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Nitric oxide modulates μ-opioid receptor function in vitro.

Lillian Huang1,2, Bruce D Wyse2, Craig M Williams3

  • 1School of Pharmacy, Faculty of Health and Behavioural Sciences, The University of Queensland, Brisbane, Queensland, Australia.

Clinical and Experimental Pharmacology & Physiology
|April 2, 2019
PubMed
Summary

Nitric oxide (NO) modulates μ-opioid receptor signaling in painful diabetic neuropathy (PDN). PRG150, an NO donor, requires the MOP receptor for cellular effects, independent of classical binding sites, suggesting a novel therapeutic pathway for PDN pain.

Keywords:
3-methylfuroxan-4-carbaldehydePRG150morphinemu opioid (MOP) receptornitric oxidenon-receptor tyrosine kinasesrc

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Area of Science:

  • Neuroscience
  • Pharmacology
  • Biochemistry

Background:

  • Painful diabetic neuropathy (PDN) is characterized by neuropathic pain and morphine hyposensitivity due to prolonged hyperglycemia.
  • Nitric oxide (NO) and its precursors/donors have shown potential in alleviating pain and restoring opioid efficacy in preclinical models of PDN.
  • Previous studies suggest a role for NO in modulating μ-opioid (MOP) receptor signaling, but the precise mechanism remains unclear.

Purpose of the Study:

  • To investigate the role of nitric oxide (NO) released from the NO donor PRG150 in modulating MOP receptor function in vitro.
  • To determine the specific opioid receptor subtypes and signaling pathways involved in PRG150's cellular effects.

Main Methods:

  • Utilized HEK-MOP cells to assess the effects of PRG150 on forskolin-stimulated cAMP responses.
  • Investigated the requirement for MOP, DOP, and KOP receptors in PRG150's cellular actions.
  • Examined the involvement of naloxone-sensitive binding sites, pertussis toxin (PTX)-sensitive Gi/o proteins, membrane lipid rafts, and src kinase.

Main Results:

  • PRG150's cellular effects on cAMP responses were absolutely dependent on the MOP receptor, but not DOP or KOP receptors.
  • PRG150 did not interact with the classical naloxone-sensitive binding site of the MOP receptor, and its effects were naloxone-insensitive.
  • The inhibitory effects of PRG150 on cAMP responses were mediated by PTX-sensitive Gi/o proteins, membrane lipid rafts, and src kinase.

Conclusions:

  • NO released from PRG150 modulates MOP receptor function through a non-classical, naloxone-insensitive pathway.
  • This NO-mediated signaling involves PTX-sensitive Gi/o proteins, lipid rafts, and src kinase, distinct from canonical opioid receptor activation.
  • These findings highlight a novel mechanism for NO in regulating MOP receptor signaling, with potential therapeutic implications for managing PDN.