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Integrated N-glycoproteomics Analysis of Human Saliva for Lung Cancer.

Journal of proteome research (2022-06-18)
Sha Liu, Huiyu Wang, Xiaoteng Jiang, Yin Ji, Zeyuan Wang, Yan Zhang, Peng Wang, Hua Xiao
RESUMEN

Aberrant protein N-glycosylation is a cancer hallmark, which has great potential for cancer detection. However, large-scale and in-depth analysis of N-glycosylation remains challenging because of its high heterogeneity, complexity, and low abundance. Human saliva is an attractive diagnostic body fluid, while few efforts explored its N-glycoproteome for lung cancer. Here, we utilized a zwitterionic-hydrophilic interaction chromatography-based strategy to specifically enrich salivary glycopeptides. Through quantitative proteomics analysis, 1492 and 1234 intact N-glycopeptides were confidently identified from pooled saliva samples of 10 subjects in the nonsmall-cell lung cancer group and 10 subjects in the normal control group. Accordingly, 575 and 404 N-glycosites were revealed for the lung cancer group and normal control group. In particular, 154 N-glycosites and 259 site-specific glycoforms were significantly dysregulated in the lung cancer group. Several N-glycosites located at the same glycoprotein and glycans attached to the same N-glycosites were observed with differential expressions, including haptoglobin, Mucin-5B, lactotransferrin, and α-1-acid glycoprotein 1. These N-glycoproteins were mainly related to inflammatory responses, infectious diseases, and cancers. Our study achieved comprehensive characterization of salivary N-glycoproteome, and dysregulated site-specific glycoforms hold promise for noninvasive detection of lung cancer.

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Millipore
Puntas de pipeta ZipTip®, C18 resin, bed volume 0.6 μL, tip volume 10 μL
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Millipore
ZipTip® Pipette Tips, C18 resin, micro, bed volume 0.2 μL, tip volume 10 μL
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