- Toshiyuki Kaji (Faculty of Pharmaceutical Sciences, Tokyo University of Science / firstname.lastname@example.org)
1) Faculty of Pharmaceutical Sciences, Tokyo University of Science , 2) Faculty of Pharmaceutical Sciences, Toho University
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.