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Angiotensin-converting enzyme (ACE) is a highly conserved metallopeptidase. In mammals, the somatic isoform governs blood pressure whereas the germinal isoform (tACE) is required for fertility. In Ecdysozoans, ACE-like enzymes are implicated in reproduction. Despite ACE orthologues being present from bacteria to humans, their function(s) remain(s) unknown in distant organisms such as Lophotrochozoans.  In silico  analysis of an oyster ( Crassostrea gigas)  EST library suggested the presence of an ACE orthologue in molluscs. Primer walking and 5′-RACE revealed that the 1.9 kb cDNA encodes  Cg ACE, a 632 amino acid protein displaying a conserved single active site and a putative C-terminal transmembrane anchor, thus resembling human tACE, as supported by molecular modelling. FRET activity assays and Maldi-TOF spectrometry indicated that  Cg ACE is a functional dipeptidyl-carboxypeptidase which is active on Angiotensin I and sensitive to ACE inhibitors and chloride ion concentration. Immunocytochemistry revealed that, as its human counterpart, recombinant  Cg ACE is synthesised as a transmembrane enzyme. RT-qPCR,  in-situ  hybridization and immunohistochemistry shed light on a tissue, and development stage, specific expression pattern for  Cg ACE, which is increased in the gonad during spermatogenesis. The use of ACE inhibitors  in vivo  indicates that the dipeptidase activity of  Cg ACE is crucial for the oyster fertilization. Our study demonstrates that a transmembrane active ACE is present in the oyster  Crassostrea gigas , and for the first time ascribes a functional role for ACE in Lophotrochozoans. Its biological function in reproduction is conserved from molluscs to humans, a finding of particular evolutionary interest especially since oysters represent the most important aquaculture resource worldwide.

A Crucial Role in Fertility for the Oyster Angiotensin-Converting Enzyme Orthologue CgACE