Isolation of Leu-Pro-Pro-Gly-Pro-Leu-Pro-Arg-Pro-NH2 (Antho-RPamide), an N-terminally protected, biologically active neuropeptide from sea anemones
Research output: Contribution to journal › Journal article › Research › peer-review
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.
| Original language | English |
|---|---|
| Journal | Peptides |
| Volume | 13 |
| Issue number | 5 |
| Pages (from-to) | 851-857 |
| Number of pages | 7 |
| ISSN | 0196-9781 |
| DOIs | |
| Publication status | Published - 1992 |
Bibliographical 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.
- Angiotensin I converting enzyme, Bradykinin, Coelenterate, Mass spectrometry, Neurohormone, Neuropeptide protecting sequence, Neurotransmitter, Peptide structure, Radioimmunoassay
Research areas
ID: 370740007