Isolation of two novel neuropeptides from sea anemones: The unusual, biologically active L-3-phenyllactyl-Tyr-Arg-Ile-NH2 and its des-phenyllactyl fragment Tyr-Arg-Ile-NH2
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Using a radioimmunoassay for the carboxyl-terminal sequence Arg-Val-NH2, two novel peptides were purified from extracts of the sea anemone Anthopleura elegantissima. These peptides were L-3-phenyllactyl-Tyr-Arg-Ile-NH2 (name: Antho-RIamide I) and its des-phenyllactyl fragment Tyr-Arg-Ile-NH2 (Antho-RIamide II). Immunocytochemical staining showed that these peptides were localized in neurons of sea anemones. Application of low concentrations (10-8 M) of Antho-RIamide I inhibited spontaneous contractions in several muscle groups of sea anemones, whereas Antho-RIamide II was inactive. Antho-RIamide I is the second neuropeptide from sea anemones that bears the unusual, amino-terminal L-3-phenyllactyl blocking group. We suggest that this group renders the peptide resistant against degradation by nonspecific aminopeptidases. In addition, the L-3-phenyllactyl residue might also play a role in receptor binding.
Original language | English |
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Journal | Peptides |
Volume | 12 |
Issue number | 6 |
Pages (from-to) | 1165-1173 |
Number of pages | 9 |
ISSN | 0196-9781 |
DOIs | |
Publication status | Published - 1991 |
Bibliographical note
Funding Information:
We thank SusanneR aabe for typing the manuscripat nd the Bundesministeriufmor Forschung und Technologic and the Deutsche Forschungsgemeinschaft (Gr 76f2o/r7 fi-n3a) ncial support.
- Coelenterate, Mass spectrometry, Neurohormone, Neuropeptide blocking group, Neurotransmitter, Peptide structure, Posttranslational modification
Research areas
ID: 370740262