Glycated tau protein in Alzheimer disease: a mechanism for induction of oxidant stress.
Open accessAbstract
The stability of proteins that constitute the neurofibrillary tangles and senile plaques of Alzheimer disease suggests that they would be ideal substrates for nonenzymatic glycation, a process that occurs over long times, even at normal levels of glucose, ultimately resulting in the formation of advanced glycation end products (AGEs). AGE-modified proteins aggregate, and they generate reactive oxygen intermediates. Using monospecific antibody to AGEs, we have colocalized these AGEs with paired helical filament tau in neurofibrillary tangles in sporadic Alzheimer disease. Such neurons also exhibited evidence of oxidant stress: induction of malondialdehyde epitopes and heme oxygenase 1 antigen. AGE-recombinant tau generated reactive oxygen intermediates and, when introduced into the cytoplasm of SH-SY5Y neuroblastoma cells, induced oxidant stress. We propose that in Alzheimer disease, AGEs in paired helical filament tau can induce oxidant stress, thereby promoting neuronal dysfunction.
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- Authors
- Yan, S. D., Chen, X., Schmidt, A. M., Brett, J., Godman, G., Zou, Y. S., Scott, C. W., Caputo, C., Frappier, T., & Smith, M. A.
- Affiliations
- Columbia University (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1994-08-02
- Volume
- 91
- Issue
- 16
- Pages
- 7787-7791
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC44487
- OpenAlex
- W2168994316
- Cited by
- 565
- References
- 45
- Citations by year
- 2026: 4 · 2025: 3 · 2024: 4 · 2023: 9 · 2022: 8 · 2021: 13 · 2020: 7 · 2019: 14 · 2018: 7 · 2017: 8 · 2016: 9 · 2015: 13 · 2014: 18 · 2013: 12 · 2012: 20
- FWCI
- 22.86
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01hl042833-10, 5p50hl021006-17, 5r01hl042507-09)
- National Heart, Lung, and Blood Institute (HL-42833, HL 42507, HL 21006)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, tau protein, advanced glycation end products, glycation, oxidative stress, neurofibrillary tangles, paired helical filaments, reactive oxygen species, malondialdehyde, heme oxygenase-1, amyloid plaques, neuronal dysfunction
- MeSH terms
- Alzheimer Disease, Brain, Humans, Immunohistochemistry, Neuroblastoma, Recombinant Proteins, Tumor Cells, Cultured, Neurofibrillary Tangles, tau Proteins, Glycation End Products, Advanced, Reactive Oxygen Species
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