Evidence map›Paper›PMID 14555725›Full record

ArticleThe Journal of physiology2004

The mechanism of the force response to stretch in human skinned muscle fibres with different myosin isoforms.

Marco Linari, Roberto Bottinelli, Maria Antonietta Pellegrino, Massimo Reconditi, Carlo Reggiani, Vincenzo Lombardi

Erratum issuedOpen access · greenAbstract readComparative Study
In one paragraph

Article in The Journal of physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
1.2field-weighted citation impact, top 19% 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

54 citing papers in PubMed, 96 citations in OpenAlex.

  1. Trial
  2. Pulmonary adaptations to swim and inspiratory muscle training.European journal of applied physiology · 2008
    Trial
  3. Trial
  4. Article
  5. Article
  6. Article
  7. Article
  8. How temperature tunes muscle mechanics during eccentric contractions.American journal of physiology. Cell physiology · 2026
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Developmental, physiologic and phylogenetic perspectives on the expression and regulation of myosin heavy chains in mammalian skeletal muscles.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2023
    Review
  15. Eccentric muscle contractions: from single muscle fibre to whole muscle mechanics.Pflugers Archiv : European journal of physiology · 2023
    Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Marco LinariLaboratorio di Fisiologia, Viale GB Morgagni, 63-50134 Firenze, Italy.
Roberto Bottinelli
Maria Antonietta Pellegrino
Massimo Reconditi
Carlo Reggiani
Vincenzo Lombardi
Istituto Nazionale per la Fisica della Materia · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Force enhancement during lengthening of an active muscle, a condition that normally occurs during locomotion in vivo, is attributed to recruitment of myosin heads that exhibit fast attachment to and detachment from actin in a cycle that does not imply ATP splitting. We investigated the kinetic and mechanical features of this cycle in Ca(2+) activated single skinned fibres from human skeletal muscles containing different myosin heavy chain (MHC) isoforms, identified with single-fibre gel electrophoresis. Fibres were activated by using a new set-up that allows development of most of the tension following a temperature jump from 0-1 degrees C to the test temperature (approximately 12 degrees C). In this way we could prevent the development of sarcomere non-uniformity and record sarcomere length changes with a striation follower in any phase of the mechanical protocol. We found that: (i) fibres with fast MHC isoforms develop 40-70% larger isometric forces than those with slow isoforms, as a result of both a larger fraction of force-generating myosin heads and a higher force per head; (ii) in both slow and fast fibres, force enhancement by stretch is due to recruitment of myosin head attachments, without increase in strain per head above the value generated by the isometric heads; and (iii) the extent of recruitment is larger in slow fibres than in fast fibres, so that the steady force and power output elicited by lengthening become similar, indicating that mechanical and kinetic properties of the actin-myosin interactions under stretch become independent of the MHC isoform.

Indexed as

AdultHumansIn Vitro TechniquesMuscle ContractionMuscle Fibers, Fast-TwitchMuscle Fibers, Slow-TwitchMuscle RelaxationMuscle, SkeletalMuscle SpindlesMyosinsProtein IsoformsReflex, StretchMyosinsProtein Isoforms

Identifiers

PMID14555725
PMCPMC1664769
OpenAlexW1573366176

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.