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Originally published In Press as doi:10.1074/jbc.M000767200 on May 31, 2000

J. Biol. Chem., Vol. 275, Issue 34, 26423-26427, August 25, 2000
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Superoxide Regulation of Endothelin-converting Enzyme*

Susana López-OngilDagger , Veronica Senchak§, Marta SauraDagger , Carlos Zaragoza, Michael Ames, Barbara Ballermann§, Manuel Rodríguez-PuyolDagger , Diego Rodríguez-PuyolDagger , and Charles J. Lowenstein||**

From the Divisions of || Cardiology and § Nephrology, the Department of Medicine, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, the Dagger  Department of Physiology, Research Unit and IRSIN, Alcala de Henares University, 28871 Madrid, Spain, and the  Nuclear Reactor Laboratory, Center for Environmental Health Sciences, Massachusetts Institute of Technology, Cambridge, Massachusetts 02138

Reactive oxygen species (ROS) act as signaling molecules in the cardiovascular system, regulating cellular proliferation and migration. However, an excess of ROS can damage cells and alter endothelial cell function. We hypothesized that endogenous mechanisms protect the vasculature from excess levels of ROS. We now show that superoxide can inhibit endothelin-converting enzyme activity (ECE) and decrease endothelin-1 synthesis. Superoxide inhibits ECE but hydrogen peroxide and nitric oxide do not. Superoxide inhibits ECE by ejecting zinc from the enzyme, and the addition of exogenous zinc restores enzymatic activity. Superoxide may inhibit other zinc metalloproteinases by a similar mechanism and may thus play an important role in regulating the biology of blood vessels.

* This work was supported in part by Grant SAF98-0054 from the Comisíon Interministerial de Ciencia y Tecnología (to D. R.-P.), Grant PM97-0067 from the Direccion General de Ensenanza Superior (to M. R. P.), a grant from CAM (to S. L.-O.), National Institutes of Health Grants P50 HL52315 (to C. J. L.), R01 HL5361 (to C. J. L.), and R01 HL63706 (to C. J. L.), the Ciccarone Center for the Prevention of Heart Disease (to C. J. L.), the Cora and John H. Davis Foundation (to C. J. L.), and the Bernard Bernard Foundation (to C. J. L.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

** To whom correspondence should be addressed: Division of Cardiology, Dept. of Medicine, The Johns Hopkins University School of Medicine, 720 Rutland Ave., Baltimore, MD 21205. E-mail: clowenst@jhmi.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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