Evidence map›Paper›PMID 20065163›Full record

ArticleCirculation2010

Molecular and functional characterization of a novel cardiac-specific human tropomyosin isoform.

Sudarsan Rajan, Ganapathy Jagatheesan, Chehade N Karam, Marco L Alves, Ilona Bodi, Arnold Schwartz, Christian F Bulcao, Karen M D'Souza, Shahab A Akhter, Greg P Boivin and 8 more

Open access · greenAbstract read
In one paragraph

Article in Circulation, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

61 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Loss of Cardiac Splicing RegulatorJACC. Basic to translational science · 2024
    Article
  8. Structural and Functional Properties of Kappa Tropomyosin.International journal of molecular sciences · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. TwoGenes · 2021
    Article
  14. Article
  15. Low-Level Nanog Expression in the Regulation of Quiescent Endothelium.Arteriosclerosis, thrombosis, and vascular biology · 2020
    Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

1 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

18 authors at 4 institutions in 1 country.

Sudarsan RajanDepartment of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati Medical Center, Cincinnati, OH 45267-0524, USA.
Ganapathy Jagatheesan
Chehade N Karam
Marco L Alves
Ilona Bodi
Arnold Schwartz
Christian F Bulcao
Karen M D'Souza
Shahab A Akhter
Greg P Boivin
Dipak K Dube
Natalia Petrashevskaya
Andrew B Herr
Roger Hullin
Stephen B Liggett
Beata M Wolska
R John Solaro
David F Wieczorek
University of Maryland Medical Center · USUniversity of Illinois Chicago · USSUNY Upstate Medical University · USUniversity of Maryland, Baltimore · US

Funding

Sarcomeric Modifications and Progressive Cardiac MaladaptationP01HL062426 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI SOLARO, R JOHN · 2000 to 2020
$42.4M
MODULATION OF CALCIUM CONTROL OF CARDIAC MYOFIBRILSR01HL022231 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI GUPTA, MADHU, SOLARO, R JOHN · 1985 to 2014
$2.9M
MODULATION OF CALCIUM CONTROL OF CARDIAC MYOFIBRILSR37HL022231 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI SOLARO, R JOHN · 1999 to 2006
$2.2M
The Regulation of Sarcomeric Function by TropomyosinR01HL081680 · NHLBI · UNIVERSITY OF CINCINNATI · PI WIECZOREK, DAVID F · 2007 to 2010
$1.6M
Control of Cardiac Function by Calcium and MyofilamentsR01HL079032 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI WOLSKA, BEATA M. · 2005 to 2008
$1.3M
NHLBI NIH HHS HL062426NHLBI NIH HHS HL081680NHLBI NIH HHS HL22231NHLBI NIH HHS HL79032NHLBI NIH HHS P01 HL062426NHLBI NIH HHS R01 HL022231NHLBI NIH HHS R01 HL079032NHLBI NIH HHS R01 HL081680NHLBI NIH HHS R37 HL022231
6 · The paper itself

Abstract

backgroundTropomyosin (TM), an essential actin-binding protein, is central to the control of calcium-regulated striated muscle contraction. Although TPM1alpha (also called alpha-TM) is the predominant TM isoform in human hearts, the precise TM isoform composition remains unclear. METHODS AND

resultsIn this study, we quantified for the first time the levels of striated muscle TM isoforms in human heart, including a novel isoform called TPM1kappa. By developing a TPM1kappa-specific antibody, we found that the TPM1kappa protein is expressed and incorporated into organized myofibrils in hearts and that its level is increased in human dilated cardiomyopathy and heart failure. To investigate the role of TPM1kappa in sarcomeric function, we generated transgenic mice overexpressing cardiac-specific TPM1kappa. Incorporation of increased levels of TPM1kappa protein in myofilaments leads to dilated cardiomyopathy. Physiological alterations include decreased fractional shortening, systolic and diastolic dysfunction, and decreased myofilament calcium sensitivity with no change in maximum developed tension. Additional biophysical studies demonstrate less structural stability and weaker actin-binding affinity of TPM1kappa compared with TPM1alpha.

conclusionsThis functional analysis of TPM1kappa provides a possible mechanism for the consequences of the TM isoform switch observed in dilated cardiomyopathy and heart failure patients.

Indexed as

Actin CytoskeletonActinsAdultAnimalsCalciumCardiomyopathy, DilatedDimerizationFemaleGene ExpressionHeart FailureHomeostasisHumansIsomerismMaleMiceMice, TransgenicActinsCalciumProtein IsoformsTPM1 protein, humanTropomyosin

Identifiers

PMID20065163
PMCPMC2822663
OpenAlexW2147694838

What OpenQuestion holds

Textmetadata
LicenceTDM
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.