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Increased soluble amyloid-β peptide and memory deficits in amyloid model mice overexpressing the low-density lipoprotein receptor-related protein
Open accessAbstract
Amyloid-β peptide (Aβ) is central to the pathogenesis of Alzheimer's disease, and the low-density lipoprotein receptor-related protein (LRP) has been shown to alter Aβ metabolism in vitro . Here, we show that overexpression of a functional LRP minireceptor in the brain of PDAPP mice results in age-dependent increase of soluble brain Aβ, with no changes in Aβ plaque burden. Importantly, soluble brain Aβ was found to be primarily in the form of monomers/dimers and to be highly correlated with deficits in spatial learning and memory. These results provide in vivo evidence that LRP may contribute to memory deficits typical of Alzheimer's disease by modulating the pool of small soluble forms of Aβ.
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“overexpression of a functional LRP1 minireceptor resulted in a 25% reduction of brain apoE levels, there was an age-dependent increase of soluble Aβ in the brain of PDAPP transgenic mice”
From ApoE4 reduction: An emerging and promising therapeutic strategy for Alzheimer's disease (2022) · cites this paper as Zerbinatti et al 2004
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“Although an ~25% reduction in brain apoE levels was observed in LRP1 transgenic mice, there was an increase in soluble and insoluble Aβ in old mice (Zerbinatti et al., 2006; Zerbinatti et al., 2004).”
From Overexpression of Low-Density Lipoprotein Receptor in the Brain Markedly Inhibits Amyloid Deposition and Increases Extracellular Aβ Clearance (2009) · cites this paper as Zerbinatti et al., 2004
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“LRP overexpression in APP V717F mice, besides augmenting intraneuronal Ab accumulation, exacerbated the memory deficit and caused an increase in soluble Ab level in the brain.41”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [41]
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“However, the transgene product was not full-length LRP and the transgene was not expressed by its endogenous promoter.”
From Receptor-Associated Protein (RAP) Plays a Central Role in Modulating Aβ Deposition in APP/PS1 Transgenic Mice (2008) · cites this paper as [24]
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“In a direct test of the role of LRP in amyloidogenesis, transgenic mice that overexpress an LRP-minireceptor, containing the ligand-binding domain II of human LRP and the region representing the transmembrane subunit including the full cytoplasmic tail (mLRP2), were mated to PDAPP mice [24].”
From Receptor-Associated Protein (RAP) Plays a Central Role in Modulating Aβ Deposition in APP/PS1 Transgenic Mice (2008) · cites this paper as [24]
In the citing paper
“The authors reported 3-fold increases in LRP levels and found increased soluble Aβ and enhanced memory impairment in PDAPP mice, but did not find evidence of a change in amyloid loads in mice harboring both transgenes as compared to mice harboring only the PDAPP transgene.”
From Receptor-Associated Protein (RAP) Plays a Central Role in Modulating Aβ Deposition in APP/PS1 Transgenic Mice (2008) · cites this paper as [24]
In the citing paper
“Zerbinatti et al. [24] reported that overexpression of an LRP minireceptor in the PDAPP mouse model of AD, resulted in increased levels of soluble Aβ but did not impact amyloid burden.”
From Receptor-Associated Protein (RAP) Plays a Central Role in Modulating Aβ Deposition in APP/PS1 Transgenic Mice (2008) · cites this paper as [24]
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Cites
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
Alzheimer's disease: the amyloid cascade hypothesis
Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484
Alzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
Alzheimer-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
Mucke, L., Masliah, E., Yu, G.-Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., & McConlogue, L. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-11-04050.2000 · Cited by 1,856
Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease
Lue, L.-F., Kuo, Y.-M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., Beach, T., Kurth, J. H., Rydel, R. E., & Rogers, J. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65184-x · Cited by 1,530
Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability
Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., & LaDu, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201750200 · Cited by 1,452
Research works printed but not linked: 1
- Rose K. Goldberg M. P. & Choi D. W. (1993) in Methods in Toxicology: In Vitro Biological Methods eds. Tyson C. A. & Frazier J. M. (Academic San Diego) pp. 46–60.
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Hladky, S. B., & Barrand, M. A. (2017) · Handbook of experimental pharmacology · doi:10.1007/164_2017_37 · Cited by 36
Yoon, I., Pietrzik, C. U., Kang, D. E., & Koo, E. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413729200 · Cited by 33
Wei, J., Fan, S., Liu, B.-S., Zhang, B., Su, J., & Yu, D. (2017) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2017.06.030 · Cited by 31
Mattei, V., Manganelli, V., Martellucci, S., Capozzi, A., Mantuano, E., Longo, A., Ferri, A., Garofalo, T., Sorice, M., & Misasi, R. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14891 · Cited by 30
Relationship of APOE, age at onset, amyloid and clinical phenotype in Alzheimer disease
Whitwell, J. L., Tosakulwong, N., Weigand, S. D., Graff‐Radford, J., Ertekin‐Taner, N., Machulda, M. M., Duffy, J. R., Schwarz, C. G., Senjem, M. L., Jack, C. R., et al. (2021) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2021.08.012 · Cited by 29
A megalin polymorphism associated with promoter activity and Alzheimer's disease risk
Vargas, T., Bullido, M. J., Martı́nez-Garcı́a, A., Antequera, D., Clarimón, J., Rosich-Estragó, M., Martín‐Requero, Á., Mateo, I., Rodríguez‐Rodríguez, E., Cuadrada, E. V., et al. (2010) · American Journal of Medical Genetics Part B Neuropsychiatric Genetics · doi:10.1002/ajmg.b.31056 · Cited by 29
LRP1 Downregulates the Alzheimer’s β-Secretase BACE1 by Modulating Its Intraneuronal Trafficking
Tanokashira, D., Motoki, K., Minegishi, S., Hosaka, A., Mamada, N., Tamaoka, A., Okada, T., Lakshmana, M. K., & Araki, W. (2015) · eNeuro · doi:10.1523/eneuro.0006-15.2015 · Cited by 25
Molecular Mechanism and Kinetics of Amyloid-β42 Aggregate Formation: A Simulation Study
Man, V. H., He, X., Ji, B., Liu, S., Xie, X., & Wang, J. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00473 · Cited by 26
Xu, G. M., Green, C. C., Fromholt, S., & Borchelt, D. (2012) · Alzheimer s Research & Therapy · doi:10.1186/alzrt110 · Cited by 21
Gelsolin Restores A β -Induced Alterations in Choroid Plexus Epithelium
Vargas, T., Antequera, D., Ugalde, C., Spuch, C., & Carro, E. (2010) · BioMed Research International · doi:10.1155/2010/805405 · Cited by 21
RetractedKalanxhi, E., & Dahle, J. (2011) · Radiation Research · doi:10.1667/rr2694.1 · Cited by 21
Lim, S., Choi, J. G., Moon, M., Kim, H. G., Lee, W., Bak, H.-R., Sung, H.-C., Park, C. H., Kim, S. Y., & Oh, M. S. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-150839 · Cited by 21
Wang, X., Miao, Y., Abulizi, J., Fu, L., Mo, Y., Wei-guo, X., & Li, Z. (2016) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2016/7603975 · Cited by 21
Lv, W., Zhang, J., Jiao, A., Wang, B., Chen, B., & Lin, J. (2018) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2016-0686 · Cited by 21
Guan, P.-P., Yang, L., Xu, G., & Wang, P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158185 · Cited by 21
Pan, T.-T., Sun, Y., Shi, Y.-F., Zhao, M., Khan, N. U., Chen, H., Ji, W., Li, J., Han, L., & Ma, Q. (2025) · Alzheimer s Research & Therapy · doi:10.1186/s13195-025-01840-5 · Cited by 19
Soluble Aβ and cognitive function in aged F-344 rats and Tg2576 mice
Lindner, M. D., Hogan, J. B., KRAUSE, R., Machet, F., Bourin, C., HODGESJR, D., Corsa, J. A., Barten, D. M., Toyn, J. H., & Stock, D. A. (2006) · Behavioural Brain Research · doi:10.1016/j.bbr.2006.06.003 · Cited by 19
Sethiya, N. K., Ghiloria, N., Srivastav, A., Bisht, D., Chaudhary, S. K., Walia, V., & Alam, M. S. (2023) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527322666230718105358 · Cited by 20
Liao, G., Zhou, M., Cheung, S., Galeano, J., Nguyen, N. V., Baudry, M., & Bi, X. (2008) · Brain Research · doi:10.1016/j.brainres.2008.10.022 · Cited by 16
Chen, Q., Zhang, Y., & Zhao, Q. (2020) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2020.09.021 · Cited by 15
Metadata
- Authors
- Zerbinatti, C. V., Wozniak, D. F., Cirrito, J., Cam, J. A., Osaka, H., Bales, K. R., Zhuo, M., Paul, S. M., Holtzman, D. M., & Bu, G.
- Affiliations
- University of Toronto (CA)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2004-01-19
- Volume
- 101
- Issue
- 4
- Pages
- 1075-1080
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC327153
- OpenAlex
- W2007048586
- Cited by
- 133
- References
- 43
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 3 · 2023: 2 · 2022: 1 · 2021: 4 · 2020: 2 · 2019: 4 · 2018: 2 · 2017: 8 · 2016: 5 · 2015: 3 · 2014: 4 · 2013: 9 · 2012: 12
- FWCI
- 7.01
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
- Funders
- National Institute on Aging (AG11355, P 50 AG05681, P50AG005681, P01AG011355)
- National Institute of Neurological Disorders and Stroke (NS41872, F32NS041872)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid-beta, soluble amyloid-beta, low density lipoprotein receptor-related protein, Alzheimer's disease, memory impairment, spatial learning, PDAPP mice, amyloid-beta metabolism, brain
- MeSH terms
- Animals, Brain, Cells, Cultured, Enzyme-Linked Immunosorbent Assay, Memory Disorders, Mice, Inbred C3H, Solubility, Amyloid beta-Peptides, LDL-Receptor Related Proteins, Mice
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