Evidence map›Paper›PMID 24072780›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2014

Inhibition of protein translation as a novel mechanism for prostaglandin E2 regulation of cell functions.

Katsuhide Okunishi, Angela J DeGraaf, Zbigniew Zasłona, Marc Peters-Golden

Abstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.4field-weighted citation impact, top 35% 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

12 citing papers in PubMed, 17 citations in OpenAlex.

  1. Mechanistic basis for the antifibrotic actions of cAMP-based therapies.European respiratory review : an official journal of the European Respiratory Society · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. PGELife science alliance · 2020
    Article
  6. Loss of DP1 Aggravates Vascular Remodeling in Pulmonary Arterial Hypertension via mTORC1 Signaling.American journal of respiratory and critical care medicine · 2020
    Article
  7. Article
  8. Special Delivery: A New Package for an Old Antifibrotic Mediator.American journal of respiratory cell and molecular biology · 2019
    Article
  9. Distinct PKA regulatory subunits mediate PGEAmerican journal of physiology. Lung cellular and molecular physiology · 2017
    Article
  10. Article
  11. Reversal of the Transcriptome by Prostaglandin E2 during Myofibroblast Dedifferentiation.American journal of respiratory cell and molecular biology · 2016
    Article
  12. 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.

Katsuhide Okunishi26301 MSRB III, 1150 W. Medical Center Drive, Ann Arbor, MI 48109-5642. petersm@umich.edu.
Angela J DeGraaf
Zbigniew Zasłona
Marc Peters-Golden
Michigan Medicine · US

Funding

Control of Fibroblast Function by Prostaglandin E2 and Plasminogen ActivationR01HL094311 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PETERS-GOLDEN, MARC L · 2009 to 2017
$3.4M
NHLBI NIH HHS HL094311NHLBI NIH HHS R01 HL094311
6 · The paper itself

Abstract

Prostaglandin E2 (PGE2) regulates numerous biological processes by modulating transcriptional activation, epigenetic control, proteolysis, and secretion of various proteins. Scar formation depends on fibroblast elaboration of matrix proteins such as collagen, and this process is strongly suppressed by PGE2 through activation of cAMP-dependent protein kinase A (PKA). However, the actual mechanism by which PGE2-PKA signaling inhibits collagen expression in fibroblasts has never been delineated, and that was the objective of this study. PGE2 unexpectedly induced a rapid reduction in procollagen I protein expression in adult lung fibroblasts, with a half-maximum effect at 1.5 h. This effect reflected its inhibition of translation rather than transcription. Global protein synthesis was also inhibited by PGE2. This action was mediated by PKA and involved both activation of ribosomal protein (rpS6) and suppression of mammalian target of rapamycin (mTOR). Similar effects of PGE2 were demonstrated in mouse peritoneal macrophages (PMs). These findings identify inhibition of translation as a new mechanism by which PGE2 regulates cellular function and a novel example of translational inhibition mediated by opposing actions on two distinct translational control pathways. Translational inhibition would be expected to contribute to dynamic alterations in cell function that accompany the changing PGE2 levels observed in disease states and with various pharmacotherapies.

Indexed as

AnimalsCell LineCollagen Type ICyclic AMP-Dependent Protein KinasesDinoprostoneFibroblastsHumansImmunoblottingImmunoprecipitationLungMacrophages, PeritonealMaleMiceMice, Inbred C57BLPolymerase Chain ReactionProtein TransportCollagen Type ICyclic AMP-Dependent Protein KinasesDinoprostoneRibosomal Protein S6TOR Serine-Threonine Kinasesfibroblastsmacrophagesmammalian target of rapamycinprotein kinase Aribosomal protein S6

Identifiers

PMID24072780
PMCPMC3868831
OpenAlexW1994207884

What OpenQuestion holds

Textmetadata
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.