Endothelial LRP1 transports amyloid-β1–42 across the blood-brain barrier
Open accessAbstract
According to the neurovascular hypothesis, impairment of low-density lipoprotein receptor-related protein-1 (LRP1) in brain capillaries of the blood-brain barrier (BBB) contributes to neurotoxic amyloid-β (Aβ) brain accumulation and drives Alzheimer's disease (AD) pathology. However, due to conflicting reports on the involvement of LRP1 in Aβ transport and the expression of LRP1 in brain endothelium, the role of LRP1 at the BBB is uncertain. As global Lrp1 deletion in mice is lethal, appropriate models to study the function of LRP1 are lacking. Moreover, the relevance of systemic Aβ clearance to AD pathology remains unclear, as no BBB-specific knockout models have been available. Here, we developed transgenic mouse strains that allow for tamoxifen-inducible deletion of Lrp1 specifically within brain endothelial cells (Slco1c1-CreER(T2) Lrp1(fl/fl) mice) and used these mice to accurately evaluate LRP1-mediated Aβ BBB clearance in vivo. Selective deletion of Lrp1 in the brain endothelium of C57BL/6 mice strongly reduced brain efflux of injected [125I] Aβ(1-42). Additionally, in the 5xFAD mouse model of AD, brain endothelial-specific Lrp1 deletion reduced plasma Aβ levels and elevated soluble brain Aβ, leading to aggravated spatial learning and memory deficits, thus emphasizing the importance of systemic Aβ elimination via the BBB. Together, our results suggest that receptor-mediated Aβ BBB clearance may be a potential target for treatment and prevention of Aβ brain accumulation in AD.
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Approximately 85% of Aβ is eliminated via blood-brain barrier-mediated efflux, primarily through LRP1.
“Approximately 85% of A β is eliminated via BBB-mediated efflux [ 16 ], primarily through low-density lipoprotein receptor-related protein 1 (LRP1), expressed on cerebrovascular endothelial cells [ 15-17 ].”
From Restores Aβ Clearance by Overcoming PCSK9–LRP1 Dysregulation and TRIB3‐Mediated Autophagy Blockade in Alzheimer's Disease (2026) · cites this paper as [17]
The Discussion reports that Aβ is cleared rapidly across the BBB and that brain endothelial LRP1 mediates approximately 48% of BBB transport. Neither the Discussion nor the clearance results give the claimed figure of approximately 85% of total Aβ elimination via BBB efflux; the results instead report that endothelial LRP1 accounts for approximately 27% of total Aβ1–42 clearance at the concentration studied. Page numbers are unavailable in our copy. (LLM, conf=0.87)
Experimental — accuracy not yet measuredEndothelial expression of LRP1 promotes the clearance of Aβ across the blood-brain barrier in vivo, a process directly modulated by PCSK9 inhibitor treatment.
“Thus, endothelial expression of LRP1 promotes the clearance of Aβ across the BBB in vivo, a process directly modulated by PCSK9 inhibitor treatment (93, 94), and the expression of CD36 parallels the ability of microglia to perform Aβ clearance (95).”
From PCSK9 and the nervous system: a no-brainer? (2023) · cites this paper as [93]
The Introduction and Discussion report that deleting Lrp1 specifically in brain endothelial cells reduced Aβ efflux across the blood-brain barrier in mice, supporting the in vivo clearance claim. Our copy does not report that PCSK9 inhibitor treatment directly modulates this process (searched: PCSK9 inhibitor treatment and proprotein convertase subtilisin/kexin 9). (LLM, conf=0.90)
Experimental — accuracy not yet measuredPCSK9 negatively regulates LDL receptor family members, including LRP1, a key mediator of blood-brain barrier Aβ efflux.
“Proprotein convertase subtilisin/kexin type 9 (PCSK9) negatively regulates low-density lipoprotein receptor family members, including low-density lipoprotein receptor -related protein 1 (LRP1), a key mediator of blood-brain barrier (BBB) Aβ efflux”
From Small-molecule PCSK9 inhibition enhances BBB amyloid-β clearance and suppresses microglial inflammation in Alzheimer’s disease models (2026) · cites this paper as [24]
The Discussion reports that brain endothelial LRP1 mediates approximately 48% of blood-brain barrier Aβ transport, supporting its description as a key mediator of Aβ efflux. Our copy does not establish that PCSK9 negatively regulates LDL receptor family members or LRP1; searches for PCSK9 and its full name found no passage addressing that part of the claim. (LLM, conf=0.88)
Experimental — accuracy not yet measuredLRP1 regulates Aβ efflux through the BBB, and its expression in the whole brain and brain capillaries appeared reduced with ageing and in AD, negatively impacting soluble Aβ clearance and leading to amyloid deposition.
“Concerning LRP1, it regulates Aβ efflux through the BBB and in addition its expression in the whole brain and brain capillaries appeared reduced with ageing and in AD, negatively impacting soluble Aβ clearance and leading to amyloid deposition [39,85,86,87].”
From The Emerging Role of PCSK9 in the Pathogenesis of Alzheimer’s Disease: A Possible Target for the Disease Treatment (2024) · cites this paper as [39]
The Introduction (page not provided) reports that LRP1 expression decreases in total brain and brain capillaries with age and is further reduced in AD. The Results and Discussion (pages not provided) support a role for endothelial LRP1 in Aβ efflux and soluble Aβ clearance. But the claim that this leads to amyloid deposition goes beyond the reported experiment: endothelial Lrp1 deletion increased soluble Aβ without a significant difference in plaque load. (LLM, conf=0.87)
Experimental — accuracy not yet measuredAβ peptides directly bind LRP1 for clearance.
“Aβ peptides have been reported to directly bind LRP1 for clearance37,38.”
From Brain-targeted drug delivery by manipulating protein corona functions (2019) · cites this paper as [38]
If LRP1 is downregulated in Parkinson's disease as in Alzheimer's disease, this could result in impaired alpha-synuclein blood-brain barrier clearance and accumulation of alpha-synuclein in brain.
“If LRP1is similarly downregulated in PD as in AD (137, 561), this could result in impaired 𝛂 -syn BBB clearance and accumulation of 𝛂 -syn in brain.”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [561]
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 [14]
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 [14]
LRP1 plays a dominant role in mediating blood-brain barrier Aβ efflux, and reduced LRP1 availability markedly compromises this process.
“Among clearance pathways, LRP1 plays a dominant role in mediating BBB Aβ efflux, and reduced LRP1 availability markedly compromises this process24.”
From Small-molecule PCSK9 inhibition enhances BBB amyloid-β clearance and suppresses microglial inflammation in Alzheimer’s disease models (2026) · cites this paper as [24]
Endothelial LRP1 is a major mediator of blood-brain barrier Aβ clearance.
“This effect is consistent with the established role of endothelial LRP1 as a major mediator of BBB Aβ clearance24”
From Small-molecule PCSK9 inhibition enhances BBB amyloid-β clearance and suppresses microglial inflammation in Alzheimer’s disease models (2026) · cites this paper as [24]
The lack of effect of SBC-115,076 on blood-to-brain-like transport is consistent with the established directionality of LRP1-mediated Aβ clearance.
“The lack of effect on blood-to-brain-like transport is consistent with the established directionality of LRP1-mediated Aβ clearance24.”
From Small-molecule PCSK9 inhibition enhances BBB amyloid-β clearance and suppresses microglial inflammation in Alzheimer’s disease models (2026) · cites this paper as [24]
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- Authors
- Storck, S. E., Meister, S., Nahrath, J., Meißner, J. N., Schubert, N., Di Spiezio, A., Baches, S., Vandenbroucke, R. E., Bouter, Y., Prikulis, I., Korth, C., Weggen, S., Heimann, A., Schwaninger, M., Bayer, T. A., & Pietrzik, C. U.
- Affiliations
- Johannes Gutenberg University Mainz (DE)
- Universitätsmedizin Göttingen (DE)
- Heinrich Heine University Düsseldorf (DE)
- Ghent University (BE)
- University of Lübeck (DE)
- Corresponding author
- Meister, Sabrina
- Nahrath, Julius
- Pietrzik, Claus U.
- ORCID
- Venue
- Journal of Clinical Investigation
- Published
- 2015-11-30
- Volume
- 126
- Issue
- 1
- Pages
- 123-136
- ISSN
- 0021-9738 (ISSN-L)
- 1558-8238
- PMC
- PMC4701557
- OpenAlex
- W2187829723
- Cited by
- 477
- References
- 66
- Citations by year
- 2026: 61 · 2025: 58 · 2024: 55 · 2023: 59 · 2022: 40 · 2021: 53 · 2020: 43 · 2019: 30 · 2018: 24 · 2017: 33 · 2016: 20
- FWCI
- 13.72
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Ghent University Academic Bibliography (Ghent University) (submittedVersion, other-oa)
- GoeScholar The Publication Server of the Georg-August-Universität Göttingen (Georg-August-Universität Göttingen) (submittedVersion, cc-by)
- GRO (submittedVersion, cc-by)
- Padua Research Archive (University of Padova) (submittedVersion, other-oa)
- Funders
- Deutsche Forschungsgemeinschaft (PI 379/8‐1)
- Topics
- Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Keywords
- LRP1, amyloid-beta 42, blood-brain barrier, brain endothelium, Alzheimer's disease, amyloid-beta clearance, 5xFAD mice, spatial learning and memory deficits
- MeSH terms
- Animals, Blood-Brain Barrier, Brain, Cognition Disorders, Mice, Inbred C57BL, Peptide Fragments, Receptors, LDL, Amyloid beta-Peptides, Protein Transport, Tumor Suppressor Proteins, Low Density Lipoprotein Receptor-Related Protein-1, Endothelial Cells, Mice, Transcytosis
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