Evidence map›Paper›PMID 40618317›Full record

ArticleBasic research in cardiology2025

Myocardial phosphoproteomics unveils a key role of DYRK1A in aortic valve replacement-induced reverse remodelling.

Fábio Trindade, João Almeida-Coelho, Cláudia Sousa-Mendes, Francisca Saraiva, Maria L Arbonés, Adelino Leite-Moreira, Rui Vitorino, Inês Falcão-Pires

Abstract read
In one paragraph

Article in Basic research in cardiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
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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

8 authors.

Fábio TrindadeRISE-Health, Department of Surgery and Physiology, Faculty of Medicine, University of Porto, 4200-319, Porto, Portugal.ORCID 0000-0002-3415-2040
João Almeida-CoelhoRISE-Health, Department of Surgery and Physiology, Faculty of Medicine, University of Porto, 4200-319, Porto, Portugal.ORCID 0000-0002-3769-8962
Cláudia Sousa-MendesRISE-Health, Department of Surgery and Physiology, Faculty of Medicine, University of Porto, 4200-319, Porto, Portugal.ORCID 0000-0002-4452-6149
Francisca SaraivaRISE-Health, Department of Surgery and Physiology, Faculty of Medicine, University of Porto, 4200-319, Porto, Portugal.ORCID 0000-0001-7961-9962
Maria L ArbonésIBMB-CSIC - Institut de Biologia Molecular de Barcelona, 08028, Barcelona, Spain.ORCID 0000-0002-6035-0235
Adelino Leite-MoreiraRISE-Health, Department of Surgery and Physiology, Faculty of Medicine, University of Porto, 4200-319, Porto, Portugal.ORCID 0000-0001-7808-3596
Rui Vitorino *RISE-Health, Department of Surgery and Physiology, Faculty of Medicine, University of Porto, 4200-319, Porto, Portugal.ORCID 0000-0003-3636-5805
Inês Falcão-Pires *RISE-Health, Department of Surgery and Physiology, Faculty of Medicine, University of Porto, 4200-319, Porto, Portugal. ipires@med.up.pt.ORCID 0000-0003-1937-3782

Funding

Fundação para a Ciência e a Tecnologia LA/P/0053/2020Fundação para a Ciência e a Tecnologia POCI-01-0145-FEDER-007628Fundação para a Ciência e a Tecnologia UIDB/00051/2020Fundação para a Ciência e a Tecnologia UIDB/04501/2020Fundação para a Ciência e a Tecnologia UIDP/00051/2020Fundação para a Ciência e a Tecnologia UIDP/00051/2020 (postdoc grant)
6 · The paper itself

Abstract

Aortic valve stenosis (AVS) is a growing healthcare burden. Aortic valve replacement (AVR) remains the only effective treatment to eliminate pressure overload and triggers myocardial reverse remodelling (RR), with regression of hypertrophy, fibrosis and diastolic function normalisation. However, many patients show an incomplete RR, being at higher risk of death. We aimed to uncover pathways and new therapeutic targets for incomplete RR through myocardial (phospho)proteomics. AVS patients were categorised based on left ventricle mass regression (LVM): complete RR (≥ 15%) or incomplete RR (≤ 5%). 83 myocardial proteins were dysregulated through LC-MS/MS. Gene ontology enrichment analysis identified inflammation, complement and immune system activation as priming events of an incomplete RR and a better mitochondrial function underscoring complete RR. Kinetic metabolic modelling corroborated the lower ATP production capacity of incomplete RR patients. To uncover therapeutic targets, kinases were predicted from phosphoproteome data. Casein kinase 2 and DYRK1A were among the most dysregulated kinases in RR. DYRK1A was found to be inversely correlated with LVM regression (r = - 0.62). DYRK1A functional role (passive, maximal tension and Ca

Indexed as

Aortic ValveAortic Valve StenosisHeart Valve Prosthesis ImplantationMyocardiumProtein Serine-Threonine KinasesProtein-Tyrosine KinasesProteomicsVentricular RemodelingAgedAnimalsDisease Models, AnimalDyrk KinasesFemaleHumansMaleMiceDyrk KinasesProtein Serine-Threonine KinasesProtein-Tyrosine KinasesAortic valve stenosisDYRK1AMyocardiumPhosphoproteomicsProteomicsReverse remodelling

Identifiers

PMID40618317
PMCPMC12518468

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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.