Evidence map›Paper›PMID 33805551›Full record

ArticleCells2021

Mechanism of Na-K-ATPase Inhibition by PGE2 in Intestinal Epithelial Cells.

Niraj Nepal, Subha Arthur, Jennifer Haynes, Balasubramanian Palaniappan, Uma Sundaram

Open access · goldAbstract read
In one paragraph

Article in Cells, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

10 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Antibacterial Activity and Mechanism ofPlants (Basel, Switzerland) · 2025
    Article
  5. Review
  6. Review
  7. NaInternational journal of molecular sciences · 2024
    Review
  8. Article
  9. Review
  10. Review
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 1 institution in 1 country.

Niraj NepalDepartment of Clinical and Translational Sciences, Appalachian Clinical and Translational Science Institute, Joan C. Edwards School of Medicine, Marshall University, 1600 Medical Center Drive, Huntington, WV 25701, USA.ORCID 0000-0003-1525-3214
Subha ArthurDepartment of Clinical and Translational Sciences, Appalachian Clinical and Translational Science Institute, Joan C. Edwards School of Medicine, Marshall University, 1600 Medical Center Drive, Huntington, WV 25701, USA.
Jennifer HaynesDepartment of Clinical and Translational Sciences, Appalachian Clinical and Translational Science Institute, Joan C. Edwards School of Medicine, Marshall University, 1600 Medical Center Drive, Huntington, WV 25701, USA.
Balasubramanian PalaniappanDepartment of Clinical and Translational Sciences, Appalachian Clinical and Translational Science Institute, Joan C. Edwards School of Medicine, Marshall University, 1600 Medical Center Drive, Huntington, WV 25701, USA.ORCID 0000-0003-2082-7534
Uma SundaramDepartment of Clinical and Translational Sciences, Appalachian Clinical and Translational Science Institute, Joan C. Edwards School of Medicine, Marshall University, 1600 Medical Center Drive, Huntington, WV 25701, USA.ORCID 0000-0002-9322-6740
Marshall University · US

Funding

NIH HHS DK-108054NIH HHS DK-67420NIH HHS P20GM121299-01U.S. Department of Veterans Affairs BX003443-01
6 · The paper itself

Abstract

The primary means of intestinal absorption of nutrients by villus cells is via Na-dependent nutrient co-transporters located in the brush border membrane (BBM). These secondary active co-transport processes require a favorable transcellular Na gradient that is provided by Na-K-ATPase. In chronic enteritis, malabsorption of essential nutrients is partially due to inhibition of villus Na-K-ATPase activity mediated by specific immune inflammatory mediators that are known to be elevated in the inflamed mucosa. However, how Prostaglandin E2 (PGE2), a specific mediator of nutrient malabsorption in the villus BBM, may mediate the inhibition of Na-K-ATPase is not known. Therefore, this study aimed to determine the effect of PGE2 on Na-K-ATPase in villus cells and define its mechanism of action. In vitro, in IEC-18 cells, PGE2 treatment significantly reduced Na-K-ATPase activity, accompanied by a significant increase in the intracellular levels of cyclic Adenosine Monophosphate (cAMP). The treatment with cAMP analog 8-Bromo-cAMP mimicked the PGE2-mediated effect on Na-K-ATPase activity, while Rp-cAMP (PKA inhibitor) pretreatment reversed the same. The mechanism of inhibition of PGE2 was secondary to a transcriptional reduction in the Na-K-ATPase α1 and β1 subunit genes, which was reversed by the Rp-cAMP pretreatment. Thus, the PGE2-mediated activation of the PKA pathway mediates the transcriptional inhibition of Na-K-ATPase activity in vitro.

Indexed as

AnimalsCell LineCell SurvivalCyclic AMPCyclic AMP-Dependent Protein KinasesDinoprostoneEpithelial CellsIntestinesIntracellular SpaceProtein SubunitsRatsReceptors, ProstaglandinRNA, MessengerSodium-Potassium-Exchanging ATPaseXanthones6-isopropoxy-9-oxoxanthene-2-carboxylic acidCyclic AMPCyclic AMP-Dependent Protein KinasesDinoprostoneProtein SubunitsReceptors, ProstaglandinRNA, MessengerSodium-Potassium-Exchanging ATPaseXanthonesIntestinal epithelial cellsNa-K-ATPasePGE2Villus

Identifiers

PMID33805551
PMCPMC8066871
OpenAlexW3145334144

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.