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Analysis of Fucosylation in Liver-Secreted N-glycoproteins From Human Hepatocellular Carcinoma Plasma Using Liquid Chromatography With Tandem Mass Spectrometry

Eun Sun Ji, Heeyoun Hwang, Gun Wook Park, Ju Yeon Lee, Hyun Kyoung Lee, Na Young Choi, Hoi Keun Jeong, Kwang Hoe Kim, Jin Young Kim, Seungho Lee, Yeong Hee Ahn, Jong Shin Yoo

Anal Bioanal Chem. 2016 Nov;408(27):7761-7774.

PMID: 27565792

Abstract:

Fucosylation of N-glycoproteins has been implicated in various diseases, such as hepatocellular carcinoma (HCC). However, few studies have performed site-specific analysis of fucosylation in liver-secreted proteins. In this study, we characterized the fucosylation patterns of liver-secreted proteins in HCC plasma using a workflow to identify site-specific N-glycoproteins, where characteristic B- and/or Y-ion series with and without fucose in collision-induced dissociation were used in tandem mass spectrometry. In total, 71 fucosylated N-glycopeptides from 13 major liver-secreted proteins in human plasma were globally identified by LC-MS/MS. Additionally, 37 fucosylated N-glycopeptides were newly identified from nine liver-secreted proteins, including alpha-1-antichymotrypsin, alpha-1-antitrypsin, alpha-2-HS-glycoprotein, ceruloplasmin, alpha-1-acid glycoprotein 1/2, alpha-2-macroglobulin, serotransferrin, and beta-2-glycoprotein 1. Of the fucosylated N-glycopeptides, bi- and tri-antennary glycoforms were the most common ones identified in liver-secreted proteins from HCC plasma. Therefore, we suggest that this analytical method is effective for characterizing fucosylation in liver-secreted proteins. Graphical abstract A global map of fucosylated and non-fucosylated glycopeptides from 13 liver-secreted glycoproteins in hepatocellular carcinoma plasma.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
AP141176923 α1-Antichymotrypsin from human plasma α1-Antichymotrypsin from human plasma 141176-92-3 Price
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