Evidence map›Paper›PMID 20368797›Full record

ReviewJournal of biomedicine & biotechnology2010

S100A1: a regulator of striated muscle sarcoplasmic reticulum Ca2+ handling, sarcomeric, and mitochondrial function.

Mirko Völkers, David Rohde, Chelain Goodman, Patrick Most

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of biomedicine & biotechnology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed, 2 pooled it
2.0field-weighted citation impact, top 14% 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

37 citing papers in PubMed, 2 syntheses or guidelines pooled it, 57 citations in OpenAlex.

  1. Calprotectin (S100A8/S100A9): a key protein between inflammation and cancer.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2018
    Pooled it
  2. Pooled it
  3. Review
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  8. Structural insights into the regulation of RyR1 by S100A1.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. S100 proteins in cardiovascular diseases.Molecular medicine (Cambridge, Mass.) · 2023
    Review
  10. Article
  11. Article
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  14. Article
  15. Article
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  17. S100 proteins in obesity: liaisons dangereuses.Cellular and molecular life sciences : CMLS · 2020
    Review
  18. Article
  19. Unbalance Between Sarcoplasmic Reticulum CaFrontiers in physiology · 2019
    Review
  20. Cellular and molecular mechanisms of sarcopenia: the S100B perspective.Journal of cachexia, sarcopenia and muscle · 2018
    Review
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

4 authors at 2 institutions in 2 countries.

Mirko VölkersDivision of Cardiology, Department of Internal Medicine III, Laboratory for Molecular and Translational Cardiology, University of Heidelberg, INF 350, 69120 Heidelberg, Germany. mirko.voelkers@med.uni-heidelberg.de
David Rohde
Chelain Goodman
Patrick Most
Heidelberg University · DEThomas 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
NHLBI NIH HHS HL 092130-02S1NHLBI NIH HHS R01 HL092130NHLBI NIH HHS R01 HL092130-01
6 · The paper itself

Abstract

Calcium (Ca(2+)) signaling plays a key role in a wide range of physiological functions including control of cardiac and skeletal muscle performance. To assure a precise coordination of both temporally and spatially transduction of intracellular Ca(2+) oscillations to downstream signaling networks and target operations, Ca(2+) cycling regulation in muscle tissue is conducted by a plethora of diverse molecules. Ca(2+) S100A1 is a member of the Ca(2+)-binding S100 protein family and represents the most abundant S100 isoform in cardiac and skeletal muscle. Early studies revealed distinct expression patterns of S100A1 in healthy and diseased cardiac tissue from animal models and humans. Further elaborate investigations uncovered S100A1 protein as a basic requirement for striated muscle Ca(2+) handling integrity. S100A1 is a critical regulator of cardiomyocyte Ca(2+) cycling and contractile performance. S100A1-mediated inotropy unfolds independent and on top of beta AR-stimulated contractility with unchanged beta AR downstream signaling. S100A1 has further been detected at different sites within the cardiac sarcomere indicating potential roles in myofilament function. More recently, a study reported a mitochondrial location of S100A1 in cardiomyocytes. Additionally, normalizing the level of S100A1 protein by means of viral cardiac gene transfer in animal heart failure models resulted in a disrupted progression towards cardiac failure and enhanced survival. This brief review is confined to the physiological and pathophysiological relevance of S100A1 in cardiac and skeletal muscle Ca(2+) handling with a particular focus on its potential as a molecular target for future therapeutic interventions.

Indexed as

AnimalsCalciumHumansMitochondriaModels, BiologicalS100 ProteinsSarcomeresSarcoplasmic ReticulumCalciumS100A1 proteinS100 Proteins

Identifiers

PMID20368797
PMCPMC2846685
OpenAlexW2089643774

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.