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Evolution of the vasopressin/oxytocin superfamily: characterization of a cDNA encoding a vasopressin-related precursor, preproconopressin, from the mollusc Lymnaea stagnalis.
Open accessAbstract
Although the nonapeptide hormones vasopressin, oxytocin, and related peptides from vertebrates and some nonapeptides from invertebrates share similarities in amino acid sequence, their evolutionary relationships are not clear. To investigate this issue, we cloned a cDNA encoding a vasopressin-related peptide, Lys-conopressin, produced in the central nervous system of the gastropod mollusc Lymnaea stagnalis. The predicted preproconopressin has the overall architecture of vertebrate preprovasopressin, with a signal peptide, Lys-conopressin, that is flanked at the C terminus by an amidation signal and a pair of basic residues, followed by a neurophysin domain. The Lymnaea neurophysin and the vertebrate neurophysins share high sequence identity, which includes the conservation of all 14 cysteine residues. In addition, the Lymnaea neurophysin possesses unique structural characteristics. It contains a putative N-linked glycosylation site at a position in the vertebrate neurophysins where a strictly conserved tyrosine residue, which plays an essential role in binding of the nonapeptide hormones, is found. The C-terminal copeptin homologous extension of the Lymnaea neurophysin has low sequence identity with the vertebrate counterparts and is probably not cleaved from the prohormone, as are the mammalian copeptins. The conopressin gene is expressed in only a few neurons in both pedal ganglia of the central nervous system. The conopressin transcript is present in two sizes, due to alternative use of polyadenylylation signals. The data presented here demonstrate that the typical organization of the prohormones of the vasopressin/oxytocin superfamily must have been present in the common ancestors of vertebrates and invertebrates.
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Metadata
- Authors
- van Kesteren, R. E., Smit, A. B., Dirks, R. W., de With, N. D., Geraerts, W. P., & Joosse, J.
- Affiliations
- Faculty of Biology, Vrije Universiteit, Amsterdam, The Netherlands.
- Vrije Universiteit Amsterdam (NL)
- ORCID
- Smit, A B
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1992-05-15
- Volume
- 89
- Issue
- 10
- Pages
- 4593-4597
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC49129
- OpenAlex
- W2155375581
- Cited by
- 120
- References
- 27
- Citations by year
- 2026: 1 · 2025: 2 · 2023: 2 · 2022: 3 · 2021: 5 · 2020: 6 · 2019: 1 · 2018: 2 · 2017: 1 · 2016: 6 · 2015: 6 · 2014: 2 · 2013: 2 · 2012: 2
- FWCI
- 2.58
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
- Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Neuroendocrine regulation and behavior
- Health Sciences › Medicine › Surgery › Cardiovascular, Neuropeptides, and Oxidative Stress Research
- Keywords
- Lymnaea stagnalis, neurophysin, copeptin, N-glycosylation, alternative polyadenylation, pedal ganglia
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, DNA, Biological Evolution, Multigene Family, Humans, Lymnaea, Molecular Sequence Data, Oligodeoxyribonucleotides, Oxytocin, Protein Precursors, RNA, Messenger, Sequence Homology, Nucleic Acid, Vasopressins, Vertebrates, Restriction Mapping, Polymerase Chain Reaction
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