Evidence map›Paper›PMID 15905217›Full record

ArticleThe Journal of physiology2005

Specificity of TRH receptor coupling to G-proteins for regulation of ERG K+ channels in GH3 rat anterior pituitary cells.

Pablo Miranda, Teresa Giráldez, Pilar de la Peña, Diego G Manso, Carlos Alonso-Ron, David Gómez-Varela, Pedro Domínguez, Francisco Barros

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 30% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Biochemical and physiological insights into TRH receptor-mediated signaling.Frontiers in cell and developmental biology · 2022
    Review
  4. Conformation-sensitive antibody reveals an altered cytosolic PAS/CNBh assembly during hERG channel gating.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  5. Influence of Kv11.1 (hERG1) KPflugers Archiv : European journal of physiology · 2021
    Article
  6. Ether-à-go-go KThe Journal of physiology · 2018
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Phosphatidylinositol 4,5-bisphosphate interactions with the HERG K(+) channel.Pflugers Archiv : European journal of physiology · 2007
    Review
  14. 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 1 institution in 1 country.

Pablo MirandaDepartamento de Bioquímica y Biología Molecular, Edificio Santiago Gascón, Campus del Cristo, Universidad de Oviedo, E-33006, Oviedo, Asturias, Spain.
Teresa Giráldez
Pilar de la Peña
Diego G Manso
Carlos Alonso-Ron
David Gómez-Varela
Pedro Domínguez
Francisco Barros
Universidad de Oviedo · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The identity of the G-protein coupling thyrotropin-releasing hormone (TRH) receptors to rat ether-à-go-go related gene (r-ERG) K+ channel modulation was studied in situ using perforated-patch clamped adenohypophysial GH(3) cells and dominant-negative variants (Galpha-QL/DN) of G-protein alpha subunits. Expression of dominant-negative Galpha(q/11) that minimizes the TRH-induced Ca2+ signal had no effect on r-ERG current inhibition elicited by the hormone. In contrast, the introduction of dominant-negative variants of Galpha13 and the small G-protein Rho caused a significant loss of the inhibitory effect of TRH on r-ERG. A strong reduction of this TRH effect was also obtained in cells expressing either dominant-negative Galpha(s) or transducin alpha subunits, an agent known to sequester free G-protein betagamma dimers. As a further indication of specificity of the dominant-negative effects, only the dominant-negative variants of Galpha13 and Rho (but not Galpha(s)-QL/DN or Galpha(t)) were able to reduce the TRH-induced shifts of human ERG (HERG) activation voltage dependence in HEK293 cells permanently expressing HERG channels and TRH receptors. Our results demonstrate that whereas the TRH receptor uses a G(q/11) protein for transducing the Ca2+ signal during the initial response to TRH, this G-protein is not involved in the TRH-induced inhibition of endogenous r-ERG currents in pituitary cells. They also identify G(s) (or a G(s)-like protein) and G13 as important contributors to the hormonal effect in these cells and suggest that betagamma dimers released from these proteins may participate in modulation of ERG currents triggered by TRH.

Indexed as

AnimalsCell LineEther-A-Go-Go Potassium ChannelsGTP-Binding ProteinsHumansIon Channel GatingKidneyPituitary GlandPotassium ChannelsProtein BindingRatsReceptors, Thyrotropin-Releasing HormoneEther-A-Go-Go Potassium ChannelsGTP-Binding ProteinsPotassium ChannelsReceptors, Thyrotropin-Releasing Hormone

Identifiers

PMID15905217
PMCPMC1464777
OpenAlexW1588175596

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.