Strategy for Glycoproteomics: Identification of Glyco-Alteration Using Multiple Glycan Profiling Tools†

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• 作者：Hiromi Ito^‡ ; ^# ; Atsushi Kuno^‡ ; ^# ; Hiromichi Sawaki^‡ ; ^# ; Maki Sogabe^‡ ; ; Hidenori Ozaki^‡ ; ; Y
• 刊名：Journal of Proteome Research
• 出版年：2009
• 出版时间：March 6, 2009
• 年：2009
• 卷：8
• 期：3
• 页码：1358-1367
• 全文大小：281K
• 年卷期：v.8,no.3(March 6, 2009)
• ISSN：1535-3907

文摘

Glycan alterations of proteins, a common feature of cancer cells, are associated with carcinogenesis, invasion and metastasis. Glycomics, the study of glycans and glycan-binding proteins in various biological systems, is an emerging field in the postgenome and postproteomics era. However, systematic and robust strategies for glycomics are still not fully established because the structural analysis of glycans, which comprise different patterns of branching, various possible linkage positions as well as monomer anomericity, is technically difficult. Here, we introduce a new strategy for glyco-alteration analysis of glycoproteins by using multiple glycan profiling tools. To understand glycan alterations of proteins by correlating the glycosyltransferase expression profile with the actual glycan structure, we systematically used three glycan profiling tools: (1) multiplex quantitative PCR (qPCR) array format for profiling the expression pattern of glycogenes, (2) lectin microarray as a multiplex glycan−lectin interaction analysis system for profiling either a pool of cell glycoproteins or a target glycoprotein, and (3) tandem mass spectrometry for identifying the glycan structure connected to a target glycoprotein. Using our system, we successfully identified glycan alterations on alpha-fetoprotein (AFP), including a novel LacdiNAc structure in addition to previously reported alterations such as α1,6 fucosylation.