Cloning, Characterization, and Expression of a G-Protein-Coupled Receptor fromLymnaea stagnalisand Identification of a Leucokinin-Like Peptide, PSFHSWSamide, as Its Endogenous Ligand

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Abstract
Neuropeptides are known to be important signaling molecules in several neural systems of the pond snailLymnaea stagnalis. Although the functions of these peptides have been studied in many neurons, the nature of the postsynaptic signal transduction is mainly unknown. The cloning and characterization of neuropeptide receptors inLymnaeathus would be very valuable in further elucidating peptidergic pathways. Indirect evidence suggests that these neuropeptides operate via G-protein-coupled mechanisms indicating the presence of G-protein-coupled receptors as the initial postsynaptic targets. Here we describe the cloning of a neuropeptide receptor fromLymnaeaand the isolation of an endogenous ligand. This peptide, PSFHSWSamide, belongs to the leucokinin family of peptides, and, thus, thisLymnaeareceptor is the first example of a leucokinin-like neuropeptide receptor, representing a new subfamily of G-protein-coupled neuropeptide receptors.