研究者詳細 - 佐藤　ちひろ

論文 - 佐藤　ちひろ

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FORMATION OF MEMBRANE MICRODOMAINS IS SIGNIFICANT IN DEVELOPING EMBRYOS OF MEDAKA(Developmental Biology,Abstracts of papers presented at the 74^<th> Annual Meeting of the Zoological Society of Japan) :

AdachiTomoko, SatoChihiro, KitajimaKen

Zoological science 20 巻 ( 12 ) 頁： 1570 2003年12月

[Frequent occurrence and biological significance of degree of polymerization in sialic acid]. 査読有り

Sato C

Seikagaku. The Journal of Japanese Biochemical Society 75 巻 ( 12 ) 頁： 1526 - 30 2003年12月

FUNCTIONS OF THE COMMON GLYCOTOPES OF GLYCOLIPIDS AND GLYCOPROTEINS IN THE MEMBRANE MICRODOMAIN OF SEA URCHIN SPERM(Developmental Biology)(Proceedings of the Seventy-Third Annual Meeting of the Zoological Society of Japan) :

MiyataShinji, MaehashiEri, OhtaKaoru, SatoChihiro, MatsudaTsukasa, KitajimaKen

Zoological science 19 巻 ( 12 ) 頁： 1443 2002年12月

Neuronal differentiation-dependent expression of the disialic acid epitope on CD166 and its involvement in neurite formation in Neuro2A cells.

Sato C, Matsuda T, Kitajima K

The Journal of biological chemistry 277 巻 ( 47 ) 頁： 45299 - 305 2002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：Journal of Biological Chemistry

We previously demonstrated that α2,8-linked disialic acid (diSia) residues occur in several glycoproteins of mammalian brains (Sato, C., Fukuoka, H., Ohta, K., Matsuda, T., Koshino, R., Kobayashi, K., Troy, F. A., II, and Kitajima, K. (2000) J. Biol. Chem. 275, 15422-15431). The role of the diSia epitope on these glycoproteins is not known, whereas the importance of the diSia epitope on glycolipids is well documented in neurite formation. In this study, we demonstrated that the diSia epitope (Neu5Acα2 → 8Neu5Acα2 → 3Gal) on glycoproteins, but not on glycolipids, is involved in neurite formation in a mouse neuroblastoma cell line, Neuro2A, based on the following lines of evidence. First, the amount of diSia epitope on glycoproteins increased during retinoic acid-induced neurite formation. Second, retinoic acid treatment primarily increased the diSia epitope on a 100-kDa glycoprotein. We identified this protein as CD166 (SC1), an immunoglobulin superfamily cell adhesion molecule involved in neurite extension. Third, a monoclonal antibody against the diSia epitope specifically inhibited neurite formation. We also demonstrated that α2,8-sialyltransferase III mRNA expression increased 1.7-fold after the induction of neurite formation, suggesting that α2,8-sialyltransferase III is responsible for formation of the diSia epitope on CD166.

DOI： 10.1074/jbc.M206046200

Web of Science

Scopus

PubMed

ジ・オリゴシアル酸構造の生物学的機能

佐藤ちひろ, 北島健

6 巻頁： A4J 2002年6月

Function of Di/oligosialic Acid Structure

Sato Chihiro, Kitajima Ken

Glycoforum 6 巻頁： A4 2002年6月

Occurrence of Oligosialic Acids on Integrin α<inf>5</inf> Subunit and Their Involvement in Cell Adhesion to Fibronectin

Nadanaka S., Sato C., Kitajima K., Katagiri K., Irie S., Yamagata T.

Journal of Biological Chemistry 276 巻 ( 36 ) 頁： 33657 - 33664 2001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：Journal of Biological Chemistry

Integrin α5β1, a major fibronectin receptor, functions in a wide variety of biological phenomena. We have found that α2-8-linked oligosialic acids with 5 ≤ degree of polymerization (DP) ≤ 7 occur on integrin α5 subunit of the human melanoma cell line G361. The integrin α5 subunit immunoprecipitated with anti-integrin α5 antibody reacted with the monoclonal antibody 12E3, which recognizes oligo/polysialic acid with DP ≥ 5 but not with the polyclonal antibody H.46 recognizing oligo/polysialic acid with DP ≥ 8. The occurrence of oligosialic acids was further demonstrated by fluorometric C7/C9 analysis on the immunopurified integrin α5 subunit. Oligosialic acids were also found in the α5 subunit of several other human cells such as foreskin fibroblast and chronic erythroleukemia K562 cells. These results suggest the ubiquitous modification with unique oligosialic acids occurs on the α 5 subunit of integrin α5β1. The adhesion of human melanoma G361 cells to fibronectin was mainly mediated by integrin α5β1. Treatment of cells with sialidase from Arthrobacter ureafaciens cleaving α2-3-, α2-6-, and α2-8-linked sialic acids inhibited adhesion to fibronectin. On the other hand, N-acetylneuraminidase II, which cleaves α2-3 and α2-6 but not α2-8 linkages, showed no inhibitory activity. After the loss of oligosialic acids, integrin α5β1 failed to bind to fibronectin-conjugated Sepharose, indicating that the oligosialic acid on the α5 subunit of integrin α5β 1 plays important roles in cell adhesion to fibronectin.

DOI： 10.1074/jbc.M011100200

Scopus

Identification and Adipocyte Differentiation-dependent Expression of the Unique Disialic Acid Residue in an Adipose Tissue-specific Glycoprotein, Adipo Q

Sato C., Yasukawa Z., Honda N., Matsuda T., Kitajima K.

Journal of Biological Chemistry 276 巻 ( 31 ) 頁： 28849 - 28856 2001年8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：Journal of Biological Chemistry

Recently, we have shown that α2,8-linked disialic acid (diSia) residue occurs in glycoproteins more frequently than ever recognized (Sato, C., Fukuoka, H., Ohta, K., Matsuda, T., Koshino, R., Kobayashi K., Troy, F. A., II, and Kitajima, K. (2000) J. Biol. Chem. 275, 15422-15431). In the course of identification of the diSia-containing glycoproteins in mammals, the 30-kDa glycoprotein was found in bovine serum. The 30-kDa glycoprotein was shown to be the bovine adipo Q, an adipocyte-specific protein, based on the partial amino acid sequences and the immuno-cross-reactivity with the recombinant mouse adipo Q. The bovine adipo Q was shown to have no N-linked but O-linked glycan(s) containing the diSia epitope, Neu5Acα2→8Neu5Acα2→3Gal. Furthermore, the diSia epitope was also found in the mouse adipo Q in serum as well as in the 3T3-L1 cells that are fully differentiated into adipocytes. Notably, among the known α2,8-sialyltransferases, only the α2,8-sialyltransferase III mRNA was detected in the 3T3-L1 cells at any stages of differentiation, and the recombinant α2,8-sialyltransferase III could sialylate the purified bovine adipo Q. Thus, this study clearly provides the new findings that adipo Q is the diSia-containing glycoprotein and a physiological substrate of α2,8-sialyltransferase III, whose substrates have not been identified so far.

DOI： 10.1074/jbc.M104148200

Scopus

昆虫におけるシアル酸，その存在と意義

佐藤ちひろ

Ｔｒｅｎｄｓ　ｉｎ　Ｇｌｙｃｏｓｃｉｅｎｃｅ　ａｎｄ　Ｇｌｙｃｏｔｅｃｈｎｏｌｏｇｙ 13 巻 ( 73 ) 頁： 507 - 517 2001年

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：FCCA(Forum: Carbohydrates Coming of Age)

数種の昆虫の発生途上にシアル酸、主に、N-アセチルノイラミン酸が見出されてきている。我々はレクチンや抗体、単糖の様々な精製および分析法を用いることによって、ショウジョウバエ (Drosophila melanogaster) の神経発達領域およびセミ(Philaenus spumarius) のマルピーギ管にポリシアル酸を検出した。これらの昆虫の成体にシアル酸は検出されなかった。シアル酸の発現は in vivo では明らかであるが、多くの昆虫培養細胞系ではその存在が明らかにされていない。また、バキュロウイルスの発現系を用いて哺乳動物型の組換え糖タンパク質 (複合型シアリル化N-型糖鎖をもつもの)を生産することは利点が多くあるため、培養細胞におけるシアル酸の生合成機構の解明が生物工学的な観点から重要視されてきている。それらの研究によって明らかになったことは、糖鎖の改変は昆虫細胞に糖転移酵素群を発現させることによってのみ可能であることである。すなわちシアル酸の生合成に関わる酵素をコードするいくつかの外来遺伝子を導入しなくてはならない。さらに、昆虫細胞に関する研究によって、シアル酸は動物界の新口動物に限られているのではなく、昆虫のような原口動物にも存在することが明らかになった。このことはシアル酸の進化に対して新しい見解を投ずるものである。

DOI： 10.4052/tigg.13.507

CiNii Research

Co-localization of receptor and transducer proteins in the glycosphingolipid-enriched, low density, detergent-insoluble membrane fraction of sea urchin sperm

Ohta K., Sato C., Matsuda T., Toriyama M., Vacquier V., Lennarz W., Kitajima K.

Glycoconjugate Journal 17 巻 ( 3-4 ) 頁： 205 - 214 2000年12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：Glycoconjugate Journal

The low density, detergent-insoluble membrane fraction (LD-DIM), where gangliosides are likely to be highly enriched, was prepared from sperm of two sea urchin species, Hemicentrotus pulcherrimus and Strongylocentrotus purpuratus. Immunoblotting showed the presence in the LD-DIM of two receptors for egg ligands, a glycosylphosphatidylinositol (GPI)-anchored protein, and four proteins which may be involved in signal transduction. Co-immunoprecipitation revealed that at least three proteins, the speract receptor, the 63kDa GPI-anchored protein and the α subunit of a heterotrimeric Gs protein, are localized in the LD-DIM. This suggests that the LD-DIM fraction may be a membrane microdomain for speract-speract receptor interaction, as well as the subsequent signal transduction pathway involved in induction of sperm respiration, motility and possibly the acrosome reaction.

DOI： 10.1023/A:1026589223811

Scopus

Frequent occurrence of pre-existing α2→8-linked disialic and oligosialic acids with chain lengths up to 7 Sia residues in mammalian brain glycoproteins. Prevalence revealed by highly sensitive chemical methods and anti-di-, oligo-, and poly-Sia antibodies specific for defined chain lengths

Sato C., Fukuoka H., Ohta K., Matsuda T., Koshino R., Kobayashi K., Troy F.A., Kitajima K.

Journal of Biological Chemistry 275 巻 ( 20 ) 頁： 15422 - 15431 2000年5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：Journal of Biological Chemistry

The pre-existence of α2→8-linked disialic acid (di-Sia) and oligosialic acid (oligo-Sia) structures with up to 7 Sia residues was shown to occur on a large number of brain glycoproteins, including neural cell adhesion molecules (N-CAMs), by two highly sensitive chemical methods (Sato, C., Inoue, S., Matsuda, T., and Kitajima, K. (1998) Anal. Biochem. 261, 191- 197; Sato, C., Inoue, S., Matsuda, T., and Kitajima, K. (1999) Anal Biochem. 266, 102-109). This unexpected finding was also confirmed using a newly developed antibody prepared using a copolymer of α2→8-linked N- acetylneuraminyl p-vinylbenzylamide and acrylamide as an immunogen and known antibodies whose immunospecificities were determined to be di- and oligo-Sia residues with defined chain lengths. The major significance of the new finding that di- and oligo-Sia chains exist on a large number of brain glycoproteins is 2-fold. First, it reveals a surprising diversity in the number and M(r) of proteins distinct from N-CAM that are covalently modified by these short sialyl glycotopes. Second, it suggests that synthesis of di- and/or oligo-Sia units may be catalyzed by α2→8-sialyltransferase(s) that are distinct from the known polysialyltransferases, STX and PST, which are partially responsible for polysialylation of N-CAM.

DOI： 10.1074/jbc.275.20.15422

Scopus

Lipid raft on gametic cells as a functional domain for sperm-egg interaction coupled with signal transduction

Ohta K., Sato C., Matsuda T., Toriyama M., Vacquier V.D., Hirohashi N., Lennarz W.J., Kitajima K.

Zygote 8 巻 ( SUPPL. ) 頁： . 2000年

Ｏ‐アセチル化シアル酸　　その検出，生物学的意義，および病気における変化

佐藤ちひろ

Ｔｒｅｎｄｓ　ｉｎ　Ｇｌｙｃｏｓｃｉｅｎｃｅ　ａｎｄ　Ｇｌｙｃｏｔｅｃｈｎｏｌｏｇｙ 12 巻 ( 63 ) 頁： 17 - 33 2000年

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：FCCA(Forum: Carbohydrates Coming of Age)

シアル酸はカルボン酸をもつ酸性9炭糖であり、一般に、細胞膜局在あるいは分泌性の複合糖質の糖鎖の最も外側に位置している。この配位は、多くの細胞間および分子間相互作用の制御に関与しやすい点で好都合である。シアル酸は構造多様性をもつが、中でも最も多く見出されるのはC-4、7、9位のO-アセチル化体である。O-アセチル化シアル酸 (O-AcSA) における構造多様性は、それを担っている糖鎖の結合様式、O-アセチル化される炭素の位置、および結合している複合糖質の性状に起因する。分析手法が改善されてきたことによって、いくつかの病気におけるO-AcSA誘導体の同定が可能になったことから、興味の中心はこの修飾反応の生物学的重要性の理解へと方向変換してきた。この総説では、様々な病理生理学的状態に伴って変化するO-アセチル化体の検出法やそれらの生物学的関連性に関する最新の情報を扱っている。特に、9-O-アセチル化シアル酸含有複合糖質 (9-OAcSA) がその病気の診断マーカーとして有用である二つの全く異なる病気である、急性リンパ球性白血病 (ALL) と内臓リーシュマニア症 (VL) に注目している。

DOI： 10.4052/tigg.12.17

CiNii Research

Lipid raft on gametic cells as a functional domain for sperm-egg interaction coupled with signal transduction

Ohta K, Sato C, Matsuda T, Toriyama M, Vacquier VD, Hirohashi N, Lennarz WJ, Kitajima K

ZYGOTE 8 巻頁： S63 - S63 2000年

Lipid raft on gametic cells as a functional domain for sperm-egg interaction coupled with signal transduction.

Ohta K, Sato C, Matsuda T, Toriyama M, Vacquier VD, Hirohashi N, Lennarz WJ, Kitajima K

Zygote (Cambridge, England) 8 Suppl 1 巻頁： S63 2000年

Glycobiology of Di- and Oligosialyl Glycotopes

Sato C., Kitajima K.

Trends in Glycoscience and Glycotechnology 11 巻 ( 62 ) 頁： 371 - 390 1999年11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

α2→8-Linked di- and oligosialic acid (diSia and oligoSia) chains with DP 2,3 Sia residues are known to be common structural units of gangliosides, and to be 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 oligomers on glycoproteins. However, it has recently been shown that glycoproteins containing di- and oligoSia groups occur in nature more frequently than was ever recognized, as analytical methods to detect di- and oligoSia structures have improved. It is thus hypothesized that these di- and oligoSia moieties on glycoproteins may have similar important functions in common with those proposed for the gangliosides. In this review, we describe the recent advances in the study of di- and oligoSia residues on glycoproteins, including analytical methods, occurrence, functions, and biosynthetic pathways.

DOI： 10.4052/tigg.11.371

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CiNii Research

Cholesterol-dependent localization of NAP-22 on a neuronal membrane microdomain (Raft)

Maekawa S., Sato C., Kitajima K., Funatsu N., Kumanogoh H., Sokawa Y.

Journal of Biological Chemistry 274 巻 ( 30 ) 頁： 21369 - 21374 1999年7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：Journal of Biological Chemistry

A membrane microdomain called raft has been under extensive study since the assembly of various signal-transducing molecules into this region has been envisaged. This domain is isolated as a low buoyant membrane fraction after the extraction with a nonionic detergent such as Triton X-100. The characteristic low density of this fraction is ascribed to the enrichment of several lipids including cholesterol. To clear the molecular mechanism of raft formation, several extraction methods were applied to solubilize raft components. Cholesterol extraction using methyl-β-cyclodextrin was found to be effective to solubilize NAP-22, a neuron-enriched Ca2+-dependent calmodulin-binding protein as well as one of the main protein components of brain raft. Purified NAP-22 bound to the liposomes that were made from phosphatidylcholine and cholesterol. This binding was dependent on the amount of cholesterol in liposomes. Calmodulin inhibited this binding in a dose- dependent manner. These results suggest that the presence of a calcium- dependent regulatory mechanism works on the assembly of raft within the neuron.

DOI： 10.1074/jbc.274.30.21369

Scopus

Isolation and characterization of low density detergent-insoluble membrane (LD-DIM) fraction from sea urchin sperm

Ohta K., Sato C., Matsuda T., Toriyama M., Lennarz W., Kitajima K.

Biochemical and Biophysical Research Communications 258 巻 ( 3 ) 頁： 616 - 623 1999年5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：Biochemical and Biophysical Research Communications

The low density detergent-insoluble membrane (LD-DIM) fraction was obtained by a sucrose-density gradient centrifugation from sperm of three sea urchin species, Hemicentrotus pulcherrimus, Strongylocentrotus purpuratus, and Anthocidaris crassispina. These LD-DIM preparations were characterized by enriched glycosphingolipids (GSL) including gangliosides and sulfatide (SLF), having more than 50% of the total amount of GSL present in these sperm. Interestingly, a minor component of H. pulcherrimus sperm (HO3S→8Neu5Acα2→8Neu5Acα2→6Glcβ1→Cer) was shown to be even more enriched in the LD-DIM as revealed by using monoclonal antibody (mAb.3G9) specific to this ganglioside. In addition to the GSL, phosphatidylserine (PS) and diacylglycerol (DG) were enriched in the LD-DIM. On the other hand, cholesterol (CL) and sphingomyelin (SM) were not so enriched, which contrasted with the LD-DIM from Madin-Darby canine kidney (MDCK) cells, where CL and SM were reported to be abundant. Because mammalian somatic cell-derived DIMs have been proposed to be associated with functional signal transduction, it seems possible that the ganglioside-enriched LD-DIM in sea urchin sperm can participate in binding to eggs and the subsequent egg activation process. To our knowledge this is the first chemical characterization of the LD-DIM fraction of a gametic cell.

DOI： 10.1006/bbrc.1999.0686

Scopus

A 42-kDa glycoprotein from chicken egg-envelope, an avian homolog of the ZPC family glycoproteins in mammalian zona pellucida. Its first identification, cDNA cloning and granulosa cell-specific expression

Takeuchi Y., Nishimura K., Aoki N., Adachi T., Sato C., Kitajima K., Matsuda T.

European Journal of Biochemistry 260 巻 ( 3 ) 頁： 736 - 742 1999年3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：European Journal of Biochemistry

A glycoprotein with molecular mass of 42 kDa was identified as the major component of the chicken egg-envelope, the filamentous, extracellular matrix known as the perivitelline layer. By using a DNA probe amplified with degenerative primers derived from the protein's partial amino acid sequences, a cDNA clone encoding the egg-envelope 42-kDa glycoprotein (gp42) was isolated from a hen's ovary cDNA library. The gp42 open reading frame encoded 435 amino acid residues, including a putative signal peptide of 20 amino acids. The deduced amino acid sequence of gp42 showed significant similarity to egg-envelope glycoproteins of the ZPC family of several other vertebrate species, including human ZP3, mouse ZP3, Xenopus laevis gp43 and medaka (Oryzias latipes) ZI3 (LS-F), which play important roles for sperm-egg interaction. A single N-glycosylation site present in chicken gp42 is conserved among all five of these proteins: carbohydrate analysis of gp42 revealed the presence of a complex type glycan chain at this site. N-terminal sequence analysis of the mature polypeptide suggests that C-terminal processing of the pro-protein occurs during synthesis and secretion. The 1.4- kb gp42 transcript was detected only in follicles, and was found to be accumulated in granulosa cells in a manner dependent on ovarian follicular development. Furthermore, a metabolically radio-labeled gp42 was immunoprecipitated from both cell lysate and culture supernatant of the granulosa cells with specific anti-gp42 antibody, suggesting granulosa cell- specific synthesis and secretion of the glycoprotein.

DOI： 10.1046/j.1432-1327.1999.00203.x

Scopus

Fluorescent-assisted detection of oligosialyl units in glycoconjugates

Sato C., Inoue S., Matsuda T., Kitajima K.

Analytical Biochemistry 266 巻 ( 1 ) 頁： 102 - 109 1999年1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：Analytical Biochemistry

A highly sensitive chemical method to detect various types of oligo/polysialic acid (oligo/polySia) units in glycoconjugates, i.e., α2 → 8-linked homooligo/polySia [N-acetylneuraminic acid (Neu5Ac), N- glcolylneuraminic acid (Neu5Gc), or 2-keto-3-deoxy-D-glycero-D-galacto- nononic acid], α2 → 8-linked heterodimers of Neu5Ac and Neu5Gc, α2 → 9- linked homooligo/polyNeu5Ac, and α2 → 5-O(glycolyl)-linked homooligo/polyNeu5Gc, was developed with an α-keto acid-reactive fluorescent labeling reagent, 1,2-diamino-4,5-methylenedioxybenzene (DMB). Fluorescent labeled di- or oligoSia was separated and quantitated by fluorometric anion- exchange high-performance liquid chromatography (HPLC). As little as 13 fmol of Neu5Acα2 → 8Neu5Ac was detectable by this method. When α2 → 8-linked oligo/polyNeu5Ac with on average eight Neu5Ac residues was labeled with DMB, DMB derivatives of oligomers with only lower degrees of polymerization of 2 to 7, were detected, due to concomitant partial depolymerization of oligo/polySia chain with the derivatization. For glycoproteins and glycolipids, mild acid hydrolysis was performed to release oligoSia prior to DMB derivatization. The mild acid hydrolysis/fluorometric HPLC method was also applicable to glycoprotein samples blotted on the membrane.

DOI： 10.1006/abio.1998.2921

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