Implications of Glycosylation in Alzheimer’s Disease
Open accessAbstract
Alzheimer’s disease (AD) is the most common cause of dementia, affecting millions of people worldwide, and no cure is currently available. The major pathological hallmarks of AD are considered to be amyloid beta plaques and neurofibrillary tangles, generated by respectively APP processing and Tau phosphorylation. Recent evidence imply that glycosylation of these proteins, and a number of other AD-related molecules is altered in AD, suggesting a potential implication of this process in disease pathology. In this review we summarize the understanding of glycans in AD pathogenesis, and discuss how glycobiology can contribute to early diagnosis and treatment of AD, serving as potential biomarkers and therapeutic targets. Furthermore, we look into the potential link between the emerging topic neuroinflammation and glycosylation, combining two interesting, and until recent years, understudied topics in the scope of AD. Lastly, we discuss how new model platforms such as induced pluripotent stem cells can be exploited and contribute to a better understanding of a rather unexplored area in AD.
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Amyloidogenic and non-amyloidogenic processing of APP is influenced not only by the biochemical properties of APP but also by the biochemical properties of the secretases.
“Amyloidogenic and non-amyloidogenic processing of APP is influence not only by the biochemical properties of APP but also by the biochemical properties of the secretases 21,24,26 .”
From Targeting Lysosomal Dysfunction to Alleviate Plaque Deposition in an Alzheimer Disease Model (2025) · cites this paper as [21]
The R47H variant of TREM2 presents an altered glycosylation pattern and decreased stability compared with wild-type TREM2.
“Interestingly, the R47H variant of TREM2, which is expressed by microglia and linked to innate immunity, has been found to present an altered glycosylation pattern and decreased stability compared with wild-type TREM2 [176], indicating a potential link between microglial neuroinflammation and glycosylation [177, 178].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [177]
In Alzheimer's disease, tau protein was found to be glycosylated and O-GlcNAcylated before becoming aberrantly phosphorylated and N-linked-glycosylated at the N410 site of the tau 2N4R heterodimer.
“In AD, tau protein was found to be glycosylated and O-GlcNAcylated before becoming aberrantly phosphorylated and N-linked-glycosylated at the N410 site of the tau 2N4R heterodimer.”
From Role of Tau Protein in Neurodegenerative Diseases and Development of Its Targeted Drugs: A Literature Review (2024) · cites this paper as [38]
Aberrant N-linked glycosylation of tau may have potential as a biomarker of early Alzheimer's disease and as a marker of Alzheimer's disease progression.
“This aberrant N-linked glycosylation may have potential as a biomarker of early AD as well as a marker of AD progression [38].”
From Role of Tau Protein in Neurodegenerative Diseases and Development of Its Targeted Drugs: A Literature Review (2024) · cites this paper as [38]
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References 119 · Cited by 114
Research works printed but not linked: 1
- American Association for the Advancement of Science (2008). Life Expectancy Around the World has Increased Steadily for Nearly 200 Years. | Learn Science at Scitable. Scitable by Nature Education Available online at: https://www.nature.com/scitable/content/life-expectancy-around-the-world-has-increased-19786/ (accessed September 14, 2020).
- Authors
- Haukedal, H., & Freude, K. K.
- Affiliations
- University of Copenhagen (DK)
- Corresponding author
- Freude, Kristine K.
- Venue
- Frontiers in Neuroscience
- Publisher
- Frontiers Media SA
- Published
- 2021-01-13
- Volume
- 14
- Pages
- 625348-625348
- ISSN
- 1662-453X (ISSN-L)
- PMC
- PMC7838500
- OpenAlex
- W3118288864
- Cited by
- 114
- References
- 119
- Citations by year
- 2026: 12 · 2025: 31 · 2024: 18 · 2023: 19 · 2022: 23 · 2021: 11
- FWCI
- 2.37
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Neuroscience (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (publishedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Novo Nordisk Fonden
- Innovationsfonden
- 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
- Alzheimer's disease, glycosylation, glycans, amyloid plaques, neurofibrillary tangles, APP processing, tau phosphorylation, biomarkers, therapeutic target, neuroinflammation, induced pluripotent stem cells, pathogenesis
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