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Antinociceptive effects of the enkephalinase inhibitor, SCH 34826, in the snail,Cepaea nemoralis

Authors
Journal
Peptides
0196-9781
Publisher
Elsevier
Publication Date
Volume
14
Issue
4
Identifiers
DOI: 10.1016/0196-9781(93)90110-3
Keywords
  • Mollusc
  • Nociception
  • Antinociception
  • Enkephalinase
  • Enkephalin Degradation
  • Opioids
  • Snail
Disciplines
  • Biology

Abstract

Abstract In vertebrates the effects of endogenous opioid peptides are limited by proteolytic enzymes such as endopeptidase 24.11 (enkephalinase), which cleaves the Gly-Phe bonds in both methionine- and leucine-enkephalin. SCH 34826 { (S)-N-[n- [1-[(2,2-dimethyl-1,3-dioxolan-4yl) methoxy]carbonyl]-2-phenylethyl]- l-phenyl-alanine-B-alanine} is a potent, highly specific, enkephalinase inhibitor that has marked analgesic effects in mammals. The present study examined the effects of SCH 34826 on opioid-mediated aversive thermal (nociceptive) responses of an invertebrate, the land snail, Cepaea nemoralis. SCH 34828 had significant, dose-related antinociceptive effects in Cepaea that were reduced by naloxone and completely blocked by the specific delta opiate antagonist, ICI-174,864, and only weakly affected by the specific kappa opiate antagonist nor-binaltrophimine. These findings with SCH 34826 suggest that an enkephalinase similar to that in vertebrates is present and involved in the mediation of opioid (enkephalin) activity in the snail, Cepaea.

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