Abstract
THE peptide Phe-Met-Arg-Phe-NH2 (FMRFamide) and structurally related peptides are present both in invertebrate and vertebrate nervous systems1,2. Although they constitute a major class of invertebrate peptide neurotransmitters3, the molecular structure of their receptors has not yet been identified. In neurons of the snail Helix aspersa4, as well as in Aplysia bursting5 and motor6 neurons, FMRFamide induces a fast excitatory depolarizing response due to direct activation of an amiloride-sensitive Na+ channel4. We have now isolated a complementary DNA from Helix nervous tissue; when expressed in Xenopus oocytes, it encodes an FMRF-amide-activated Na+ channel (FaNaCh) that can be blocked by amiloride. The corresponding protein shares a very low sequence identity with the previously cloned epithelial Na+ channel subunits7â12 and Caenorhabditis elegans degenerins13â15, but it displays the same overall structural organization. To our knowledge, this is the first characterization of a peptide-gated ionotropic receptor.
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Lingueglia, E., Champigny, G., Lazdunski, M. et al. Cloning of the amiloride-sensitive FMRFamide peptide-gated sodium channel. Nature 378, 730â733 (1995). https://doi.org/10.1038/378730a0
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DOI: https://doi.org/10.1038/378730a0
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