Evidence map›Paper›PMID 22309199›Full record

ArticleJournal of proteome research2012

Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.

Kristofer S Fritz, James J Galligan, Matthew D Hirschey, Eric Verdin, Dennis R Petersen

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2012. 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
8.5field-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, 119 citations in OpenAlex.

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  8. Brain ethanol metabolism and mitochondria.Current topics in biochemical research · 2022
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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

5 authors at 2 institutions in 1 country.

Kristofer S FritzDepartment of Pharmaceutical Sciences, University of Colorado Denver , Aurora, Colorado, United States.
James J Galligan
Matthew D Hirschey
Eric Verdin
Dennis R Petersen
University of Colorado Denver · USGladstone Institutes · US

Funding

Virology CoreP30AI027763 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STEVEN Grant DEEKS · 1988 to 2026
$93.6M
Lipid Aldehyde and Ethanol Induced Liver DamageR37AA009300 · NIAAA · UNIVERSITY OF COLORADO DENVER · PI PETERSEN, DENNIS · 2008 to 2017
$4.4M
Proteomic profiling of NASH: disease mechanisms and novel treatmentR01DK074487 · NIDDK · UNIVERSITY OF COLORADO DENVER · PI PETERSEN, DENNIS · 2007 to 2011
$1.5M
Modification of PDI by 4-HNE and 4-ONE and its Role in Ethanol-Induced ER StressF31AA018606 · NIAAA · UNIVERSITY OF COLORADO DENVER · PI GALLIGAN, JAMES J · 2009 to 2011
$77k
NIAAA NIH HHS F31 AA018606NIAAA NIH HHS F31AA018606-01NIAAA NIH HHS R37 AA009300NIAAA NIH HHS R37AA09300NIAID NIH HHS P30 AI027763NIDDK NIH HHS R01 DK074487NIDDK NIH HHS R01DK074487-01
6 · The paper itself

Abstract

Mitochondrial protein hyperacetylation is a known consequence of sustained ethanol consumption and has been proposed to play a role in the pathogenesis of alcoholic liver disease (ALD). The mechanisms underlying this altered acetylome, however, remain unknown. The mitochondrial deacetylase sirtuin 3 (SIRT3) is reported to be the major regulator of mitochondrial protein deacetylation and remains a central focus for studies on protein acetylation. To investigate the mechanisms underlying ethanol-induced mitochondrial acetylation, we employed a model for ALD in both wild-type (WT) and SIRT3 knockout (KO) mice using a proteomics and bioinformatics approach. Here, WT and SIRT3 KO groups were compared in a mouse model of chronic ethanol consumption, revealing pathways relevant to ALD, including lipid and fatty acid metabolism, antioxidant response, amino acid biosynthesis and the electron-transport chain, each displaying proteins with altered acetylation. Interestingly, protein hyperacetylation resulting from ethanol consumption and SIRT3 ablation suggests ethanol-induced hyperacetylation targets numerous biological processes within the mitochondria, the majority of which are known to be acetylated through SIRT3-dependent mechanisms. These findings reveal overall increases in 91 mitochondrial targets for protein acetylation, identifying numerous critical metabolic and antioxidant pathways associated with ALD, suggesting an important role for mitochondrial protein acetylation in the pathogenesis of ALD.

Indexed as

AcetylationAcetyltransferasesAldehyde DehydrogenaseAldehyde Dehydrogenase, MitochondrialAnimalsChemical and Drug Induced Liver InjuryDisease Models, AnimalElectrophoresis, Gel, Two-DimensionalEthanolIsocitrate DehydrogenaseLipid MetabolismLiver Diseases, AlcoholicMaleMiceMice, Inbred C57BLMice, KnockoutAcetyltransferasesAldehyde DehydrogenaseAldehyde Dehydrogenase, MitochondrialALDH2 protein, mouseEthanolIsocitrate DehydrogenaseMitochondrial ProteinsProteomeSirt3 protein, mouseSirtuin 3Superoxide DismutaseSuperoxide Dismutase 2

Identifiers

PMID22309199
PMCPMC3324946
OpenAlexW1970967418

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.