Structural characterization of neuropeptide Y from the brain of the dogfish, Scyliorhinus canicula

J. Michael Conlon, Christina Bjenning, Neil Hazon

Research output: Contribution to journalArticlepeer-review

31 Citations (Scopus)


A peptide of the pancreatic polypeptide (PP) family was isolated in pure form from the brain of an elasmobranch fish, Scyliorhinus canicula (European common dogfish). The primary structure of the peptide was established as: Tyr-Pro-Ser-Lys-Pro-Asp-Asn-Pro-Gly-Glu10-Gly-Ala-Pro-Ala-Glu-Asp-Leu-Ala-Lys-Tyr20-Tyr-Ser-Ala-Leu-Arg-His- Tyr-Ile-Asn-Leu30-Ile-Thr-Arg-Gln-Arg-Tyr-NH2. This sequence contains only two amino acid substitutions compared with pig neuropeptide Y (NPY) (Gly for Asp11 and Lys for Arg19), and two substitutions (Gly for Asp11 and Leu for Met17) compared with frog NPY. The amino acid sequence of NPY from dogfish brain is appreciably different from the neuropeptide Y-related peptide previously isolated from dogfish pancreas (five amino acid substitutions). The data indicate that evolutionary pressure to conserve the complete primary structure of neuropeptide Y has been very strong. It is suggested that the NPY-related peptide present in the pancreas of elasmobranch and teleost fish represents the piscine equivalent of mammalian peptide tyrosine tyrosine (PYY).

Original languageEnglish
Pages (from-to)493-497
Number of pages5
Issue number3
Publication statusPublished - 1992
Externally publishedYes


  • Brain
  • Dogfish
  • Elasmobranch
  • Neuropeptide Y
  • Pancreatic polypeptide family
  • Peptide tyrosine tyrosine

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience


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