Evidence map›Paper›PMID 24162314›Full record

ArticleJournal of muscle research and cell motility2013

A re-interpretation of the rate of tension redevelopment (k(TR)) in active muscle.

Li Wang, Masataka Kawai

Abstract read
In one paragraph

Article in Journal of muscle research and cell motility, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Frontiers in physiology · 2020
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. 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

2 authors.

Li WangDepartments of Anatomy and Cell Biology, and Internal Medicine, University of Iowa, Iowa City, IA, 52242, USA, li-wang-1@uiowa.edu.
Masataka Kawai

Funding

Role of actin domains in force generation in myocardiumR01HL070041 · NHLBI · UNIVERSITY OF IOWA · PI KAWAI, MASATAKA · 2002 to 2011
$2.5M
NHLBI NIH HHS HL070041NHLBI NIH HHS R01 HL070041
6 · The paper itself

Abstract

A slackening to zero tension by large length release (~20%) and a restretch of active muscle fibres cause a fall and a redevelopment in tension. According to the model of Brenner (Proc Natl Acad Sci USA 85(9):3265-3269, 1988), the rate constant of tension redevelopment (k TR) is the sum of attachment and detachment rate constants, hence is limited by the fast reaction. Here we propose a model in which, after restretch, cross-bridges cycle many times by stretching series elastic elements, hence k(TR) is limited by a slow reaction. To set up this model, we made an assumption that the stepping rate (v) decreases linearly with tension (F), which is consistent with the Fenn effect. The distance traveled by a cross-bridge stretches series elastic elements with stiffness σ. With these assumptions, we set up a first order differential equation, which results in an exponential time course with the rate constant k(TR) = ση(0)ν(0)(1 - λ)/F(1), where λ = ν(1)/ν(0), η = step size, the subscript 0 indicates unloaded condition, and the subscript 1 indicate isometric condition. We demonstrate that the ATP hydrolysis rate (=[myosin head]/ν(0)) is proportionate to k(TR) as the ambient temperature is changed, and that the published data fit to this relationship well if λ = 0.28. We conclude that k(TR) is limited by the cross-bridge turnover rate; hence it represents the rate constant of the slowest reaction of the cross-bridge cycle, i.e. the ADP isomerization step before ADP is released.

Indexed as

AnimalsBiomechanical PhenomenaIsometric ContractionMuscle ContractionMuscle, SkeletalRabbits

Identifiers

PMID24162314
PMCPMC3909470

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.