Role of glycosylation in hyperphosphorylation of tau in Alzheimer's disease
Abstract
In Alzheimer's disease (AD) brain, microtubule‐associated protein tau is abnormally modified by hyperphosphorylation and glycosylation, and is aggregated as neurofibrillary tangles of paired helical filaments. To investigate the role of tau glycosylation in neurofibrillary pathology, we isolated various pools of tau protein from AD brain which represent different stages of tau pathology. We found that the non‐hyperphosphorylated tau from AD brain but not normal brain tau was glycosylated. Monosaccharide composition analyses and specific lectin blots suggested that the tau in AD brain was glycosylated mainly through N‐linkage. In vitro phosphorylation indicated that the glycosylated tau was a better substrate for cAMP‐dependent protein kinase than the deglycosylated tau. These results suggest that the glycosylation of tau is an early abnormality that can facilitate the subsequent abnormal hyperphosphorylation of tau in AD brain.
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N-glycosylated tau is prone to phosphorylation, but shows reduced aggregation.
“Several studies suggest that N-glycosylated tau is prone to phosphorylation, but shows reduced aggregation [184, 185].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [184]
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References 45 · Cited by 167
- Authors
- Liu, F., Zaidi, T., Iqbal, K., Grundke-Iqbal, I., Merkle, R. K., & Gong, C.-X.
- Affiliations
- New York State Office for People With Developmental Disabilities (US)
- University of Georgia (US)
- Corresponding author
- Gong, Cheng-Xin
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2002-01-13
- Volume
- 512
- Issue
- 1-3
- Pages
- 101-106
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1985696068
- Cited by
- 167
- References
- 45
- Citations by year
- 2026: 5 · 2025: 14 · 2024: 9 · 2023: 8 · 2022: 12 · 2021: 12 · 2020: 10 · 2019: 12 · 2018: 8 · 2017: 4 · 2016: 6 · 2015: 7 · 2014: 3 · 2013: 3 · 2012: 9
- FWCI
- 3.80
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ag008076-09, 5r01ag005892-16, 2p41rr005351-21, 5r01ns018105-17)
- National Institute on Aging (AG-05892, AG 08076, AG16760, R01AG016760)
- National Institute of Mental Health (MH.NS 31862)
- National Institute of Neurological Disorders and Stroke (NS 18105)
- National Center for Research Resources (2P41-RR05351-06)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- tau protein, glycosylation, hyperphosphorylation, Alzheimer's disease, neurofibrillary tangles, paired helical filaments, N-glycosylation, protein kinase A, lectin blotting, monosaccharide composition
- MeSH terms
- Acetylglucosamine, Alzheimer Disease, Glycosylation, Hexoses, Humans, Nucleotidyltransferases, Phosphorylation, Protein Processing, Post-Translational, Neurofibrillary Tangles, tau Proteins, N-Acetylneuraminic Acid
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