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(Circulation. 1997;95:14-16.)
© 1997 American Heart Association, Inc.

Articles

Modulation of Myocardial Oxygen Consumption Through ACE Inhibitors

NO Effect?

Jørn Bech Laursen, MD; David G. Harrison, MD

the Department of Medicine, Emory University School of Medicine (J.B.L., D.G.H.), Atlanta, Ga; the Atlanta Veterans Administration Medical Center (D.G.H.), Atlanta, Ga; and Medical Department B, Division of Cardiology (J.B.L.), Rigshospitalet, Denmark.

Correspondence to David G. Harrison, Professor of Medicine, Cardiology Division, Emory University School of Medicine, Atlanta, GA 30322.

Key Words: Editorials • endothelium-derived factors • angiotensin

	Introduction

 
In this issue of Circulation,¹ Zhang and coworkers provide convincing evidence that ACE inhibitors reduce myocardial oxygen consumption by preventing the degradation of bradykinin, which subsequently stimulates the release of nitric oxide (NO). They propose that NO inhibits mitochondrial respiration, thus reducing myocyte oxygen use. This is an exciting observation because it provides a new mechanism whereby ACE inhibitors might benefit ischemia beyond simply inhibiting the formation of angiotensin II, thus reducing the vasoconstrictor effect of this octapeptide. These results are further evidence for a role of bradykinin in the response of tissues to ACE inhibitors. The mechanism enabling these interactions to occur is coming to light on the basis of studies such as the current one from Zhang et al.

Interest in bradykinin and related kinins as cardiovascular mediators has grown tremendously in the past several years, largely because it has been recognized that they potently stimulate release of NO and prostacyclin from endothelial cells. Bradykinin and Lys-bradykinin, respectively, are formed when one of a family of enzymes, known as kallikreins, act on either heavy- or low-molecular-weight kininogens.² This action involves cleavage of amino acids from both the C- and N-terminal ends of the kininogen peptides and takes place both in plasma (for heavy-molecular-weight kininogen) and tissues (for low-molecular-weight kininogen). The kininogens were previously thought to be expressed primarily by hepatocytes; however, it is now clear that many tissues, including vascular cells^{3 4} and the heart,⁵ also express kininogens. The kallikreins as well are made by many cell types . . . [Full Text of this Article]

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