Evidence map›Paper›PMID 20037178›Full record

ArticleMolecular & cellular proteomics : MCP2010

Proteomics analysis of the cardiac myofilament subproteome reveals dynamic alterations in phosphatase subunit distribution.

Xiaoke Yin, Friederike Cuello, Ursula Mayr, Zhiqi Hao, Martin Hornshaw, Elisabeth Ehler, Metin Avkiran, Manuel Mayr

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

45 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
  2. Article
  3. Proteomics of the heart.Physiological reviews · 2024
    Review
  4. Article
  5. Loss of protein phosphatase 2A regulatory subunitFrontiers in cardiovascular medicine · 2024
    Article
  6. Best practices in assessing cardiac proteinAmerican journal of physiology. Heart and circulatory physiology · 2023
    Article
  7. Article
  8. Article
  9. Regulation of Cardiac PKA Signaling by cAMP and Oxidants.Antioxidants (Basel, Switzerland) · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Using cAMP Sensors to Study Cardiac Nanodomains.Journal of cardiovascular development and disease · 2018
    Review
  16. Article
  17. Article
  18. Article
  19. Roles and regulation of protein phosphatase 2A (PP2A) in the heart.Journal of molecular and cellular cardiology · 2016
    Review
  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

8 authors at 3 institutions in 2 countries.

Xiaoke YinKing's British Heart Foundation Centre, King's College London, London SE5 9NU, United Kingdom.
Friederike Cuello
Ursula Mayr
Zhiqi Hao
Martin Hornshaw
Elisabeth Ehler
Metin Avkiran
Manuel Mayr
British Heart Foundation · GBThermo Fisher Scientific (United Kingdom) · GBThermo Fisher Scientific (United States) · US

Funding

British Heart Foundation FS/08/002/24537Medical Research Council G0400153
6 · The paper itself

Abstract

Myofilament proteins are responsible for cardiac contraction. The myofilament subproteome, however, has not been comprehensively analyzed thus far. In the present study, cardiomyocytes were isolated from rodent hearts and stimulated with endothelin-1 and isoproterenol, potent inducers of myofilament protein phosphorylation. Subsequently, cardiomyocytes were "skinned," and the myofilament subproteome was analyzed using a high mass accuracy ion trap tandem mass spectrometer (LTQ Orbitrap XL) equipped with electron transfer dissociation. As expected, a small number of myofilament proteins constituted the majority of the total protein mass with several known phosphorylation sites confirmed by electron transfer dissociation. More than 600 additional proteins were identified in the cardiac myofilament subproteome, including kinases and phosphatase subunits. The proteomic comparison of myofilaments from control and treated cardiomyocytes suggested that isoproterenol treatment altered the subcellular localization of protein phosphatase 2A regulatory subunit B56alpha. Immunoblot analysis of myocyte fractions confirmed that beta-adrenergic stimulation by isoproterenol decreased the B56alpha content of the myofilament fraction in the absence of significant changes for the myosin phosphatase target subunit isoforms 1 and 2 (MYPT1 and MYPT2). Furthermore, immunolabeling and confocal microscopy revealed the spatial redistribution of these proteins with a loss of B56alpha from Z-disc and M-band regions but increased association of MYPT1/2 with A-band regions of the sarcomere following beta-adrenergic stimulation. In summary, we present the first comprehensive proteomics data set of skinned cardiomyocytes and demonstrate the potential of proteomics to unravel dynamic changes in protein composition that may contribute to the neurohormonal regulation of myofilament contraction.

Indexed as

Actin CytoskeletonAdrenergic beta-AgonistsAnimalsCells, CulturedEndothelin-1IsoproterenolMaleMiceMyocardial ContractionMyocytes, CardiacNeurotransmitter AgentsPhosphorylationPhosphotransferasesProtein Phosphatase 1Protein Phosphatase 2ProteomeAdrenergic beta-AgonistsB56alpha protein, ratEndothelin-1IsoproterenolNeurotransmitter AgentsPhosphotransferasesPpp1r12a protein, ratProtein Phosphatase 1Protein Phosphatase 2Proteome

Identifiers

PMID20037178
PMCPMC2849712
OpenAlexW1976507381

What OpenQuestion holds

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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.