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LymnaDFamides, a new family of neuropeptides from the pond snail, Lymnaea stagnalis. Clue to cholecystokinin immunoreactivity in invertebrates?

A H Johnsen, J F Rehfeld

17 Citations (Scopus)

Abstract

Five tridecapeptides have been identified from the central nervous system of the pond snail, Lymnaea stagnalis. The sequences are Pro-Xaa-Asp-Arg-Ile-Ser-Yaa-Ser-Ala-Phe-Ser-Asp-Phe. NH2, where Xaa is either Tyr or Phe and Yaa either Asn, Ser or Gly. The peptides are named lymnaDFamides to acknowledge identity with the C-terminal dipeptide of the mammalian neuropeptides, cholecystokinin (CCK) and gastrin. They were detected by an antiserum that recognizes the biologically active C-termini of cholecystokinin and gastrin. LymnaDFamide-1 (Xaa = Tyr and Yaa = Asn) had no effect on trout gallbladder, which responds equally to CCK and gastrin. We propose that the lymnaDFamides belong to an Asp-Phe-amide superfamily, which includes CCK and gastrin, and suggest that the widespread CCK/gastrin immunoreactivity in invertebrates is due to peptides belonging to such a superfamily.

Original languageEnglish
JournalEuropean Journal of Biochemistry
Volume213
Issue number2
Pages (from-to)875-9
Number of pages5
ISSN0014-2956
DOIs
Publication statusPublished - 15 Apr 1993
Externally publishedYes

Keywords

  • Amino Acid Sequence
  • Animals
  • Cholecystokinin/chemistry
  • Chromatography, Gel
  • Gallbladder/drug effects
  • Ganglia/chemistry
  • Gastrins/chemistry
  • Humans
  • In Vitro Techniques
  • Lymnaea
  • Mass Spectrometry
  • Molecular Sequence Data
  • Muscle Contraction/drug effects
  • Muscle, Smooth/drug effects
  • Neuropeptides/chemistry
  • Radioimmunoassay
  • Sequence Homology, Amino Acid
  • Trout

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