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Green tea epigallocatechin-3-gallate (EGCG) reduces β-amyloid mediated cognitive impairment and modulates tau pathology in Alzheimer transgenic mice
Abstract
We previously reported that intraperitoneal (i.p.) injection (20 mg/kg) of (-)-epigallocatechin-3-gallate (EGCG), the main polyphenolic constituent of green tea, decreased beta-amyloid (Abeta) levels and plaques via promotion of the non-amyloidogenic alpha-secretase proteolytic pathway in "Swedish" mutant amyloid precursor protein overexpressing (APPsw, Tg) mice. Here, we find that EGCG administered orally in drinking water (50 mg/kg) similarly reduces Abeta deposition in these mice. Following a six month treatment of an 8 month old cohort, immunohistochemical analysis of coronal sections reveals that plaque burdens were reduced in the cingulate cortex, hippocampus, and entorhinal cortex by 54%, 43%, and 51%, respectively. Congo red plaque burdens were decreased in the cingulate cortex, hippocampus, and entorhinal cortex by 53%, 53%, and 58%, respectively as well. ELISA of brain homogenates of the treatment Tg mice revealed consistent reductions in both Abeta1-40 and 1-42 soluble and insoluble forms. In the present study we also investigated the effect EGCG administration had on tau pathology and cognition in Tg mice. Both i.p. and orally-treated Tg animals were found to have modulated tau profiles, with markedly suppressed sarkosyl-soluble phosphorylated tau isoforms. Radial arm water maze (RAWM) testing for working memory indicated that EGCG provided cognitive benefit to Tg mice with both i.p. and oral administration, although i.p.-treated animals showed a more pronounced benefit because of the greater impairment of their Tg controls at the time of testing. Taken together, these data further the notion of EGCG dietary supplementation as a potentially safe and effective prophylaxis for Alzheimer's disease.
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“This protein known as the BACE performs proteolysis by generating a soluble fragment in the extracellular space known as “soluble APPβ” and an additional fragment bound to the plasma membrane, CTFβ peptide that undergoes proteolysis yet again by γ-secretase to generate toxic neuropeptides Aβ with 40–43 amino acids, finally causing the amyloid plaques characteristic of AD [165,166,167].”
From Multi-Target Mechanisms of Phytochemicals in Alzheimer’s Disease: Effects on Oxidative Stress, Neuroinflammation and Protein Aggregation (2022) · cites this paper as [166]
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Metadata
- Authors
- Rezai-Zadeh, K., Arendash, G. W., Hou, H., Fernandez, F., Jensen, M., Runfeldt, M., Shytle, R. D., & Tan, J.
- Affiliations
- University of South Florida (US)
- USF Health Byrd Alzheimer's Institute (US)
- Corresponding author
- Tan, Jun
- Venue
- Brain Research
- Publisher
- Elsevier BV
- Published
- 2008-06
- Volume
- 1214
- Pages
- 177-187
- ISSN
- 0006-8993 (ISSN-L)
- OpenAlex
- W2052380265
- Cited by
- 459
- References
- 50
- Citations by year
- 2026: 14 · 2025: 28 · 2024: 17 · 2023: 26 · 2022: 27 · 2021: 30 · 2020: 37 · 2019: 20 · 2018: 28 · 2017: 31 · 2016: 20 · 2015: 27 · 2014: 27 · 2013: 33 · 2012: 32
- FWCI
- 13.81
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Brain Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (AG04418, P01AG004418, R21AG031037, P50AG025711, AG025711, AG031037)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Agricultural and Biological Sciences › Food Science › Tea Polyphenols and Effects
- Health Sciences › Medicine › Complementary and alternative medicine › Medicinal Plants and Neuroprotection
- Keywords
- epigallocatechin gallate, green tea polyphenols, Alzheimer's disease, amyloid plaques, tau phosphorylation, oral administration, working memory, cognitive impairment, dietary supplementation, neuroprotection
- MeSH terms
- Alzheimer Disease, Analysis of Variance, Animals, Catechin, Cognition Disorders, Disease Models, Animal, Enzyme-Linked Immunosorbent Assay, Mice, Transgenic, Mutation, Phosphorylation, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, tau Proteins, Neuroprotective Agents, Maze Learning, Mice
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