Cited by 430Alzheimer's disease research and treatmentsAdvanced Proteomics Techniques and ApplicationsDementia and Cognitive Impairment Research

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Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain

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Hasegawa, M, Morishima-Kawashima, M, Takio, K, Suzuki, M, Titani, K, Ihara, Y·1992·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(18)41890-x

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Abstract

Tau with unusually slow mobilities in sodium dodecyl sulfate-polyacrylamide gel electrophoresis was purified from the Sarkosyl-insoluble pellet of Alzheimer's disease brain homogenates. Such species of tau (PHF-tau) are considered to construct the framework of the sodium dodecyl sulfate-soluble form of paired helical filaments (PHF). Detailed comparison of peptide maps of PHF-tau and normal tau before and after dephosphorylation pointed to three anomalously eluted peaks which contained abnormally phosphorylated peptides, residues 191-225, 226-240, 260-267, and 386-438, according to the numbering of the longest tau isoform (Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., and Crowther, R. A. (1989) Neuron 3, 519-526). Protein sequence and mass spectrometric analyses localized Thr-231 and Ser-235 as the abnormal phosphorylation sites and further indicated that each tau 1 site (residues 191-225) and the most carboxyl-terminal portion of the protein (residues 386-438) carries more than two abnormal phosphates. Ser-262 was also phosphorylated in a fraction of PHF-tau. Modifications other than phosphorylation, removal of the initiator methionine, and N alpha-acetylation at the amino terminus and deamidation at 2 asparaginyl residues were found in PHF-tau, but these modifications were also present in normal tau.

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Authors: Hasegawa, M., Morishima-Kawashima, M., Takio, K., Suzuki, M., Titani, K., & Ihara, Y.
Affiliations: The University of Tokyo (JP)
ORCID: Hasegawa, M
Suzuki, M
Ihara, Y
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1992-10
Volume: 267
Issue: 24
Pages: 17047-17054
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(18)41890-x
OpenAlex: W1598318710
Cited by: 430
References: 43
Citations by year: 2026: 4 · 2025: 10 · 2024: 8 · 2023: 10 · 2022: 7 · 2021: 8 · 2020: 19 · 2019: 14 · 2018: 10 · 2017: 3 · 2016: 17 · 2015: 11 · 2014: 5 · 2013: 10 · 2012: 9
FWCI: 22.71
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 10240 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: tau protein, Alzheimer's disease, paired helical filaments, phosphorylation sites, dephosphorylation, peptide mapping, protein modification, N-terminal acetylation, deamidation
MeSH terms: Alzheimer Disease, Amino Acid Sequence, Brain, Brain Chemistry, Electrophoresis, Polyacrylamide Gel, Humans, Molecular Sequence Data, Peptide Fragments, Peptide Mapping, Mass Spectrometry, tau Proteins

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Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain

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