Kazue Terasawa

Publications (2)9 Total impact

• Article: Sphingosine kinase 2 inhibitor SG-12 induces apoptosis via phosphorylation by sphingosine kinase 2.

  Miki Hara-Yokoyama, Kazue Terasawa, Shizuko Ichinose, Akihiko Watanabe, Katarzyna A Podyma-Inoue, Kazunari Akiyoshi, Yasuyuki Igarashi, Masaki Yanagishita
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  ABSTRACT: Sphingosine kinase (SPHK), which catalyzes the phosphorylation of sphingosine to generate sphingosine 1-phosphate, has two mammalian isotypes, SPHK1 and SPHK2. Both isozymes are promising anti-cancer therapeutic targets. In this report, we found that SG-12, a synthetic analogue of sphingosine that acts as a SPHK2 inhibitor, induces apoptosis via phosphorylation by SPHK2. The present results revealed the novel anti-cancer potential of a sphingosine analogue in the pathological setting where SPHK2 is upregulated.
  Bioorganic & medicinal chemistry letters 01/2013; · 2.65 Impact Factor
• Article: Tetrameric interaction of the ectoenzyme CD38 on the cell surface enables its catalytic and raft-association activities.

  Miki Hara-Yokoyama, Mutsuko Kukimoto-Niino, Kazue Terasawa, Satoru Harumiya, Katarzyna A Podyma-Inoue, Nobumasa Hino, Kensaku Sakamoto, Satsuki Itoh, Noritaka Hashii, Yoko Hiruta, [......], Motoaki Wakiyama, Mikako Shirouzu, Takeshi Kasama, Hiroshi Takayanagi, Naoko Utsunomiya-Tate, Kiyoshi Takatsu, Toshiaki Katada, Yoshio Hirabayashi, Shigeyuki Yokoyama, Masaki Yanagishita
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  ABSTRACT: The leukocyte cell-surface antigen CD38 is the major nicotinamide adenide dinucleotide glycohydrolase in mammals, and its ectoenzyme activity is involved in calcium mobilization. CD38 is also a raft-dependent signaling molecule. CD38 forms a tetramer on the cell surface, but the structural basis and the functional significance of tetramerization have remained unexplored. We identified the interfaces contributing to the homophilic interaction of mouse CD38 by site-specific crosslinking on the cell surface with an expanded genetic code, based on a crystallographic analysis. A combination of the three interfaces enables CD38 to tetramerize: one interface involving the juxtamembrane α-helix is responsible for the formation of the core dimer, which is further dimerized via the other two interfaces. This dimerization of dimers is required for the catalytic activity and the localization of CD38 in membrane rafts. The glycosylation prevents further self-association of the tetramer. Accordingly, the tetrameric interaction underlies the multifaceted actions of CD38.
  Structure 08/2012; 20(9):1585-95. · 6.35 Impact Factor