Evidence map›Paper›PMID 28336537›Full record

ArticleJournal of applied physiology (Bethesda, Md. : 1985)2017

Muscle-specific and age-related changes in protein synthesis and protein degradation in response to hindlimb unloading in rats.

Leslie M Baehr, Daniel W D West, Andrea G Marshall, George R Marcotte, Keith Baar, Sue C Bodine

Open access · bronzeAbstract read
In one paragraph

Article in Journal of applied physiology (Bethesda, Md. : 1985), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
5.3field-weighted citation impact, top 3% 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

75 citing papers in PubMed, 114 citations in OpenAlex.

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15 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 1 country.

Leslie M BaehrVeterans Affairs Northern California Health Care System, Mather, California.
Daniel W D WestVeterans Affairs Northern California Health Care System, Mather, California.
Andrea G MarshallDepartment of Physiology and Membrane Biology, University of California Davis, Davis, California; and.
George R MarcotteVeterans Affairs Northern California Health Care System, Mather, California.
Keith BaarVeterans Affairs Northern California Health Care System, Mather, California.
Sue C BodineVeterans Affairs Northern California Health Care System, Mather, California; scbodine@ucdavis.edu.
University of California, Davis · USVA Northern California Health Care System · US

Funding

LAT1 and the development of anabolic resistanceR01AG045375 · NIA · UNIVERSITY OF CALIFORNIA AT DAVIS · PI BAAR, KEITH · 2014 to 2018
$1.7M
NIA NIH HHS R01 AG045375
6 · The paper itself

Abstract

Disuse is a potent inducer of muscle atrophy, but the molecular mechanisms driving this loss of muscle mass are highly debated. In particular, the extent to which disuse triggers decreases in protein synthesis or increases in protein degradation, and whether these changes are uniform across muscles or influenced by age, is unclear. We aimed to determine the impact of disuse on protein synthesis and protein degradation in lower limb muscles of varied function and fiber type in adult and old rats. Alterations in protein synthesis and degradation were measured in the soleus, medial gastrocnemius, and tibialis anterior (TA) muscles of adult and old rats subjected to hindlimb unloading (HU) for 3, 7, or 14 days. Loss of muscle mass was progressive during the unloading period, but highly variable (-9 to -38%) across muscle types and between ages. Protein synthesis decreased significantly in all muscles, except for the old TA. Atrophy-associated gene expression was only loosely associated with protein degradation as muscle RING finger-1, muscle atrophy F-box (MAFbx), and Forkhead box O1 expression significantly increased in all muscles, but an increase in proteasome activity was only observed in the adult soleus. MAFbx protein levels were significantly higher in the old muscles compared with adult muscles, despite the old having higher expression of microRNA-23a. These results indicate that adult and old muscles respond similarly to HU, and the greatest loss in muscle mass occurs in predominantly slow-twitch extensor muscles due to a concomitant decrease in protein synthesis and increase in protein degradation.

Indexed as

AnimalsHindlimbHindlimb SuspensionMaleMuscle Fibers, SkeletalMuscle ProteinsMuscular AtrophyProtein BiosynthesisProteolysisRatsRats, Inbred F344Muscle ProteinsagingmiR-23amuscle atrophyproteasome

Identifiers

PMID28336537
PMCPMC5451534
OpenAlexW2600155173

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.