Monitoring phagocytic uptake of amyloid β into glial cell lysosomes in real time
Open accessPublished version of a preprint
Abstract
Glial cell phagocytosis of pH-dependent amyloid-β, Aβ pH , in live and fixed cultures, brain tissue sections, retina, cortex and in live animals useful for studying function in health and disease.
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The aggregated states of the Aβ1-42 peptides have been thoroughly characterized using atomic force microscopy and western blotting in previous papers.
“The aggregated states of the Aβ1–42 peptides have been thoroughly characterized using atomic force microscopy and western blotting in our previous papers.100,47”
From Amyloid-β induces lipid droplet-mediated microglial dysfunction via the enzyme DGAT2 in Alzheimer’s disease (2025) · cites this paper as [47]
The Results section (page unavailable) reports AFM characterization of Aβ1–42 oligomers, and the Methods section says the AFM analysis followed previously published protocols. The passages do not establish that previous papers thoroughly characterized the peptides’ aggregated states using both AFM and western blotting; western blotting is not documented in the retrieved passages. (LLM, conf=0.85)
Experimental — accuracy not yet measuredAβpH has been thoroughly characterized in vitro in primary cell culture and in vivo in a previous study.
“AβpH is a pH-sensitive fluorophore conjugate of Aβ1–42 peptide that is generated within our laboratory and has been thoroughly characterized in vitro in primary cell culture as well as in vivo experiments in our previous study.47”
From Amyloid-β induces lipid droplet-mediated microglial dysfunction via the enzyme DGAT2 in Alzheimer’s disease (2025) · cites this paper as [47]
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References 62 · Cited by 45
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- Authors
- Prakash, P., Jethava, K. P., Korte, N., Izquierdo, P., Favuzzi, E., Rose, I. V. L., Guttenplan, K. A., Manchanda, P., Dutta, S., Rochet, J.-C., Fishell, G., Liddelow, S. A., Attwell, D., & Chopra, G.
- Affiliations
- Purdue University West Lafayette (US)
- University College London (GB)
- Harvard University (US)
- New York University (US)
- Stanford Medicine (US)
- Corresponding author
- Chopra, Gaurav
- ORCID
- Venue
- Chemical Science
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2021
- Volume
- 12
- Issue
- 32
- Pages
- 10901-10918
- ISSN
- 2041-6520 (ISSN-L)
- 2041-6539
- PMC
- PMC8372545
- OpenAlex
- W3184506354
- Cited by
- 45
- References
- 62
- Citations by year
- 2026: 5 · 2025: 13 · 2024: 5 · 2023: 14 · 2022: 5 · 2021: 3
- FWCI
- 4.24
- Type
- journal article
- Language
- en
- Open access
- diamond
- doi.org
- Locations
- Chemical Science (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Minerva Access (University of Melbourne) (submittedVersion, cc-by)
- Funders
- Purdue University
- Purdue Research Foundation
- Ralph W. and Grace M. Showalter Research Trust Fund
- National Institutes of Health (P30 CA023168, R03NS108229)
- National Center for Advancing Translational Sciences
- U.S. Department of Defense (W81XWH2010665)
- Indiana Alzheimer Disease Center, School of Medicine, Indiana University
- Eli Lilly and Company
- Indiana Clinical and Translational Sciences Institute (UL1TR002529)
- Wellcome Trust (099222, 219366)
- Biotechnology and Biological Sciences Research Council
- European Molecular Biology Organization (ALTF 444-2018)
- Stanford University
- School of Medicine, New York University
- Blas Frangione Foundation
- Cure Alzheimer's Fund
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- amyloid-beta, phagocytosis, glial cells, lysosomes, real-time imaging, Alzheimer's disease, amyloid-beta clearance
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