A novel G protein-coupled receptor mediating both vasopressin- and oxytocin-like functions of Lys-conopressin in Lymnaea stagnalis
@article{Kesteren1995ANG, title={A novel G protein-coupled receptor mediating both vasopressin- and oxytocin-like functions of Lys-conopressin in Lymnaea stagnalis}, author={Ronald E. van Kesteren and Cornelis P. Tensen and August Benjamin Smit and J. H. van Minnen and Paul F. van Soest and Karel S. Kits and Wolfgang Meyerhof and Dietmar Richter and Harm van Heerikhuizen and Erno Vreugdenhil and Wijnand P. M. Geraerts}, journal={Neuron}, year={1995}, volume={15}, pages={897-908} }
79 Citations
Co-evolution of Ligand-Receptor Pairs in the Vasopressin/Oxytocin Superfamily of Bioactive Peptides (*)
- BiologyThe Journal of Biological Chemistry
- 1996
A theory of the molecular co-evolution of the functionally distinct ligand-receptor pairs of the vasopressin/oxytocin superfamily of bioactive peptides is provided.
Vasopressin/oxytocin-related conopressin induces two separate pacemaker currents in an identified central neuron of Lymnaea stagnalis.
- BiologyJournal of neurophysiology
- 1997
The results suggest that two distinct conopressin receptors are involved in the activation of both currents, and induce or enhance a region of negative slope resistance in the steady-state current-voltage relation.
Activation of protein kinase C by oxytocin-related conopressin underlies pacemaker current in Lymnaea central neurons.
- BiologyJournal of neurophysiology
- 2000
It is concluded that conopressin activates the ion channels carrying I(LVA) and I (HVA) through different second-messenger cascades and that PKC-dependent phosphorylation underlies activation of I(HVA).
The Lymnaea Cardioexcitatory Peptide (LyCEP) Receptor: A G-Protein–Coupled Receptor for a Novel Member of the RFamide Neuropeptide Family
- BiologyThe Journal of Neuroscience
- 1998
Data confirm that LyCEP is an RFamide ligand for GRL106, and shows significant similarity to the Achatina cardioexcitatory peptide as well as to the recently identified family of mammalian prolactin-releasing peptides.
Identification of a novel receptor for an invertebrate oxytocin/vasopressin superfamily peptide: molecular and functional evolution of the oxytocin/vasopressin superfamily.
- BiologyThe Biochemical journal
- 2004
The identification of an endogenous AnR (annetocin receptor) and the first description concerning the functional correlation between an invertebrate OT/VP-related peptide and egg-laying behaviour are described.
Cloning, expression and pharmacological characterization of a vasopressin-related receptor in an annelid, the leech Theromyzon tessulatum.
- BiologyThe Journal of endocrinology
- 2005
The characterization of a novel AVP/OT superfamily receptor in annelids is described, which is considered the most distant group of coelomate metazoans possessing a functional A VP/OT-related endocrine system.
Cloning , expression and pharmacological characterization of a vasopressin-related receptor in an annelid , the leech Theromyzon
- Biology
- 2004
The characterization of a novel AVP/OT superfamily receptor in annelids is described, which is considered the most distant group of coelomate metazoans possessing a functional A VP/OT-related endocrine system.
Novel evolutionary lineages of the invertebrate oxytocin/vasopressin superfamily peptides and their receptors in the common octopus (Octopus vulgaris).
- BiologyThe Biochemical journal
- 2005
The findings suggest that the CT and OP genes, similar to the OT/VP family, evolved through duplication, but the ligand-receptor selectivity were established through different evolutionary lineages from those of their vertebrate counterparts.
A vasopressin/oxytocin-related conopeptide with γ-carboxyglutamate at position 8
- Biology
- 2007
NMR spectroscopy of the peptide isolated directly from the cone snails revealed that the native γ-conopressin-vil undergoes structural changes in the presence of calcium, which suggests that the peptides binds calcium, and the calcium-binding process is mediated by the ε-carboxyglutamate residue.
References
SHOWING 1-10 OF 60 REFERENCES
Co-localized neuropeptides conopressin and ALA-PRO-GLY-TRP-NH2 have antagonistic effects on the vas deferens of lymnaea
- BiologyNeuroscience
- 1995
Receptors for neuropeptides are induced by exogenous poly(A)+ RNA in oocytes from Xenopus laevis.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 1988
This work has suggested that the V1-type (liver), not the V2- type (kidney), vasopressin receptor can be expressed and electrophysiologically identified in the oocyte, and that the drug chlordiazepoxide suppressed the thyrotropin-releasing hormone response.
Structural and functional evolution of the vasopressin/oxytocin superfamily: vasopressin-related conopressin is the only member present in Lymnaea, and is involved in the control of sexual behavior
- BiologyThe Journal of neuroscience : the official journal of the Society for Neuroscience
- 1995
It is suggested that invertebrates contain only a single member of the vasopressin/oxytocin gene family and that the amino acid change that distinguishes vasopressingin from oxytocin is functionally neutral in invertebrate species.
Molecular cloning and functional characterization of V2 [8-lysine] vasopressin and oxytocin receptors from a pig kidney cell line.
- BiologyEuropean journal of biochemistry
- 1993
The molecular cloning of the V2 [Lys8]VP receptor and the oxytocin receptor from LLC-PK1 cells is reported, revealing a single 5.5-kb transcript in the uterus from pregnant guinea pig and a ligand specificity typical of mammalian Oxytocin receptors.
Molecular cloning and expression of a rat Via arginine vasopressin receptor
- Biology, MedicineNature
- 1992
The cloning of a complementary DNA encoding the liver cDNA encodes a protein with seven putative transmembrane domains, which binds arginine vasopressin and related compounds with affinities similar to the native rat Via receptor.
Molecular cloning and functional expression of a cDNA encoding the human V1b vasopressin receptor.
- Biology, MedicineThe Journal of biological chemistry
- 1994
A vasotocin-like peptide in Aplysia kurodai ganglia: HPLC and RIA evidence for its identity with Lys-conopressin G
- BiologyPeptides
- 1992
Evolution of the vasopressin/oxytocin superfamily: characterization of a cDNA encoding a vasopressin-related precursor, preproconopressin, from the mollusc Lymnaea stagnalis.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 1992
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.
Structure, function, and phylogeny of [Arg8]vasotocin receptors from teleost fish and toad.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 1994
The presence of a 5.0-kb transcript in various teleost tissues points to a physiological role for the fish AVT receptor in metabolic, osmoregulatory, and sensory processes and shows that it represents, or is closely related to, an ancestral nonapeptide receptor.
Cloning and characterization of a vasopressin V2 receptor and possible link to nephrogenic diabetes insipidus
- Biology, MedicineNature
- 1992
The cloning of the rat kidney V2 AVP receptor complementary DNA that encodes a 370-amino-acid protein with a transmembrane topography characteristic of G protein-coupled receptors, and with similarity to the Via (hepatic) AVP receptors2 in its seven membrane-spanning domains is reported.