Evidence map›Paper›PMID 19794142›Full record

ArticleAmerican journal of physiology. Cell physiology2009

Maitotoxin converts the plasmalemmal Ca(2+) pump into a Ca(2+)-permeable nonselective cation channel.

William G Sinkins, Mark Estacion, Vikram Prasad, Monu Goel, Gary E Shull, Diana L Kunze, William P Schilling

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

12 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Effect of protein S-glutathionylation on Ca2+ homeostasis in cultured aortic endothelial cells.American journal of physiology. Heart and circulatory physiology · 2011
    Article
  10. Article
  11. Article
  12. Review
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

7 authors at 3 institutions in 2 countries.

William G SinkinsDepartment of Physiology, Rammelkamp Center for Education and Research, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.
Mark Estacion
Vikram Prasad
Monu Goel
Gary E Shull
Diana L Kunze
William P Schilling
Laboratory of Molecular Genetics · PLUniversity of Cincinnati Medical Center · USCase Western Reserve University · US

Funding

Mouse Models for Ion Homeostasis Defects in HeartR01HL061974 · NHLBI · UNIVERSITY OF CINCINNATI · PI SHULL, GARY EDWARD · 1999 to 2010
$5.1M
Role of Ion Channels in Cell DeathR01HL065323 · NHLBI · CASE WESTERN RESERVE UNIVERSITY · PI SCHILLING, WILLIAM P · 2002 to 2005
$1.2M
Regulation of PMCA Pump-Channels by Oxidant StressR01HL097355 · NHLBI · CASE WESTERN RESERVE UNIVERSITY · PI SCHILLING, WILLIAM P · 2009 to 2010
$788k
NHLBI NIH HHS HL61974NHLBI NIH HHS HL-65323NHLBI NIH HHS HL-97355NHLBI NIH HHS R01 HL097355
6 · The paper itself

Abstract

Maitotoxin (MTX) activates Ca(2+)-permeable nonselective cation channels and causes a dramatic increase in cytosolic free Ca(2+) concentration ([Ca(2+)](i)) in every cell examined to date, but the molecular identity of the channels involved remains unknown. A clue came from studies of a structurally related marine toxin called palytoxin (PTX). PTX binds to the plasmalemmal Na(+)-K(+)-ATPase (NKA) and converts the Na(+) pump into a nonselective cation channel. Given the high permeability of the MTX channel for Ca(2+), we considered the possibility that MTX may bind to the plasmalemmal Ca(2+)-ATPase (PMCA) pump, and like PTX, convert the pump into a channel. To test this hypothesis, the PMCA was overexpressed in Spodoptera frugiperda (Sf9) insect cells and in human embryonic kidneys (HEK) 293 cells. In both cell types, enhanced expression of the PMCA was associated with a significant increase in MTX-induced whole cell membrane currents. The effect of MTX on whole cell currents in both wild-type and PMCA overexpressing HEK cells was sensitive to pump ligands including Ca(2+) and ATP. MTX-induced currents were significantly reduced by knockdown of PMCA1 in HEK cells using small interfering RNA or in mouse embryonic fibroblasts from genetically modified mice with the PMCA1(+/-) PMCA4(-/-) genotype. Finally, PMCA catalytic activity (i.e., Ca(2+)-ATPase) in isolated membranes, or in purified PMCA preparations, was inhibited by MTX. Together, these results suggest that MTX binds to and converts the PMCA pump into a Ca(2+)-permeable nonselective cation channel.

Indexed as

Adenosine TriphosphateAnimalsAnimals, Genetically ModifiedCalciumCationsCation Transport ProteinsCell MembraneCells, CulturedDown-RegulationElectric ConductivityFibroblastsHumansIon ChannelsKidneyMarine ToxinsMiceAdenosine TriphosphateATP2B4 protein, humanCalciumCationsCation Transport ProteinsIon ChannelsmaitotoxinMarine ToxinsOxocinsPlasma Membrane Calcium-Transporting ATPasesPolyether ToxinsRNA, Small Interfering

Identifiers

PMID19794142
PMCPMC2793065
OpenAlexW2013235676

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.