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First published online October 5, 2007
Journal of Experimental Biology 210, 3601-3606 (2007)
Published by The Company of Biologists 2007
doi: 10.1242/jeb.009035
Male accessory glands of Drosophila melanogaster make a secreted angiotensin I-converting enzyme (ANCE), suggesting a role for the peptide-processing enzyme in seminal fluid

1 Institute of Integrative and Comparative Biology, Faculty of Biological
Sciences, University of Leeds, Leeds LS2 9JT, UK
2 Institute of Molecular and Cellular Biology, Faculty of Biological
Sciences, University of Leeds, Leeds LS2 9JT, UK
3 Department of Biological Sciences, Lancaster University, Lancaster, LA1
4YQ, UK
Author for correspondence (e-mail:
r.e.isaac{at}leeds.ac.uk)
Accepted 26 July 2007
Angiotensin I-converting enzyme (ACE) expressed on the surface of endothelial cells is responsible for the last step in the synthesis of circulating angiotensin II and the inactivation of bradykinin. Mammalian ACE is also expressed in the prostate with other components of the renin–angiotensin system, and in developing spermatids, where the peptidase activity is known to be critical for normal sperm function. The importance of an ACE gene to male fertility has also been demonstrated in Drosophila melanogaster, where Ance is expressed in spermatids, and hypomorphic alleles of Ance cause a defect in spermiogenesis. Here we show that ANCE, which shares many enzymatic properties with mammalian ACE, is also a product of the male accessory gland of D. melanogaster. It is expressed in the secondary cells and is associated with the electron dense granule within the large vesicles of these cells. ACE proteolytic activity is lost from the accessory glands during mating, consistent with transfer to the mated female in the seminal fluid. The accessory gland ACE-like activity might have an evolutionarily conserved function processing biologically active peptides with a role in male fertility.
Key words: Drosophila, male accessory gland, angiotensin I-converting enzyme, dicarboxypeptidase, ANCE