Evidence map›Paper›PMID 12668438›Full record

ArticleBiophysical journal2003

Polyvalent cations as permeant probes of MIC and TRPM7 pores.

Hubert H Kerschbaum, J Ashot Kozak, Michael D Cahalan

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
10.0field-weighted citation impact, top 1% 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

63 citing papers in PubMed, 118 citations in OpenAlex.

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  12. Functional expression of TRPM7 as a CaPhysiological reports · 2019
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3 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

3 authors at 2 institutions in 2 countries.

Hubert H KerschbaumDepartment of Physiology and Biophysics, University of California, Irvine, California 92697-4561 USA.
J Ashot Kozak
Michael D Cahalan
University of California, Irvine · USUniversity of Salzburg · AT

Funding

Molecular Mechanisms of lon Channels in T LymphocytesR01NS014609 · NINDS · UNIVERSITY OF CALIFORNIA-IRVINE · PI CAHALAN, MICHAEL D · 1985 to 2022
$7.0M
Molecular Mechanisms of Ion Channels in T LymphocytesR37NS014609 · NINDS · UNIVERSITY OF CALIFORNIA-IRVINE · PI CAHALAN, MICHAEL D · 2006 to 2012
$3.3M
Molecular Mechanisms of lon Channels in T LymphocytesR56NS014609 · NINDS · UNIVERSITY OF CALIFORNIA-IRVINE · PI CAHALAN, MICHAEL D · 2018 to 2018
$514k
NINDS NIH HHS NS14609NINDS NIH HHS R01 NS014609NINDS NIH HHS R37 NS014609NINDS NIH HHS R56 NS014609
6 · The paper itself

Abstract

Recent studies in Jurkat T cells and in rat basophilic leukemia cells revealed an Mg(2+)-inhibited cation (MIC) channel that has electrophysiological properties similar to TRPM7 Eyring rate model expressed exogenously in mammalian cells. Here we compare the characteristics of several polyvalent cations and Mg(2+) to block monovalent MIC current from the outside. Putrescine, spermidine, spermine, PhTX-343 (a derivative of the naturally occurring polyamine toxin philanthotoxin), and Mg(2+) each blocked in a dose- and voltage-dependent manner, indicating a blocking site within the electric field of the ion channel. Spermine and the relatively bulky PhTX-343 exhibited voltage dependence steeper than that expected for the number of charges on the molecule. Polyamines and Mg(2+) are permeant blockers, as judged by relief of block at strongly negative membrane potentials. Intracellular dialysis with spermine (300 microM) had no effect, indicating an asymmetrical pore. At the single-channel level, spermine and Mg(2+) induced flickery block of 40-pS single channels. I/V characteristics and polyamine block are similar in expressed TRPM7 and in native MIC currents, consistent with the conclusion that native MIC channels are composed of TRPM7 subunits. An Eyring rate model is developed to account for I/V characteristics and block of MIC channels by polyvalent cations from the outside.

Indexed as

Ion ChannelsMembrane ProteinsAnimalsCalcium ChannelsCationsCation Transport ProteinsCell LineCell Line, TumorCell Membrane PermeabilityCHO CellsCricetinaeDose-Response Relationship, DrugElectric ConductivityHumansIon Channel GatingJurkat CellsCalcium ChannelsCationsCation Transport ProteinsIon ChannelsMagnesiumMembrane ProteinsPhenolsphilanthotoxin 343PolyaminesPutrescineSpermidineSpermineTRPM2 protein, humanTRPM Cation Channels

Identifiers

PMID12668438
PMCPMC1302796
OpenAlexW1971372933

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.