Evidence map›Paper›PMID 25972815›Full record

ArticleFrontiers in physiology2015

Proteomic analysis of media from lung cancer cells reveals role of 14-3-3 proteins in cachexia.

Julie B McLean, Jennifer S Moylan, Erin M W Horrell, Francisco H Andrade

Open access · goldAbstract read
In one paragraph

Article in Frontiers in physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. The expression landscape of cachexia-inducing factors in human cancers.Journal of cachexia, sarcopenia and muscle · 2020
    Article
  3. Effects of conditioned media from murine lung cancer cells and human tumor cells on cultured myotubes.American journal of physiology. Endocrinology and metabolism · 2020
    Article
  4. Article
  5. Article
  6. Cancer cachexia-when proteasomal inhibition is not enough.Journal of cachexia, sarcopenia and muscle · 2016
    Article
  7. 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 1 institution in 1 country.

Julie B McLeanDepartment of Physiology, University of Kentucky Lexington, KY, USA ; Center for Muscle Biology, University of Kentucky Lexington, KY, USA.
Jennifer S MoylanDepartment of Physiology, University of Kentucky Lexington, KY, USA ; Center for Muscle Biology, University of Kentucky Lexington, KY, USA ; Center for Clinical and Translational Science, University of Kentucky Lexington, KY, USA.
Erin M W HorrellDepartment of Physiology, University of Kentucky Lexington, KY, USA ; Markey Cancer Center, University of Kentucky Lexington, KY, USA.
Francisco H AndradeDepartment of Physiology, University of Kentucky Lexington, KY, USA ; Center for Muscle Biology, University of Kentucky Lexington, KY, USA.
University of Kentucky · US

Funding

Kentucky Center for Clinical and Translational ScienceUL1TR000117 · NCATS · UNIVERSITY OF KENTUCKY · PI KERN, PHILIP A · 2012 to 2015
$13.3M
Respiratory Muscle Weakness in Chronic InflammationR01AR055974 · NIAMS · UNIVERSITY OF KENTUCKY · PI ANDRADE, FRANCISCO H · 2009 to 2013
$1.6M
NCATS NIH HHS UL1 TR000117NIAMS NIH HHS R01 AR055974
6 · The paper itself

Abstract

aimsAt the time of diagnosis, 60% of lung cancer patients present with cachexia, a severe wasting syndrome that increases morbidity and mortality. Tumors secrete multiple factors that contribute to cachectic muscle wasting, and not all of these factors have been identified. We used Orbitrap electrospray ionization mass spectrometry to identify novel cachexia-inducing candidates in media conditioned with Lewis lung carcinoma cells (LCM).

resultsOne-hundred and 58 proteins were confirmed in three biological replicates. Thirty-three were identified as secreted proteins, including 14-3-3 proteins, which are highly conserved adaptor proteins known to have over 200 binding partners. We confirmed the presence of extracellular 14-3-3 proteins in LCM via western blot and discovered that LCM contained less 14-3-3 content than media conditioned with C2C12 myotubes. Using a neutralizing antibody, we depleted extracellular 14-3-3 proteins in myotube culture medium, which resulted in diminished myosin content. We identified the proposed receptor for 14-3-3 proteins, CD13, in differentiated C2C12 myotubes and found that inhibiting CD13 via Bestatin also resulted in diminished myosin content.

conclusionsOur novel findings show that extracellular 14-3-3 proteins may act as previously unidentified myokines and may signal via CD13 to help maintain muscle mass.

Indexed as

14-3-3 proteinscachexiacancermyosinproteomicsskeletal muscle

Identifiers

PMID25972815
PMCPMC4411971
OpenAlexW2022412624

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.