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Ta-Wei Liu,Hiroyuki Kaji,Akira Togayachi,Hiromi Ito,Kiyohiko Angata,Takashi Sato,Hisashi Narimatsu 한국당과학회 2012 한국당과학회 학술대회 Vol.2012 No.1
Fucose-containing glycoconjugates play important roles in numerous physiological and pathological processes. Given the biological importance of posttranslational glycosylation, a specific and robust strategy for the identification of fucosylated glycoproteins is highly desirable. In this study, we demonstrate an alternative way of labeling of fucosylated structures by metabolic engineering, using a chemoenzymatic approach. In this approach, the activities of Bacteroides fragilis 9343 L-fucokinase/GDP-fucose pyrophosphorylase and human α1,3-fucosyltransferase 9 are combined in a Namalwa cellular model. Interestingly, this system could be applied to labeling of alkyne-modified fucosylated glycoproteins. N-glycan site mapping and identification was done using an in vitro selective chemical ligation reaction and isotope-coded glycosylation site-specific tagging, subsequent to liquid chromatography-tandem mass spectrometry analysis. This work illustrates the use of a click chemistry-based strategy combined with a glycoproteomic technique to get further insight into the pattern of fucose-mediated biological processes and functions.
Hiroyuki Kaji,Akira Togayachi,Makoto Ochou,Maki Sogabe,Takashi Okura,Hirofumi Nozaki,Takashi Angata,Yasunori Chiba,Hidenori Ozaki,Atsushi Kuno,Yasuhito Tanaka,Yuzuru Ikehara,Masashi Mizokami,Hisashi N 한국당과학회 2012 한국당과학회 학술대회 Vol.2012 No.1
We present here a high-throughput strategy to discover serological biomarkers for early-detection of hepatocellular carcinoma (HCC). Our strategy is also applicable to assess the progressed liver fibrosis that is associated with virus hepatitis. The glycan structure on glycoproteins derived from cancerous cells is known to be different from that derived from normal cells, specifically, the increased aberrant glycosylation appears in patient serum with virus hepatitis along with either or both the initiation and progression. Based on the above perceptions, in order to identify glycoproteins carrying aberrant glycosylation in serum of liver disease patients, we analyzed lectin-captured glycopeptides by the IGOT method. Many glycoproteins carrying altered glycans were successfully identified. The increased amount of these glycoproteins was clinically relevant to the progression of the liver diseases. We are now selecting appropriate molecules depending on the feasibility to detect an abnormality in the liver, such as the occurrence of liver cell neoplasm.