Evidence map›Paper›PMID 33670142›Full record

ArticleInternational journal of molecular sciences2021

Mass Spectrometry-Based Redox and Protein Profiling of Failing Human Hearts.

Tamara Tomin, Matthias Schittmayer, Simon Sedej, Heiko Bugger, Johannes Gollmer, Sophie Honeder, Barbara Darnhofer, Laura Liesinger, Andreas Zuckermann, Peter P Rainer and 1 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. 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
1.2field-weighted citation impact, top 23% 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, 18 citations in OpenAlex.

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  11. Novel Targets for Old and Diseased Hearts.International journal of molecular sciences · 2022
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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

11 authors at 3 institutions in 2 countries.

Tamara TominFaculty of Technical Chemistry, Institute of Chemical Technologies and Analytics, Vienna University of Technology-TU Wien, Getreidemarkt 9/164, 1060 Vienna, Austria.ORCID 0000-0002-7071-2316
Matthias SchittmayerFaculty of Technical Chemistry, Institute of Chemical Technologies and Analytics, Vienna University of Technology-TU Wien, Getreidemarkt 9/164, 1060 Vienna, Austria.ORCID 0000-0003-3249-655X
Simon SedejBiotechMed-Graz, Mozartgasse 12/II, 8010 Graz, Austria.
Heiko BuggerDivision of Cardiology, Medical University of Graz, Auenbruggerplatz 15, 8036 Graz, Austria.
Johannes GollmerDivision of Cardiology, Medical University of Graz, Auenbruggerplatz 15, 8036 Graz, Austria.
Sophie HonederDiagnostic and Research Institute of Pathology, Medical University of Graz, Stiftingtalstrasse 6, 8010 Graz, Austria.ORCID 0000-0002-7201-6293
Barbara DarnhoferDiagnostic and Research Institute of Pathology, Medical University of Graz, Stiftingtalstrasse 6, 8010 Graz, Austria.
Laura LiesingerDiagnostic and Research Institute of Pathology, Medical University of Graz, Stiftingtalstrasse 6, 8010 Graz, Austria.
Andreas ZuckermannCardiac Transplantation, Department of Cardiac Surgery, Medical University of Vienna, Spitalgasse 23, 1090 Vienna, Austria.
Peter P RainerBiotechMed-Graz, Mozartgasse 12/II, 8010 Graz, Austria.ORCID 0000-0002-2840-6454
Ruth Birner-GruenbergerFaculty of Technical Chemistry, Institute of Chemical Technologies and Analytics, Vienna University of Technology-TU Wien, Getreidemarkt 9/164, 1060 Vienna, Austria.ORCID 0000-0003-3950-0312
Medical University of Graz · ATTU Wien · ATMedical University of Vienna · AT

Funding

Austrian Herzfonds 201901Austrian Ministry of Science, Research and Economy Omics Center GrazAustrian Science Fund F73Austrian Science Fund KLI425Austrian Science Fund KLI645Austrian Science Fund W1266Austrian Science Fund FWF KLI 425Austrian Science Fund FWF KLI 645Austrian Science Fund FWF W 1226
6 · The paper itself

Abstract

Oxidative stress contributes to detrimental functional decline of the myocardium, leading to the impairment of the antioxidative defense, dysregulation of redox signaling, and protein damage. In order to precisely dissect the changes of the myocardial redox state correlated with oxidative stress and heart failure, we subjected left-ventricular tissue specimens collected from control or failing human hearts to comprehensive mass spectrometry-based redox and quantitative proteomics, as well as glutathione status analyses. As a result, we report that failing hearts have lower glutathione to glutathione disulfide ratios and increased oxidation of a number of different proteins, including constituents of the contractile machinery as well as glycolytic enzymes. Furthermore, quantitative proteomics of failing hearts revealed a higher abundance of proteins responsible for extracellular matrix remodeling and reduced abundance of several ion transporters, corroborating contractile impairment. Similar effects were recapitulated by an in vitro cell culture model under a controlled oxygen atmosphere. Together, this study provides to our knowledge the most comprehensive report integrating analyses of protein abundance and global and peptide-level redox state in end-stage failing human hearts as well as oxygen-dependent redox and global proteome profiles of cultured human cardiomyocytes.

Indexed as

Gene Expression ProfilingMass SpectrometryAgedFemaleHeart FailureHeart VentriclesHumansMaleMiddle AgedMuscle ProteinsMyocardiumMuscle Proteinscardiomyopathyfailing heartsoxidative stressredox proteomics

Identifiers

PMID33670142
PMCPMC7916846
OpenAlexW3128493287

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.