Coelenterate Neuropeptides: Structure, Action and Biosynthesis

Evolutionary "old" nervous systems such as those of coelenteratesare peptidergic: Using various radioimmunoassays we have nowisolated 13 novel neuropeptides from sea anemones and severalothers from hydrozoan polyps and medusae. These peptides areall structurally related and contain the C-terminal sequenceArg-X-NH₂ or Lys-X-NH₂, where X is Ala, Asn, Ile, Phe, Pro orTrp. Three neuropeptides have a novel N-terminal L-3-phenyllactylresidue, which protects against degradation by nonspecific aminopeptidases.The neuropeptides from sea anemones are produced by differentsets of neurones and have excitatory or inhibitory actions onisolated muscle preparations, suggesting that they are neurotransmittersor neuromodulators. We have also cloned the precursor proteinfor the sea-anemone neuropeptide Antho-RFamide (<Glu-Gly-Arg-Phe-NH₂).In Calliactis parasitica this precursor harbours 19 copies ofimmature Antho-RFamide (Gln-Gly-Arg-Phe-Gly) together with 7other, putative neuropeptide sequences. The precursor of Anthopleuraelegantissima contains 14 copies of Antho-RFamide and 19 other,putative neuropeptides. This shows that the biosynthetic machineryfor neuropeptides in coelenterates, the lowest animal grouphaving a nervous system, is already very efficient and similarto that of higher invertebrates, such as molluscs and insects,and vertebrates.