Isolation of Leu-Pro-Pro-Gly-Pro-Leu-Pro-Arg-Pro-NH2 (Antho-RPamide), an N-terminally protected, biologically active neuropeptide from sea anemones

Klaus Carstensen; Kenneth L. Rinehart; Ian D. McFarlane; Cornelis J.P. Grimmelikhuijzen

doi:10.1016/0196-9781(92)90040-A

Isolation of Leu-Pro-Pro-Gly-Pro-Leu-Pro-Arg-Pro-NH₂ (Antho-RPamide), an N-terminally protected, biologically active neuropeptide from sea anemones

Klaus Carstensen, Kenneth L. Rinehart, Ian D. McFarlane, Cornelis J.P. Grimmelikhuijzen^*

^*Corresponding author af dette arbejde

Cell- and Neurobiology

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

29 Citationer (Scopus)

Abstract

Using a radioimmunoassay against the C-terminal sequence Arg-Pro-NH₂ (RPamide), we have isolated the peptide Leu-Pro-Pro-Gly-Pro-Leu-Pro-Arg-Pro-NH₂ (Antho-RPamide) from an extract of the sea anemone Anthopleura elegantissima. Antho-RPamide is located in neurons of sea anemones. Application of low concentrations of Antho-RPamide to tentacle preparations of sea anemones strongly increased the frequency and duration of spontaneous contractions, suggesting that this peptide is involved in neurotransmission. Antho-RPamide has a free N-terminus, yet its X-Pro-Pro sequence makes it relatively resistant to degradation by nonspecific aminopeptidases. Thus, we have discovered another strategy by which sea anemones protect the N-termini of their bioactive neuropeptides.

Originalsprog	Engelsk
Tidsskrift	Peptides
Vol/bind	13
Udgave nummer	5
Sider (fra-til)	851-857
Antal sider	7
ISSN	0196-9781
DOI	https://doi.org/10.1016/0196-9781(92)90040-A
Status	Udgivet - 1992

Bibliografisk note

Funding Information:
We thank Susanne Raabe and Dagmar Boshold for typing the manuscript, Furong Sun for mass spectra, and the Bundesministerium flit Forschung und Technologie, the Deutsche Forschungsgemeinschaft (Gr 762/7-3), NATO (Collaborative Research Grant to C.J.P.G.), and the National Institute of General Medical Sciences (GM 27029, to K.L.R.) for fnancial support. A part of this article is based on a doctoral study by K.C. in the Faculty of Biology, University of Hamburg.

Adgang til dokumentet

10.1016/0196-9781(92)90040-A

Andre filer og links

Link to publication in Scopus

Citationsformater

@article{0646caa9d6f04b49b8463f4d225a948d,

title = "Isolation of Leu-Pro-Pro-Gly-Pro-Leu-Pro-Arg-Pro-NH2 (Antho-RPamide), an N-terminally protected, biologically active neuropeptide from sea anemones",

abstract = "Using a radioimmunoassay against the C-terminal sequence Arg-Pro-NH2 (RPamide), we have isolated the peptide Leu-Pro-Pro-Gly-Pro-Leu-Pro-Arg-Pro-NH2 (Antho-RPamide) from an extract of the sea anemone Anthopleura elegantissima. Antho-RPamide is located in neurons of sea anemones. Application of low concentrations of Antho-RPamide to tentacle preparations of sea anemones strongly increased the frequency and duration of spontaneous contractions, suggesting that this peptide is involved in neurotransmission. Antho-RPamide has a free N-terminus, yet its X-Pro-Pro sequence makes it relatively resistant to degradation by nonspecific aminopeptidases. Thus, we have discovered another strategy by which sea anemones protect the N-termini of their bioactive neuropeptides.",

keywords = "Angiotensin I converting enzyme, Bradykinin, Coelenterate, Mass spectrometry, Neurohormone, Neuropeptide protecting sequence, Neurotransmitter, Peptide structure, Radioimmunoassay",

author = "Klaus Carstensen and Rinehart, {Kenneth L.} and McFarlane, {Ian D.} and Grimmelikhuijzen, {Cornelis J.P.}",

note = "Funding Information: We thank Susanne Raabe and Dagmar Boshold for typing the manuscript, Furong Sun for mass spectra, and the Bundesministerium flit Forschung und Technologie, the Deutsche Forschungsgemeinschaft (Gr 762/7-3), NATO (Collaborative Research Grant to C.J.P.G.), and the National Institute of General Medical Sciences (GM 27029, to K.L.R.) for fnancial support. A part of this article is based on a doctoral study by K.C. in the Faculty of Biology, University of Hamburg.",

year = "1992",

doi = "10.1016/0196-9781(92)90040-A",

language = "English",

volume = "13",

pages = "851--857",

journal = "Peptides",

issn = "0196-9781",

publisher = "Elsevier",

number = "5",

}

TY - JOUR

T1 - Isolation of Leu-Pro-Pro-Gly-Pro-Leu-Pro-Arg-Pro-NH2 (Antho-RPamide), an N-terminally protected, biologically active neuropeptide from sea anemones

AU - Carstensen, Klaus

AU - Rinehart, Kenneth L.

AU - McFarlane, Ian D.

AU - Grimmelikhuijzen, Cornelis J.P.

N1 - Funding Information: We thank Susanne Raabe and Dagmar Boshold for typing the manuscript, Furong Sun for mass spectra, and the Bundesministerium flit Forschung und Technologie, the Deutsche Forschungsgemeinschaft (Gr 762/7-3), NATO (Collaborative Research Grant to C.J.P.G.), and the National Institute of General Medical Sciences (GM 27029, to K.L.R.) for fnancial support. A part of this article is based on a doctoral study by K.C. in the Faculty of Biology, University of Hamburg.

PY - 1992

Y1 - 1992

N2 - Using a radioimmunoassay against the C-terminal sequence Arg-Pro-NH2 (RPamide), we have isolated the peptide Leu-Pro-Pro-Gly-Pro-Leu-Pro-Arg-Pro-NH2 (Antho-RPamide) from an extract of the sea anemone Anthopleura elegantissima. Antho-RPamide is located in neurons of sea anemones. Application of low concentrations of Antho-RPamide to tentacle preparations of sea anemones strongly increased the frequency and duration of spontaneous contractions, suggesting that this peptide is involved in neurotransmission. Antho-RPamide has a free N-terminus, yet its X-Pro-Pro sequence makes it relatively resistant to degradation by nonspecific aminopeptidases. Thus, we have discovered another strategy by which sea anemones protect the N-termini of their bioactive neuropeptides.

AB - Using a radioimmunoassay against the C-terminal sequence Arg-Pro-NH2 (RPamide), we have isolated the peptide Leu-Pro-Pro-Gly-Pro-Leu-Pro-Arg-Pro-NH2 (Antho-RPamide) from an extract of the sea anemone Anthopleura elegantissima. Antho-RPamide is located in neurons of sea anemones. Application of low concentrations of Antho-RPamide to tentacle preparations of sea anemones strongly increased the frequency and duration of spontaneous contractions, suggesting that this peptide is involved in neurotransmission. Antho-RPamide has a free N-terminus, yet its X-Pro-Pro sequence makes it relatively resistant to degradation by nonspecific aminopeptidases. Thus, we have discovered another strategy by which sea anemones protect the N-termini of their bioactive neuropeptides.

KW - Angiotensin I converting enzyme

KW - Bradykinin

KW - Coelenterate

KW - Mass spectrometry

KW - Neurohormone

KW - Neuropeptide protecting sequence

KW - Neurotransmitter

KW - Peptide structure

KW - Radioimmunoassay

UR - http://www.scopus.com/inward/record.url?scp=0026451936&partnerID=8YFLogxK

U2 - 10.1016/0196-9781(92)90040-A

DO - 10.1016/0196-9781(92)90040-A

M3 - Journal article

C2 - 1480510

AN - SCOPUS:0026451936

SN - 0196-9781

VL - 13

SP - 851

EP - 857

JO - Peptides

JF - Peptides

IS - 5

ER -