Evidence map›Paper›PMID 28544616›Full record

ArticleAging cell2017

Biochemical isolation of myonuclei employed to define changes to the myonuclear proteome that occur with aging.

Alicia A Cutler, Eric B Dammer, Duc M Doung, Nicholas T Seyfried, Anita H Corbett, Grace K Pavlath

Open access · goldAbstract read
In one paragraph

Article in Aging cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

20 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
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  5. Skeletal muscle wasting: the estrogen side of sexual dimorphism.American journal of physiology. Cell physiology · 2022
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  9. MuscleAtlasExplorer: a web service for studying gene expression in human skeletal muscle.Database : the journal of biological databases and curation · 2020
    Article
  10. Sample multiplexing for targeted pathway proteomics in aging mice.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
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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.

Alicia A CutlerDepartment of Pharmacology, Emory University, Atlanta, GA, 30322, USA.
Eric B DammerDepartment of Biochemistry, Emory University, Atlanta, GA, 30322, USA.
Duc M DoungDepartment of Biochemistry, Emory University, Atlanta, GA, 30322, USA.
Nicholas T SeyfriedDepartment of Biochemistry, Emory University, Atlanta, GA, 30322, USA.
Anita H CorbettDepartment of Biology, Emory University, Atlanta, GA, 30322, USA.
Grace K PavlathDepartment of Pharmacology, Emory University, Atlanta, GA, 30322, USA.
Emory University · US

Funding

Training Program in Biochemistry, Cell and Molecular BiologyT32GM008367 · NIGMS · EMORY UNIVERSITY · PI BOISE, LAWRENCE H., CORBETT, ANITA H. · 1990 to 2019
$5.6M
Nucleocytoplasmic Transport in Skeletal MuscleR01AR062483 · NIAMS · EMORY UNIVERSITY · PI PAVLATH, GRACE K · 2012 to 2016
$1.7M
Interplay between nuclear import and transcriptional activity during myogenesisF31AR067645 · NIAMS · EMORY UNIVERSITY · PI CUTLER, ALICIA A · 2015 to 2017
$128k
NIAMS NIH HHS F31 AR067645NIAMS NIH HHS R01 AR062483NIGMS NIH HHS T32 GM008367
6 · The paper itself

Abstract

Skeletal muscle aging is accompanied by loss of muscle mass and strength. Examining changes in myonuclear proteins with age would provide insight into molecular processes which regulate these profound changes in muscle physiology. However, muscle tissue is highly adapted for contraction and thus comprised largely of contractile proteins making the nuclear proteins difficult to identify from whole muscle samples. By developing a method to purify myonuclei from whole skeletal muscle, we were able to collect myonuclei for analysis by flow cytometry, biochemistry, and mass spectrometry. Nuclear purification dramatically increased the number and intensity of nuclear proteins detected by mass spectrometry compared to whole tissue. We exploited this increased proteomic depth to investigate age-related changes to the myonuclear proteome. Nuclear levels of 54 of 779 identified proteins (7%) changed significantly with age; these proteins were primarily involved in chromatin maintenance and RNA processing. To determine whether the changes we detected were specific to myonuclei or were common to nuclei of excitatory tissues, we compared aging in myonuclei to aging in brain nuclei. Although several of the same processes were affected by aging in both brain and muscle nuclei, the specific proteins involved in these alterations differed between the two tissues. Isolating myonuclei allowed a deeper view into the myonuclear proteome than previously possible facilitating identification of novel age-related changes in skeletal muscle. Our technique will enable future studies into a heretofore underrepresented compartment of skeletal muscle.

Indexed as

AgingAnimalsBrainCell FractionationCell NucleusGene OntologyMaleMiceMice, Inbred C57BLMice, TransgenicMolecular Sequence AnnotationMuscle, SkeletalNuclear ProteinsOrgan SpecificityProteomeNuclear ProteinsProteomeagingbrainmyonucleinuclear isolationproteomeskeletal muscle

Identifiers

PMID28544616
PMCPMC5506426
OpenAlexW2619563438

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.