Evidence map›Paper›PMID 17510191›Full record

ArticleThe Journal of physiology2007

TRPM7 channel is sensitive to osmotic gradients in human kidney cells.

Bret F Bessac, Andrea Fleig

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Osmoregulatory inositol transporter SMIT1 modulates electrical activity by adjusting PI(4,5)P2 levels.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Article
  16. Article
  17. Role of TRP channels in the cardiovascular system.American journal of physiology. Heart and circulatory physiology · 2015
    Review
  18. Article
  19. TRPM7.Handbook of experimental pharmacology · 2014
    Review
  20. TRPM7 is regulated by halides through its kinase domain.Cellular and molecular life sciences : CMLS · 2013
    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

2 authors at 1 institution in 1 country.

Bret F BessacLaboratory of Cell and Molecular Signalling, Center for Biomedical Research at The Queen's Medical Center and John A. Burns School of Medicine at the University of Hawaii, Honolulu, Hawaii 96813, USA.
Andrea Fleig
Queen's Medical Center · US

Funding

Magnesium-nucleotide depletion activated ion channelR01GM065360 · NIGMS · QUEEN'S MEDICAL CENTER · PI FLEIG, ANDREA · 2002 to 2005
$1.1M
NIGMS NIH HHS R01 GM065360NIGMS NIH HHS R01-GM65360
6 · The paper itself

Abstract

TRPM7 (transient-receptor-potential melastatin 7) is an ion channel with alpha-kinase function. TRPM7 is divalent-selective and regulated by a range of receptor-stimulated second messenger pathways, intracellular Mg-nucleotides, divalent and polyvalent cations and pH. TRPM7 is ubiquitously found in mammalian cells, including kidney, the responsible organ for osmolyte regulation, posing the question whether the channel is osmosensitive. Recent reports investigated the sensitivity of native TRPM7-like currents to cell swelling with contradictory results. Here, we assess the sensitivity of TRPM7 to both hypo- and hyperosmotic conditions and explored the involvement of the channel's kinase domain. We find that hypotonicity facilitates TRPM7 at elevated intracellular magnesium and Mg.ATP (3-4 mm), but has no effect in the absence of these solutes. Hypertonic conditions, in contrast, inhibit TRPM7 with an IC(50) of 430 mosmol l(-1). This inhibitory effect is maintained in the complete absence of intra- and extracellular divalent ions, although shifted to higher osmolarities (IC(50) = 510 mosmol l(-1)). TRPM7 senses osmotic gradients rather than ionic strength and this is independent of cAMP or not affected by cytochalasin D treatment. Furthermore, the kinase-domain deletion mutant of TRPM7 shows a similar behaviour to osmolarity as the wild-type protein, both in the presence and absence of divalent ions. This indicates that at least part of the osmosensitivity resides in the channel domain. Physiologically, TRPM7 channels do not seem to play an active role in regulatory volume changes, but rather those volume changes modulate TRPM7 activity through changes in the cytosolic concentrations of free Mg, Mg-nucleotides and a further unidentified factor. We conclude that TRPM7 senses osmotically induced changes primarily through molecular crowding of solutes that affect channel activity.

Indexed as

Cell LineCell SizeCyclic AMPCytochalasin DHumansKidneyOsmolar ConcentrationPatch-Clamp TechniquesProtein Serine-Threonine KinasesTRPM Cation ChannelsCyclic AMPCytochalasin DProtein Serine-Threonine KinasesTRPM7 protein, humanTRPM Cation Channels

Identifiers

PMID17510191
PMCPMC2075261
OpenAlexW2145599647

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.