Journal
ANALYTICAL CHEMISTRY
Volume 92, Issue 1, Pages 867-874Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.9b03555
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Funding
- National Key Research and Development Program of China [2018YFA0507501, 2017YFA0505001, 2016YFB0201702]
- National Nature Science Foundation of China [31570825]
- Shanghai Science and Technology Research Project [16ZR1402400]
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Protein N-glycosylation is ubiquitous in the brain. and is closely related to cognition and memory. Alzheimer's disease (AD) is a multifactorial disorder that lacks a clear pathogenesis and treatment. Aberrant N-glycosylation has been suggested to be involved in AD pathology. However, the systematic variations in protein N-glycosylation and their roles in AD have not been thoroughly investigated due to technical challenges. Here, we applied multilayered N-glycoproteomics to quantify the global protein expression levels, N-glycosylation sites, N-glycans, and site-specific N-glycopeptides in AD (APP/PS1 transgenic) and wild-type mouse brains. The N-glycoproteomic landscape exhibited highly complex site-specific heterogeneity in AD mouse brains. The generally dysregulated N-glycosylation in AD, which involved proteins such as glutamate receptors as well as fucosylated and oligomannose glycans, were explored by quantitative analyses. Furthermore, functional studies revealed the crucial effects of N-glycosylation on proteins and neurons. Our work provides a systematic multilayered N-glycoproteomic strategy for AD and can be applied to diverse biological systems.
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