The carboxyl terminus of mouse delta-opioid receptor is not required for agonist-dependent activation

Biochem Biophys Res Commun. 1997 Mar 17;232(2):513-6. doi: 10.1006/bbrc.1997.6324.

Abstract

The pharmacological effects caused by use of opiate are exerted through the opioid receptors (ORs). ORs couple to the inhibitory G protein (Gi) and result in decreased cAMP levels upon activation by specific agonists. To initiate study of the structure-function relationship during this process, we first ectopically expressed the wild-type delta OR and a C-terminally truncated mutant in CHO cells to investigate the necessity of its C-terminus. The binding potency of both the wild-type and truncated delta ORs to ligands including DPDPE, DSLET, DAGO, and U-50488 was compared. Their membrane localization and ability to mediate signal transduction were also studied. We conclude that the C-terminus of delta OR is not essential for plasma membrane targeting, ligand specificity, and agonist-dependent activation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence / physiology*
  • Animals
  • Biological Transport
  • CHO Cells
  • Cell Line
  • Cricetinae
  • Diprenorphine / metabolism
  • Enkephalin, D-Penicillamine (2,5)-
  • Enkephalin, Leucine / analogs & derivatives
  • Enkephalin, Leucine / metabolism
  • Enkephalins / metabolism
  • Humans
  • Kidney / embryology
  • Mice
  • Receptors, Opioid, delta / chemistry*
  • Receptors, Opioid, delta / physiology*
  • Signal Transduction*
  • Transfection

Substances

  • Enkephalins
  • Receptors, Opioid, delta
  • Diprenorphine
  • Enkephalin, Leucine
  • enkephalin, Ser(2), Leu(5), Thr(6)-
  • Enkephalin, D-Penicillamine (2,5)-