Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease.

Wischik, C M; Novak, M; Thøgersen, H C; Edwards, P C; Runswick, M J; Jakes, R; Walker, J E; Milstein, C; Roth, M; Klug, A

doi:10.1073/pnas.85.12.4506

Cited by 939Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease.

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Wischik, C M, Novak, M, Thøgersen, H C, Edwards, P C, Runswick, M J, Jakes, R, Walker, J E, Milstein, C +2 more·1988·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.85.12.4506PMC PMC280459

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Abstract

A substantially enriched preparation of Alzheimer paired helical filaments (PHFs) has been used as a starting point for biochemical studies. Pronase treatment, which strips off adhering proteins, leaves a resistant core that is structurally intact. This has been used to raise a monoclonal antibody that decorates the filament core. The antibody has been used to follow the extraction of two peptide fragments (9.5 and 12 kDa) by immunoblotting. The link between the PHF as a morphological entity and these peptides has been established independently by photoaffinity labeling with a chemical ligand to the PHF core. Sequence analysis of these peptides was used to design oligonucleotide probes for cloning a cognate cDNA, which leads to its identification as human microtubule-associated tau protein. The sequencing of the 9.5- and 12-kDa peptides shows they are derived from a conserved region of tau containing three repeating segments. Since these fragments have been copurified with the Pronase-resistant core and are only released by subsequent steps, the corresponding part of the tau molecule must be tightly bound in the PHF core.

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The composition of paired helical filaments in Alzheimer's disease includes all 6 isoforms of tau protein, including isoforms with 3-repeats and 4-repeats in the microtubule binding domain.
“The composition of PHF in AD includes all 6 isoforms of tau protein, including isoforms with 3-repeats (3R tau) and 4-repeats (4R tau) in the microtubule binding domain.”
From The neuropathological diagnosis of Alzheimer's disease (2019) · cites this paper as [59]

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“Both a loss of normal function and a toxic gain of function are postulated, whereby PHFs are able to co-aggregate with normal tau proteins [61].”
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Authors: Wischik, C. M., Novak, M., Thøgersen, H. C., Edwards, P. C., Runswick, M. J., Jakes, R., Walker, J. E., Milstein, C., Roth, M., & Klug, A.
Affiliations: MRC Laboratory of Molecular Biology (GB)
Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.
ORCID: Edwards, P C
Walker, J E
Roth, M
Klug, A
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1988-06
Volume: 85
Issue: 12
Pages: 4506-4510
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.85.12.4506
PMC: PMC280459
OpenAlex: W2018908557
Cited by: 939
References: 0
Citations by year: 2026: 12 · 2025: 17 · 2024: 20 · 2023: 24 · 2022: 21 · 2021: 35 · 2020: 36 · 2019: 30 · 2018: 30 · 2017: 34 · 2016: 40 · 2015: 26 · 2014: 29 · 2013: 20 · 2012: 26
FWCI: 35.06
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)
Topics: Health Sciences › Medicine › Physiology › 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, monoclonal antibodies, peptide fragments, photoaffinity labeling, cDNA cloning, microtubule-associated proteins, protein sequence analysis, oligonucleotide probes
MeSH terms: Alzheimer Disease, Amino Acid Sequence, Brain, Cytoskeleton, Microscopy, Electron, Microtubule-Associated Proteins, Molecular Sequence Data, Nerve Tissue Proteins, Peptide Fragments, tau Proteins

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Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease.

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