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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.
Overview of JCGGDB including New Released GlycoProtDB
Toshihide Shikanai,Hiroyuki Kaji,Yoshinori Suzuki,Noriaki Fujita,Masako Maeda,HonglingWen,Madoka Ishizaki,Hiromichi Sawaki,Hisashi Narimatsu. 한국당과학회 2012 한국당과학회 학술대회 Vol.2012 No.1
The JST/NBDC integrated database project has kicked off last year. JCGGDB was selected as a promotion program of DB integration, aiming to integrate all the glycan-related databases in Japan and build user- friendly search systems. As part of the project, the construction of ACGG-DB (an integrated database for the ACGG: Asian Communications for Glycobiology and Glycotechnology) is also planned in cooperation with Asian countries. As of now we have consolidated data from various Japanese institutes into JCGGDB and developed a cross-search function by keyword entry and integrated search functions by glycan stcurctures. These functions enabled users to easily access various glycan-related databases with a single search. Cheminformatics technologies using chemical structural formula for glycan has been also adopted to provide a search for glycan structures, glycan synthetic products by organic chemistry and recombinant enzymes, glycogene inhibitors, glycosides, and commercial glycans. This Summer, we have released AIST GlycoProtDB, which stores the data of experimentally-proven glycosylation sites on each mouse tissue. We are continuously accumulating experimental results of glycosylation sites, while collecting more information from scientific journals, toward the release of ACGG Glycoprotein Database in autumn. For the future, we will keep developing base technologies for DB integration and linking with databases related to glycoscience as well as other study areas. Some more bioinformatics tools are also being developed to support experimental study. Our aim is to create contents which could be easily and intuitively understood by every user.
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.
Spectral type and geometric albedo of (98943) 2001 CC21, the Hayabusa2# mission target
Jooyeon Geem,Masateru Ishiguro,Mikae,Granvik,Hiroyuki Naito,Hiroshi Akitaya,Tomohiko Sekiguchi,Sunao Hasegawa,Daisuke Kuroda,Tatsuharu Oono,Yoonsoo P. Bach,Sunho Jin,Rio Imazawa,Kaji S. Kawabata,Seiko 한국천문학회 2023 天文學會報 Vol.48 No.2
Identification of glyco-biomarker candidates for lung cancer using novel glyco-technologies
Yoshitoshi Hirao,Hideki Matsuzaki,Jun Iwaki,Minako Abe,Akira Togayachi,Atsushi Kuno,Takashi Ohkura,Hiroyuki Kaji,Masaharu Nomura,Masayuki Noguchi,Yuzuru Ikehara,Hisashi Narimatsu 한국당과학회 2012 한국당과학회 학술대회 Vol.2012 No.1
Lung cancer is the leading cause of cancer death worldwide. Currently, lung cancer is classified into two major types, small-cell lung cancer carcinoma (SCLC) and non-small-cell lung carcinoma (NSCLC), based on the histological appearance. The histological classification has important implications in the clinical practice guideline and the prediction of the patient prognosis. However, conventional serum markers used in clinical tests are insufficient for clinical demands due to the low sensitivity and the low specificity to distinguish them. We have identified a number of glyco-biomarker candidate molecules from lung cancer cell lines using our developed glycoproteomics technologies such as lectin microarray and LC/MS-based protein analysis. On the validation studies, we found out that the selected molecules showed characteristic lectin biding profiles depending on either SCLC or NSCLC. Therefore, combination of these glyco-biomarkers could be expected to improve the diagnostic accuracy for histological classification in lung cancer compared to protein expression alone.