Evidence map›Paper›PMID 29342106›Full record

ArticleInternational journal of molecular sciences2018

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"?

Robert Root-Bernstein, Miah Turke, Udaya K Tiruttani Subhramanyam, Beth Churchill, Joerg Labahn

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

11 citing papers in PubMed, 21 citations in OpenAlex.

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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

5 authors at 2 institutions in 2 countries.

Robert Root-BernsteinDepartment of Physiology, Michigan State University, 567 Wilson Road, Room 2201 Biomedical and Physical Sciences Building, East Lansing, MI 48824, USA. rootbern@msu.edu.ORCID 0000-0002-3298-9306
Miah TurkeDepartment of Physiology, Michigan State University, 567 Wilson Road, Room 2201 Biomedical and Physical Sciences Building, East Lansing, MI 48824, USA. turkemia@msu.edu.
Udaya K Tiruttani SubhramanyamCentre for Structural Systems Biology (CSSB), Notkestraße 85, 22607 Hamburg, Germany. udaya.tiruttani@desy.de.
Beth ChurchillDepartment of Physiology, Michigan State University, 567 Wilson Road, Room 2201 Biomedical and Physical Sciences Building, East Lansing, MI 48824, USA. church49@msu.edu.
Joerg LabahnCentre for Structural Systems Biology (CSSB), Notkestraße 85, 22607 Hamburg, Germany. j.labahn@fz-juelich.de.
Michigan State University · USForschungszentrum Jülich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Extensive evidence demonstrates functional interactions between the adrenergic and opioid systems in a diversity of tissues and organs. While some effects are due to receptor and second messenger cross-talk, recent research has revealed an extracellular, allosteric opioid binding site on adrenergic receptors that enhances adrenergic activity and its duration. The present research addresses whether opioid receptors may have an equivalent extracellular, allosteric adrenergic binding site that has similar enhancing effects on opioid binding. Comparison of adrenergic and opioid receptor sequences revealed that these receptors share very significant regions of similarity, particularly in some of the extracellular and transmembrane regions associated with adrenergic binding in the adrenergic receptors. Five of these shared regions from the mu opioid receptor (muOPR) were synthesized as peptides and tested for binding to adrenergic, opioid and control compounds using ultraviolet spectroscopy. Adrenergic compounds bound to several of these muOPR peptides with low micromolar affinity while acetylcholine, histamine and various adrenergic antagonists did not. Similar studies were then conducted with purified, intact muOPR with similar results. Combinations of epinephrine with methionine enkephalin or morphine increased the binding of both by about half a log unit. These results suggest that muOPR may be allosterically enhanced by adrenergic agonists.

Indexed as

Protein Interaction Domains and MotifsAcetylcholineAdrenergic AgonistsAmino Acid SequenceAnimalsEnkephalin, MethionineHistamineHumansMethionineMiceMorphineProtein BindingReceptors, Adrenergic, alpha-1Receptors, Opioid, muSpectrophotometry, UltravioletAcetylcholineAdrenergic AgonistsEnkephalin, MethionineHistamineMethionineMorphineReceptors, Adrenergic, alpha-1Receptors, Opioid, muallostericbiased opioidsdimerizationenhancementepinephrinemethionine-enkephalinmorphinemu opioid receptornorepinephrinereceptor dimerssynergy

Identifiers

PMID29342106
PMCPMC5796218
OpenAlexW2785557807

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.