Evidence map›Paper›PMID 20645037›Full record

ReviewJournal of cardiovascular translational research2010

S100A1: a multifaceted therapeutic target in cardiovascular disease.

David Rohde, Julia Ritterhoff, Mirko Voelkers, Hugo A Katus, Thomas G Parker, Patrick Most

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of cardiovascular translational research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

30 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. S100 Proteins in Fatty Liver Disease and Hepatocellular Carcinoma.International journal of molecular sciences · 2022
    Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Observational
  11. Article
  12. Article
  13. Article
  14. S100A1 DNA-based Inotropic Therapy Protects Against Proarrhythmogenic Ryanodine Receptor 2 Dysfunction.Molecular therapy : the journal of the American Society of Gene Therapy · 2015
    Article
  15. Article
  16. Review
  17. S100 proteins in cancer.Nature reviews. Cancer · 2015
    Review
  18. Article
  19. Article
  20. 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

6 authors at 4 institutions in 3 countries.

David RohdeLaboratory for Molecular and Translational Cardiology, Division of Cardiology, Department of Internal Medicine III, University of Heidelberg, INF 350, 69120 Heidelberg, Germany.
Julia Ritterhoff
Mirko Voelkers
Hugo A Katus
Thomas G Parker
Patrick Most
Heidelberg University · DESan Diego State University · USSt. Michael's Hospital · CAThomas Jefferson University · US

Funding

S100A1: A Novel Modulator of Myocardial Infarct Inflammation and RegenerationR01HL092130 · NHLBI · THOMAS JEFFERSON UNIVERSITY · PI PEPPEL, KARSTEN · 2008 to 2012
$2.2M
CIHRNHLBI NIH HHS HL092130-02S1NHLBI NIH HHS R01 HL092130NHLBI NIH HHS R01 HL092130-01
6 · The paper itself

Abstract

Cardiovascular disease is the leading cause of death worldwide, showing a dramatically growing prevalence. It is still associated with a poor clinical prognosis, indicating insufficient long-term treatment success of currently available therapeutic strategies. Investigations of the pathomechanisms underlying cardiovascular disorders uncovered the Ca(2+) binding protein S100A1 as a critical regulator of both cardiac performance and vascular biology. In cardiomyocytes, S100A1 was found to interact with both the sarcoplasmic reticulum ATPase (SERCA2a) and the ryanodine receptor 2 (RyR2), resulting in substantially improved Ca(2+) handling and contractile performance. Additionally, S100A1 has been described to target the cardiac sarcomere and mitochondria, leading to reduced pre-contractile passive tension as well as enhanced oxidative energy generation. In endothelial cells, molecular analyses revealed a stimulatory effect of S100A1 on endothelial NO production by increasing endothelial nitric oxide synthase activity. Emphasizing the pathophysiological relevance of S100A1, myocardial infarction in S100A1 knockout mice resulted in accelerated transition towards heart failure and excessive mortality in comparison with wild-type controls. Mice lacking S100A1 furthermore displayed significantly elevated blood pressure values with abrogated responsiveness to bradykinin. On the other hand, numerous studies in small and large animal heart failure models showed that S100A1 overexpression results in reversed maladaptive myocardial remodeling, long-term rescue of contractile performance, and superior survival in response to myocardial infarction, indicating the potential of S100A1-based therapeutic interventions. In summary, elaborate basic and translational research established S100A1 as a multifaceted therapeutic target in cardiovascular disease, providing a promising novel therapeutic strategy to future cardiologists.

Indexed as

Genetic TherapyAnimalsCardiovascular AgentsCardiovascular DiseasesEndothelial CellsHumansModels, MolecularMolecular Targeted TherapyMyocytes, CardiacProtein ConformationS100 ProteinsSignal TransductionTranslational Research, BiomedicalCardiovascular AgentsS100A1 proteinS100 Proteins

Identifiers

PMID20645037
PMCPMC2933808
OpenAlexW2004519256

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.