Evidence map›Paper›PMID 18411228›Full record

ArticleCardiovascular research2008

The molecular phenotype of human cardiac myosin associated with hypertrophic obstructive cardiomyopathy.

Adam M Jacques, Natalia Briceno, Andrew E Messer, Clare E Gallon, Shapour Jalilzadeh, Edwin Garcia, Gaelle Kikonda-Kanda, Jennifer Goddard, Sian E Harding, Hugh Watkins and 4 more

Open access · hybridAbstract readComparative Study
In one paragraph

Article in Cardiovascular research, 2008. 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
3.3field-weighted citation impact, top 7% 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, 43 citations in OpenAlex.

  1. Evidence for a role of adverse sarcomere signaling in atrial fibrillation induction.Journal of molecular and cellular cardiology plus · 2026
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  7. Cardiomyopathies and Related Changes in Contractility of Human Heart Muscle.International journal of molecular sciences · 2018
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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

14 authors at 4 institutions in 2 countries.

Adam M JacquesCardiac Medicine, National Heart and Lung Institute, Imperial College London, Guy Scadding Building, Dovehouse Street, London, UK.
Natalia Briceno
Andrew E Messer
Clare E Gallon
Shapour Jalilzadeh
Edwin Garcia
Gaelle Kikonda-Kanda
Jennifer Goddard
Sian E Harding
Hugh Watkins
M Tomé Esteban
Victor T Tsang
William J McKenna
Steven B Marston
Imperial College London · GBJohn Radcliffe Hospital · GBUniversity College London · GBLung Institute · US

Funding

British Heart Foundation RG/07/012/24110Department of Health
6 · The paper itself

Abstract

aimThe aim of the study was to compare the functional and structural properties of the motor protein, myosin, and isolated myocyte contractility in heart muscle excised from hypertrophic cardiomyopathy patients by surgical myectomy with explanted failing heart and non-failing donor heart muscle.

methodsMyosin was isolated and studied using an in vitro motility assay. The distribution of myosin light chain-1 isoforms was measured by two-dimensional electrophoresis. Myosin light chain-2 phosphorylation was measured by sodium dodecyl sulphate-polyacrylamide gel electrophoresis using Pro-Q Diamond phosphoprotein stain.

resultsThe fraction of actin filaments moving when powered by myectomy myosin was 21% less than with donor myosin (P = 0.006), whereas the sliding speed was not different (0.310 +/- 0.034 for myectomy myosin vs. 0.305 +/- 0.019 microm/s for donor myosin in six paired experiments). Failing heart myosin showed 18% reduced motility. One myectomy myosin sample produced a consistently higher sliding speed than donor heart myosin and was identified with a disease-causing heavy chain mutation (V606M). In myectomy myosin, the level of atrial light chain-1 relative to ventricular light chain-1 was 20 +/- 5% compared with 11 +/- 5% in donor heart myosin and the level of myosin light chain-2 phosphorylation was decreased by 30-45%. Isolated cardiomyocytes showed reduced contraction amplitude (1.61 +/- 0.25 vs. 3.58 +/- 0.40%) and reduced relaxation rates compared with donor myocytes (TT(50%) = 0.32 +/- 0.09 vs. 0.17 +/- 0.02 s).

conclusionContractility in myectomy samples resembles the hypocontractile phenotype found in end-stage failing heart muscle irrespective of the primary stimulus, and this phenotype is not a direct effect of the hypertrophy-inducing mutation. The presence of a myosin heavy chain mutation causing hypertrophic cardiomyopathy can be predicted from a simple functional assay.

Indexed as

Muscle ContractionActin CytoskeletonAdultCardiac MyosinsCardiomyopathy, HypertrophicGenotypeHeart FailureHumansMiddle AgedMutationMyocytes, CardiacMyosin Heavy ChainsMyosin Light ChainsPhenotypePhosphorylationYoung AdultCardiac MyosinshALC-1 protein, humanMYH7 protein, humanMyosin Heavy Chainsmyosin light chain 2myosin light chain IMyosin Light Chains

Identifiers

PMID18411228
PMCPMC2492731
OpenAlexW2074688769

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.