Human blood-brain barrier receptors for Alzheimer's amyloid-beta 1- 40. Asymmetrical binding, endocytosis, and transcytosis at the apical side of brain microvascular endothelial cell monolayer.
Open accessAbstract
A soluble monomeric form of Alzheimer's amyloid-beta (1-40) peptide (sAbeta1-40) is present in the circulation and could contribute to neurotoxicity if it crosses the brain capillary endothelium, which comprises the blood-brain barrier (BBB) in vivo. This study characterizes endothelial binding and transcytosis of a synthetic peptide homologous to human sAbeta1-40 using an in vitro model of human BBB. 125I-sAbeta1-40 binding to the brain microvascular endothelial cell monolayer was time dependent, polarized to the apical side, and saturable with high- and low-affinity dissociation constants of 7.8+/-1.2 and 52.8+/-6.2 nM, respectively. Binding of 125I-sAbeta1-40 was inhibited by anti-RAGE (receptor for advanced glycation end products) antibody (63%) and by acetylated low density lipoproteins (33%). Consistent with these data, transfected cultured cells overexpressing RAGE or macrophage scavenger receptor (SR), type A, displayed binding and internalization of 125I-sAbeta1-40. The internalized peptide remains intact > 94%. Transcytosis of 125I-sAbeta1-40 was time and temperature dependent, asymmetrical from the apical to basolateral side, saturable with a Michaelis constant of 45+/-9 nM, and partially sensitive to RAGE blockade (36%) but not to SR blockade. We conclude that RAGE and SR mediate binding of sAbeta1-40 at the apical side of human BBB, and that RAGE is also involved in sAbeta1-40 transcytosis.
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RAGE is not known to be related to oxytocin or oxytocin signalling.
“RAGE, a member of the immunoglobulin superfamily of pattern recognition receptors, is not known to be related to oxytocin or oxytocin signalling22–33.”
From Vascular RAGE transports oxytocin into the brain to elicit its maternal bonding behaviour in mice (2019) · cites this paper as [31]
The three RAGE forms bind various ligands with similar affinities, including AGEs and amyloid β peptide.
“The three RAGE forms bind various ligands with similar affinities, including multiple advanced glycation end-products (AGEs) and amyloid β peptide31–37.”
From Vascular RAGE transports oxytocin into the brain to elicit its maternal bonding behaviour in mice (2019) · cites this paper as [31]
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- Authors
- Mackic, J. B., Stins, M., McComb, J. G., Calero, M., Ghiso, J., Kim, K. S., Yan, S. D., Stern, D., Schmidt, A. M., Frangione, B., & Zlokovic, B. V.
- Affiliations
- University of Southern California (US)
- NYU Langone Health (US)
- Columbia University (US)
- Venue
- Journal of Clinical Investigation
- Published
- 1998-08-15
- Volume
- 102
- Issue
- 4
- Pages
- 734-743
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC508936
- OpenAlex
- W2150611166
- Cited by
- 242
- References
- 51
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 2 · 2023: 9 · 2022: 6 · 2021: 7 · 2020: 4 · 2019: 10 · 2018: 5 · 2017: 9 · 2016: 9 · 2015: 14 · 2014: 2 · 2013: 6 · 2012: 15
- FWCI
- 6.22
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- KU ScholarWorks (University of Kansas) (submittedVersion, other-oa)
- Funders
- American Heart Association
- National Institutes of Health (1r03ag014526-01)
- National Institute on Aging (AG-14526, AG05891)
- National Institute of Neurological Disorders and Stroke (NS34467)
- 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
- Aβ40, blood-brain barrier, RAGE, receptor for advanced glycation end products, transcytosis, endocytosis, brain microvascular endothelial cells, receptor binding, acetylated low density lipoprotein, Alzheimer's disease, peptide internalization
- MeSH terms
- Receptor for Advanced Glycation End Products, Alzheimer Disease, Amino Acid Sequence, Biological Transport, Blood-Brain Barrier, Endocytosis, Endothelium, Vascular, Humans, Membrane Proteins, Microcirculation, Molecular Sequence Data, Peptide Fragments, Receptors, Immunologic, Recombinant Proteins, Amyloid beta-Peptides, Cell Polarity, Receptors, Lipoprotein, Receptors, Scavenger, Scavenger Receptors, Class A, Scavenger Receptors, Class B
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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