Faculty Profiles - SATO, Chihiro

Papers - SATO, Chihiro

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Sato Chihiro, Gu Jianguo, Fukuda Tomohiko, Kadomatsu Kenji, Ikenaka Kazuhiro

GLYCOSCIENCE: BASIC SCIENCE TO APPLICATIONS: INSIGHTS FROM THE JAPAN CONSORTIUM FOR GLYCOBIOLOGY AND GLYCOTECHNOLOGY (JCGG) page： 209 - 219 2019

New Functions and Applications of an Acidic Glycan, Polysialic Acid: Repulsive and Attractive Fields of Polysialic Acid

SATO Chihiro

KAGAKU TO SEIBUTSU Vol. 56 ( 6 ) page： 422 - 431 2018.5

Polysialyltransferase ST8SIA2 and psychiatric disorders

Hane Masaya, Kitajima Ken, Sato Chihiro

Vol. 89 ( 5 ) page： 634 - 643 2017

ポリシアル酸転移酵素遺伝子ST8SIA2と精神疾患の関わり Reviewed

羽根正弥, 佐藤ちひろ

生化学 Vol. 89 page： 634 - 643 2017

Hsp70の酸性複合糖質結合活性の発見. 糖の意外な働き． Reviewed

佐藤ちひろ

化学と生物 Vol. 55, page： 22 - 26 2017

The Out of Africa and mental disorders: Adaptation with reduction in STX promoter activity

Fujito Naoko, Satta Yoko, Hane Masaya, Matsui Atsushi, Yashima Kenta, Kitajima Ken, Sato Chihiro, Takahata Naoyuki, Hayakawa Toshiyuki

GENES & GENETIC SYSTEMS Vol. 91 ( 6 ) page： 343 - 343 2016.12

A Uniquely Human Evolutionary Change in ST8Sia-II Impacts Enzyme Stability and Polysialic Acid Function

Vaill Michael, Hane Masaya, Naito-Matsui Yuko, Diaz Sandra, Davies Leela, Kitajima Ken, Sato Chihiro, Varki Ajit

GLYCOBIOLOGY Vol. 26 ( 12 ) page： 1423 - 1423 2016.12

Binding Activity of Hsp70 toward Acidic Glycoconjugates

HARADA Yoichiro, SATO Chihiro, KITAJIMA Ken

KAGAKU TO SEIBUTSU Vol. 55 ( 1 ) page： 22 - 26 2016

Spread of reduced activity of STX promoter throughout Great Journey

Fujito Naoko, Satta Yoko, Hane Masaya, Matsui Atsushi, Kitajima Ken, Sato Chihiro, Hayakawa Toshiyuki

GENES & GENETIC SYSTEMS Vol. 90 ( 6 ) page： 379 - 379 2015.12

Protective effects of polysialic acid on proteolytic cleavage of FGF2 and proBDNF/BDNF. Open Access

Hane M, Matsuoka S, Ono S, Miyata S, Kitajima K, Sato C

Glycobiology Vol. 25 ( 10 ) page： 1112 - 24 2015.10

Language：English Publishing type：Research paper (scientific journal) Publisher：Glycobiology

Polysialic acid (polySia) is a linear polymer of sialic acid that modifies neural cell adhesion molecule (NCAM) in the vertebrate brain. PolySia is a large and exclusive molecule that functions as a negative regulator of cell-cell interactions. Recently, we demonstrated that polySia can specifically bind fibroblast growth factor 2 (FGF2) and BDNF; however, the protective effects of polySia on the proteolytic cleavage of these proteins remain unknown, although heparin/heparan sulfate has been shown to impair the cleavage of FGF2 by trypsin. Here, we analyzed the protective effects of polySia on the proteolytic cleavage of FGF2 and proBDNF/BDNF. We found that polySia protected intact FGF2 from tryptic activity via the specific binding of extended polySia chains on NCAM to FGF2. Oligo/polySia also functioned to impair the processing of proBDNF by plasmin via binding of oligo/polySia chains on NCAM. In addition, the polySia structure synthesized by mutated polysialyltransferase, ST8SIA2/STX(SNP7), which was previously identified from a schizophrenia patient, was impaired for these functions compared with polySia produced by normal ST8SIA2. Taken together, these data suggest that the protective effects of polySia toward FGF2 and proBDNF may be involved in the regulation of the concentrations of these neurologically active molecules.

DOI： 10.1093/glycob/cwv049

Web of Science

Scopus

PubMed

Ganglioside contained in the neuronal tissue-enriched acidic protein of 22 kDa (NAP-22) fraction prepared from the detergent-resistant membrane microdomain of rat brain inhibits the phosphatase activity of calcineurin.

Kobayashi Y, da Silva R, Kumanogoh H, Miyata S, Sato C, Kitajima K, Nakamura S, Morita M, Hayashi F, Maekawa S

Journal of neuroscience research Vol. 93 ( 9 ) page： 1462 - 70 2015.9

Language：English Publishing type：Research paper (scientific journal) Publisher：Journal of Neuroscience Research

Neurons have well-developed membrane microdomains called "rafts" that are recovered as a detergent-resistant membrane microdomain fraction (DRM). Neuronal tissue-enriched acidic protein of 22 kDa (NAP-22) is one of the major protein components of neuronal DRM. To determine the cellular function of NAP-22, interacting proteins were screened with an immunoprecipitation assay, and calcineurin (CaN) was detected. Further studies with NAP-22 prepared from DRM and CaN expressed in bacteria showed the binding of these proteins and a dose-dependent inhibitory effect of the NAP-22 fraction on the phosphatase activity of CaN. On the other hand, NAP-22 expressed in bacteria showed low binding to CaN and a weak inhibitory effect on phosphatase activity. To solve this discrepancy, identification of a nonprotein component that modulates CaN activity in the DRM-derived NAP-22 fraction was attempted. After lyophilization, a lipid fraction was extracted with chloroform/methanol. The lipid fraction showed an inhibitory effect on CaN without NAP-22, and further fractionation of the extract with thin-layer chromatography showed the presence of several lipid bands having an inhibitory effect on CaN. The mobility of these bands coincided with that of authentic ganglioside (GM1a, GD1a, GD1b, and GT1b), and authentic ganglioside showed an inhibitory effect on CaN. Treatment of lipid with endoglycoceramidase, which degrades ganglioside to glycochain and ceramide, caused a diminution of the inhibitory effect. These results show that DRM-derived NAP-22 binds several lipids, including ganglioside, and that ganglioside inhibits the phosphatase activity of CaN.

DOI： 10.1002/jnr.23599

Rapid Trimming of Cell Surface Polysialic Acid (PolySia) by Exovesicular Sialidase Triggers Release of Preexisting Surface Neurotrophin. Open Access

Sumida M, Hane M, Yabe U, Shimoda Y, Pearce OM, Kiso M, Miyagi T, Sawada M, Varki A, Kitajima K, Sato C

The Journal of biological chemistry Vol. 290 ( 21 ) page： 13202 - 14 2015.5

Language：English Publishing type：Research paper (scientific journal) Publisher：Journal of Biological Chemistry

As acidic glycocalyx on primary mouse microglial cells and a mouse microglial cell line Ra2, expression of polysialic acid (polySia/PSA), a polymer of the sialic acid Neu5Ac (N-acetylneuraminic acid), was demonstrated. PolySia is known to modulate cell adhesion, migration, and localization of neurotrophins mainly on neural cells. PolySia on Ra2 cells disappeared very rapidly after an inflammatory stimulus. Results of knockdown and inhibitor studies indicated that rapid surface clearance of polySia was achieved by secretion of endogenous sialidase Neu1 as an exovesicular component. Neu1-mediated polySia turnover was accompanied by the release of brain-derived neurotrophic factor normally retained by polySia molecules. Introduction of a single oxygen atom change into polySia by exogenous feeding of the non-neural sialic acid Neu5Gc (N-glycolylneuraminic acid) caused resistance to Neu1-induced polySia turnover and also inhibited the associated release of brain-derived neurotrophic factor. These results indicate the importance of rapid turnover of the poly-Sia glycocalyx by exovesicular sialidases in neurotrophin regulation.

DOI： 10.1074/jbc.M115.638759

Web of Science

Scopus

PubMed

Sulfatide-Hsp70 interaction promotes Hsp70 clustering and stabilizes binding to unfolded protein. Open Access

Harada Y, Sato C, Kitajima K

Biomolecules Vol. 5 ( 2 ) page： 958 - 73 2015.5

Language：English Publishing type：Research paper (scientific journal) Publisher：Biomolecules

The 70-kDa heat shock protein (Hsp70), one of the major stress-inducible molecular chaperones, is localized not only in the cytosol, but also in extracellular milieu in mammals. Hsp70 interacts with various cell surface glycolipids including sulfatide (3'-sulfogalactosphingolipid). However, the molecular mechanism, as well as the biological relevance, underlying the glycolipid-Hsp70 interaction is unknown. Here we report that sulfatide promotes Hsp70 oligomerization through the N-terminal ATPase domain, which stabilizes the binding of Hsp70 to unfolded protein in vitro. We find that the Hsp70 oligomer has apparent molecular masses ranging from 440 kDa to greater than 669 kDa. The C-terminal peptide-binding domain is dispensable for the sulfatide-induced oligomer formation. The oligomer formation is impaired in the presence of ATP, while the Hsp70 oligomer, once formed, is unable to bind to ATP. These results suggest that sulfatide locks Hsp70 in a high-affinity state to unfolded proteins by clustering the peptide-binding domain and blocking the binding to ATP that induces the dissociation of Hsp70 from protein substrates.

DOI： 10.3390/biom5020958

Discovery, primary, and crystal structures and capacitation-related properties of a prostate-derived heparin-binding protein WGA16 from boar sperm.

Garénaux E, Kanagawa M, Tsuchiyama T, Hori K, Kanazawa T, Goshima A, Chiba M, Yasue H, Ikeda A, Yamaguchi Y, Sato C, Kitajima K

The Journal of biological chemistry Vol. 290 ( 9 ) page： 5484 - 501 2015.2

Language：English Publishing type：Research paper (scientific journal) Publisher：Journal of Biological Chemistry

Mammalian sperm acquire fertility through a functional maturation process called capacitation, where sperm membrane molecules are drastically remodeled. In this study, we found that a wheat germ agglutinin (WGA)-reactive protein on lipid rafts, named WGA16, is removed from the sperm surface on capacitation. WGA16 is a prostate-derived seminal plasma protein that has never been reported and is deposited on the sperm surface in themalereproductive tract. BasedonproteinandcDNAsequences for purified WGA16, it is a homologue of human zymogen granule protein16(ZG16) belonging to the Jacalin-related lectin (JRL) family in crystal and primary structures. A glycan array shows that WGA16 binds heparin through a basic patch containing Lys-53/ Lys-73 residues but not the conventional lectin domain of the JRL family. WGA16 is glycosylated, contrary to other ZG16 members, and comparative mass spectrometry clearly shows its unique N-glycosylation profile among seminal plasma proteins. It has exposed GlcNAc and GalNAc residues without additional Gal residues. The GlcNAc/GalNAc residues can work as binding ligands foraspermsurface galactosyltransferase,whichactually galactosylatesWGA16in situ in the presence of UDP-Gal. Interestingly, surface removal of WGA16 is experimentally induced by either UDPGal or heparin. In the crystal structure, N-glycosylated sites and a potential heparin-binding site face opposite sides. This geography of two functional sites suggest that WGA16 is deposited on the sperm surface through interaction between its N-glycans and the surface galactosyltransferase, whereas its heparin-binding domain may be involvedinbindingto sulfatedglycosaminoglycansinthefemaletract, enabling removal ofWGA16from the sperm surface.

DOI： 10.1074/jbc.M114.635268

Web of Science

Scopus

PubMed

Adaptive evolution of the promoter region of the Sialyltransferase 8B (STX) gene

Fujito Naoko T., Hayakawa Toshiyuki, Hane Masaya, Kitajima Ken, Sato Chihiro, Satta Yoko

GENES & GENETIC SYSTEMS Vol. 89 ( 6 ) page： 327 - 327 2014.12

An anti-schizophrenic drug affects the surface expression of polySia-NCAM in IMR-32 human neuroblastoma cells

Nishimura Saki, Hane Masaya, Niimi Yuki, Kitajima Ken, Sato Chihiro

GLYCOBIOLOGY Vol. 24 ( 11 ) page： 1193 - 1193 2014.11

Insight into single nucleotide polymorphisms (SNPs) of the polysialyltransferase ST8SIA2/STX in psychiatric disorders

Hane Masaya, Nishimura Saki, Hayakawa Toshiyuki, Kitajima Ken, Sato Chihiro

GLYCOBIOLOGY Vol. 24 ( 11 ) page： 1206 - 1206 2014.11

Polysialic acid: Biosynthesis, novel functions and applications

Colley Karen J., Kitajima Ken, Sato Chihiro

CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY Vol. 49 ( 6 ) page： 498 - 532 2014.11

The Synthesis of Sialo-containing Glycopolymers by pi-Allyl Nickel Catalyzed Coordination Polymerization

Ohira Shuichi, Yasuda Yu, Sato Chihiro, KItajima Ken, Tomita Ikuyoshi, Takahashi Takashi, Tanaka Hiroshi

GLYCOBIOLOGY Vol. 24 ( 11 ) page： 1119 - 1120 2014.11

Crystal Structure of Anti-polysialic Acid Antibody Single Chain Fv Fragment Complexed with Octasialic Acid INSIGHT INTO THE BINDING PREFERENCE FOR POLYSIALIC ACID

Nagae Masamichi, Ikeda Akemi, Hane Masaya, Hanashima Shinya, Kitajima Ken, Sato Chihiro, Yamaguchi Yoshiki

JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 288 ( 47 ) page： 33784 - 33796 2013.11

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Papers - SATO, Chihiro