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Related Experiment Videos

Morphine activates opioid receptors without causing their rapid internalization

D E Keith1, S R Murray, P A Zaki

  • 1Department of Psychiatry and Biobehavioral Sciences, University of California, Los Angeles, California 90024, USA.

The Journal of Biological Chemistry
|August 9, 1996
PubMed
Summary
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Agonist drugs like etorphine rapidly internalize opioid receptors, but morphine does not, revealing distinct trafficking pathways for G protein-coupled receptors despite similar signaling effects.

Area of Science:

  • Molecular Pharmacology
  • Cell Biology
  • G protein-coupled receptor (GPCR) trafficking

Background:

  • Opioid receptors (delta and mu) are G protein-coupled receptors activated by various ligands.
  • Receptor trafficking, including endocytosis, is crucial for regulating cellular responses to agonists.

Purpose of the Study:

  • To investigate the endocytic trafficking patterns of delta and mu opioid receptors.
  • To compare the effects of different agonists (peptide enkephalins, etorphine, morphine) on opioid receptor internalization.

Main Methods:

  • Epitope-tagged delta and mu opioid receptors were expressed in human embryonic kidney (HEK) 293 cells.
  • Internalization was assessed by monitoring receptor localization in endosomes and response to hypertonic media.

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Main Results:

  • Enkephalins and etorphine induced rapid internalization of opioid receptors (t1/2 ~6 min).
  • Internalized receptors colocalized with transferrin in endosomes, indicating a common endocytic pathway.
  • Morphine, despite potent signaling (adenylyl cyclase inhibition), failed to stimulate rapid internalization of either receptor type.

Conclusions:

  • Agonist ligands with similar signaling potencies can exhibit markedly different effects on GPCR intracellular trafficking.
  • This suggests distinct endocytic mechanisms are engaged by different classes of opioid receptor agonists.