Evidence map›Paper›PMID 8558596›Full record

ArticleThe Journal of membrane biology1995

Human macrophages contain a stretch-sensitive potassium channel that is activated by adherence and cytokines.

D K Martin, M R Bootcov, T J Campbell, P W French, S N Breit

Abstract read
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Article in The Journal of membrane biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

13 citing papers in PubMed, 57 citations in OpenAlex.

  1. Targeting myeloid cell-mediated fibrosis through FAK.Nature biomedical engineering · 2026
    Article
  2. Review
  3. Article
  4. Downregulation of calponin 2 contributes to the quiescence of lung macrophages.American journal of physiology. Cell physiology · 2019
    Article
  5. Physical and mechanical regulation of macrophage phenotype and function.Cellular and molecular life sciences : CMLS · 2015
    Review
  6. Immune mediators of postoperative ileus.Langenbeck's archives of surgery · 2012
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. HIV-1 gp120 and chemokines activate ion channels in primary macrophages through CCR5 and CXCR4 stimulation.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  12. Article
  13. Involvement of stretch-activated Cl- channels in ramification of murine microglia.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998
    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 3 institutions in 2 countries.

D K MartinDepartment of Clinical Pharmacology, St. Vincent's Hospital, Sydney, New South Wales, Australia.
M R Bootcov
T J Campbell
P W French
S N Breit
St Vincent's Hospital Sydney · AUSt. Vincent's Birmingham · USUNSW Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A variety of stimuli, including cytokines and adhesion to surfaces and matrix proteins, can regulate macrophage function, in part through changes in Ca(2+)- dependent second messengers. While fluctuation in intracellular Ca2+ is an important modulator of cellular activation, little attention has been paid to the roles of other ions whose cytoplasmic concentrations can be rapidly regulated by ion channels. To examine the role of ion channels in macrophage function, we undertook patch clamp studies of human culture-derived macrophages grown under serum-free conditions. The major ionic current in these cells was carried by an outwardly rectifying K+ channel, which had a single-channel conductance of 229 pS in symmetrical K(+)-rich solution and macroscopic whole-cell conductance of 9.8 nS. These channels opened infrequently in resting cells but were activated immediately by (i) adhesion of mobile cells onto a substrate, (ii) stretch applied to isolated membrane patches in Ca(2+)-free buffers, (iii) intracellular Ca2+ (EC50 of 0.4 microM), and (iv) the cytokine IL-2. Furthermore, barium and 4-aminopyridine, blockers of this channel, altered the organization and structure of the cytoskeletal proteins actin, tubulin and vimentin. These cytoskeletal changes were associated with reversible alteration to the morphology of the cells. Thus, we have identified an outwardly rectifying K+ channel that appeared to be involved in cytokine and adherence-mediated macrophage activation, and in the maintenance of cytoskeletal integrity and cell shape.

Indexed as

Cell AdhesionCells, CulturedCytoskeletonHumansInterleukin-2Ion Channel GatingMacrophagesPotassium ChannelsStress, MechanicalInterleukin-2Potassium Channels

Identifiers

PMID8558596
OpenAlexW1976675460

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.