Evidence map›Paper›PMID 20203068›Full record

ArticleJournal of applied physiology (Bethesda, Md. : 1985)2010

A new method to study in vivo protein synthesis in slow- and fast-twitch muscle fibers and initial measurements in humans.

J M Dickinson, J D Lee, B E Sullivan, M P Harber, S W Trappe, T A Trappe

Abstract readComparative Study
In one paragraph

Article in Journal of applied physiology (Bethesda, Md. : 1985), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

32 citing papers in PubMed, 45 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Fast and slow muscle fiber transcriptome dynamics with lifelong endurance exercise.Journal of applied physiology (Bethesda, Md. : 1985) · 2024
    Article
  8. Review
  9. Review
  10. Postabsorptive muscle protein synthesis is higher in outpatients as compared to inpatients.American journal of physiology. Endocrinology and metabolism · 2023
    Article
  11. Article
  12. Fiber typing human skeletal muscle with fluorescent immunohistochemistry.Journal of applied physiology (Bethesda, Md. : 1985) · 2019
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. DNA methylation assessment from human slow- and fast-twitch skeletal muscle fibers.Journal of applied physiology (Bethesda, Md. : 1985) · 2017
    Article
  19. Article
  20. Review
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 1 institution in 1 country.

J M DickinsonHuman Performance Laboratory, Ball State University, Muncie, IN 47306, USA.
J D Lee
B E Sullivan
M P Harber
S W Trappe
T A Trappe
Ball State University · US

Funding

Analgesics and resistance training in older individualsR01AG020532 · NIA · UNIVERSITY OF ARKANSAS MED SCIS LTL ROCK · PI TRAPPE, TODD A · 2004 to 2008
$1.4M
NIA NIH HHS R01-AG-020532
6 · The paper itself

Abstract

The aim of this study was to develop an approach to directly assess protein fractional synthesis rate (FSR) in isolated human muscle fibers in a fiber type-specific fashion. Individual muscle fibers were isolated from biopsies of the vastus lateralis (VL) and soleus (SOL) obtained from eight young men during a primed, continuous infusion of [5,5,5-(2)H3]leucine performed under basal conditions. To determine mixed protein FSR, a portion of each fiber was used to identify fiber type, fibers of the same type were pooled, and the [5,5,5-(2)H3]leucine enrichment was determined via GC-MS. Processing isolated slow-twitch [myosin heavy chain (MHC) I] and fast-twitch (MHC IIa) fibers for mixed protein bound [5,5,5-(2)H3]leucine enrichment yielded mass ion chromatographic peaks that were similar in shape, abundance, and measurement reliability as tissue homogenates. In the VL, MHC I fibers exhibited a 33% faster (P<0.05) mixed protein FSR compared with MHC IIa fibers (0.068+/-0.006 vs. 0.051+/-0.003%/h). MHC I fibers from the SOL (0.060+/-0.005%/h) and MHC I fibers from the VL displayed similar (P>0.05) mixed protein FSR. Feasibility of processing isolated human muscle fibers for analysis of myofibrillar protein [5,5,5-(2)H3]leucine enrichment was also confirmed in non-fiber-typed pooled fibers from the VL. These methods can be applied to the study of fiber type-specific responses in human skeletal muscle. The need for this level of investigation is underscored by the different contributions of each fiber type to whole muscle function and the numerous distinct adaptive functional and metabolic changes in MHC I and MHC II fibers originating from the same muscle.

Indexed as

Gas Chromatography-Mass SpectrometryBiopsyFeasibility StudiesHumansInfusions, IntravenousKeto AcidsKineticsLeucineMaleMuscle Fibers, Fast-TwitchMuscle Fibers, Slow-TwitchMyosin Heavy ChainsMyosin Type IQuadriceps MuscleSkeletal Muscle MyosinsTritiumalpha-ketoisocaproic acidKeto AcidsLeucineMyosin Heavy ChainsMyosin Type ISkeletal Muscle MyosinsTritium

Identifiers

PMID20203068
PMCPMC2867531
OpenAlexW2151022076

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.