Blood–brain barrier P-glycoprotein function in Alzheimer's disease
Abstract
A major pathological hallmark of Alzheimer's disease is accumulation of amyloid-β in senile plaques in the brain. Evidence is accumulating that decreased clearance of amyloid-β from the brain may lead to these elevated amyloid-β levels. One of the clearance pathways of amyloid-β is transport across the blood-brain barrier via efflux transporters. P-glycoprotein, an efflux pump highly expressed at the endothelial cells of the blood-brain barrier, has been shown to transport amyloid-β. P-glycoprotein function can be assessed in vivo using (R)-[(11)C]verapamil and positron emission tomography. The aim of this study was to assess blood-brain barrier P-glycoprotein function in patients with Alzheimer's disease compared with age-matched healthy controls using (R)-[(11)C]verapamil and positron emission tomography. In 13 patients with Alzheimer's disease (age 65 ± 7 years, Mini-Mental State Examination 23 ± 3), global (R)-[(11)C]verapamil binding potential values were increased significantly (P = 0.001) compared with 14 healthy controls (aged 62 ± 4 years, Mini-Mental State Examination 30 ± 1). Global (R)-[(11)C]verapamil binding potential values were 2.18 ± 0.25 for patients with Alzheimer's disease and 1.77 ± 0.41 for healthy controls. In patients with Alzheimer's disease, higher (R)-[(11)C]verapamil binding potential values were found for frontal, parietal, temporal and occipital cortices, and posterior and anterior cingulate. No significant differences between groups were found f…
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Studies using [11C]verapamil, an ABCB1 (P-gp) ligand and PET, have shown increased uptake of verapamil in certain brain regions in individuals with early AD.
“Studies using [ 11 C]verapamil, an ABCB1 (P-gp) ligand and PET, have shown increased uptake of verapamil in certain brain regions in individuals with early AD, suggesting diminished ABCB1-mediated active efflux of xenobiotics and drugs at the BBB (33, 142), and possibly faulty A 𝛃 BBB clearance based on experimental studies (115, 400, 632).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [33]
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- Authors
- van Assema, D. M. E., Lubberink, M., Bauer, M., van der Flier, W. M., Schuit, R. C., Windhorst, A. D., Comans, E. F. I., Hoetjes, N. J., Tolboom, N., Langer, O., Müller, M., Scheltens, P., Lammertsma, A. A., & van Berckel, B. N. M.
- Affiliations
- Uppsala University Hospital (SE)
- Medical University of Vienna (AT)
- Amsterdam UMC Location Vrije Universiteit Amsterdam (NL)
- ORCID
- Venue
- Brain
- Publisher
- Oxford University Press (OUP)
- Published
- 2011-11-25
- Volume
- 135
- Issue
- 1
- Pages
- 181-189
- ISSN
- 0006-8950 (ISSN-L)
- 1460-2156
- OpenAlex
- W2059631065
- Cited by
- 318
- References
- 71
- Citations by year
- 2026: 12 · 2025: 19 · 2024: 15 · 2023: 29 · 2022: 28 · 2021: 28 · 2020: 30 · 2019: 15 · 2018: 26 · 2017: 14 · 2016: 17 · 2015: 18 · 2014: 25 · 2013: 23 · 2012: 18
- FWCI
- 10.38
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Brain (publishedVersion)
- PubMed (publishedVersion)
- Pure Amsterdam UMC (publishedVersion)
- Amsterdam UMC (VU Amsterdam) - Institutional Repository (publishedVersion)
- Digital Academic REpository of VU University Amsterdam (Vrije Universiteit Amsterdam) (submittedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Topics
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
- Keywords
- Alzheimer's disease, P-glycoprotein, blood-brain barrier, amyloid-beta clearance, efflux pumps, binding potential, positron emission tomography, sporadic Alzheimer's disease, amyloid-beta deposition
- MeSH terms
- Aged, Alzheimer Disease, Blood-Brain Barrier, Brain, Female, Humans, Male, Middle Aged, Neuropsychological Tests, Radionuclide Imaging, Verapamil, ATP Binding Cassette Transporter, Subfamily B, Member 1
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