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Journal of Experimental Biology, Vol 154, Issue 1 421-437, Copyright © 1990 by Company of Biologists

JOURNAL ARTICLES

Seven FMRFamide-related and two SCP-related cardioactive peptides from Helix

DA Price, W Lesser, TD Lee, KE Doble and MJ Greenberg
Whitney Laboratory, St Augustine, FL 32086.

Pulmonate snails have a more complex array of cardioexcitatory peptides than other molluscs, and Helix has a more complex array than most other pulmonates. Since a full characterisation of the cardioexcitatory peptides is necessary for an understanding of physiology, we sought to identify the members of two families of such peptides - the small cardioactive peptides (SCPs) and the FMRFamide-related peptides (FaRPs) - from Helix aspersa. We characterised the peaks of immunoreactivity from HPLC both by their elution times and by their molecular weights as determined by fast atom bombardment mass spectrometry (FABms). These two criteria, used in parallel, facilitated our identification of several known peptides: MNYLAFPRMamide, identical to SCPB of Aplysia; two tetrapeptide FaRPs, FRMRamide and FLRFamide; and three hepatapeptide FaRPs, NDPFLRFamide, SDPFLRFamide and pQDPFLRFamide. Of these peptides, only FMRFamide and pQDPFLRFamide have previously been reported from Helix. We also discovered an additional SCP and two novel FaRPs and sequenced them. The SCP is Ser-Gly-Tyr-Leu-Ala-Phe-Pro-Arg-Met-amide (SGYLAFPRMamide), and the heptapeptide FaRPs are Asn-Asp-Pro-Tyr-Leu-Arg-Phe-amide (NDPYLRFamide) and Ser-Glu-Pro-Tyr-Leu-Arg-Phe-amide (SEPYLRFamide). When these nine peptides were tested on isolated Helix ventricles, the SCPs were the most potent cardioexcitors, the heptapeptide FaRPs were next, and the tetrapeptides had the least activity.


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© The Company of Biologists Ltd 1990