Evidence map›Paper›PMID 7741690›Full record

ArticleThe Biochemical journal1995

Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy.

R Medina, S S Wing, A L Goldberg

Abstract read
In one paragraph

Article in The Biochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
7.4field-weighted citation impact, top 2% 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

76 citing papers in PubMed, 291 citations in OpenAlex.

  1. Article
  2. Review
  3. The proteasome regulates body weight and systemic nutrient metabolism during fasting.American journal of physiology. Endocrinology and metabolism · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Mitochondrial Bioenergetics and Turnover during Chronic Muscle Disuse.International journal of molecular sciences · 2021
    Review
  8. Article
  9. Article
  10. Interactions of the super complexes: When mTORC1 meets the proteasome.The international journal of biochemistry & cell biology · 2019
    Review
  11. Article
  12. Article
  13. Disrupted autophagy undermines skeletal muscle adaptation and integrity.Mammalian genome : official journal of the International Mammalian Genome Society · 2016
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. CYLD-mediated signaling and diseases.Current drug targets · 2015
    Review

16 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

R MedinaDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
S S Wing
A L Goldberg
Harvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Most of the increased protein degradation in muscle atrophy caused by starvation and denervation is due to activation of a non-lysosomal ATP-dependent proteolytic process. To determine whether expression of the ubiquitin-proteasome-dependent pathway is activated in atrophying muscles, we measured the levels of mRNA for ubiquitin (Ub) and proteasome subunits, and Ub content. After rats had been deprived of food for 1 or 2 days, the concentration of the two polyubiquitin (polyUb) transcripts increased 2-4-fold in the pale extensor digitorum longus muscle and 1-2.5-fold in the red soleus, whereas total muscle RNA and total mRNA content fell by 50%. After denervation of the soleus, there was a progressive 2-3-fold increase in polyUb mRNA for 1-3 days, whereas total RNA content fell. On starvation or denervation, Ub concentration in the muscles also rose by 60-90%. During starvation, polyUb mRNA levels also increased in heart, but not in liver, kidney, spleen, fat, brain or testes. Although the polyUb gene is a heat-shock gene that is induced in muscles under certain stressful conditions, the muscles of starving rats or after denervation did not express other heat-shock genes. On starvation or denervation, mRNA for several proteasome subunits (C-1, C-3, C-5, C-8 and C-9) also increased 2-4-fold in the atrophying muscles. When the food-deprived animals were re-fed, levels of Ub and proteasome mRNA in their muscles returned to control values within 1 day. In contrast, no change occurred in the levels of muscle mRNAs encoding cathepsin L, cathepsin D and calpain 1 on denervation or food deprivation. Thus polyUb and proteasome mRNAs increased in atrophying muscles in co-ordination with activation of the ATP-dependent proteolytic process.

Indexed as

Adenosine TriphosphateAnimalsBiopolymersCysteine EndopeptidasesEndopeptidasesGene ExpressionHeat-Shock ProteinsMaleMultienzyme ComplexesMuscle DenervationMuscle, SkeletalMuscular AtrophyMyocardiumPolyubiquitinProteasome Endopeptidase ComplexRatsAdenosine TriphosphateBiopolymersCysteine EndopeptidasesEndopeptidasesHeat-Shock ProteinsMultienzyme ComplexesPolyubiquitinProteasome Endopeptidase ComplexRNA, MessengerUbiquitinsNon-programmatic

Identifiers

PMID7741690
PMCPMC1136697
OpenAlexW1729354010

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.