Journal
JOURNAL OF PROTEOME RESEARCH
Volume 13, Issue 5, Pages 2328-2338Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr4011519
Keywords
N-linked glycopeptides; vitronectin; HCC; quantification; TMT; haptoglobin
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Funding
- Converging Research Center Program through the Ministry of Science, ICT and Future Planning, Korea [2013K000426]
- National R&D Program for Cancer Control [1120200]
- Ministry of Health and Welfare
- World Class University (WCU) grant [R31-2008-000-10086-0]
- Korea Health Promotion Institute [1120200] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Aberrant structures of site-specific N-linked glycans are closely associated with the tumorigenesis of hepatocellular carcinoma (HCC), one of the most common fatal cancers worldwide. Vitronectin (VTN) is considered a candidate glycobiomarker of HCC. In this study, we describe a reliable and simple quantification strategy based on abundance ratios of site-specific N-linked glycopeptides of VTN to screen for potential biomarkers. A total of 14 unique N-linked glycans corresponding to 27 unique N-linked glycopeptides were characterized at three N-linked sites (Asn-86, -169, and -242) present in VTN. These glycans could be good candidate markers for HCC. Among these glycans, the abundance ratio of two representative glycoforms (fucosyl vs non-fucosyl) was significantly increased in HCC plasma relative to normal plasma. This strategy was also successfully applied to another potential HCC biomarker, haptoglobin. Furthermore, we demonstrate that our approach employing tandem mass tag (TMT) and target N-linked glycopeptides of VTN is a useful tool for quantifying specific glycans in HCC plasma relative to normal plasma. Our strategy represents a simple and potentially useful screening platform for the discovery of cancer-specific glycobiomarkers
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