A Crucial Role in Fertility for the Oyster Angiotensin- Converting Enzyme Orthologue CgACE
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 fro...
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ftciteseerx:oai:CiteSeerX.psu:10.1.1.287.1953 2023-05-15T15:58:11+02:00 A Crucial Role in Fertility for the Oyster Angiotensin- Converting Enzyme Orthologue CgACE Guillaume Riviere Re Fellous Alban Franco Benoit Bernay Pascal Favrel The Pennsylvania State University CiteSeerX Archives application/zip http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.287.1953 en eng http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.287.1953 Metadata may be used without restrictions as long as the oai identifier remains attached to it. ftp://ftp.ncbi.nlm.nih.gov/pub/pmc/43/ea/PLoS_One_2011_Dec_9_6(12)_e27833.tar.gz text ftciteseerx 2016-01-07T21:20:31Z 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 59-RACE revealed that the 1.9 kb cDNA encodes CgACE, 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 CgACE 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 CgACE 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 CgACE, which is increased in the gonad during spermatogenesis. The use of ACE inhibitors in vivo indicates that the dipeptidase activity of CgACE 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 Text Crassostrea gigas Unknown |
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English |
description |
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 59-RACE revealed that the 1.9 kb cDNA encodes CgACE, 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 CgACE 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 CgACE 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 CgACE, which is increased in the gonad during spermatogenesis. The use of ACE inhibitors in vivo indicates that the dipeptidase activity of CgACE 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 |
author2 |
The Pennsylvania State University CiteSeerX Archives |
format |
Text |
author |
Guillaume Riviere Re Fellous Alban Franco Benoit Bernay Pascal Favrel |
spellingShingle |
Guillaume Riviere Re Fellous Alban Franco Benoit Bernay Pascal Favrel A Crucial Role in Fertility for the Oyster Angiotensin- Converting Enzyme Orthologue CgACE |
author_facet |
Guillaume Riviere Re Fellous Alban Franco Benoit Bernay Pascal Favrel |
author_sort |
Guillaume Riviere |
title |
A Crucial Role in Fertility for the Oyster Angiotensin- Converting Enzyme Orthologue CgACE |
title_short |
A Crucial Role in Fertility for the Oyster Angiotensin- Converting Enzyme Orthologue CgACE |
title_full |
A Crucial Role in Fertility for the Oyster Angiotensin- Converting Enzyme Orthologue CgACE |
title_fullStr |
A Crucial Role in Fertility for the Oyster Angiotensin- Converting Enzyme Orthologue CgACE |
title_full_unstemmed |
A Crucial Role in Fertility for the Oyster Angiotensin- Converting Enzyme Orthologue CgACE |
title_sort |
crucial role in fertility for the oyster angiotensin- converting enzyme orthologue cgace |
url |
http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.287.1953 |
genre |
Crassostrea gigas |
genre_facet |
Crassostrea gigas |
op_source |
ftp://ftp.ncbi.nlm.nih.gov/pub/pmc/43/ea/PLoS_One_2011_Dec_9_6(12)_e27833.tar.gz |
op_relation |
http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.287.1953 |
op_rights |
Metadata may be used without restrictions as long as the oai identifier remains attached to it. |
_version_ |
1766393916815310848 |