Cited by 1,036Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

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Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans

Goedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., Crowther, R. A.·1996·Nature

DOI 10.1038/383550a0

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Abstract

The paired helical filament (PHF) is the major component of the neurofibrillary deposits that form a defining neuropathological characteristic of Alzheimer's disease. PHFs are composed of microtubule-associated protein tau, in a hyperphosphorylated state. Hyperphosphorylation of tau results in its inability to bind to microtubules and is believed to precede PHF assembly. However, it is unclear whether hyperphosphorylation of tau is either necessary or sufficient for PHF formation. Here we show that non-phosphorylated recombinant tau isoforms with three microtubule-binding repeats form paired helical-like filaments under physiological conditions in vitro, when incubated with sulphated glycosaminoglycans such as heparin or heparan sulphate. Furthermore, heparin prevents tau from binding to microtubules and promotes microtubule disassembly. Finally, we show that heparan sulphate and hyperphosphorylated tau coexist in nerve cells of the Alzheimer's disease brain at the earliest known stages of neurofibrillary pathology. These findings, with previous studies which show that heparin stimulates tau phosphorylation by a number of protein kinases, indicate that sulphated glycosaminoglycans may be a key factor in the formation of the neurofibrillary lesions of Alzheimer's disease.

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Authors: Goedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., & Crowther, R. A.
Affiliations: MRC Laboratory of Molecular Biology (GB)
ORCID: Goedert, M.
Hasegawa, M.
Smith, M. J.
Crowther, R. A.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1996-10
Volume: 383
Issue: 6600
Pages: 550-553
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/383550a0
OpenAlex: W1994282166
Cited by: 1,036
References: 32
Citations by year: 2026: 29 · 2025: 35 · 2024: 43 · 2023: 47 · 2022: 57 · 2021: 50 · 2020: 43 · 2019: 47 · 2018: 50 · 2017: 48 · 2016: 26 · 2015: 27 · 2014: 20 · 2013: 42 · 2012: 30
FWCI: 27.47
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: tau protein, paired helical filaments, Alzheimer's disease, neurofibrillary tangles, sulfated glycosaminoglycans, heparin, heparan sulfate, tau hyperphosphorylation, microtubule binding, microtubule disassembly, tau isoforms, neurofibrillary pathology
MeSH terms: Alzheimer Disease, Escherichia coli, Heparin, Heparitin Sulfate, Heparan Sulfate, Hippocampus, Humans, Neurofibrils, Phosphorylation, Protein Binding, Recombinant Proteins, tau Proteins

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Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans

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