The DOI matches its Crossref record; 47 of the 48 references it cites were found in a registry or an index.
Apolipoprotein E and Low Density Lipoprotein Receptor-related Protein Facilitate Intraneuronal Aβ42 Accumulation in Amyloid Model Mice
Open accessAbstract
The low density lipoprotein receptor-related protein (LRP) is highly expressed in the brain and has been shown to alter the metabolism of amyloid precursor protein and amyloid-beta peptide (Abeta) in vitro. Previously we developed mice that overexpress a functional LRP minireceptor (mLRP2) in their brains and crossed them to the PDAPP mouse model of Alzheimer disease. Overexpression of mLRP2 in 22-month-old PDAPP mice with amyloid plaques increased a pool of carbonate-soluble Abeta in the brain and worsened memory-related behavior. In the current study, we examined the effects of mLRP2 overexpression on 3-month-old PDAPP mice that had not yet developed amyloid plaques. We found significantly higher levels of membrane-associated Abeta42 in the hippocampus of mice that overexpressed mLRP2. Using immunohistochemical methods, we observed significant intraneuronal Abeta42 in the hippocampus and frontal cortex of PDAPP mice, which frequently co-localized with the lysosomal marker LAMP-1. Interestingly, PDAPP mice lacking apolipoprotein E (apoE) had much less intraneuronal Abeta42. We also found that PC12 cells overexpressing mLRP2 cleared Abeta42 and Abeta40 more rapidly from media than PC12 cells transfected with the vector only. Preincubation of apoE3 or apoE4 with Abeta42 increased the rate of Abeta clearance, and this effect was partially blocked by receptor-associated protein. Our results support the hypothesis that LRP binds and endocytoses Abeta42 both directly and via apoE…
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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., 2006
In the citing paper
“The propensity of ApoE to bind Ab and its efficient internalization by neurons implicates ApoE in promoting neuronal Ab uptake.15”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [15]
In the citing paper
“Overexpression of low-density lipoprotein receptor-related protein (LRP) in several neuronal cell lines resulted in increased intraneuronal Ab accumulation.15,40”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [15]
In the citing paper
“Similar to observations in APP SW /PS1 dE9 /ApoE KO mice, KO of ApoE in APP V717F mice was also reported to cause marked reduction in the intraneuronal Ab accumulation.15”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [15]
In the citing paper
“Modulating LRP1 has also been reported to affect brain apoE levels (Liu et al., 2007; Zerbinatti et al., 2006)”
From Overexpressing low‐density lipoprotein receptor reduces tau‐associated neurodegeneration in relation to apoE‐linked mechanisms (2021) · cites this paper as Zerbinatti et al., 2006
In the citing paper
“Conversely, overexpression of the LDL receptor (Kim et al., 2009) or of LRP1 mini receptors reduces systemic levels of APOE in the CNS (Zerbinatti et al., 2006).”
From The Pro-Neurotrophin Receptor Sortilin Is a Major Neuronal Apolipoprotein E Receptor for Catabolism of Amyloid-β Peptide in the Brain (2013) · cites this paper as Zerbinatti et al., 2006
In the citing paper
“Finally, neuron-specific inactivation of Lrp1 was shown to decrease (Liu et al., 2007) while overexpression of a LRP1 mini receptor to increase brain Aβ levels (Zerbinatti et al., 2006).”
From The Pro-Neurotrophin Receptor Sortilin Is a Major Neuronal Apolipoprotein E Receptor for Catabolism of Amyloid-β Peptide in the Brain (2013) · cites this paper as Zerbinatti et al., 2006
Citations
Cites
Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles
Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126
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
Billings, L. M., Oddo, S., Green, K. N., McGaugh, J. L., & LaFerla, F. M. (2005) · Neuron · doi:10.1016/j.neuron.2005.01.040 · Cited by 1,294
In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
Stine, W. B., Dahlgren, K. N., Krafft, G. A., & LaDu, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210207200 · Cited by 1,015
Intraneuronal Aβ42 Accumulation in Human Brain
Gouras, G. K., Tsai, J., Naslund, J., Vincent, B., Edgar, M., Checler, F., Greenfield, J. P., Haroutunian, V., Buxbaum, J. D., Xu, H., et al. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64700-1 · Cited by 991
Holtzman, D. M., Bales, K. R., Tenkova, T., Fagan, A. M., Parsadanian, M., Sartorius, L. J., Mackey, B., Olney, J., McKeel, D., Wozniak, D., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.050004797 · Cited by 937
Self-citationLRP: a multifunctional scavenger and signaling receptor
Herz, J., & Strickland, D. K. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13992 · Cited by 908
Lack of apolipoprotein E dramatically reduces amyloid β-peptide deposition
Bales, K. R., Verina, T., Dodel, R. C., Du, Y., Altstiel, L., Bender, M., Hyslop, P., Johnstone, E. M., Little, S. P., Cummins, D. J., et al. (1997) · Nature Genetics · doi:10.1038/ng1197-263 · Cited by 830
Self-citationLRP/Amyloid β-Peptide Interaction Mediates Differential Brain Efflux of Aβ Isoforms
Deane, R., Wu, Z., Sagare, A., Davis, J., Du Yan, S., Hamm, K., Xu, F., Parisi, M., LaRue, B., Hu, H. W., et al. (2004) · Neuron · doi:10.1016/j.neuron.2004.07.017 · Cited by 828
Takahashi, R. H., Milner, T. A., Li, F., Nam, E. E., Edgar, M. A., Yamaguchi, H., Beal, M. F., Xu, H., Greengard, P., & Gouras, G. K. (2002) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64463-x · Cited by 706
Flagged first, then by citations
1 of the 48 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Herz, 2001, J. Clin. Investig., 108, 779, 10.1172/JCI200113992 · DOI · Paper page
Cited by
Sorted by citations
Items 101–129 of 129
Origin(s) of Intraneuronal Amyloid
D’Andrea, M. R. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-804256-4.00002-4 · Cited by 2
Banerjee, V., Oren, O., Dagan, B., Taube, R., Engel, S., & Papo, N. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00491 · Cited by 2
Alzheimer disease models and human neuropathology: similarities and diVerences
Duyckaerts, C. J., Potier, M., & Delatour, B. (2008) · Cited by 2
Cell-type-specific APOE4 cascade across the Alzheimer’s disease continuum
Shostak, D. M., Liang, Z., & Huang, Y. (2026) · Neuron · doi:10.1016/j.neuron.2026.04.024 · Cited by 1
Autophagy-Derived Alzheimer’s Pathogenesis
Ling, D., & Paul, M. (2011) · InTech eBooks · doi:10.5772/17681 · Cited by 1
Stephens, G. S., You, J. C., Fu, C.-H., & Chin, J. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809324-5.21126-7 · Cited by 1
Yeast as a Model for Studying Aβ Aggregation, Toxicity and Clearance
Bharadwaj, P. (2011) · Australasian Journal of Paramedicine · Cited by 1
The Role of Apolipoprotein E Concentration and Isoform in Amyloid-beta Metabolism In Vivo
Castellano, J. M. (2011) · Open Scholarship Institutional Repository (Washington University in St. Louis) · doi:10.7936/k7416v3s
Brain sterol metabolism : modulating Alzheimer’s disease
Vanmierlo, T. (2010) · Research Publications (Maastricht University) · doi:10.26481/dis.20100930tv
Role of Oxidatively Stressed Lipids in Amyloid Formation and Toxicity
Axelsen, P. H., & Komatsu, H. (2010) · Wiley eBooks · doi:10.1002/9780470572702.ch27
Modulating Amyloid Beta Clearance by Altering Cellular and Whole Brain Apolipoprotein E Metabolism
Basak, J. M. (2014) · Open Scholarship Institutional Repository (Washington University in St. Louis) · doi:10.7936/k7dz06bk
Distinct Pools of -Amyloid in Alzheimer Disease–Affected Brain
Steinerman, J. R., Irizarry, M. C., Scarmeas, N., Raju, S., Brandt, J., Albert, M., Blacker, D., Hyman, B. T., & Stern, Y. (2022) · doi:10.7916/j0pe-r896
Pathological Consequences of Aβ From Extracellular to Intraneuronal
D’Andrea, M. R. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-804256-4.00004-8
Implications of Intraneuronal Aβ
D’Andrea, M. R. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-804256-4.00009-7
Is Apolipoprotein E4 an Important Risk Factor for Dementia in Persons with Down
Rohn, T. T., McCarty, K. L., Love, J. E., & Head, E. (2014)
Alzheimer’s Disease Therapeutics Targeting Apolipoprotein E
Liao, F., & Holtzman, D. M. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802173-6.00010-1
Self-citationIntraneuronal Amyloid and Plaque Formation
D’Andrea, M. R. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-804256-4.00005-x
Fitzsimmons, C., Johnstone, D. M., Conant, K. E., Hillaire, C. S., Parsons, C. H., Stins, M. F., Moir, R. D., & Milward, E. A. (2016) · Analytical Methods · doi:10.1039/c6ay02438f
PPARγ Agonists for the Treatment of Alzheimer's Disease
Jiang, Q., Mandrekar, S., & Landreth, G. E. (2007) · Springer eBooks · doi:10.1007/7355_2007_014
Foley, A. R., & Raskatov, J. A. (2022) · ChemBioChem · doi:10.1002/cbic.202200146
Negative Regulation of Cathepsins by β-Amyloid
Lundin, B., Comby, A.-C., Berezovska, O., & Maesako, M. (2024) · eNeuro · doi:10.1523/eneuro.0258-23.2023 · Cited by 2
Viana, R. J. S. (2010) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)
REGULATION OF LOW DENSITY LIPOPROTEIN RECEPTOR SPLICING EFFICIENCY
Ling, I. (2009) · UKnowledge (University of Kentucky)
Regulation of BAX/BAK-Dependent Cell Death Program
Kim, H. (2009) · Open Scholarship Institutional Repository (Washington University in St. Louis) · doi:10.7936/k7rb72m2
Self-citationRôle des ADAM dans le processus physiopathologique de la maladie d'Alzheimer
Laumet, G. O. (2010) · theses.fr (ABES) · doi:10.70675/94126786zf990z488ezb471z5f1d5686766c
Sepulveda-Diaz, J. E. (2013) · theses.fr (ABES) · doi:10.70675/56c42bcbz41dfz432bzbb78z77110b373285
Souchet, B. (2018) · theses.fr (ABES) · doi:10.70675/5510ef76zecf1z41f2z9496z015aa6a093be
Lysosomal Involvement in the Pathogenesis of Alzheimer's Disease
Zheng, L. P. (2012) · DiVA (Linkoping University)
Metadata
- Authors
- Zerbinatti, C. V., Wahrle, S. E., Kim, H., Cam, J. A., Bales, K., Paul, S. M., Holtzman, D. M., & Bu, G.
- Affiliations
- Washington University in St. Louis (US)
- Eli Lilly (United States) (US)
- Corresponding author
- Bu, Guojun
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-11
- Volume
- 281
- Issue
- 47
- Pages
- 36180-36186
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2041371648
- Cited by
- 129
- References
- 48
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 2 · 2023: 1 · 2022: 2 · 2021: 2 · 2020: 3 · 2019: 1 · 2018: 4 · 2017: 6 · 2016: 11 · 2015: 4 · 2014: 11 · 2013: 9 · 2012: 7
- FWCI
- 7.75
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
- Funders
- National Institute on Aging (R01AG027924)
- National Institute of Neurological Disorders and Stroke (F32-NS41872, F32NS041872)
- 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
- apolipoprotein E, low density lipoprotein receptor-related protein, amyloid-beta 42, amyloid plaques, PDAPP mice, Alzheimer's disease, amyloid clearance, lysosomes, LAMP1, receptor-associated protein, APOE3, APOE ε4, hippocampus, frontal cortex, memory impairment
- MeSH terms
- Animals, Apolipoproteins E, Brain, Endocytosis, Hippocampus, Humans, Immunohistochemistry, Lysosomes, Mice, Transgenic, Neurons, Peptide Fragments, Amyloid beta-Peptides, PC12 Cells, Low Density Lipoprotein Receptor-Related Protein-1, Mice, Rats
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review