Evidence map›Paper›PMID 22796357›Full record

ArticleJournal of proteomics2012

Proteomic analyses of transgenic LQT1 and LQT2 rabbit hearts elucidate an increase in expression and activity of energy producing enzymes.

Hitesh K Jindal, Elisabeth Merchant, James A Balschi, Yajie Zhangand, Gideon Koren

Abstract readComparative Study
In one paragraph

Article in Journal of proteomics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-weighted citation impact, top 32% 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

5 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. NCX-Mediated Subcellular CaBiophysical journal · 2018
    Article
  3. Article
  4. Article
  5. 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

5 authors at 2 institutions in 1 country.

Hitesh K JindalCardiovascular Research Center, Division of Cardiology, Rhode Island Hospital, Alpert Medical School of Brown University, 1 Hoppin Street, West Coro-5, Providence, RI 02903, USA.
Elisabeth Merchant
James A Balschi
Yajie Zhangand
Gideon Koren
Rhode Island Hospital · USBrigham and Women's Hospital · US

Funding

HEART AND MUSCLE K+ CHANNELS--STRUCTURE AND FUNCTIONR01HL046005 · NHLBI · RHODE ISLAND HOSPITAL · PI KOREN, GIDEON · 1991 to 2013
$5.9M
Sex Hormones and Cardiac Arrhythmia in Transgenic LQT2 RabbitsR01HL093205 · NHLBI · RHODE ISLAND HOSPITAL · PI KOREN, GIDEON · 2009 to 2012
$2.3M
CD SPECTROPHOTOMETER: STRUCTURAL BIOL, PROTEIN, MOLECULAR PHARMACOLOGYS10RR020923 · NCRR · BROWN UNIVERSITY · PI MIERKE, DALE F · 2006 to 2006
$105k
NCRR NIH HHS 1S10RR020923NCRR NIH HHS S10 RR020923NHLBI NIH HHS R01 HL046005NHLBI NIH HHS R01-HL-046005-19NHLBI NIH HHS R01 HL093205NHLBI NIH HHS R01-HL-093205-03
6 · The paper itself

Abstract

Various biochemical and genomic mechanisms are considered to be a hallmark of metabolic remodeling in the stressed heart, including the hypertrophied and failing heart. In this study, we used quantitative proteomic 2-D Fluorescence Difference In-Gel Electrophoresis (2-D DIGE) in conjunction with mass spectrometry to demonstrate differential protein expression in the hearts of transgenic rabbit models of Long QT Syndrome 1 (LQT1) and Long QT Syndrome 2 (LQT2) as compared to littermate controls (LMC). The results of our proteomic analysis revealed upregulation of key metabolic enzymes involved in all pathways associated with ATP generation, including creatine kinase in both LQT1 and LQT2 rabbit hearts. Additionally, the expression of lamin-A protein was increased in both LQT1 and LQT2 rabbit hearts as was the expression of mitochondrial aldehyde dehydrogenase and desmoplakin in LQT1 and LQT 2 rabbit hearts, respectively. Results of the proteomic analysis also demonstrated down regulation in the expression of protein disulfide-isomerase A3 precuorsor and dynamin-like 120 kDa protein (mitochondrial) in LQT1, and of alpha-actinin 2 in LQT2 rabbit hearts. Up regulation of the expression of the enzymes associated with ATP generation was substantiated by the results of selective enzyme assays in LQT1 and LQT2 hearts, as compared to LMC, which revealed increases in the activities of glycogen phosphorylase (+50%, +65%, respectively), lactate dehydrogenase (+25%, +25%) pyruvate dehydrogenase (+31%, +22%), and succinate dehydrogenase (+32%, +60%). The activity of cytochrome c-oxidase, a marker for the mitochondrial function was also found to be significantly elevated (+80%) in LQT1 rabbit hearts as compared with LMC. Western blot analysis in LQT1 and LQT2 hearts compared to LMC revealed an increase in the expression of very-long chain-specific acyl-CoA dehydrogenase (+35%, +33%), a rate-limiting enzymes in β-oxidation of fatty acids. Collectively, our results demonstrate similar increases in the expression and activities of key ATP-generating enzymes in LQT1 and LQT2 rabbit hearts, suggesting an increased demand, and in turn, increased energy supply across the entire metabolic pathway by virtue of the upregulation of enzymes involved in energy generation.

Indexed as

Energy MetabolismProteomicsAnimalsAnimals, Genetically ModifiedEnzyme ActivationEnzymesERG1 Potassium ChannelEther-A-Go-Go Potassium ChannelsGene Expression Regulation, EnzymologicHeartKCNQ1 Potassium ChannelLong QT SyndromeMaleMyocardiumProteomeRabbitsEnzymesERG1 Potassium ChannelEther-A-Go-Go Potassium ChannelsKCNQ1 Potassium ChannelProteome

Identifiers

PMID22796357
PMCPMC4386689
OpenAlexW2070997371

What OpenQuestion holds

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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.