| Literature DB >> 2905621 |
C J Grimmelikhuijzen1, M Hahn, K L Rinehart, A N Spencer.
Abstract
The hydromedusa Polyorchis penicillatus is a good model system to study neurotransmission in coelenterates. Using a radioimmunoassay for the peptide sequence Arg-Phe-NH2 (RFamide), two peptides have now been purified from acetic acid extracts of this medusa. The structure of one of these peptides was established as pyroGlu-Leu-Leu-Gly-Gly-Arg-Phe-NH2, and was named Pol-RFamide. This peptide belongs to the same peptide family as a recently isolated neuropeptide from sea anemones (pyroGlu-Gly-Arg-Phe-NH2). Using antisera to Pol-RFamide, the peptide was found to be exclusively localized in neurones of Polyorchis, among them neurones associated with smooth-muscle fibres. This suggests that Pol-RFamide might be a transmitter or modulator at neuromuscular junctions.Entities:
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Year: 1988 PMID: 2905621 DOI: 10.1016/0006-8993(88)90219-3
Source DB: PubMed Journal: Brain Res ISSN: 0006-8993 Impact factor: 3.252