Green tea Epigallocatechin-3-Gallate (EGCG) Modulates Amyloid Precursor Protein Cleavage and Reduces Cerebral Amyloidosis in Alzheimer Transgenic Mice
Open accessAbstract
Alzheimer's disease (AD) is a progressive neurodegenerative disorder pathologically characterized by deposition of beta-amyloid (Abeta) peptides as senile plaques in the brain. Recent studies suggest that green tea flavonoids may be used for the prevention and treatment of a variety of neurodegenerative diseases. Here, we report that (-)-epigallocatechin-3-gallate (EGCG), the main polyphenolic constituent of green tea, reduces Abeta generation in both murine neuron-like cells (N2a) transfected with the human "Swedish" mutant amyloid precursor protein (APP) and in primary neurons derived from Swedish mutant APP-overexpressing mice (Tg APPsw line 2576). In concert with these observations, we find that EGCG markedly promotes cleavage of the alpha-C-terminal fragment of APP and elevates the N-terminal APP cleavage product, soluble APP-alpha. These cleavage events are associated with elevated alpha-secretase activity and enhanced hydrolysis of tumor necrosis factor alpha-converting enzyme, a primary candidate alpha-secretase. As a validation of these findings in vivo, we treated Tg APPsw transgenic mice overproducing Abeta with EGCG and found decreased Abeta levels and plaques associated with promotion of the nonamyloidogenic alpha-secretase proteolytic pathway. These data raise the possibility that EGCG dietary supplementation may provide effective prophylaxis for AD.
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EGCG increases α-cleavage of APP.
“experimental studies have provided evidence that EGCG increases the α-cleavage of APP (Rezai-Zadeh et al., 2005; Ettcheto et al., 2020)”
From Exploring the Therapeutic Potential of Phytochemicals in Alzheimer’s Disease: Focus on Polyphenols and Monoterpenes (2022) · cites this paper as Rezai-Zadeh et al., 2005
In transgenic APPSWE Tg2576 mice, intraperitoneal EGCG for 2 months significantly reduces Aβ levels.
“In transgenic APPSWE Tg2576 mice, the intraperitoneal treatment with EGCG for 2 months is associated to a significant reduction of the Aβ levels”
From Exploring the Therapeutic Potential of Phytochemicals in Alzheimer’s Disease: Focus on Polyphenols and Monoterpenes (2022) · cites this paper as Rezai-Zadeh et al., 2005
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Cites
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864 · see citing works
Self-citationAmyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works
Self-citationCorrelative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210 · see citing works
Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
De Strooper, B., Saftig, P., Craessaerts, K., Vanderstichele, H., Guhde, G., Annaert, W., Von Figura, K., & Van Leuven, F. (1998) · Nature · doi:10.1038/34910 · Cited by 1,818 · see citing works
Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity
Yan, R., Bienkowski, M. J., Shuck, M. E., Miao, H., Tory, M. C., Pauley, A. M., Brashler, J. R., Stratman, N. C., Mathews, W. R., Buhl, A. E., et al. (1999) · Nature · doi:10.1038/990107 · Cited by 1,438 · see citing works
Chow, H.-H. S., Cai, Y., Hakim, I. A., Crowell, J. A., Shahi, F., Brooks, C. A., Dorr, R. T., Hara, Y., & Alberts, D. S. (2003) · PubMed · Cited by 699 · see citing works
Johnson‐Wood, K., Lee, M., Motter, R. N., Hu, K., Gordon, G., Barbour, R., Khan, K., Gordon, M. N., Tan, H. T., Games, D., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.4.1550 · Cited by 634 · see citing works
ADAMs family members as amyloid precursor protein α‐secretases
Allinson, T. M. J., Parkin, E. T., Turner, A. J., & Hooper, N. M. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10737 · Cited by 441 · see citing works
Cellular mechanisms of β-amyloid production and secretion
Sinha, S., & Lieberburg, I. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11049 · Cited by 438 · see citing works
Levites, Y., Amit, T., Youdim, M. B. H., & Mandel, S. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202832200 · Cited by 417 · see citing works
Mandel, S. A., Weinreb, O., Amit, T., & Youdim, M. B. H. (2004) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02291.x · Cited by 379 · see citing works
Levites, Y., Amit, T., Mandel, S. A., & Youdim, M. B. H. (2003) · The FASEB Journal · doi:10.1096/fj.02-0881fje · Cited by 372 · see citing works
Aktaş, O., Prozorovski, T., Тихоновна, С. А., Savaskan, N. E., Lauster, R., Kloetzel, P., Infante‐Duarte, C., Brocke, S., & Zipp, F. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.9.5794 · Cited by 316 · see citing works
Steiner, H., Duff, K., Capell, A., Romig, H., Grim, M. G., Lincoln, S., Hardy, J., Yu, X., Picciano, M., Fechteler, K., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.40.28669 · Cited by 303 · see citing works
Self-citationGolde, T. E., Eckman, C. B., & Younkin, S. G. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00043-0 · Cited by 300 · see citing works
A Single Ascending Dose Study of Epigallocatechin Gallate in Healthy Volunteers
Ullmann, U., Haller, J., Decourt, J., Girault, N., Girault, J., Richard-Caudron, A., Pineau, B., & Weber, P. (2003) · Journal of International Medical Research · doi:10.1177/147323000303100205 · Cited by 299 · see citing works
Ahmed, S., Rahman, A., Hasnain, A.-U., Lalonde, M. S., Goldberg, V. M., & Haqqi, T. M. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01004-3 · Cited by 287 · see citing works
Tea and Cancer Prevention: Studies in Animals and Humans
Chung, F., SCHWARTZ, J. L., Herzog, C. R., & Yang, Y. (2003) · Journal of Nutrition · doi:10.1093/jn/133.10.3268s · Cited by 275 · see citing works
Chyu, K., Babbidge, S. M., Zhao, X., Dandillaya, R., Rietveld, A. G., Yano, J., Dimayuga, P. C., Cercek, B., & Shah, P. K. (2004) · Circulation · doi:10.1161/01.cir.0000128034.70732.c2 · Cited by 223 · see citing works
Role of CD40 ligand in amyloidosis in transgenic Alzheimer's mice
Tan, J., Town, T., Crawford, F., Mori, T., DelleDonne, A., Crescentini, R., Obregon, D., Flavell, R. A., & Mullan, M. J. (2002) · Nature Neuroscience · doi:10.1038/nn968 · Cited by 217 · see citing works
Self-citationLi, R., Huang, Y., Du, F., & Le, W. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20315 · Cited by 205 · see citing works
Moyers, S. B., & Kumar, N. B. (2004) · Nutrition Reviews · doi:10.1111/j.1753-4887.2004.tb00041.x · Cited by 193 · see citing works
Advances in the Cellular and Molecular Biology of the Beta-Amyloid Protein in Alzheimer 's Disease
Sambamurti, K., Greig, N. H., & Lahiri, D. K. (2002) · NeuroMolecular Medicine · doi:10.1385/nmm:1:1:1 · Cited by 184 · see citing works
Green tea catechins as a BACE1 (β-Secretase) inhibitor
Jeon, S.-Y., Bae, K., Seong, Y.-H., & Song, K. (2003) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2003.09.018 · Cited by 168 · see citing works
Slack, B. E., Leona, K., & Seah, C. C. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3570787 · Cited by 159 · see citing works
Funamoto, S., Morishima‐Kawashima, M., Tanimura, Y., Hirotani, N., Saido, T. C., & Ihara, Y. (2004) · Biochemistry · doi:10.1021/bi049399k · Cited by 131 · see citing works
Cancer chemoprevention by tea polyphenols.
Lin, J., & Liang, Y. (2000) · PubMed · Cited by 130 · see citing works
The Search for α-Secretase and its Potential as a Therapeutic Approach to Alzheimer's Disease
Hooper, N. M., & Turner, A. J. (2002) · Current Medicinal Chemistry · doi:10.2174/0929867023370121 · Cited by 127 · see citing works
Han, M. (2003) · Experimental & Molecular Medicine · doi:10.1038/emm.2003.19 · Cited by 120 · see citing works
Endocannabinoids accumulate in spinal cord of SOD1G93A transgenic mice
Witting, A., Weydt, P., Hong, S. Y., Kliot, M., Möller, T., & Stella, N. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02544.x · Cited by 112 · see citing works
Skovronsky, D., Fath, S., Lee, V. M.-Y., & Milla, M. E. (2001) · Journal of Neurobiology · doi:10.1002/neu.1064 · Cited by 80 · see citing works
Mechanisms of cancer prevention by tea polyphenols based on inhibition of TNF‐α expression
Suganuma, M., Sueoka, E., Sueoka, N., Okabe, S., & Fujiki, H. (2000) · BioFactors · doi:10.1002/biof.5520130112 · Cited by 71 · see citing works
Regulation of the amyloid precursor protein ectodomain shedding by the 5‐HT4 receptor and Epac
Robert, S. J., Maillet, M., Morel, É., Launay, J., Fischmeister, R., Mercken, L., & Lezoualc’h, F. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.01.010 · Cited by 53 · see citing works
Closing in on the Amyloid Cascade
Doms, R. W., & Huse, J. T. (2000) · Molecular Neurobiology · doi:10.1385/mn:22:1-3:081 · Cited by 49 · see citing works
Intracerebroventricular passive immunization with anti‐Aβ antibody in Tg2576
Chauhan, N. B., & Siegel, G. J. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10721 · Cited by 45 · see citing works
Gandhi, S., Refolo, L. M., & Sambamurti, K. (2004) · Journal of Molecular Neuroscience · doi:10.1385/jmn:24:1:137 · Cited by 42 · see citing works
Roßner, S., Beck, M., Stahl, T., Mendla, K. D., Schliebs, R., & Bigl, V. (2000) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2000.00211.x · Cited by 41 · see citing works
Inhibitors of β-Amyloid Formation Based on the β-Secretase Cleavage Site
Abbenante, G., Kovacs, D. M., Leung, D., et al. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2098 · Cited by 35 · see citing works
Expression and Function of Tumour Necrosis Factor-α-Converting Enzyme in the Central Nervous System
Moro, M. Á., Hurtado, O., Cárdenas, A., Romera, C., Madrigal, J. L. M., Fernández-Tomé, P., Leza, J. C., Lorenzo, P. L., & Lizasoaín, I. (2003) · Neurosignals · doi:10.1159/000071814 · Cited by 20 · see citing works
Moyers, S. B., & Kumar, N. B. (2004) · Nutrition Reviews · doi:10.1301/nr.2004.may.204-211 · Cited by 20 · see citing works
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Blennow, K., de Leon, M. J., & Zetterberg, H. (2006) · The Lancet · doi:10.1016/s0140-6736(06)69113-7 · Cited by 3,134 · see citing works
Alzheimer's Disease: From Pathology to Therapeutic Approaches
Jakob‐Roetne, R., & Jacobsen, H. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200802808 · Cited by 626 · see citing works
Qin, W., Yang, T., Ho, L., Zhao, Z., Wang, J., Chen, L., Zhao, W., Thiyagarajan, M., MacGrogan, D., Rodgers, J. T., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602909200 · Cited by 626 · see citing works
Rezai-Zadeh, K., Arendash, G. W., Hou, H., Fernandez, F., Jensen, M., Runfeldt, M., Shytle, R. D., & Tan, J. (2008) · Brain Research · doi:10.1016/j.brainres.2008.02.107 · Cited by 459 · see citing works
Williams, R. J., & Spencer, J. P. E. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.09.010 · Cited by 448 · see citing works
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Giunta, B., Fernandez, F., Nikolic, W. V., Obregon, D., Rrapo, E., Town, T., & Tan, J. (2008) · Journal of Neuroinflammation · doi:10.1186/1742-2094-5-51 · Cited by 327 · see citing works
Self-citationSmith, A., Giunta, B., Bickford, P. C., Fountain, M., Tan, J., & Shytle, R. D. (2010) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2010.01.012 · Cited by 280 · see citing works
Self-citationDurairajan, S. S. K., Liu, L.-F., Lu, J.-H., Chen, L.-L., Yuan, Q., Chung, S. K., Huang, L., Li, X.-S., Huang, J.-D., & Li, M. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.02.016 · Cited by 271 · see citing works
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Hatcher, H. C., Singh, R. N., Torti, F. M., & Torti, S. V. (2009) · Future Medicinal Chemistry · doi:10.4155/fmc.09.121 · Cited by 242 · see citing works
Tea consumption and cognitive impairment and decline in older Chinese adults
Ng, T.-P., Feng, L., Niti, M., Kua, E.-H., & Yap, K.-B. (2008) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/88.1.224 · Cited by 236 · see citing works
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Shal, B., Ding, W., Ali, H., Kim, Y. S., & Khan, S. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00548 · Cited by 234 · see citing works
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Ayaz, M., Junaid, M., Ullah, F., Subhan, F., Sadiq, A., Ali, G., Ovais, M., Shahid, M., Ahmad, A., Wadood, A., et al. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00697 · Cited by 220 · see citing works
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Sahni, J. K., Doggui, S., Ali, J., Baboota, S., Dao, L., & Ramassamy, C. (2011) · Journal of Controlled Release · doi:10.1016/j.jconrel.2010.11.033 · Cited by 219 · see citing works
Noguchi-Shinohara, M., Yuki, S., Dohmoto, C., Ikeda, Y., Samuraki, M., Iwasa, K., Yokogawa, M., Asai, K., Komai, K., Nakamura, H., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0096013 · Cited by 174 · see citing works
Mandel, S., Amit, T., Bar-Am, O., & Youdim, M. B. H. (2007) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2007.06.001 · Cited by 164 · see citing works
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“EGCG reduce βamyloid generation by promoting α-secretase cleavage of amyloid precursor protein (11) and efficiently inhibits the fibrillogenesis of amyloid-beta by directly binding to the natively unfolded polypeptides and preventing their conversion into toxic, on-pathway aggregation intermediates (12).”
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Zhang, S., Zhu, Q., Chen, J.-Y., OuYang, D., & Lu, J.-H. (2020) · Phytomedicine · doi:10.1016/j.phymed.2020.153316 · Cited by 74 · see citing works
Piccialli, I., Tedeschi, V., Caputo, L., D’Errico, S., Ciccone, R., De Feo, V., Secondo, A., & Pannaccione, A. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.876614 · Cited by 73 · see citing works
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- Authors
- Rezai-Zadeh, K., Shytle, D., Sun, N., Mori, T., Hou, H., Jeanniton, D., Ehrhart, J., Townsend, K., Zeng, J., Morgan, D., Hardy, J., Town, T., & Tan, J.
- Affiliations
- University of South Florida (US)
- Saitama Medical University (JP)
- National Institutes of Health (US)
- Yale University (US)
- Corresponding author
- Tan, Jun
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2005-09-21
- Volume
- 25
- Issue
- 38
- Pages
- 8807-8814
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6725500
- OpenAlex
- W2154508412
- Cited by
- 713
- References
- 40
- Citations by year
- 2026: 23 · 2025: 29 · 2024: 21 · 2023: 25 · 2022: 34 · 2021: 36 · 2020: 36 · 2019: 33 · 2018: 32 · 2017: 31 · 2016: 29 · 2015: 37 · 2014: 48 · 2013: 35 · 2012: 57
- FWCI
- 17.58
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- University of South Florida
- York University
- National Institutes of Health
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Pathology and Forensic Medicine › 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 precursor protein, amyloid-beta, alpha-secretase, transarterial chemoembolization, APP cleavage, soluble APP alpha, cerebral amyloidosis, neurodegeneration, dietary supplementation
- MeSH terms
- Alzheimer Disease, Amyloidosis, Animals, Catechin, Cells, Cultured, Female, Flavonoids, Mice, Transgenic, Tea, Amyloid beta-Protein Precursor, Mice
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