Functional characterization of the putative orphan neuropeptide G-protein coupled receptor C26F1.6 in Caenorhabditis elegans

In this study, we describe the cloning and the characterization of the third FMRFamide-related peptide (FaRP) receptor in Caenorhabditis elegans, the VRFa receptor 1. Numerous structurally different FaRPs were synthesized and used to screen the orphan C26F1.6 receptor for activation. Two peptides en...

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Bibliographic Details
Published in:FEBS letters 2004-08, Vol.573 (1), p.55-60
Main Authors: Mertens, Inge, Vandingenen, Anick, Meeusen, Tom, Janssen, Tom, Luyten, Walter, Nachman, Ronald J., De Loof, Arnold, Schoofs, Liliane
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Binding Sites
Caenorhabditis elegans
Caenorhabditis elegans - genetics
Caenorhabditis elegans - metabolism
Caenorhabditis elegans Proteins - chemistry
Caenorhabditis elegans Proteins - genetics
Caenorhabditis elegans Proteins - metabolism
Calcium Signaling - drug effects
Cell Line
CHO, Chinese hamster ovary
Cloning, Molecular
Dose-Response Relationship, Drug
Drm-sNPF-R, Drosophila melanogaster short Neuropeptide F receptor
FaRPs, FMRFamide-related peptides
flp, FMRFamide-like protein gene
Fluorescence
FMRFamide related peptide
G16, G-protein 16
GPCR, G-protein coupled receptor
Humans
Molecular Sequence Data
Neuropeptides - genetics
Neuropeptides - metabolism
Neuropeptides - pharmacology
Peptide Library
Phylogeny
Receptors, G-Protein-Coupled - chemistry
Receptors, G-Protein-Coupled - genetics
Receptors, G-Protein-Coupled - metabolism
Receptors, Peptide - chemistry
Receptors, Peptide - genetics
Receptors, Peptide - metabolism
Reverse pharmacology
Sequence Alignment
VRF-amide receptor 1
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Description
Summary:In this study, we describe the cloning and the characterization of the third FMRFamide-related peptide (FaRP) receptor in Caenorhabditis elegans, the VRFa receptor 1. Numerous structurally different FaRPs were synthesized and used to screen the orphan C26F1.6 receptor for activation. Two peptides ending in M(orL)VRFamide elicited a calcium response in receptor expressing mammalian cells. The response is dose-dependent and appeared to be very specific, since very closely related FaRPs were less active, even the other peptides ending in M(orL)VRFamide. Pharmacological profiling of the most active peptide suggests that SMVRFa is the most active binding core. N-terminal extension decreases peptide activity.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2004.07.058