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Originally published In Press as doi:10.1074/jbc.M004006200 on May 30, 2000

J. Biol. Chem., Vol. 275, Issue 34, 26259-26264, August 25, 2000
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Physiological Non-equivalence of the Two Isoforms of Angiotensin-converting Enzyme*

Sean P. KesslerDagger , Theresa M. RoweDagger , Janette B. GomosDagger , Patricia M. Kessler§, and Ganes C. SenDagger

From the Departments of Dagger  Molecular Biology and § Cancer Biology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195

The structurally related somatic and germinal isoforms of angiotensin-converting enzyme (ACE) contain the same catalytic active center and are encoded by the same gene, whose disruption causes renal atrophy, hypotension, and male sterility. The reason for the evolutionary conservation of both isozymes is an enigma, because, in vitro, they have very similar enzymatic properties. Despite the common enzymatic properties, discrete expression of both isoforms is maintained in alternate cell types. We have previously shown that sperm-specific expression of transgenic germinal ACE in Ace -/- male mice restores fertility without curing their other abnormalities (Ramaraj, P., Kessler, S. P., Colmenares, C. & Sen, G. C. (1998) J. Clin. Invest. 102, 371-378). In this report we tested the biological equivalence of somatic ACE and germinal ACE utilizing an in vivo isozymic substitution approach. Here we report that restoration of male fertility was not achieved by the transgenic expression of enzymatically active, somatic ACE in the sperm of Ace -/- mice. Therefore, the requisite physiological functions of the two tissue-specific isozymes of ACE are not interchangeable.

* This work was supported by National Institutes of Health Grant HL 48258.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: Dept. of Molecular Biology, NC20, Lerner Research Institute, 9500 Euclid Ave., Cleveland, OH 44195. Tel.: 216-444-0636; Fax: 216-444-0513; E-mail: seng@ccf.org.

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