Evidence map›Paper›PMID 15905219›Full record

ArticleThe Journal of physiology2005

Different effects of cardiac versus skeletal muscle regulatory proteins on in vitro measures of actin filament speed and force.

Emilie Warner Clemmens, Michelle Entezari, Donald A Martyn, Michael Regnier

Open access · greenAbstract readComparative Study
In one paragraph

Article in The Journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Molecular mechanisms underlying deoxy-ADP.Pi activation of pre-powerstroke myosin.Protein science : a publication of the Protein Society · 2017
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
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  12. Myofilament length dependent activation.Journal of molecular and cellular cardiology · 2010
    Review
  13. Investigations into tropomyosin function using mouse models.Journal of molecular and cellular cardiology · 2010
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

4 authors at 1 institution in 1 country.

Emilie Warner Clemmens
Michelle Entezari
Donald A Martyn
Michael Regnier
University of Washington · US

Funding

COOPERATIVE THIN FILAMENT ACTIVATION IN STRIATED MUSCLER01HL065497 · NHLBI · UNIVERSITY OF WASHINGTON · PI REGNIER, MICHAEL · 2001 to 2012
$4.5M
Bioengineering Cardiovascular Training GrantT32EB001650 · NIBIB · UNIVERSITY OF WASHINGTON · PI REGNIER, MICHAEL · 2004 to 2019
$3.6M
LENGTH REGULATION OF CARDIAC CONTRACTIONR01HL067071 · NHLBI · UNIVERSITY OF WASHINGTON · PI MARTYN, DONALD ALLYN · 2001 to 2010
$2.3M
CARDIAC CONTRACTILE KINETICSR01HL061683 · NHLBI · UNIVERSITY OF WASHINGTON · PI REGNIER, MICHAEL · 1999 to 2009
$2.1M
NHLBI NIH HHS HL61683NHLBI NIH HHS HL65497NHLBI NIH HHS HL67071NHLBI NIH HHS R01 HL061683NHLBI NIH HHS R01 HL065497NHLBI NIH HHS R01 HL067071NIBIB NIH HHS T32 EB001650
6 · The paper itself

Abstract

Mammalian cardiac and skeletal muscle express unique isoforms of the thin filament regulatory proteins, troponin (Tn) and tropomyosin (Tm), and the significance of these different isoforms in thin filament regulation has not been clearly identified. Both in vitro and skinned cellular studies investigating the mechanism of thin filament regulation in striated muscle have often used heterogeneous mixtures of Tn, Tm and myosin isoforms, and variability in reported results might be explained by different combinations of these proteins. Here we used in vitro motility and force (microneedle) assays to investigate the influence of cardiac versus skeletal Tn and Tm isoforms on actin-heavy meromyosin (HMM) mechanics. When interacting with skeletal HMM, thin filaments reconstituted with cardiac Tn/Tm or skeletal Tn/Tm exhibited similar speed-calcium relationships and significantly increased maximum speed and force per filament length (F/l) at pCa 5 (versus unregulated actin filaments). However, augmentation of F/l was greater with skeletal regulatory proteins. Reconstitution of thin filaments with the heterogeneous combination of skeletal Tn and cardiac Tm decreased sliding speeds at all [Ca2+] relative to thin filaments with skeletal Tn/Tm. Finally, for filaments reconstituted with any heterogeneous mix of Tn and Tm isoforms, force was not potentiated over that of unregulated actin filaments. Combined the results suggest (1) that cardiac regulatory proteins limit the allosteric enhancement of force, and (2) that Tn and Tm isoform homogeneity is important when studying Ca2+ regulation of crossbridge binding and kinetics as well as mechanistic differences between cardiac and skeletal muscle.

Indexed as

ActinsAnimalsCalciumMaleMolecular Motor ProteinsMuscle, SkeletalMyocardiumRatsStress, MechanicalTropomyosinTroponinActinsCalciumMolecular Motor ProteinsTropomyosinTroponin

Identifiers

PMID15905219
PMCPMC1464789
OpenAlexW1512100286

What OpenQuestion holds

Textmetadata
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.