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

Research output: Contribution to journalArticlepeer-review

Abstract

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
JournalPeptides
Volume12
Issue number5
DOIs
Publication statusPublished (in print/issue) - 1991

Funding

The authors gratefully acknowledge Christian J. Mussap for assistance with preparation of BH-Scy H and the National Health and Medical Research Council of Australia for partial support of this project.

    Keywords

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

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