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The cytoplasmic domain of the LDL receptor-related protein regulates multiple steps in APP processing
Open accessAbstract
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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May, P., & Herz, J. (2003) · Traffic · doi:10.1034/j.1600-0854.2003.00086_4_5.x · Cited by 60
Auderset, L., Cullen, C. L., & Young, K. M. (2016) · PLOS ONE · doi:10.1371/journal.pone.0155878 · Cited by 62
LRP1 modulates APP trafficking along early compartments of the secretory pathway
Waldron, E., Heilig, C., Schweitzer, A., Nadella, N., Jaeger, S., Martin, A. M., Weggen, S., Brix, K., & Pietrzik, C. U. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.04.006 · Cited by 61
Self-citationPocivavsek, A., MIKHAILENKO, I. A., Strickland, D. K., & Rebeck, G. W. (2009) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2009.06.010 · Cited by 63
Lakshmana, M. K., Chung, J. Y., Wickramarachchi, S., Tak, E., Bianchi, E., Koo, E. H., & Kang, D. E. (2009) · The FASEB Journal · doi:10.1096/fj.09-136457 · Cited by 58
Self-citationAPP Processing and the APP-KPI Domain Involvement in the Amyloid Cascade
Menéndez‐González, M., Pérez‐Piñera, P., Martínez-Rivera, M., Calatayud, M. T. R., & Menes, B. B. (2005) · Neurodegenerative Diseases · doi:10.1159/000092315 · Cited by 68
Erickson, M. A., Niehoff, M. L., Farr, S. A., Morley, J. E., Dillman, L. A., Lynch, K. M., & Banks, W. A. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111517 · Cited by 58
Genomics of Dementia:APOE- andCYP2D6-Related Pharmacogenetics
Cacabelos, R., Martínez, R., Fernández‐Novoa, L., Carril, J. C., Lombardi, V., Carrera, I., Corzo, L., Tellado, I., Leszek, J., McKay, A., et al. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/518901 · Cited by 55
LRP-1: Functions, Signaling and Implications in Kidney and Other Diseases
Lin, L., & Hu, K. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms151222887 · Cited by 60
Receptor-associated Protein Interacts with Amyloid-β Peptide and Promotes Its Cellular Uptake
Kanekiyo, T., & Bu, G. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.015032 · Cited by 44
Bilousova, T. V., Melnik, M., Miyoshi, E., Gonzalez, B. L., Poon, W. W., Vinters, H. V., Miller, C. A., Corrada, M. M., Kawas, C. H., Hatami, A., et al. (2019) · American Journal Of Pathology · doi:10.1016/j.ajpath.2019.04.010 · Cited by 57
PCSK9 acts as a key regulator of Aβ clearance across the blood–brain barrier
Mazura, A. D., Ohler, A., Storck, S. E., Kurtyka, M., Scharfenberg, F., Weggen, S., Becker-Pauly, C., & Pietrzik, C. U. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04237-x · Cited by 53
“Rabbit anti-1704 antibody was used to identify the LRP1 β-chain [46].”
MethodSelf-citationConcepts for the treatment of Alzheimer's disease: molecular mechanisms and clinical application
Pietrzik, C. U., & Behl, C. (2005) · International Journal of Experimental Pathology · doi:10.1111/j.0959-9673.2005.00435.x · Cited by 52
Self-citationLRP1 is critical for the surface distribution and internalization of the NR2B NMDA receptor subtype
Maier, W., Bednorz, M., Meister, S., Roebroek, A., Weggen, S., Schmitt, U., & Pietrzik, C. U. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-25 · Cited by 50
Self-citationPathogenic mechanisms in Alzheimer's disease
Pastorino, L., & Lu, K. P. (2006) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2006.06.078 · Cited by 52
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“The association of LRP with APP alters its cellular trafficking, resulting in an increase in the production of the A peptide (Ulery et al., 2000; Pietrzik et al., 2002, 2004), and thus LRP1 has been implicated in the pathology of Alzheimer’s disease.”
BackgroundMethodImpact of late-onset Alzheimer’s genetic risk factors on beta-amyloid endocytic production
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Pivotal role of RanBP9 in integrin‐dependent focal adhesion signaling and assembly
Woo, J. A., Roh, S., Lakshmana, M. K., & Kang, D. E. (2012) · The FASEB Journal · doi:10.1096/fj.11-194423 · Cited by 45
Brain endothelial LRP1 maintains blood–brain barrier integrity
Storck, S. E., Kurtyka, M., & Pietrzik, C. U. (2021) · Fluids and Barriers of the CNS · doi:10.1186/s12987-021-00260-5 · Cited by 48
Self-citationTargeting ApoE4/ApoE receptor LRP1 in Alzheimer's disease
Martiskainen, H., Haapasalo, A., Kurkinen, K. M. A., Pihlajamäki, J., Soininen, H. S., & Hiltunen, M. O. (2013) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2013.789862 · Cited by 49
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Self-citationData-driven modeling of Alzheimer Disease pathogenesis
Anastasio, T. J. (2011) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2011.08.038 · Cited by 44
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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