Cox K J, Tensen C P, Van der Schors R C, Li K W, van Heerikhuizen H, Vreugdenhil E, Geraerts W P, Burke J F
Sussex Centre for Neuroscience, School of Biological Sciences, University of Sussex, Brighton BN1 9QG, United Kingdom.
J Neurosci. 1997 Feb 15;17(4):1197-205. doi: 10.1523/JNEUROSCI.17-04-01197.1997.
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.
已知神经肽是椎实螺神经系统中的重要信号分子。尽管这些肽的功能已在许多神经元中得到研究，但突触后信号转导的本质仍主要未知。因此，椎实螺神经肽受体的克隆和表征对于进一步阐明肽能途径非常有价值。间接证据表明，这些神经肽通过G蛋白偶联机制发挥作用，这表明存在G蛋白偶联受体作为最初的突触后靶点。在此，我们描述了从椎实螺中克隆神经肽受体以及分离内源性配体的过程。这种肽，PSFHSWSamide，属于亮氨酸激肽家族肽，因此，这种椎实螺受体是亮氨酸激肽样神经肽受体的首个例子，代表了G蛋白偶联神经肽受体的一个新亚家族。
