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The first peptide-gated ion channel

¹School of Biomedical Sciences, University of St Andrews, Fife, UK. gac@st-and.ac.uk

The Journal of Experimental Biology

|October 31, 1997

Summary

The neuropeptide Phe-Met-Arg-Phe-NH2 (FMRFamide) directly opens a sodium (Na+) channel, identified as FaNaCh. This discovery reveals the first peptide-gated ion channel, crucial for fast excitatory signaling in neurons.

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Area of Science:

Neuroscience
Molecular Biology
Ion Channel Physiology

Background:

Neuropeptides like Phe-Met-Arg-Phe-NH2 (FMRFamide) modulate neuronal activity.
The precise mechanism of FMRFamide's excitatory action on specific ion channels was unclear.

Purpose of the Study:

To identify and characterize the ion channel directly gated by FMRFamide.
To provide the first evidence of a peptide-gated ion channel.

Main Methods:

Patch-clamp electrophysiology on Helix aspersa neurons.
cDNA cloning and sequencing of the FMRFamide-gated sodium channel (FaNaCh).
Expression and functional characterization of FaNaCh in Xenopus laevis oocytes.

Main Results:

FMRFamide directly gates an amiloride-sensitive Na+ channel in C2 neurons.
The cloned FaNaCh cDNA sequence encodes a protein with two transmembrane domains.
Expressed FaNaCh in oocytes responded to FMRFamide, confirming its identity.
FKRFamide acted as an effective antagonist for both native and expressed channels.

Conclusions:

This study presents the first direct evidence for a peptide-gated ion channel (FaNaCh).
FaNaCh is responsible for the fast excitatory effects of FMRFamide.
Homologs of FaNaCh exist across diverse species, suggesting conserved functions.

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