Mutation S363A in the human delta-opioid receptor selectively reduces down-regulation by a peptide agonist

Eur J Pharmacol. 2004 Feb 6;485(1-3):341-3. doi: 10.1016/j.ejphar.2003.11.067.

Abstract

Chemically distinct opioid agonists have different abilities to down-regulate opioid receptors. The present study investigated the role of Ser(363) in human delta-opioid receptor down-regulation by a delta-selective peptide- and non-peptide agonist. Cyclic[D-Pen(2),D-Pen(5)]enkephalin (DPDPE)-mediated down-regulation was significantly attenuated by a S363A mutation. In contrast, this mutation had no effect on down-regulation by (+)-4-[(alpha R)-alpha-((2S,5R)-4-allyl-2,5-dimethyl-1-piperazinyl)-3-methoxybenzyl]N,N-diethylbenzamide (SNC80). These results demonstrate that the molecular mechanism of the human delta-opioid receptor down-regulation is agonist-specific.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alanine / genetics
  • Amino Acid Substitution / genetics*
  • Benzamides / pharmacology
  • Down-Regulation / drug effects
  • Down-Regulation / genetics*
  • Enkephalin, D-Penicillamine (2,5)- / agonists*
  • Enkephalin, D-Penicillamine (2,5)- / pharmacology
  • Humans
  • Mutation*
  • Piperazines / pharmacology
  • Receptors, Opioid, delta / agonists*
  • Receptors, Opioid, delta / genetics*
  • Serine / genetics

Substances

  • Benzamides
  • Piperazines
  • Receptors, Opioid, delta
  • 4-(alpha-(4-allyl-2,5-dimethyl-1-piperazinyl)-3-methoxybenzyl)-N,N-diethylbenzamide
  • Serine
  • Enkephalin, D-Penicillamine (2,5)-
  • Alanine