Premium
Identification and analysis of α1,6‐fucosylated proteins in human normal liver tissues by a target glycoproteomic approach
Author(s) -
Dai Zhi,
Fan Jia,
Liu Yinkun,
Zhou Jian,
Bai Dousheng,
Tan Changjun,
Guo Kun,
Zhang Yu,
Zhao Yan,
Yang Pengyuan
Publication year - 2007
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.200700233
Subject(s) - glycoprotein , fucosylation , lectin , glycan , biochemistry , glycoproteomics , fucose , glycosylation , biology , microbiology and biotechnology , chemistry
Abstract α1,6‐Fucose residues within the N ‐glycan core structures were commonly observed in many glycoproteins. Our previous studies showed that aberrantly α1,6‐fucosylated glycoproteins might be associated with metastasis of hepatocellular carcinoma (HCC). Little is known about human normal liver tissues (HNLTs) in the literatures. In this study, a target glycoproteomic approach which consists of lectin‐affinity chromatography, 2‐DE, protein immunoprecipitation and lectin blot, and MALDI‐MS/MS, was utilized to screen physiologically α1,6‐fucosylated glycoproteins. Lens culinaris agglutinin (LCA)‐affinity glycoprotein profiles of HNLT were established and analyzed, which allowed identification of 53 proteins by MS analysis, including haptoglobin precursor, α‐enolase, etc . Gene ontology (GO) annotation proved that these proteins distribute predominately in organelle and play crucial roles in binding and catalytic reactions. The present methodology enabled the identification of all the specific subsets of glycoprotein, and the corresponding data could contribute to the finding of more aberrantly α1,6‐fucosylated glycoproteins related to liver diseases.