The Ratio of Monomeric to Aggregated Forms of Aβ40 and Aβ42 Is an Important Determinant of Amyloid-β Aggregation, Fibrillogenesis, and Toxicity
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Aggregation and fibril formation of amyloid-beta (Abeta) peptides Abeta40 and Abeta42 are central events in the pathogenesis of Alzheimer disease. Previous studies have established the ratio of Abeta40 to Abeta42 as an important factor in determining the fibrillogenesis, toxicity, and pathological distribution of Abeta. To better understand the molecular basis underlying the pathologic consequences associated with alterations in the ratio of Abeta40 to Abeta42, we probed the concentration- and ratio-dependent interactions between well defined states of the two peptides at different stages of aggregation along the amyloid formation pathway. We report that monomeric Abeta40 alters the kinetic stability, solubility, and morphological properties of Abeta42 aggregates and prevents their conversion into mature fibrils. Abeta40, at approximately equimolar ratios (Abeta40/Abeta42 approximately 0.5-1), inhibits (> 50%) fibril formation by monomeric Abeta42, whereas inhibition of protofibrillar Abeta42 fibrillogenesis is achieved at lower, substoichiometric ratios (Abeta40/Abeta42 approximately 0.1). The inhibitory effect of Abeta40 on Abeta42 fibrillogenesis is reversed by the introduction of excess Abeta42 monomer. Additionally, monomeric Abeta42 and Abeta40 are constantly recycled and compete for binding to the ends of protofibrillar and fibrillar Abeta aggregates. Whereas the fibrillogenesis of both monomeric species can be seeded by fibrils composed of either peptide, Abeta42 protofibrils selectively seed the fibrillogenesis of monomeric Abeta42 but not monomeric Abeta40. Finally, we also show that the amyloidogenic propensities of different individual and mixed Abeta species correlates with their relative neuronal toxicities. These findings, which highlight specific points in the amyloid peptide equilibrium that are highly sensitive to the ratio of Abeta40 to Abeta42, carry important implications for the pathogenesis and current therapeutic strategies of Alzheimer disease.
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Aquaporin-4 localizes at perivascular astrocytic end feet ensheathing the cerebral vasculature and mediates brain waste clearance through the lymphatic pathway.
“Astroglial water channel aquaporin‐4 (AQP4), which localizes at the perivascular astrocytic end feet ensheathing the cerebral vasculature, mediates brain waste clearance through the lymphatic pathway.[ 34 ]”
From Multifunctional Nanostructure RAP‐RL Rescues Alzheimer's Cognitive Deficits through Remodeling the Neurovascular Unit (2021) · cites this paper as [34]
The paper’s discussion of amyloid-β aggregation and vascular pathology does not address AQP4 localization or lymphatic waste clearance. Searches for aquaporin-4, perivascular astrocytic end feet, and the lymphatic pathway found no passage supporting the claim; page numbers were unavailable in our copy. (LLM, conf=0.75)
Experimental — accuracy not yet measuredThe lymphatic system is impaired in Alzheimer's disease with reduction of AQP4 on astrocytic end feet.
“Third, the lymphatic system, which is impaired in AD with the reduction of AQP4 on astrocytic end feet,[ 34 ]”
From Multifunctional Nanostructure RAP‐RL Rescues Alzheimer's Cognitive Deficits through Remodeling the Neurovascular Unit (2021) · cites this paper as [34]
The supplied passages and the paper’s discussion of amyloid-β aggregation address Alzheimer’s disease but not lymphatic impairment or AQP4 on astrocytic end feet. Searches for AQP4, astrocytic end feet, lymphatic impairment, and glymphatic dysfunction found no passage addressing the attributed claim. (LLM, conf=0.75)
Experimental — accuracy not yet measuredAβ42 is a key player in initiating plaque formation and AD pathogenesis.
“Therefore, Aβ42 is thought to be a key player in initiating plaque formation and AD pathogenesis [31].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [31]
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- Authors
- Jan, A., Gokce, O., Luthi-Carter, R., & Lashuel, H. A.
- Affiliations
- École Polytechnique Fédérale de Lausanne (CH)
- Corresponding author
- Lashuel, Hilal A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2008-10
- Volume
- 283
- Issue
- 42
- Pages
- 28176-28189
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2661389
- OpenAlex
- W2130111915
- Cited by
- 291
- References
- 75
- Citations by year
- 2026: 5 · 2025: 13 · 2024: 25 · 2023: 11 · 2022: 18 · 2021: 12 · 2020: 16 · 2019: 9 · 2018: 15 · 2017: 15 · 2016: 16 · 2015: 20 · 2014: 13 · 2013: 26 · 2012: 28
- FWCI
- 11.29
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Leicester Research Archive (University of Leicester) (submittedVersion)
- Funders
- National Science Foundation
- École Polytechnique Fédérale de Lausanne
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (110027, 310000)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- amyloid-beta, Aβ40, amyloid-beta 42, amyloid-beta aggregation, fibril formation, protofibrils, fibril seeding, amyloid-beta toxicity, Alzheimer disease pathogenesis, peptide solubility
- MeSH terms
- Alzheimer Disease, Animals, Cell Line, Humans, Models, Biological, Neurons, Peptide Fragments, Peptides, Polymers, Protein Binding, Thiazoles, Time Factors, Amyloid beta-Peptides, Microscopy, Electron, Transmission, Rats, Benzothiazoles
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