TY - JOUR
T1 - Mass Spectrometry-Based Analysis of Serum N-Glycosylation Changes in Patients with Parkinson's Disease
AU - Xu, Mingming
AU - Jin, Hong
AU - Wu, Zhen
AU - Han, Ying
AU - Chen, Jing
AU - Mao, Chengjie
AU - Hao, Piliang
AU - Zhang, Xumin
AU - Liu, Chun Feng
AU - Yang, Shuang
N1 - Publisher Copyright:
© 2022 American Chemical Society. All rights reserved.
PY - 2022/6/15
Y1 - 2022/6/15
N2 - It is urgently needed to find reliable biofluid biomarkers for early diagnosis of Parkinson's disease in order to achieve better treatment. Promising biomarkers can be found in Parkinson's disease-related glycoproteins as aberrant protein glycosylation plays an important role in disease progression. However, current information on serum N-glycoproteomic changes in Parkinson's disease is still limited. Here, we used glycoproteomics methods, which combine the solid-phase chemoenzymatic method, lectin affinity chromatography, and hydrophilic interaction chromatography with high-resolution mass spectrometry, to analyze the glycans, glycosites, and intact glycopeptides of serum. Increased abundance of glycans containing core fucose, sialic acid, and bisecting N-acetyl glucosamine was detected at the overall glycan level and also at specific glycosites of glycopeptides. Five Parkinson's disease-associated proteins with this type of N-glycosylation changes were also identified. We propose that the revealed site-specific N-glycosylation changes in serum can be potential biomarkers for Parkinson's disease.
AB - It is urgently needed to find reliable biofluid biomarkers for early diagnosis of Parkinson's disease in order to achieve better treatment. Promising biomarkers can be found in Parkinson's disease-related glycoproteins as aberrant protein glycosylation plays an important role in disease progression. However, current information on serum N-glycoproteomic changes in Parkinson's disease is still limited. Here, we used glycoproteomics methods, which combine the solid-phase chemoenzymatic method, lectin affinity chromatography, and hydrophilic interaction chromatography with high-resolution mass spectrometry, to analyze the glycans, glycosites, and intact glycopeptides of serum. Increased abundance of glycans containing core fucose, sialic acid, and bisecting N-acetyl glucosamine was detected at the overall glycan level and also at specific glycosites of glycopeptides. Five Parkinson's disease-associated proteins with this type of N-glycosylation changes were also identified. We propose that the revealed site-specific N-glycosylation changes in serum can be potential biomarkers for Parkinson's disease.
KW - Parkinson's disease
KW - biomarker
KW - glycosylation
KW - mass spectrometry
KW - serum
UR - http://www.scopus.com/inward/record.url?scp=85132022520&partnerID=8YFLogxK
U2 - 10.1021/acschemneuro.2c00264
DO - 10.1021/acschemneuro.2c00264
M3 - Article
C2 - 35640092
AN - SCOPUS:85132022520
SN - 1948-7193
VL - 13
SP - 1719
EP - 1726
JO - ACS Chemical Neuroscience
JF - ACS Chemical Neuroscience
IS - 12
ER -