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Hsp90β positively regulates μ-opioid receptor function.

Yixin Zhang1, Peilan Zhou1, Zhen Wang2

  • 1State Key Laboratory of Toxicology and Medical Countermeasures, Beijing Key Laboratory of Neuropsychopharmacology, Beijing Institute of Pharmacology and Toxicology, 27th Taiping Road, Beijing 100850, China.

Life Sciences
|April 19, 2020
PubMed
Summary

Heat shock protein 90 beta (Hsp90β) positively regulates μ-opioid receptor (MOR) signaling. Inhibiting Hsp90β with 17-AAG reduces morphine tolerance and dependence, suggesting therapeutic potential.

Keywords:
17-AAGDependenceHsp90βToleranceμ-Opioid receptor

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Area of Science:

  • Pharmacology
  • Molecular Biology
  • Neuroscience

Background:

  • The μ-opioid receptor (MOR) signaling pathway is modulated by associated proteins.
  • Heat shock protein 90 isoform beta (Hsp90β) was identified as a MOR-interacting protein.

Purpose of the Study:

  • To investigate the role of Hsp90β in MOR signaling transduction and function.
  • To explore the therapeutic potential of Hsp90β modulation in opioid treatment.

Main Methods:

  • Co-immunoprecipitation and immunofluorescence confirmed Hsp90β-MOR interaction.
  • In vitro and in vivo studies assessed Hsp90β's effects on MOR signaling.
  • Morphine tolerance and dependence were evaluated using hot plate and CPP tests with the Hsp90β inhibitor 17-AAG.

Main Results:

  • Hsp90β, not Hsp90α, interacted with MOR, enhanced by morphine.
  • Hsp90β-MOR complex modulated cAMP, PKA, MOR phosphorylation, and internalization.
  • 17-AAG inhibited Hsp90β-MOR interaction, reduced morphine anti-nociception, and attenuated tolerance and dependence.

Conclusions:

  • Hsp90β acts as a positive co-regulator of MOR signaling through G-protein and β-arrestin pathways.
  • Hsp90β modulation offers potential to improve the pharmacological profile of opiates.
  • Hsp90β inhibitors like 17-AAG may reduce opioid-induced tolerance and dependence in clinical settings.