Cited by 262Alzheimer's disease research and treatmentsBarrier Structure and Function StudiesDrug Transport and Resistance Mechanisms

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Low‐density lipoprotein receptor‐related protein‐1: a serial clearance homeostatic mechanism controlling Alzheimer’s amyloid β‐peptide elimination from the brain

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Zlokovic, Berislav V., Deane, Rashid, Sagare, Abhay P., Bell, Robert D., Winkler, Ethan A.·2010·Journal of Neurochemistry

DOI 10.1111/j.1471-4159.2010.07002.xPMC PMC2972355

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Abstract

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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Authors: Zlokovic, B. V., Deane, R., Sagare, A. P., Bell, R. D., & Winkler, E. A.
Affiliations: University of Rochester Medicine (US)
ORCID: Deane, Rashid
Sagare, Abhay P.
Bell, Robert D.
Winkler, Ethan A.
Venue: Journal of Neurochemistry
Publisher: Wiley
Published: 2010-10-05
Volume: 115
Issue: 5
Pages: 1077-1089
ISSN: 0022-3042 (ISSN-L)
1471-4159
DOI: 10.1111/j.1471-4159.2010.07002.x
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
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
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: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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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Low‐density lipoprotein receptor‐related protein‐1: a serial clearance homeostatic mechanism controlling Alzheimer’s amyloid β‐peptide elimination from the brain

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