Coelenterate Neuropeptides: Structure, Action and Biosynthesis |
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Authors: | GRIMMELIKHUIJZEN CORNELIS J P; CARSTENSEN KLAUS; DARMER DOROTHEA; MOOSLER ANGELIKA; NOTHACKER HANS-PETER; REINSCHEID RAINER K; SCHMUTZLER CORNELIA; VOLLERT HENNING; MCFARLANE IAN; RINEHART KENNETH L |
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Institution: | University of Hamburg, Centre for Molecular Neurobiology (ZMNH) Martinistrasse 52, 2000 Hamburg 20, FRG
University of Hull, Department of Applied Biology Hull HU6 7RX, UK
University of Illinois, School of Chemical Sciences 1209 West California Street, Urbana, Illinois 61801 |
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Abstract: | 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. |
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