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Peripherally administered antibodies against amyloid β-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
Abstract
One hallmark of Alzheimer disease is the accumulation of amyloid beta-peptide in the brain and its deposition as plaques. Mice transgenic for an amyloid beta precursor protein (APP) mini-gene driven by a platelet-derived (PD) growth factor promoter (PDAPP mice), which overexpress one of the disease-linked mutant forms of the human amyloid precursor protein, show many of the pathological features of Alzheimer disease, including extensive deposition of extracellular amyloid plaques, astrocytosis and neuritic dystrophy. Active immunization of PDAPP mice with human amyloid beta-peptide reduces plaque burden and its associated pathologies. Several hypotheses have been proposed regarding the mechanism of this response. Here we report that peripheral administration of antibodies against amyloid beta-peptide, was sufficient to reduce amyloid burden. Despite their relatively modest serum levels, the passively administered antibodies were able to enter the central nervous system, decorate plaques and induce clearance of preexisting amyloid. When examined in an ex vivo assay with sections of PDAPP or Alzheimer disease brain tissue, antibodies against amyloid beta-peptide triggered microglial cells to clear plaques through Fc receptor-mediated phagocytosis and subsequent peptide degradation. These results indicate that antibodies can cross the blood-brain barrier to act directly in the central nervous system and should be considered as a therapeutic approach for the treatment of Alzheimer disease and other neurological disorders.
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In the citing paper
“This finding suggests that anti-apoE antibody might modulate similar inflammatory responses, which is consistent with the effect of certain anti-Aβ antibodies (Bard et al., 2000; Wilcock et al., 2004).”
From Anti-apoE immunotherapy inhibits amyloid accumulation in a transgenic mouse model of Aβ amyloidosis (2012) · cites this paper as Bard et al., 2000
In the citing paper
“Recruitment and activation of microglia around plaques and subsequent Aβ degradation/clearance have been proposed as one of the mechanisms by which Aβ immunotherapy decreases amyloid levels (Bard et al., 2000; Koenigsknecht-Talboo et al., 2008; Wang et al., 2011).”
From Anti-apoE immunotherapy inhibits amyloid accumulation in a transgenic mouse model of Aβ amyloidosis (2012) · cites this paper as Bard et al., 2000
In the citing paper
“One of the major mechanisms for removal of the plaques in response to some anti-A antibodies is microglial-mediated phagocytosis (Bard et al., 2000;Demattos et al., 2012).”
From Anti-ApoE Antibody Given after Plaque Onset Decreases Aβ Accumulation and Improves Brain Function in a Mouse Model of Aβ Amyloidosis (2014) · cites this paper as Bard et al., 2000
In the citing paper
“We used mAb 10D5 direct against Aβ3–7 epitope [10], which is known to penetrate the blood–brain-barrier (BBB) and directly binds to deposited Aβ triggering microglial cells to clear Aβ plaques through Fc receptor-mediated phagocytosis [9].”
From APOE Genotype Differentially Modulates Effects of Anti-Aβ, Passive Immunization in APP Transgenic Mice (2017) · cites this paper as [9]
In the citing paper
“The dose of 10D5 mAb used in this study was previously shown to be effective in removing Aβ plaques in PDAPP AD Tg mice expressing wild type murine apoE [9, 10, 22].”
From APOE Genotype Differentially Modulates Effects of Anti-Aβ, Passive Immunization in APP Transgenic Mice (2017) · cites this paper as [9]
In the citing paper
“The primary mechanism of action of 10D5 mAb is based on its direct binding to deposited Aβ and stimulating Fc receptor-mediated Aβ plaque removal by activated microglia and possibly blood derived macrophages [9, 34].”
From APOE Genotype Differentially Modulates Effects of Anti-Aβ, Passive Immunization in APP Transgenic Mice (2017) · cites this paper as [9]
In the citing paper
“In preclinical studies, the murine form of the antibody (3D6) was shown to bind to fibrillar, oligomeric, and monomeric forms of Aβ, reduce the amount of Aβ in the brain, and improve memory in transgenic mice that overproduced Aβ.4–8”
From Two Phase 3 Trials of Bapineuzumab in Mild-to-Moderate Alzheimer's Disease (2014) · cites this paper as [4]
In the citing paper
“In preclinical studies, the murine form of the antibody (3D6) was shown to bind to fibrillar, oligomeric, and monomeric forms of Aβ, reduce the amount of Aβ in the brain, and improve memory in transgenic mice that overproduced Aβ.4–8”
From Two Phase 3 Trials of Bapineuzumab in Mild-to-Moderate Alzheimer's Disease (2014) · cites this paper as [4]
In the citing paper
“In preclinical studies, the murine form of the antibody (3D6) was shown to bind to fibrillar, oligomeric, and monomeric forms of Aβ, reduce the amount of Aβ in the brain, and improve memory in transgenic mice that overproduced Aβ.4–8”
From Two Phase 3 Trials of Bapineuzumab in Mild-to-Moderate Alzheimer's Disease (2014) · cites this paper as [4]
In the citing paper
“Experimental therapies, such as Aβ immunotherapy [8, 53, 138, 164, 178], were not only shown to reduce cerebral Aβ, but even more importantly, to improve behavior in transgenic mouse models of AD-like cerebral β-amyloidosis.”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [8]
Citations
Cites
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
Self-citationAlzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
Games, D., Adams, D., Alessandrini, R., Barbour, R., Borthelette, P., Blackwell, C., Carr, T., Clemens, J., Donaldson, T., Gillespie, F., et al. (1995) · Nature · doi:10.1038/373523a0 · Cited by 2,516
Self-citation(1997) · doi:10.1073/pnas.94.4.1550 · Cited by 535
Self-citationMasliah, E., Sisk, A., Mallory, M. E., Mucke, L., Schenk, D., & Games, D. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-18-05795.1996 · Cited by 389
Self-citationSlow 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 275
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
Hyman, B. T., Tanzi, R. E., Marzloff, K., Barbour, R., & Schenk, D. (1992) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199201000-00009 · Cited by 135
Self-citationLaboratory Investigation of Cerebrospinal Fluid Proteins
Thompson, E. J., & Keir, G. (1990) · Annals of Clinical Biochemistry International Journal of Laboratory Medicine · doi:10.1177/000456329002700503 · Cited by 68
Antibody clears senile plaques
George‐Hyslop, P. S., & Westaway, D. A. (1999) · Nature · doi:10.1038/22006 · Cited by 41
Curing amyloidosis: will it work in humans?
Duff, K. (1999) · Trends in Neurosciences · doi:10.1016/s0166-2236(99)01489-7 · Cited by 14
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Mouse Models of Alzheimer's Disease: A Quest for Plaques
Richardson, J. A., & Burns, D. K. (2002) · ILAR Journal · doi:10.1093/ilar.43.2.89 · Cited by 53
Yamada, K., & Iwatsubo, T. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05225-z · Cited by 62
Learning and Memory Deficits in APP Transgenic Mouse Models of Amyloid Deposition
Morgan, D. (2003) · Neurochemical Research · doi:10.1023/a:1023255106106 · Cited by 52
Nicolau, C. S., Greferath, R., Balaban, T. S., Lazarte, J. E., & Hopkins, R. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.022627199 · Cited by 52
Receptor-Mediated Abeta Amyloid Antibody Targeting to Alzheimer’s Disease Mouse Brain
Zhou, Q.-H., Fu, A., Boado, R. J., Hui, E. K., Lu, J. Z., & Pardridge, W. M. (2010) · Molecular Pharmaceutics · doi:10.1021/mp1003515 · Cited by 52
Robert, R., Dolezal, O., Waddington, L. J., Hattarki, M. K., Cappai, R., Masters, C. L., Hudson, P. J., & Wark, K. (2008) · Protein Engineering Design and Selection · doi:10.1093/protein/gzn052 · Cited by 52
Wang, C., Wang, Z., Xie, J., Cai, J., Wang, T., Xu, Y., Wang, X., & Li, A. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5845 · Cited by 53
Beta‐sheet breaker strategy for the treatment of Alzheimer's disease
Adessi, C., & Soto, C. A. (2002) · Drug Development Research · doi:10.1002/ddr.10074 · Cited by 51
β-Secretase, APP and Aβ in Alzheimer’s Disease
Vassar, R. J. (2006) · Springer eBooks · doi:10.1007/0-387-23226-5_4 · Cited by 52
Human monoclonal antibodies against amyloid-beta from healthy adults
Geylis, V., Kourilov, V., Meiner, Z., Nennesmo, I., Bogdanović, N., & Steinitz, M. O. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.06.008 · Cited by 52
Lee, E. B., Leng, L. Z., Lee, V. M. ‐., & Trojanowski, J. Q. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.03.070 · Cited by 52
Cellular Prion Protein as a Therapeutic Target in Alzheimer's Disease
Laurén, J. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130950 · Cited by 55
Walker, L. C., & LeVine, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00160-3 · Cited by 51
Neprilysin protects neurons against Aβ peptide toxicity
El‐Amouri, S. S., Zhu, H., Yu, J., Gage, F. H., Verma, I. M., & Kindy, M. S. (2007) · Brain Research · doi:10.1016/j.brainres.2007.03.072 · Cited by 51
Vaccination as a Therapeutic Approach to Alzheimer's Disease
Wısnıewskı, T., & Boutajangout, A. (2010) · Mount Sinai Journal of Medicine A Journal of Translational and Personalized Medicine · doi:10.1002/msj.20156 · Cited by 53
Natural Antibodies as Rheostats for Susceptibility to Chronic Diseases in the Aged
Rothstein, T. L. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00127 · Cited by 50
Targeting the Endocannabinoid System in Alzheimer's Disease
Koppel, J. L., & Davies, P. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-15315 · Cited by 51
Juszczyk, P., Paraschiv, G., Szymańska, A., Kolodziejczyk, A. S., Rodziewicz‐Motowidło, S., Grzonka, Z., & Przybylski, M. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm801115e · Cited by 51
Wang, Y., Pollard, A., Zhong, J., Dong, X., Wu, X., Zhou, H., & Zhou, X. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.06.013 · Cited by 51
Antibody Therapeutics Targeting Aβ and TauPreprint
Gallardo, G., & Holtzman, D. M. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024331 · Cited by 55
Alzheimer therapy with an antibody against N-terminal Abeta 4-X and pyroglutamate Abeta 3-X
Antonios, G., Borgers, H., Richard, B. C., Brauß, A., Meißner, J., Weggen, S., Pena, V., Pillot, T., Davies, S. L., Bakrania, P., et al. (2015) · Scientific Reports · doi:10.1038/srep17338 · Cited by 61
NAKAI, T., Yamada, K., & Mizoguchi, H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115549 · Cited by 53
Multiphoton in vivo imaging of amyloid in animal models of Alzheimer’s disease
Dong, J., Revilla-Sanchez, R., Moss, S. J., & Haydon, P. G. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.04.007 · Cited by 51
Liu, B., Frost, J. L., Sun, J., Fu, H., Grimes, S., Blackburn, P., & Lemere, C. A. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.5924-12.2013 · Cited by 50
Rommy von Bernhardi, M., Ramírez, G., Toro, R., & Eugenín, J. L. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.12.006 · Cited by 51
The therapeutic potential of the endocannabinoid system for Alzheimer's disease
Karl, T., Cheng, D., Garner, B., & Arnold, J. C. (2012) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2012.671812 · Cited by 51
Vugmeyster, Y., Szklut, P., Wensel, D. L., Ross, J. E., Xu, X., Awwad, M., Gill, D. S., Tchistiakov, L., & Warner, G. L. (2011) · Pharmaceutical Research · doi:10.1007/s11095-011-0405-x · Cited by 50
Neuroprotective roles of the P2Y2 receptor
Weisman, G. A., Ajit, D., Garrad, R. C., Peterson, T. S., Woods, L. T., Thebeau, C. N., Camden, J. M., & Erb, L. (2012) · Purinergic Signalling · doi:10.1007/s11302-012-9307-6 · Cited by 55
Circulating Autoantibodies Recognize and Bind Dying Neurons Following Injury to the Brain
Stein, T. D., Fedynyshyn, J. P., & Kalil, R. E. (2002) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/61.12.1100 · Cited by 50
Crehan, H., Liu, B., Kleinschmidt, M., Rahfeld, J., Le, K. X., Caldarone, B. J., Frost, J. L., Hettmann, T., Hutter‐Paier, B., O’Nuallain, B., et al. (2020) · Alzheimer s Research & Therapy · doi:10.1186/s13195-019-0579-8 · Cited by 48
Zamora, E. D., Handisurya, A., Shafti‐Keramat, S., Borchelt, D., Rudow, G. L., Conant, K. E., Cox, C., Troncoso, J. C., & Kirnbauer, R. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.4.2662 · Cited by 51
Presenilins as therapeutic targets for the treatment of Alzheimer's disease
Golde, T. E., & Younkin, S. G. (2001) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(01)02064-0 · Cited by 49
Imaginem oblivionis: the prospects of neuroimaging for early detection of Alzheimer's disease
Villemagne, V. L., Rowe, C. C., Macfarlane, S., Novakovic, K. E., & Masters, C. L. (2005) · Journal of Clinical Neuroscience · doi:10.1016/j.jocn.2004.03.011 · Cited by 50
Alzheimer's disease: molecular concepts and therapeutic targets
Fassbender, K. C., Masters, C. L., & Beyreuther, K. T. (2001) · Die Naturwissenschaften · doi:10.1007/s001140100237 · Cited by 51
A safer vaccine for Alzheimer’s disease?
Sigurdsson, E. M., Wısnıewskı, T., & Frangione, B. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00124-0 · Cited by 50
An ultra‐sensitive immunoassay detects and quantifies soluble Aβ oligomers in human plasma
Liu, L., Kwak, H., Lawton, T., Jin, S., Meunier, A. L., Dang, Y., Ostaszewski, B. L., Pietras, A., Stern, A. M., & Selkoe, D. J. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12457 · Cited by 49
Epitope‐based DNA vaccine for Alzheimer's disease: Translational study in macaques
Evans, C. F., Davtyan, H., Petrushina, I., Hovakimyan, A., Davtyan, A., Hannaman, D., Cribbs, D. H., Agadjanyan, M. G., & Ghochikyan, A. (2013) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.04.505 · Cited by 47
Irving, E. A., Vinson, M. C., Rosin, C., Roberts, J. C., Chapman, D. M., Facci, L., Virley, D. J., Skaper, S. D., Burbidge, S. A., Walsh, F. S., et al. (2005) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600011 · Cited by 49
Panza, F., Solfrizzi, V., Frisardi, V., Imbimbo, B. P., Capurso, C. A., D’Introno, A., Colacicco, A. M., Seripa, D., Vendemiale, G., Capurso, A., et al. (2009) · Aging Clinical and Experimental Research · doi:10.1007/bf03327445 · Cited by 49
Klaver, A. C., Finke, J. M., Digambaranath, J. L., Balasubramaniam, M., & Loeffler, D. A. (2009) · International Immunopharmacology · doi:10.1016/j.intimp.2009.10.005 · Cited by 49
Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies
Le, N. P. L., Bowden, T. A., Struwe, W. B., & Crispin, M. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.04.016 · Cited by 48
Closing in on the Amyloid Cascade
Doms, R. W., & Huse, J. T. (2000) · Molecular Neurobiology · doi:10.1385/mn:22:1-3:081 · Cited by 50
Searching for new animal models of Alzheimer′s disease
Epis, R., Gardoni, F., Marcello, E. E., Genazzani, A. A., Canonico, P. L., & Luca, M. D. (2009) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2009.10.020 · Cited by 51
Carty, N., Wilcock, D. M., Rosenthal, A., Grimm, J., Pons, J., Ronan, V., Gottschall, P. E., Gordon, M. N., & Morgan, D. (2006) · Journal of Neuroinflammation · doi:10.1186/1742-2094-3-11 · Cited by 50
Spooner, E. T., Desai, R. V., Mori, C., Leverone, J. F., & Lemere, C. A. (2002) · Vaccine · doi:10.1016/s0264-410x(02)00464-4 · Cited by 49
A new role for astrocytes: β-amyloid homeostasis and degradation
Nicoll, J. A. R., & Weller, R. O. (2003) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(03)00109-6 · Cited by 51
Future Therapeutics in Alzheimer’s Disease: Development Status of BACE Inhibitors
Evin, G. M. (2016) · BioDrugs · doi:10.1007/s40259-016-0168-3 · Cited by 52
A Foldamer-Dendrimer Conjugate Neutralizes Synaptotoxic β-Amyloid Oligomers
Fülöp, L., Mándity, I. M., Juhász, G., Szegedi, V., Hetényi, A., Wéber, E., Bozsó, Z., Simon, D., Benkő, M., Király, Z., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039485 · Cited by 48
Solanezumab for Alzheimer's disease
Samadi, H., & Sultzer, D. L. (2011) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2011.578573 · Cited by 48
Brenner, T., Nizri, E., Irony-Tur-Sinai, M., Hamra‐Amitay, Y., & Wirguin, I. (2008) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2008.05.022 · Cited by 47
BiP/GRP78-Induced Production of Cytokines and Uptake of Amyloid-β(1-42) Peptide in Microglia
Kakimura, J., Kitamura, Y., Taniguchi, T., Shimohama, S., & Gebicke‐Haerter, P. J. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4299 · Cited by 48
Mouse models in neurological disorders: Applications of non-invasive imaging
Waerzeggers, Y., Monfared, P., Viel, T., Winkeler, A., & Jacobs, A. H. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.04.009 · Cited by 47
Hirko, A. C., Meyer, E. M., King, M. A., & Hughes, J. A. (2007) · Molecular Therapy · doi:10.1038/sj.mt.6300253 · Cited by 49
Vasilevko, V., Xu, F., Previti, M. L., Nostrand, W. E. V., & Cribbs, D. H. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.2788-07.2007 · Cited by 48
Estrogen (E2) and glucocorticoid (Gc) effects on microglia and Aβ clearance in vitro and in vivo
Harris‐White, M. E., Chu, T., Miller, S., Simmons, M., Teter, B., Nash, D., Cole, G. M., & Frautschy, S. A. (2001) · Neurochemistry International · doi:10.1016/s0197-0186(01)00051-1 · Cited by 48
Human prions and plasma lipoproteins
Safar, J., Wille, H., Geschwind, M. D., Deering, C., Latawiec, D., Serban, A. V., King, D. J., Legname, G., Weisgraber, K. H., Mahley, R. W., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604021103 · Cited by 49
Current therapeutic strategy in Alzheimer's disease.
Singh, S., Kushwah, A. S., Singh, R., Farswan, M., & Kaur, R. (2012) · PubMed · Cited by 47
The advent of Alzheimer treatments will change the trajectory of human aging
Selkoe, D. J. (2024) · Nature Aging · doi:10.1038/s43587-024-00611-5 · Cited by 49
Bard, F., Fox, M., Friedrich, S. W., Seubert, P. A., Schenk, D., Kinney, G. G., & Yednock, T. A. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.07.022 · Cited by 47
Self-citationSweepers in the CNS: Microglial Migration and Phagocytosis in the Alzheimer Disease Pathogenesis
Noda, M., & Suzumura, A. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/891087 · Cited by 52
Lathuilière, A., Mach, N., & Schneider, B. L. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160510578 · Cited by 48
Neurobiological aspects of Alzheimer's disease
Chopra, K., Misra, S., & Kuhad, A. (2011) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2011.557363 · Cited by 47
Kawanishi, S., Takata, K., Itezono, S., Nagayama, H., Konoya, S., Chisaki, Y., Toda, Y., Nakata, S., Yano, Y., Kitamura, Y., et al. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170994 · Cited by 47
MORGAN, D. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2006.03.017 · Cited by 46
Chen, G., Chen, K. S., Kobayashi, D. T., Barbour, R., Motter, R. N., Games, D., Martin, S. J., & Morris, R. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.3710-06.2007 · Cited by 47
Self-citationA limited role for microglia in antibody mediated plaque clearance in APP mice
Garcı́a-Alloza, M., Ferrara, B. J., Dodwell, S. A., Hickey, G. A., Hyman, B. T., & Bacskai, B. J. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.07.019 · Cited by 47
Possible role of scavenger receptor SRCL in the clearance of amyloid‐βin Alzheimer's disease
Nakamura, K. D., Ohya, W., Funakoshi, H., Sakaguchi, G., Kato, A., Takeda, M., Kudo, T., & Nakamura, T. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20992 · Cited by 46
Intracerebroventricular passive immunization with anti‐Aβ antibody in Tg2576
Chauhan, N. B., & Siegel, G. J. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10721 · Cited by 45
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 48
Self-citationAlzheimer Disease Therapeutics
Irizarry, M. C., & Hyman, B. T. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.10.923 · Cited by 49
Pathogenic and physiological autoantibodies in the central nervous system
Gold, M., Pul, R., Bach, J., Stangel, M., & Dodel, R. C. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01128.x · Cited by 47
Platt, T. L., Reeves, V. L., & Murphy, M. P. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.04.017 · Cited by 48
Marin‐Argany, M., Rivera-Hernández, G., Martı́, J., & Villegas, S. (2011) · Biochemical Journal · doi:10.1042/bj20101712 · Cited by 46
Malm, T., Ort, M., Tähtivaara, L., Jukarainen, N., Goldsteins, G., Puoliväli, J. T., Nurmi, A., Pussinen, R., Ahtoniemi, T., Miettinen, T.-K., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602896103 · Cited by 47
A Changing Perspective on the Role of Neuroinflammation in Alzheimer's Disease
Wilcock, D. M. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/495243 · Cited by 48
Lathuilière, A., Laversenne, V., Astolfo, A., Kopetzki, E., Jacobsen, H., Stampanoni, M., Bohrmann, B., Schneider, B. L., & Aebischer, P. (2016) · Brain · doi:10.1093/brain/aww036 · Cited by 49
The cAMP-specific phosphodiesterase 4B mediates Aβ-induced microglial activation
Sebastiani, G., Morissette, C., Lagacé, C., Boulé, M., Ouellette, M., McLaughlin, R. W., Lacombe, D., Gervais, F., & Tremblay, P. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.03.024 · Cited by 45
Novel tricyclic pyrone compounds prevent intracellular APP C99-induced cell death
Jin, L., Hua, D. H., Shie, F., Maezawa, I., Sopher, B. L., & Martin, G. M. (2002) · Journal of Molecular Neuroscience · doi:10.1007/s12031-002-0011-9 · Cited by 46
Probing the origins, diagnosis and treatment of amyloid diseases using antibodies
Dumoulin, M., & Dobson, C. M. (2004) · Biochimie · doi:10.1016/j.biochi.2004.09.012 · Cited by 45
Pangalos, M. N., Jacobsen, S. J., & Reinhart, P. H. (2005) · Biochemical Society Transactions · doi:10.1042/bst0330553 · Cited by 48
Microglial overexpression of the M-CSF receptor augments phagocytosis of opsonized Aβ
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Craft, D. (2002) · Bulletin of Mathematical Biology · doi:10.1006/bulm.2002.0304 · Cited by 64
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Bales, K. R. (2012) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2012.666234 · Cited by 46
Terazaki, H., Ando, Y., Fernandes, R., Yamamura, K., Maeda, S., & Saraiva, M. J. (2005) · Laboratory Investigation · doi:10.1038/labinvest.3700365 · Cited by 47
Alecou, T., Giannakou, M., & Damianou, C. (2017) · Journal of Ultrasound in Medicine · doi:10.1002/jum.14256 · Cited by 50
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Metadata
- Authors
- Bard, F., Cannon, C., Barbour, R., Burke, R.-L., Games, D., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., Kholodenko, D., Lee, M., Lieberburg, I., Motter, R., Nguyen, M., Soriano, F., Vasquez, N., Weiss, K., Welch, B., Seubert, P., Schenk, D., & Yednock, T.
- Affiliations
- Elan Pharmaceuticals, Inc. (Ireland) (IE)
- Corresponding author
- Bard, Frédérique
- Venue
- Nature Medicine
- Published
- 2000-08
- Volume
- 6
- Issue
- 8
- Pages
- 916-919
- ISSN
- 1078-8956 (ISSN-L)
- 1546-170X
- OpenAlex
- W1567490604
- Cited by
- 2,012
- References
- 11
- Citations by year
- 2026: 23 · 2025: 36 · 2024: 38 · 2023: 41 · 2022: 49 · 2021: 32 · 2020: 73 · 2019: 46 · 2018: 41 · 2017: 48 · 2016: 76 · 2015: 66 · 2014: 107 · 2013: 89 · 2012: 107
- FWCI
- 67.08
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Medicine (publishedVersion)
- PubMed (publishedVersion)
- 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 › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, amyloid-beta, passive immunization, anti-amyloid antibodies, blood-brain barrier penetration, amyloid plaques, microglial phagocytosis, Fc receptors, PDAPP mice, amyloid precursor protein, plaque clearance, antibody therapy
- MeSH terms
- Alzheimer Disease, Animals, Antibodies, Disease Models, Animal, Humans, Immunization, Mice, Transgenic, Phagocytosis, Amyloid beta-Peptides, Mice, Plaque, Amyloid, In Vitro Techniques
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