Binding sites for tachykinin peptides in the brain and stomach of the dogfish, Scyliorhinus canicula

Paul L.M. Van Giersbergen, J. Michael Conlon, Stephen H. Buck

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)


In membranes of dogfish brain and stomach, two binding sites for tachykinins were identified. One site specifically bound [125I]-Bolton-Hunter substance P (BH-SP) and the rank potency of tachykinins to compete for BH-SP binding revealed similarities with the rank potency of an NK1 receptor. The pharmacology of the other site, which specifically bound [125I]-Bolton-Hunter scyliorhinin II (BH-Scy II), did not resemble any of the mammalian tachykinin receptors. The rank potency to inhibit BH-Scy II binding to this second site was: scyliorhinin II ≈ scyliorhinin I > eledoisin ≈ substance P ≈ neurokinin A > phyllomedusin ≈ physalaemin > [Sar9Met(O2)11]substance P. Neurokinin B and senktide did not displace BH-Scy II binding. In addition, nucleotide analogues inhibited BH-SP binding but not BH-Scy II binding. Our binding data suggest the existence of a mammalian-like NK1 receptor and of a nonmammalian tachykinin receptor in the dogfish.

Original languageEnglish
Pages (from-to)1161-1163
Number of pages3
Issue number5
Publication statusPublished - 1991
Externally publishedYes


  • Brain
  • Dogfish
  • G-protein
  • Scyliorhinus caniculus
  • Stomach
  • Tachykinin receptors
  • Tachykinins
  • [I]-Bolton-Hunter scyliorhinin II
  • [I]-Bolton-Hunter substance P

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience


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