Low‐density lipoprotein receptor‐related protein‐1: a serial clearance homeostatic mechanism controlling Alzheimer’s amyloid β‐peptide elimination from the brain
Open accessAbstract
J. Neurochem. (2010) 115 , 1077–1089. Low‐density lipoprotein receptor‐related protein‐1 (LRP1), a member of the low‐density lipoprotein receptor family, has major roles in the cellular transport of cholesterol, endocytosis of 40 structurally diverse ligands, transcytosis of ligands across the blood–brain barrier, and transmembrane and nuclear signaling. Recent evidence indicates that LRP1 regulates brain and systemic clearance of Alzheimer’s disease (AD) amyloid β‐peptide (Aβ). According to the two‐hit vascular hypothesis for AD, vascular damage precedes cerebrovascular and brain Aβ accumulation ( hit 1 ) which then further amplifies neurovascular dysfunction ( hit 2 ) preceding neurodegeneration. In this study, we discuss the roles of LRP1 during the hit 1 and hit 2 stage of AD pathogenesis and describe a three‐level serial LRP1‐dependent homeostatic control of Aβ clearance including (i) cell‐surface LRP1 at the blood–brain barrier and cerebrovascular cells mediating brain‐to‐blood Aβ clearance (ii) circulating LRP1 providing a key endogenous peripheral ‘sink’ activity for plasma Aβ which prevents free Aβ access to the brain, and (iii) LRP1 in the liver mediating systemic Aβ clearance. Pitfalls in experimental Aβ brain clearance measurements with the concurrent use of peptides/proteins such as receptor‐associated protein and aprotinin are also discussed. We suggest that LRP1 has a critical role in AD pathogenesis and is an important therapeutic target in AD.
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Brain-to-blood transfer of monomeric Aβ is highly dependent on LRP1.
“The brain-to-blood transfer of monomeric Aβ is highly dependent on low-density lipoprotein receptor-related protein 1 (LRP1) [13, 14], which in brain endothelium is primarily located at the abluminal side [13, 15].”
From PCSK9 acts as a key regulator of Aβ clearance across the blood–brain barrier (2022) · cites this paper as [13]
In “Level 1 – LRP1 at the blood-brain barrier and in brain vascular cells” (page unavailable), the paper calls LRP1 the main receptor for Aβ clearance across the BBB into blood and reports that blocking LRP1 substantially inhibits clearance. It does not specify that this finding concerns monomeric Aβ, so the monomer-specific part of the claim is not established by our copy. (LLM, conf=0.83)
Experimental — accuracy not yet measuredAβ40 and Aβ42 peptides are cleared from brain-to-blood by LRP1-mediated transvascular clearance.
“a key mechanism by which A 𝛃 40 and 42 peptides are cleared from brain-toblood (696).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [696]
LRP1 in brain endothelium is primarily located at the abluminal side.
“The brain-to-blood transfer of monomeric Aβ is highly dependent on low-density lipoprotein receptor-related protein 1 (LRP1) [13, 14], which in brain endothelium is primarily located at the abluminal side [13, 15].”
From PCSK9 acts as a key regulator of Aβ clearance across the blood–brain barrier (2022) · cites this paper as [13]
LRP1 is a key mediator of cerebral Aβ clearance by rapid Aβ transport across the BBB into the periphery.
“LRP1 is a key mediator of cerebral Aβ clearance by its rapid Aβ transport across the BBB into the periphery [13, 14].”
From PCSK9 acts as a key regulator of Aβ clearance across the blood–brain barrier (2022) · cites this paper as [13]
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- Authors
- Zlokovic, B. V., Deane, R., Sagare, A. P., Bell, R. D., & Winkler, E. A.
- Affiliations
- University of Rochester Medicine (US)
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2010-10-05
- Volume
- 115
- Issue
- 5
- Pages
- 1077-1089
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- PMC
- PMC2972355
- OpenAlex
- W1957213374
- Cited by
- 261
- References
- 125
- Citations by year
- 2026: 8 · 2025: 17 · 2024: 19 · 2023: 18 · 2022: 18 · 2021: 11 · 2020: 15 · 2019: 16 · 2018: 7 · 2017: 24 · 2016: 27 · 2015: 17 · 2014: 13 · 2013: 8 · 2012: 25
- FWCI
- 1.66
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (R37AG023084)
- National Institute of Neurological Disorders and Stroke (R37NS034467, R01NS034467, R37NS34467)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Keywords
- LRP1, Alzheimer's disease, blood-brain barrier, hepatic clearance, neurovascular dysfunction, receptor-associated protein, aprotinin, therapeutic target
- MeSH terms
- Alzheimer Disease, Animals, Brain, Homeostasis, Humans, Amyloid beta-Peptides, LDL-Receptor Related Protein-Associated Protein
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