Evidence map›Paper›PMID 12944292›Full record

ArticleBiophysical journal2003

Ca2+ regulation of rabbit skeletal muscle thin filament sliding: role of cross-bridge number.

Bo Liang, Ying Chen, Chien-Kao Wang, Zhaoxiong Luo, Michael Regnier, Albert M Gordon, P Bryant Chase

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.4field-weighted citation impact, top 17% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Creatine Kinase Equilibration and ΔGInternational journal of molecular sciences · 2023
    Article
  4. The structure of the native cardiac thin filament at systolic CaProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  5. Mechanical contribution to muscle thin filament activation.The Journal of biological chemistry · 2020
    Article
  6. Article
  7. Frontiers in physiology · 2020
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Slowed Dynamics of Thin Filament Regulatory Units Reduces CaCellular and molecular bioengineering · 2013
    Article
  14. Article
  15. Article
  16. Article
  17. Myofilament length dependent activation.Journal of molecular and cellular cardiology · 2010
    Review
  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

7 authors at 2 institutions in 1 country.

Bo LiangDepartment of Physiology and Biophysics, University of Washington, Seattle, Washington 98195, USA.
Ying Chen
Chien-Kao Wang
Zhaoxiong Luo
Michael Regnier
Albert M Gordon
P Bryant Chase
University of Washington · USFlorida State University · US

Funding

COOPERATIVE THIN FILAMENT ACTIVATION IN STRIATED MUSCLER01HL065497 · NHLBI · UNIVERSITY OF WASHINGTON · PI REGNIER, MICHAEL · 2001 to 2012
$4.5M
CARDIAC CONTRACTILE KINETICSR01HL061683 · NHLBI · UNIVERSITY OF WASHINGTON · PI REGNIER, MICHAEL · 1999 to 2009
$2.1M
REGULATION OF ACTOMYOSIN INTERACTIONS IN CARDIAC MUSCLESP01HL052558 · NHLBI · UNIVERSITY OF WASHINGTON · PI GORDON, ALBERT M · 1994 to 1998
–
NHLBI NIH HHS HL52558NHLBI NIH HHS HL61683NHLBI NIH HHS R01 HL061683NHLBI NIH HHS R01 HL065497
6 · The paper itself

Abstract

We investigated how strong cross-bridge number affects sliding speed of regulated Ca(2+)-activated, thin filaments. First, using in vitro motility assays, sliding speed decreased nonlinearly with reduced density of heavy meromyosin (HMM) for regulated (and unregulated) F-actin at maximal Ca(2+). Second, we varied the number of Ca(2+)-activatable troponin complexes at maximal Ca(2+) using mixtures of recombinant rabbit skeletal troponin (WT sTn) and sTn containing sTnC(D27A,D63A), a mutant deficient in Ca(2+) binding at both N-terminal, low affinity Ca(2+)-binding sites (xxsTnC-sTn). Sliding speed decreased nonlinearly as the proportion of WT sTn decreased. Speed of regulated thin filaments varied with pCa when filaments contained WT sTn but filaments containing only xxsTnC-sTn did not move. pCa(50) decreased by 0.12-0.18 when either heavy meromyosin density was reduced to approximately 60% or the fraction of Ca(2+)-activatable regulatory units was reduced to approximately 33%. Third, we exchanged mixtures of sTnC and xxsTnC into single, permeabilized fibers from rabbit psoas. As the proportion of xxsTnC increased, unloaded shortening velocity decreased nonlinearly at maximal Ca(2+). These data are consistent with unloaded filament sliding speed being limited by the number of cycling cross-bridges so that maximal speed is attained with a critical, low level of actomyosin interactions.

Indexed as

Actin CytoskeletonActinsActomyosinAdenosine TriphosphateAnimalsCalciumDose-Response Relationship, DrugMicroscopy, FluorescenceMovementMuscle, SkeletalMutationMyosinsRabbitsRecombinant ProteinsTime FactorsTroponinActinsActomyosinAdenosine TriphosphateCalciumMyosinsRecombinant ProteinsTroponin

Identifiers

PMID12944292
PMCPMC1303351
OpenAlexW1977129158

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.