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Analysis of microtubule-associated protein tau glycation in paired helical filaments.
Open accessAbstract
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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“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 [177]
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“Glycated tau is only detected in PHF-tau isolated from AD brain samples, but not in soluble tau from AD or normal brain samples [177, 179].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [177]
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“The pro-aggregation PTMs of Tau include phosphorylation [7–10], truncation [11, 12], glycation [13], acetylation [14, 15], sumoylation [16, 17], ubiquitination [18, 19] and nitration [20–22].”
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Characterization of tau proteins in human neuroblastoma SH-SY5Y cell line
Uberti, D. L., Rizzini, C., Spano, P., & Memo, M. (1997) · Neuroscience Letters · doi:10.1016/s0304-3940(97)00715-5 · Cited by 51
Reynolds, M. R., Lukas, T. J., Berry, R. W., & Binder, L. I. (2006) · Biochemistry · doi:10.1021/bi052142h · Cited by 55
Pei, J.-J., Sjögren, M., & Winblad, B. (2008) · Current Opinion in Psychiatry · doi:10.1097/yco.0b013e328314b78b · Cited by 49
Thome, J., Münch, G. W., Müller, R., Schinzel, R., Kornhuber, J., Blum-Degen, D., Sitzmann, L., Rösler, M., Heidland, A., & Riederer, P. F. (1996) · Life Sciences · doi:10.1016/0024-3205(96)00349-9 · Cited by 50
Intracellular Toxic AGEs (TAGE) Triggers Numerous Types of Cell Damage
Takeuchi, M., Sakai, A., Takata, T., Takino, J.-I., Koriyama, Y., Kikuchi, C., Furukawa, A., Nagamine, K., Hori, T., & Matsunaga, T. (2021) · Biomolecules · doi:10.3390/biom11030387 · Cited by 51
“, the accumulation of Aβ is increased by Aβ glycation, and the formation of NFT from phosphorylated tau is accelerated by glycation of the tau protein [55,56].”
BackgroundSayre, L. M., Perry, G. L., & Smith, M. A. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)09012-6 · Cited by 49
Moreno, F. J., Medina, M., Pérez, M., de Garcini, E. M., & Ávila, J. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00934-2 · Cited by 47
Alzheimer's disease: Is this a brain specific diabetic condition?
Rani, V., Deshmukh, R. R., Jaswal, P., Kumar, P., & Bariwal, J. B. (2016) · Physiology & Behavior · doi:10.1016/j.physbeh.2016.05.041 · Cited by 46
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Jhamandas, J. H., & MacTavish, D. (2011) · APOPTOSIS · doi:10.1007/s10495-011-0656-3 · Cited by 45
“RAGE is also implicated in development of diabetic vascular complications [9].”
BackgroundŽilka, N., Korenova, M., & Novák, M. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0499-y · Cited by 47
“In Alzheimer disease and non-AD tauopathies, tau undergoes pathological posttranslational modifications such as truncation [117–119], hyperphosphorylation [59], glycosylation [166], glycation [93, 172], ubiquitination [16], polyamination [159] and nitration [66] that can influence the conformational properties of tau…”
Robert, M., & Mathuranath, P. S. (2007) · Neurology India · doi:10.4103/0028-3886.30420 · Cited by 45
“Moreover, the tau found in PHFs are often ubiquitinated and glycated in AD (Ledesma et al., 1994) Tau isoforms with three repeats assemble into PHFs, whereas tau isoforms”
BackgroundGlucose Slows Down the Heat-Induced Aggregation of β-Lactoglobulin at Neutral pH
Pinto, M. D. S., Bouhallab, S., de Carvalho, A. F., Henry, G., Putaux, J., & Léonil, J. (2011) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf2037664 · Cited by 43
Kurata, T., Miyazaki, K., Morimoto, N., Kawai, H., Ohta, Y., Ikeda, Y., & Abe, K. (2013) · Neurological Research · doi:10.1179/1743132812y.0000000127 · Cited by 44
Takeuchi, M., Sato, T., Takino, J.-I., Kobayashi, Y., Furuno, S., Kikuchi, S., & Yamagishi, S. (2007) · Medical Hypotheses · doi:10.1016/j.mehy.2006.12.017 · Cited by 43
Janke, C., Holzer, M., Klose, J., & Arendt, T. (1996) · FEBS Letters · doi:10.1016/0014-5793(95)01522-1 · Cited by 39
Genetic deficiency of neuronal RAGE protects against AGE-induced synaptic injury
Zhang, H., Wang, Y., Yan, S., Wu, L., Wu, L., Yan, S. S. D., & Yan, S. S. D. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.248 · Cited by 40
Detection of d-aspartate in tau proteins associated with Alzheimer paired helical filaments
Kenessey, Á., Yen, S.-H. C., Liu, W.-K., Yang, X.-R., & Dunlop, D. S. (1995) · Brain Research · doi:10.1016/0006-8993(95)00061-t · Cited by 39
Coughlan, C. M. (2000) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(00)00036-x · Cited by 39
The role of the Maillard reaction in other pathologies: Alzheimer's disease
Colaco, C. A. L. S., Ledesma, M. D., Harrington, C. R., & Ávila, J. (1996) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/11.supp5.7 · Cited by 37
“The relevance of glycation as an additional pathological modification of tau in vivo is supported by the immunohistochemical co-localization of AGEs with both neurofibrillary tangles and PHFs [20,24].”
BackgroundResultInfluentialSelf-citationStructural Analysis and Aggregation Propensity of Reduced and Nonreduced Glycated Insulin Adducts
Alavi, P., Yousefi, R., Amirghofran, S., Karbalaei-Heidari, H., & Moosavi-Movahedi, A. (2013) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-013-0207-1 · Cited by 38
Tau Abnormalities and the Potential Therapy in Alzheimer’s Disease
Almansoub, H. A. M. M., Tang, H. R., Wu, Y., Wang, D., Mahaman, Y. A. R., Wei, N., Almansob, Y. A. M., He, W., & Liu, D. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180868 · Cited by 39
Cognitive Impairment and Diabetes
Dash, S. K. (2013) · Recent Patents on Endocrine Metabolic & Immune Drug Discovery · doi:10.2174/1872214811307020009 · Cited by 36
Hyperphosphorylation-induced self assembly of murine tau: a comparison with human tau
Chohan, M. O., Haque, N., Alonso, A., El-Akkad, E., Grundke, I., Grover, A., & Iqbal, K. (2004) · Journal of Neural Transmission · doi:10.1007/s00702-004-0241-9 · Cited by 36
“, 1987), glycated (Ledesma et al., 1994), and O-GlcNacylated (Dong et al.”
Role of Oxidative Stress in Frontotemporal Dementia
Gerst, J. L., Siedlak, S. L., Nunomura, A., Castellani, R. J., Perry, G. L., & Smith, M. A. (1999) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000051220 · Cited by 36
“, 1997], carbonyl-modified neurofilament protein and free carbonyls [Smith et al., 1994b, 1995a, b, 1996; Ledesma et al., 1994; Vitek et al., 1994; Yan et al., 1994; Montine et al., 1996a; Sayre et al., 1997] are all associated with neuronal damage.”
BackgroundTauons and Prions: Infamous Cousins?
Novák, P., Prčina, M., & Kontseková, E. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110194 · Cited by 36
“Furthermore, it is subject to a multitude of modifications : truncation [14], hyperphosphorylation [15], glycosylation[16], glycation [17], ubiquitination [18], nitration [19], or polyamination [20].”
The in vitro formation of recombinant τ polymers
Ledesma, M. D., Medina, M., & Ávila, J. (1996) · Molecular and Chemical Neuropathology · doi:10.1007/bf02815107 · Cited by 36
Self-citation
Metadata
- 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)
- 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
- 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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