title: LymnaDFamides, a new family of neuropeptides from the pond snail, Lymnaea stagnalis. Clue to cholecystokinin immunoreactivity in invertebrates?
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.
authors: Department of Clinical Biochemistry, Rigshospitalet University of Copenhagen, Denmark.
authors: A H
authors: AH
authors: Johnsen
authors: J F
authors: JF
authors: Rehfeld
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002766:Cholecystokinin / Q000737:chemistry* / Q000276:immunology; D002850:Chromatography, Gel; D005704:Gallbladder / Q000187:drug effects / Q000502:physiology; D005724:Ganglia / Q000737:chemistry*; D005755:Gastrins / Q000737:chemistry; D006801:Humans; D066298:In Vitro Techniques; D008195:Lymnaea; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D009119:Muscle Contraction / Q000187:drug effects; D009130:Muscle, Smooth / Q000187:drug effects / Q000502:physiology; D009479:Neuropeptides / Q000737:chemistry* / Q000276:immunology / Q000302:isolation & purification / Q000494:pharmacology; D011863:Radioimmunoassay; D017386:Sequence Homology, Amino Acid; D014337:Trout
chemical_list: D005755:Gastrins; D009479:Neuropeptides; D002766:Cholecystokinin