Fundamental Toxicological Sciences

Paper Details

Fundamental Toxicological Sciences
Vol. 5 No. 6 December 11, 2018 p.181-184
A zinc complex that suppresses the expression of a reactive sulfur species-producing enzyme, cystathionine γ-lyase, in cultured vascular endothelial cells
  • Toshiyuki Kaji (Faculty of Pharmaceutical Sciences, Tokyo University of Science /
Akane Takahashi 1) , Musubu Takahashi 1) , Tomoya Fujie 2) , Takato Hara 2) , Eiko Yoshida 1) , Chika Yamamoto 2) , Toshiyuki Kaji 1)
1) Faculty of Pharmaceutical Sciences, Tokyo University of Science , 2) Faculty of Pharmaceutical Sciences, Toho University
Keywords: Zinc complex, Cystathionine γ-lyase, Cystathionine β-synthase, Reactive sulfur species, Vascular endothelial cell

Persulfide species present in mammalian cells play important toxicological roles against oxidative stress and methylmercury. Cystathionine γ-lyase (CSE) and cystathionine β-synthase (CBS) are enzymes that produce persulfide species using cysteine as a substrate in the presence of vitamin B6. However, little is known about the regulatory mechanisms underlying the expression of these enzymes. In the present study, we searched for molecular probes from a library of 27 zinc complexes to analyze the mechanisms in vascular endothelial cells. We found dichloro(1,10-phenanthroline)zinc(II), termed Zn11, as a zinc complex that suppressed endothelial CSE expression without any change in CBS expression. This zinc complex can be used as molecular probes to analyze the regulation underlying endothelial CSE expression.