THE FMRFamide-LIKE NEUROPEPTIDE OF APLYSIA IS FMRFamide

Abstract

The head ganglia from 350 A. brasiliana were extracted and purified by gel (Sephadex G-15) and cation exchange (CM-Sephadex) chromatography; the fractions were examined with radioimmunoassays (RIA) for the molluscan neuropeptides, phenylalanylmethionylarginylphenylalainamide (FMRFamide) and SCPB. Immunoreactive (ir-) FMRFamide (but not ir-SCPB) coeluted with authentic FMRFamide from both chromatographic columns. The amino acid composition of the purified peptide was: phenylalanine 2: arginine 1: methionine 1. Digestion of purified ir-FMRFamide with carboxypeptidase Y indicated that the 4 residues were in the same sequence as occurs in FMRFamide. The dose-response curves for purified and synthetic FMRFamide on the radula protractor muscle of Busycon contrarium were coincident, as were their inhibition binding curves in the FMRFamide RIA. The highest concentrations of ir-FMRFamide were in the pedal and pleural ganglia; but SCPB was concentrated in the buccal ganglion. Synthetic SCPB has no effect on the radula protractor muscle of Busycon or the isolated heart of Mercenaria. The FMRFamide-like peptide in the gastropod Aplysia is FMRFamide, so this peptide has now been identified in 2 molluscan classes. The proposed structural relationship between FMRFamide and SCPB is fortuitous, and these 2 peptides should have different physiological functions in Aplysia.