Evidence map›Paper›PMID 21670146›Full record

ArticleMolecular and cellular biology2011

PINCH proteins regulate cardiac contractility by modulating integrin-linked kinase-protein kinase B signaling.

Benjamin Meder, Inken G Huttner, Farbod Sedaghat-Hamedani, Steffen Just, Tillman Dahme, Karen S Frese, Britta Vogel, Doreen Köhler, Wanda Kloos, Jessica Rudloff and 3 more

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 44 citations in OpenAlex.

  1. Trial
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  11. Rsu1-dependent control of PTEN expression is regulated via ATF2 and cJun.Journal of cell communication and signaling · 2019
    Article
  12. Mutations in ILK, encoding integrin-linked kinase, are associated with arrhythmogenic cardiomyopathy.Translational research : the journal of laboratory and clinical medicine · 2019
    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

13 authors at 3 institutions in 2 countries.

Benjamin MederDepartment of Medicine III, University of Heidelberg, Heidelberg, Germany.
Inken G Huttner
Farbod Sedaghat-Hamedani
Steffen Just
Tillman Dahme
Karen S Frese
Britta Vogel
Doreen Köhler
Wanda Kloos
Jessica Rudloff
Sabine Marquart
Hugo A Katus
Wolfgang Rottbauer
Heidelberg University · DEUniversität Ulm · DEVictor Chang Cardiac Research Institute · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Integrin-linked kinase (ILK) is an essential component of the cardiac mechanical stretch sensor and is bound in a protein complex with parvin and PINCH proteins, the so-called ILK-PINCH-parvin (IPP) complex. We have recently shown that inactivation of ILK or β-parvin activity leads to heart failure in zebrafish via reduced protein kinase B (PKB/Akt) activation. Here, we show that PINCH proteins localize at sarcomeric Z disks and costameres in the zebrafish heart and skeletal muscle. To investigate the in vivo role of PINCH proteins for IPP complex stability and PKB signaling within the vertebrate heart, we inactivated PINCH1 and PINCH2 in zebrafish. Inactivation of either PINCH isoform independently leads to instability of ILK, loss of stretch-responsive anf and vegf expression, and progressive heart failure. The predominant cause of heart failure in PINCH morphants seems to be loss of PKB activity, since PKB phosphorylation at serine 473 is significantly reduced in PINCH-deficient hearts and overexpression of constitutively active PKB reconstitutes cardiac function in PINCH morphants. These findings highlight the essential function of PINCH proteins in controlling cardiac contractility by granting IPP/PKB-mediated signaling.

Indexed as

Myocardial ContractionAnimalsHeart FailureMuscle ProteinsMuscle, SkeletalMyocardiumPhosphorylationProtein Serine-Threonine KinasesProto-Oncogene Proteins c-aktSarcomeresScaffold Protein ILKSignal TransductionZebrafishZebrafish Proteinslims1 protein, zebrafishlims2 protein, zebrafishMuscle ProteinsProtein Serine-Threonine KinasesProto-Oncogene Proteins c-aktScaffold Protein ILKZebrafish Proteins

Identifiers

PMID21670146
PMCPMC3147799
OpenAlexW1990452466

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.