models of Alzheimer’s Disease: A Systematic Review and Meta-analysis
Zhai, Z., Xie, D., Qin, T., Zhong, Y., Xu, Y., & Sun, T. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.09.012 · Cited by 11 · see citing works
Immune modulations and immunotherapies for Alzheimer’s disease: a comprehensive review
Mahdiabadi, S., Momtazmanesh, S., Perry, G. L., & Rezaei, N. (2021) · Reviews in the Neurosciences · doi:10.1515/revneuro-2021-0092 · Cited by 12 · see citing works
Therapeutic approaches to microglial dysfunction in Alzheimer's disease: Enhancing phagocytosis and metabolic regulation
Almalki, W. H., & Almujri, S. S. (2024) · Pathology - Research and Practice · doi:10.1016/j.prp.2024.155614 · Cited by 9 · see citing works
Animal Models of Alzheimer’s Disease: Utilization of Transgenic Alzheimer’s Disease Models in Studies of Amyloid Beta Clearance
Malm, T., Magga, J. M., & Koıstınaho, J. (2012) · Current Translational Geriatrics and Experimental Gerontology Reports · doi:10.1007/s13670-011-0004-z · Cited by 9 · see citing works
Extracellular Hsp90α stimulates a unique innate gene profile in microglial cells with simultaneous activation of Nrf2 and protection from oxidative stress
Okusha, Y., Lang, B. J., Murshid, A., Borges, T. J., Holton, K. M., Clark, J., Doshi, S., Ikezu, T., & Calderwood, S. K. (2022) · Cell Stress and Chaperones · doi:10.1007/s12192-022-01279-9 · Cited by 7 · see citing works
Self-citation
The influence of tumour necrosis factor- α (TNF-α) on amyloid-β (Aβ)-degrading enzymes in vitro.
Culpan, D., Palmer, J. C., Miners, J. S., Love, S., & Kehoe, P. G. (2011) · PubMed Central · Cited by 7 · see citing works
Entwined processes in Alzheimer's disease: Brain cellular senescence and Alzheimer's disease pathology
Li, W., Han, Y., Wang, P., & Qiao, S. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70803 · Cited by 6 · see citing works
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Rodríguez-Carreiro, S., Nogales, M. D. C., Jiménez-Galán, D., Carmona-Lorenzo, S., Caro-Martín, A., Navarro, E., & Esteras, N. (2024) · Regenerative medicine reports . · doi:10.4103/regenmed.regenmed-d-24-00005 · Cited by 3 · see citing works
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Wu, G., Wu, Z., Sang, N., & Hershey, J. C. (2015) · International Journal of Neuroscience · doi:10.3109/00207454.2014.952730 · Cited by 3 · see citing works
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Wu, B., Chen, M., Meng, L., Tian, Q., & Dong, Z. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-240096 · Cited by 3 · see citing works
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Tokuraku, K., & Ikezu, T. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-394431-3.00011-0 · Cited by 5 · see citing works
Self-citation
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Murshid, A., Lang, B. J., Borges, T. J., Okusha, Y., Doshi, S., Yasmine, S., Clark, J., Choudhury, R., Ang, L., Woodbury, M. E., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.16.440151 · Cited by 2 · see citing works
Self-citation
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Brandys, N., & Chadzińska, M. (2021) · Postępy Higieny i Medycyny Doświadczalnej · doi:10.2478/ahem-2021-0014 · Cited by 1 · see citing works
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Donley, D. W., Jenkins, T., Deiter, C. S., Campbell, R., Realing, M., Chopra, V., Hersch, S., Gigley, J. P., & Fox, J. H. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/550624 · Cited by 1 · see citing works
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Syk and Yea Shall Find
Wolozin, B. L., & Ikezu, T. (2015) · EBioMedicine · doi:10.1016/j.ebiom.2015.11.012
Self-citation
Peripheral Inflammation and Alzheimer’s Disease: Periodontal Disease
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Inflammatory pathology in neurodegenerative dementias
Niedermayer, G. (2014)
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Kang, N., Liu, Y., & He, R. (2025) · Springer eBooks · doi:10.1007/978-981-96-7281-3_12
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Slater, O., & Kontoyianni, M. (2025) · Molecules · doi:10.3390/molecules30204116
Additional file 1 of Low-dose brain irradiation normalizes TSPO and CLUSTERIN levels and promotes the non-amyloidogenic pathway in pre-symptomatic TgF344-AD rats
Ceyzériat, K., Zilli, T., Millet, P., Koutsouvelis, N., Dipasquale, G., Fossey, C., Cailly, T., Fabis, F., Frisoni, G. B., Garibotto, V., et al. (2023) · Figshare · doi:10.6084/m9.figshare.22605007
Additional file 1 of The neutrophil to lymphocyte ratio associates with markers of Alzheimer’s disease pathology in cognitively unimpaired elderly people
Jacobs, T., Jacobson, S. R., Fortea, J., Berger, J. S., Vedvyas, A., Marsh, K., He, T., Gutiérrez‐Jiménez, E., Fillmore, N. R., Gonzalez, M., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25853015
Additional file 2 of Low-dose brain irradiation normalizes TSPO and CLUSTERIN levels and promotes the non-amyloidogenic pathway in pre-symptomatic TgF344-AD rats
Ceyzériat, K., Zilli, T., Millet, P., Koutsouvelis, N., Dipasquale, G., Fossey, C., Cailly, T., Fabis, F., Frisoni, G. B., Garibotto, V., et al. (2023) · Figshare · doi:10.6084/m9.figshare.22605010
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van Rijn, J. M. (2014) · Utrecht University Repository (Utrecht University)

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Koenigsknecht-Talboo, J., & Landreth, G. E. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1808-05.2005 · Cited by 477 · see citing works
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P1‐299: AMYLOID BETA IN CIRCULATING MONOCYTES
Torsetnes, S. B., Wettergreen, M., & Fladby, T. (2018) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2018.06.305
Degradation of fibrillar forms of Alzheimer's amyloid β-peptide by macrophages
Majumdar, A., Chung, H., Dolios, G., Wang, R., Asamoah, N., Lobel, P., & Maxfield, F. R. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.12.001 · Cited by 92 · see citing works
Hippocampal expression of murine TNFα results in attenuation of amyloid deposition in vivo
Chakrabarty, P., Herring, A., Ceballos-Diaz, C., Das, P., & Golde, T. E. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-16 · Cited by 117 · see citing works

Authors: Yamamoto, M., Kiyota, T., Walsh, S. M., Liu, J., Kipnis, J., & Ikezu, T.
Affiliations: University of Nebraska Medical Center (US)
University of Virginia (US)
ORCID: Kiyota, Tomomi
Walsh, Shannon M
Kipnis, Jonathan
Ikezu, Tsuneya
Venue: The Journal of Immunology
Publisher: Oxford University Press (OUP)
Published: 2008-09
Volume: 181
Issue: 6
Pages: 3877-3886
ISSN: 0022-1767 (ISSN-L)
1550-6606
DOI: 10.4049/jimmunol.181.6.3877
PMC: PMC2603577
OpenAlex: W1641618604
Cited by: 100
References: 38
Citations by year: 2026: 1 · 2025: 7 · 2024: 9 · 2023: 4 · 2022: 7 · 2021: 4 · 2020: 2 · 2019: 4 · 2018: 1 · 2017: 5 · 2016: 7 · 2015: 7 · 2014: 6 · 2013: 6 · 2012: 6
FWCI: 5.43
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: academic.oup.com/pages/standard-publication-reuse-rights (vor)
Locations: The Journal of Immunology (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: Nebraska Tobacco Settlement Biomedical Research Development Fund
National Institutes of Health (NS043985)
National Institute of Neurological Disorders and Stroke (P01NS043985)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: amyloid beta degradation, fibrillar amyloid-beta, monocyte-derived macrophages, microglia, inflammatory cytokines, anti-inflammatory cytokines, interferon-gamma, insulin-degrading enzyme, heat shock proteins, lysosomal degradation, Alzheimer's disease, amyloid-beta clearance, amyloid-beta oligomers
MeSH terms: Acetylation, Cells, Cultured, Humans, Iodine Radioisotopes, Lipoproteins, LDL, Macrophages, Peptide Fragments, Cytokines, Amyloid beta-Peptides, Microglia, Microscopy, Atomic Force, Inflammation Mediators, Coculture Techniques

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Cytokine-Mediated Inhibition of Fibrillar Amyloid-β Peptide Degradation by Human Mononuclear Phagocytes

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