Induction of Neuronal Death by Microglial AGE-Albumin: Implications for Alzheimer’s Disease
Open accessAbstract
Advanced glycation end products (AGEs) have long been considered as potent molecules promoting neuronal cell death and contributing to neurodegenerative disorders such as Alzheimer's disease (AD). In this study, we demonstrate that AGE-albumin, the most abundant AGE product in human AD brains, is synthesized in activated microglial cells and secreted into the extracellular space. The rate of AGE-albumin synthesis in human microglial cells is markedly increased by amyloid-β exposure and oxidative stress. Exogenous AGE-albumin upregulates the receptor protein for AGE (RAGE) and augments calcium influx, leading to apoptosis of human primary neurons. In animal experiments, soluble RAGE (sRAGE), pyridoxamine or ALT-711 prevented Aβ-induced neuronal death in rat brains. Collectively, these results provide evidence for a new mechanism by which microglial cells promote death of neuronal cells through synthesis and secretion of AGE-albumin, thereby likely contributing to neurodegenerative diseases such as AD.
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Binding of the AGE-albumin adduct to RAGE provides a link to neuronal apoptosis by activating the proapoptotic JNK and Bax pathways.
“The binding of the AGE-albumin adduct to RAGE provides a link to neuronal apoptosis by activating the proapoptotic JNK and Bcl-2-associated X protein (Bax) pathways111.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [111]
The formation of the AGE-albumin adduct is intensified by elevated oxidative stress and Aβ aggregation.
“The formation of the AGE-albumin adduct is intensified by elevated oxidative stress and Aβ aggregation111.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [111]
Aβ is produced by the AGE-albumin-RAGE interaction, which in turn supports AGE-albumin adduct formation in a positive feed-forward cycle.
“Aβ is also produced by the AGE-albumin-RAGE interaction, which in turn supports AGE-albumin adduct formation in a positive feed-forward cycle.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [111]
The AGE-albumin adduct is one of the most abundant AGE-protein adducts in the brain, confirmed by mass spectral analysis, and causes RAGE overexpression in primary neurons in human AD brains.
“One of the most abundant AGE-protein adducts in the brain is the AGE-albumin adduct, which was confirmed by mass spectral analysis, and causes RAGE overexpression in primary neurons in human AD brains.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [111]
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- Authors
- Byun, K., Bayarsaikhan, E., Kim, D., Kim, C. Y., Mook-Jung, I., Paek, S. H., Kim, S. U., Yamamoto, T., Won, M.-H., Song, B.-J., Park, Y. M., & Lee, B.
- Affiliations
- Gachon University (KR)
- Seoul National University (KR)
- University of British Columbia (CA)
- Niigata University (JP)
- Kangwon National University (KR)
- National Institutes of Health (US)
- Korea Basic Science Institute (KR)
- Corresponding author
- Park, Young Mok
- ORCID
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2012-05-25
- Volume
- 7
- Issue
- 5
- Pages
- e37917
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3360664
- OpenAlex
- W1964539405
- Cited by
- 75
- References
- 32
- Citations by year
- 2025: 5 · 2024: 4 · 2023: 3 · 2022: 9 · 2021: 5 · 2019: 3 · 2018: 4 · 2017: 9 · 2016: 9 · 2015: 10 · 2014: 10 · 2013: 4
- FWCI
- 4.93
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- National Research Foundation
- Universiteit Maastricht
- Korea Basic Science Institute (G30124)
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Keywords
- advanced glycation end products, microglia, Alzheimer's disease, neuronal cell death, amyloid-beta, oxidative stress, receptor for advanced glycation end products, soluble RAGE, pyridoxamine, ALT-711, calcium influx, apoptosis, neuroinflammation
- MeSH terms
- Receptor for Advanced Glycation End Products, Albumins, Alzheimer Disease, Animals, Brain, Cell Line, Humans, Male, Neurons, Receptors, Immunologic, Amyloid beta-Peptides, Cell Death, Glycation End Products, Advanced, Rats, Sprague-Dawley, Apoptosis, Microglia, Oxidative Stress, Rats, Protein Multimerization
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