Partial characterization of a novel cardioinhibitory peptide from the brain of the snail Helix aspersa.
1. We report the isolation of a peptide from the brain of the snail Helix aspersa by radioimmunoassay using an antisomatostatin. 2. The sequencing of an immunopositive fraction showed the presence of a new tridecapeptide, termed Helix cardioinhibitory peptide (HCIP), with the following primary structure: H-Val-Phe-Gln-Asn-Gln-Phe-Lys-Gly-Ile-Gln-Gly-Arg-Phe-NH2. It is structurally related to the Achatina cardioexcitatory peptide (ACEP-1) and the terminal-amino acid sequence of HCIP is identical to that of FMRFamide family peptides. 3. The synthetic HCIP was tested on heart and neuronal activities and it was found to have inhibitory actions not only on the ventricle but also on visceral neurons of the central nervous system of Helix. Immunocytochemical investigation indicates its presence in visceral and parietal ganglia, in which cells taking part in the regulation of the heartbeat have been previously identified.
Baud
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Laboratoire de Biologie des Organismes et Ecosystèmes, UFR Sciences et Techniques, Besançon, France.
Darbon
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Li
K W
KW
Marchand
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CR
D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000166:cytology; D001923:Brain Chemistry; D019835:FMRFamide / Q000737:chemistry; D017952:Ganglia, Invertebrate / Q000166:cytology; D006321:Heart / Q000187:drug effects*; D006372:Helix, Snails; D007150:Immunohistochemistry; D009474:Neurons / Q000187:drug effects / Q000502:physiology*; D009479:Neuropeptides / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D009479:Neuropeptides; C113729:VFQNQFKGIQGRF; C063480:Achatina cardio-excitatory peptide 1; D019835:FMRFamide