Evidence map›Paper›PMID 31235809›Full record

ArticleScientific reports2019

Hepatocyte PRMT1 protects from alcohol induced liver injury by modulating oxidative stress responses.

Jie Zhao, Abby Adams, Steven A Weinman, Irina Tikhanovich

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

  1. Dysregulated mScience advances · 2026
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  15. Matrix stiffness and shear stresses modulate hepatocyte functions in a fibrotic liver sinusoidal model.American journal of physiology. Gastrointestinal and liver physiology · 2021
    Article
  16. A critical role for hepatic protein arginine methyltransferase 1 isoform 2 in glycemic control.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    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

4 authors at 1 institution in 1 country.

Jie ZhaoDepartment of Internal Medicine, University of Kansas Medical Center, Kansas, United States.
Abby AdamsDepartment of Internal Medicine, University of Kansas Medical Center, Kansas, United States.
Steven A WeinmanDepartment of Internal Medicine, University of Kansas Medical Center, Kansas, United States.
Irina TikhanovichDepartment of Internal Medicine, University of Kansas Medical Center, Kansas, United States. itikhanovich@kumc.edu.
University of Kansas Medical Center · US

Funding

Role of alcohol adapted Kupffer cells in the progression and resolution of ALDR01AA012863 · NIAAA · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI STEVEN A WEINMAN · 2000 to 2026
$10.2M
NIAAA NIH HHS R01 AA012863
6 · The paper itself

Abstract

Protein Arginine methyltransferase 1 (PRMT1) is the main enzyme of cellular arginine methylation. Previously we found that PRMT1 activity in the liver is altered after alcohol exposure resulting in epigenetic changes. To determine the impact of these PRMT1 changes on the liver's response to alcohol, we induced a hepatocyte specific PRMT1 knockout using AAV mediated Cre delivery in mice fed either alcohol or control Lieber-DeCarli liquid diet. We found that in alcohol fed mice, PRMT1 prevents oxidative stress and promotes hepatocyte survival. PRMT1 knockout in alcohol fed mice resulted in a dramatic increase in hepatocyte death, inflammation and fibrosis. Additionally, we found that alcohol promotes PRMT1 dephosphorylation at S297. Phosphorylation at this site is necessary for PRMT1-dependent protein arginine methylation. PRMT1 S297A, a dephosphorylation mimic of PRMT1 had reduced ability to promote gene expression of pro-inflammatory cytokines, pro-apoptotic genes BIM and TRAIL and expression of a suppressor of hepatocyte proliferation, Hnf4α. On the other hand, several functions of PRMT1 were phosphorylation-independent, including expression of oxidative stress response genes, Sod1, Sod2 and others. In vitro, both wild type and S297A PRMT1 protected hepatocytes from oxidative stress induced apoptosis, however S297D phosphorylation mimic PRMT1 promoted cell death. Taken together these data suggest that PRMT1 is an essential factor of liver adaptation to alcohol; alcohol-induced dephosphorylation shifts PRMT1 toward a less pro-inflammatory, more pro-proliferative and pro-survival form.

Indexed as

Oxidative StressAnimalsApoptosisCell LineChemical and Drug Induced Liver InjuryEthanolGene Knockout TechniquesHepatocytesMiceMice, Inbred C57BLProtein-Arginine N-MethyltransferasesEthanolPrmt1 protein, mouseProtein-Arginine N-Methyltransferases

Identifiers

PMID31235809
PMCPMC6591482
OpenAlexW2954488559

What OpenQuestion holds

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LicenceCC BY
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.