Evidence map›Paper›PMID 18482991›Full record

ArticleThe Journal of biological chemistry2008

Rapid, opioid-sensitive mechanisms involved in transient receptor potential vanilloid 1 sensitization.

Irina Vetter, Wei Cheng, Madusha Peiris, Bruce D Wyse, Sarah J Roberts-Thomson, Jie Zheng, Gregory R Monteith, Peter J Cabot

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

23 citing papers in PubMed, 65 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Opioid Receptors and Protonation-Coupled Binding of Opioid Drugs.International journal of molecular sciences · 2021
    Review
  6. Distribution and Assembly of TRP Ion Channels.Advances in experimental medicine and biology · 2021
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Capsaicin, Nociception and Pain.Molecules (Basel, Switzerland) · 2016
    Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. TRPV1: a stress response protein in the central nervous system.American journal of neurodegenerative disease · 2012
    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

8 authors at 2 institutions in 2 countries.

Irina VetterSchool of Pharmacy, The University of Queensland, St Lucia, Queensland 4072, Australia.
Wei Cheng
Madusha Peiris
Bruce D Wyse
Sarah J Roberts-Thomson
Jie Zheng
Gregory R Monteith
Peter J Cabot
University of Queensland · AUUniversity of California, Davis · US

Funding

EXTRAMURAL RESEARCH FACILITIES CONSTRUCTIONC06RR012088 · NCRR · UNIVERSITY OF CALIFORNIA DAVIS · PI CURRY, FITZ-ROY E · 1996 to 1996
–
NCRR NIH HHS C06 RR012088NCRR NIH HHS C06-RR-12088-01PHS HHS REY016754A
6 · The paper itself

Abstract

TRPV1 is a nociceptive, Ca2+-selective ion channel involved in the development of several painful conditions. Sensitization of TRPV1 responses by cAMP-dependent PKA crucially contributes to the development of inflammatory hyperalgesia. However, the pathways involved in potentiation of TRPV1 responses by cAMP-dependent PKA remain largely unknown. Using HEK cells stably expressing TRPV1 and the mu opioid receptor, we demonstrated that treatment with the adenylate cyclase activator forskolin significantly increased the multimeric TRPV1 species. Pretreatment with the mu opioid receptor agonist morphine reversed this increased TRPV1 multimerization. FRET analysis revealed that treatment with forskolin did not cause multimerization of pre-existing TRPV1 monomers on the plasma membrane and that intracellular pools of TRPV1 exist mostly as monomers in this model. This suggests that increased TRPV1 multimerization occurred from an intracellular store of inactive TRPV1 monomers. Treatment with forskolin also caused an increase in TRPV1 expression on the plasma membrane not resulting from increased TRPV1 expression, and this rapid TRPV1 translocation was inhibited by treatment with morphine. Thus, potentiation of TRPV1 responses by cAMP-dependent PKA involves plasma membrane insertion of functional TRPV1 multimers formed from an intracellular store of inactive TRPV1 monomers. This potentiation occurs rapidly and can be dynamically modulated by activation of the mu opioid receptor under conditions where cAMP levels are raised, such as with inflammation. Increased translocation and multimerization of TRPV1 channels provide a cellular mechanism for fine-tuning of nociceptive responses that allow for rapid modulation of TRPV1 responses independent of transcriptional changes.

Indexed as

Models, BiologicalAdenylyl CyclasesAnalgesics, OpioidAnimalsColforsinCyclic AMPCyclic AMP-Dependent Protein KinasesEnzyme ActivatorsFluorescence Resonance Energy TransferGene Expression RegulationHumansMaleMorphineProtein TransportRatsRats, WistarAdenylyl CyclasesAnalgesics, OpioidColforsinCyclic AMPCyclic AMP-Dependent Protein KinasesEnzyme ActivatorsMorphineReceptors, Opioid, muTRPV1 protein, humanTrpv1 protein, ratTRPV Cation Channels

Identifiers

PMID18482991
PMCPMC2443658
OpenAlexW2071677901

What OpenQuestion holds

Textmetadata
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.