NAKAKITA Shinichi

Faculty
Faculty of Medicine
School of Medicine
PositionAssociate Professor
Last Updated :2022/11/25

Researcher Profile and Settings

Education

  •   1994 04  - 1998 09 , Osaka University, Graduate School of Science

Degree

  • 博士(理学), 大阪大学

Association Memberships

  • THE JAPANESE SOCIETY OF CARBOHYDRATE RESEARCH

Academic & Professional Experience

  •  - 現在, Kagawa University

Research Activities

Research Areas

  • Life sciences / Functional biochemistry

Research Interests

    希少糖, ウイルス, 構造解析, 糖鎖

Published Papers

  • Preparation of a molecular library of branched β-glucan oligosaccharides derived from laminarin, Shunji Natsuka, Aki Tachibana, Wataru Sumiyoshi, Shin-ichi Nakakita, Noriko Suzuki, Journal of Applied Glycoscience, 65, (4) 45 - 49,   2018 , [Refereed]
  • [Review: Symposium on Amylases and Related Enzymes] Biosensor and Sugar Related Molecule, Miyanishi Nobumitsu, Nakakita Shin-ichi, Sumiyoshi Wataru, Hirabayashi Jun, Bulletin of Applied Glycoscience, 1, (2) 174 - 178,   2011 01 28
  • Carbohydrate-related eznymes and biosensors using enzyme complex system, Miyanishi Nobumitsu, Nakakita Shinichi, Sumiyoshi Wataru, Hirabayashi Jun, Journal of Applied Glycoscience Supplement, 2010,   2010
  • Characterization of novel endo-β-N-acetylglucosaminidase from Bacteroides nordii that hydrolyzes multi-branched complex type N-glycans., Kristina Mae Bienes, Feunai Agape Papalii Tautau, Ai Mitani, Takashi Kinoshita, Shin-Ichi Nakakita, Yujiro Higuchi, Kaoru Takegawa, Journal of bioscience and bioengineering, 134, (1) 7 - 13,   2022 07
  • Glycan detecting tools developed from the Clostridium botulinum whole hemagglutinin complex, Ea Kristine Clarisse Tulin, Chiaki Nakazawa, Tomomi Nakamura, Shion Saito, Naoki Ohzono, Keiko Hiemori, Shin-ichi Nakakita, Hiroaki Tateno, Takashi Tonozuka, Atsushi Nishikawa, SCIENTIFIC REPORTS, 11,   2021 11 , [Refereed]
  • Substrate specificities of α1,2- and α1,3-galactosyltransferases and characterization of Gmh1p and Otg1p in Schizosaccharomyces pombe., Takamasa Fukunaga, Naotaka Tanaka, Toshio Furumoto, Shinichi Nakakita, Takao Ohashi, Yujiro Higuchi, Hiromi Maekawa, Kaoru Takegawa, Glycobiology, 31, (8) 1037 - 1045,   2021 09 09 , [Refereed]
  • Structures of human galectin-10/monosaccharide complexes demonstrate potential of monosaccharides as effectors in forming Charcot-Leyden crystals., Aiko Itoh, Yasuhiro Nonaka, Shin-Ichi Nakakita, Hiromi Yoshida, Nozomu Nishi, Takanori Nakamura, Shigehiro Kamitori, Biochemical and biophysical research communications,   2020 02 17 , [Refereed]
  • N-glycan structures of human alveoli provide insight into influenza A virus infection and pathogenesis., Nongluk Sriwilaijaroen, Shin-Ichi Nakakita, Sachiko Kondo, Hirokazu Yagi, Koichi Kato, Takeomi Murata, Hiroaki Hiramatsu, Toshio Kawahara, Yohei Watanabe, Yasushi Kanai, Takao Ono, Jun Hirabayashi, Kazuhiko Matsumoto, Yasuo Suzuki, The FEBS journal, 285, (9) 1611 - 1634,   2018 05 , [Refereed]
  • Trisaccharide containing alpha 2,3-linked sialic acid is a receptor for mumps virus, Marie Kubota, Kaoru Takeuchi, Shumpei Watanabe, Shinji Ohno, Rei Matsuoka, Daisuke Kohda, Shin-ichi Nakakita, Hiroaki Hiramatsu, Yasuo Suzuki, Tetsuo Nakayama, Tohru Terada, Kentaro Shimizu, Nobutaka Shimizu, Mitsunori Shiroishi, Yusuke Yanagi, Takao Hashiguchi, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 113, (41) 11579 - 11584,   2016 10 , [Refereed]
  • Occurrence of free sialyl oligosaccharides related to N-glycans (sialyl free N-glycans) in animal sera, Junichi Seino, Haruhiko Fujihira, Shin-ichi Nakakita, Yuki Masahara-Negishi, Eiji Miyoshi, Jun Hirabayashi, Tadashi Suzuki, GLYCOBIOLOGY, 26, (10) 1072 - 1085,   2016 10 , [Refereed]
  • A rationally engineered yeast pyruvyltransferase Pvg1p introduces sialylation-like properties in neo-human-type complex oligosaccharide, Yujiro Higuchi, Sho Yoshinaga, Ken-ichi Yoritsune, Hiroaki Tateno, Jun Hirabayashi, Shin-ichi Nakakita, Miho Kanekiyo, Yoshimitsu Kakuta, Kaoru Takegawa, SCIENTIFIC REPORTS, 6,   2016 05 , [Refereed]
  • Transglycosylation Activity of Glycosynthase Mutants of Endo-beta-N-Acetylglucosaminidase from Coprinopsis cinerea, Yasunari Eshima, Yujiro Higuchi, Takashi Kinoshita, Shin-Ichi Nakakita, Kaoru Takegawa, PLOS ONE, 10,   2015 07 , [Refereed]
  • Engineering of a 3 '-sulpho-Gal beta 1-4GlcNAc-specific probe by a single amino acid substitution of a fungal galectin, Dan Hu, Hang Huang, Hiroaki Tateno, Shin-ichi Nakakita, Takashi Sato, Hisashi Narimatsu, Xinsheng Yao, Jun Hirabayashi, JOURNAL OF BIOCHEMISTRY, 157, (4) 197 - 200,   2015 04 , [Refereed]
  • Improved Method for Drawing of a Glycan Map, and the First Page of Glycan Atlas, Which Is a Compilation of Glycan Maps for a Whole Organism, Shunji Natsuka, Mayumi Masuda, Wataru Sumiyoshi, Shin-ichi Nakakita, PLOS ONE, 9,   2014 07 , [Refereed]
  • Carbohydrate recognition mechanism of HA70 from Clostridium botulinum deduced from X-ray structures in complexes with sialylated oligosaccharides, Satoshi Yamashita, Hiromi Yoshida, Noboru Uchiyama, Yukari Nakakita, Shin-Ichi Nakakita, Takashi Tonozuka, Keiji Oguma, Atsushi Nishikawa, Shigehiro Kamitori, FEBS Letters, 586, (16) 2404 - 2410,   2012 07 30
  • Bovine milk whey for preparation of natural n-glycans: Structural and quantitative analysis, Nongluk Sriwilaijaroen, Sachiko Kondo, Hirokazu Yagi, Hiroaki Hiramatsu, Shin-ichi Nakakita, Keita Yamada, Hiromi Ito, Jun Hirabayashi, Hisashi Narimatsu, Koichi Kato, Yasuo Suzuki, Open Glycoscience, 5, (1) 41 - 50,   2012 , [Refereed]
  • Structural analysis of alpha 1,3-linked galactose-containing oligosaccharides in Schizosaccharomyces pombe mutants harboring single and multiple alpha-galactosyltransferase genes disruptions, Takao Ohashi, Shin-ichi Nakakita, Wataru Sumiyoshi, Naotaka Yamada, Yuka Ikeda, Naotaka Tanaka, Kaoru Takegawa, GLYCOBIOLOGY, 21, (3) 340 - 351,   2011 03 , [Refereed]
  • X-ray structures of human galectin-9 C-terminal domain in complexes with a biantennary oligosaccharide and sialyllactose, Hiromi Yoshida, Misa Teraoka, Nozomu Nishi, Shin-Ichi Nakakita, Takanori Nakamura, Mitsuomi Hirashima, Shigehiro Kamitori, Journal of Biological Chemistry, 285, (47) 36969 - 36976,   2010 11 19 , [Refereed]
  • Production of heterologous glycoproteins by a glycosylation-defective alg3och1 mutant of Schizosaccharomyces pombe, Takao Ohashi, Shin-ichi Nakakita, Wataru Sumiyoshi, Kaoru Takegawa, JOURNAL OF BIOTECHNOLOGY, 150, (3) 348 - 356,   2010 11 , [Refereed]
  • Crystallization and preliminary X-ray diffraction analysis of a protease-resistant mutant form of human galectin-8, Hiromi Yoshida, Nozomu Nishi, Shin-Ichi Nakakita, Shigehiro Kamitori, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 65, (5) 512 - 514,   2009 , [Refereed]
  • The och1 mutant of schizosaccharomyces pombe produces galactosylated core structures of n-linked oligosaccharides, Takao Ohashi, Yuka Ikeda, Naotaka Tanaka, Shin-Ichi Nakakita, Shunji Natsuka, Yuko Giga-Hama, Kaoru Takegawa, Bioscience, Biotechnology and Biochemistry, 73, (2) 407 - 414,   2009 , [Refereed]
  • Development of an amperometric flow analysis sensor for specific detection of D-psicose, Nobumitsu Miyanishi, Naruhide Sato, Shin-Ichi Nakakita, Wataru Sumiyoshi, Kenji Morimoto, Hirokazu Okuma, Masaaki Tokuda, Ken Lzumori, Etsuo Watanabe, Jun Hirabayashi, BIOSENSORS & BIOELECTRONICS, 23, (9) 1347 - 1352,   2008 04 , [Refereed]
  • A practical approach to N-glycan production by hydrazinolysis using hydrazine monohydrate, Shin-ichi Nakakita, Wataru Sumiyoshi, Nobumitsu Miyanishi, Jun Hirabayashi, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 362, (3) 639 - 645,   2007 10 , [Refereed]
  • Free oligosaccharides with lewis x structure expressed in the segmentation period of zebrafish embryo, Kaznnobu Moriguchi, Tatsuya Takemoto, Takafuini Aoki, Shin-Ichi Nakakita, Shunji Natsuka, Sumihiro Hase, Journal of Biochemistry, 142, (2) 213 - 227,   2007 08 , [Refereed]
  • Structure determination of a sulfated N-glycans, candidate for a precursor of the selectin ligand in bovine lung, Tomonori Murakami, Shunji Natsuka, Shin-Ichi Nakakita, Sumihiro Hase, Glycoconjugate Journal, 24, (4-5) 195 - 206,   2007 07 , [Refereed]
  • Gas-phase pyridylamination of saccharides: development and applications., Shin-ichi Nakakita, Wataru Sumiyoshi, Nobumitsu Miyanishi, Shunji Natsuka, Sumihiro Hase, Jun Hirabayashi, Analytical chemistry, 79, (7) 2674 - 9,   2007 04 01 , [Refereed]
  • Developmental changes in the expression of glycogenes and the content of N-glycans in the mouse cerebral cortex, Akihiro Ishii, Takeshi Ikeda, Seiji Hitoshi, Ichiro Fujimoto, Tomohiro Torii, Keiichiro Sakuma, Shin-ichi Nakakita, Sumihiro Hase, Kazuhiro Ikenaka, GLYCOBIOLOGY, 17, (3) 261 - 276,   2007 03 , [Refereed]
  • Alteration of brain type N-glycans in neurological mutant mouse brain, Shin-Ichi Nakakita, Shunji Natsuka, Jun Okamoto, Kazuhiro Ikenaka, Sumihiro Hase, Journal of Biochemistry, 138, (3) 277 - 283,   2005 09 , [Refereed]
  • Xenopus galectin-VIIa binds N-glycans of members of the cortical granule lectin family (xCGL and xCGL2), Hiroki Shoji, Kazuhiro Ikenaka, Shin-Ichi Nakakita, Koh Hayama, Jun Hirabayashi, Yoichiro Arata, Ken-Ichi Kasai, Nozomu Nishi, Takanori Nakamura, Glycobiology, 15, (7) 709 - 720,   2005 07 , [Refereed]
  • Changes in N-linked sugar chain patterns induced by moderate-to-high expression of the galactosyltransferase I gene in a brain-derived cell line, CG4, KN Menon, T Ikeda, Fujimoto, I, H Narimatsu, S Nakakita, S Hase, K Ikenaka, JOURNAL OF NEUROSCIENCE RESEARCH, 80, (1) 29 - 36,   2005 04 , [Refereed]
  • Expression of complex-type N-glycans in developmental periods of zebrafish embryo, Tatsuya Takemoto, Shunji Natsuka, Shin-Ichi Nakakita, Sumihiro Hase, Glycoconjugate Journal, 22, (1-2) 21 - 26,   2005 02 , [Refereed]
  • Conversion of pyridylamino sugar chains to corresponding reducing sugar chains, C Takahashi, S Nakakita, S Hase, JOURNAL OF BIOCHEMISTRY, 134, (1) 51 - 55,   2003 07 , [Refereed]
  • Analysis of oligosaccharide structures of glycoproteins in polyacrylamide gel, Shin-ichi Nakakita, Daisuke Ama, Shunji Natsuka, Sumihiro Hase, Analytical Biochemistry, 303, (2) 206 - 209,   2002 04 15 , [Refereed]
  • Structural analysis of N-linked glycans in Caenorhabditis elegans, Shunji Natsuka, Jiro Adachi, Masahumi Kawaguchi, Shin-Ichi Nakakita, Sumihiro Hase, Akira Ichikawa, Koji Ikura, Journal of Biochemistry, 131, (6) 807 - 813,   2002 , [Refereed]
  • Detection of tissue-specific sugar chains by two-dimensional HPLC sugar mapping of pyridylaminated sugar chains, S Nakakita, K Ikenaka, S Hase, NEW DEVELOPMENTS IN GLYCOMEDICINE, 1223,   2001 , [Refereed]
  • beta 1-4Galactosyltransferase activity of mouse brain as revealed by analysis of brain-specific complex-type N-linked sugar chains, S Nakakita, KK Menon, S Natsuka, K Ikenaka, S Hase, JOURNAL OF BIOCHEMISTRY, 126, (6) 1161 - 1169,   1999 12 , [Refereed]
  • Systematic analysis of N-linked sugar chains from whole tissue employing partial automation, Ichiro Fujimoto, Krishna K. Menon, Yosuke Otake, Fumihiro Tanaka, Hiromi Wada, Hitoshi Takahashi, Shoji Tsuji, Shunji Natsuka, Shin-Ichi Nakakita, Sumihiro Hase, Kazuhiro Ikenaka, Analytical Biochemistry, 267, (2) 336 - 343,   1999 02 15 , [Refereed]
  • Development-dependent expression of complex-type sugar chains specific to mouse brain, S Nakakita, S Natsuka, K Ikenaka, S Hase, JOURNAL OF BIOCHEMISTRY, 123, (6) 1164 - 1168,   1998 06 , [Refereed]

Misc

  • Detection of Glycan Binding Activity of Influenza Virus, 中北愼一, 中北ゆかり, 鈴木康夫, 河原敏男, 平松宏明, 渡邊洋平, 小野尭生, 金井康, 松本和彦, 平林淳, 日本糖質学会年会要旨集, 39th,   2020
  • ガレクチン10・単糖複合体のX線結晶構造解析, 野中康宏, 伊藤愛子, 吉田裕美, 中北愼一, 中村隆範, 西望, 神鳥成弘, 日本生化学会大会(Web), 92nd,   2019
  • An alternative strategy for structural glucanomics using β-gluco-oligosaccharides from the brown algae Ecklonia stolonifera as models, Wataru Sumiyoshi, Nobumitsu Miyanishi, Shin-Ichi Nakakita, Shoko Tsutsui, Keita Yamada, Yukari Nakakita, Shin Yoshioka, Masakatsu Asao, Jun Hirabayashi, Bioactive Carbohydrates and Dietary Fibre, 5, (2), 137 - 145,   2015 04 01 , [Refereed]
    Studies of β-glucans are often hampered by their structural diversity and complexity, which is problematic because interest in their effects on animal cells has increased in recent years. Herein, we present a comprehensive strategy for structural characterization of branched β-glucans, and as a proof-of-concept study, characterized laminarin and acid-soluble β-gluco-oligosaccharides (< 4000 Da, void volume elute fraction of gel filtration on Bio-gel P-2) from the brown algae, Ecklonia stolonifera. The strategy involves quantitative fluorescence detection-high performance liquid chromatography that enables the characterization of di- and oligosaccharides after acid hydrolysis of the glucan. We found that laminarin is composed of β1-3 (72% in mol) and β1-6 (28%) anomeric bonds, whereas the E. stolonifera glucan is composed of β1-3 (57%) and β1-6 (43%) anomeric bonds. This composition is distinct from that of other brown algae β-glucans, for which the β1-6 bond content is much smaller. We also performed a detailed structural analysis of the 11 major β-gluco-oligosaccharides prepared by mild acid hydrolysis and β1-3-specific laminarinase digestion. All 11 oligosaccharides contained branches joined to the backbone by β1-6 bonds. Five of the oligosaccharides had extended branches in this regard, the E. stolonifera glucan is unlike other characterized β-glucans. Our strategy should enable structural characterizations of β-branched glucans, for which no practical approach has been available until now.
  • Catch a Glimpse of Life by Using the Biosensor for the Sugar Detection, 88, (5), 173 - 179,   2014 05
  • ヒトガレクチン9変異体のX線構造と糖鎖親和性の解析, 寺岡美沙, 吉田裕美, 西望, 中北愼一, 神鳥成弘, 日本生化学会大会(Web), 86th,   2013
  • プロテアーゼ耐性型ヒト由来ガレクチン8/シアリルラクトース/ラクトース複合体のX線結晶解析によるドメイン間の基質親和性の検討, 吉田裕美, 西望, 寺岡美沙, 山下哲, 中北愼一, 神鳥成弘, 日本蛋白質科学会年会プログラム・要旨集, 11th,   2011
  • ヒト由来ガレクチン9のC末端糖鎖認識ドメイン・シアリルラクトース複合体およびプロテアーゼ耐性型ヒト由来ガレクチン8のX線結晶解析, 吉田裕美, 西望, 寺岡美沙, 中北愼一, 中村隆範, 平島光臣, 神鳥成弘, 日本蛋白質科学会年会プログラム・要旨集, 10th,   2010
  • X線構造に基づくガレクチン9のシアル化糖鎖認識機構の解明, 吉田裕美, 吉田裕美, 寺岡美沙, 西望, 西望, 中北愼一, 中北愼一, 中村隆範, 平島光臣, 神鳥成弘, 神鳥成弘, 日本結晶学会年会講演要旨集, 2010,   2010
  • Precise recognition of "brain-type"β1-4galactosyltransferase, NAKAKITA Shin-ichi, NATSUKA Shunji, IKENAKA Kazuhiro, HASE Sumihiro, Japanese journal of electrophoresis, 48, (1), 1 - 4,   2004 03 15
  • Characterization of N- and O-linked galactosylated oligosaccharides from fission yeast species., Takamasa Fukunaga, Naotaka Tanaka, Toshio Furumoto, Shinichi Nakakita, Takao Ohashi, Yujiro Higuchi, Hiromi Maekawa, Kaoru Takegawa, Journal of bioscience and bioengineering, 130, (2), 128 - 136,   2020 08
    The N- and O-linked oligosaccharides from fission yeast Schizosaccharomyces pombe not only contain large amounts of d-mannose (Man) but also contain large amounts of d-galactose (Gal). Although the galactomannans of S. pombe are mainly composed of α1,2- or α1,3-linked Gals, some of the terminal α1,2-linked Gals are found to be linked to pyruvylated β1,3-linked galactose (PvGal). We have determined the structural characteristics of the N-glycans and O-glycans in three Schizosaccharomyces species (S. japonicus, S. octosporus, and S. cryophilus) using lectin blot, 1H NMR spectroscopy, and size-fractionation high performance liquid chromatography (HPLC), and found that the galactosylation of oligosaccharides was a common feature in fission yeasts. In addition, each of the terminal Galα1,2-, Galβ1,3- and non-substituted Man residues exhibited distinct characteristics. A BLAST search of gene databases in Schizosaccharomyces identified genes homologous to pvg1 encoding pyruvyltransferase of S. pombe. These genes, when expressed in an S. pombe pvg1Δ strains, led to the pyruvylation of non-reducing terminal β-linked Gal, suggesting the biosynthetic pathway of PvGal-containing oligosaccharides is highly conserved in fission yeasts.
  • Antigenic and Receptor Binding Properties of Enterovirus 68, Tadatsugu Imamura, Michiko Okamoto, Shin-ichi Nakakita, Akira Suzuki, Mariko Saito, Raita Tamaki, Socorro Lupisan, Chandra Nath Roy, Hiroaki Hiramatsu, Kan-etsu Sugawara, Katsumi Mizuta, Yoko Matsuzaki, Yasuo Suzuki, Hitoshi Oshitani, JOURNAL OF VIROLOGY, 88, (5), 2374 - 2384,   2014 03 , [Refereed]
    Increased detection of enterovirus 68 (EV68) among patients with acute respiratory infections has been reported from different parts of the world in the late 2000s since its first detection in pediatric patients with lower-respiratory-tract infections in 1962. However, the underlying molecular mechanisms for this trend are still unknown. We therefore aimed to study the antigenicity and receptor binding properties of EV68 detected in recent years in comparison to the prototype strain of EV68, the Fermon strain. We first performed neutralization (NT) and hemagglutination inhibition (HI) tests using antisera generated for EV68 strains detected in recent years. We found that the Fermon strain had lower HI and NT titers than recently detected EV68 strains. The HI and NT titers were also significantly different between strains of different genetic lineages among recently detected EV68 strains. We further studied receptor binding specificities of EV68 strains for sialyloligosaccharides using glycan array analysis. In glycan array analysis, all tested EV68 strains showed affinity for alpha 2-6-linked sialic acids (alpha 2-6 SAs) compared to alpha 2-3 SAs. Our study demonstrates that emergence of strains with different antigenicity is the possible reason for the increased detection of EV68 in recent years. Additionally, we found that EV68 preferably binds to alpha 2-6 SAs, which suggests that EV68 might have affinity for the upper respiratory tract. IMPORTANCE Numbers of cases of enterovirus 68 (EV68) infection in different parts of the world increased significantly in the late 2000s. We studied the antigenicity and receptor binding properties of recently detected EV68 strains in comparison to the prototype strain of EV68, Fermon. The hemagglutination inhibition (HI) and neutralization (NT) titers were significantly different between strains of different genetic lineages among recently detected EV68 strains. We further studied receptor binding specificities of EV68 strains for sialyloligosaccharides using glycan array analysis, which showed affinity for alpha 2-6-linked sialic acids (alpha 2-6 SAs) compared to alpha 2-3 SAs. Our study suggested that the emergence of strains with different antigenicities was the possible reason for the increased detections of EV68 in recent years. Additionally, we revealed that EV68 preferably binds to alpha 2-6 SAs. This is the first report describing the properties of EV68 receptor binding to the specific types of sialic acids.
  • Self-association of the galectin-9 C-terminal domain via the opposite surface of the sugar-binding site, Yasuhiro Nonaka, Takashi Ogawa, Souichi Oomizu, Shin-ichi Nakakita, Nozomu Nishi, Shigehiro Kamitori, Mitsuomi Hirashima, Takanori Nakamura, JOURNAL OF BIOCHEMISTRY, 153, (5), 463 - 471,   2013 05 , [Refereed]
    Galectin-9 is a lectin, which has various biological functions such as T-cell differentiation and apoptosis. Multivalency of carbohydrate binding is required for galectin-9 to function. Although galectin-1 (a proto-type galectin) forms an oligomer to obtain its multivalency, galectin-9 (a tandem-repeat-type one) has two carbohydrate recognition domains (CRD) in one polypeptide. However, a single CRD of galectin-9, especially the C-terminal one, exhibited pro-apoptotic activity suggesting oligomer formation capability. In this study, we monitored the nuclear magnetic resonance (NMR) signals of the backbone atoms of the galectin-9 C-terminal CRD (G9CCRD). Protein concentration dependence of the signals suggested that a region (F1-F4 strands) opposite to the ligand-binding site was involved in the self-association of G9CCRD. Site-directed mutagenesis in this region (Leu210, Trp277 and Leu279 to Thr; G9CCRD-3T) inhibited the self-association of G9CCRD, and improved the solubility, whereas it reduced its pro-apoptotic activity towards T cells. The high pro-apoptotic activity of G9CCRD seems to be due to the ability to form an oligomer. In addition, the same substitution in two-CRD-containing galectin-9 (G9Null-3T) also diminished the self-association and improved its solubility, although it hardly reduced the anti-proliferative and pro-apoptotic activities. G9CCRD contributes the self-association of full-length galectin-9 at high protein concentrations.
  • Development of a chemical strategy to produce rare aldohexoses from ketohexoses using 2-aminopyridine, Kayo Hasehira, Nobumitsu Miyanishi, Wataru Sumiyoshi, Jun Hirabayashi, Shin-ichi Nakakita, CARBOHYDRATE RESEARCH, 346, (17), 2693 - 2698,   2011 12 , [Refereed]
    Rare sugars are monosaccharides that are found in relatively low abundance in nature. Herein, we describe a strategy for producing rare aldohexoses from ketohexoses using the classical Lobry de Bruyn-Alberda van Ekenstein transformation. Upon Schiff-base formation of keto sugars, a fluorescence-labeling reagent, 2-aminopyridine (2-AP), was used. While acting as a base catalyst, 2-AP efficiently promoted the ketose-to-aldose transformation, and acting as a Schiff-base reagent, it effectively froze the ketose-aldose equilibrium. We could also separate a mixture of Sor, Gul, and Ido in their Schiff-base forms using a normal-phase HPLC separation system. Although Gul and Ido represent the most unstable aldohexoses, our method provides a practical way to rapidly obtain these rare aldohexoses as needed. (C) 2011 Elsevier Ltd. All rights reserved.
  • Structural analysis of N-glycans of the planarian Dugesia japonica, Shunji Natsuka, Yukiko Hirohata, Shin-ichi Nakakita, Wataru Sumiyoshi, Sumihiro Hase, FEBS JOURNAL, 278, (3), 452 - 460,   2011 02 , [Refereed]
    To investigate the relationship between phylogeny and glycan structures, we analyzed the structure of planarian N-glycans. The planarian Dugesia japonica, a member of the flatworm family, is a lower metazoan. N-glycans were prepared from whole worms by hydrazinolysis, followed by tagging with the fluorophore 2-aminopyridine at their reducing end. The labeled N-glycans were purified, and separated by three HPLC steps. By comparison with standard pyridylaminated N-glycans, it was shown that the N-glycans of planarian include high mannose-type and pauci-mannose-type glycans. However, many of the major N-glycans from planarians have novel structures, as their elution positions did not match those of the standard glycans. The results of mass spectrometry and sugar component analyses indicated that these glycans include methyl mannoses, and that the most probable linkage was 3-O-methylation. Furthermore, the methyl residues on the most abundant glycan may be attached to the non-reducing-end mannose, as the glycans were resistant to alpha-mannosidase digestion. These results indicate that methylated high-mannose-type glycans are the most abundant structure in planarians.
  • Carbohydrate-recognition domains of galectin-9 are involved in intermolecular interaction with galectin-9 itself and other members of the galectin family., Nobumitsu Miyanishi, Nozomu Nishi, Hiroko Abe, Yumiko Kashio, Rika Shinonaga, Shin-ichi Nakakita, Wataru Sumiyoshi, Akira Yamauchi, Takanori Nakamura, Mitsuomi Hirashima, Jun Hirabayashi, Glycobiology, 17, (4), 423 - 32,   2007 04
    Galectin-9 (Gal-9) is a tandem-repeat-type member of the galectin family associated with diverse biological processes, such as apoptosis, cell aggregation, and eosinophil chemoattraction. Although the detailed sugar-binding specificity of Gal-9 has been elucidated, molecular mechanisms that underlie these functions remain to be investigated. During the course of our binding study by affinity chromatography and surface plasmon resonance (SPR) analysis, we found that human Gal-9 interacts with immobilized Gal-9 in the protein-protein interaction mode. Interestingly, this intermolecular interaction strongly depended on the activity of the carbohydrate recognition domain (CRD), because the addition of potent saccharide inhibitors abolished the binding. The presence of multimers was also confirmed by Ferguson plot analysis of result of polyacrylamide gel electrophoresis and matrix-assisted laser-desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry (MS). Moreover, this intermolecular interaction was observed between Gal-9 and other galectin members, such as Gal-3 and Gal-8, but not Gal-1. Because such properties have not been reported yet, they may explain an unidentified mechanism underlying the diverse functions of Gal-9.

Conference Activities & Talks

  • Characterization of N-glycans of candidate-target glycoprotein of Xenopus galectin, 第77回日本生化学会大会,   2004

Research Grants & Projects

  • 糖鎖構造解析


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