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.

journal_name

Peptides

journal_title

Peptides

authors

Carstensen K,Rinehart KL,McFarlane ID,Grimmelikhuijzen CJ

doi

10.1016/0196-9781(92)90040-a

subject

Has Abstract

pub_date

1992-09-01 00:00:00

pages

851-7

issue

5

eissn

0196-9781

issn

1873-5169

pii

0196-9781(92)90040-A

journal_volume

13

pub_type

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