Inhibitory activities of metal chelators on endothelin-converting enzyme. I. In vitro studies.
N Ashizawa, H Okumura, F Kobayashi, T Aotsuka, M Takahashi, R Asakura, K Arai, A Matsuura
Index: Biol. Pharm. Bull. 17(2) , 207-11, (1994)
Full Text: HTML
Abstract
The effects of various metal chelators on endothelin (ET)-converting enzyme (ECE) activity were examined in vitro. Three chelators, 2,3-dimercapto-1-propanol (DMP), toluene-3,4-dithiol (TDT) and 8-mercaptoquinoline (8-MQ), were found to dose-dependently inhibit ECE activity, but this inhibition was much weaker compared with EDTA. In the presence of Zn2+, the inhibitory activity of all these compounds, including EDTA, was abolished. The addition of Ca2+ and Mg2+ markedly attenuated the inhibitory activity of EDTA, but the other three chelators were still able to inhibit ECE. ECE, once inactivated by EDTA or 8-MQ, was reactivated by the addition of divalent cations such as Zn2+ and Mn2+. These compounds also inhibited angiotensin-converting enzyme activity in a manner similar to the inhibition exhibited towards ECE. Chelate-titration indicated that DMP, TDT and 8-MQ chelate Zn2+ but not Ca2+ and Mg2+. These results suggest that the ECE inhibition exhibited by these compounds is mainly attributable to their chelating activities. The metal-selective chelating activity by DMP, TDT and 8-MQ may contribute to the retention of ECE inhibition in the presence of Ca2+ and Mg2+.
Related Compounds
Related Articles:
[J. Chromatogr. A. 652(2) , 187-94, (1994)]
1994-03-01
[Pharmacol. Toxicol. 74(3) , 185-92, (1994)]
Inhibitory activities of metal chelators on endothelin-converting enzyme. II. In vivo studies.
1994-02-01
[Biol. Pharm. Bull. 17(2) , 212-6, (1994)]
Synthesis and coordination chemistry of tetradentate ligands containing two bidentate thioquinoline units: mononuclear complexes with Cu (I) and Cu (II), and a coordination polymer with Cu (I). Tavacoli S, et al.
[Polyhedron 22(4) , 507-14, (2003)]