Evidence map›Paper›PMID 10748234›Full record

ArticleThe Journal of experimental medicine2000

Extracellular K(+) and opening of voltage-gated potassium channels activate T cell integrin function: physical and functional association between Kv1.3 channels and beta1 integrins.

M Levite, L Cahalon, A Peretz, R Hershkoviz, A Sobko, A Ariel, R Desai, B Attali, O Lider

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

81 citing papers in PubMed, 209 citations in OpenAlex.

  1. KArchiv der Pharmazie · 2026
    Article
  2. Ion channels and actin: A tale of two friends.Histology and histopathology · 2025
    Review
  3. Identification of Novel Kv1.3 Channel-Interacting Proteins Using Proximity Labelling in T-Cells.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. A Meta-Analysis Study to Infer Voltage-Gated KAntioxidants (Basel, Switzerland) · 2023
    Article
  9. Review
  10. Review
  11. Article
  12. Antagonistic roles of Ras-MAPK and Akt signaling in integrin-KFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022
    Article
  13. The voltage-gated KPlatelets · 2022
    Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Review

21 more citing papers are in PubMed but not listed here.

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

9 authors at 1 institution in 1 country.

M LeviteDepartment of Immunology, The Weizmann Institute of Science, Rehovot 76100, Israel. mia.levite@weizmann.ac.il
L Cahalon
A Peretz
R Hershkoviz
A Sobko
A Ariel
R Desai
B Attali
O Lider
Weizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Elevated extracellular K(+) ([K(+)](o)), in the absence of "classical" immunological stimulatory signals, was found to itself be a sufficient stimulus to activate T cell beta1 integrin moieties, and to induce integrin-mediated adhesion and migration. Gating of T cell voltage-gated K(+) channels (Kv1.3) appears to be the crucial "decision-making" step, through which various physiological factors, including elevated [K(+)](o) levels, affect the T cell beta1 integrin function: opening of the channel leads to function, whereas its blockage prevents it. In support of this notion, we found that the proadhesive effects of the chemokine macrophage-inflammatory protein 1beta, the neuropeptide calcitonin gene-related peptide (CGRP), as well as elevated [K(+)](o) levels, are blocked by specific Kv1.3 channel blockers, and that the unique physiological ability of substance P to inhibit T cell adhesion correlates with Kv1.3 inhibition. Interestingly, the Kv1.3 channels and the beta1 integrins coimmunoprecipitate, suggesting that their physical association underlies their functional cooperation on the T cell surface. This study shows that T cells can be activated and driven to integrin function by a pathway that does not involve any of its specific receptors (i.e., by elevated [K(+)](o)). In addition, our results suggest that undesired T cell integrin function in a series of pathological conditions can be arrested by molecules that block the Kv1.3 channels.

Indexed as

Potassium Channels, Voltage-GatedCell AdhesionCell MovementCell PolarityChemokine CCL4Electric ConductivityHumansIntegrin beta1Ion Channel GatingKv1.3 Potassium ChannelLymphocyte ActivationMacrophage Inflammatory ProteinsPotassiumPotassium Channel BlockersPotassium ChannelsSubstance PChemokine CCL4Integrin beta1KCNA3 protein, humanKv1.3 Potassium ChannelMacrophage Inflammatory ProteinsPotassiumPotassium Channel BlockersPotassium ChannelsPotassium Channels, Voltage-GatedSubstance P

Identifiers

PMID10748234
PMCPMC2193178
OpenAlexW2128957241

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.