Evidence map›Paper›PMID 32647007›Full record

ArticleThe Journal of biological chemistry2020

Cathepsin A contributes to left ventricular remodeling by degrading extracellular superoxide dismutase in mice.

Mathias Hohl, Manuel Mayr, Lisa Lang, Alexander G Nickel, Javier Barallobre-Barreiro, Xiaoke Yin, Thimoteus Speer, Simina-Ramona Selejan, Claudia Goettsch, Katharina Erb and 9 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.5field-weighted citation impact, top 15% 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

10 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. In Silico Structural Analysis of Serine CarboxypeptidaseInternational journal of molecular sciences · 2022
    Article
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

19 authors at 7 institutions in 4 countries.

Mathias HohlKlinik für Innere Medizin III, Universität des Saarlandes, Homburg/Saar, Germany.ORCID 0000-0001-6946-9825
Manuel MayrKing's BHF Centre of Research Excellence, The James Black Centre, London, United Kingdom.ORCID 0000-0002-0597-829X
Lisa LangKlinik für Innere Medizin III, Universität des Saarlandes, Homburg/Saar, Germany.
Alexander G NickelKlinik für Innere Medizin III, Universität des Saarlandes, Homburg/Saar, Germany.
Javier Barallobre-BarreiroKing's BHF Centre of Research Excellence, The James Black Centre, London, United Kingdom.
Xiaoke YinKing's BHF Centre of Research Excellence, The James Black Centre, London, United Kingdom.ORCID 0000-0002-5172-0935
Thimoteus SpeerKlinik für Innere Medizin IV, Universität des Saarlandes, Homburg/Saar, Germany.
Simina-Ramona SelejanKlinik für Innere Medizin III, Universität des Saarlandes, Homburg/Saar, Germany.
Claudia GoettschMedizinische Fakultät, Medizinische Klinik 1, Kardiologie, Universitätsklinikum, Aachen, Germany.ORCID 0000-0002-7973-1329
Katharina ErbKlinik für Innere Medizin III, Universität des Saarlandes, Homburg/Saar, Germany.
Claudia Fecher-TrostInstitut für Experimentelle und Klinische Pharmakologie und Toxikologie Universität des Saarlandes, Homburg/Saar, Germany.ORCID 0000-0002-8799-4188
Jan-Christian ReilKlinik für Innere Medizin III, Universität des Saarlandes, Homburg/Saar, Germany.
Benedikt LinzFaculty of Health and Medical Sciences, Department of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark.ORCID 0000-0002-7611-4130
Sven RufSanofi-Aventis Deutschland GmbH, Frankfurt, Germany.
Thomas HübschleSanofi-Aventis Deutschland GmbH, Frankfurt, Germany.
Christoph MaackKlinik für Innere Medizin III, Universität des Saarlandes, Homburg/Saar, Germany.ORCID 0000-0003-3694-4559
Michael BöhmKlinik für Innere Medizin III, Universität des Saarlandes, Homburg/Saar, Germany.ORCID 0000-0002-2976-2514
Thorsten SadowskiSanofi-Aventis Deutschland GmbH, Frankfurt, Germany.
Dominik LinzKlinik für Innere Medizin III, Universität des Saarlandes, Homburg/Saar, Germany dominik.linz@mumc.nl.ORCID 0000-0003-4893-0824
Saarland University · DESanofi (Germany) · DEUniversitätsklinikum Würzburg · DERoyal Adelaide Hospital · AUUniversitäres Kinderwunschzentrum Lübeck · DEUniversitätsklinikum Aachen · DEUniversity of Copenhagen · DK

Funding

British Heart Foundation RG/16/14/32397Medical Research Council MC_UP_1502/3
6 · The paper itself

Abstract

In the heart, the serine carboxypeptidase cathepsin A (CatA) is distributed between lysosomes and the extracellular matrix (ECM). CatA-mediated degradation of extracellular peptides may contribute to ECM remodeling and left ventricular (LV) dysfunction. Here, we aimed to evaluate the effects of CatA overexpression on LV remodeling. A proteomic analysis of the secretome of adult mouse cardiac fibroblasts upon digestion by CatA identified the extracellular antioxidant enzyme superoxide dismutase (EC-SOD) as a novel substrate of CatA, which decreased EC-SOD abundance 5-fold.

Indexed as

ProteolysisVentricular RemodelingAnimalsCathepsin AMaleMiceMice, TransgenicMyocytes, CardiacSuperoxide DismutaseCathepsin ASod3 protein, mouseSuperoxide Dismutasecarboxypeptidasecardiac hypertrophycardiac remodelingcathepsin AEC-SODextracellular matrix proteinextracellular superoxide dismutasefibrosisheart diseaseheart failureleft ventricular dysfunctionoxidative stressoxygen radicalssecretomesuperoxide dismutase (SOD)

Identifiers

PMID32647007
PMCPMC7476717
OpenAlexW3041526784

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.