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Specific G protein activation and mu-opioid receptor internalization caused by morphine, DAMGO and endomorphin I

N T Burford1, L M Tolbert, W Sadee

  • 1Department of Biopharmaceutical Sciences and Pharmaceutical Chemistry, University of California, San Francisco 94143-0446, USA. ntburf@itsa.ucsf.edu

Insights

Morphine, DAMGO, and endomorphin I activate G proteins similarly, but only DAMGO and endomorphin I induce mu-opioid receptor internalization. This suggests receptor internalization is independent of G protein activation.

Area of Science:

  • Pharmacology
  • Molecular Biology
  • Cell Biology

Background:

  • Mu-opioid receptor (MOR) signaling is complex, involving G protein activation and receptor trafficking.
  • Previous research indicated that agonists like DAMGO induce MOR internalization, unlike morphine.

Purpose of the Study:

  • To investigate the relationship between MOR internalization and specific G protein activation by morphine, DAMGO, and endomorphin I.
  • To elucidate the signaling pathways downstream of MOR activation.

Main Methods:

  • Utilized human embryonic kidney (HEK) cells expressing MOR.
  • Assessed MOR internalization via ligand treatment.
  • Measured G protein activation (Gi1α/Gi2α, Gαo, Gi3α, Gqα/G11α, Gsα) in HEK cell membranes using specific assays.

Main Results:

  • Endomorphin I and DAMGO, but not morphine, induced significant mu-opioid receptor internalization.
  • Morphine, DAMGO, and endomorphin I activated Gi1α/Gi2α, Gαo, and Gi3α to comparable levels.
  • No significant activation of Gqα/G11α or Gsα was observed for any of the tested ligands.

Conclusions:

  • Mu-opioid receptor internalization is not directly correlated with the activation of specific G proteins (Gi1α/Gi2α, Gαo, Gi3α) by morphine, DAMGO, and endomorphin I.
  • Ligand-specific pathways likely regulate MOR internalization, independent of broad G protein activation patterns.

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