Nociceptin receptor-mediated Ca2+ channel inhibition and its desensitization in NG108-15 cells

Eur J Pharmacol. 1998 Jun 19;351(2):247-52. doi: 10.1016/s0014-2999(98)00306-9.

Abstract

It has been shown that the membrane of hybrid NG108-15 neuroblastoma x glioma cells contains a high-affinity binding site for nociceptin. In the present study, we first demonstrated the expression of nociceptin receptor mRNA in NG108-15 cells. Application of nociceptin to NG108-15 cells produced a concentration-dependent (EC50 = 29 nM) inhibition of Ca2+ channel currents in a pertussis toxin-sensitive fashion. This nociceptin-induced inhibition of Ca2+ channel currents was prevented in the presence of omega-conotoxin GVIA, a blocker of the N-type Ca2+ channel, and had both voltage-dependent and -independent components. Prolonged application of nociceptin elicited homologous desensitization of the inhibition with a time constant of 5.3 min. These results indicate that the nociceptin receptor is coupled to the N-type Ca2+ channel via pertussis toxin-sensitive G proteins in NG108-15 cells and that this coupling is associated with rapid and homologous desensitization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calcium Channels / metabolism*
  • Cell Line
  • DNA Probes
  • GTP-Binding Proteins / metabolism
  • Hybrid Cells
  • Mice
  • Nociceptin
  • Nociceptin Receptor
  • Opioid Peptides / pharmacology
  • RNA, Messenger / metabolism
  • Rats
  • Receptors, Opioid / genetics
  • Receptors, Opioid / metabolism*

Substances

  • Calcium Channels
  • DNA Probes
  • Opioid Peptides
  • RNA, Messenger
  • Receptors, Opioid
  • GTP-Binding Proteins
  • Nociceptin Receptor