CLONING, CHARACTERIZATION, AND EXPRESSION OF A G-PROTEIN-COUPLED RECEPTOR FROM LYMNAEA-STAGNALIS AND IDENTIFICATION OF A LEUCOKININ-LIKE PEPTIDE, PSFHSWSAMIDE, AS ITS ENDOGENOUS LIGAND
Kja. Cox et al., CLONING, CHARACTERIZATION, AND EXPRESSION OF A G-PROTEIN-COUPLED RECEPTOR FROM LYMNAEA-STAGNALIS AND IDENTIFICATION OF A LEUCOKININ-LIKE PEPTIDE, PSFHSWSAMIDE, AS ITS ENDOGENOUS LIGAND, The Journal of neuroscience, 17(4), 1997, pp. 1197-1205
Neuropeptides are known to be important signaling molecules in several
neural systems of the pond snail Lymnaea stagnalis. Although the func
tions 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 in Lymnaea thus would
be very valuable in further elucidating peptidergic pathways. Indirect
evidence suggests that these neuropeptides operate via G-protein-coup
led mechanisms indicating the presence of G-protein-coupled receptors
as the initial postsynaptic targets. Here we describe the cloning of a
neuropeptide receptor from Lymnaea and the isolation of an endogenous
ligand. This peptide, PSFHSWSamide, belongs to the leucokinin family
of peptides, and, thus, this Lymnaea receptor is the first example of
a leucokinin-like neuropeptide receptor, representing a new sub-family
of G-protein-coupled neuropeptide receptors.