Faculty Profiles - SATO, Chihiro

Papers - SATO, Chihiro

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Occurrence of free deaminoneuraminic acid (KDN)-containing complex-type N-glycans in human prostate cancers

Yabu Masahiko, Korekane Hiroaki, Hatano Koji, Kaneda Yasufumi, Nonomura Norio, Sato Chihiro, Kitajima Ken, Miyamoto Yasuhide

GLYCOBIOLOGY Vol. 23 ( 6 ) page： 634 - 642 2013.6

Impact of structural aberrancy of polysialic acid and its synthetic enzyme ST8SIA2 in schizophrenia

Sato Chihiro, Kitajima Ken

FRONTIERS IN CELLULAR NEUROSCIENCE Vol. 7 ( APR ) page： 61 2013

Polysialic Acid

Sato Chihiro

SIALOBIOLOGY: BIOSYNTHESIS, STRUCTURE AND FUNCTION: SIALIC ACID GLYCOCONJUGATES IN HEALTH AND DISEASE page： 33 - 75 2013

ポリシアル酸による神経機能の調節. 実験医学 31巻 10号 (増刊) pp. 26-33; 第三の生命鎖 Reviewed

佐藤ちひろ

実験医学 Vol. 31 page： 26 - 33 2013

Sialome analysis of the cephalochordate Branchiostoma belcheri, a key organism for vertebrate evolution Open Access

Guerardel Yann, Chang Lan-Yi, Fujita Akiko, Coddeville Bernadette, Maes Emmanuel, Sato Chihiro, Harduin-Lepers Anne, Kubokawa Kaoru, Kitajima Ken

GLYCOBIOLOGY Vol. 22 ( 4 ) page： 479 - 491 2012.4

Structural and functional impairments of polysialic acid (polySia)-neural cell adhesion molecule (NCAM) synthesized by a mutated polysialyltransferase of a schizophrenic patient Open Access

Hane Masaya, Sumida Mizuki, Kitajima Ken, Sato Chihiro

PURE AND APPLIED CHEMISTRY Vol. 84 ( 9 ) page： 1895 - 1906 2012

Co-expression of two distinct polysialic acids, alpha 2,8-and alpha 2,9-linked polymers of N-acetylneuraminic acid, in distinct glycoproteins and glycolipids in sea urchin sperm

Miyata Shinji, Yamakawa Nao, Toriyama Masaru, Sato Chihiro, Kitajima Ken

GLYCOBIOLOGY Vol. 21 ( 12 ) page： 1596 - 605 2011.12

New Functions of Polysialic Acid and Its Relationship to Schizophrenia

Sato Chihiro, Kitajima Ken

Trends in Glycoscience and Glycotechnology Vol. 23 ( 133 ) page： 221 - 238 2011.9

Language：Japanese Publishing type：Research paper (scientific journal) Publisher：FCCA(Forum: Carbohydrates Coming of Age)

Polysialic acid (polySia), particularly α2,8-linked polyNeu5Ac (DP=8∼400), is a unique polymer that spatio-temporally modifies neural cell adhesion molecule (NCAM), predominantly in embryonic brains. PolySia is considered to function as a negative regulator of adhesion between cells, and between cells and extracellular matrix due to its extremely polyanionic nature and steric hindrance. Through its anti-adhesive property and spatio-temporal expression, polySia is involved in cell migration, neural outgrowth, axonal guidance, synaptic plasticity, and the development of normal neural circuits and neurogenesis. Due to improvements of polySia-detection methods, it has been shown that polySia expression persists in the hippocampus and olfactory bulb of adults, where neurogenesis is ongoing; however, the functions of polySia, particularly in adult brains, remain incompletely resolved. Recently, we demonstrated that polySia functions not only as an anti-adhesive molecule, but also as a reservoir for specific bioactive molecules, such as neurotrophic factors, neurotransmitters, and growth factors, which regulate neural function. In addition, studies have revealed that the enzymatic activity of STX, which is involved in the synthesis of polySia, derived from schizophrenic patient is low and that the product of the enzyme, polySia on NCAM is impaired with respect to both quantity and quality. Notably, impaired polySia-NCAM cannot effectively retain bioactive molecules, including BDNF, dopamine, and FGF2. Taken together, the impairment of polySia might influence the retention function of polySia and lead to the development of psychiatric disorders, such as schizophrenia, which are reported to express either lower or elevated amounts of polySia compared with normal brains.

DOI： 10.4052/tigg.23.221

Web of Science

Scopus

CiNii Research

Structural and Functional Impairments of Polysialic Acid by a Mutated Polysialyltransferase Found in Schizophrenia Open Access

Isomura Ryo, Kitajima Ken, Sato Chihiro

JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 286 ( 24 ) page： 21535 - 45 2011.6

IgG2 dominancy and carbohydrate recognition specificity of C3H/He mouse antibodies directed to cross-reactive carbohydrate determinants (CCDs) bearing beta-(1,2)-xylose and alpha-(1,3)-fucose

Hino Shingo, Umeda Fumiko, Inumaru Shigeki, Aoki Naohito, Sato Chihiro, Okajima Tetsuya, Nadano Daita, Matsuda Tsukasa

IMMUNOLOGY LETTERS Vol. 133 ( 1 ) page： 28 - 34 2010.9

Extensive enrichment of N-glycolylneuraminic acid in extracellular sialoglycoproteins abundantly synthesized and secreted by human cancer cells

Inoue Sadako, Sato Chihiro, Kitajima Ken

GLYCOBIOLOGY Vol. 20 ( 6 ) page： 752 - 62 2010.6

Glycans and schizophrenia

Vol. 61 ( 2 ) page： 160 - 166 2010.4

MEASUREMENT OF GLYCAN-BASED INTERACTIONS BY FRONTAL AFFINITY CHROMATOGRAPHY AND SURFACE PLASMON RESONANCE

Sato Chihiro, Yamakawa Nao, Kitajima Ken

METHODS IN ENZYMOLOGY, VOL 478: GLYCOMICS Vol. 478 ( C ) page： 219 - 32 2010

糖鎖と統合失調症

佐藤ちひろ

生体の科学 61 page： 160 - 166 2010

Complex Formation of a Brain-Derived Neurotrophic Factor and Glycosaminoglycans

KANATO Yukihiro, ONO Sayaka, KITAJIMA Ken, SATO Chihiro

Bioscience, Biotechnology, and Biochemistry Vol. 73 ( 12 ) page： 2735 - 41 2009.12

Language：English Publishing type：Research paper (scientific journal) Publisher：Japan Society for Bioscience, Biotechnology, and Agrochemistry

Glycosaminoglycans (GAGs), large anionic glycopolymers, are the glycan portion of proteoglycans and are important components of the extracellular matrix. Recently we reported that polysialic acid, a polyanionic glycopolymer specific to the brain, binds neurotrophic factors to form a large complex. It is not clear whether GAGs also bind neurotrophic factors to form a large complex. In the present study, we demonstrate that a brain-derived neurotrophic factor (BDNF) dimer directly binds GAGs other than chondroitin and hyaluronic acid to form a large complex. Neurotrophin-3 showed similar GAG binding properties. Furthermore, BDNF, after forming a large complex with GAG, bound to the BDNF receptors tropomyosin-related kinase (Trk) B and p75 neurotrophin receptor (NTR). These findings suggest that GAGs function to produce a reservoir of BDNF and other neurotrophic factors, and may serve to regulate their local concentrations on the cell surface.

DOI： 10.1271/bbb.90637

Developmental regulation of oligosialylation in zebrafish

Chang Lan-Yi, Harduin-Lepers Anne, Kitajima Ken, Sato Chihiro, Huang Chang-Jen, Khoo Kay-Hooi, Guerardel Yann

GLYCOCONJUGATE JOURNAL Vol. 26 ( 3 ) page： 247 - 261 2009.4