Evidence map›Paper›PMID 25557043›Full record

ArticleAntioxidants & redox signaling2015

The σ1 receptor engages the redox-regulated HINT1 protein to bring opioid analgesia under NMDA receptor negative control.

María Rodríguez-Muñoz, Pilar Sánchez-Blázquez, Raquel Herrero-Labrador, Ricardo Martínez-Murillo, Manuel Merlos, José Miguel Vela, Javier Garzón

Open access · hybridAbstract read
In one paragraph

Article in Antioxidants & redox signaling, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed, 1 pooled it
4.4field-weighted citation impact, top 5% 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

46 citing papers in PubMed, 1 synthesis or guideline pooled it, 76 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. The SigmaPharmacological reports : PR · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Sigma-1 receptor and seizures.Pharmacological research · 2023
    Review
  10. Review
  11. Article
  12. International journal of molecular sciences · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Involvement of Chaperone Sigma1R in the Anxiolytic Effect of Fabomotizole.International journal of molecular sciences · 2021
    Article
  18. Article
  19. Article
  20. Article
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

7 authors at 2 institutions in 2 countries.

María Rodríguez-Muñoz1 Neurofarmacología, Instituto Cajal, Consejo Superior de Investigaciones Científicas (CSIC) , Madrid, Spain .
Pilar Sánchez-Blázquez
Raquel Herrero-Labrador
Ricardo Martínez-Murillo
Manuel Merlos
José Miguel Vela
Javier Garzón
Consejo Superior de Investigaciones Científicas · ESDrug Discovery Laboratory (Norway) · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

aimsThe in vivo pharmacology of the sigma 1 receptor (σ1R) is certainly complex; however, σ1R antagonists are of therapeutic interest, because they enhance mu-opioid receptor (MOR)-mediated antinociception and reduce neuropathic pain. Thus, we investigated whether the σ1R is involved in the negative control that glutamate N-methyl-d-aspartate acid receptors (NMDARs) exert on opioid antinociception.

resultsThe MOR C terminus carries the histidine triad nucleotide-binding protein 1 (HINT1) coupled to the regulator of G-protein signaling RGSZ2-neural nitric oxide synthase assembly. Activated MORs stimulate the production of nitric oxide (NO), and the redox zinc switch RGSZ2 converts this signal into free zinc ions that are required to recruit the redox sensor PKCγ to HINT1 proteins. Then, PKCγ impairs HINT1-RGSZ2 association and enables σ1R-NR1 interaction with MOR-HINT1 complexes to restrain opioid signaling. The inhibition of NOS or the absence of σ1Rs prevents HINT1-PKCγ interaction, and MOR-NMDAR cross-regulation fails. The σ1R antagonists transitorily remove the binding of σ1Rs to NR1 subunits, facilitate the entrance of negative regulators of NMDARs, likely Ca(2+)-CaM, and prevent NR1 interaction with HINT1, thereby impairing the negative feedback of glutamate on opioid analgesia. INNOVATION: A redox-regulated process situates MOR signaling under NMDAR control, and in this context, the σ1R binds to the cytosolic C terminal region of the NMDAR NR1 subunit.

conclusionThe σ1R antagonists enhance opioid analgesia in naïve mice by releasing MORs from the negative influence of NMDARs, and they also reset antinociception in morphine tolerant animals. Moreover, σ1R antagonists alleviate neuropathic pain, probably by driving the inhibition of up-regulated NMDARs.

Indexed as

Analgesics, OpioidAnimalsCell MembraneMiceMice, KnockoutMorphineNerve Tissue ProteinsNitric OxideOxidation-ReductionProtein Kinase CReceptors, N-Methyl-D-AspartateReceptors, sigmaRGS ProteinsSigma-1 ReceptorZincAnalgesics, OpioidHint1 protein, mouseMorphineNerve Tissue ProteinsNitric OxideProtein Kinase Cprotein kinase C gammaReceptors, N-Methyl-D-AspartateReceptors, sigmaRGS17 protein, mouseRGS ProteinsSigma-1 ReceptorZinc

Identifiers

PMID25557043
PMCPMC4367239
OpenAlexW2328689172

What OpenQuestion holds

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LicenceCC BY-NC
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Registered trials

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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.