Evidence map›Paper›PMID 22433979›Full record

ArticleBrain research2012

Sigma-1 receptor alters the kinetics of Kv1.3 voltage gated potassium channels but not the sensitivity to receptor ligands.

Maho Kinoshita, Yoshikazu Matsuoka, Takeshi Suzuki, Jennifer Mirrielees, Jay Yang

Abstract read
In one paragraph

Article in Brain research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed, 2 pooled it
1.7field-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

33 citing papers in PubMed, 2 syntheses or guidelines pooled it, 53 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Sigma 1 Receptor and Its Pivotal Role in Neurological Disorders.ACS pharmacology & translational science · 2025
    Review
  4. Review
  5. Sigma-1 receptor and seizures.Pharmacological research · 2023
    Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Partners in Crime: Towards New Ways of Targeting Calcium Channels.International journal of molecular sciences · 2019
    Review
  13. Review
  14. Article
  15. Review
  16. Role of Sigma Receptors in Alcohol Addiction.Frontiers in pharmacology · 2019
    Review
  17. Review
  18. Review
  19. Review
  20. TRPV1 channels and the progesterone receptor Sig-1R interact to regulate pain.Proceedings of the National Academy of Sciences of the United States of America · 2018
    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

5 authors at 1 institution in 1 country.

Maho KinoshitaDepartment of Anesthesiology, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706, USA. mkinoshita@wisc.edu
Yoshikazu Matsuoka
Takeshi Suzuki
Jennifer Mirrielees
Jay Yang
University of Wisconsin–Madison · US

Funding

Mitochondrial Kv1.3 potassium channels and lymphocyte apoptosis in sepsisR01GM086401 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI YANG, JAY · 2008 to 2011
$1.2M
NIGMS NIH HHS R01 GM086401NIGMS NIH HHS R01GM086401
6 · The paper itself

Abstract

Sigma1 receptors (Sigma1R) are intracellular chaperone proteins that bind psychotropic drugs and also clinically used drugs such as ketamine and haloperidol. Co-expression of the Sigma1R has been reported to enhance the sensitivity of several voltage-gated ion channels to Sigma1R ligands. Kv1.3 is the predominant voltage-gated potassium channel expressed in T lymphocytes with a documented role in immune activation. To gain a better understanding of Sigma1R modulation of Kv ion channels, we investigated the effects of Sigma1R co-expression on Kv1.3 physiology and pharmacology in ion channels expressed in Xenopus oocytes. We also explored the protein domains of Kv1.3 necessary for protein:protein interaction between Kv1.3 and Sigma1R through co-immunoprecipitation studies. Slowly inactivating outward-going currents consistent with Kv1.3 expression were elicited on step depolarizations. The current characterized by E(rev), V(1/2), and slope factor remained unchanged when co-expressed with Sigma1R. Analysis of inactivation time constant revealed a faster Kv1.3 current decay when co-expressed with Sigma1R. However the sensitivity to Sigma1R ligands remained unaltered when co-expressed with the Sigma1R in contrast to the previously reported modulation of ligand sensitivity in closely related Kv1.4 and Kv1.5 voltage gated potassium channels. Co-immunoprecipitation assays of various Kv1.3 truncation constructs indicated that the transmembrane domain of the Kv1.3 protein was responsible for the protein:protein interaction with the Sigma1R. Sigma1R likely interacts with different domains of Kv ion channel family proteins resulting in distinct modulation of different channels.

Indexed as

AnimalsFemaleHumansKv1.3 Potassium ChannelKv1.4 Potassium ChannelKv1.5 Potassium ChannelLigandsOocytesPatch-Clamp TechniquesProtein BindingReceptors, sigmaXenopusKv1.3 Potassium ChannelKv1.4 Potassium ChannelKv1.5 Potassium ChannelLigandsReceptors, sigma

Identifiers

PMID22433979
PMCPMC3670091
OpenAlexW2070900717

What OpenQuestion holds

Textmetadata
LicenceTDM
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.