Cited by 333Alzheimer's disease research and treatmentsAdvanced Glycation End Products researchDementia and Cognitive Impairment Research

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Analysis of microtubule-associated protein tau glycation in paired helical filaments.

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Ledesma, M.D., Bonay, P., Colaço, C., Avila, J.·1994·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(17)31849-5

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Abstract

Alzheimer's disease is typified by the characteristic histopathological lesions of neurofibrillar plaques and tangles. The latter are composed of paired helical filaments (PHFs), the major components of which are modified forms of the microtubule-associated protein tau. The exact nature of these modifications remains unknown, although the presence of hyperphosphorylated tau in PHFs argues strongly that phosphorylation is one of the modifications that result in the polymerization of tau into PHFs. However, hyperphosphorylation alone is insufficient to explain the formation of PHFs. In an attempt to characterize other post-translational modifications of PHF-tau, we have analyzed its glycation. A fraction of PHF-tau seems to be glycated in vivo, whereas soluble tau from either Alzheimer's disease or non-demented human brain is not glycated at all. Purified tau from bovine brain can be efficiently glycated in vitro. Tau glycation is accompanied by a decrease in the tau binding to tubulin. These results support the view that glycation may be one of the modifications hampering the binding of tau to tubulin in Alzheimer's disease, thus facilitating tau aggregation into PHFs.

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Authors: Ledesma, M. D., Bonay, P., Colaço, C., & Avila, J.
Affiliations: Consejo Superior de Investigaciones Científicas (ES)
ORCID: Ledesma, M.D.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1994-08
Volume: 269
Issue: 34
Pages: 21614-21619
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(17)31849-5
OpenAlex: W1577069180
Semantic Scholar: 68928334bcb2a45f531ceaeaa8ef0e1a72308735
Cited by: 333
References: 72
Citations by year: 2026: 1 · 2025: 2 · 2024: 7 · 2023: 6 · 2022: 4 · 2021: 8 · 2020: 2 · 2019: 12 · 2018: 13 · 2017: 7 · 2016: 10 · 2015: 5 · 2014: 13 · 2013: 11 · 2012: 13
FWCI: 11.84
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, 9581 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion, cc-by)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: tau protein, glycation, paired helical filaments, Alzheimer's disease, post-translational modification, tau aggregation, neurofibrillary tangles, hyperphosphorylation
MeSH terms: Aged, Aged, 80 and over, Alzheimer Disease, Amino Acid Sequence, Animals, Brain Chemistry, Cattle, Diabetes Mellitus, Humans, Lysine, Microtubules, Molecular Sequence Data, Protein Binding, Neurofibrillary Tangles, tau Proteins, Glycation End Products, Advanced, Diabetes Complications

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Analysis of microtubule-associated protein tau glycation in paired helical filaments.

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