Evidence map›Paper›PMID 16308684›Full record

ArticleJournal of molecular medicine (Berlin, Germany)2006

Reduced stress tolerance of glutamine-deprived human monocytic cells is associated with selective down-regulation of Hsp70 by decreased mRNA stability.

Maja Munk Eliasen, Marianne Brabec, Christopher Gerner, Jürgen Pollheimer, Herbert Auer, Maria Zellner, Gertrude Weingartmann, Fritz Garo, Erich Roth, Rudolf Oehler

Abstract read
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In one paragraph

Article in Journal of molecular medicine (Berlin, Germany), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

10 citing papers in PubMed, 43 citations in OpenAlex.

  1. Trial
  2. Trial
  3. Trial
  4. Article
  5. How wasting is saving: weight loss at altitude might result from an evolutionary adaptation.BioEssays : news and reviews in molecular, cellular and developmental biology · 2014
    Article
  6. [Immunonutrition in intensive care medicine].Medizinische Klinik, Intensivmedizin und Notfallmedizin · 2013
    Review
  7. Article
  8. Article
  9. The HSP72 stress response of monocytes from patients on haemodialysis is impaired.Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association · 2009
    Article
  10. 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

10 authors at 1 institution in 1 country.

Maja Munk EliasenDepartment of Surgery-Research Laboratories, Medical University of Vienna, AKH (8G9.05), Waehringer-Guertel 18-20, 1090, Vienna, Austria. rudolf.oehler@meduniwien.ac.at
Marianne Brabec
Christopher Gerner
Jürgen Pollheimer
Herbert Auer
Maria Zellner
Gertrude Weingartmann
Fritz Garo
Erich Roth
Rudolf Oehler
Medical University of Vienna · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In critically ill patients, clinicians observe a reverse correlation of survival and a decreased plasma concentration of the most abundant free amino acid, glutamine (Gln). However, in this context, the role of Gln remains largely elusive. Gln is used as an energy substrate by monocytes. Gln deprivation of these cells results in an increased susceptibility to cell stress and apoptosis, as well as in a reduced responsiveness to pro-inflammatory stimuli. We performed a systematic study to elucidate the molecular mechanism by which Gln depletion affects the heat stress response of the monocytic cell line U937. Proteomic analysis revealed that Gln depletion was associated with specific changes in the protein expression pattern. However, the overall level of tRNA-bound Gln remained unaffected. The stress protein heat shock protein (Hsp) 70 showed the highest reduction in protein synthesis. This was due to enhanced mRNA decay during Gln starvation while the transcriptional and the translational control of Hsp70 expression remained unchanged. A physiological Gln concentration and above was found to be necessary for maximum Hsp70 accumulation upon heat shock. Thus, the study shows a specific link between Gln metabolism and the regulation of heat shock proteins.

Indexed as

Down-RegulationCells, CulturedGlutamineHSP70 Heat-Shock ProteinsHumansMonocytesPolyribosomesRNA, MessengerTemperatureTime FactorsGlutamineHSP70 Heat-Shock ProteinsRNA, Messenger

Identifiers

PMID16308684
OpenAlexW2080298706

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.