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Multilayered N-glycoproteomics reveals impaired N-glycosylation promoting Alzheimer’s disease
Open accessPreprint — published as 10.1021/acs.analchem.9b03555
Abstract
Alzheimer’s disease (AD) is one of the most common neurodegenerative diseases that currently lacks clear pathogenesis and effective treatment. Protein glycosylation is ubiquitous in brain tissue and site-specific analysis of N-glycoproteome, which is technically challenging, can advance our understanding of the glycoproteins’ role in AD. In this study, we profiled the multilayered variations in proteins, N-glycosites, N-glycans, and in particular site-specific N-glycopeptides in the APP/PS1 and wild type mouse brain through combining pGlyco 2.0 strategy with other quantitative N-glycoproteomic strategies. The comprehensive brain N-glycoproteome landscape was constructed, and rich details of the heterogeneous site-specific protein N-glycosylations were exhibited. Quantitative analyses explored generally downregulated N-glycosylation involving proteins such as glutamate receptors, as well as fucosylated and oligo-mannose type glycans in APP/PS1 mice versus wild type mice. Moreover, our preliminary functional study revealed that N-glycosylation was crucial for the membrane localization of NCAM1 and for maintaining the excitability and viability of neuron cells. Our work offered a panoramic view of the N-glycoproteomes in Alzheimer’s disease and revealed that generally impaired N-glycosylation promotes Alzheimer’s disease progression.
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Metadata
- Authors
- Fang, P., Xie, J.-J., Sang, S.-M., Zhang, L., Liu, M.-Q., Yang, L.-J., Xu, Y.-T., Yan, G.-Q., Yao, J., Gao, X., Qian, W.-J., Wang, Z.-F., Zhang, Y., Yang, P.-Y., & Shen, H.-L.
- Affiliations
- Fudan University (CN)
- Shanghai Medical College of Fudan University (CN)
- Corresponding author
- Zhang, Yang
- Venue
- Analytical Chemistry
- Publisher
- openRxiv
- Published
- 2019-04-22
- Volume
- 92
- Issue
- 1
- Pages
- 867-874
- ISSN
- 0003-2700 (ISSN-L)
- OpenAlex
- W2990324610
- Cited by
- 60
- References
- 1
- Citations by year
- 2026: 2 · 2025: 10 · 2024: 4 · 2023: 10 · 2022: 14 · 2021: 8 · 2020: 11 · 2019: 1
- FWCI
- 2.81
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- Analytical Chemistry (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- Natural Science Foundation of Shanghai (16ZR1402400)
- National Natural Science Foundation of China (31570825)
- Chinese Academy of Sciences
- Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences
- Ministry of Science and Technology of the People's Republic of China (2018YFA0507501, 2016YFB0201702, 2017YFA0505001)
- Fudan University
- Directorate for Biological Sciences
- National Key Research and Development Program of China (2018YFA0507501, 2017YFA0505001)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Keywords
- Alzheimer's disease, N-glycosylation, N-glycoproteomics, APP/PS1 mice, N-glycan profiling, glutamate receptors, fucosylated glycans, high-mannose glycans, brain proteome, neuronal dysfunction
- MeSH terms
- Alzheimer Disease, Animals, Brain, Brain Chemistry, Cell Line, Glycopeptides, Glycoproteins, Glycosylation, Humans, Mice, Transgenic, Polysaccharides, Protein Processing, Post-Translational, Proteome, Proteomics, Mice, Tandem Mass Spectrometry
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