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
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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.
Originalsprog | Engelsk |
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Tidsskrift | Peptides |
Vol/bind | 12 |
Udgave nummer | 6 |
Sider (fra-til) | 1165-1173 |
Antal sider | 9 |
ISSN | 0196-9781 |
DOI | |
Status | Udgivet - 1991 |
ID: 370740262