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 NK 1 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 > [Sar 9Met(O 2) 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 NK 1 receptor and of a nonmammalian tachykinin receptor in the dogfish.

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