Neuropeptides in coelenterates: a review
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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 tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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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