Quantitative Site-Specific Glycoproteomics Reveals Glyco-Signatures for Breast Cancer Diagnosis

Intact glycopeptide characterization by mass spectrometry has proven to be a versatile tool for site-specific glycoproteomics analysis and biomarker screening. Here, we present a method using a new model of a Q-TOF instrument equipped with a Zeno trap for intact glycopeptide identification and demon...

Full description

Saved in:
Bibliographic Details
Published in:Analytical chemistry (Washington) 2025-01, Vol.97 (1), p.114-121
Main Authors: Yang, Yi, Zhao, Dan, Luo, Ji, Lin, Ling, Lin, Yuxiang, Shan, Baozhen, Chen, Hongxu, Qiao, Liang
Format: Article
Language:English
Subjects:
Biomarkers
Biomarkers, Tumor - analysis
Biomarkers, Tumor - blood
Breast cancer
Breast Neoplasms - blood
Breast Neoplasms - diagnosis
Female
Glycopeptides
Glycopeptides - analysis
Glycopeptides - blood
Glycoproteins - analysis
Glycoproteins - blood
Humans
Machine Learning
Mass spectrometry
Mass spectroscopy
Observational learning
Polysaccharides
Polysaccharides - analysis
Polysaccharides - blood
Polysaccharides - chemistry
Proteomes
Proteomics - methods
Citations: Items that this one cites
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Intact glycopeptide characterization by mass spectrometry has proven to be a versatile tool for site-specific glycoproteomics analysis and biomarker screening. Here, we present a method using a new model of a Q-TOF instrument equipped with a Zeno trap for intact glycopeptide identification and demonstrate its ability to analyze large-cohort glycoproteomes. From 124 clinical serum samples of breast cancer, noncancerous diseases, and nondisease controls, a total of 6901 unique site-specific glycans on 807 glycosites of proteins were detected. Much more differences of glycoproteome were observed in breast diseases than the proteome. By employing machine learning, 15 site-specific glycans were determined as potential glyco-signatures in detecting breast cancer. The results demonstrate that our method provides a powerful tool in glycoproteomic studies.
ISSN:0003-2700
1520-6882
1520-6882
DOI:10.1021/acs.analchem.4c03069