Evidence map›Paper›PMID 25454745›Full record

ArticleRedox biology2014

Proteomic analysis of 4-hydroxynonenal (4-HNE) modified proteins in liver mitochondria from chronic ethanol-fed rats.

Kelly K Andringa, Uduak S Udoh, Aimee Landar, Shannon M Bailey

Open access · goldAbstract read
In one paragraph

Article in Redox biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

34 citing papers in PubMed, 51 citations in OpenAlex.

  1. Siah2 regulates lipid uptake in adipose tissue macrophages.The Journal of biological chemistry · 2026
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  7. Protein Haptenation and Its Role in Allergy.Chemical research in toxicology · 2024
    Review
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  12. Article
  13. Review
  14. Article
  15. Mass Spectrometry in Advancement of Redox Precision Medicine.Advances in experimental medicine and biology · 2019
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Kelly K AndringaDepartment of Medicine, Division of Nephrology, University of Alabama at Birmingham, Birmingham, AL, USA; Department of Environmental Health Sciences, University of Alabama at Birmingham, Birmingham, AL, USA.
Uduak S UdohDepartment of Pathology, Division of Molecular and Cellular Pathology, University of Alabama at Birmingham, Birmingham, AL, USA.
Aimee LandarDepartment of Pathology, Division of Molecular and Cellular Pathology, University of Alabama at Birmingham, Birmingham, AL, USA.
Shannon M BaileyDepartment of Environmental Health Sciences, University of Alabama at Birmingham, Birmingham, AL, USA; Department of Pathology, Division of Molecular and Cellular Pathology, University of Alabama at Birmingham, Birmingham, AL, USA. Electronic address: sbailey@uab.edu.
University of Alabama at Birmingham · US

Funding

Alcoholic Liver Dysfunction Potentiation by Hyperlipidemia and Cigarette SmokeR01AA018841 · NIAAA · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BAILEY, SHANNON MARIE · 2009 to 2013
$1.5M
Redox Modification of Thiols in Alcohol HepatotoxicityR01AA015172 · NIAAA · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BAILEY, SHANNON MARIE · 2004 to 2008
$1.4M
NIAAA NIH HHS R01 AA015172NIAAA NIH HHS R01 AA018841
6 · The paper itself

Abstract

Chronic ethanol-mediated oxidative stress and lipid peroxidation increases the levels of various reactive lipid species including 4-hydroxynonenal (4-HNE), which can subsequently modify proteins in the liver. It has been proposed that 4-HNE modification adversely affects the structure and/or function of mitochondrial proteins, thereby impairing mitochondrial metabolism. To determine whether chronic ethanol consumption increases levels of 4-HNE modified proteins in mitochondria, male rats were fed control and ethanol-containing diets for 5 weeks and mitochondrial samples were analyzed using complementary proteomic methods. Five protein bands (approx. 35, 45, 50, 70, and 90kDa) showed strong immunoreactivity for 4-HNE modified proteins in liver mitochondria from control and ethanol-fed rats when proteins were separated by standard 1D SDS-PAGE. Using high-resolution proteomic methods (2D IEF/SDS-PAGE and BN-PAGE) we identified several mitochondrial proteins immunoreactive for 4-HNE, which included mitofilin, dimethylglycine dehydrogenase, choline dehydrogenase, electron transfer flavoprotein α, cytochrome c1, enoyl CoA hydratase, and cytochrome c. The electron transfer flavoprotein α consistently showed increased 4-HNE immunoreactivity in mitochondria from ethanol-fed rats as compared to mitochondria from the control group. Increased 4-HNE reactivity was also detected for dimethylglycine dehydrogenase, enoyl CoA hydratase, and cytochrome c in ethanol samples when mitochondria were analyzed by BN-PAGE. In summary, this work identifies new targets of 4-HNE modification in mitochondria and provides useful information needed to better understand the molecular mechanisms underpinning chronic ethanol-induced mitochondrial dysfunction and liver injury.

Indexed as

ProteomicsAldehydesAnimalsChronic DiseaseEthanolLiver Diseases, AlcoholicMaleMitochondria, LiverMitochondrial ProteinsProtein Processing, Post-TranslationalRatsRats, Sprague-Dawley4-hydroxy-2-nonenalAldehydesEthanolMitochondrial Proteins4-HydroxynonenalAlcoholLiverMitochondriaPosttranslational modificationProteome

Identifiers

PMID25454745
PMCPMC4297939
OpenAlexW1985385891

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.