Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Caenorhabditis elegans / genetics
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Caenorhabditis elegans / metabolism*
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Caenorhabditis elegans Proteins / chemistry
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Caenorhabditis elegans Proteins / genetics
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Caenorhabditis elegans Proteins / metabolism
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Calcium Signaling / drug effects
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Cell Line
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Cloning, Molecular
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Dose-Response Relationship, Drug
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Fluorescence
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Humans
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Molecular Sequence Data
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Neuropeptides / genetics
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Neuropeptides / metabolism*
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Neuropeptides / pharmacology
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Peptide Library
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Phylogeny
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Receptors, G-Protein-Coupled / chemistry
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Receptors, G-Protein-Coupled / genetics
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Receptors, G-Protein-Coupled / metabolism*
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Receptors, Peptide / chemistry
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Receptors, Peptide / genetics
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Receptors, Peptide / metabolism*
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Sequence Alignment
Substances
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Caenorhabditis elegans Proteins
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Neuropeptides
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Peptide Library
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Receptors, G-Protein-Coupled
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Receptors, Peptide
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VRFamide receptor 1, C elegans