Evidence map›Paper›PMID 16840579›Full record

ArticleJournal of applied physiology (Bethesda, Md. : 1985)2006

Myosin and actin expression and oxidation in aging muscle.

Ladora V Thompson, David Durand, Nicole A Fugere, Deborah A Ferrington

Open access · greenAbstract read
In one paragraph

Article in Journal of applied physiology (Bethesda, Md. : 1985), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

34 citing papers in PubMed, 80 citations in OpenAlex.

  1. Trial
  2. Mechanisms of Biological Aging with Special Reference to the Skeletal Muscle.Advances in experimental medicine and biology · 2025
    Review
  3. Article
  4. Article
  5. Effect ofFrontiers in nutrition · 2023
    Article
  6. Protein Oxidation in Muscle Foods: A Comprehensive Review.Antioxidants (Basel, Switzerland) · 2021
    Review
  7. Article
  8. The Effects of Calcium-Oxidative medicine and cellular longevity · 2020
    Article
  9. Sarcopenia: Aging-Related Loss of Muscle Mass and Function.Physiological reviews · 2019 · on this map
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Age-induced oxidative stress: how does it influence skeletal muscle quantity and quality?Journal of applied physiology (Bethesda, Md. : 1985) · 2016
    Review
  16. Improved single muscle fiber quality in the oldest-old.Journal of applied physiology (Bethesda, Md. : 1985) · 2016
    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 2 institutions in 1 country.

Ladora V ThompsonDepartment of Physical Medicine and Rehabilitation, University of Minnesota, Minneapolis, Minnesota 55455, USA. thomp067@umn.edu
David Durand
Nicole A Fugere
Deborah A Ferrington
University of Minnesota · USTwin Cities Orthopedics · US

Funding

Structural and Calcium Regulatory Proteins in SarcopeniaR01AG017768 · NIA · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMPSON, LADORA V · 2001 to 2012
$3.0M
Myosin Modifications in Aged MuscleK02AG021626 · NIA · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMPSON, LADORA V · 2003 to 2007
$541k
NIA NIH HHS AG-17768NIA NIH HHS AG-21626NIA NIH HHS K02 AG021626NIA NIH HHS R01 AG017768
6 · The paper itself

Abstract

While the age-related loss in muscle mass partially explains the decline in strength, other yet undefined mechanisms contribute. This study investigates whether changes in myosin-actin stoichiometry and oxidative modification could help explain the decrement in muscle strength with aging. Protein expression and oxidation were evaluated in myosin and actin isolated from the soleus and semimembranosus muscles from young adult, old, and very old Fischer 344 rats. In the soleus muscle, actin and myosin content did not change with aging. In the semimembranosus, actin content was stable, but myosin exhibited decreased content in muscles from very old rats, resulting in a decrease in the myosin-to-actin ratio. 3-Nitrotyrosine and 4-hydroxy-2-nonenal were used as markers of protein oxidative damage. Although myosin and actin are modified with 3-nitrotyrosine and 4-hydroxy-2-nonenal, the extent of chemical modification does not increase with age. The results suggest that the decline in force production with age is not due to the accumulation of these two specific markers of protein oxidation on the myofibrillar proteins. Additionally, age-dependent changes in myofibrillar stoichiometry do not contribute to the decline in force production in the soleus, but may play a role in the semimembranosus with advanced age.

Indexed as

ActinsAgingAnimalsGene ExpressionMaleMuscle, SkeletalMyosinsOxidation-ReductionRatsRats, Inbred F344ActinsMyosins

Identifiers

PMID16840579
PMCPMC4394392
OpenAlexW2127699568

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.