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The cytoplasmic domain of the LDL receptor-related protein regulates multiple steps in APP processing
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The low-density lipoprotein receptor-related protein (LRP) has recently been implicated in numerous intracellular signaling functions, as well as in Alzheimer's disease pathogenesis. Studies have shown that the beta-amyloid precursor protein (APP) interacts with LRP and that this association may impact the production of amyloid beta-protein (Abeta). In this report, we provide evidence that LRP regulates trafficking of intracellular proteins independently of its lipoprotein receptor functions. We show that in the absence of LRP, Abeta production, APP secretion, APP internalization, turnover of full-length APP and stability of APP C-terminal fragments are affected. Importantly, these changes are not APP isoform dependent. Using deletion constructs, the critical region in LRP that modulates APP processing was mapped to a seven peptide domain around the second NPXY domain (residues 4504-4510). Therefore, we propose a model by which LRP functionally modulates APP processing, including those steps critical for Abeta production, through interactions of the cytosolic domains.
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“For example, unlike LDLR, LRP1 is an APP binding protein that influences APP endocytic trafficking and cellular distribution such that processing to Aβ and its extracellular release is enhanced (Pietrzik et al., 2002; Ulery et al., 2000).”
From Overexpression of Low-Density Lipoprotein Receptor in the Brain Markedly Inhibits Amyloid Deposition and Increases Extracellular Aβ Clearance (2009) · cites this paper as Pietrzik et al., 2002
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“In addition, an interaction between the C-terminal domain of APP and LRP, mediated by the cytoplasmic adaptor protein Fe65, impacts APP internalization (18 -23).”
From The Low Density Lipoprotein Receptor-related Protein (LRP) Is a Novel β-Secretase (BACE1) Substrate (2005) · cites this paper as [20]
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“Since LRP1 is known to increase the production of Aβ peptide (Ulery et al., 2000; Pietrzik et al., 2002), LRP1-deficient cell lines were chosen to eliminate any possible contribution of LRP1 to this process.”
From LRAD3, A Novel Low-Density Lipoprotein Receptor Family Member That Modulates Amyloid Precursor Protein Trafficking (2011) · cites this paper as Pietrzik et al., 2002
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“Co-transfection with LC did not enhance BACE internalization from the cell surface in LRP-null CHO cells (13-5-1) in contrast to known enhancement of APP endocytosis with LC (20).”
From The Low Density Lipoprotein Receptor-related Protein (LRP) Is a Novel β-Secretase (BACE1) Substrate (2005) · cites this paper as [20]
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“Likely, the multiple alternative functions assigned to this receptor in AD, including intracellular APP transport (Ulery et al., 2000; Pietrzik et al., 2002), blockade of APP signaling (Kinoshita et al., 2003), or Aβ shunt across the blood-brain-barrier (Deane et al., 2004) complicate interpretation of the available experimental data.”
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 Pietrzik et al., 2002
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Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876
Morgenstern, J. P., & Land, H. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.12.3587 · Cited by 2,099
Shibata, M., Yamada, S., Kumar, S. R., Calero, M., Bading, J., Frangione, B., Holtzman, D. M., Miller, C. A., Strickland, D. K., Ghiso, J., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10498 · Cited by 1,413
A Transcriptively Active Complex of APP with Fe65 and Histone Acetyltransferase Tip60
Cao, X., & Südhof, T. C. (2001) · Science · doi:10.1126/science.1058783 · Cited by 1,202
Identification of a Novel Aspartic Protease (Asp 2) as β-Secretase
Hussain, I., Powell, D., Howlett, D. R., Tew, D. G., Meek, T. D., Chapman, C., Gloger, I. S., Murphy, K. E., Southan, C. D., Ryan, D. M., et al. (1999) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.1999.0811 · Cited by 1,080
Hiesberger, T., Trommsdorff, M., Howell, B. W., Goffinet, A., Mumby, M. C., Cooper, J. A., & Herz, J. (1999) · Neuron · doi:10.1016/s0896-6273(00)80861-2 · Cited by 916
Evidence that production and release of amyloid beta-protein involves the endocytic pathway
Koo, E. H., & Squazzo, S. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32449-3 · Cited by 829
Self-citationDistinct sites of intracellular production for Alzheimer's disease Aβ40/42 amyloid peptides
Hartmann, T., Bieger, S. C., Brühl, B., Tienari, P. J., Ida, N., Allsop, D., Roberts, G. W., Masters, C. L., Dotti, C. G., Unsicker, K., et al. (1997) · Nature Medicine · doi:10.1038/nm0997-1016 · Cited by 719
Proteolytic processing and cell biological functions of the amyloid precursor protein
Strooper, B. D., & Annaert, W. G. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.11.1857 · Cited by 643
Trommsdorff, M., Borg, J.-P., Margolis, B., & Herz, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.50.33556 · Cited by 453
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Betts, G. N., van der Geer, P., & Komives, E. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709514200 · Cited by 43
Waldron, E., Isbert, S., Kern, A., Jaeger, S., Martín, A., Hébert, S. S., Behl, C., Weggen, S., Strooper, B. D., & Pietrzik, C. U. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.05.003 · Cited by 43
Self-citationRanganathan, S., Cao, C., Catania, J., Migliorini, M., Zhang, L., & Strickland, D. K. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.265413 · Cited by 41
von Einem, B., Schwanzar, D., Rehn, F., Beyer, A.-S., Weber, P., Wagner, M., Schneckenburger, H., & Arnim, C. A. F. V. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2010.05.017 · Cited by 40
Hunter, S., Arendt, T., & Brayne, C. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8445-3 · Cited by 41
Chen, X., Wagener, J. F., Morgan, D. H., Hui, L., Ghribi, O., & Geiger, J. D. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-101323 · Cited by 42
Rabiej, V. K., Pflanzner, T., Wagner, T., Goetze, K., Storck, S. E., Eble, J. A., Weggen, S., Mueller‐Klieser, W., & Pietrzik, C. U. (2015) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.11.020 · Cited by 39
Self-citationAssociation of ApoE and LRP mRNA levels with dementia and AD neuropathology
Akram, A. M., Schmeidler, J., Katsel, P., Hof, P. R., & Haroutunian, V. H. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.04.010 · Cited by 37
Polymorphisms of APOE and LRP Genes in Brazilian Individuals With Alzheimer Disease
Bahia, V. S., Kok, F., Marie, S. K. N., Oba‐Shinjo, S. M., Caramelli, P., & Nitríni, R. (2008) · Alzheimer Disease & Associated Disorders · doi:10.1097/wad.0b013e31815a9da7 · Cited by 37
Rolyan, H., Feike, A. C., Upadhaya, A. R., Waha, A., Dooren, T. V., Haass, C., Birkenmeier, G., Pietrzik, C. U., LEUVEN, F. V., & Thal, D. R. (2011) · Journal of Neural Transmission · doi:10.1007/s00702-010-0572-7 · Cited by 39
Self-citationInactivation of the proximal NPXY motif impairs early steps in LRP1 biosynthesis
Reekmans, S. M., Pflanzner, T., Gordts, P. L. S. M., Isbert, S., Zimmermann, P., Annaert, W. G., Weggen, S., Roebroek, A., & Pietrzik, C. U. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0171-7 · Cited by 39
Self-citationPassarella, D., Ciampi, S., Liberto, V. D., Zuccarini, M., Ronci, M., Medoro, A., Foderà, E., Frinchi, M., Mignogna, D., Russo, C., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23168921 · Cited by 38
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Hooper, N. M., Taylor, D. R., & Watt, N. T. (2008) · Biochemical Society Transactions · doi:10.1042/bst0361272 · Cited by 35
Ruzali, W. A. W., Kehoe, P. G., & Love, S. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121336 · Cited by 36
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Zhang, Y., Gao, H., Zheng, W., & Xu, H. J. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105824 · Cited by 31
Lichtenthaler, S. F. (2006) · Neurodegenerative Diseases · doi:10.1159/000095265 · Cited by 30
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Wiley, J. C., Smith, E. A., Hudson, M. P., Ladiges, W., & Bothwell, M. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706024200 · Cited by 28
Hu, Q., Wang, L., Yang, Z., Cool, B. H., Zitnik, G., & Martin, G. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411855200 · Cited by 28
Kang, D. E., Roh, S. E., Woo, J. A., Liu, T., Bu, J. H., Jung, A., & Lim, Y. (2011) · Experimental Neurobiology · doi:10.5607/en.2011.20.2.67 · Cited by 26
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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
Medoro, A., Bartollino, S., Mignogna, D., Passarella, D., Porcile, C., Pagano, A., Florio, T., Nizzari, M., Guerra, G., Marco, R. D., et al. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170628 · Cited by 25
Matrone, C. (2013) · BioEssays · doi:10.1002/bies.201300041 · Cited by 24
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Waldron, E., Jaeger, S., & Pietrzik, C. U. (2006) · Neurodegenerative Diseases · doi:10.1159/000095261 · Cited by 24
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Ruzali, W. A. W., Kehoe, P. G., & Love, S. (2012) · Neuroscience Letters · doi:10.1016/j.neulet.2012.07.065 · Cited by 25
Guan, P.-P., Yang, L., Xu, G., & Wang, P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158185 · Cited by 21
Čaušević, M., Ramoz, N., Haroutunian, V. H., Davis, K. L., & Buxbaum, J. D. (2003) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/62.10.999 · Cited by 19
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Spoelgen, R., Adams, K. W., Koker, M., Thomas, A. V., Andersen, O. M., Hallett, P. J., Bercury, K. K., Joyner, D., Deng, M., Stoothoff, W. H., et al. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.10.061 · Cited by 17
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Arriagada, C., Bustamante, M., Atwater, I. J., Rojas, E., Caviedes, R., & Caviedes, P. A. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.12.062 · Cited by 15
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Self-citationPetersen, H. H., Hilpert, J., Jacobsen, C. B., Lauwers, A., Roebroek, A., & Willnow, T. E. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.03.069 · Cited by 14
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Takano-Kawabe, K., Matoba, K., Nakamura, Y., & Moriyama, M. (2023) · Neurochemical Research · doi:10.1007/s11064-023-04022-7 · Cited by 10
Cuzzo, L. M., Ross‐Cisneros, F. N., Yee, K. M. P., Wang, M. Y., & Sadun, A. A. (2011) · Journal of Neuro-Ophthalmology · doi:10.1097/wno.0b013e31821b602c · Cited by 10
Chen, G., Payne, T. J., Lou, X.-Y., Ma, J. Z., Zhu, J. Z., & Li, M. D. (2008) · Human Genetics · doi:10.1007/s00439-008-0558-9 · Cited by 11
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Shi, X., Ren, S., Zhang, B., Guo, S., He, W., Yuan, C., Yang, X., Ig-lzevbekhai, K., Sun, T., Wang, Q., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-90982-1 · Cited by 9
Larios, J. A., & Marzolo, M.-P. (2012) · Frontiers in Biology · doi:10.1007/s11515-011-1186-7 · Cited by 9
Kim, W. S., Hill, A. F., Fitzgerald, M. L., Freeman, M. W., Evin, G. M., & Garner, B. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110521 · Cited by 10
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Mulvihill, M. M., Guttman, M., & Komives, E. A. (2011) · Biochemistry · doi:10.1021/bi200508f · Cited by 8
Orlando, R. A. (2003) · Experimental Cell Research · doi:10.1016/j.yexcr.2003.11.004 · Cited by 8
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Minopoli, G., Passaro, F., Aloia, L., Carlomagno, F., Melillo, R. M., Santoro, M. M., Forzati, F., Zambrano, N., & Russo, T. (2007) · Neurodegenerative Diseases · doi:10.1159/000101833 · Cited by 7
Hou, H., Habib, A., Zi, D., Tian, K., Tian, J., Giunta, B. N., Sawmiller, D. R., & Tan, J. (2017) · NeuroMolecular Medicine · doi:10.1007/s12017-017-8446-x · Cited by 6
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Li, Q., Shang, Y., Huang, H., Dai, X., & Lao, F. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05329-y · Cited by 5
Grana, T. R., LaMarre, J., & Kalisch, B. E. (2012) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-012-9894-3 · Cited by 5
Pashaei, S., Shabani, S., Mohammadi, S., Morozova‐Roche, L. A., Salari, N., Rahimi, Z., & Khodarahmi, R. (2024) · Neurochemical Research · doi:10.1007/s11064-024-04253-2 · Cited by 4
Xu, J., Huang, X., Guo, Y., Ma, X., Li, P., Zhou, S., Zhang, C., Chen, R., Halm‐Lutterodt, N. V., & Yuan, L. (2022) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12855 · Cited by 4
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Hunter, S., & Brayne, C. (2013) · Springer eBooks · doi:10.1007/978-3-642-30574-0_52 · Cited by 3
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Wu, P., Bhore, N., Lee, Y.-L., Chou, J., Chen, Y., Wu, P., Hsu, W., Lee, H., Huang, Y., Lu, P., et al. (2020) · The FASEB Journal · doi:10.1096/fj.202000113r · Cited by 2
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Marr, R. A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802851-3.00004-8 · Cited by 2
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Tam, J. H. K. (2015) · Scholarship@Western (Western University)
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de dans la maladie d'Alzheimer
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Auderset, L. (2020) · UTAS Research Repository · doi:10.25959/100.00034806
Cuchillo‐Ibáñez, I., Lennol, M. P., Escamilla, S., Mata‐Balaguer, T., López‐Font, I., Ferrer, I., & Sáez‐Valero, J. (2021) · Research Square · doi:10.21203/rs.3.rs-220026/v1
Pur-alpha participates in the progression of Alzheimer's disease through direct and indirect waysPreprint
Shi, X., Ren, S., Zhang, B., Guo, S., He, W., Yuan, C., Yang, X., Ig-lzevbekhai, K., Sun, T., Wang, Q., et al. (2020) · doi:10.21203/rs.3.rs-19973/v1
The role of NPxY domains in LRP1 receptor maturation and function
Pflanzner, T. (2011) · Gutenberg Open Science · doi:10.25358/openscience-3281
Margolis, B. L., & Traub, L. M. (2008) · Wiley eBooks · doi:10.1002/9783527610754.pp04
Brain endothelial LRP1 maintains blood brain-barrier integrityPreprint
Storck, S. E., & Pietrzik, C. U. (2021) · Research Square · doi:10.21203/rs.3.rs-233246/v1
Self-citationAssays for Analysis of APP Secretion and Recycling
Yamazaki, T., Koo, E. H., & Kummer, M. P. (2004) · CRC Press eBooks · doi:10.1201/9780203492185.ch2
Self-citationPur-alpha participates in the progression of Alzheimer's disease through direct and indirect waysPreprint
Shi, X., Ren, S., Zhang, B., Guo, S., He, W., Yuan, C., Yang, X., Ig-lzevbekhai, K., Sun, T., Wang, Q., et al. (2020) · doi:10.21203/rs.3.rs-21919/v1
Alzheimer’s Research Gains Momentum and Spreads Out
Behl, C. (2023) · Springer eBooks · doi:10.1007/978-3-031-31570-1_14
Die Amyloid-Forschung zieht weitere Kreise und nimmt Fahrt auf
Behl, C. (2026) · Springer eBooks · doi:10.1007/978-3-662-72210-7_14
Chandrashekar, D. V., Roules, G. C., Panchal, U. R., Jagadeesan, N., Newhart, C., Chu, J., Carson, B., Win, S., Than, T. A., Kaplowitz, N., et al. (2026) · Research Square · doi:10.21203/rs.3.rs-10843451/v1
Wenhua, Y., Wenjing, M., Yan, D., Fei, L., Chen, J., Xia, T., Guan, Y., Xin, L., Huang, Y., Guo, Y., et al. (2026) · Frontiers in Neurology · doi:10.3389/fneur.2026.1934307
Metadata
- Authors
- Pietrzik, C. U., Busse, T., Merriam, D. E., Weggen, S., & Koo, E. H.
- Affiliations
- University of California San Diego (US)
- Corresponding author
- Koo, Edward H.
- Venue
- The EMBO Journal
- Published
- 2002-11-01
- Volume
- 21
- Issue
- 21
- Pages
- 5691-5700
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC131065
- OpenAlex
- W2069323313
- Cited by
- 198
- References
- 46
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 3 · 2023: 4 · 2022: 4 · 2021: 7 · 2020: 5 · 2019: 3 · 2018: 4 · 2017: 9 · 2016: 4 · 2015: 4 · 2014: 4 · 2013: 9 · 2012: 14
- FWCI
- 8.21
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Health Assistance Foundation
- National Institutes of Health
- National Institute on Aging (AG 12376, R01AG012376)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- low density lipoprotein receptor-related protein, APP processing, amyloid precursor protein, amyloid-beta production, APP secretion, APP C-terminal fragments, NPXY motif, cytoplasmic domain, Alzheimer's disease, protein trafficking
- MeSH terms
- Animals, Cell Line, Cytoplasm, Enzyme-Linked Immunosorbent Assay, Fibroblasts, Precipitin Tests, Protein Processing, Post-Translational, Blotting, Western, Amyloid beta-Protein Precursor, DNA, Complementary, Low Density Lipoprotein Receptor-Related Protein-1, Mice
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