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Cited by 52Metabolism, Diabetes, and CancerRedox biology and oxidative stressAlcohol Consumption and Health Effects

The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.

Effect of ethanol on hydrogen peroxide-induced AMPK phosphorylation

Open access
Liangpunsakul, Suthat, Wou, Sung-Eun, Zeng, Yan, Ross, Ruth A., Jayaram, Hiremagalur N., Crabb, David W.·2008·American Journal of Physiology-Gastrointestinal and Liver Physiology
DOI 10.1152/ajpgi.90349.2008PMC PMC2604799
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Abstract

AMP-activated protein kinase (AMPK) responds to oxidative stress. Previous work has shown that ethanol treatment of cultured hepatoma cells and of mice inhibited the activity of AMPK and reduced the amount of AMPK protein. Ethanol generates oxidative stress in the liver. Since AMPK is activated by reactive oxygen species, it seems paradoxical that ethanol would inhibit AMPK in the hepatoma cells. In an attempt to understand the mechanism whereby ethanol inhibits AMPK, we studied the effect of ethanol on AMPK activation by exogenous hydrogen peroxide. The effects of ethanol, hydrogen peroxide, and inhibitors of protein phosphatase 2A (PP2A) [either okadaic acid or PP2A small interference RNA (siRNA)] on AMPK phosphorylation and activity were examined in rat hepatoma cells (H4IIEC3) and HeLa cells. In H4IIEC3 cells, hydrogen peroxide (H(2)O(2), 1 mM) transiently increased the level of phospho-AMPK to 1.5-fold over control (P < 0.05). Similar findings were observed in HeLa cells, which do not express the upstream AMPK kinase, LKB1. H(2)O(2) markedly increased the phosphorylation of LKB1 in H4IIEC3 cells. Ethanol significantly inhibited the phosphorylation of PKC-zeta, LKB1, and AMPK caused by exposure to H(2)O(2). This inhibitory effect of ethanol required its metabolism. More importantly, the inhibitory effects of ethanol on H(2)O(2)-induced AMPK phosphorylation were attenuated by the presence of the PP2A inhibitor, okadaic acid, or PP2A siRNA. The inhibitory effect of ethanol on AMPK phosphorylation is exerted through the inhibition of PKC-zeta and LKB1 phosphorylation and the activation of PP2A.

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Crossref · 10.1152/ajpgi.90349.2008

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  • In H4IIEC3 cells, exogenous hydrogen peroxide transiently increased phosphor-AMPK by LKB1 signaling, while in HeLa cells it promoted AMPK phosphorylation by CaMKK signaling.

    “In H4IIEC3 cells, exogenous hydrogen peroxide transiently increased the level of phosphor-AMPK by LKB1 signaling, while exogenous hydrogen peroxide promoted AMPK phosphorylation in HeLa cells by CaMKK signaling [42].”

    From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [42]

  • AMPK is responsive to imbalanced redox status.

    “Recent lines of evidence have demonstrated AMPK responsiveness to imbalanced redox status, thus bringing new insights into the networks of redox-stimulated signals upstream of AMPK (Table 1) [42,43,44,45,46,47,48,49,50,51].”

    From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [42]

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Metadata

Authors
Liangpunsakul, S., Wou, S.-E., Zeng, Y., Ross, R. A., Jayaram, H. N., & Crabb, D. W.
Affiliations
  • Indiana University Hospital (US)
  • Indiana University Bloomington (US)
ORCID
Venue
American Journal of Physiology-Gastrointestinal and Liver Physiology
Publisher
American Physiological Society
Published
2008-12
Volume
295
Issue
6
Pages
G1173-G1181
ISSN
  • 0193-1857 (ISSN-L)
  • 1522-1547
DOI
10.1152/ajpgi.90349.2008
PMC
PMC2604799
OpenAlex
W2099287991
Cited by
52
References
26
Citations by year
2026: 2 · 2025: 1 · 2024: 1 · 2023: 1 · 2022: 2 · 2021: 4 · 2020: 3 · 2019: 3 · 2018: 3 · 2017: 1 · 2016: 2 · 2015: 3 · 2014: 5 · 2013: 6 · 2012: 2
FWCI
1.65
Type
journal article
Language
en
Open access
Locations
  • American Journal of Physiology-Gastrointestinal and Liver Physiology (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institute on Alcohol Abuse and Alcoholism (R01 AA15070, K08AA016570, P60 AA 07611, R01AA015070, P60AA007611)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Health Sciences › Medicine › Pathology and Forensic Medicine › Alcohol Consumption and Health Effects
Keywords
ethanol, AMPK, AMPK phosphorylation, hydrogen peroxide, oxidative stress, protein phosphatase 2A, okadaic acid, LKB1, PKC zeta, hepatoma cells, alcohol metabolism, reactive oxygen species
MeSH terms
AMP-Activated Protein Kinase Kinases, Protein Kinase C zeta, Ethanol, Animals, Enzyme Activation, HeLa Cells, Humans, Hydrogen Peroxide, Liver Neoplasms, Experimental, Phosphorylation, Protein Kinase C, Protein Kinases, Tumor Cells, Cultured, Protein Serine-Threonine Kinases, Oxidative Stress, Rats, Protein Phosphatase 2, AMP-Activated Protein Kinases

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