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(Circulation. 1998;98:2788-2790.)
© 1998 American Heart Association, Inc.

Editorials

Inhibiting Tissue Angiotensin-Converting Enzyme

A Pound of Flesh Without the Blood?

Lawrence S. Zisman, MD

From the Rush Heart Institute, Chicago, Ill.

Correspondence to Lawrence S. Zisman, MD, The Rush Heart Institute, Center for Pulmonary Heart Disease, Rush Presbyterian St Luke's Medical Center, 1725 W Harrison St, Suite 020, Chicago, IL 60612. E-mail lzisman@rush.edu

Key Words: Editorials • heart failure • angiotensin • enzymes • endothelium • bradykinin

"This bond doth give thee here no jot of blood. The words expressly are `a pound of flesh.' "

Portia, in Shakespeare's The Merchant of Venice

Angiotensin-converting enzyme catalyzes the formation of angiotensin II (Ang II) from Ang I but also degrades bradykinin (BK). Ang II, acting through the AT₁ receptor, is a potent vasoconstrictor, stimulates norepinephrine release from sympathetic nerve terminals in the heart, and causes hypertrophy of cardiac myocytes. BK, via activation of the BK₂ receptor, stimulates the release of NO and prostaglandins and may counteract Ang II–mediated effects. ACE inhibition may exert beneficial effects both by interrupting Ang II–mediated AT₁ receptor signal transduction and by augmenting BK₂ receptor activation. Because of the proven survival benefit from ACE-inhibitor therapy in patients with heart failure, great attention has been given to understanding the structure and function of ACE and to the design of optimally effective ACE inhibitors. In this issue of Circulation, Hornig and colleagues¹ compare the effects of 2 such ACE inhibitors, enalaprilat and quinaprilat, on the peripheral circulation in patients with heart failure. To understand the implications of their work, a discussion of the ACE molecule itself, the chemical structure of ACE inhibitors, and their interaction with ACE is required. The major issue to be examined is the proposed dichotomy between high- and low-affinity tissue ACE inhibitors.

In somatic tissues, ACE is a glycoprotein of 140 kDa; in testicular cells, it is synthesized from the same gene but at an alternative transcription start site that results . . . [Full Text of this Article]

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