scholarly journals Adrenergic Agonists Bind to Adrenergic-Receptor-Like Regions of the Mu Opioid Receptor, Enhancing Morphine and Methionine-Enkephalin Binding: A New Approach to “Biased Opioids”?

2018 ◽  
Vol 19 (1) ◽  
pp. 272 ◽  
Author(s):  
Robert Root-Bernstein ◽  
Miah Turke ◽  
Udaya Subhramanyam ◽  
Beth Churchill ◽  
Joerg Labahn
Keyword(s):  
Opioid Receptor ◽  
Adrenergic Receptor ◽  
Mu Opioid Receptor ◽  
Adrenergic Agonists ◽  
New Approach ◽  
Methionine Enkephalin ◽  
Mu Opioid

scholarly journals Dual single-scission event analysis of constitutive transferrin receptor (TfR) endocytosis and ligand-triggered β2-adrenergic receptor (β2AR) or Mu-opioid receptor (MOR) endocytosis

2014 ◽  
Vol 25 (19) ◽  
pp. 3070-3080 ◽  
Author(s):  
Marko Lampe ◽  
Fabienne Pierre ◽  
Suleiman Al-Sabah ◽  
Cornelius Krasel ◽  
Christien J. Merrifield
Keyword(s):  
Opioid Receptor ◽  
Transferrin Receptor ◽  
Adrenergic Receptor ◽  
Mu Opioid Receptor ◽  
Event Analysis ◽  
Coated Pits ◽  
Mu Opioid ◽  
Dynamic Relationship ◽  
Β2 Adrenergic Receptor ◽  
Endocytic Vesicles

The dynamic relationship between constitutive and ligand-triggered clathrin-mediated endocytosis is only poorly characterized, and it remains controversial whether clathrin-coated pits specialize to internalize particular receptor cargo. Here we analyzed the ligand-triggered endocytosis of the model G-protein–coupled receptors (GPCRs) β2-adrenergic receptor (β2AR) and Mu-opioid receptor (MOR) at the level of individual endocytic events using a total internal reflection fluorescence microscopy (TIRFM)–based assay. Similar to the constitutive endocytosis of transferrin receptor (TfR), ligand- triggered endocytosis of β2AR occurs via quantized scission events hosted by clathrin spots and plaques of variable size and persistence. To address whether clathrin-coated structures (CCSs) specialize to internalize particular GPCRs, we adapted the TIRFM imaging assay to simultaneously quantify the internalization of TfR and the ligand- triggered endocytosis of the β2AR or MOR. Agonist-triggered β2AR or MOR endocytosis extended the maturation time of CCSs, as shown previously, but did not affect the rate of constitutive TfR endocytosis or loading of TfR into individual endocytic vesicles. Both the β2AR and the MOR receptors entered cells in the same vesicles as TfR, and the overall evidence for CCS specialization was weak. These data support a simple model in which different cargoes internalize through common CCSs.

scholarly journals Variation of the human mu-opioid receptor (OPRM1) gene predicts vulnerability to frustration

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Alan M. Daniel ◽  
Brenda G. Rushing ◽  
Karla Y. Tapia Menchaca
Keyword(s):  
Individual Differences ◽  
Animal Models ◽  
Opioid Receptor ◽  
Receptor Gene ◽  
Emotional Reaction ◽  
Mu Opioid Receptor ◽  
Reward Processing ◽  
Physical Pain ◽  
Mu Opioid ◽  
Allelic Differences

AbstractUnderstanding the emotional reaction to loss, or frustration, is a critical problem for the field of mental health. Animal models of loss have pointed to the opioid system as a nexus of frustration, physical pain, and substance abuse. However, few attempts have been made to connect the results of animal models of loss to human behavior. Allelic differences in the human mu opioid receptor gene, notably the A118G single nucleotide polymorphism, have been linked to individual differences in pain sensitivity, depressive symptoms, and reward processing. The present study explored the relationship between A118G and behavior in two frustrating tasks in humans. Results showed that carriers of the mutant G-allele were slower to recover behavior following a reward downshift and abandoned a frustrating task earlier than those without the mutation. Additionally, G-carriers were more sensitive to physical pain. These results highlight the overlap between frustration and pain, and suggest that genetic variation in opioid tone may contribute to individual differences in vulnerability and resilience following emotional disturbances.

scholarly journals Allelic expression imbalance of human mu opioid receptor (OPRM1) caused by variant A118G. VOLUME 280 (2005) PAGES 32618-32624

2005 ◽  
Vol 280 (46) ◽  
pp. 38888
Author(s):  
Ying Zhang ◽  
Danxin Wang ◽  
Andrew D. Johnson ◽  
Audrey C. Papp ◽  
Wolfgang Sadée
Keyword(s):  
Opioid Receptor ◽  
Mu Opioid Receptor ◽  
Allelic Expression ◽  
Allelic Expression Imbalance ◽  
Mu Opioid

scholarly journals Naltrexone is neuroprotective against traumatic brain injury in mu opioid receptor knockout mice

2021 ◽  
Author(s):  
Yu‐Syuan Wang ◽  
Tsai‐Wei Hung ◽  
Eun‐Kyung Bae ◽  
Kuo‐Jen Wu ◽  
Wei Hsieh ◽  
...  
Keyword(s):  
Traumatic Brain Injury ◽  
Brain Injury ◽  
Opioid Receptor ◽  
Knockout Mice ◽  
Mu Opioid Receptor ◽  
Mu Opioid
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