Evidence map›Paper›PMID 20070945›Full record

ArticleJournal of molecular biology2010

TRPM7 activates m-calpain by stress-dependent stimulation of p38 MAPK and c-Jun N-terminal kinase.

Li-Ting Su, Hsiang-Chin Chen, Omayra González-Pagán, Jeffrey D Overton, Jia Xie, Lixia Yue, Loren W Runnels

Abstract read
In one paragraph

Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
5.0field-weighted citation impact, top 5% 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

45 citing papers in PubMed, 78 citations in OpenAlex.

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  8. Review
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  11. The Presence and Distribution of TRPM7 in the Canine Mammary Glands.Animals : an open access journal from MDPI · 2020
    Article
  12. Article
  13. TRPM7, Magnesium, and Signaling.International journal of molecular sciences · 2019
    Review
  14. Article
  15. Article
  16. Article
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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 2 institutions in 1 country.

Li-Ting SuDepartment of Pharmacology, UMDNJ-Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ 08854, USA.
Hsiang-Chin Chen
Omayra González-Pagán
Jeffrey D Overton
Jia Xie
Lixia Yue
Loren W Runnels
Johnson University · USUConn Health · US

Funding

Ca2+ signaling mechanisms in cardiac fibrosisR01HL078960 · NHLBI · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI YUE, LIXIA · 2005 to 2015
$3.9M
Functional Analysis of the Bifunctional Ion Channel and Kinase TRPM7R01GM080753 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI RUNNELS, LOREN W · 2007 to 2016
$3.0M
NHLBI NIH HHS R01 HL078960NIGMS NIH HHS 1R01GM080753NIGMS NIH HHS R01 GM080753
6 · The paper itself

Abstract

TRPM7 is a Ca(2)(+)-permeant and Mg(2)(+)-permeant ion channel in possession of its own kinase domain. In a previous study, we showed that overexpression of the channel-kinase in HEK-293 cells produced cell rounding and loss of adhesion, which was dependent on the Ca(2+)-dependent protease m-calpain. The TRPM7-elicited change in cell morphology was channel-dependent and occurred without any significant increase in cytosolic Ca(2+). Here we demonstrate that overexpression of TRPM7 increased levels of cellular reactive oxygen species (ROS) and nitric oxide, causing the activation of p38 mitogen-activated protein kinase (MAPK) and c-Jun N-terminal kinase (JNK). Application of inhibitors of p38 MAPK and JNK blocked TRPM7-induced cell rounding and activation of m-calpain, without affecting the phosphorylation state of the protease. Overexpression of TRPM7 increased intracellular Mg(2+); however, when the concentration of either external Ca(2+) or Mg(2+) was increased to favor the permeation of one divalent cation over the other, a similar increase in cell rounding and calpain activity was detected, indicating that TRPM7-mediated activation of m-calpain is not dependent on the nature of the divalent conducted by the channel. Application of inhibitors of nitric oxide synthase and mitochondrial-derived ROS reduced TRPM7-induced increases in nitric oxide and ROS production, blocked the change in cell morphology, and reduced cellular calpain activity. Collectively, our data reveal that excessive TRPM7 channel activity causes oxidative and nitrosative stresses, producing cell rounding mediated by p38 MAPK/JNK-dependent activation of m-calpain.

Indexed as

AnimalsCalciumCalpainCell AdhesionCell LineCell ShapeFeedback, PhysiologicalGene ExpressionHumansJNK Mitogen-Activated Protein KinasesMAP Kinase Signaling SystemMiceNitric OxideOxidative Stressp38 Mitogen-Activated Protein KinasesProtein Serine-Threonine KinasesCalciumCalpainJNK Mitogen-Activated Protein Kinasesm-calpainNitric Oxidep38 Mitogen-Activated Protein KinasesProtein Serine-Threonine KinasesReactive Oxygen SpeciesRecombinant ProteinsTRPM7 protein, humanTrpm7 protein, mouseTRPM Cation Channels

Identifiers

PMID20070945
PMCPMC2825087
OpenAlexW2052152153

What OpenQuestion holds

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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.