Evidence map›Paper›PMID 35061679›Full record

ArticlePloS one2022

MOP and NOP receptor interaction: Studies with a dual expression system and bivalent peptide ligands.

M F Bird, J McDonald, B Horley, J P O'Doherty, B Fraser, C L Gibson, R Guerrini, G Caló, D G Lambert

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.4field-weighted citation impact, top 21% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed, 14 citations in OpenAlex.

  1. Structural Modification and Development ofJournal of medicinal chemistry · 2026
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 2 countries.

M F BirdDepartment of Cardiovascular Sciences, Anaesthesia, Critical Care and Pain Management, University of Leicester, Leicester, United Kingdom.
J McDonaldDepartment of Cardiovascular Sciences, Anaesthesia, Critical Care and Pain Management, University of Leicester, Leicester, United Kingdom.
B HorleyDepartment of Cardiovascular Sciences, Anaesthesia, Critical Care and Pain Management, University of Leicester, Leicester, United Kingdom.
J P O'DohertyDepartment of Cardiovascular Sciences, Anaesthesia, Critical Care and Pain Management, University of Leicester, Leicester, United Kingdom.
B FraserDepartment of Neuroscience, Psychology and Behaviour, University of Leicester, Leicester, United Kingdom.
C L GibsonSchool of Psychology, University of Nottingham, Psychology Building, University Park, Nottingham, United Kingdom.
R GuerriniDepartment of Chemical, Pharmaceutical and Agricultural Sciences, University of Ferrara, Ferrara, Italy.
G CalóDepartment of Pharmaceutical and Pharmacological Sciences, University of Padova, Padova, Italy.
D G LambertDepartment of Cardiovascular Sciences, Anaesthesia, Critical Care and Pain Management, University of Leicester, Leicester, United Kingdom.ORCID 0000-0003-4769-8090
University of Leicester · GBUniversity of Ferrara · ITUniversity of Nottingham · GBUniversity of Padua · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Opioids targeting mu;μ (MOP) receptors produce analgesia in the peri-operative period and palliative care. They also produce side effects including respiratory depression, tolerance/dependence and addiction. The N/OFQ opioid receptor (NOP) also produces analgesia but is devoid of the major MOP side effects. Evidence exists for MOP-NOP interaction and mixed MOP-NOP ligands produce analgesia with reduced side effects. We have generated a HEKMOP/NOP human expression system and used bivalent MOP-NOP and fluorescent ligands to (i) probe for receptor interaction and (ii) consequences of that interaction. We used HEKMOP/NOP cells and two bivalent ligands; Dermorphin-N/OFQ (MOP agonist-NOP agonist; DeNO) and Dermorphin-UFP101 (MOP agonist-NOP antagonist; De101). We have determined receptor binding profiles, GTPγ[35S] binding, cAMP formation and ERK1/2 activation. We have also probed MOP and NOP receptor interactions in HEK cells and hippocampal neurones using the novel MOP fluorescent ligand, DermorphinATTO488 and the NOP fluorescent ligand N/OFQATTO594. In HEKMOP/NOP MOP ligands displaced NOP binding and NOP ligands displaced MOP binding. Using fluorescent probes in HEKMOP/NOP cells we demonstrated MOP-NOP probe overlap and a FRET signal indicating co-localisation. MOP-NOP were also co-localised in hippocampal tissue. In GTPγ[35S] and cAMP assays NOP stimulation shifted the response to MOP rightwards. At ERK1/2 the response to bivalent ligands generally peaked later. We provide evidence for MOP-NOP interaction in recombinant and native tissue. NOP activation reduces responsiveness of MOP activation; this was shown with conventional and bivalent ligands.

Indexed as

Nociceptin ReceptorOpioid PeptidesReceptors, OpioidReceptors, Opioid, muAnimalsCyclic AMPHEK293 CellsHumansLigandsMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3NeuronsPeptidesProtein BindingCyclic AMPdermorphinLigandsMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Nociceptin ReceptorOpioid PeptidesOPRL1 protein, humanPeptidesReceptors, OpioidReceptors, Opioid, mu

Identifiers

PMID35061679
PMCPMC8782398
OpenAlexW4207035970

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.