Evidence map›Paper›PMID 22606238›Full record

ArticlePloS one2012

Redox proteomics identification of oxidatively modified myocardial proteins in human heart failure: implications for protein function.

Maura Brioschi, Gianluca Polvani, Pasquale Fratto, Alessandro Parolari, Piergiuseppe Agostoni, Elena Tremoli, Cristina Banfi

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.3field-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

16 citing papers in PubMed, 28 citations in OpenAlex.

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  15. Doxorubicin-induced carbonylation and degradation of cardiac myosin binding protein C promote cardiotoxicity.Proceedings of the National Academy of Sciences of the United States of America · 2014
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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 3 institutions in 2 countries.

Maura BrioschiCentro Cardiologico Monzino IRCCS, Milan, Italy.
Gianluca Polvani
Pasquale Fratto
Alessandro Parolari
Piergiuseppe Agostoni
Elena Tremoli
Cristina Banfi
Centro Cardiologico Monzino · ITUniversity of Milan · ITAzienda Socio Sanitaria Territoriale Grande Ospedale Metropolitano Niguarda · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Increased oxidative stress in a failing heart may contribute to the pathogenesis of heart failure (HF). The aim of this study was to identify the oxidised proteins in the myocardium of HF patients and analyse the consequences of oxidation on protein function. The carbonylated proteins in left ventricular tissue from failing (n = 14) and non-failing human hearts (n = 13) were measured by immunoassay and identified by proteomics. HL-1 cardiomyocytes were incubated in the presence of stimuli relevant for HF in order to assess the generation of reactive oxygen species (ROS), the induction of protein carbonylation, and its consequences on protein function. The levels of carbonylated proteins were significantly higher in the HF patients than in the controls (p<0.01). We identified two proteins that mainly underwent carbonylation: M-type creatine kinase (M-CK), whose activity is impaired, and, to a lesser extent, α-cardiac actin. Exposure of cardiomyocytes to angiotensin II and norepinephrine led to ROS generation and M-CK carbonylation with loss of its enzymatic activity. Our findings indicate that protein carbonylation is increased in the myocardium during HF and that these oxidative changes may help to explain the decreased CK activity and consequent defects in energy metabolism observed in HF.

Indexed as

AdultCase-Control StudiesCreatine Kinase, MM FormEnergy MetabolismFemaleHeart FailureHumansMaleMiddle AgedMuscle ProteinsMyocardiumMyocytes, CardiacOxidation-ReductionOxidative StressProtein CarbonylationProteomicsCreatine Kinase, MM FormMuscle ProteinsReactive Oxygen Species

Identifiers

PMID22606238
PMCPMC3351458
OpenAlexW2057842040

What OpenQuestion holds

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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.