研究者業績

川口 眞理

カワグチ マリ  (Kawaguchi Mari)

基本情報

所属
上智大学 理工学部物質生命理工学科 准教授
学位
修士(理学)(東京都立大学)
博士(理学)(上智大学)

研究者番号
00612095
J-GLOBAL ID
201301084945465719
researchmap会員ID
7000004358

外部リンク

2008年~2011年 東京大学大気海洋研究所
   「孵化酵素と卵膜の分子共進化」

2011年~現在 上智大学理工学部物質生命理工学科
   「魚類の繁殖戦略の進化」

(研究テーマ)
魚類の繁殖戦略の進化


論文

 54
  • Yukie Yokota, Nazuna Itabashi, Mari Kawaguchi, Hiroshi Uchida, Nick Serpone, Satoshi Horikoshi
    Molecules 30(9) 1871-1871 2025年4月22日  査読有り
    In a ground-breaking recent study, we unveiled the remarkable cellular uptake of 60 nm ZnO and TiO2 nanoparticles by NIH/3T3 mouse skin fibroblasts under microwave irradiation. Even more stimulating is our current demonstration of the potent ability of Ag nanoparticles (147 nm) and Au nanoparticles (120 nm) to stifle the growth of Escherichia coli (E. coli—a prokaryote whose cells lack a membrane-bound nucleus and other membrane-bound organelles), vastly smaller than the NIH/3T3 cells, when exposed to significantly optimized low-power microwave irradiation conditions. Our rigorous assessment of the method’s effectiveness involved scrutinizing the growth rate of E. coli bacteria under diverse conditions involving silver and gold nanoparticles. This indisputably underscores the potential of microwave–nanoparticle interactions in impeding bacterial proliferation. Furthermore, our noteworthy findings on the uptake of fluorescent organosilica nanoparticles by E. coli cells following brief, repeated microwave irradiation highlight the bacteria’s remarkable ability to assimilate extraneous substances.
  • Tatsuki Nagasawa, Nagatoshi Machii, Mitsuto Aibara, Mari Kawaguchi, Shigeki Yasumasu, Masato Nikaido
    Authorea (preprint) 2025年3月  
  • Sakuto Yamanaka, Mari Kawaguchi, Shigeki Yasumasu, Kenji Sato, Masato Kinoshita
    Journal of Experimental Zoology Part B: Molecular and Developmental Evolution 2025年1月  査読有り
  • Shigeki Yasumasu, Miyuki Horie, Mayuko Horie, Kodai Sakuma, Chihiro Sato, Hikari Sato, Taiki Nakajima, Tatsuki Nagasawa, Mari Kawaguchi, Ichiro Iuchi
    The Journal of Biochemistry 2024年9月16日  査読有り
    Abstract During the fertilization of fish eggs, the hardening of the egg envelope is mediated by transglutaminase (hTGase). After fertilization, TGase undergoes processing. We isolated hTGase from extracts of unfertilized and water-activated rainbow trout eggs. Rainbow trout hTGase (Rt-hTGase) appeared as an 80 kDa protein, and its processed form was 55 kDa. Their N-terminal amino acid sequences were nearly identical, suggesting processing in the C-terminal region. The specific activities were not significantly different, indicating that C-terminal processing does not activate the enzyme itself. We cloned the cDNA by reverse transcription polymerase chain reaction (RT-PCR) using degenerate primers followed by RACE-PCR. The deduced amino acid sequence of the cDNA was similar to that of factor XIII subunit A (FXIIIA). Molecular phylogenetic and gene syntenic analyses clearly showed that hTGase was produced by duplication of FXIIIA during the evolution to Teleostei. The 55 kDa processed form of Rt-hTGase is predominantly composed of an enzyme domain predicted from the amino acid sequence of the cDNA. It is hypothesized that the C-terminal domain of Rt-hTGase binds to egg envelope proteins, and that processing allows the enzyme to move freely within the egg envelope, increasing substrate–enzyme interaction and thereby accelerating hardening.
  • Christian Nanga Chick, Yusuke Sasaki, Mari Kawaguchi, Eri Tanaka, Takako Niikura, Toyonobu Usuki
    Bioorganic & Medicinal Chemistry 90 117351-117351 2023年7月  査読有り責任著者

MISC

 13

書籍等出版物

 5

講演・口頭発表等

 149

共同研究・競争的資金等の研究課題

 21

社会貢献活動

 5

メディア報道

 16