Neuropeptides in coelenterates: a review

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Standard

Neuropeptides in coelenterates : a review. / Grimmelikhuijzen, C. J.P.; Graff, D.; Koizumi, O.; Westfall, J. A.; McFarlane, I. D.

I: Hydrobiologia, Bind 216-217, Nr. 1, 06.1991, s. 555-563.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Grimmelikhuijzen, CJP, Graff, D, Koizumi, O, Westfall, JA & McFarlane, ID 1991, 'Neuropeptides in coelenterates: a review', Hydrobiologia, bind 216-217, nr. 1, s. 555-563. https://doi.org/10.1007/BF00026513

APA

Grimmelikhuijzen, C. J. P., Graff, D., Koizumi, O., Westfall, J. A., & McFarlane, I. D. (1991). Neuropeptides in coelenterates: a review. Hydrobiologia, 216-217(1), 555-563. https://doi.org/10.1007/BF00026513

Vancouver

Grimmelikhuijzen CJP, Graff D, Koizumi O, Westfall JA, McFarlane ID. Neuropeptides in coelenterates: a review. Hydrobiologia. 1991 jun.;216-217(1):555-563. https://doi.org/10.1007/BF00026513

Author

Grimmelikhuijzen, C. J.P. ; Graff, D. ; Koizumi, O. ; Westfall, J. A. ; McFarlane, I. D. / Neuropeptides in coelenterates : a review. I: Hydrobiologia. 1991 ; Bind 216-217, Nr. 1. s. 555-563.

Bibtex

@article{6140c5abfbd24f8bb6244410b7728143,
title = "Neuropeptides in coelenterates: a review",
abstract = "Coelenterate neurones produce peptides containing an Arg-Phe-NH2(RF-amide)-like carboxyterminus. RF-amide-like peptides are located in neuronal dense-cored vesicles, indicating that they are released by exocytosis and that they might function as neurotransmitters or neurohormones. Using a radioimmunoassay for the sequence RF-amide, 3 peptides were isolated from the sea anemone Anthopleura elegantissima: < Glu-Gly-Arg-Phe-NH2(Antho-RF-amide), <Glu-Ser-Leu-Arg-Trp-NH2(Antho-RWamide I) and <Glu-Gly-Leu-Arg-Trp-NH2(Antho-RW-amide II). The general structure of these peptides can be described as <Glu...Arg-X-NH2, where X is an aromatic amino acid. From the hydromedusa Polyorchis penicillatus, the peptide <Glu-Leu-Leu-Gly-Gly-Arg-Phe-NH2(Pol-RF-amide I) was isolated, which also belongs to the <Glu...Arg-X-NH2 family. Using specific antisera, it was shown that all 4 peptides were located in neurones, many of which were associated with smooth muscle fibres. Application of low doses of Antho-RF-amide or of Antho-RW-amide I and II induced contractions of endodermal muscles of sea anemones. This suggests that these peptides are transmitters or modulators at neuromuscular junctions.",
keywords = "coelenterates, neurones, Neuropeptides",
author = "Grimmelikhuijzen, {C. J.P.} and D. Graff and O. Koizumi and Westfall, {J. A.} and McFarlane, {I. D.}",
year = "1991",
month = jun,
doi = "10.1007/BF00026513",
language = "English",
volume = "216-217",
pages = "555--563",
journal = "Journal of Applied Phycology",
issn = "0921-8971",
publisher = "Springer",
number = "1",

}

RIS

TY - JOUR

T1 - Neuropeptides in coelenterates

T2 - a review

AU - Grimmelikhuijzen, C. J.P.

AU - Graff, D.

AU - Koizumi, O.

AU - Westfall, J. A.

AU - McFarlane, I. D.

PY - 1991/6

Y1 - 1991/6

N2 - Coelenterate neurones produce peptides containing an Arg-Phe-NH2(RF-amide)-like carboxyterminus. RF-amide-like peptides are located in neuronal dense-cored vesicles, indicating that they are released by exocytosis and that they might function as neurotransmitters or neurohormones. Using a radioimmunoassay for the sequence RF-amide, 3 peptides were isolated from the sea anemone Anthopleura elegantissima: < Glu-Gly-Arg-Phe-NH2(Antho-RF-amide), <Glu-Ser-Leu-Arg-Trp-NH2(Antho-RWamide I) and <Glu-Gly-Leu-Arg-Trp-NH2(Antho-RW-amide II). The general structure of these peptides can be described as <Glu...Arg-X-NH2, where X is an aromatic amino acid. From the hydromedusa Polyorchis penicillatus, the peptide <Glu-Leu-Leu-Gly-Gly-Arg-Phe-NH2(Pol-RF-amide I) was isolated, which also belongs to the <Glu...Arg-X-NH2 family. Using specific antisera, it was shown that all 4 peptides were located in neurones, many of which were associated with smooth muscle fibres. Application of low doses of Antho-RF-amide or of Antho-RW-amide I and II induced contractions of endodermal muscles of sea anemones. This suggests that these peptides are transmitters or modulators at neuromuscular junctions.

AB - Coelenterate neurones produce peptides containing an Arg-Phe-NH2(RF-amide)-like carboxyterminus. RF-amide-like peptides are located in neuronal dense-cored vesicles, indicating that they are released by exocytosis and that they might function as neurotransmitters or neurohormones. Using a radioimmunoassay for the sequence RF-amide, 3 peptides were isolated from the sea anemone Anthopleura elegantissima: < Glu-Gly-Arg-Phe-NH2(Antho-RF-amide), <Glu-Ser-Leu-Arg-Trp-NH2(Antho-RWamide I) and <Glu-Gly-Leu-Arg-Trp-NH2(Antho-RW-amide II). The general structure of these peptides can be described as <Glu...Arg-X-NH2, where X is an aromatic amino acid. From the hydromedusa Polyorchis penicillatus, the peptide <Glu-Leu-Leu-Gly-Gly-Arg-Phe-NH2(Pol-RF-amide I) was isolated, which also belongs to the <Glu...Arg-X-NH2 family. Using specific antisera, it was shown that all 4 peptides were located in neurones, many of which were associated with smooth muscle fibres. Application of low doses of Antho-RF-amide or of Antho-RW-amide I and II induced contractions of endodermal muscles of sea anemones. This suggests that these peptides are transmitters or modulators at neuromuscular junctions.

KW - coelenterates

KW - neurones

KW - Neuropeptides

UR - http://www.scopus.com/inward/record.url?scp=4243795796&partnerID=8YFLogxK

U2 - 10.1007/BF00026513

DO - 10.1007/BF00026513

M3 - Journal article

AN - SCOPUS:4243795796

VL - 216-217

SP - 555

EP - 563

JO - Journal of Applied Phycology

JF - Journal of Applied Phycology

SN - 0921-8971

IS - 1

ER -

ID: 370740128