Cited by 879Alzheimer's disease research and treatmentsParkinson's Disease Mechanisms and TreatmentsPrion Diseases and Protein Misfolding

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Initiation and Synergistic Fibrillization of Tau and Alpha-Synuclein

Giasson, Benoit I., Forman, Mark S., Higuchi, Makoto, Golbe, Lawrence I., Graves, Charles L., Kotzbauer, Paul T., Trojanowski, John Q., Lee, Virginia M.-Y.·2003·Science

DOI 10.1126/science.1082324

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Abstract

Alpha-synuclein (alpha-syn) and tau polymerize into amyloid fibrils and form intraneuronal filamentous inclusions characteristic of neurodegenerative diseases. We demonstrate that alpha-syn induces fibrillization of tau and that coincubation of tau and alpha-syn synergistically promotes fibrillization of both proteins. The in vivo relevance of these findings is grounded in the co-occurrence of alpha-syn and tau filamentous amyloid inclusions in humans, in single transgenic mice that express A53T human alpha-syn in neurons, and in oligodendrocytes of bigenic mice that express wild-type human alpha-syn plus P301L mutant tau. This suggests that interactions between alpha-syn and tau can promote their fibrillization and drive the formation of pathological inclusions in human neurodegenerative diseases.

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Additional file 3 of Cerebrospinal fluid α-synuclein predicts neurodegeneration and clinical progression in non-demented elders
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“…labeled tufted astrocytes in the PSP midbrain [57], consistent with previous observations of isSID reactive tau-tangles[57] and known interactions between α syn and tau[17, 28, 30]. α Syn also bound to neuromelanin in midbrain and in the grafts, regardless of diagnosis and synucleinopathy status.”
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Authors: Giasson, B. I., Forman, M. S., Higuchi, M., Golbe, L. I., Graves, C. L., Kotzbauer, P. T., Trojanowski, J. Q., & Lee, V. M.-Y.
Affiliations: University of Medicine and Dentistry of New Jersey (US)
Corresponding author: Lee, Virginia M.-Y.
ORCID: Giasson, Benoit I.
Higuchi, Makoto
Golbe, Lawrence I.
Kotzbauer, Paul T.
Trojanowski, John Q.
Lee, Virginia M.-Y.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2003-04-25
Volume: 300
Issue: 5619
Pages: 636-640
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.1082324
OpenAlex: W2073893553
Cited by: 879
References: 27
Citations by year: 2026: 23 · 2025: 29 · 2024: 37 · 2023: 35 · 2022: 58 · 2021: 32 · 2020: 50 · 2019: 52 · 2018: 49 · 2017: 42 · 2016: 35 · 2015: 31 · 2014: 39 · 2013: 42 · 2012: 33
FWCI: 26.70
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
Keywords: alpha-synuclein, tau protein, amyloid fibril formation, protein aggregation, neurodegenerative diseases, synucleinopathies, tauopathy, oligodendrocytes, P301L tau, A53T alpha-synuclein, transgenic mouse model, intraneuronal inclusions
MeSH terms: Amyloid, Animals, Biopolymers, Brain Chemistry, Humans, Mice, Inbred C3H, Mice, Inbred C57BL, Mice, Transgenic, Microscopy, Electron, Microscopy, Fluorescence, Nerve Tissue Proteins, Neurons, Oligodendroglia, Protein Conformation, Microscopy, Immunoelectron, tau Proteins, Neurodegenerative Diseases, Protein Isoforms, Tauopathies, Mice, Synucleins, alpha-Synuclein

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Initiation and Synergistic Fibrillization of Tau and Alpha-Synuclein

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