Novel tachykinins from the brain of the sea lamprey, Petromyzon marinus, and the skate, Raja rhina

David Waugh, Stacia Sower, Christina Bjenning, J. Michael Conlon

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25 Citations (Scopus)


Using radioimmunoassays for mammalian tachykinins, peptides with substance P-like immunoreactivity and neurokinin A-like immunoreactivity were identified in an extract of the brain of the longnose skate, Raja rhina (elasmobranch) but only a peptide with neurokinin A-like immunoreactivity was identified in the brain of the sea lamprey, Petromyzon marinus (agnathan). The primary structure of the skate peptide with substance P-like immunoreactivity (Ala-Lys-His-Asp-Lys-Phe-Tyr-Gly-Leu-Met-NH2) shows one amino acid substitution (Phe3 → His) compared with scyliorhinin I, previously isolated from dogfish brain and gut. The skate neurokinin A-related peptide (His-Lys-Leu-Gly-Ser-Phe-Val-Gly-Leu-Met-NH2) shows two substitutions (Thr3 → Leu and Asp4 → Gly) compared with mammalian neurokinin A. Although the COOH-terminus of the lamprey tachykinin (Arg-Lys-Pro-His-Pro-Lys-Glu-Phe-Val-Gly-Leu-Met-NH2) resembles neurokinin A, the presence of the strongly conserved Lys/Arg-Pro-Xaa-Pro motif at the NH2-terminus of the peptide indicates greater structural similarity with substance P. The additional arginine residue at position 1 in the peptide suggests that the lamprey is utilizing a site of posttranslational processing in the tachykinin precursor that is different from the equivalent site in mammalian and other lower vertebrate preprotachykinin(s).

Original languageEnglish
Pages (from-to)155-161
Number of pages7
Issue number1
Publication statusPublished (in print/issue) - Jan 1994


  • Agnathan
  • Elasmobranch
  • Neurokinin A
  • Substance P
  • Tachykinin


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