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(Hypertension. 2003;41:390.)
© 2003 American Heart Association, Inc.

Editorial Commentary

Commentary on Tikellis et al

There Is More to Discover About Angiotensin-Converting Enzyme

From the Hypertension and Vascular Disease Center, Wake Forest University Health Science Center, Winston-Salem, NC.

Correspondence to Carlos M. Ferrario, MD, Hypertension and Vascular Disease Center, Wake Forest University Health Science Center, Winston-Salem, NC 27154. E-mail cferrari@wfubmc.edu

An extract of the first 250 words of the full text is provided, because this article has no abstract.

Irvine H. Page used to say that the regular occurrence of constant amounts of a substance in the body is seldom without purpose and that organisms exhibit an inner economy and prudence by using one substance for several functions. Almost 50 years later, we are now challenged again to decipher just how complicated and how physiologically relevant are newly discovered biochemical pathways contributing to the formation of biologically active forms of angiotensin peptides. The need to revisit the role of angiotensin-forming enzymes was stimulated by the finding of a new gene encoding a protein having highest homology to the testes-specific isoform of angiotensin-converting enzyme (ACE).^1,2

In 1991, we first suggested³ that angiotensin II (Ang II) should be viewed as one but not the sole principal product of the renin-angiotensin system. The proposal was based on the characterization of biological actions of the heptapeptide angiotensin-(1–7) [Ang-(1–7)] and its forming enzymes. There was reluctance to accept this concept in part because the potential role of Ang-(1–7) in cardiovascular regulation was still at an embryonic stage, there was little evidence that Ang II could act at more than one receptor, and a full characterization of other enzymic pathways for angiotensin peptide formation had not been achieved yet. The situation is quite different today; a growing body of literature now implicates Ang-(1–7)^3–7 and angiotensin IV (Ang-3–8)⁸ as components of the system, and additional work has identified chymase, prolyl endopeptidase 24.26, neutral endopeptidase 24.11, metalloendopeptidase 24.15,⁹ and now a homologue of ACE¹⁰ as angiotensin prohormone . . . [Full Text of this Article]

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