Evidence map›Paper›PMID 23844019›Full record

ArticlePloS one2013

The cardiac acetyl-lysine proteome.

D Brian Foster, Ting Liu, Jasma Rucker, Robert N O'Meally, Lauren R Devine, Robert N Cole, Brian O'Rourke

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

58 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Proteomics of the heart.Physiological reviews · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. The cardioprotective role of sirtuins is mediated in part by regulating KAmerican journal of physiology. Cell physiology · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. 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

7 authors at 2 institutions in 1 country.

D Brian FosterDivision of Cardiology, Department of Medicine, The Johns Hopkins University School of Medicine, Baltimore, Maryland, USA. dbrianfoster@jhmi.edu
Ting Liu
Jasma Rucker
Robert N O'Meally
Lauren R Devine
Robert N Cole
Brian O'Rourke
Johns Hopkins University · USJohns Hopkins Medicine · US

Funding

Redox Modification of the Arrhythmic Substrate in Heart FailureR01HL105216 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI O'ROURKE, BRIAN, TRAYANOVA, NATALIA A. · 2011 to 2014
$3.0M
MItochondrial Dysfunction in Cardiac Hypertrophy and FailureR01HL101235 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI BERS, DONALD M, BLATTER, LOTHAR A · 2010 to 2013
$2.8M
A Systems Biology Approach To Cardiomyopathy in the D. Melanogaster Model SystemR21HL108052 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI FOSTER, D BRIAN, O'ROURKE, BRIAN · 2012 to 2013
$457k
NHLBI NIH HHS HHSN268201000032CNHLBI NIH HHS R01 HL101235NHLBI NIH HHS R01HL101235NHLBI NIH HHS R01 HL105216NHLBI NIH HHS R21 HL108052NHLBI NIH HHS R21HL108052
6 · The paper itself

Abstract

In the heart, lysine acetylation has been implicated in processes ranging from transcriptional control of pathological remodeling, to cardioprotection arising from caloric restriction. Given the emerging importance of this post-translational modification, we used a proteomic approach to investigate the broader role of lysine acetylation in the heart using a guinea pig model. Briefly, hearts were fractionated into myofilament-, mitochondrial- and cytosol-enriched fractions prior to proteolysis and affinity-enrichment of acetylated peptides. LC-MS/MS analysis identified 1075 acetylated peptides, harboring 994 acetylation sites that map to 240 proteins with a global protein false discovery rate <0.8%. Mitochondrial targets account for 59% of identified proteins and 64% of sites. The majority of the acetyl-proteins are enzymes involved in fatty acid metabolism, oxidative phosphorylation or the TCA cycle. Within the cytosolic fraction, the enzymes of glycolysis, fatty acid synthesis and lipid binding are prominent. Nuclear targets included histones and the transcriptional regulators E1A(p300) and CREB binding protein. Comparison of our dataset with three previous global acetylomic studies uniquely revealed 53 lysine-acetylated proteins. Specifically, newly-identified acetyl-proteins include Ca(2+)-handling proteins, RyR2 and SERCA2, and the myofilament proteins, myosin heavy chain, myosin light chains and subunits of the Troponin complex, among others. These observations were confirmed by anti-acetyl-lysine immunoblotting. In summary, cardiac lysine acetylation may play a role in cardiac substrate selection, bioenergetic performance, and maintenance of redox balance. New sites suggest a host of potential mechanisms by which excitation-contraction coupling may also be modulated.

Indexed as

Protein Processing, Post-TranslationalAcetylationAnimalsCell FractionationChromatography, LiquidCitric Acid CycleFatty AcidsGene ExpressionGlycolysisGuinea PigsLysineMaleMitochondriaMolecular Motor ProteinsMolecular Sequence AnnotationMyocardiumFatty AcidsLysineMolecular Motor ProteinsProteome

Identifiers

PMID23844019
PMCPMC3699649
OpenAlexW2087737687

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.