Faculty Profiles - SATO, Chihiro

Papers - SATO, Chihiro

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Developmental stage-dependent expression of an α2,8-trisialic acid unit on glycoproteins in mouse brain. Reviewed

Inoko, E., Nishiura, Y., Tanaka, H., Takahashi, T., Furukawa, K., Kitajima, K., and Sato, C.

Glycobiology Vol. 20 page： 916-928 2010

Survival signals of hepatic stellate cells in liver regeneration are regulated by glycosylation changes in rat vitronectin, especially decreased sialylation. Reviewed

Sano K, Miyamoto Y, Kawasaki N, Hashii N, Itoh S, Murase M, Date K, Yokoyama M, Sato, C, Kitajima K, Ogawa H

J Biol Chem Vol. 285 page： 17301-17309 2010

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

Inoue, S, Sato, C, Kitajima, K

Glycobiology Vol. 20 page： 752-762 2010

糖鎖と統合失調症 Invited

佐藤ちひろ

生体の科学 Vol. 61 page： 160-166 2010

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. Reviewed

Hino S, Umeda F, Inumaru S, Aoki N, Sato, C, Okajima T, Nadano D, Matsuda T

Immunol Lett Vol. 133 page： 28-34 2010

Periodate-resistant carbohydrate epitopes recognized by IgG and IgE antibodies from some of the immunized mice and patients with allergy Reviewed

Shingo Hino, Takeshi Matsubara, Atsuo Urisu, Naohito Aoki, Chihiro Sato, Tetsuya Okajima, Daita Nadano, Tsukasa Matsuda

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS Vol. 380 ( 3 ) page： 632 - 7 2009.3

Language：English Publishing type：Research paper (scientific journal) Publisher：ACADEMIC PRESS INC ELSEVIER SCIENCE

The beta(1,2)-xylose- and/or alpha(1,3)-fucose-containing cross-reactive carbohydrate determinants (CCDs) are present in various plant and insect N-glycans, and have been attracted as potential antigens in IgE-mediated allergies and immunologically undesired post-translational products on some recombinant therapeutic proteins. By using ELISA and immunoblotting, CCDs-specific IgG and IgE antibodies from some, but not all, of mice and humans were found to fully retain their binding activity after a typical periodate-treatment to CCDs, which did cause the CCDs' antigenic activity to those from the other mice and rabbits to disappear almost completely. Furthermore, the mouse IgE recognizing the periodate-resistant CCDs induced the CCDs/IgE-dependent degranulation of rat basophilic RBL-2H3 cells. These findings indicate that in some cases CCDs include those dependent of the core trisaccharide more strongly than the terminal xylose and fucose, which might have been screened out in the CCDs analyses based on the loss of antibody-binding by the periodate-treatment. (C) 2009 Elsevier Inc. All rights reserved.

DOI： 10.1016/j.bbrc.2009.01.138

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Membrane microdomains from early gastrula embryos of medaka, Oryzias latipes are a plat form of E-cadherin and carbohydrate-mediated cell-cell interactions during epiboly Reviewed

Adachi T., Sato, C., Kishi, Y., Totani, K., Murata, T., Usui, T., and Kitajima, K

Glycoconjugate J. Vol. 26 page： 285-299 2009

Complex formation of a brain-derived neurotrophic factor and glycosaminoglycans. Reviewed

Kanato, Y., Kitajima, K. and Sato, C.

Biosci. Biotech. Biosci. Vol. 12 page： 1044-1053 2009

Developmental regulation of oligosialylation in zebrafish. Reviewed

Chang LY, Harduin-Lepers A, Kitajima K, Sato C, Huang CJ, Khoo KH, Guérardel Y.

Glycoconjugate J. Vol. 26 page： 247-61 2009

Complex formation of a brain-derived neurotrophic factor and glycosaminoglycans. Reviewed

Kanato, Y, Kitajima, K, Sato, C

Biosci. Biotech. Biosci. Vol. 12 page： 1044-1053 2009

Developmental regulation of oligosialylation in zebrafish. Reviewed

Chang LY, Harduin-Lepers A, Kitajima K, Sato C, Huang CJ, Khoo KH, Guérardel Y

Glycoconjugate J. Vol. 26 page： 247-61 2009

Membrane microdomains from early gastrula embryos of medaka, Oryzias latipes are a plat form of E-cadherin and carbohydrate-mediated cell-cell interactions during epiboly Reviewed

Adachi T, Sato, C, Kishi, Y, Totani, K, Murata, T, Usui, T, Kitajima, K

Glycoconjugate J. Vol. 26 page： 285-299 2009

[Regulation of signal transduction by polysialic acid]. Reviewed

Sato C, Kitajima K

Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme Vol. 53 ( 12 Suppl ) page： 1577 - 1583 2008.9

Direct binding of polysialic acid to a brain-derived neurotrophic factor depends on the degree of polymerization Reviewed

Kanato, Y, Kitajima, K., and Sato, C.

Glycobiology Vol. 12 page： 1044-1053 2008

ポリシアル酸構造による細胞シグナルの調節機構 Invited

佐藤ちひろ、北島健

蛋白質核酸酵素 Vol. 53 ( 1577-1583 ) 2008

Direct binding of polysialic acid to a brain-derived neurotrophic factor depends on the degree of polymerization Reviewed

Kanato, Y, Kitajima, K, Sato, C

Glycobiology Vol. 12 page： 1044-1053 2008

Glycobiology of polysialic acids on sea urchin gametes

Miyata Shinji, Sato Chihiro, Kitajima Ken

TRENDS IN GLYCOSCIENCE AND GLYCOTECHNOLOGY Vol. 19 ( 106 ) page： 85-98 2007.3

Identification of an inflammation-inducible serum protein recognized by anti-disialic acid antibodies as carbonic anhydrase II Reviewed

Zenta Yasukawa, Chihiro Sato, Ken Kitajima

JOURNAL OF BIOCHEMISTRY Vol. 141 ( 3 ) page： 429 - 41 2007.3

Language：English Publishing type：Research paper (scientific journal) Publisher：JAPANESE BIOCHEMICAL SOC

Acute-phase proteins are an important marker of inflammation and sometimes have a role in the general defense response towards tissue injury. In the present study, we identified a 32-kDa protein that was immunoreactive with monoclonal antibody 2-4B (mAb.2-4B), which is specific to di/oligoNeu5Gc structures, and that behaved as an acute-phase protein following stimulation with either turpentine oil or lipopolysaccharides. The 32-kDa protein was identified as carbonic anhydrase II (CA-II), based on matrix-assisted laser desorption/ionization time-of-flight mass spectrometry analyses of the purified protein. Mouse and human CA-II was immunoreactive and immunoprecipitated with mAb.2-4B, but contained no sialic acid. In addition to mAb.2-4B, the mAb. S2-566 an antibody specific for diNeu5Ac-containing glycans, recognized the CA-II, whereas an anti-oligo/polysialic acid antibody did not. These results indicate that a part of the CA-II protein structure mimics the disialic acid structure recognized by the monoclonal antibodies. This is the first report that CA-II circulates in the serum following inflammation.

DOI： 10.1093/jb/mvm047

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PubMed

Heterocomplex formation and cell-surface accumulation of hen's serum zona pellucida B1 (ZPB1) with ZPC expressed by a mammalian cell line (COS-7): A possible initiating step of egg-envelope matrix construction

Okumura Hiroki, Aoki Naohito, Sato Chihiro, Nadano Daita, Matsuda Tsukasa

BIOLOGY OF REPRODUCTION Vol. 76 ( 1 ) page： 9-18 2007.1

Hiroki Okumura, Naohito Aoki, Chihiro Sato, Daita Nadano, Tsukasa Matsuda

BIOLOGY OF REPRODUCTION Vol. 76 ( 1 ) page： 9 - 18 2007.1

Language：English Publishing type：Research paper (scientific journal) Publisher：SOC STUDY REPRODUCTION

The egg envelope, referred to as zona pellucida (ZP) in mammalian eggs, is a fibrous and noncollagenous extracellular matrix surrounding vertebrate eggs, and composed of three to four homologous glycoproteins with a common ZP domain. In birds, a liver-derived ZP glycoprotein (ZP1/ZPB1) is transported through the bloodstream to ovarian follicles and joins the egg-envelope matrix construction together with the other ZP glycoproteins, such as ZPC and ZPD/ZPX2, both secreted from follicular granulosa cells. We report here that, through its ZP domain, ZPB1 specifically associates with ZPC, which might lead to the construction of egg-envelope matrix. The ZPB1 in laying hen's serum specifically bound to ZPC, but not to ZPX2, separated by SDS-PAGE and blotted on a membrane. Hemagglutinin (HA)-tagged ZPC expressed in a mammalian cell line (COS-7) cells was processed and secreted as a mature-form into the culture medium. From the culture supernatant of ZPC-expressing transfectants cultured in the presence of ZPB1, both ZPB1 and ZPC were recovered as heterocomplexes by immunoprecipitation using either anti-HA or anti-ZPB1 antibody. Interestingly, a monoclonal antibody, 8E1, which immunoprecipitated free ZPB1, did not immunoprecipitate the ZPB1-ZPC heterocomplexes. An 8E1 epitope was mapped on a C-terminal region of the ZP domain in a ZPB1 molecule by identifying an 8E1-positive peptide using mass spectroscopy. Furthermore, by laser scanning confocal microscopy, ZPB1 and ZPC were observed to colocalize on the surface of ZPC-expressing transfectants cultured in the presence of ZPB1, whereas almost no ZPC was detected on the surface of the transfectants cultured in the absence of ZPB1. Taken together, these results suggest that ZPB1 transported into ovarian follicles encounters and associates with ZPC secreted from granulosa cells, resulting in the formation of heterocomplexes around an oocyte. In addition, it appears that such ZPB1-ZPC complexes accumulated on the oocyte surface act as a scaffold for subsequent matrix construction events including ZPX2 association.

DOI： 10.1095/biolreprod.106.056267

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