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Evidence for aggregation-independent, PrP C -mediated Aβ cellular internalization
Abstract
Significance: Amyloid β (Aβ) aggregation has been the therapeutic target of several Alzheimer’s disease (AD) clinical trials. Aβ exists in many different aggregated forms, making it exceedingly challenging to target. Evidence links intracellular Aβ accumulation and AD pathogenesis. We report that amino acids 1 to 30 of Aβ, Aβ (1–30), do not aggregate yet display cellular uptake stereospecificity when compared to its mirror image, suggesting that Aβ uptake is predominantly receptor-mediated and may be independent from its aggregation state. Additionally, we found Aβ (1–30) internalization to depend on PrP C expression. Aβ (1–30) thus represents a powerful tool to study mechanisms of Aβ cellular internalization and suggests that Aβ uptake could be modulated by therapeutically targeting high-affinity Aβ receptors.
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“Given that PrPC can bind APP and can alter levels of Aβ40 and Aβ42 [38]”
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Cites
Intracellular amyloid-β in Alzheimer's disease
LaFerla, F. M., Green, K. N., & Oddo, S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2168 · Cited by 1,942
Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M. (2009) · Nature · doi:10.1038/nature07761 · Cited by 1,560
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
History and progress of hypotheses and clinical trials for Alzheimer’s disease
Liu, P.-P., Xie, Y., Meng, X.-Y., & Kang, J.-S. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0063-8 · Cited by 723
Um, J. W., Kaufman, A. C., Kostylev, M., Heiss, J. K., Stagi, M., Takahashi, H., Kerrisk, M. E., Vortmeyer, A., Wisniewski, T., Koleske, A. J., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.06.036 · Cited by 572
Mechanisms of Aβ Clearance and Degradation by Glial Cells
Ries, M., & Sastre, M. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00160 · Cited by 527 · cited 7×
“S. Jin et al., Amyloid-β(1-42) aggregation initiates its cellular uptake and cytotoxicity.”
BackgroundInfluentialSynthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein
Balducci, C., Beeg, M., Stravalaci, M., Bastone, A., Sclip, A., Biasini, E., Tapella, L., Colombo, L., Manzoni, C., Borsello, T., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911829107 · Cited by 466
Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide
Hu, X., Crick, S. L., Bu, G., Frieden, C., Pappu, R. V., & Lee, J.-M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911281106 · Cited by 426 · cited 8×
“An increase in intracellular Aβ can create local gradients of particularly high concentrations of Aβ which may favor intracellular Aβ aggregation, ultimately leading to increased pathogenicity and extracellular release of Aβ aggregates which can further act as a seed for fibril growth (10, 11).”
BackgroundInfluentialMechanism of amyloid plaque formation suggests an intracellular basis of Aβ pathogenicity
Friedrich, R. P., Tepper, K., Rönicke, R., Soom, M., Westermann, M., Reymann, K., Kaether, C., & Fändrich, M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904532106 · Cited by 303 · cited 8×
“An increase in intracellular Aβ can create local gradients of particularly high concentrations of Aβ which may favor intracellular Aβ aggregation, ultimately leading to increased pathogenicity and extracellular release of Aβ aggregates which can further act as a seed for fibril growth (10, 11).”
BackgroundInfluentialA resurrection of aducanumab for Alzheimer's disease
Schneider, L. (2020) · The Lancet Neurology · doi:10.1016/s1474-4422(19)30480-6 · Cited by 286 · cited 7×
“S. Jin et al., Amyloid-β(1-42) aggregation initiates its cellular uptake and cytotoxicity.”
BackgroundInfluentialAmyloid-β Receptors: The Good, the Bad, and the Prion Protein
Jarosz-Griffiths, H. H., Noble, E., Rushworth, J. V., & Hooper, N. M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.702704 · Cited by 256
A 3D human brain–like tissue model of herpes-induced Alzheimer’s disease
Cairns, D. M., Rouleau, N., Parker, R. N., Walsh, K. G., Gehrke, L., & Kaplan, D. L. (2020) · Science Advances · doi:10.1126/sciadv.aay8828 · Cited by 247
Zerbinatti, C. V., Wahrle, S. E., Kim, H., Cam, J. A., Bales, K., Paul, S. M., Holtzman, D. M., & Bu, G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604436200 · Cited by 129
Cao, Q., Shin, W. S., Chan, H., Vuong, C. K., Dubois, B., Li, B., Murray, K. A., Sawaya, M. R., Feigon, J., Black, D. L., et al. (2018) · Nature Chemistry · doi:10.1038/s41557-018-0147-z · Cited by 75
Is the Mirror Image a True Reflection? Intrinsic Membrane Chirality Modulates Peptide Binding
Henriques, S. T., Peacock, H., Benfield, A. H., Wang, C. K., & Craik, D. J. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b11194 · Cited by 56 · cited 7×
“However, recent work performed by Craik and coworkers demonstrated that the chirality of membrane phospholipids can also modulate interactions of peptides with membranes (33).”
BackgroundInfluential
Research works printed but not linked: 45
- 10.1146/annurev-neuro-061010-113613 · DOI · Paper page
- 10.1038/nrm2101 · DOI · Paper page
- 10.1126/science.1079469 · DOI · Paper page
- 10.1016/S0896-6273(03)00434-3 · DOI · Paper page
- 10.1038/nm.1868 · DOI
- 10.1016/j.nbd.2018.01.015 · DOI
- 10.1073/pnas.1605104113 · DOI
- 10.1038/s41598-017-02227-9 · DOI
- 10.1016/S0306-4522(01)00460-2 · DOI
- 10.1074/jbc.M112.400358 · DOI
- 10.1038/s41467-018-07699-5 · DOI
- 10.1523/JNEUROSCI.0395-10.2010 · DOI · Paper page
- 10.1093/brain/awt375 · DOI
- 10.1093/brain/awv356 · DOI
- 10.1002/anie.201706279 · DOI
- 10.1002/cbic.201800708 · DOI
- Z. Y. Wang ., Knockdown of prion protein (PrP) by RNA interference weakens the protective activity of wild-type PrP against copper ion and antagonizes the cytotoxicity of fCJD-associated PrP mutants in cultured cells. Int. J. Mol. Med. 28, 413–421 (2011).
- 10.1074/jbc.M116.762526 · DOI
- 10.1016/j.molcel.2018.10.009 · DOI
- 10.1073/pnas.87.12.4761 · DOI
- 10.1073/pnas.1112600108 · DOI
- 10.1073/pnas.89.16.7437 · DOI · Paper page
- 10.1016/j.bbapap.2010.10.012 · DOI
- 10.1074/jbc.RA118.003319 · DOI
- 10.1074/jbc.M112.423954 · DOI
- 10.1016/bs.apha.2017.09.007 · DOI
- 10.1146/annurev.pathmechdis.3.121806.154326 · DOI
- 10.1021/acschemneuro.9b00646 · DOI
- 10.1038/ncomms1341 · DOI
- 10.1371/journal.pone.0159119 · DOI
- 10.1126/science.1242077 · DOI · Paper page
- 10.1523/JNEUROSCI.1459-11.2011 · DOI
- 10.1523/JNEUROSCI.1327-16.2016 · DOI
- 10.1021/bi971843e · DOI
- 10.1038/s41557-018-0031-x · DOI
- 10.1074/jbc.M115.691840 · DOI
- 10.1126/sciadv.1600947 · DOI
- 10.1073/pnas.1618417114 · DOI
- 10.3389/fgene.2018.00362 · DOI
- 10.1007/s40263-020-00737-1 · DOI
- 10.1371/journal.pone.0021456 · DOI
- G. P. Roseman “The central region of the cellular prion protein attenuates the intrinsic toxicity of N-terminus ” PhD thesis University of California Santa Cruz CA (2019).
- 10.1016/j.str.2016.04.017 · DOI
- 10.1016/j.str.2012.12.002 · DOI
- 10.1007/BF00197809 · DOI
Cited by
Sorted by citations
Di Caro, V., Cho, E., Thiel, J., Lizama, B. N., Koel-Simmelink, M. J. A., Pandey, K., Duong, D., Seyfried, N. T., Grundman, M., Teunissen, C. E., et al. (2026) · Alzheimer's Research & Therapy · doi:10.1186/s13195-026-02025-4 · Cited by 1
Metadata
- Authors
- Foley, A. R., Roseman, G. P., Chan, K., Smart, A., Finn, T. S., Yang, K., Lokey, R. S., Millhauser, G. L., & Raskatov, J. A.
- Affiliations
- Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2020-11-02
- Volume
- 117
- Issue
- 46
- Pages
- 28625-28631
- ISSN
- 0027-8424
- 1091-6490
- Cited by
- 38
- References
- 15
- Language
- en
- Funders
- HHS | National Institutes of Health (2R25GM058903-20-IMSD, R21AG058074, R35GM131781, S10OD024980, S10OD018455, GM131135)
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