Faculty Profiles - SATO, Chihiro

Papers - SATO, Chihiro

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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 Vol. 20 ( 12 ) page： 1570 2003.12

[Frequent occurrence and biological significance of degree of polymerization in sialic acid]. Reviewed

Sato C

Seikagaku. The Journal of Japanese Biochemical Society Vol. 75 ( 12 ) page： 1526 - 30 2003.12

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 Vol. 19 ( 12 ) page： 1443 2002.12

Neuronal differentiation-dependent expression of the disialic acid epitope on CD166 and its involvement in neurite formation in neuro2A cells

Sato C, Matsuda T, Katajima K

JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 277 ( 47 ) page： 45299 - 305 2002.11

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

Vol. 6 page： A4J 2002.6

Function of Di/oligosialic Acid Structure

Sato Chihiro, Kitajima Ken

Glycoforum Vol. 6 page： A4 2002.6

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 Vol. 276 ( 36 ) page： 33657 - 33664 2001.9

Language：Japanese Publishing type：Research paper (scientific journal) Publisher：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.

Journal of Biological Chemistry Vol. 276 ( 31 ) page： 28849 - 28856 2001.8

The Occurrence and Significance of Sialic Acids in Insects.

Schauer Roland

Trends in Glycoscience and Glycotechnology Vol. 13 ( 73 ) page： 507 - 517 2001

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

Sialic acids, mainly N-acetylneuraminic acid, have been found during the development of a few insect species. In Drosophila melanogaster and the cicada Philaenus spumarius we detected polysialic acids, using lectins, antibodies, and various methods for the isolation and analysis of the monosaccharide subunits, in areas of neuronal development and in Malpighian tubules, respectively. However, sialic acids were not found in the adult animals of these species. Although the expression of these acidic sugars has unequivocally been demonstrated in vivo, their occurrence in insect cell cultures was, in most cases, not clearly demonstrated. The biosynthesis of sialic acids in cell cultures would be of great biotechnological significance, since the production of recombinant glycoproteins with mammalian type, complex, sialylated N-glycans using the baculovirus expression system would be of great benefit. From the studies dedicated to this problem it appears that the engineering of such glycans may only be possible by the expression of exogenous genes in insect cells. Several genes encoding sialic acid-metabolizing enzymes have therefore been transfected. The work on insect cells shows that sialic acids are not only restricted to the Deuterostomia branch of the animal kingdom but also occur in some Protostomia species, as in insects. This throws new light on the evolution of this acidic sugar.

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.

Glycoconjugate Journal Vol. 17 ( 3-4 ) page： 205 - 214 2000.12

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 Vol. 275 ( 20 ) page： 15422 - 15431 2000.5

Language：Japanese Publishing type：Research paper (scientific journal) Publisher：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.

Zygote Vol. 8 ( SUPPL. ) page： . 2000

O-Acetylated Sialic Acids. Their Detection, Biological Significance and Alteration in Diseases.

Sinha D., Chatterjee M., Mandal C.

Trends in Glycoscience and Glycotechnology Vol. 12 ( 63 ) page： 17 - 33 2000

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

Sialic acids are acidic, 9-carbon carboxylated monosaccharides, typically expressed on the outermost end of the sugar chains of membrane and secreted glycoconjugates. This particular location provides it accessibility reflected in its regulation of a multitude of cellular and molecular interactions. Amongst the diverse structural variations that occur, the commonest is O-acetylation at C-4, 7, 8 and9 carbon positions. This diversity in O-acetylated sialic acid (O-AcSA) derivatives is attributed to their linkage to the underlying sugar chain, the carbon position that gets O-acetylated and nature of the glycoconjugates to which they are attached. Steady refinement of analytical techniques has allowed for identification of O-AcSA derivatives in several diseases leading to a shift in focus towards understanding the biological importance of this modification. The present review deals primarily with the recently evolved information regarding detection of altered O-acetylation in various pathophysiological conditions and their biological relevance. Particular attention is focused on two diverse diseases, namely, Acute Lymphoblastic Leukemia (ALL) and Visceral Leishmaniasis (VL) in which 9-O acetylated sialoglycoconjugates (9-OAcSGs) have proved to be effective biomarkers for monitoring their clinical status.

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 Vol. 8 page： S63 - S63 2000

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) Vol. 8 Suppl 1 page： S63 2000

Glycobiology of Di- and Oligosialyl Glycotopes.

Sato Chihiro, Kitajima Ken

Trends in Glycoscience and Glycotechnology Vol. 11 ( 62 ) page： 371 - 390 1999.11

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

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

Scopus

CiNii Research

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

Maekawa S.

Journal of Biological Chemistry Vol. 274 ( 30 ) page： 21369 - 21374 1999.7

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

Ohta K.

Biochemical and Biophysical Research Communications Vol. 258 ( 3 ) page： 616 - 623 1999.5

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.

European Journal of Biochemistry Vol. 260 ( 3 ) page： 736 - 742 1999.3

Fluorescent-assisted detection of oligosialyl units in glycoconjugates

Sato C.

Analytical Biochemistry Vol. 266 ( 1 ) page： 102 - 109 1999.1

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Papers - SATO, Chihiro