τ Protein from Alzheimer's Disease Patients Is Glycated at Its Tubulin‐Binding Domain
Abstract
Abstract: Glycated residues of τ protein from paired helical filaments isolated from the brains of Alzheimer's disease patients were localized by doing a proteolytic cleavage of the protein, fractionation of the resulting peptides, and identification of those peptides using specific antibodies. The most suitable residues for glycation, lysines, present at the tubulin‐binding motif of τ protein, seem to be preferentially modified compared with those lysines present at other regions. Among these modified lysines, those located in the sequence comprising residues 318–336 (in the largest human τ isoform) were found to be glycated, as determined by the reaction with an antibody that recognizes a glycated peptide containing this sequence. Because those lysines are present in a tubulin binding motif of τ protein, its modification could result in a decrease in the interaction of τ with tubulin.
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Tau is preferentially glycated at Lys residues within the microtubule-binding domain, where advanced glycation end products are generated.
“Tau is preferentially glycated at Lys residues within the microtubule-binding domain, where advanced glycation end products are generated [177–179].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [178]
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- Authors
- Ledesma, M. D., Bonay, P., & Avila, J.
- Affiliations
- Consejo Superior de Investigaciones Científicas (ES)
- Corresponding author
- Ledesma, M. Dolores
- ORCID
- Ledesma, M. Dolores
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 1995-10
- Volume
- 65
- Issue
- 4
- Pages
- 1658-1664
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W1965302577
- Cited by
- 109
- References
- 0
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 3 · 2023: 1 · 2022: 4 · 2021: 4 · 2020: 6 · 2019: 5 · 2018: 3 · 2017: 4 · 2016: 6 · 2015: 3 · 2014: 5 · 2013: 2 · 2012: 3
- FWCI
- 4.99
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Keywords
- tau protein, glycation, lysine modification, paired helical filaments, Alzheimer's disease, post-translational modification, peptide mapping
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Animals, Cattle, Glycosylation, Humans, Peptide Fragments, Serine Endopeptidases, Tubulin, tau Proteins
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