Evidence map›Paper›PMID 20026058›Full record

ArticleBiochemical and biophysical research communications2010

Impaired methylation as a novel mechanism for proteasome suppression in liver cells.

Natalia A Osna, Ronda L White, Terrence M Donohue, Michael R Beard, Dean J Tuma, Kusum K Kharbanda

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

21 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  11. Homocysteine Increases Tau Phosphorylation, Truncation and Oligomerization.International journal of molecular sciences · 2018
    Article
  12. Article
  13. Review
  14. Regulation of cardiac proteasomes by ubiquitination, SUMOylation, and beyond.Journal of molecular and cellular cardiology · 2014
    Review
  15. Review
  16. Article
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  18. Article
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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

6 authors at 3 institutions in 2 countries.

Natalia A OsnaLiver Study Unit, The Omaha Veterans Affairs (VA) Medical Center, Omaha, NE 68105, USA. nosna@UNMC.edu
Ronda L White
Terrence M Donohue
Michael R Beard
Dean J Tuma
Kusum K Kharbanda
University of Nebraska Medical Center · USOmaha VA Medical Center · USUniversity of Adelaide · AU

Funding

Effects of Ethanol on Proteasome-HCV Core Protein InteractionsR21AA017232 · NIAAA · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI OSNA, NATALIA ALEKSANDR · 2009 to 2010
$345k
Accumulation of Isoaspartyl Residue-Bearing Proteins and Alcoholic Liver DiseaseR21AA017296 · NIAAA · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI KHARBANDA, KUSUM K. · 2008 to 2009
$328k
NIAAA NIH HHS R21 AA017232NIAAA NIH HHS R21 AA017296NIAAA NIH HHS R21AA017296NIAAA NIH HHS R21AA01732
6 · The paper itself

Abstract

The proteasome is a multi-catalytic protein degradation enzyme that is regulated by ethanol-induced oxidative stress; such suppression is attributed to CYP2E1-generated metabolites. However, under certain conditions, it appears that in addition to oxidative stress, other mechanisms are also involved in proteasome regulation. This study investigated whether impaired protein methylation that occurs during exposure of liver cells to ethanol, may contribute to suppression of proteasome activity. We measured the chymotrypsin-like proteasome activity in Huh7CYP cells, hepatocytes, liver cytosols and nuclear extracts or purified 20S proteasome under conditions that maintain or prevent protein methylation. Reduction of proteasome activity of hepatoma cell and hepatocytes by ethanol or tubercidin was prevented by simultaneous treatment with S-adenosylmethionine (SAM). Moreover, the tubercidin-induced decline in proteasome activity occurred in both nuclear and cytosolic fractions. In vitro exposure of cell cytosolic fractions or highly purified 20S proteasome to low SAM:S-adenosylhomocysteine (SAH) ratios in the buffer also suppressed proteasome function, indicating that one or more methyltransferase(s) may be associated with proteasomal subunits. Immunoblotting a purified 20S rabbit red cell proteasome preparation using methyl lysine-specific antibodies revealed a 25kDa proteasome subunit that showed positive reactivity with anti-methyl lysine. This reactivity was modified when 20S proteasome was exposed to differential SAM:SAH ratios. We conclude that impaired methylation of proteasome subunits suppressed proteasome activity in liver cells indicating an additional, yet novel mechanism of proteasome activity regulation by ethanol.

Indexed as

AnimalsAntimetabolites, AntineoplasticCell Line, TumorChymotrypsinEthanolHumansLiverMethylationMiceMice, Inbred C57BLProteasome Endopeptidase ComplexRabbitsS-AdenosylhomocysteineS-AdenosylmethionineTubercidinAntimetabolites, AntineoplasticChymotrypsinEthanolProteasome Endopeptidase ComplexS-AdenosylhomocysteineS-AdenosylmethionineTubercidin

Identifiers

PMID20026058
PMCPMC2812660
OpenAlexW2027752589

What OpenQuestion holds

Textmetadata
LicenceTDM
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.