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Next Article 
Volume 17, Number 4,
Issue of February 15, 1997
pp. 1197-1205
Copyright ©1997 Society for Neuroscience
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
Received July 9, 1996; revised Nov. 7, 1996; accepted Nov. 22, 1996.
Kingsley J. A. Cox1,
Cornelis P. Tensen2,
Roel
C. Van der Schors4,
Ka Wan Li4,
Harm van
Heerikhuizen3,
Erno Vreugdenhil3,
Wijnand P. M. Geraerts4, and
Julian F. Burke1
1 Sussex Centre for Neuroscience, School of Biological
Sciences, University of Sussex, Brighton BN1 9QG, United Kingdom,
2 Amsterdam Leiden Institute for Immunology, Vrije
Universiteit Hospital, 1081 HV Amsterdam, The Netherlands, and
Departments of 3 Biochemistry and 4 Molecular
Neurobiology, Graduate School of Neurosciences Amsterdam, Institute of
Neuroscience, Vrije Universiteit, 1081 HV Amsterdam, The Netherlands
Neuropeptides are known to be important signaling molecules in
several neural systems of the pond snail Lymnaea
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 in Lymnaea thus 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 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 subfamily of G-protein-coupled
neuropeptide receptors.
Key words:
neuropeptide receptor;
mollusc;
CHO-K1;
HPLC;
calcium;
neural networks
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