Evidence map›Paper›PMID 18299397›Full record

ArticleThe Journal of general physiology2008

Troponin and titin coordinately regulate length-dependent activation in skinned porcine ventricular muscle.

Takako Terui, Munguntsetseg Sodnomtseren, Douchi Matsuba, Jun Udaka, Shin'ichi Ishiwata, Iwao Ohtsuki, Satoshi Kurihara, Norio Fukuda

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.5field-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

32 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
  2. CaJournal of molecular and cellular cardiology · 2025
    Article
  3. Review
  4. Article
  5. Titin force in muscle cells alters lattice order, thick and thin filament protein formation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Microscopic heat pulses activate cardiac thin filaments.The Journal of general physiology · 2019
    Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Calcium sensitivity of residual force enhancement in rabbit skinned fibers.American journal of physiology. Cell physiology · 2014
    Article
  19. Cardiac thin filament regulation and the Frank-Starling mechanism.The journal of physiological sciences : JPS · 2014
    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 2 institutions in 1 country.

Takako TeruiDepartment of Cell Physiology, The Jikei University School of Medicine, Tokyo 105-8461, Japan. pu-cha@jikei.ac.jp
Munguntsetseg Sodnomtseren
Douchi Matsuba
Jun Udaka
Shin'ichi Ishiwata
Iwao Ohtsuki
Satoshi Kurihara
Norio Fukuda
Jikei University School of Medicine · JPWaseda University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We investigated the molecular mechanism by which troponin (Tn) regulates the Frank-Starling mechanism of the heart. Quasi-complete reconstitution of thin filaments with rabbit fast skeletal Tn (sTn) attenuated length-dependent activation in skinned porcine left ventricular muscle, to a magnitude similar to that observed in rabbit fast skeletal muscle. The rate of force redevelopment increased upon sTn reconstitution at submaximal levels, coupled with an increase in Ca2+ sensitivity of force, suggesting the acceleration of cross-bridge formation and, accordingly, a reduction in the fraction of resting cross-bridges that can potentially produce additional active force. An increase in titin-based passive force, induced by manipulating the prehistory of stretch, enhanced length-dependent activation, in both control and sTn-reconstituted muscles. Furthermore, reconstitution of rabbit fast skeletal muscle with porcine left ventricular Tn enhanced length-dependent activation, accompanied by a decrease in Ca2+ sensitivity of force. These findings demonstrate that Tn plays an important role in the Frank-Starling mechanism of the heart via on-off switching of the thin filament state, in concert with titin-based regulation.

Indexed as

Ventricular FunctionAnimalsConnectinIn Vitro TechniquesKineticsMuscle ProteinsMuscle, SkeletalMyocardial ContractionMyocardiumProtein KinasesRabbitsSwineTroponin CConnectinMuscle ProteinsProtein KinasesTroponin C

Identifiers

PMID18299397
PMCPMC2248715
OpenAlexW1963870829

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.