Evidence map›Paper›PMID 27022107›Full record

ArticleMolecular & cellular proteomics : MCP2016

Delineation of Molecular Pathways Involved in Cardiomyopathies Caused by Troponin T Mutations.

Jennifer E Gilda, Xianyin Lai, Frank A Witzmann, Aldrin V Gomes

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.1field-weighted citation impact, top 20% 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

8 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Untying the knot: protein quality control in inherited cardiomyopathies.Pflugers Archiv : European journal of physiology · 2019
    Review
  7. Article
  8. Proteasome dysfunction in cardiomyopathies.The Journal of physiology · 2017
    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

4 authors at 3 institutions in 1 country.

Jennifer E GildaFrom the ‡Department of Neurobiology, Physiology, and Behavior.
Xianyin Lai¶Department of Cellular and Integrative Physiology, Indiana University School of Medicine, Indianapolis, Indiana 46202.
Frank A Witzmann¶Department of Cellular and Integrative Physiology, Indiana University School of Medicine, Indianapolis, Indiana 46202.
Aldrin V GomesFrom the ‡Department of Neurobiology, Physiology, and Behavior, §Department of Physiology and Membrane Biology, University of California, Davis, California 95616; avgomes@ucdavis.edu.
University of California, Davis · USIndiana University – Purdue University Indianapolis · USIndiana University School of Medicine

Funding

The Role of the Proteasome in Troponin related CardiomyopathiesR01HL096819 · NHLBI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI GOMES, ALDRIN V. · 2010 to 2014
$1.9M
NHLBI NIH HHS R01 HL096819
6 · The paper itself

Abstract

Familial hypertrophic cardiomyopathy (FHC) is associated with mild to severe cardiac problems and is the leading cause of sudden death in young people and athletes. Although the genetic basis for FHC is well-established, the molecular mechanisms that ultimately lead to cardiac dysfunction are not well understood. To obtain important insights into the molecular mechanism(s) involved in FHC, hearts from two FHC troponin T models (Ile79Asn [I79N] and Arg278Cys [R278C]) were investigated using label-free proteomics and metabolomics. Mutations in troponin T are the third most common cause of FHC, and the I79N mutation is associated with a high risk of sudden cardiac death. Most FHC-causing mutations, including I79N, increase the Ca(2+) sensitivity of the myofilament; however, the R278C mutation does not alter Ca(2+) sensitivity and is associated with a better prognosis than most FHC mutations. Out of more than 1200 identified proteins, 53 and 76 proteins were differentially expressed in I79N and R278C hearts, respectively, when compared with wild-type hearts. Interestingly, more than 400 proteins were differentially expressed when the I79N and R278C hearts were directly compared. The three major pathways affected in I79N hearts relative to R278C and wild-type hearts were the ubiquitin-proteasome system, antioxidant systems, and energy production pathways. Further investigation of the proteasome system using Western blotting and activity assays showed that proteasome dysfunction occurs in I79N hearts. Metabolomic results corroborate the proteomic data and suggest the glycolytic, citric acid, and electron transport chain pathways are important pathways that are altered in I79N hearts relative to R278C or wild-type hearts. Our findings suggest that impaired energy production and protein degradation dysfunction are important mechanisms in FHCs associated with poor prognosis and that cardiac hypertrophy is not likely needed for a switch from fatty acid to glucose metabolism.

Indexed as

AnimalsCardiomyopathy, Hypertrophic, FamilialDisease Models, AnimalGene Expression RegulationHumansMetabolomicsMiceMutationProteomicsSignal TransductionTroponin TTroponin T

Identifiers

PMID27022107
PMCPMC5083082
OpenAlexW2327151570

What OpenQuestion holds

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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.