Evidence map›Paper›PMID 14636157›Full record

ArticleThe Biochemical journal2004

Glucocorticoids regulate mRNA levels for subunits of the 19 S regulatory complex of the 26 S proteasome in fast-twitch skeletal muscles.

Lydie Combaret, Daniel Taillandier, Dominique Dardevet, Daniel Béchet, Cécile Rallière, Agnès Claustre, Jean Grizard, Didier Attaix

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2004. 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
4.2field-weighted citation impact, top 5% 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, 75 citations in OpenAlex.

  1. Trial
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  7. Molecular and cellular mechanisms of skeletal muscle atrophy: an update.Journal of cachexia, sarcopenia and muscle · 2012
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  12. FOXO3a mediates signaling crosstalk that coordinates ubiquitin and atrogin-1/MAFbx expression during glucocorticoid-induced skeletal muscle atrophy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2010
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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

8 authors.

Lydie CombaretHuman Nutrition Research Center of Clermont-Ferrand, and Nutrition and Protein Metabolism Unit, Institut National de la Recherche Agronomique, 63122 Ceyrat, France.
Daniel Taillandier
Dominique Dardevet
Daniel Béchet
Cécile Rallière
Agnès Claustre
Jean Grizard
Didier Attaix

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Circulating levels of glucocorticoids are increased in many traumatic and muscle-wasting conditions that include insulin-dependent diabetes, acidosis, infection, and starvation. On the basis of indirect findings, it appeared that these catabolic hormones are required to stimulate Ub (ubiquitin)-proteasome-dependent proteolysis in skeletal muscles in such conditions. The present studies were performed to provide conclusive evidence for an activation of Ub-proteasome-dependent proteolysis after glucocorticoid treatment. In atrophying fast-twitch muscles from rats treated with dexamethasone for 6 days, compared with pair-fed controls, we found (i) increased MG132-inhibitable proteasome-dependent proteolysis, (ii) an enhanced rate of substrate ubiquitination, (iii) increased chymotrypsin-like proteasomal activity of the proteasome, and (iv) a co-ordinate increase in the mRNA expression of several ATPase (S4, S6, S7 and S8) and non-ATPase (S1, S5a and S14) subunits of the 19 S regulatory complex, which regulates the peptidase and the proteolytic activities of the 26 S proteasome. These studies provide conclusive evidence that glucocorticoids activate Ub-proteasome-dependent proteolysis and the first in vivo evidence for a hormonal regulation of the expression of subunits of the 19 S complex. The results suggest that adaptations in gene expression of regulatory subunits of the 19 S complex by glucocorticoids are crucial in the regulation of the 26 S muscle proteasome.

Indexed as

Adenosine TriphosphatasesAnimalsChymotrypsinCulture TechniquesCysteine EndopeptidasesCysteine Proteinase InhibitorsDexamethasoneEndopeptidasesGene Expression RegulationGlucocorticoidsLeupeptinsMaleMultienzyme ComplexesMuscle Fibers, Fast-TwitchMuscle ProteinsMuscle, Skeletal26S proteasome non-ATPase regulatory subunit 13Adenosine TriphosphatasesATP dependent 26S proteasebenzyloxycarbonylleucyl-leucyl-leucine aldehydeChymotrypsinCysteine EndopeptidasesCysteine Proteinase InhibitorsDexamethasoneEndopeptidasesGlucocorticoidsLeupeptinsMultienzyme ComplexesMuscle ProteinsPeptide HydrolasesProteasome Endopeptidase ComplexProtein SubunitsRNA, MessengerUbiquitins

Identifiers

PMID14636157
PMCPMC1223943
OpenAlexW2038499449

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.