Evidence map›Paper›PMID 17854134›Full record

ReviewWorld journal of gastroenterology2007

Implication of altered proteasome function in alcoholic liver injury.

Natalia A Osna, Terrence-M Donohue

Open access · greenAbstract readReview
In one paragraph

Review in World journal of gastroenterology, 2007. 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
2.3field-weighted citation impact, top 12% 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, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Alcohol-induced alterations of the hepatocyte cytoskeleton.World journal of gastroenterology · 2010
    Review
  15. Effects of ethanol on the proteasome interacting proteins.World journal of gastroenterology · 2010
    Review
  16. Impaired methylation as a novel mechanism for proteasome suppression in liver cells.Biochemical and biophysical research communications · 2010
    Article
  17. Focus on the liver: alcohol use, highly active antiretroviral therapy, and liver disease in HIV-infected patients.Alcohol research & health : the journal of the National Institute on Alcohol Abuse and Alcoholism · 2010
    Review
  18. Article
  19. Article
  20. Acute alcohol intoxication increases atrogin-1 and MuRF1 mRNA without increasing proteolysis in skeletal muscle.American journal of physiology. Regulatory, integrative and comparative physiology · 2008
    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

2 authors at 1 institution in 1 country.

Natalia A OsnaLiver Study Unit, Research Service (151), VA Medical Center, 4101 Woolworth Ave, Omaha, NE 68105, USA. nosna@unmc.edu
Terrence-M Donohue
National Institute on Alcohol Abuse and Alcoholism · US

Funding

Ethanol Effects on Antigen Presentation in Liver CellsR21AA015379 · NIAAA · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI OSNA, NATALIA ALEKSANDR · 2005 to 2006
$326k
NIAAA NIH HHS 5R21 AA015379-02NIAAA NIH HHS R21 AA015379
6 · The paper itself

Abstract

The proteasome is a major protein-degrading enzyme, which catalyzes degradation of oxidized and aged proteins, signal transduction factors and cleaves peptides for antigen presentation. Proteasome exists in the equilibrium of 26S and 20S particles. Proteasome function is altered by ethanol metabolism, depending on oxidative stress levels: low oxidative stress induces proteasome activity, while high oxidative stress reduces it. The proposed mechanisms for modulation of proteasome activity are related to oxidative modification of proteasomal proteins with primary and secondary products derived from ethanol oxidation. Decreased proteolysis by the proteasome results in the accumulation of insoluble protein aggregates, which cannot be degraded by proteasome and which further inhibit proteasome function. Mallory bodies, a common signature of alcoholic liver diseases, are formed by liver cells, when proteasome is unable to remove cytokeratins. Proteasome inhibition by ethanol also promotes the accumulation of pro-apoptotic factors in mitochondria of ethanol-metabolizing liver cells that are normally degraded by proteasome. In addition, decreased proteasome function also induces accumulation of the negative regulators of cytokine signaling (I-kappaB and SOCS), thereby blocking cytokine signal transduction. Finally, ethanol-elicited blockade of interferon type 1 and 2 signaling and decreased proteasome function impairs generation of peptides for MHC class I-restricted antigen presentation.

Indexed as

EthanolHumansLiver Diseases, AlcoholicOxidative StressProteasome Endopeptidase ComplexUbiquitinEthanolProteasome Endopeptidase ComplexUbiquitin

Identifiers

PMID17854134
PMCPMC4434615
OpenAlexW2415230796

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.