Evidence map›Paper›PMID 11032346›Full record

ArticleJournal of muscle research and cell motility2000

Actomyosin interactions in a novel single muscle fiber in vitro motility assay.

P Hook, L Larsson

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Journal of muscle research and cell motility, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
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

19 citing papers in PubMed.

  1. Trial
  2. Article
  3. Sarcopenia: Aging-Related Loss of Muscle Mass and Function.Physiological reviews · 2019 · on this map
    Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Evolving concepts on the age-related changes in "muscle quality".Journal of cachexia, sarcopenia and muscle · 2012
    Article
  9. Article
  10. Disrupted myosin cross-bridge cycling kinetics triggers muscle weakness in nebulin-related myopathy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Skeletal muscle contractile protein function is preserved in human heart failure.Journal of applied physiology (Bethesda, Md. : 1985) · 2008
    Article
  17. Article
  18. Article
  19. 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.

P HookDepartment of Clinical Neuroscience, Karolinska Hospital, Stockholm, Sweden.
L Larsson

Funding

SARCOPENIA--UNDERLYING MECHANISMSR01AR045627 · NIAMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI DWORKIN, BARRY R · 2000 to 2003
$1.3M
NIAMS NIH HHS AR45627
6 · The paper itself

Abstract

A novel in vitro motility assay has been developed to study the actomyosin interaction, in which the molecular motor protein myosin has been extracted and immobilized directly from 2-4 mm single rat skeletal muscle fiber segments. This method study was carried out to investigate: (1) the amount of myofibrillar proteins extracted from the fiber segment; (2) the effects of temperature on the speed at which actin is propelled by fast and slow myosin; and (3) the effects of myosin isoform expression on motility speed. Approximately 80% of the myosin and myosin-associated proteins were extracted from the fiber segments. while no significant extraction was shown of the thin filament proteins. Fluorescently labeled actin filaments moved with constant speed in a bi-directional motion over the high-density myosin region in the experimental chamber, and motility speed was highly dependent on the myosin heavy chain (MyHC) isoform extracted. At 25 degrees C, significant (P < 0.001) differences in motility speed were obtained between type I (1.31 +/- 0.23 microm/s, n = 11) and IIxb (5.81 +/- 0.35 microm/s, n = 6), or llb (6.07 +/- 0.33 microm/s, n = 8) MyHC isoforms. The motility speed and maximum velocity of unloaded shortening (V0) in single fibers were well correlated, indicating that filament speed is a good molecular analogue to contractile speed at the fiber level. The effects of temperature on filament motility speed were analyzed from 10 to 35 degrees C. The Q10 values, calculated in the 10-25 degrees C temperature range, differed between slow (4.20) and fast (2.38) myosin. In conclusion, this in vitro motility assay offers a unique possibility to compare the regulatory and modulatory influence of myosin isoforms and thin filament proteins on shortening velocity, at the cellular and molecular level in the same muscle fiber.

Indexed as

Biological AssayActinsActomyosinAnimalsMovementMuscle ContractionMyosin Heavy ChainsMyosinsProtein IsoformsRatsRats, WistarTemperatureActinsActomyosinMyosin Heavy ChainsMyosinsProtein Isoforms

Identifiers

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.