Coelenterate neuropeptides: Structure, action and biosynthesis
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Coelenterate neuropeptides : Structure, action and biosynthesis. / 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.
I: Integrative and Comparative Biology, Bind 32, Nr. 1, 1992, s. 1-12.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Coelenterate neuropeptides
T2 - Structure, action and biosynthesis
AU - Grimmelikhuijzen, Cornelis J.P.
AU - Carstensen, Klaus
AU - Darmer, Dorothea
AU - Moosler, Angelika
AU - Nothacker, Hans Peter
AU - Reinscheid, Rainer K.
AU - Schmutzler, Cornelia
AU - Vollert, Henning
AU - Mcfarlane, Ian
AU - Rinehart, Kenneth L.
N1 - Funding Information: We thank Dagmar Diekhoff and Doris Nollmeyer for excellent technical assis tance, Susanne Raabe for typing the manuscript, and the Bundesministerium fur Forschung und Technologie and the Deutsche Forschungsgemeinschaft (Gr 762/ 7-3) for financial support.
PY - 1992
Y1 - 1992
N2 - Evolutionary "old" nervous systems such as those of coelenterates are peptidergic: Using various radioimmunoassays we have now isolated 13 novel neuropeptides from sea anemones and several others from hydrozoan polyps and medusae. These peptides are all structurally related and contain the C-terminal sequence Arg-X-NH2 or Lys-X-NH2, where X is Ala, Asn, Ile, Phe, Pro or Trp. Three neuropeptides have a novel N-terminal L-3-phenyllactyl residue, which protects against degradation by nonspecific aminopeptidases. The neuropeptides from sea anemones are produced by different sets of neurones and have excitatory or inhibitory actions on isolated muscle preparations, suggesting that they are neurotransmitters or neuromodulators. We have also cloned the precursor protein for the sea-anemone neuropeptide Antho-RFamide (<Glu-Gly-Arg-Phe-NH2). In Calliactis parasitica this precursor harbours 19 copies of immature Antho-RFamide (Gln-Gly-Arg-Phe-Gly) together with 7 other, putative neuropeptide sequences. The precursor of Anthopleura elegantissima contains 14 copies of Antho-RFamide and 19 other, putative neuropeptides. This shows that the biosynthetic machinery for neuropeptides in coelenterates, the lowest animal group having a nervous system, is already very efficient and similar to that of higher invertebrates, such as molluscs and insects, and vertebrates.
AB - Evolutionary "old" nervous systems such as those of coelenterates are peptidergic: Using various radioimmunoassays we have now isolated 13 novel neuropeptides from sea anemones and several others from hydrozoan polyps and medusae. These peptides are all structurally related and contain the C-terminal sequence Arg-X-NH2 or Lys-X-NH2, where X is Ala, Asn, Ile, Phe, Pro or Trp. Three neuropeptides have a novel N-terminal L-3-phenyllactyl residue, which protects against degradation by nonspecific aminopeptidases. The neuropeptides from sea anemones are produced by different sets of neurones and have excitatory or inhibitory actions on isolated muscle preparations, suggesting that they are neurotransmitters or neuromodulators. We have also cloned the precursor protein for the sea-anemone neuropeptide Antho-RFamide (<Glu-Gly-Arg-Phe-NH2). In Calliactis parasitica this precursor harbours 19 copies of immature Antho-RFamide (Gln-Gly-Arg-Phe-Gly) together with 7 other, putative neuropeptide sequences. The precursor of Anthopleura elegantissima contains 14 copies of Antho-RFamide and 19 other, putative neuropeptides. This shows that the biosynthetic machinery for neuropeptides in coelenterates, the lowest animal group having a nervous system, is already very efficient and similar to that of higher invertebrates, such as molluscs and insects, and vertebrates.
UR - http://www.scopus.com/inward/record.url?scp=77957212575&partnerID=8YFLogxK
U2 - 10.1093/icb/32.1.1
DO - 10.1093/icb/32.1.1
M3 - Journal article
AN - SCOPUS:77957212575
VL - 32
SP - 1
EP - 12
JO - Integrative and Comparative Biology
JF - Integrative and Comparative Biology
SN - 1540-7063
IS - 1
ER -
ID: 370739837