Updated on 2022/10/29

写真a

 
FURUKAWA Junichi
 
Organization
Institute for Glyco-core Research Designated professor
Title
Designated professor
 

Papers 6

  1. Establishment of the removal method of undifferentiated induced pluripotent stem cells coexisting with chondrocytes using R-17F antibody Reviewed

    Takuji Miyazaki, Hisatoshi Hanamatsu, Tomohiro Onodera, Jun-Ichi Furukawa, Liang Xu, Kentaro Homan, Rikiya Baba, Toshisuke Kawasaki, Norimasa Iwasaki

    Regenerative Medicine   Vol. 17 ( 11 ) page: 793 - 803   2022.11

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    Authorship:Corresponding author   Language:English   Publishing type:Research paper (scientific journal)  

    DOI: DOI: 10.2217/rme-2022-0010

  2. Toolbox Accelerating Glycomics (TAG): Improving Large-Scale Serum Glycomics and Refinement to Identify SALSA-Modified and Rare Glycans Invited Reviewed

    Nobuaki Miura 1, Hisatoshi Hanamatsu, Ikuko Yokota, Keiko Akasaka-Manya, Hiroshi Manya, Tamao Endo, Yasuro Shinohara and Jun-ichi Furukawa

    Int. J. Mol. Sci.   Vol. 23 ( 21 ) page: 13097   2022.10

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    Authorship:Last author, Corresponding author   Language:English   Publishing type:Research paper (scientific journal)  

    DOI: https://doi.org/10.3390/ijms232113097

  3. Comprehensive Cellular Glycan Profiling of Glycoproteins and Glycosphingolipids by Glycoblotting and BEP Methods Invited

    Hisatoshi Hanamatsu, Jun-Ichi Furukawa

    Methods in Molecular Biology     page: 1 - 18   2022.9

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    Authorship:Last author, Corresponding author   Language:English   Publishing type:Part of collection (book)  

    DOI: DOI: 10.1007/978-1-0716-2635-1_1

  4. Glycosphingolipid GM3 prevents albuminuria and podocytopathy induced by anti-nephrin antibody

    Kawashima Nagako, Naito Shokichi, Hanamatsu Hisatoshi, Nagane Masaki, Takeuchi Yasuo, Furukawa Jun-ichi, Iwasaki Norimasa, Yamashita Tadashi, Nakayama Ken-ichi

    SCIENTIFIC REPORTS   Vol. 12 ( 1 )   2022.9

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    Language:Japanese   Publisher:Scientific Reports  

    Podocytopathy, which is characterized by injury to podocytes, frequently causes proteinuria or nephrotic syndrome. There is currently a paucity of effective therapeutic drugs to treat proteinuric kidney disease. Recent research suggests the possibility that glycosphingolipid GM3 maintains podocyte function by acting on various molecules including nephrin, but its mechanism of action remains unknown. Here, various analyses were performed to examine the potential relationship between GM3 and nephrin, and the function of GM3 in podocytes using podocytopathy mice, GM3 synthase gene knockout mice, and nephrin injury cells. Reduced amounts of GM3 and nephrin were observed in podocytopathy mice. Intriguingly, this reduction of GM3 and nephrin, as well as albuminuria, were inhibited by administration of valproic acid. However, when the same experiment was performed using GM3 synthase gene knockout mice, valproic acid administration did not inhibit albuminuria. Equivalent results were obtained in model cells. These findings indicate that GM3 acts with nephrin in a collaborative manner in the cell membrane. Taken together, elevated levels of GM3 stabilize nephrin, which is a key molecule of the slit diaphragm, by enhancing the environment of the cell membrane and preventing albuminuria. This study provides novel insight into new drug discovery, which may offer a new therapy for kidney disease with albuminuria.

    DOI: 10.1038/s41598-022-20265-w

    Web of Science

    Scopus

  5. Evaluation of the context of downstream N- and free N-glycomic alterations induced by swainsonine in HepG2 cells

    Morikawa Chie, Sugiura Kanako, Kondo Keina, Yamamoto Yurie, Kojima Yuma, Ozawa Yurika, Yoshioka Hiroki, Miura Nobuaki, Piao Jinhua, Okada Kazue, Hanamatsu Hisatoshi, Tsuda Masumi, Tanaka Shinya, Furukawa Jun-ichi, Shinohara Yasuro

    BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS   Vol. 1866 ( 9 )   2022.9

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    Language:Japanese   Publisher:Biochimica et Biophysica Acta - General Subjects  

    Swainsonine (SWA), a potent inhibitor of class II α-mannosidases, is present in a number of plant species worldwide and causes severe toxicosis in livestock grazing these plants. The mechanisms underlying SWA-induced animal poisoning are not fully understood. In this study, we analyzed the alterations that occur in N- and free N-glycomic upon addition of SWA to HepG2 cells to understand better SWA-induced glycomic alterations. After SWA addition, we observed the appearance of SWA-specific glycomic alterations, such as unique fucosylated hybrid-type and fucosylated M5 (M5F) N-glycans, and a remarkable increase in all classes of Gn1 FNGs. Further analysis of the context of these glycomic alterations showed that (fucosylated) hybrid type N-glycans were not the precursors of these Gn1 FNGs and vice versa. Time course analysis revealed the dynamic nature of glycomic alterations upon exposure of SWA and suggested that accumulation of free N-glycans occurred earlier than that of hybrid-type N-glycans. Hybrid-type N-glycans, of which most were uniquely core fucosylated, tended to increase slowly over time, as was observed for M5F N-glycans. Inhibition of swainsonine-induced unique fucosylation of hybrid N-glycans and M5 by coaddition of 2-fluorofucose caused significant increases in paucimannose- and fucosylated paucimannose-type N-glycans, as well as paucimannose-type free N-glycans. The results not only revealed the gross glycomic alterations in HepG2 cells induced by swainsonine, but also provide information on the global interrelationships between glycomic alterations.

    DOI: 10.1016/j.bbagen.2022.130168

    Web of Science

    Scopus

  6. Comprehensive and Comparative Structural Glycome Analysis in Mouse Epiblast-like Cells Invited

    Federico Pecori, Hisatoshi Hanamatsu, Jun-ichi Furukawa, Shoko Nishihara

    Methods in Molecular Biology     page: 179 - 193   2022.4

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    Authorship:Corresponding author   Language:English   Publishing type:Part of collection (book)  

    DOI: DOI: 10.1007/978-1-0716-2281-0_13

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KAKENHI (Grants-in-Aid for Scientific Research) 1

  1. 包括的組織グライコームによる糖鎖分子ネットワークの構築と老化の客観的評価

    Grant number:22H03502  2022.4 - 2026.3

    科学研究費助成事業  基盤研究(B)

    古川 潤一, 萬谷 博, 三浦 信明

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    Authorship:Principal investigator 

    Grant amount:\17420000 ( Direct Cost: \13400000 、 Indirect Cost:\4020000 )

    申請者はこれまでに特定のサブグライコームだけではなく、種々のサブグライコームを解析する技術の開発によって、細胞や血清の包括的なグライコームを利用した網羅的なバイオマーカ探索等を行ってきた。本申請課題では、申請者が有する独自技術を基盤として組織や体液の包括的なグライコーム(全糖鎖)解析法を確立し、組織横断的な総合グライコームを明らかにする。さらに老化に伴うグライコーム変化と糖鎖合成・代謝に関わる遺伝子発現変動を統合した糖鎖分子ネットワーク変化を指標とした老化の客観的評価法について精査する。