Evidence map›Paper›PMID 35028803›Full record

ArticleInflammation2022

Enrichment of Newly Synthesized Proteins following treatment of C2C12 Myotubes with Endotoxin and Interferon-γ.

Catherine S Coleman, Bruce A Stanley, Charles H Lang

Open access · greenAbstract read
In one paragraph

Article in Inflammation, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 60% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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

3 authors at 2 institutions in 1 country.

Catherine S ColemanDepartment of Cellular and Molecular Physiology, Penn State College of Medicine, Hershey, PA, 17033, USA.
Bruce A StanleySection of Research Resources, Penn State College of Medicine, Hershey, PA, 17033, USA.
Charles H LangDepartment of Cellular and Molecular Physiology, Penn State College of Medicine, Hershey, PA, 17033, USA. chl1@psu.edu.ORCID http://orcid.org/0000-0002-3260-7363
Pennsylvania State University · USPenn State Milton S. Hershey Medical Center · US

Funding

Regulation of Nutrient Sensing and Muscle Wasting by AlcoholR01AA011290 · NIAAA · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI LANG, CHARLES H. · 1997 to 2011
$3.5M
Regulation of Nutrient Sensing and Muscle Wasting by AlcoholR37AA011290 · NIAAA · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI LANG, CHARLES H. · 2012 to 2021
$3.4M
NIAAA NIH HHS R01 AA011290NIAAA NIH HHS R37 AA011290
6 · The paper itself

Abstract

Inflammation in muscle induces the synthesis of mediators that can impair protein synthesis and enhance proteolysis, and when sustained lead to muscle atrophy. Furthermore, muscle-derived mediators that are secreted may participate in disrupting the function of other peripheral organs. Selective identification of newly synthesized proteins can provide insight on biological processes that depend on the continued synthesis of specific proteins to maintain homeostasis as well as those proteins that are up- or down-regulated in response to inflammation. We used puromycin-associated nascent chain proteomics (PUNCH-P) to characterize new protein synthesis in C2C12 myotubes and changes resulting from their exposure to the inflammatory mediators lipopolysaccharide (LPS) and interferon (IFN)-γ for either a short (4 h) or prolonged (16 h) time period. We identified sequences of nascent polypeptide chains belonging to a total of 1523 proteins and report their detection from three independent samples of each condition at each time point. The identified nascent proteins correspond to approximately 15% of presently known proteins in C2C12 myotubes and are enriched in specific cellular components and pathways. A subset of these proteins was identified only in treated samples and has functional characteristics consistent with the synthesis of specific new proteins in response to LPS/IFNγ. Thus, the identification of proteins from their nascent polypeptide chains provides a resource to analyze the role of new synthesis of proteins in both protein homeostasis and in proteome responses to stimuli in C2C12 myotubes. Our results reveal a profile of actively translating proteins for specific cellular components and biological processes in normal C2C12 myotubes and a different enrichment of proteins in response to LPS/IFNγ. Collectively, our data disclose a highly interconnected network that integrates the regulation of cellular proteostasis and reveal a diverse immune response to inflammation in muscle which may underlie the concomitantly observed atrophy and be important in inter-organ communication.

Indexed as

Interferon-gammaLipopolysaccharidesMuscle Fibers, SkeletalProtein BiosynthesisHumansInflammationInterferon-gammaLipopolysaccharidesImmune responseInflammationLPSMuscleProteome

Identifiers

PMID35028803
PMCPMC9106851
OpenAlexW4205731173

What OpenQuestion holds

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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.