Coelenterate neuropeptides: Structure, action and biosynthesis

Research output: Contribution to journal › Journal article › Research › peer-review

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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.

In: Integrative and Comparative Biology, Vol. 32, No. 1, 1992, p. 1-12.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Grimmelikhuijzen, CJP, Carstensen, K, Darmer, D, Moosler, A, Nothacker, HP, Reinscheid, RK, Schmutzler, C, Vollert, H, Mcfarlane, I & Rinehart, KL 1992, 'Coelenterate neuropeptides: Structure, action and biosynthesis', Integrative and Comparative Biology, vol. 32, no. 1, pp. 1-12. https://doi.org/10.1093/icb/32.1.1

APA

Grimmelikhuijzen, C. J. P., Carstensen, K., Darmer, D., Moosler, A., Nothacker, H. P., Reinscheid, R. K., Schmutzler, C., Vollert, H., Mcfarlane, I., & Rinehart, K. L. (1992). Coelenterate neuropeptides: Structure, action and biosynthesis. Integrative and Comparative Biology, 32(1), 1-12. https://doi.org/10.1093/icb/32.1.1

Vancouver

Grimmelikhuijzen CJP, Carstensen K, Darmer D, Moosler A, Nothacker HP, Reinscheid RK et al. Coelenterate neuropeptides: Structure, action and biosynthesis. Integrative and Comparative Biology. 1992;32(1):1-12. https://doi.org/10.1093/icb/32.1.1

Author

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. / Coelenterate neuropeptides : Structure, action and biosynthesis. In: Integrative and Comparative Biology. 1992 ; Vol. 32, No. 1. pp. 1-12.

Bibtex

@article{0fc7a944805a46739cdc3c25dd7ea8ed,
title = "Coelenterate neuropeptides: Structure, action and biosynthesis",
abstract = "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.",
author = "Grimmelikhuijzen, {Cornelis J.P.} and Klaus Carstensen and Dorothea Darmer and Angelika Moosler and Nothacker, {Hans Peter} and Reinscheid, {Rainer K.} and Cornelia Schmutzler and Henning Vollert and Ian Mcfarlane and Rinehart, {Kenneth L.}",
note = "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.",
year = "1992",
doi = "10.1093/icb/32.1.1",
language = "English",
volume = "32",
pages = "1--12",
journal = "Integrative and Comparative Biology",
issn = "1540-7063",
publisher = "Oxford University Press",
number = "1",

}

RIS

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