研究者詳細 - 佐藤　ちひろ

論文 - 佐藤　ちひろ

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A MAJOR GANGLIOSIDE FROM HEMICENTROTUS PULCHERRIMUS SPERM SPECIFICALLY INTERACTS WITH PHOSPHOLIPIDS(Developmental Biology,Abstracts of papers presented at the 75^<th> Annual Meeting of the Zoological Society of Japan) :

YamakawaNao, SatoChihiro, KitajimaKen

Zoological science 21 巻 ( 12 ) 頁： 1292 2004年12月

CELL GROWTH STIMULATING ACTIVITY OF THE PEPTIDES DERIVED FROM CORTICAL ALVEOLUS GLYCOPROTEINS OF FISH EGG (HYOSOPHORIN)(Developmental Biology,Abstracts of papers presented at the 75^<th> Annual Meeting of the Zoological Society of Japan) :

MaedaEri, SatoChihiro, KitajimaKen

Zoological science 21 巻 ( 12 ) 頁： 1292 2004年12月

THE 130 KDA GLYCOPROTEIN IS SECRETED FROM SPERM DURING ACROSOME REACTION OF SEA URCHIN, HEMICENTROTUS PULCHERRIMUS(Developmental Biology,Abstracts of papers presented at the 75^<th> Annual Meeting of the Zoological Society of Japan) :

MiyataShinji, SatoChihiro, ToriyamaMasaru, HirohashiNoritaka, VacquierVictor, KitajimaKen

Zoological science 21 巻 ( 12 ) 頁： 1292 2004年12月

A major ganglioside from Hemicentrotus pulcherrimus sperm specifically interacts with phospholipids

Yamakawa Nao, Sato Chihiro, Kitajima Ken

ZOOLOGICAL SCIENCE 21 巻 ( 12 ) 頁： 1292 - 1292 2004年12月

The 130 kDa glycoprotein is secreted from sperm during acrosome reaction of sea urchin, Hemicentrotus pulcherrimus

Miyata Shinji, Sato Chihiro, Toriyama Masaru, Hirohashi Noritaka, Vacquier Victor, Kitajima Ken

ZOOLOGICAL SCIENCE 21 巻 ( 12 ) 頁： 1292 - 1292 2004年12月

A newly identified zona pellucida glycoprotein, ZPD, and dimeric ZP1 of chicken egg envelope are involved in sperm activation on sperm-egg interaction.

Okumura H, Kohno Y, Iwata Y, Mori H, Aoki N, Sato C, Kitajima K, Nadano D, Matsuda T

The Biochemical journal 384 巻 ( Pt 1 ) 頁： 191 - 9 2004年11月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：Biochemical Journal

Fertilization begins with interaction between the sperm and the egg. The surface of the vertebrate oocyte is covered with the egg envelope, which is composed of ZP (zona pellucida) glycoproteins. We have identified two glycoproteins, ZP1/gp97 and ZPC/gp42, as the major components of the chicken egg envelope. In the present study, another 42 kDa protein, designated ZPD, has been found as a new major component of the chicken egg envelope. ZPD was specifically released from the egg envelope by ultrasonication treatment without urea. ZPD cDNA was cloned using a chicken granulosa cell cDNA pool. The deduced amino acid sequence showed that preproprotein of ZPD is composed of 418 amino acid residues with four potential N-glycosylation sites and includes a ZP domain, common in vertebrate ZP glycoproteins, and a transmembrane domain. ZPD belongs phylogenetically to a distinct group from known ZP glycoprotein subfamilies, ZPA, ZPB, and ZPC. In two-dimensional gel electrophoresis ZPD proteins were identified to be several isoforms with different pi values between 5 and 7. ZP1, ZPC and the newly identified ZPD were confirmed to be the major components of chicken egg envelope by MS of proteolytic digests of whole egg envelope. The in vitro incubation of chicken sperm with calcium ionophore A23187 induced sperm activation, resulting in the fragmentation and release of a 41 kDa PNA (peanut agglutinin)-positive glyco-protein and the decrease or loss of sperm PNA-stainability. The incubation with ZPD and dimeric ZP1, but not ZPC and monomeric ZPl, also induced the decrease or loss of sperm PNA-stainability, suggesting the in vitro sperm activation by these ZP components. Collectively, ZPD might bind loosely to egg envelope matrix and play a key role in the sperm activation on avian sperm-egg interaction.

DOI： 10.1042/BJ20040299

Development of sensitive chemical and immunochemical methods for detecting sulfated sialic acids and their application to localization and quantitation studies of sea urchin sperm and eggs

Yamakawa N, Maehashi E, Miyata S, Sato C, Furuhata K, Kitajima K

GLYCOBIOLOGY 14 巻 ( 11 ) 頁： 1146 - 1146 2004年11月

Effects of exogenously administered mannose and deaminoneuraminic acid (KDN) to mice or murine cultured cells on the metabolism of KDN

Go S, Sato C, Kitajima K

GLYCOBIOLOGY 14 巻 ( 11 ) 頁： 1166 - 1167 2004年11月

Mouse heat shock protein 70 recognizes negatively charged glycolipids and phospholipids

Harada Y, Sato C, Kitajima K

GLYCOBIOLOGY 14 巻 ( 11 ) 頁： 1101 - 1102 2004年11月

Occurrence and characterization of a novel sulfated alpha 2,9-linked polysialic acid-containing glycoprotein in sea urchin sperm flagellum

Miyata S, Sato C, Kitajima K

GLYCOBIOLOGY 14 巻 ( 11 ) 頁： 1146 - 1146 2004年11月

Mouse T cell CD166 is a disialic acid-containing glycoprotein and involved in T cell activation

Sato C, Nohara K, Matsuda T, Kitajima K

GLYCOBIOLOGY 14 巻 ( 11 ) 頁： 1136 - 1136 2004年11月

Studies on chemical properties of cyclic sialic acid using their synthetic S- and O-glycosides as model compounds

Iwata, S; Sato, C; Ando, H; Kiso, M; Kannagi, R; Kitajima, K

GLYCOBIOLOGY 14 巻 ( 11 ) 頁： 1163 - 1163 2004年11月

Specificity of human trans-sialidase as probed with gangliosides

Nikonova, EY; Tertov, VV; Sato, C; Kitajima, K; Bovin, NV

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS 14 巻 ( 20 ) 頁： 5161 - 5164 2004年10月

「シアル酸研究の新たな潮流」の特集にあたって

SATO Chihiro

Trends in glycoscience and glycotechnology 16 巻 ( 91 ) 頁： 291 - 292 2004年9月

Preface for the special issue entitled "new waves in sialobioscience"

Sato C.

Trends in Glycoscience and Glycotechnology 16 巻 ( 91 ) 頁： 291 - 292 2004年9月

Chain length diversity of sialic acids and its biological significance

Sato C.

Trends in Glycoscience and Glycotechnology 16 巻 ( 91 ) 頁： 331 - 344 2004年9月

記述言語：日本語掲載種別：研究論文（学術雑誌）出版者・発行元：Trends in Glycoscience and Glycotechnology

Sialic acids are commonly present as monosialyl residues at the non-reducing terminal end of glycoconjugates. In some cases, αc2→8 linked di/oligosialic acid chains with DP 2 or 3 sialic acid residues are common structural units of gangliosides, and involved in various biological processes, such as cell adhesion, cell differentiation, signal transduction, and surface expression of stage specific antigen. In contrast, little attention has been paid to the occurrence and functions of such short sialyl di/oligomers on glycoproteins, while polysialic acid (DP≥8) in embryonic NCAM has been extensively studied as a regulator of cell adhesion in neurogenesis. As analytical methods to detect di/oligosialic acid structures have been improved, several glycoproteins containing di/oligo/polysialic acid chains have been identified. It is thus hypothesized that these di/oligosialic acid residues on glycoproteins may have similar important functions in common with those proposed for the gangliosides or may have new functions. Currently, several studies showing the importance of di/oligosialic acid-containing glycoproteins have emerged. In this review, recent advances in such studies of di/ oligosialic acid residues on glycoproteins, including analytical methods, occurrence, biosynthetic pathways, and functions, are described.

DOI： 10.4052/tigg.16.331

Scopus

CiNii Research

Developmental Expression of a Sialyltransferase Responsible for Sialylation of Cortical Alveolus Glycoprotein during Oogenesis in Rainbow Trout (Oncorhynchus mykiss)

ASAHINA Shinji, SATO Chihiro, KITAJIMA Ken

Journal of Biochemistry 136 巻 ( 2 ) 頁： 189 - 198 2004年8月

Developmental expression of a sialyltransferase responsible for sialylation of cortical alveolus glycoprotein during oogenesis in rainbow trout (Oncorhynchus mykiss).

Asahina S, Sato C, Kitajima K

Journal of biochemistry 136 巻 ( 2 ) 頁： 189 - 98 2004年8月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：Journal of Biochemistry

Polysialoglycoprotein (PSGP) is a major cortical alveolus glycoprotein of rainbow trout eggs that is characterized by the attachment of a polysialic acid structure to its O-glycan chains. It has been demonstrated that the polysialic acid structure is synthesized by at least three sialyltransferases mostly localized in cortical alveoli. Here we have cloned a cDNA encoding the sialyltransferase, designated rtST6GalNAc, responsible for the transfer of the first sialic acid residue onto the O-glycan chain of PSGP. This enzyme belongs to the vertebrate ST6GalNAc II family, and is strongly expressed in ovaries. Of those O-glycoproteins tested as substrates, asialo-PSGP is the best substrate. These results indicate that rtST6GalNAc is the enzyme responsible for the sialylation of PSGP during oogenesis. Furthermore, the rtST6GalNAc mRNA is expressed throughout oogenesis, is down-regulated at the late yolk vesicle stage (May), and then up-regulated during vitellogenesis (until August). This developmental profile is highly similar to that of STL2, a cortical alveolus lectin, while it is quite different from that of PSGP, which is extensively expressed at the yolk vesicle stage and down-regulated at later stages. Thus, not all cortical alveolus components are transcribed concomitantly. This is the first description of a developmental change in the transcription of a glycosyltransferase during oogenesis.

DOI： 10.1093/jb/mvh106

Alpha-C-mannosyltryptophan is not recognized by conventional mannose-binding lectins.

Nishikawa T, Kajii S, Sato C, Yasukawa Z, Kitajima K, Isobe M

Bioorganic & medicinal chemistry 12 巻 ( 9 ) 頁： 2343 - 8 2004年5月

記述言語：英語掲載種別：研究論文（学術雑誌）出版者・発行元：Bioorganic and Medicinal Chemistry

α-C-Mannosyltryptophan (C-Man-Trp) is a novel, naturally occurring C-linked carbohydrate-protein linkage first found in 1994 from human ribonuclease 2. Since then, a number of C-Man-Trp residue have been found from several important proteins such as interleukin 12β, components of complement system, thrombospondin-1, and erythropoietin receptor, however, the biological functions have remained unknown even though its biosynthetic pathway has been revealed. In order to find a clue as to the biological functions, we examined the affinity of C-Man-Trp with conventional mannose lectin such as concanavarin A (Con A) and mannose-binding lectin (MBL). The affinity of C-Man-Trp with Con A, a typical mannose-binding lectin from plant was examined using a Con A-Sepharose column. Unlike p-nitrophenyl-α-O-Man, C-Man-Trp was not retained on the column. MBL-C, a major mannose-binding lectin purified from mouse serum, did not bind with N-biotinylated C-Man-Trp, judging from ELISA based assay. These results imply that C-Man-Trp may be recognized with the other specific proteins associated with its unknown biological functions. © 2004 Elsevier Ltd.

DOI： 10.1016/j.bmc.2004.02.009

Web of Science

Scopus

PubMed

ジシアル酸・オリゴシアル酸・ポリシアル酸の生物学的機能

佐藤ちひろ

Functional Glycomics 3 頁： 40 - 47 2004年

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