The dogfish peptides scyliorhinin I and scyliorhinin II bind with differential selectivity to mammalian tachykinin receptors

  • Eur J Pharmacol. 1987 Nov 24;144(1):109-11. doi: 10.1016/0014-2999(87)90017-3.
S H Buck  1 ,  J L Krstenansky
Affiliations
  • 1. Merrell Dow Research Institute, Cincinnati, OH 45215.
PMID: 2830117 DOI: 10.1016/0014-2999(87)90017-3
Abstract

The dogfish intestinal, linear tachykinin scyliorhinin I (SCYI) and cyclic tachykinin scyliorhinin II (SCYII) bound with differential selectivity to mammalian tachykinin, membrane receptor sites. SCYI bound with highest affinity to NK-1 sites in rat submandibular gland (KI = 0.9 nM) and to NK-2 sites in hamster urinary bladder (KI = 2 nM) whereas SCYII bound with highest affinity to NK-3 sites in rat cerebral cortex (KI = 2.5 nM). These results suggest that SCYI is a dual NK-1/NK-2 tachykinin receptor agonist while SCYII is an NK-3 selective tachykinin receptor agonist.

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